lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Sequence:
MVKAILLDIEGTIAPLSFVKEVMFPYSKKKLREFLEKNWEKPEIKKIVQEVEKIEGRELSLEEAVQLFSRWIDEDRKITPLKELQGHIWEEGFKSGELKAPLYEDAYEKIKEWKEKGIPVYIYSSGSVKAQNLFFGHSVYGDIRNLFSGFFDTKIGSKRERSSYEKIAKEIGLPPHEILFISDNPEELKAAKEAGMKVIQSVREGVEPSGDFEKITSFRELEI
The following text describes a protein:
Function:
Lipid droplet-associated protein which plays a role in lipid droplet clustering.
Subcellular Localization:
Lipid droplet.
Sequence:
MTDVEQPVSVEDQQAQAQSYYDQVLGNAYVQTAINAYTKTKEFHPLLNSTLNSAEEKVSTVGNYAAQKAYDGYNSYYVKPKNTAYEAVSYGTERAKTAVESGKQAAIVGGTFGIGAAVVLTQFSLALSAGGAALVLEQVDSAKKLGSSAISTIKEAELAVEHRIFSALHQAQRIAMVPVEKITENTNSLLDILDGAVQKGLNIEVPPSVNLTIGQRVKNLASLIVQGVSNKLFKAHDHVIDPINERARNYLEQLSQSFVLLDIVREKKTWVIEKSNELSTSVFDFKKTLEEEAQKYKVAPEEMLMKHIQSTSEQLSTQLQSLREKGQNVFGDGTKIDSTIDYLENLKKNFTDAEDVYKVRDEVLNEGRQRIAELSTWTTSLLIISAEWQFEPEDLLIEELYFDAPPPVRTRNLYRNRA
The following text describes a protein:
Function:
RAF-like protein kinase acting as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process. Photosynthesis signaling kinase involved in the regulation of the sucrose metabolism involving PGM1. Necessary for optimal chloroplast electron transport rate (ETR).
Subcellular Localization:
Cytoplasm. Note=Broadly distributed to both membrane-associated and intracellular punctate structures.
Sequence:
MVVREAMIVPQTVQGGGKGVNGCSLVSNYQNSRDLCLQSAAMEQKSKGVIENCNLGPHDVGVGWKRNSSEGSISSMDSLPCGETVFSPSDPHNSVFRKPRRLGVSESDDESVIDQSQEESLLRKSKRSVMGGTVQPHSAMAQSVDEAAPDHSSTPSDDGKDFPSSRVKFMCSFGGKILPRPSDQQLRYVGGQTRIIGINRDVNFSELRNKMRESFGQCYTFKYQLPDEDLDALVTVSSDEDLENMMEEYDKLEADGSSRLRVFLFPADQDATSFDIDSTGDLRNSEQRYVDAVNGIAESSTRRISDGVLGASPVSSDLLGLELSEPSWGLARGPDAVPMAMLATHHDPNLIHQVPVAHPVSALTGNLSNRSNAPSAPSSAPSSPPLLARNLHGKLPLVGELHQFQYLQDSQFKGVGPQYTGMPSEVAHQDSESYGGSGGSSAASQHEMHYRSTDSRRGPESPPKKFHDALHQDHPITVEQRRLSGTKMPRIGSHGKLTRLSEHSELAPSSRVDSQQMPDIHMAPGELQRLFPQQVPLQQTLWPHAMDTQQDSYRRPDMLQSSGAQPAVSGQQQQGYQPQQQLQHLFRSGLSQTGANHEGAYRQGDQQQQSQQFQEDLHVNPNYIPRSVSSHAIAAGIAAGQSTSYHGSAPSSPRPGFRELPSRHLPGGPQLQHQWTFNGAGYVDQGFGRRVMNYPDQATRSFRLSSSPPRYRDHHPHSEERLHRQAQQVSEPLHHEQVPVSGQLKFETNSVSQAQYDLVPRPQVPQYKGHNPFQEKITSFQDHQEVGDIRRHVLQQGKDNQLLAGQQHLHSILQPQRIDYQESLKQQGDQSIPIHPRFQDGQEKVAEWMVQERALEEEEARKRVLGRIRQAELEEEAAAEAVVSQHKDTHQGVYAGLHLPNDEDLLTSSLGDYPSGNRRNERLESSISNAFPFRHLPPSVLGGYTAPKSRVNPTETSHVAQYVSRPVDTDYLAVAGLRGGGNGQDMRSAALFEVNGLQQTSGYQMPSGPHRLMEERLMPSAFNPITQLQKLRINDNLALNNDMRWSGSEDVRNEPSIPARDRMGGIYEDHHQGLPGLTLGRSAGKLSRPSSNTSIPNLLDETIGEGSLLPSGPSYGTQAQGTNLIDITQSISAIDNPLYSTSYASRLSNTSLGLDSPLVTSGGMLNSSLEGTSFSDYYKIKMGDDLPNAKMPSSKIPSAEDNLSRSSSSSLSELSKSGSEDGLGGQLTMDQRTVDMVVAALDLDRSGSVVQSVLESSDAKEASLSESVHDHSLGKLGSVVGSVGTQSVWPLDSAPTLAAGLWEKKLDEAGMTEETFERHITSDGTTFEELTADDHEVLASTVDKENQEEVRTGLDEPADEDKANSTGLGSDPAAKAIARGLQTIKNADLEELRELGSGTFGTVYHGKWRGTDVAIKRIKASCFAGRPSEQERLIEDFWREACNLGHLHHPNVVAFYGVVADGPGGTLATVTEYMVNGSLKQVLQKKDRTIDRRKRLLIAMDAAFGMEYLHGKNIVHFDLKCENLLVNMRDPHRPICKVGDLGLSKVKHQTMVSGGVRGTLPWMAPELLNGNSSLVTEKVDVFSFGIVMWELLTGEEPYDKMHYGAIIGGIVNNTLRPLIPSWCDPAWRSLMERCWANEPAVRPSFSDIAKELRTMAAALQPKTQAQTQGQSHPHPQMQIV
The following text describes a protein:
Function:
Isomerase that catalyzes the conversion of deoxy-ribose 1-phosphate (dRib-1-P) and ribose 1-phosphate (Rib-1-P) to deoxy-ribose 5-phosphate (dRib-5-P) and ribose 5-phosphate (Rib-5-P), respectively.
Subcellular Localization:
Cytoplasm.
Sequence:
MSKFNRIHLVVLDSVGIGAAPDANNFVNAGVPDGASDTLGHISKTVGLNVPNMAKIGLGNIPRETPLKTVAAESNPTGYATKLEEVSLGKDTMTGHWEIMGLNITEPFDTFWNGFPEEILTKIEEFSGRKVIRETNKPYSGTAVIYDFGPRQMETGELIIYTSADPVLQIAAHEDIIPLDELYRICEYARSITLERPALLGRIIARPYVGEPGNFTRTANRRDLAVSPFSPTVLDKLNEAGIDTYAVGKINDIFNGAGINHDMGHNKSNSHGIDTLLKTMGLAEFEKGFSFTNLVDFDALYGHRRNAHGYRDCLHEFDERLPEIIAAMRENDLLLITADHGNDPTYAGTDHTREYIPLLAYSPAFKGNGLIPVGHFADISATVADNFGVETAMIGESFLDKLV
The following text describes a protein:
Function:
NodD regulates the expression of the nodABCFE genes which encode other nodulation proteins. NodD is also a negative regulator of its own expression. Binds flavonoids as inducers.
Sequence:
MNQDVIDIRLLEAFAAVMSAGSITGAARLLGRSQPVVTRQIQDLEADVGYLLFTRNGPRISPTPKGVLFHAEVERLLMGLKHIRQRANAIGAGALPVLSLAAIPALAAGFVPAALAALERKLLPSQVHVQALSAENVVQSVLSQSVDFGLASLPIQHPGLDMQWVCEVPCVACLAMDHPLAKKKVIRLRDLAGVRLLTMANPYRLRRRVEEALEREGVVPAEVIDTNASLTAIAMAKQSLGIAVVEPVLTSSLPVEGVVTRPLDVSIPFLFAAIAPTGRELTPTVAALNDALRAAVALMPGAKLHSGAAALAEAGDETSEFEKAPS
The following text describes a protein:
Function:
Regulates high density lipoprotein (HDL) cholesterol metabolism by promoting the ubiquitination and degradation of the oxysterols receptors LXR (NR1H2 and NR1H3).
