lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the swi5-sfr1 complex, a complex required for double-strand break repair via homologous recombination.
Subcellular Localization:
Nucleus.
Sequence:
METTPIKPTAADETTPSAEQSSNRSSTAKPMSASLREKLKRSRHSFKSPLSVVKRLKIEDDTEPQPSQQGEEEKHGVKDDRDSNVTETDVNRNDMKLQRDSNHTAELPSQQCEALRKAVKERTETLRRLKMVKMYRKKNDLNELQRLTDKWRSCAQSVLYELQRELATGGKQASLSQLIDSFGINDKLLHFDRTEEDFTDT
The following text describes a protein:
Function:
Required for assembly of dynein regulatory complex (DRC) and inner dynein arm (IDA) complexes, which are responsible for ciliary beat regulation, thereby playing a central role in motility in cilia and flagella. Probably acts together with CCDC40 to form a molecular ruler that determines the 96 nanometer (nm) repeat length and arrangements of components in cilia and flagella. Not required for outer dynein arm complexes assembly.
Sequence:
MSSYLDEILKTLGWEDGFQIPVANAENQQLEAEVARLTLQKIKEKTALETSAVKLENIQNHLKYVKQESEQNQNLITAHAQQLQSEESRLRLSAAEKDKFEQDIKQCEKQFADIQARQSIKKNQLERYVKKLDKLKSETDWDSEALKAWEESLKKRDDDNELIKKFSKQDDRKYNELEARRQNLEVEFANRKQTIDKMVSDLINYERVLERTGKIMKQQVVERNALIQQWKESVNILHQRDNDIDRLQAQMLETQEIISKEEEKLEEQKQFYENEVRNNNELQHEAQQLNLLNSRIRRELNEMSQNMLVLNSQADTLRRTMILVANQLEKERLHKKHAWEEIEKMEHKIAIFRANLDVLKTKNEQVKQSTLSADERMKHLEKLIDYEQKQQKTLQLEAESLQNAYFRSQHELQEQQSIGKMRDLEIYGMTTNINHLRKHNDDQKKALGKRKEDAYDLDYRIDEVQRKILINENVLHSDDTEELEGKLIELENKIAEHTEIKNLLKDQVNKIRDDMRRLTTAIVADQNQLSVLKDKLQHQNLNFEGGQKQLQVLKNGIQEKQVEENILRLRVNQLNKAMKKEENSIYTMKKFKLTLEQATQERMLEIETSKDILLAKKRNLGEDNGRLRCDIAERRLKLDHFKKKYDIILTSLGKDEDGQPLSVTHFKIKNAQEKYLLQQEGDELDMKIKKAEKEILAMENTLKVVNLTNAAFKQSLGAVEDDGREMSEMKMLENEMLLINDTLRENRKKMAVKRQELEEVQNALKELEIKRDQAKDALFDLEEEYLKTEKESSEKEEKLKRAERCLKLAQKKVRHKEREKYDRDLEIRQLKEANLSAMQRLVEMSIRYQEMAPLITRYTLEYDVKLPEKRTIASLCACSESTRSTSSSSCNQEKDVSDVKSVKSESSSTKSSAISKVSITFQM
The following text describes a protein:
Function:
Methyltransferase that adds a 2'-O-methyl group at the 3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. This probably protects the 3'-end of piRNAs from uridylation activity and subsequent degradation. Required for programmed DNA elimination.
Subcellular Localization:
Nucleus. Note=Localizes to the macronucleus.
Sequence:
MIEAYETDVFMDPIGMKVWEKRHQYVATKLSALNCKRVLDMGTNTCKLIQRLSRSLQFTQIDGLDIDGQLLETQGIQNAKPDLIQNQYASMRDHQLVVNLYQGSALNKIQHLKDQQYDAVILVELIEHLQVEDVFLIEQNLFGFLRPQFVIVTTPNSDFNVYFNFKEQGVLFRDKDHKFEWSQNQFQIWAQKVCQNYGYKVIELTGVGEHKTEGTKNGFCTQIVVFEKDTQQEKYLNFAFFNLQEGEIRQVCQILYPFESKEQHFQREVVDSIRYILHITDKQNQFEDGSYQNYTTLSRIMQNHSISSNWQIQGDYFKLKTYIQNISEFLVHENQFNFQESFVTLNYQAQMEDEENEDQLESDSENVKMQQQQYYFSNDNCFSTKDTTYSSFSTADNLFSQKIQLGQQQMALEEIELEDTIDY
The following text describes a protein:
Function:
Transcription factor acting as a regulator of arbuscular mycorrhiza (AM)-related genes (e.g. STR). Required for the morphogenesis of arbuscules upon symbiosis with AM fungi (e.g. Glomus versiforme). Also involved in restricting mycorrhizal colonization of the root meristem (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MSPALYASTFKCEVDENPSLMGSYYASLYPNLPILENSATSTWILNPFSDHETETIRDHKKLKRSTVTIPIWFANFSSHSNSFFNNINSNNNSVNSIPRLHFRDHIRTYKQRYFASEAVEEAAEDNFNYNNCEAEEDGSCADGMRLVQLLIACAEAVACRDKSHASVLLSELKSNALVFGSSFQRVASCFVQGLTERLTLIQPIGNNSAGSDTKSMMNIMDAASEEMEEAFKLVYENCPHIQFGHFVANSIILEAFEGESFLHVVDLGMSLGLPHGHQWRGLIQSLADRSSHRVRRLRITAIGLCIARIQVIGEELSIYAKNLGIHLEFSIVEKNLENLKPKDIKVNEKEVLVVNSILQLHCVVKESRGALNAVLQMIHGLSPKVLVMAEQDSGHNGPFFLGRFMESLHYYSAIFDSLDAMLPKYDTKRAKMEQFYFAEEIKNIVSCEGPLRMERHEKVDQWRRRMSRAGFQGSPIKMVVQAKQWLVKNNVCDGYTVVEEKGCLVLGWKSKPIVAVSCWKC
The following text describes a protein:
Function:
Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA.
