lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Negative regulatory component of the MBF complex involved in cell-cycle-dependent transcription.
Miscellaneous:
MISCELLANEOUS: Present with 2880 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSIMKQRLPLGEFSSSKINKLAIANIADASEPRNHGENNVGTVCLPSIKSLMVSPEVYENTKSLPVPLMRSSGGGMACASKSSCQDGISTKTTSRDYSELSKKLQIRLQFAYYKYKTKQTDKNFTDLKSKHSITRPSKVATHSKSEPLTRRRKLVLSQGHYKTPARSKIKTPSSICSHDNTSSFTSFRGVSESSSTTADMNVADTTTPIRNNINTKHSNSHNRTLYQRQETPTSIKAAKSLIHLFTSNQ
The following text describes a protein:
Function:
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MSTILKTGPAPHIRTAETVESVMYDVVIALIPAFAMAVYTFGVRALILTAVSVLTCILTEYLCQKALKRDIEAFDGSAILTGILFSFVVPAIMPLQYVVVGNIVAITLGKMVYGGLGHNIFNPALVGRAFVQASWPVAITTFAFDGKAGATVLDAMKRGIPLSDALLENTNQYIDAFLGQMGGCLGETSSLALLIGGAYLIYKKHIDWKVPAVMIGTVFVLTWAMGADPLMQIFSGGLFLGAFFMATDMVTSPTTSKGRVVFALGLGVLISLIRMKGGYPEGTAYAILIMNGVVPLIDRYIRPKKFGGVSKNGK
The following text describes a protein:
Function:
Component of the spliceosome C complex required for the selective processing of microRNAs during embryonic stem cell differentiation (By similarity). Required for the biogenesis of all miRNAs from the pri-miR-17-92 primary transcript except miR-92a (By similarity). Only required for the biogenesis of miR-290 and miR-96 from the pri-miR-290-295 and pri-miR-96-183 primary transcripts, respectively (By similarity). Required during the transition of embryonic stem cells (ESCs) from the naive to primed state (By similarity). By enhancing miRNA biogenesis, promotes exit of ESCs from the naive state to an intermediate state of poised pluripotency, which precedes transition to the primed state (By similarity). Involved in pre-mRNA splicing as component of the spliceosome.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: Based on a readthrough transcript which may produce a ISY1-RAB43 fusion protein.
Subcellular Localization:
Nucleus.
Sequence:
MARNAEKAMTALARFRQAQLEEGKVKERRPFLASECTELPKAEKWRRQIIGEISKKVAQIQNAGLGEFRIRDLNDEINKLLREKGHWEVRIKELGGPDYGKVGPKMLDHEGKEVPGNRGYKYFGAAKDLPGVRELFEKEPLPPPRKTRAELMKAIDFEYYGYLDEDDGVIVPLEQEYEKKLRAELVEKWKAEREARLARGEKEEEEEEEEEINIYAVTEEESDEEGSQEKGGDDSQQKFIAHVPVPSQQEIEEALVRRKKMELLQKYASETLQAQSEEARRLLGY
The following text describes a protein:
Function:
ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction. Participates in DNA replication and repair (By similarity). Involved in 5'-end resection of DNA during double-strand break (DSB) repair (By similarity). Negatively regulates sister chromatid exchange (SCE) (By similarity). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution (By similarity). Binds DNA. Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction (By similarity).
Subcellular Localization:
Nucleus.
Domain:
The N-terminal region mediates dimerization and homooligomerization. Both the helicase ATP-binding domain and the helicase C-terminal domain form intramolecular interactions with the HRDC domain in a ATP-dependent manner (By similarity). The HRDC domain is required for single-stranded DNA (ssDNA) and DNA Holliday junction binding (By similarity).