Sequence:
MDAVWACRLRGRGNRVAALRPRPRRGGSAGQSPFSLPCAGLSPEPRAGVGSEFPAWFLGGSSRRRNMALVGSRAELEADEDIFEDALETISISSHSDMATSSLHFASCDTQQAPRQRGASTVNSSSSTKVDLKSGLEECAVALNLFLSNKFTDALELLRPWAKESMYHALGYSTIVVLQAVLTFEQQDIQNGISAMKDALQTCQKYRKKYTVVESFSSLLSRGSLEQLSEEEMHAEICYAECLLQKAALTFVQDENMINFIKGGLKIRTSYQIYKECLSILHEIQKNKLQQEFFYEFEGGVKLGTGAFNLMLSLLPARIIRLLEFIGFSGNRELGLLQLREGASGKSMRSALCCLTILAFHTYISLILGTGEVNVAEAERLLAPFLQQFPNGSLVLFYHARIELLKGNLEEAQEVFRKCVSVQEEWKQFHHLCYWELMWINVFQQNWMQAYYYSDLLCKESKWSKATYVFLKAAILSMLPEEDVVATNENVVTLFRQVDSLKQRIAGKSLPTEKFAVRKARRYSASLPAPVKLILPALEMMYVWNGFSIVSKRKDLSENLLVTVEKAEAALQSQNFNSFSVDDECLVKLLKGCCLKNLQRPLQAELCYNHVVESEKLLKYDHYLVPFTLFELASLYKSQGEIDKAIKFLETARNNYKDYSLESRLHFRIQAALHLWRKPSSD
The following text describes a protein:
Function:
Auxiliary factor required, together with HCF173, for the biogenesis of photosystem II (PSII), especially for the synthesis of the reaction center proteins (e.g. D1), via the regulation of the corresponding mRNA (e.g. psbA) translation initiation (ribosomal loading) and stabilization. Forms a trimeric complex with OHP1 and OHP2 that is required to promote PSII core subunit assembly. The trimeric complex forms a transient PSII reaction center-like complex with PsbA, PsbD, PsbE, PsbF and PsbI subunits in thylakoids for early assembly of PSII as well as PSII repair. The trimeric complex is required for the recruitment of ribosomes to the psbA mRNA during PSII biogenesis and repair.
Subcellular Localization:
Plastid, chloroplast stroma. Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side. Note=Predominantly present at thylakoid membranes.
Sequence:
MASLRLPAQLVTRGNLIHHNSSSSSSGRLSWRRSLTPENTIPLFPSSSSSSLNRERSIVVPVTCSAAAVNLAPGTPVRPTSILVVGATGTLGRQIVRRALDEGYDVRCLVRPRPAPADFLRDWGATVVNADLSKPETIPATLVGIHTVIDCATGRPEEPIKTVDWEGKVALIQCAKAMGIQKYVFYSIHNCDKHPEVPLMEIKYCTEKFLQESGLNHITIRLCGFMQGLIGQYAVPILEEKSVWGTDAPTRVAYMDTQDIARLTLIALRNEKINGKLLTFAGPRAWTTQEVITLCERLAGQDANVTTVPVSVLRVTRQLTRFFQWTNDVADRLAFSEVLSSDTVFSAPMTETNSLLGVDQKDMVTLEKYLQDYFSNILKKLKDLKAQSKQSDIYF
The following text describes a protein:
Function:
Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates degradation of glutamate receptors in neurons. The BCR(kel-8) ubiquitin ligase complex mediates ubiquitination and subsequent degradation of rpy-1. Indirectly regulates the protein turnover of glr-1, possibly via ubiquitination and degradation of rpy-1.
Subcellular Localization:
Synapse. Note=Localizes to postsynaptic clusters.