Subcellular Localization:
Nucleus.
Sequence:
MDEQVIFTTAVSGTVCQVHSVGQANLRQCAASTPNSAVLMGDKLLVAQANKALINVYSVDSRSKKEALEQRLPLPEQLSCLAVVENHTGDAGVHQQLPYLLLGSTPSGKLYVWEAGSGKLLTVKAMAHYQAITKMQAIINGKYVVTAGADSRLIIWQTASLVLEEEPKPLYVLHDHTLAITDFAVSNAHNGKYLNSKLYTVSEDMTVRCYQLSSQLEQPQLLATFTFPLALTSIALDPADRCLYVGTREGAFALPLFYKLDSSGATLVNLLQPGKHQIYSIVPEQAGVEVNKQELYRMGQLLCSKMLSCHVSLIRVSMDGSMVLLATGSGNCVVVDTYSKQPVKELAPLLAPGTQTGPVSNIITRSMTVKSDSLLQDLNLADARATEAIKIPALAKTVFDKTGTHDIIYCAPTDTLSSVLPRALDLPQYLDMIAEEDSVFANTPVTRSTVKVVGELAPAKAEALPASSAEAQQSADDTDAEVARLRESLQQLTGAYKDLRALHEKLYEEHEKLLQTSK
The following text describes a protein:
Function:
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Subcellular Localization:
Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum.
Sequence:
MRYTSLPRTATFAWSPDPFLPASQNPSSSASANTHSEHQAELDQFNSPLLATGTASGVLDSSFSTDSKLEIWSPFTSDSAEAKGTVTLQSRFHRLAWGHAAGLRPRGVIAAGMENAELDIWDPIEILAGQGPEKALVSKMKNHNGPIKGLDFNPVKNNLLASGASKGEVFIWDLNNPVKPFAPPSSRSLDDVSSVNWNHIVQSVLAASSNNGYTVVWDIREANGQKGREVATLSYSGSVNQMPAYGQPQPGMMGGPQYGSQWMGPAGGRPGSVSSVVWHPENPTKLVTASDDDASPIVLVWDLRNARAPERILAGHEKGILSLAWCKQDSDLLVSCGKDCRTICWNPTSGEIVAELPPSSNWSFQSDWCPRNPDLIATASFDGRIAINSLQSTGEESETVEPPSTSGPAVDGSDIFGDQGLLALNSAKAAVSCKQAPKWYKRPSAATFAFGGKVVTIDNPSPPNPTQQAPGDNTSIKTSPVVKIRQVVTEPTLVERALKLENASQARNLQTLCEERANRLPSHASTIELQSWKLLSTLFKSDSSEELVNLLGFSKSEVKSMVERQIESYKPSKVSNSLSRTASEMGPTSTALETSPSDNDSIPREPLVTFAETPREGLSASSEGGGEATVSSADAAPSEASVSAISDGTKLAEAESEITEPSLFGDDNANAAGQTAASVDFYNSMRTNRPAGLPDHVFSRVSAAASSVGATIGSQTSSVASEITRSNTFQIYPSEESKGDRLITRALVVGDFESAVSLCISSERWADALLLGVRGGPELLQKAQKAYFGKQTVNHPYLRLYQSIVLDDLMDVVQNADLSEWQEIFVVLCTFAKKEEFSNLVEQLGQRLEYMSHPSTPTESPGQQPSSVSTAEFRKNAILCYLAAGKLEKVTSIWIEQMEEEEAALLKNVDADDQQSAFSIHADVLQTLIEKVTVFQSAINYVDLDLAQTNESVGATKTDAKEYKLAMLYDCYYEYAELLASQGLSNTALRFVAQTPLGYTPSRTSPSSSARERLSKSVGLTSLVADRQFPAEQRTPTSATAVPPLDKPFAEVPSTQNAYQNSYNPSNNLSAYSNTAYQPSSMGAPGGNIDGNYSNPYGSSYNQMPMGQNNYAPMSTGSFLPPPPAPIGTSPIPSRAPSVSQLPPAARQPPSQVGGWNDAPVVNNTRKNVPPPGGPKAVISSPFPNASQTMSPAQPYPNQFGGYGAPQTGYQQGSPGGPPPPPRGGSRTPGNAANVVPPPPKFGQHPPGGVPQTPQQYGQPGGNVAPQSGHPGPYGPPKAQHPGAGPPAQPRQVNFSTPTQQASYQAQPVMQSPMQQQTPYGSGPPPQMYPQQRGSLSGAQAAGQYGIPPAGQGMPPSGQNMPPGQGPPQSQRPGTAPPVPKPEPPKSKYPPGDRSHIPEASKPIYVSLQRLMNQMKQGLPANQKKLVDDTERRLNVLFDALNCETVPASVIDELTDIVKAIEARNLQLALQLHVSLLTSGIKSDQLTTYMPAIKMLITKLQ
The following text describes a protein:
Function:
Constitutive protein of the cell wall. Antigen target of host humoral immune response.
