lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Subcellular Localization:
Nucleus. Chromosome, telomere.
Sequence:
MGKKRKRPVKEPVKDDPICRAKSSPQQPAGNTARSLSTNRNQAADAGKICHPVISLYYRHVVTLRQYILQRIPRSSRARRRRIAAVGGHSAARDGLAAVPKNEKDLADLLDTTLVGILKELPPTRSEERRRDFIAFTQAQQTTQTGTDSGPIVDFAISSIFNRPSHGKLENVLSHGYRQGGGRLPCSIPNVAAQFPNKNVQMLKQSPWTEVLALLGSNGDEIMLKLLLDCGLFMAVDARKGVYCQISGQAISSLKPIDTSPEDCPAAFNGSSSPVKRHAVPWQGAAPRAHTKGPKENQQQLSPNAIIFCRQRMLYARPHLNANGGITFGLPNHVLSRFHSAKSLQQTVHVMKYVFPRQFGLHNVFTSHSSYYENPLSKNYSSREEEIARKEGLEAARNQLRKSGFHAAIGERQESIKIPKRLRGKPLELIRQLQNRSRRCCYKKLLQYYCSEELSGPWILGQLSAESNSVLSTSSSRPLVTQPSLAHQDMQRELRPTSYAKGFSKGSGATKPKENLTDHATPAASVSAFCRAVIRNLIPLEFFGVGEQGITHQKMILGHVDRFIRMRRFESLSLHEVCEGIKPESLRQAPSENNISASDLQKRRELFHEFLYYLFDSILLPLIRGSFYVTESQVHRYRLFYFRHDVWRRLTAQPLAHLRASIFEELAPETAEKLLSGKKSIGYGSLRLLPKTTGIRPILNLRRRTLVRSIYAGKNRYHPAQSVNSAIAPVYSMLNYERGRRNDLLGSSMFSVGDMHSRLKKFKESLMSRGWDQRKRLYFVKLDIQSCFDTIPQAKIVRLVEKLVSEENYHWMKYVEMRLASEFDNMWPLRKPQQRRTWSKYLQRVGPVGRPENLADAIANGSVVGRRNTVLVDTIAQKEYNGEGLLDILNEHIRNNLVKIGKKYFRQRKGIPQGSVLSSLLCSLLYAEMERDVLGFLQTDDALLLRLLDDFLLVTLDSGLAMDFLRVMVRGQPDYGISVNPAKSLVNFAAVVDGAQIPRLVDTPLFPYCGSLIDTRTLEIFRDQDRMLEGADSASVALSDSLSIDSTRTPGRSFYRKVLASIKQSMHPMYLDSTHNSLPAVLLNVYKSFVTAAMKMYRYTRSLPGRARPRPEVVVRTIHDATQLGYRLIRGRHGLCRVTHPQLQYLGGAAFQFVLGRKQTQYAGVLRWLDGTLAEARQSVGNSVLLAQAVQKGNRTYREWRF
The following text describes a protein:
Function:
Degradation of glucosinolates (glucose residue linked by a thioglucoside bound to an amino acid derivative) to glucose, sulfate and any of the products: thiocyanates, isothiocyanates, nitriles, epithionitriles or oxazolidine-2-thiones.
Subcellular Localization:
Vacuole.