Sequence:
MPVYAKAIFGSFPSVQQVRVENGERCLIEAMDELNKNEKGLYRPVRLENGDQISTTDDVLNGKLARVSYTPFEEFELVSNSKGSCMEYENQEQSSKIMEQMRILRQTEELCDVELLVAGSVIRAHRYILAAASPYFKAMFTNGMVEMKKLTIELQDIPEESVRIIVDYIYTDKIAITMNNVHQLIFTATVLQMDVIVVACQQFLATMITSHNCMSLYHFSDIYNCTNLISSIEDFASSQFRCIRKSPEFNSISFHHLKSLLNRSDLNVSEEQDVFETIVQWVSSNPRDRQHHFVQLFKTLRLHLVGWNFLCEAVNSNSYVKNSQECREIISAMVLDAMTPSKRKHPESNHENTSEYSASMACPSLTASSSSSTSTFRKSVAGAIFCAGGRGKAGGPFSSVEAYDWRRNQWIEVPDMMSQRRHVGVVSANGNLYAIGGHDGTAHLATAEAFQPSIRQWKRIASMKTARRGIAVASIENVIYAVGGLDDTTCYKTVERYDIEEDEWSTVADMDVQRGGVGVAVIGRYLFAIGGNDGTSSLETCERFDPMIDKWKRIASMKNRRAGSGVCVLDGYLYAIGGFDDNAPLETCERYDPDADKWITLDKMSSPRGGVGVAALGGKVYAIGGHDGSDYLNTVECYDPIANRWQPAAEIKECRAGAGVAWANVRMHQLSRTPEKCDSGCAPSGGSYCI
The following text describes a protein:
Function:
Bacteriocin with specific antibacterial activity against strains of P.freudenreichii. No antibacterial activity was detected against P.acidipropionici, P.jensenii and P.thoenii.
Subcellular Localization:
Secreted.
Sequence:
MNTKAVNLKSENTTKLVSYLTENQLDEFIRRIRIDGALVEEVSQNAKQALDNTGLNGWINTDCDEGLLSDFISKIASARWIPLAESIRPAVTDRDKYRVSCWFYQGMNIAIYANIGGVANIIGYTEAAVATLLGAVVAVAPVVPGTPTPPKDKSSQYKEVPLAVRLSETYHEEGVRGLFDELNYSESRMISTLRRASTDGVLINSWNDGQDTILLKKYNFQDLQLTVRSRIVGNQTIIEECKITDGRKTLSDETV
The following text describes a protein:
Function:
Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.
Sequence:
MSANPLQSLKIRIQSQKDELDKIKDDLELKCKEVDDEKMKRSSIELELTALCRRLKLIEQEYNLAQSRLESAKEKLNSLVETAELSENHRKMYESQVSVSDDRSTSLDQLVKESKERANNAEIKMNEASRKLKMLLNELDRAEERATEAERAKVVTARFENVCNMAIESRYLAIVKPNNLMEFV
The following text describes a protein:
Function:
Regulates the composition and fluidity of the plasma membrane. Inhibits the incorporation of membrane-fluidizing phospholipids containing omega-3 long-chain polyunsaturated fatty acids (LCPUFA) and thereby promotes membrane rigidity. Does not appear to have any effect on LCPUFA synthesis.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MRQLAELLTDLLGPVPTMFLWVIVSFAFFRALQFIVRWYLFGKWTWPNFNFFDIRNRIRRRRRGGQEAENTENPPENEAEAGEQVEQEPEPDSRDLSAIPPNKKWRISNECVSLFHSVISGLWAAYALLYYKQLVQDLVNYRCDVAINLVLMSAGYLFHDLVDLLVNEQSARIIELLFHHVVVLSAFAVTMFFNRFLGVVVFGLLMELNSIFLHSRSLLNLYGVDKKSPSFRIIALLNMVTLFAFRLCVSAYLVYFVVVSIPDLEWYVSIINGLVIASLASTNTVLTYRLLAADGLLGSRRTRRTPAATAETQVGDVESGPLRTQVEDEDHHTIGVQTIHGTTEDATQTV
The following text describes a protein:
Function:
Displays inhibitory activity against calcium carbonate precipitation, binds calcium and affects crystallization of calcium carbonate in vitro. May be involved in calcification of the prismatic layer of the shell.