Subcellular Localization:
Secreted, cell wall.
Sequence:
MRFSALTSLLAWGAFAGVLATPTKVSWAPSLVERDFAAVTSVVAAISSKVDTLDANIKAYTGGDTSAIVDASADLISTINDGTSTVAAQPALSQVDALNLVNPILALTNKVKTTIDDLISKKSLIVEAGAGPTTYSQLLDQYTASSNLATTLSGKVPEALKQVAEELSSGITSAIQKGIDAYKDVSTPPTTTTSSTSTPPTTSPTTTPTETSTPCETTTTTTETSTPCETTTTTTPPPETSTPCETTTTTTETSTPCETTTTPTETSTPCETTTTPTETSTPCETTTTPTETSTPCETTTTTTETSTPCETTTTPTETSTPCETTTTPTETSTPCETTTTPTETSTPCETTTTTTETSTPCETTTTTTPPPETSTPCETTTTPTETSTPCETTTTPTETSTPCETTTTTTPPPETSTPCETTTTPTETSTPCETTTTPTETSTPCETTTTPPETSTPCETTTTTTPPTETTTTPTTPPAETTTTTNVPVPPVTSTTTATETTPCHECEGTTSVPNPPGPTTLTTVPACTTCGGSGGGGGGEQPTPPVVVPQPSPSSPTTIAPPGGLSTGAASKPGSSLGTAMAIAAFALLL
The following text describes a protein:
Function:
Elongator complex-associated factor that is not a structural subunit but rather transiently contacts the complex. Required for an early step in synthesis of 5-methoxycarbonylmethyl (mcm5) and 5-carbamoylmethyl (ncm5) groups present on uridines at the wobble position in tRNA (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MPLIIVSGYPSSGKTTRSNELKKALEDRIHQNIDNTKDYRVIIINDESLNIEKETYRESKNEKAARGLLYSAVQRELSKSTFVICDALNYIKGFRYQLYCESKSMYTTHCVIHVAVPQDLCRKFNSNKEQPYPDDVLEQLMFRYEEPNGMTRWDSPLFTVLHDDASCPIDDIWSVLIHNKNVKPNQATMVKPPAEVNYLYELDKTTQDVIMLILDNSNDTSLITVPGSKLQIALPSVTVSLPLLQRLRRQFIQINRQQSYNTNVLKEMFVEFLNGQFETLD
The following text describes a protein:
Function:
Plant-specific actin binding protein. May be part of a membrane-cytoskeletal adapter complex.