Sequence:
MAQKLNLPNLAVLPNVNRSSFPSTFTFGVATSAYQIEGGWNEGKKGPNIWDKFTHLEGKVLDGSNGDVAVDHYHRYKEDVELIGTLGFSAYRFSISWSRIFPDGLGTEVNEEGVAFYNNLINSLLEKGIEPFVTLYHWDLPSHLQESIGGWTNRKIVDYFGLYADACFASFGDRVKHWITLNEPLQTSVNGHCIGIFAPGRKEKPLVEPYLVSHHQVLAHATAVSIYRSKYKESQGGQIGLSVDCEWAEANSEKMEDKVAAGRRIDFQLGWFLDPLFYGDYPASMRQKLGDNLPTFTPEEREFMLQNSWDFLGVNHYTSRLIAHVSNKEAESDFYQAQELERLVEWEDGEPIGERAASDWLYVVPWGIRRTLNYISKKYNHPPIFITENGMDDEDDGSASMHEMLDDKRRVAYFKSYLANVAEAIKDGVDIKGYFAWSLLDNFEWAQGFTKRFGLVYVDYKNGLSRHPKSSAYWFMKFLKGDEDNKGKKD
The following text describes a protein:
Function:
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Sequence:
MSSLASPGRIARVFAALHARREVAFIPFITAGDPDLETTAEALLTLDRNGADLLELGLPYSDPLADGPTIQAAATRALARGTTPGAVLDLVARLTPELRAPLIVFTYFNLILAVGIEAFVERLAASGASGLLVPDLPVEEGDALQTAANVQGLDVIWLVAPTSPPERLRRIAERTTGFVYLVSTTGVTGARTQVASSVRTSLAQLRALTTRPVAVGFGISTPEQAHEVASLGADGVIVGSACVQLLATAAPEERLGQLAEFCRQLKKASQTLPVKS
The following text describes a protein:
Function:
Coordinates cell shape changes during formation of the ventral furrow and invagination of the posterior midgut primordium, by inducing apical constriction of cells in spatially and temporally defined manners. Could function as a secreted signal to initiate apical constriction by acting as a ligand for an unidentified G protein-coupled receptor, which in turn activates the G protein alpha subunit encoded by concertina, in neighboring cells. Such an intracellular pathway would ultimately induce contraction of the apical actin-myosin network. In the ventral furrow, fog appears to ensure that all the cells initiate constriction within several minutes of each other. In the posterior midgut invagination, fog appears to direct the ordered progression of constriction initiations out from a central region and also to delimit the peripheral extent of this spreading.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MSPPNCLLAVLALTVFIGANNALPITSRPIEGNVQRMVWEDWVNLDPEQRNLTKEKKITAKSIFTLPFRHCPQGHTLFNQLCIPQSNIDPTDLVKQELILAGGSNGSPPPPPIGDYDYGDDEESEEIVYDLSVIPTAMQDGLPPSVGTGDQALPSEDAPLKFNIFEKKFPTGTGEHEEMPLPPDMAAATYAKNISTTPETSTSITPTSTTTFAVPSVPSGEASNRIPGGVDLLAAPSDAFSTSTTLSMPTSNTTTTSNKDIGQVESIVLPADQEHDGLVHLVTSSLSDNDSDDSSTTLNGFNAEADLAQLLKVDAFWPVYDGSIELLPPLFSHRKVAPPLSADQDVKTKHAVDAAEKVGAELEEEVGEEEVTATDILPSEEDEYTTETATTTGDTTVAEASMDTSTATSTSGQSSPHPPEEPEIDERENRLVLIKSKVQPVQLTTTTSATATTAADVANSSSSTDRFHYQHFVEDESSTTTATPEPSSSTPGDPIEQSDMPASDNDNLMTNTIGGRGDDDDDGGHKATSEIHVQQELRLINELVKGKQRQQHQPQKQQLEPTSTEITSALTSTSTEDATTTTTTTTAYTNWSKVMPQLGQSTSETAATTETVATSGQVNEISLTATSASTEVKHFSITNRSYRNSKIIREDRLTVEPEGIVESAASTESAGTAATTPNSSSNPDGYTPLWWLPSIGWRLDRHLDGNGEDQSLLLRFFSTFRGSNTAATTR
The following text describes a protein:
Function:
Homeostatic regulator of a chemically distinct subset of diacylglycerols (DAGs) with C36 chain length that prevents the toxic accumulation of these specific DAGs in the logarithmic growth phase, which otherwise leads to endoplasmic reticulum stress. Maintains the basal level of DAG subspecies by directly facilitating DAG to triacylglycerol (TAG) conversion process, possibly via adenylation activity of its FLD domains. Does not affect the abundant DAG species (representing over 90% of total DAG pool), comprised of C32 and C34 chain lengths. Required for vacuole fusion-mediated osmoadaptation.
Miscellaneous:
MISCELLANEOUS: Present with 41 molecules/cell in log phase SD medium.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein. Mitochondrion membrane; Multi-pass membrane protein. Note=Localizes at mitochondria-vacuole contact sites.