Sequence:
MRSLLVLLALAACASAQYFFRGGDDDNGFFGGDDDNGYFGYFPRFSYPIYRPIYRPIYYPQIIRPFYGYGYGGFNGGYGGLGLYGGYGGFGGYGYRPFSYGYNPFSYGYYGFGDDDGGFDD
The following text describes a protein:
Function:
Has a major role in enamel formation. Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MATAGNPWGWFLGYLILGVAGSLVSGSCSQIINGEDCSPHSQPWQAALVMENELFCSGVLVHPQWVLSAAHCFQNSYTIGLGLHSLEADQEPGSQMVEASLSVRHPEYNRPLLANDLMLIKLDESVSESDTIRSISIASQCPTAGNSCLVSGWGLLANGRMPTVLQCVNVSVVSEEVCSKLYDPLYHPSMFCAGGGHDQKDSCNGDSGGPLICNGYLQGLVSFGKAPCGQVGVPGVYTNLCKFTEWIEKTVQAS
The following text describes a protein:
Function:
Involved in DNA repair and mitotic recombination. May play an active role in recombination processes in concert with other members of the RAD52 epistasis group.
Subcellular Localization:
Nucleus.
Sequence:
MRRSAAPSQLQGNSFKKPKFIPPGRSNPGRSNPGLNEEITKLNPDIKLFEGVAVNNTFLPSQNDLRICSLNLPSEESTREINYRGNCSGKYCFEAPTLATLDPPHTVHLAPKEVAVSKEQEEKSDSLVKYFSVVWCKPSKKKHKKWEGDAVLIVKGKSFILKNLEGKDIGRGIGYKFKELEKIEEGQTLMICGKEIEVMGVISPDDFSSGRCFQLGGGSTAISRSSQVARKCFSNPFKSVCKPSSKENRQNDFQNCKPRHDPYTPNSLVMPRPDKNHQWVFNKNCFPLVDVVIDPYLVYHLRPHQKEGIIFLYECVMGMRMNGRCGAILADEMGLGKTLQCISLIWTLQCQGPYGGKPVIKKTLIVTPGSLVNNWKKEFQKWLGSERIKIFTVDQDHKVEEFIKSIFYSVLIISYEMLLRSLDQIKNIKFDLLICDEGHRLKNSAIKTTTALISLSCEKRIILTGTPIQNDLQEFFALIDFVNPGILGSLSSYRKIYEEPIILSREPSASEEEKELGERRAAELTCLTGLFILRRTQEIINKYLPPKIENVVFCRPGALQIELYRKLLNSQVVRFCLQGLLENSPHLICIGALKKLCNHPCLLFNSIKEKECSSTCDKNEEKSLYKGLLSVFPADYNPLLFTEKESGKLQVLSKLLAVIHELRPTEKVVLVSNYTQTLNILQEVCKRHGYAYTRLDGQTPISQRQQIVDGFNSQHSSFFIFLLSSKAGGVGLNLIGGSHLILYDIDWNPATDIQAMSRVWRDGQKYPVHIYRLLTTGTIEEKIYQRQISKQGLCGAVVDLTKTSEHIQFSVEELKNLFTLHESSDCVTHDLLDCECTGEEVHTGNSLEKFIVSRDCQLGPHHQKSNSLKPLSMSQLKQWKHFSGDHLNLTDPFLERITENVSFIFQNITTQATGI
The following text describes a protein:
Function:
RNA helicase.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MTSISISSDKWQTADVEVMDGDFDDDMLQFLGSFEEVLPETVDKVSERKLKKTSKKQKKKEENTVGSKNPENEEKSIEERRLAKKLKRKEQMAANRKQRKERLARRKEQKELEKGQESMETPIENGKKKRKGGEIQENNDKKKKAKKETDVSAWKQFYFLPNEILEAIEQMGFSQPTEIQSAVLPIAVRDRQDVLGAAETGSGKTLAFGIPLVSRLLEALSNKEEEEPPKGPRALIVAPTRELVIQIMRHINSLIATTPLKAVSIVGGLAQVKQERVISQQNPDIVVATPGRLWAMIQVSVSGIFQYSPPKHSNITPGHKCWNTPPPTIFHKVGGGVQKMFFLIFCLKIKRTQPNYA
The following text describes a protein:
Function:
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.
Sequence:
MLQKGEQFPIFKLENQDGTVITNDTLKGKKAIIYFYPRDNTPTCTTEACDFRDNLEMFNDLDVAVYGISGDSKKKHQNFIEKHGLNFDLLVDEDFKLAKETGVYQLKKSFGKESMGIVRTTFIIDEQGKVLDVIEKVKVKTQIEELKNILG
The following text describes a protein:
Function:
Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes retinyl esters (By similarity). Hydrolyzes p-nitrophenyl butyrate (PNPB), triacylglycerol and monoacylglycerol. Shows higher activity against PNPB, a short-chain fatty acid ester, than against triolein, a long-chain fatty acid ester. Shows no detectable activity against diacylglycerol, cholesterol ester or phospholipids. May play a role in adipocyte lipolysis.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Subcellular Localization:
Lipid droplet. Cytoplasm, cytosol. Endoplasmic reticulum. Microsome.