Sequence:
MEIAAKSNSKRMYSWWWDSHNTPKNSKWLQDNLADMDSNVKQMIKVLEEDADSFARRAEMYYRKRPELMKLVEEFYRAYRALAERYNHATGVIHKAHETIAEAFPNQVPLIFGDESHGGALTNDVDPQTPDMPPPFRARGNPDEFQQDALGFSLSHVHDVKRNIDFSEEPLFVSNGKARKGLNFNDHGDGKGRNGLKDHILSESERASKAEAEVVALKDSLSKMQAEKQASLALFEKNLERLSNLESEVSRAQADSRGINDRAASAEAEIQTLRETLYKLESEKESSFLQYHKCLQKIADLEDGLSVAHKEAGERASKAETETLALKRSLAKAETDKETALIQYRQCLNTISNLEERLRKAEEDARLINERAEKAGVEVENLKQTVSKLIKDKEASELQFQQCLNIIASLKVKLHHAQEETQSLSHEIEDGVAKLKFSEEKCLLLERSNQNLHSELDSLLEKLGNQSQKLTEKQTELVKLWSCVQAEHLHFQEAETAFQTLQQLHSQSQEELNNLAVELQTVSQIMKDMEMRNNELHEELEQAKVENKGLNDLNFTMEKLVQKNLMLEKSISYLNSELESFRRKLKTFEEACQSLSEEKSCLISENQHNVIENTVLIEWLRQLRLEAVGIATEKTDLEGKAKTIGDKLTDAETENLQLKRNLLSIRSEKHHLEDEITNVKDQLHEKEKEFEEIKMEKEKLIQEVFKERKQVELWESQAATFFCDKQISVVHETLIEATTRELAEACKNLESKSASRDADIEKLKRSQTIVLLNESIKSLEDYVFTHRESAGEVSKGADLMDEFLKLEGMCLRIKAIAEAIMEKEKFLMLENTNTYSMLEASLKQIKELKTGGGRSMRKQDGGSGRMRKQSHETEMVMKDIVLDQTSDGSSYEIVSKKGNSELDHLGFVELKPVKTHKTETKALSEESLIVEKVEIFDGFMDPNREVNKRRVLERLDSDLQKLENLQITVEDLKSKVETVEKEKTKVGENEYKTIKGQLEEGEEAIEKLFTVNRKLTTKAESEKDIDRRRRIFEHARRGTEKIGRLQSEIQRIQFLLMKLEGEREHRLRSKISDTKVLLRDYIYGRTRSVSMKKRTKKRSVFCGCVQQPESP
The following text describes a protein:
Function:
Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. In the PRC1 complex, it is required to stimulate the E3 ubiquitin-protein ligase activity of rnf2.
Subcellular Localization:
Nucleus.
Sequence:
MTMHRTTRIKITELNPHLMCVLCGGYFIDATTIIECLHSFCKTCIVGYLESSKYCPICDVQVHKTKPLLNIRSDKTLQDIVYKLVPGLFKNEMKRRRDFYAAHPSIDATNGSNEDRGEVADEDKRIITDDEIISLSIEFFDHSKAEKQGAAEKDKPKEEVNDKRYLRCPAAMTVMHLRKFLRSKMDIPCTFQIEVMYEDEPLKDYYTLMDIAYIYTWRRNGPLPLKYRVRPSCKRLKVNPAHEGLPGPRSEMESDSGSDKASSPAGVPSTSSSLPSPSTPVQSPHPHFPHISTTVNGTSANPNPIRPPPFCSKARKTSLNGSSTSSG
The following text describes a protein:
Function:
Catalyzes the hydrolysis of endogenous amidated lipids like the sleep-inducing lipid oleamide ((9Z)-octadecenamide), the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules. Also catalyzes the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol). FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Golgi apparatus membrane; Single-pass membrane protein. Note=Seems to be associated with the endoplasmic reticulum and/or Golgi apparatus.
Sequence:
MVQEELWAAFSGPSGVALACCLVAAALALRWSSRRMARGAAARARQRQQAALETMDKAAQRFRLQNPDLDSEMLLALPLPQLVQKVRSGELSPEAVLFSYLQKAWEVNRGTNCVTTYLADCEAQLCQAPGQGLLYGVPVSLKECFSCKGHDSTLGLSRNQGTPAECDCVVVQVLKLQGAVPFVHTNVPQSMFSYDCSNPLFGQTTNPWMSSKSPGGSSGGEGALIAAGGSPLGLGTDIGGSIRFPSAFCGICGIKPTGNRISKSGLKGSVYGQVAVQLSVGPMARDVESLALCLRALLCEDMFRLDPTVPPLPFNEEVYASSRPLRVGYYETDNYTMPTPAMRRALLETKRSLEAAGHTLIPFLPANIPHALEALSTGGLFSDGGKRLLQNFEGDYVDSCLGDLISILRLPKWLKGLLAFMLRPLLPRLAGFLSSLRPRSAGKLWELQHEIEMYRHSVIAQWRALDLDVVLTPMLSPALDLNAPGKATGAVSYTLLYNCLDFPAGVVPVTTVTAEDEAQMEHYKGYFGDIWDKVVQKAMKRSVGLPVAVQCVALPWQEELCLRFMREVERLMAPGRQPS
The following text describes a protein:
Function:
GTPase involved in activation of the TORC1 signaling pathway, which promotes growth and represses autophagy in nutrient-rich conditions.