Domain:
The fatty acyl-AMP ligase-like domains (FLDs) are essential for the redirection of the flux of DAG subspecies to storage lipid, triacylglycerols, probably via adenylation activity.
Sequence:
MDFSIPPTLPLDLQSRLNELIQDYKDENLTRKGYETKRKQLLDKFEISQMRPYTPLRSPNSRKSKHLHRRNTSLASSITSLPNSIDRRHSIYRVTTINSTSANNTPRRRSKRYTASLQSSLPGSSDENGSVKDAVYNPMIPLLPRHTGAENTSSGDSAMTDSLPLILRGRFEHYDGQTAMISINSKGKETFITWDKLYLKAERVAHELNKSHLYKMDKILLWYNKNDVIEFTIALLGCFISGMAAVPVSFETYSLREILEIIKVTNSKFVLISNACHRQLDNLYSSSNHSKVKLVKNDVFQQIKFVKTDDLGTYTKAKKTSPTFDIPNISYIEFTRTPLGRLSGVVMKHNILINQFETMTKILNSRSMPHWKQKSQSIRKPFHKKIMATNSRFVILNSLDPTRSTGLIMGVLFNLFTGNLMISIDSSILQRPGGYENIIDKFRADILLNDQLQLKQVVINYLENPESAFSKKHKIDFSCIKSCLTSCTTIDTDVSEMVVHKWLKNLGCIDAPFCYSPMLTLLDFGGIFISIRDQLGNLENFPIHNSKLRLQNELFINREKLKLNEVECSITAMINSSSSFKDYLKLETFGFPIPDITLCVVNPDTNTLVQDLTVGEIWISSNHITDEFYQMDKVNEFVFKAKLNYSEMFSWAKYEMPTNEKSQAVTEQLDTILNICPANTYFMRTKLMGFVHNGKIYVLSLIEDMFLQNRLIRLPNWAHTSNLLYAKKGNQSAQPKGNTGAESTKAIDISSLSGETSSGYKRVVESHYLQQITETVVRTVNTVFEVAAFELQHHKEEHFLVMVVESSLAKTEEESKNGETTDTTLMKFAETQRNKLETKMNDLTDQIFRILWIFHKIQPMCILVVPRDTLPRRYCSLELANSTVEKKFLNNDLSAQFVKFQFDNVILDFLPHSAYYNESILSEHLSKLRKMALQEEYAMIEPAYRNGGPVKPKLALQCSGVDYRDESVDTRSHTKLTDFKSILEILEWRISNYGNETAFSDGTNTNLVNSSASNDNNVHKKVSWASFGKIVAGFLKKIVGSKIPLKHGDPIIIMCENSVEYVAMIMACLYCNLLVIPLPSVKESVIEEDLKGLVNIIQSYKVKRVFVDAKLHSLLNDNNVVNKCFKKYKSLIPKITVFSKVKTKNALTVSMFKNVLKQKFGAKPGTRIGMTPCVVWVNTEYDVTSNIHVTMTHSSLLNASKIVKETLQLRNNSPLFSICSHTSGLGFMFSCLLGIYTGASTCLFSLTDVLTDPKEFLIGLQNLNVKDLYLKLETLYALLDRASSLIEGFKNKKENINSAKNNTSGSLREDVFKGVRNIMIPFPNRPRIYTIENILKRYSTISLSCTQISYVYQHHFNPLISLRSYLDIPPVDLYLDPFSLREGIIREVNPNDVSAGNYIKIQDSGVVPVCTDVSVVNPETLLPCVDGEFGEIWCCSEANAFDYFVCNSSKNKLYKDPFITEQFKSKMKSEVNNTLSYLRTGDLGFIKNVSCTNSQGEVVNLNLLFVLGSIHESIEILGLTHFVSDLERTVKDVHSDIGSCLIAKAGGLLVCLIRCKERHNPILGNLTTLIVSELLNKHGVILDLCTFVRTKGISPKNSSMIMEVWAKNRASIMQAWFDQKIQIEAQFGINYGENISIYLLSDYEKDNI
The following text describes a protein:
Function:
May act as a component of the auxin efflux carrier.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MIDGVAIYNIVAALVPLYVPMILAYASVLWWKIFTPEQCSGINRLVALYSVPFLNFNFLAFNNPYAMNLRFIAADTLQKVIILGALFLWSAFTKCGNLDWTITLFSLSTLPNTLIVGVPLLTAMYGDSSGSLMSQIFVMQGVVWFTLMLFLYEYRGAKSLISNQFPENGGSIASFTVDSDVNSLNGNEPLQADVEMKENGELHVVVRSHSFNNDSPCNCSTSNHCSEAEICSMQRSLSFNTTRDLKREGSKEEMSKIDQEKMSRKDACNHLSNGVKHESIDMSPNLKAMGDKEVGIVNVVQYPLSEGLKEEKIEEGDAYKKQQQMPRGSVMTRLVLTMVWRNLIRNPNTYACVLGLAWSLISFRWNIKMPSIAKGSILILSKTGTGMAMFSLGLFMALQPKTIACGKTWTTISMVARFVVGPAVIAVTSIVIGIRGVLLRVAIVQAALPQAVLSFVFAKEYNLHADIISTAVIFGTVISLPITIIYFVLLGL
The following text describes a protein:
Function:
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (Probable). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (Probable). Histone deacetylases act via the formation of large multiprotein complexes. Involved in the regulation of flowering time by repressing FLC and AGL27/MAF1 expression. Forms a histone deacetylase complex with HDA6, FLD and MSI4/FVE that represses FLC gene expression to control flowering time. Unlike its tandem duplication HDA18, HDA5 does not seem to be required for the cellular patterning in the root epidermis.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MAMAGESSGKKIGDCDGKVAGNRQRKVGLIYDETMCKHDTPDGEDHPECPDRIRVIWEKLQLAGVSQRCVVLGSSKAEDKHLQLVHTKDHVNLVKSISTKQKDYRRNRIASQLNSIYLNGGSSEAAYLAAGSVVKLAEKVAEGELDCGFAIVRPPGHHAEADEAMGFCLFNNVAVAASFLLNERPDLGVKKILIVDWDVHHGNGTQKMFWKDPRVLFFSVHRHEYGGFYPAGDDGDYNMVGEGPGEGFNINVPWDQGRCGDADYLAAWDHILIPVAREFNPDVIFLSAGFDAAINDPLGGCCVTPYGYSVMLKKLMEFAQGKIVLALEGGYNLDSIAKSSLACVQVLLEDKQIQGPPEAYPFESTWRVIQAVRKRLCTYWPSLADELSWKLINQKTPTPIILISSSDSETEDNAQGLLDQMSKLSIENPQGTLLENHQVEPASTSWRADLAKVDVWYASFGSNMWKPRFLCYIQGGQVDGLKKVCVGSMDKSPPKETVWETFPHRLFFGRESSVGWGVGGVAFTNPLANLIDQTHMCLYRITLEQFNDVLSQENGLNVDSDSPVFDLAALQLVDNKGSILEAPLNSWYGNVVCLGKERDIPILTMTCTLSAVEKFKSGEIPIRPPAKAYANTLIRGLVEGGRLSKEEAEAYIDKAVSKPL
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm).
Miscellaneous:
MISCELLANEOUS: Present with 4590 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Nuclear basket.
Domain:
Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. FG repeat types and their physico-chemical environment change across the NPC from the nucleoplasmic to the cytoplasmic side.