Sequence:
MFLSTLFLVSLATCVICGNPSSPPVVDTAHGKVLGKHVNVEGFSQPVAVFLGIPFAKPPLGSLRFAPPQPAEPWSSVKNATTYPPMCSQDAARGQAVNDLITNRKEKIHLEFSEDCLYLNIYTPADFSKNSRLPVMVWIHGGGLKLGGASSFDGRALSAYENVVVVAIQYRLSIWGFFSTGDEHSRGNWGHLDQVAALHWVQDNIANFGGDPGSVTIFGESAGGYSVSILILSPLSKNLFHRAISESGVAFIPGMFTKDVRPITEQIAVTAGCKTTTSAVIVHCMRQKTEEELLEIMHKLNLYKLSLQGDTKNSDQFVTSVLDGVVLPKDPKEILAEKNFNTVPYIVGINKQECGWLLPTMTGFLPADVKLDKKKAIALLEQFASMTGIPEDIIPVAVEKYTKGSDDPDQIREGVLDAMGDVAFGVPSVIVSRGHRDTGAPTYMYEYQYYPSFSSPQRPKNVVGDHADDVYSVFGAPILREGASEEEINLSKMVMKFWANFARNGNPNGKGLPHWPKYDQKEGYLHIGGTTQQAQRLKEEEVTFWTQSLAKKQPQPYHNEL
The following text describes a protein:
Function:
Methylates eRF1 on 'Gln-182' using S-adenosyl L-methionine as methyl donor. eRF1 needs to be complexed to eRF3 in its GTP-bound form to be efficiently methylated.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MLSTPVTSQLRLKEFQDVYEPAEDTFALLDALEKDAKKLRQMAEMKNLLTAEIGCGSGCASSFLKSGILKNKPIVHFMSDISNSACRASKITALNNRELYKDDNGLFITVQTSFLDGIRLGNGVDILIFNPPYVPTEFEEIPSEAATIASAWAGGTDGMDVTSTLLNQLKDILSQDGVFYMVAVARNKLHSICEILQKDGFIVNETLKRKAGRETLSILRIYRIGNTIWDE
The following text describes a protein:
Function:
May act as a GTPase-activating protein for Rab family protein(s). Involved in neuronal projections development, probably through a negative modulation of ARF6 function. Involved in the regulation of synaptic vesicle trafficking.
Subcellular Localization:
Cytoplasmic vesicle membrane. Endomembrane system; Peripheral membrane protein. Synapse.
Sequence:
MRLEMIQVSRTPGFSNLGNMNSFSHISTDQDFSSMATDRRQRSRSQYDSEESKSIESQKQTEEISVRPRSRSFYSFEMSEQSSNHSMESFLRSSPLRQKASTVFKSLAPKKEDVSGVHVTSRGIKPKLNKHSHSSELDGGKSSAKPMITISELDSWDICSSSGMKYGQFVDWEKIDPESASKYQQILNSEHKQLKAMGRQGFWAMPHTLRAKAYYHIIHCFTCSKANAPDREVYYELAKKLFGEQKLSNHPVPEYMEDGDIPRYCLNKAGLNSVKKILLCIGNYFPEMNYCPILPALVSVMLHFSEDEAECFFSVSRLICYKDTNKRYIDQTFLTYRASCMTFGDIANRCCKGIRKLIASSHQNLFEFYSDWIMWIFADLPFTYAIRVLDVYLLEGYKVLYRVALALLDLYKVSVSSRVADVQDFRTDMKRFVQSVDRYCTVENLLERAFMIPMATRAELNLLFNANKDSLIQKGVSKDQKRQTVETEDFTNFFSSIVTKVEMRVIWAWIPERFALFSPVQLFSTAEHERSLASLYSHVEGHEPVVLIIKTMDEEVFGAFLSTDVRERNQHNSQTPMYFGTGECFVFTLRPSMERYQRAMVYILTRIASPQQVSGFGNSPMSSPTGIYQNPGNLNISCSASLENSLTAKEPKRSKDQYASMFIAGDDRRLIIGTS
The following text describes a protein:
Function:
Functions as a component of both the DNA-binding general transcription initiation factor complex TFIID and the transcription coactivator SAGA complex. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA acts as a general cofactor required for essentially all RNA polymerase II transcription. At the promoters, SAGA is required for transcription pre-initiation complex (PIC) recruitment. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (via core/TAF module) and promoter selectivity, interaction with transcription activators (via Tra1/SPT module), and chromatin modification through histone acetylation (via HAT module) and deubiquitination (via DUB module). SAGA preferentially acetylates histones H3 (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac) and H2B and deubiquitinates histone H2B. SAGA interacts with DNA via upstream activating sequences (UASs) (By similarity). Regulates the genes involved in ubiquitin-dependent proteolysis during the progression of M-phase of mitosis.