Sequence:
MSTSASSRKKLLLMGRSGSGKSSMRSIIFSNYSALDTRRLGATIDVELSHLRFLGNMTLNLWDCGGQTVFMDNYFTNQKDHIFKMVQVLIHVFDVESKSINKDIEIFIKSLTNLQQYSPGAKVFVLLHKMDLVQIDKRQELFEIMMEKLQKISNPYHFKLIGFPTSIWDESLYKAWSQIVCSLIPNINLFNNNLIEFNSILDAEEIILFEKTTFLVISSTASIQQQQQQQQQQQQQQQQQQQQQQQQQKSIDNDQDSTNEELDPKRFEKISNIIKTYKQSITKLRTNFKNLIIRGSNGTNFYIDIITDNMFIMIVLKDKKDTQNMIQQHEELLILDNIKAARRWFEKIENNE
The following text describes a protein:
Function:
Binds to extracellular matrix proteins. Binds to pathogen-associated molecular patterns (PAMPs) present on the cell walls of Gram-positive and Gram-negative bacteria and fungi, behaving as a pattern recognition receptor (PRR). Induces bacterial and fungal aggregation and subsequent inhibition of PAMP-induced cytokine release. Does not possess intrinsic bactericidal activity. May play a role in the innate defense and homeostasis of certain epithelial surfaces.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MIWSFADPLYGVRLVGGENRCEGRVELWKDGQWGTVCDDHWKKEIATMVCQELRCGPVMKTPAGRLYYQSCLVQHIWNPMCQGTELTLAECEEDVVDCDNHEEDAGAICGVPLHLEGTRLVNGPGPCTGRVEVKYAGEWGTVCNEDWNLQDAKVLCHELGCGRPLLTKGSCKKDQQGRGEIWLSQVKCRGSEASLRDCPTAPVGENNCTHYDDVWVQCEEPFALRLVDGGDKCSGRVEVFHKGLWGSVCNDGWGEKEDQVVCQEMKCGKALLQKSGTRKRFGLGKGQIWLDDVSCKGKEASLKQCQHRLWGRHDCTHREDVSVVCSGMLEDYGEPRLGWGVTFLSSA
The following text describes a protein:
Function:
Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation of actin at 'His-73'. Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery. Does not have protein-lysine N-methyltransferase activity and probably only catalyzes histidine methylation of actin.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Localizes mainly in the cytoplasm.
Domain:
The SET domain specifically recognizes and binds actin, suggesting that it does not accommodate substrates diverging from actin.
Sequence:
MGKKSRVKTQKSGTGATASVSPKETLNLTSELLQKCSSPAPGPGKEWEEYVQIRSLVEKIRKKQKGLSVTFDGKREDYFPDLMKWASENGASVEGFEMVNFKEEGFGLRATRDIKAEELFLWVPRKLLMTVESAKNSVLGPLYSQDRILQAMGNITLAFHLLCERADPNSFWQPYIQTLPSEYDTPLYFEEDEVRDLQSTQAIHDVFSQYKNTARQYAYFYKVIQTHPHANKLPLKDAFTYEDYRWAVSSVMTRQNQIPTEDGSRVTLALIPLWDMCNHTNGLITTGYNLEDDRCECVALRDFRAGEQIYIFYGTRSNAEFVIHSGFFFDNNSHDRVKIKLGVSKSDRLYAMKAEVLARAGIPTSSVFALHYTDPPVSAQLLAFLRVFCMTEEELKEHLLGDNALDRIFTLGNSEYPVSWDNEVRLWTFLEDRASLLLKTYKTTIEEDKSFLRNHDLSVRATMAIKLRLGEKEILEKAVKSAAANREHYRKQMQAGAPLPRCEESGTAGARLPLALRDLEAEASVQEALSLTEAVGRAKAVENGLVNGENSIPNGTRSGKENFNQEGSERATEGTKESSSDSTAGARE
The following text describes a protein:
Function:
Cytochrome P450 whose physiological substrate is unknown. In vitro, is able to catalyze the selective hydroxylation of mevastatin to pravastatin, the widely used therapeutic agent for hypercholesterolemia.
Sequence:
MKKVTVDDFSSPENMHDVIGFYKKLTEHQEPLIRLDDYYGLGPAWVALRHDDVVTILKNPRFLKDVRKFTPLQDKKDSIDDSTSASKLFEWMMNMPNMLTVDPPDHTRLRRLASKAFTPRMIENLRPRIQQITNELLDSVEGKRNMDLVADFSFPLPIIVISEMLGIPPLDQKRFRDWTDKLIKAAMDPSQGAVVMETLKEFIDYIKKMLVEKRNHPDDDVMSALLQAHEQEDKLSENELLSTIWLLITAGHETTAHLISNGVLALLKHPEQMRLLRDNPSLLPSAVEELLRYAGPVMIGGRFAGEDIIMHGKMIPKGEMVLFSLVAANIDSQKFSYPEGLDITREENEHLTFGKGIHHCLGAPLARMEAHIAFGTLLQRFPDLRLAIESEQLVYNNSTLRSLKSLPVIF
The following text describes a protein:
Function:
Transcription factor. Interacts, when in complex with WRKY71, specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Represses specifically gibberellic acid (GA)-induced promoters in aleurone cells, probably by interfering with GAM1.
Subcellular Localization:
Nucleus.