Sequence:
MHRKSLRRASATVPSAPYRKQIISNAHNKPSLFSKIKTFFTQKDSARVSPRNNVANKQPRNESFNRRISSMPGGYFHSEISPDSTVNRSVVVSAVGEARNDIENKEEEYDETHETNISNAKLANFFSKKGNEPLSEIEIEGVMSLLQKSSKSMITSEGEQKSAEGNNIDQSLILKESGSTPISISNAPTFNPKYDTSNASMNTTLGSIGSRKYSFNYSSLPSPYKTTVYRYSAAKKIPDTYTANTSAQSIASAKSVRSGVSKSAPSKKISNTAAALVSLLDENDSKKNNAASELANPYSSYVSQIRKHKRVSPNAAPRQEISEEETTVKPLFQNVPEQGEEPMKQLNATKISPSAPSKDSFTKYKPARSSSLRSNVVVAETSPEKKDGGDKPPSSAFNFSFNTSRNVEPTENAYKSENAPSASSKEFNFTNLQAKPLVGKPKTELTKGDSTPVQPDLSVTPQKSSSKGFVFNSVQKKSRSNLSQENDNEGKHISASIDNDFSEEKAEEFDFNVPVVSKQLGNGLVDENKVEAFKSLYTF
The following text describes a protein:
Function:
Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication.
Subcellular Localization:
Virion.
Sequence:
MATDQMDISGPPPKKQHVDTESQIPKMYEMIRDQMRTLASTHKIPLNIDHNCEVIGSIIMAACTNNRDLRPVDKYWFLMGPAGAEVMTEVEIDIQPQLQWAKGAVHDPKYKGQWYPFLALLQISNKTKDTILWQKYPVTQELEISNSLEIYANGHGIKDRLKNSRPRSVGPLVHLLHLKRLQENPPKNPKTKKPLESPAVNGIRKSIVGHLKRQCIGETQKAMINQFEMGRWESLSTFAASLLAIKPRIENHFVLTYPLIANCEDFAGATLSDEWVFKAMEKISNKKTLRVCGPDEKWISFMNQIYIHSVFQTTGEDLGVLEWVFGGRFCQRKEFGRYCKKSQTKVIGLFTFQYEYWSKPLKSAPRSIEGSKRGQISCRPSFKGKRPSYNNFTSIDALQSASGSQTVSFYDQVREECQKYMDLKVEGTTCFYRKGGHVEVEFPGSAHCNTYLFG
The following text describes a protein:
Function:
Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
Subcellular Localization:
Cytoplasm.
Sequence:
MHQHVAAPVFSSAPVSRLRLAERLQRGLWTLTGLYLLAGVVWLLLGNRMLDLAGAPQPERWSDAGFLLISSVVIHLVLRRFAQQIVEEHGELAQSLALLQAKFHALPSPAWIYDLATLRILDANPAALEFFGWERDALLEQTIHAIWPDADAGRLEEIVAQIRTKGDDTCALTEDLLTRSGLRHVEIRSNQLHLASGPARLVVTVDRSEERQAQQLRDEALNRLEEAQAIARVGSWELDRATGVGRYSPAVYRLLGRSVPMHRRDHRLEELLTASDTATQARIVRMIEDMCTGGEVQIDVLLPLVGGDSQPRTVHLRAESVTTPTGARHIHGTLQDVTEREQSRRLLREREEQFRELVRVLPDGVLILADEHVMYANAAGSAQFGFQGETILGEPLQTLVGDADLPVVREYLRAGSDRNEPVSSARAMRRRDGSTFYAGLSAGDIRYGGRDCKLLVVRDLSEPERMRDALAESNAELQAMAKRLFSLQEDERRAISRDLHDDIGQAITAMKLSAHAALDEADPVARREDLQEIVSLADSTVTKLRNLSMLLRPPQLDALGLEAALRWQASMLFRASQVRLELDIQALDERPGNEIEQACFRIAQESLTNALRHACAGEVRMSLQSIDGNGFRLEVSDDGDGFEPEGPRGLGLIVMRERAQTVGGALAIESAPGAGTRVTLRLPYHPVGESVPEDGGR
The following text describes a protein:
Function:
Essential for the assembly of ubiquinol-cytochrome c reductase. It has a direct effect on the correct occurrence of the Rieske protein, core 4, core 5 and apocytochrome b (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MAAKKPVNWWLWTKMLLGGAAICVGGPAFTYWLTPTDEELFQKYNPELQKRSLERRFERQQEFDDFVTKLKEYSKSDKPIWTVQAEAEEKERQQRASVQKSLALADEVKARKEAMRREAGLPLEK
The following text describes a protein:
Function:
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Subcellular Localization:
Nucleus.