Subcellular Localization:
Nucleus.
Domain:
The C-terminal WD40 motifs are required for its incorporation into TFIID and function in SAGA.
Sequence:
MSATNGPQPQDLNRIVLDYLAKKGYSRTEAMLRLEASGSGVSVEEKLKSIEETPDAYTHTYTILRDWVDSSLELYKAELHRILFPIFVHSYLNLLSQDHYEAAKQFYELFKDDHTDLHDFDVKNLKSLSLPSHVAEDRTAQQYRQNKYQLHFSRITFDLLLHFLFENVSNGGSIIIKLINQHIDIHIVPGRPTVLENAKVINEQEGITGQSFERGDAQLQPVKLQQMPMDKEMEKIVEMDLEEEDMMHQNDPNNQSPKLLKEFRKLHEPNAEDAPSRDYIPLPPHKGVDILSEVEAVKDWSKRLHLGPRASLPSVCMYTFHHTNNNMNCAEFSPDSTMIACGFQESYIRLWSIKADKKSLPKSTSVEDSDGSVRLLSHSGPVYGTTFSPDNKYLLSCSEDASARLWSVDTKTALVAYKGHTGPVWDVAFGPFGHYFATASHDQTAQLWSCDHIYPLRVFAGHLSDVDCVTFHPNSAYVLTGSSDKTCRLWDVHRGHSVRVFNGHTQPVTAVAIAPDGHTMASADSEGLIHLWDIGTGRRIKTMRGHRGNIYSLSFSRESTVLVSGGSDCTVRAWDVFKTNYNNPVSSSLTGSVVTPFSAKTSTFNEVNWSTSPDQMVALYTKQTPIFNVSFTRRNLCLAISVS
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that trimethylates elongation factor 1-alpha (TEF1 and TEF2) at 'Lys-79'. Required for replication of Brome mosaic virus (BMV).
Miscellaneous:
MISCELLANEOUS: Present with 3060 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MSDSDSDSDYELTLSANALAALEEFKREEQQHQEAFQKLYDETDEDFQKKKKEEGMKLFKEDWQLSQFWYSDDTAAILADAILEGADENTVIAIVSAPSVYAAIQKKPTNEIPTEHIYLFEFDKRFELLAGRDHFFFYDYNKPLDFSDEIKGKVDRLLIDPPFLNEDCQTKSSITAKCLLAPNDNSKTKKGVFKHRLISCTGERMSEVISKVYSDTRITTFLPEHSNGLSNEFRCYANFECSSWKFAS
The following text describes a protein:
Function:
Protease subunit of subtilase cytotoxin SubAB5. An endoprotease specific for host endoplasmic reticulum (ER) chaperone BiP/HSPA5, has no activity on human HSP70 or HSPA8. Cleaves between 'Leu-416' and 'Leu-417' of BiP/HSPA5 in the hinge between BiP's ATPase and protein-binding domains. This induces host ER stress response and eventual cell death. Culture supernatant of E.coli expressing both subA and subB are toxic for Vero cells (African green monkey kidney cell line), Chinese hamster ovary cells and Hct-8 cells (human colonic epithelial cell line); the subunits are not toxic individually. Purified SubAB5 is highly toxic, <0.1 pg is able to kill at least 50% of 30'000 Vero cells in a microtiter plate assay after 3 days; no cytotoxicity is seen at 24 hours. Preabsorption with cells expressing a ganglioside GM2 mimic reduced cytotoxicity of SubAB5 by 93% in the Vero cytotoxicity assay. Intraperitoneal injection of 200 ng of purified SubAB5 kills mice; the higher the dose the faster the mice die. Animals injected intraperitoneally with purified SubAB5 have microvascular thrombi in the brain and other organs, including the renal tubules and glomeruli. Injection induces an unfolded response in mice. Mice fed E.coli cells expressing cloned SubAB5 experience drastic weight loss and appear ill and lethargic. Protein synthesis in Vero cells is transiently inhibited by SubAB5; both subunits are required for this effect. Inhibition of protein synthesis is prevented by brefeldin A; cells are arrested in the G1 phase. SubAB5 at 100 ng/ml induced caspase-dependent apoptosis in Vero cells through mitochondrial membrane damage.