Sequence:
MSDCSTGTDSPRADSVDEQPPADAESPGGGQSKRDQPSPSSPLPPPKRSRRSVEKRVVSVPIAECGERAKTNGEGPPPPDSWAWRKYGQKPIKGSPYPRGYYRCSSSKGCPARKQVERSRADPTVLLVTYSYDHNHPWPAPKTGCHPNKSSPRLVDPKPEPGTPVECQPEQGPEAPEQEQEEEHEQKPVIGLADPAAITTVTAAAEEEEESFDFGWFDQYPTWPRTALYVPAFDVAPPPEDWERELQGEDALFAGLGELPECAIVFGRRRELALAATAPCS
The following text describes a protein:
Function:
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a variety of xenobiotic and endogenous compounds, including dopamine, T3 (triiodo-L-thyronine), T4 (thyroxine), estrone, DHEA (dehydroepiandrosterone), flavonoids, isoflavonoids and other phenolic compounds.
Subcellular Localization:
Cytoplasm.
Sequence:
MEISDFSSMKLNSRPELIDFEGISMIHYFTDNWEKVKNFQARPDDILIATYPKAGTTWVSYILDLLYFGNESPERQTSQPIYMRVPFLEACFEGIPFGTELADNLPTSPRLIKTHLPVQLVPKSFWEQNSKVVYVARNAKDNAVSYFHFDRMNMGQPEPGDWNTFLQKFMEGRNVFGPWYDHVNGYWKKKQTYSNILYMFYEDMVENTGREVERLCSFLGLSTSAAERERITKGVQFDAMKQNKMTNYSTIPVMDFKISPFMRKGKVGDWRNHFTVAQNEQFDEVYKQKMKNTTVKFRTEL
The following text describes a protein:
Function:
Acts in signal transduction. Activates CDC42 and RHO5.
Miscellaneous:
MISCELLANEOUS: Present with 1750 molecules/cell in log phase SD medium.
Sequence:
MLSFCDYFWSEDLVSGLDVLFDRLYHGCEQCDLFIQLFASRMQFEVSHGRQLFGIEAGMDNLKAVQEDEDEGVTVSRALRGILQEMSQEGTHHLTIASNIESLVLQPFSKWCIEHRERIQYSEKTLLTNVNNFRKSKKYVGKLEKEYFNKCRQLEEFKRTHFNEDELANAMKSLKIQNKYEEDVAREKDHRFFNRIAGIDFDYKTMKETLQLLLTKLPKTDYKLPLISYSLSNTNNGGEITKFLLDHMSLKDIDQAETFGQDLLNLGFLKYCNGVGNTFVNSKKFQYQWKNTAYMFANVPMPGSEEPTTGESLISRFNNWDGSSAKEIIQSKIGNDQGAAKIQAPHISDNERTLFRMMDALAASDKKYYQECFKMDALRCSVEELLIDHLSFMEKCESDRLNAIKKATLDFCSTLGNKISSLRLCIDKMLTLENDIDPTADLLQLLVKYKTGSFKPQAIVYNNYYNPGSFQNFGVDLETRCRLDKKVVPLIISSIFSYMDKIYPDLPNDKVRTSIWTDSVKLSLTHQLRNLLNKQQFHNEGEIFDILSTSKLEPSTIASVVKIYLLELPDPLIPNDVSDILRVLYLDYPPLVETALQNSTSSPENQQDDDNEEGFDTKRIRGLYTTLSSLSKPHIATLDAITTHFYRLIKILKMGENGNEVADEFTVSISQEFANCIIQSKITDDNEIGFKIFYDLLTHKKQIFHELKRQNSKN
The following text describes a protein:
Function:
Involved in serotonin biosynthesis. Catalyzes the decarboxylation of L-tryptophan to produce tryptamine, which is converted to serotonin by tryptamine 5-hydroxylase. May play a major role in serotonin biosynthesis during senescence. Accumulation of serotonin attenuates leaf senescence. Catalyzes the decarboxylation of 5-hydroxy-L-tryptophan to produce serotonin.
Sequence:
MGSLDTNPTAFSAFPAGEGETFQPLNADDVRSYLHKAVDFISDYYKSVESMPVLPNVKPGYLQDELRASPPTYSAPFDVTMKELRSSVVPGMTHWASPNFFAFFPSTNSAAAIAGDLIASAMNTVGFTWQASPAATEMEVLALDWLAQMLNLPTSFMNRTGEGRGTGGGVILGTTSEAMLVTLVAARDAALRRSGSDGVAGLHRLAVYAADQTHSTFFKACRLAGFDPANIRSIPTGAETDYGLDPARLLEAMQADADAGLVPTYVCATVGTTSSNAVDPVGAVADVAARFAAWVHVDAAYAGSACICPEFRHHLDGVERVDSISMSPHKWLMTCLDCTCLYVRDTHRLTGSLETNPEYLKNHASDSGEVTDLKDMQVGVGRRFRGLKLWMVMRTYGVAKLQEHIRSDVAMAKVFEDLVRGDDRFEVVVPRNFALVCFRIRAGAGAAAATEEDADEANRELMERLNKTGKAYVAHTVVGGRFVLRFAVGSSLQEEHHVRSAWELIKKTTTEMMN
The following text describes a protein:
Function:
Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides.