Sequence:
MEGSISSIDQESTTSDSLSIAPAASSSTMIKSSTTIKLPPESGLCRMGSGTSVIIDAENGVEAESRKLPSSRYKGVVPQPNGRWGAQIYEKHQRVWLGTFNEENEAARAYDIAAQRFRGRDAVTNFKPLLENQESDDMEIAFLNSHSKAEIVDMLRKHTYIDELEQSKRLFGFTKDGMIKRKDGLVISSFFGSTNDKVNCKAREQLFEKVVTPSDVGKLNRLVIPKQHAEKHFPLQNGNNSKGVLLNFEDLNGKVWRFRYSYWNSSQSYVLTKGWSRFVKEKNLKAGDIVSFQRSTSGDKQLYIDFKAKNVGNTSMVVTNQVQAQVQVPLVQMVRLFGVNICKVPANVSNVIILGGFCFEVFTEFGSFVGNNANFSKKLVIYAKRLSGLEEALRIRRERELRGSTTATRRPPLRRGRVSQRLPVPDDIPKPPYVGSRELPEISSEHQIHDAEGIARMRAACELAARVVDYAGTLVRDPKCTLDVSTQKFICYHLITVAHSASLIPSVTTNEIDKAVHQMIIDAGAYPSPLGYGGFPKSVCTSVNECMCHGIPDSRQLQDGDIINIDVTVYLNGYHGDTSKTFFCGDVSESIKRLVKVTEECLHYGIAVCRDGALYRKIGKRISEHAEKFGYGVVDRFVGHGIGTVFHSEPLIFHHQPILTLGSTECVTWEDNWTTLTADGSPAAQFEHTILITKTGAEILTTY
The following text describes a protein:
Function:
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MASSTTATLSIAVATAAMKTTTLSSLPFNQSVFGLKSQRKGRFTMASHKVTLITPSGTKQFDCSDGDYILDRAEEVGMDLPYSCRAGACSSCAGLIKQGTVDQSDNSFLDDELIDAGFVLTCVAIPKSDVIIETHKEEDLVS
The following text describes a protein:
Function:
Sinapate glucosyltransferase (SGT) required for the biosynthesis of the glucose ester sinapoylglucose and subsequently sinapoylmalate and sinapoylcholine. Is the major SGT activity in plant. Plays an important role in sinapoylation of anthocyanins. Sinapoylglucose produced by UGT84A2 is a significant source of sinapoyl moieties for anthocyanins. Indole-3-butyric acid (IBA)-specific glucosyltransferase that catalyzes the glucosylation of the auxin IBA, but not indole-3-acetic acid (IAA). May be involved in flowering regulation through IBA-mediated transcriptional repression of the auxin-response factors ARF6 and ARF8 and downstream flowering pathway genes. Can glucosylate the phytotoxic xenobiotic compound 2,4,5-trichlorophenol (TCP).
Miscellaneous:
MISCELLANEOUS: Ectopic expression of UGT84A2 causes delay in flowering increase of indole-3-butyric acid (IBA) level, down-regulation of the auxin-response factors ARF6 and ARF8, and down-regulation of the flowering-related genes FT, SOC1, AP1, and LFY.
Sequence:
MELESSPPLPPHVMLVSFPGQGHVNPLLRLGKLLASKGLLITFVTTESWGKKMRISNKIQDRVLKPVGKGYLRYDFFDDGLPEDDEASRTNLTILRPHLELVGKREIKNLVKRYKEVTKQPVTCLINNPFVSWVCDVAEDLQIPCAVLWVQSCACLAAYYYYHHNLVDFPTKTEPEIDVQISGMPLLKHDEIPSFIHPSSPHSALREVIIDQIKRLHKTFSIFIDTFNSLEKDIIDHMSTLSLPGVIRPLGPLYKMAKTVAYDVVKVNISEPTDPCMEWLDSQPVSSVVYISFGTVAYLKQEQIDEIAYGVLNADVTFLWVIRQQELGFNKEKHVLPEEVKGKGKIVEWCSQEKVLSHPSVACFVTHCGWNSTMEAVSSGVPTVCFPQWGDQVTDAVYMIDVWKTGVRLSRGEAEERLVPREEVAERLREVTKGEKAIELKKNALKWKEEAEAAVARGGSSDRNLEKFVEKLGAKPVGKVQNGSHNHVLAGSIKSF
The following text describes a protein:
Function:
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular Localization:
Cytoplasm.