Miscellaneous:
MISCELLANEOUS: The E.coli strain this operon was isolated from causes hemolytic uremic syndrome (HUS) and also encodes Stx, a Shigella-type toxin.
Subcellular Localization:
Secreted. Host cytoplasm, host cytosol. Host endoplasmic reticulum lumen. Note=Colocalizes with host BiP/HSPA5 in the endoplasmic reticulum of Vero cells, its activity on BiP/HSPA5 is blocked by pretreatment with brefeldin A, which disrupts the Golgi apparatus and inhibits retrograde transport from the cell surface to the Golgi. Using different inhibitors it has been shown to be actively internalized by membrane-bound vesicles and undergoes clathrin-dependent retrograde transport, via early endosomes and the Golgi network, to the endoplasmic reticulum. Trafficking is similar in Vero cells, human HeLa cells and murine N2A cells.
Domain:
The catalytic charge relay system lies at the bottom of a deep cleft which probably accounts for its substrate specificity. The C-terminal A2 domain (approximately residues 322-347) penetrates into the central pore of the SubB pentamer, making different contacts with each SubB subunit.
Sequence:
MLKILWTYILFLLFISASARAEKPWYFDAIGLTETTMSLTDKNTPVVVSVVDSGVAFIGGLSDSEFAKFSFTQDGSPFPVKKSEALYIHGTAMASLIASRYGIYGVYPHALISSRRVIPDGVQDSWIRAIESIMSNVFLAPGEEKIINISGGQKGVASASVWTELLSRMGRNNDRLIVAAVGNDGADIRKLSAQQRIWPAAYHPVSSVNKKQDPVIRVAALAQYRKGETPVLHGGGITGSRFGNNWVDIAAPGQNITFLRPDAKTGTGSGTSEATAIVSGVLAAMTSCNPRATATELKRTLLESADKYPSLVDKVTEGRVLNAEKAISMFCKKNYIPVRQGRMSEEL
The following text describes a protein:
Function:
Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate or 10-formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to folylpolyglutamate derivatives.
Sequence:
MTVAPSEQASSVTVPSANAPLEQWLAYLLSIHPTEIDMGLTRVSKVAQRLNVLDLGPSKVVTVGGTNGKGTTCAMLENILRLSGLTVGVYSSPHMLKYNERVRINGQDQSDEAFVAAFEQIEAARGNISLTFFEYATLAGLILFKAAKLDVVILEVGLGGRLDATNMIDADISAVTSVDLDHEAYLGNTRELVGREKAGIFRQGKPAIVGEPNLPHTVNDVAQQLGAKLYRVGTEFTYQQNGHTWDYQGQVLKLKQLSLPTLPNAATVIAIVEHGWPEIAADIIAKGISSARLTGRLEQVSEQPLILLDVAHNPHAARFLVKQLTPIVAGKRVFALCGMLKDKDIGGVLPVVSPLIDTWYLVSLQGERGAHASLLRQTLTQETKACEFEDIATAWTALKAQIQPDDVVIVFGSFYTVAGFKSLFKQDNRFV
The following text describes a protein:
Function:
[CLE25p]: Extracellular signal peptide that regulates cell fate. Represses root apical meristem maintenance. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2.
Subcellular Localization:
[CLE25p]: Secreted, extracellular space.
Sequence:
MGGNGIRALVGVIASLGLIVFLLVGILANSAPSVPSSENVKTLRFSGKDVNLFHVSKRKVPNGPDPIHNRKAETSRRPPRV