Sequence:
MKKVRLTREGYEKLKKELEDLKRKFMYEISERIKEARELGDLSENSEYEAAKNEQGRVGSRIMEIEQILSNAEIIEDSEESDEVTLGKWVVIKNLDTGEEHKFRIVTPQEADFFAQKLSSDSPLGKSLLGRKVGDVVKVKAPSGVQRYQVIAVMNK
The following text describes a protein:
Function:
Forms L-glutamate from L-glutamine and 2-oxoglutarate. Represents an alternative pathway to L-glutamate dehydrogenase for the biosynthesis of L-glutamate. Participates with glutamine synthetase in ammonia assimilation processes. The enzyme is specific for NADH, L-glutamine and 2-oxoglutarate.
Sequence:
MKLQRDLAAAALNEAECAHPEMDAELNGMNAPVYNYDVSNNDSWAGALPKEQGLYNPDFEKDACGVGFVCQIRGLRSHKIVTDARLLLCNMTHRGATGADTRDGDGAGVMTSMPHEFMAKEFKQSLNVTIPASGRYAVGNVFFSPEEDIRKAAIEEFTNIAEEAGLAILGWRSVPCDNTILGPAALSREPVILQPCVIHKAMHDGAQEFDSAVFDRQLFILRKRSTHRIGMQKWFYICSLNRETIVYKGQLAPVQVYNYFLDLNNAEYNAHFALVHSRFSTNTFPSWDRAQPMRFAAHNGEINTLRGNKNWMRAREGIMKSELFGDELQSLLPTIEKGGSDSAAFDNVLELLCLSGTLSLPEAVMLLIPEAWQTNPNISDEKSAFYEWAACQMEPWDGPALFTFADGRYCGANLDRNGLRPCRYYLTSNDIMVCASEVGTIGIDPEVVTQKGRLYPGRMLLVDTKEGRVVDDKELKHTISTRYDFRSWLDSELINMNSLVDALEDSSEVDITPEVDNTGLAEDKRLLAFGYTLEQVNMIIGPMASEGKETLGSMGNDAALACLSEKPRLVYDYFRQLFAQVTNPPIDPIRESVVMSLQCYVGPSGNLLEIEQSQCRRLCLPTPILTLEEFNAIKNINVVHPDWNVESIDITFPKNGSYVNAIDRICQEASDAVDNNKQIIVLSDRAVSAERVPIASLMAVGAVHHHLVQAKKRSRVAIVVESGDAREVHHMCMLLCYGVDAICPYLAIESIIKLHHQNALKPGVPVEKAVDNFKHSINGGIMKVMSKIGISTLQSYKGAQICEILGLDNDVVDKCFAGTASRIRGVSFDYISRDALALHERGFPTKYTISSKGLPDMGDFHYRDGGEEHVNHPKAIAQLQYAVRNRNDAAYQEFARIHQEQIRKCTLRGMLDFDYSGEGIPIEQVEPWTEIVRRFCTGAMSYGSISMESHSAMAIAMNRLGGKSNTGEGGEDPARSQRLPNGDTMRSAIKQIASGRFGVTSYYLSDADELQIKMAQGAKPGEGGELPGYKVSESIARTRHSTPGVGLISPPPHHDIYSIEDLKQLIYDLKASNPRARVSVKLVSEVGVGIVASGVAKAKADHILVSGHDGGTGASRWTGIKYAGLPWELGVAETHQTLVLNDLRGRVVIQTDGQLRTGRDVAIACLLGAEEWGFATTPLIALGCVMMRKCHLNTCPVGIATQDPELRKKFTGLPDHVVNFFYYVAEELRSIMAKLGFRTINEMVGRSDKLKVADHVINEKSKKLDLSPLLTPAFTLRPGAATYNVRKQDHRLYTRLDNKLIDEAELTLEDGIPSVIDCEIINTDRALGATLSNRISKRFGEEGLPTDSVRVNVFGSAGQSFGAFLAPGVTLQLEGDCNDYVGKGLSGGRLIVYPPKVSSFKSEENIIVGNTCLYGATSGIAFIRGVAAERFGVRNSGATAVVEGCGDHGCEYMTGGRVVILGSTGRNFAAGMSGGIAYVYDLQQDFAKKVNMEMVELCQVTDPAEIAFLRGLILDHRHYTGSEVADRILNDFLRNLPRFVKVLPRDYKAVLEREAAKKAEAKRLQYPKAFMPGNPIREQLEKNSKDEPAVADVEDVVGGAKTEQRLDKLRGFMKYQRRSEKYRNPVKRTNDWKEVSQRLREGELRLQTARCMDCGTPFCQSDYGCPISNKIFTWNDLVFKQQWKEAWNELSKTNNFPDITGRVCPAPCEGACTLGITDAPVGIKSVERAIFDKAWEEGWVVPNPPKYRTDKHIAIVGSGPAGLAAADQLNKAGHNVTVLERDSAPGGLLHYGIPNMKLDKLILKARIDLMTQEGITFETNAKVGPDGLYTIEELSEKYDAVILATGSTVPRDLQIPNRDAAGIHFAMEFLHKNTESLEKSNLLDGNYINAKGKDVIVIGGGDTGNDCLGTSVRHGAKSIKNLELLPIPPRERADDNPWPQYPRVFRVDYGHAEVQAHYGSDPREYSILTKSFEKDEEGNVKGINTVRIEWVKNSKGRWIMKEIRNSEEFFPADLVILALGFLGPDEEATSGTDIEKDGRSNIKTVERSYRTSLPNVYAAGDCHRGQSLVVWAIQEGRQCAREVDGALTGKTYLPGNGGVVQSTVLQN
The following text describes a protein:
Function:
Serine-type endopeptidase involved in atrial natriuretic peptide (NPPA) processing. Converts through proteolytic cleavage the non-functional propeptide NPPA into the active hormone, thereby regulating blood pressure in heart and promoting natriuresis, diuresis and vasodilation (By similarity). Proteolytic cleavage of pro-NPPA also plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus (By similarity). Also acts as a regulator of sodium reabsorption in kidney. May also process pro-NPPB the B-type natriuretic peptide (By similarity).