Sequence:
MQQHEKRRIRGCDLVPREKFEKLEGVVRKIYSQIGVIKEDGLWMPIYPETEKTLGYCFIEYNTPQEAELAKEKTHGYKLDRAHIFAVSMFDDFDRFMKVPNEWAPPETKPYTPGENLQDWLTDAKARDQFVIRAGSDTEVLWNDARHLKPDPVYKRAFGQSFVQWSPLGTYLATVHRQGAAVWGGAASFNKLMRYSHPQVKLIDFSPGEKYLVTYISHEPSNPRDANRVVINIFDVRTGKVMRDLGSADDFAVGGAGGVTGVSWSVFKYYLVKVENIMDFCWSSTDPIIALVVPDMGGGNQPARVSLIQIPSKEELRQKNLFSVGDCKITYTGFELFRIKERDIPIEVLELENKNDKIIAFAWEPKGHRFAVIHGDNPKPNVIYSMRTGQNSQVSKLTTLKGKQANALFWSPAGRYIVLAGLKGFNGQLEFYNVDELKTMATAEHFMATDIEWDPTGRMVSVWSFNGKHLYRILKDHLFQFLWRPRPPSFLTPEKEEEIAKNLKKYSIYEAEDQDVSLPLSEQEREKCRMLKEDWDKWVNEWKQIHEESLQRQKLRDGEASDEEEEYEAKDMEVEEVMDVTEEVLHLEYGHWSRV
The following text describes a protein:
Function:
Binds S-adenosyl-L-methionine (AdoMet).
Sequence:
MNITPFPTLSPATIDAINVIGQWLAQDDFSGEVPYQADCVILAGNAVMPTIDAACKIARDQQIPLLISGGIGHSTTFLYSAIAQHPHYNTIRTTGRAEATILADIAHQFWHIPHEKIWIEDQSTNCGENARFSIALLNQAVERVHTAIVVQDPTMQRRTMATFRRMTGDNPDAPRWLSYPGFVPQLGNNADSVIFINQLQGLWPVERYLSLLTGELPRLRDDSDGYGPRGRDFIVHVDFPAEVIHAWQTLKHDAVLIEAMESRSLR
The following text describes a protein:
Function:
Sodium-dependent, high-affinity amino acid transporter that mediates aspartate uptake. Has only very low glutamate transport activity. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions, resulting in electrogenic transport. Na(+) binding enhances the affinity for aspartate. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport. In contrast to mammalian homologs, transport does not depend on pH or K(+) ions.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
Contains eight transmembrane regions plus two helical hairpins that dip into the membrane. These helical hairpin structures play an important role in the transport process. The first enters the membrane from the cytoplasmic side, the second one from the extracellular side. During the transport cycle, the regions involved in amino acid transport, and especially the helical hairpins, move vertically by about 15-18 Angstroms, alternating between exposure to the aqueous phase and reinsertion in the lipid bilayer. In contrast, regions involved in trimerization do not move.
Sequence:
MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYADAVKTYVKPFGDLFVRLLKMLVMPIVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQQFQPKQAPPLVKILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSAETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVKVVGELAKVTAAVYVGLTLQILLVYFVLLKIYGIDPISFIKKAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYSFTLPLGATINMDGTALYQGVCTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGAIMLAMVLESVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGDLTGTAIVAKTEGELEKGVIA
The following text describes a protein:
Function:
Regulatory subunit that interacts with and increases the activity of different structure-specific endonucleases. Has several distinct roles in protecting genome stability by resolving diverse forms of deleterious DNA structures. Component of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for simple Y, 5'-flap and replication fork-like structures. It cleaves the strand bearing the 5'-non-homologous arm at the branch site junction and generates ligatable, nicked products from the 5'-flap or replication fork substrates. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. Has Holliday junction resolvase activity in vitro. Interacts with the structure-specific RAD1-RAD10 endonuclease and promotes RAD1-RAD10-dependent 3'-non-homologous tail removal (NHTR) during repair of double-strand breaks by single-strand annealing. SLX4 also promotes recovery from DNA-alkylation-induced replisome stalling during DNA replication by facilitating the error-free mode of lesion bypass. This does not require SLX1 or RAD1-RAD10, but probably RTT107.