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein. Cytoplasmic vesicle; [Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment]: Secreted. Note=Soluble form produced following cleavage by ADAM10.
Sequence:
MGRVSFNVRVSSVRRARCSCPGRCYLSCRVPPTTALHALNGFGRAGVLGETAGGTVGLGPSGTRGFLSGSKFQASGSLKDCFGAPPAPDVLRADSSVGEGCPQKLVTANLLRFLLLVLIPCICALIVLLAILLSFVGTLKKVYFKSNDSEPLVTDGEVRVPGVIHVNRYENTGAPSMPPSQSIPAWTPRAPSLEDQSHGNTSTCVNITHRQCQILPYHSTLAPLLPIVKNMDTEKFLKFFTYLHRLGCYQHILLFGCSLAFPKCIVDGDDRHGLLPCRSFCEAAKEGCESVLGMVNSSWPDSLRCSQFRYHTENNSDASRICFSLQQEHGKQSLCGGGESFLCTSGLCISKKLQCNGYNDCDDWSDEAHCNCSEDLFHCGTGKCLHHSLVCDGYDDCGDLSDEQNCDCNLTKEHRCGDGRCIAAEWVCDGDHDCVDKSDEVNCSCPSQGLVECRSGQCIPSTFQCDGDEDCKDGSDEENCSDRPTPCPGGDRGCLDSSCVESCAGSSLCDSDSSLSNCSHCEPITLELCMNLPYNLTHYPNYLGHRTQKEASISWESALFPALVQTNCYKYLMFFACTILVPKCDVNTGQRVPPCRLLCEHSKERCESVLGIVGLQWPEDTDCSQFPEQSSDNQTCLLPNEDVEECSPSHFKCRSGRCVLGSRRCDGQADCDDDSDEENCGCKERDLWECPLNKQCLKHTLICDGFPDCSDSMDEKNCSFCQDDELECANHECVPRDLWCDGWTDCSDSSDEWGCVTLSKNGNSSSFLTVHRSARDHHVCADGWQETLSQLACRQMGLGEPSVTELVQGQEGQQWLRLHSSWENLNGSTLQELLVHRRSCPSGSEISLLCTKQDCGRRPAARMNKRILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGREDADVWKVVFGINNLDHPSGFMQTRFVKTILLHPRYSRAVVDYDISVVELSDDINETSYVRPVCLPSPREFLEPDTYCYITGWGHMGNKMPFKLQEGEVRIIPLEQCQSYFDMKTITNRMICAGYESGTVDSCMIDSGGPLVCERPGGQWTLFGLTSWGSVCFSKVLGPGVYSNVSYFVDWIERQIYIQTFLQKKSQG
The following text describes a protein:
Function:
Magnesium-independent phospholipid phosphatase with broad substrate specificity. Preferentially catalyzes the conversion of diacylglycerol pyrophosphate into phosphatidate but can also act on phosphatidate and lysophosphatidate. Phospholipid phosphatases are involved in both the synthesis of lipids and the degradation or generation of lipid-signaling molecules like diacylglycerol.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MMRALLEELGIRALLFGVFVFTEFLDPFQRVIQPEEIWLYKNPLVQSDNIPTRMMFAISFLTPLAVIFVVKIIVRTDRTEVKEACLAVSLALALNGVCTNTIKLIVGRPRPDFFYRCFPDGVSNEGMHCTGDASVVAEGRKSFPSIHSSFAFAGLGFTSFYLAGKLHCFTEIGQGKSWRLCAAVLPLYCAMMIALSRMCDYKHHWQDSFVGGVIGLILAYLCYRQHYPPLTHSSCHRPSVCLHQVAPQKKEQRMPTENSDGLMHEGLTEGPV