Miscellaneous:
MISCELLANEOUS: Present with 274 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MELQRAQRNLKFLQNEDYVNVTDQTNLNGESQNAYSLGMETQVPEMQFSLSSDDDSIGTQVKSVTAQKSPMTQETTKNDTERNKDVDKSCNPVSTSHPDLGGSNIEENIFINTQIQSRLDDAEEETNLKLKLEKFKYSFKSSNADDTHSNANVTAKRRPAIRKANSKLKTKPKTKRDPKIIKNITDFNINNYERSRTASLLKQLSGKHKKVLDIIKTQNEGNSDKPPRARNNKGEKATFDTYSEQEWKDIMKLLLQKFPQSEETDLNEVQKFLYGSEKSSNSLDNQESSQQRLWTASQLPPELPDEAIQPEQEERIRDTQSAVNFLSLSQVMDDKSEIMKDEESIIISRGDSTSSQEYGNGLEPQQPVGNVVGEDIELAVGTRINAFSLTDYKACKPMSVEVSRRCENSTDNDYDNISIVSDTTDETSTLFPLDQYRYVFIENDERPPLATDTIGSTQFFTPNTSPLDGIIDLTQESFKAVRSLISPLKVENNKTGVTSQASNQVQVPATRTPTIIPQKNLTTTLKTEEEKNNIGSSIRVKLLQESVVKLNPKLVKHNFYRVEANDSEEEETEFDDQFCIADIQLVDSSKISTKDSTQNPTTSNDIIDTSAASSIASPEKFCEIMMSQSMKELRQSLKTVGLKPMRTKVEIIQSLQTASQILSTANPDNKGEHGGVANFSKIEIFDHLTELIEAFPDFLERIYTFEPIPLNELIEKLFSAEPFVSQIDEMTIREWADVQGICLRNDKK
The following text describes a protein:
Function:
Vacuolar Fe(2+) uptake transporter.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Sequence:
MDSPKSIEACGKKDSHATAQEEKTIEKLARAQWLRAAILGANDGLLSTTSLMLGVGAAKDQDQRSMVLSGIAGALAGACSMAVGEFVSVSTQRDIAKSIAYELKGSSSTNIAETKQGEVPHDMVFHSKLATSTQGGKLLYESPVRIQSNSLTPSRSPLTKVMEFDARRTMMEESKQDNAIKLEPLPSPLKSAAASSLAFLFGAFVPMMPALLVSENRIRIFLMVLVASLALCLFGGIGAYLGGSSVKISAMRVLLGGWISMALSYGLLKPFAHDD
The following text describes a protein:
Function:
Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MRTRHLVGLISGVLILSVLLPVGLSIWLAHQQVETSFIEELDTYSSRVAIRANKVATQGKDALQELERWQGAACSEAHLMEMRRVSYSYRYIQEVAYIDNNVPQCSSLEHESPPDTFPEPGKISKDGYRVWLTSHNDLGIIRYMVAMGTAHYVVMIDPASFIDVIPYSSWQIDAAIIGNAHNVVITSSDEIAQGIITRLQKTPGEHIENNGIIYDILPLPEMNISIITWASTKMLQKGWHRQVFIWLPLGLVIGLLAAMFVLRILRRIQSPHHRLQDAIENRDICVHYQPIVSLANGKIVGAEALARWPQTDGSWLSPDSFIPLAQQTGLSEPLTLLIIRSVFEDMGDWLRQHPQQHISINLESPVLTSEKIPQLLRDMINHYQVNPRQIALELTEREFADPKTSAPIISRYREAGHEIYLDDFGTGYSSLSYLQDLDVDILKIDKSFVDALEYKNVTPHIIEMAKTLKLKMVAEGIETSKQEEWLRQHGVHYGQGWLYSKALPKEDFLRWAEQHL