Sequence:
MEEARAATNGGSGESQKLSNGEKSSQLEPGDVGNELLADIELEEDDYLDVVPPSPEEELPSFSPSVRNVSNIFKESPTDGRSAVHGTESEPELMAPKQPAAEQDSSAEHADKGLHLEQQLYSVMEDICKLVDAIPLHELTSISCAKELLQQRELRRKLLADSGALNTNSVNGPRNWKACVQQDPSSRPGTPLCSGPGRGVSSVGSTPKSTNLPSVLSRTVNSSSFSTIRNQTLDKLDTSYSSKETDQEVICLEPAALPSPKVNGKGSTSLSRPSEASFNGSWCEKPTGRDSGNWRVPERPTASTALKAQHTAPAGNPASGCWDVNDTDFDLDHFDIDDFDEGWEEAVAPEAAPEAPPAPQWQPLREGSASLRCRLLAAAAGSAPGPHPTAPKSGCGISAKSSSEPLVHNPAHERFRGMKFSHSEEMLKIFHRKFGLHSFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSAGVTVVISPLRSLIIDQVQKLKTLDIASTYLTGDITDADASKTYMQLSKKDPIIKLLYVTPEKVCASNRLLSALENLYNRKLLARFVIDEAHCVSQWGHDFRKDYKRLNMLRKKFHSVPMMALTATANPRVQKDIQNQLEMLKPQVFTMSFNRHNLKYDVLPKKPKKVAMDCLEWIKKYHPHDSGIIYCLSRHECDTTAAILQKEGLAALAYHAGLTDSNRDLVQKKWVNQEGCQVICATIAFGMGIDKPDVRYVIHASLPKSIEGYYQESGRAGRDGEMSHCLLFYSYSDVTRLRRLILMEKDGNSHTRQTHFNNLYSMVHYCENVVDCRRIQLLAYFGETDFNPNFCKDHPEVICDNCSRKKDYKSRNVTDEVKSIIRFVQQHCGQVGGINGNRNTGSGRYTLNMMVDIFLGAKSAKIQSGIFGKGAAYSRHNVERLFRKLVLDKILDEDLYITANDQAVAYVVLGEKAQAVLNGLLQVEFHETENASAIRKQRASVTKMSQREEMVKKCLGELTDTCKTLGKIFDVHYFNIFSTSTLKKIAETLSSDAEVLLQIDGVTEDKLEKYGAEIIKVMDKYSEWTTPEDAACQSVDTAPGSAGTPGSEEEAADDVVTSSYFGGNANQRRKRKRLPNSGESKRKKTSSGGSQQFYSKGARYRRARRAPGSRAAAPAQSSALRGAGARLGIMAPPKPSSRHFLQPSYAVL
The following text describes a protein:
Function:
Vacuolar Fe(2+) uptake transporter.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Sequence:
MHFQWLRAAVLGASDDLVSTASLMLGIGAACPADEHAVLLSGLAGLVAVAWPSASRPPVRANRPRRRPRAARCLAGRNRARGPAPASAPAGLRLQAAAVSPSSQATAASTLSFAAGAMFPLLAAWFVASYASRRLLPPQSSAPAAPPGRSPATVTASSFSRRRRRPEQRRPFSFSSPTTPTCSSERGLFWSVEVWKMVKIF
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).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MTTTAKTDDIPIDTVILDIEGTVCPITFVKDTLFPYFIEKLPSILDKFQYPLSNTSASSDDQVLNILKQLPDNITKSSESIYKHFKNLVDQDIKDPILKSLQGLIWKQGYEKNELQAPIYQDSIEFIESFPTKSSTNNKIYIYSSGSIKAQILLFGHVKSTTTTITNEVIDLNPKLNGYFDITTAGFKNQSNSYKKILQEINKSSTPKSVLFLSDNINEVNAAIEAGMKSYIVIRPGNPPIDDDDDGNDDKINHKIIYSLDELDL
The following text describes a protein:
Function:
Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTLRATKARQQRVSPHIGHTFSFGNLVGDPFAISTLSISTIAWLITLGGGIATKKMPHFSWWGIAFQFVMMVCFVVIYLWDLVDYYRGFLAAGVGVAFVYSTNSCSQLIYQEEPQQAAGSAGFMMLSIVNMIWMFYFGADNAAPANRWIDSFSIRGIRASQVESSLALARSQKAVASPQPAATAFYGGLEGHSQKYVSSTALNGFENTDPHTSTAFALGPEGPTQRNLDTHGTSTYVTDTTNGNTETTMGDTLGLYSDMGDELVNFPYTAKALYAYEADASDAYEISFQQGEILRVGDIEGRWWKAKKANGETGIIPSNYVELVDDPAAL
The following text describes a protein:
Function:
Together with methyltransferase FTSJ1, methylates the 2'-O-ribose of nucleotides at position 32 of the anticodon loop of substrate tRNAs.
Sequence:
MDIHVTNMEDPTLVYQELRNKLEAVNDKPGPARLLLQCLEDNNPTQQAIMLKTLAVGPKLKEAASDATLQPQRLVCVDVLVSMYLQCTVHSSLRGTLVSMLQSLPAELKTQAVDKLSTQVKELLVVPSERLRYNINILGLLLENFSMGATVVAKNLPAVLNFVEKSLEVLLVDAKDVSTAKSSQAMQDCTTVLKLLTALLQKCQADILALITTDHGSHESYLLAEITCTLYSILQFDWVLQACHSSAGIALPATIRAFLLNDNEATVKAVFAILYPDHSTEFLNEVKLKKLHKFLQSCRANLPSFSRLCLCKGILAKLSPEMLSTMFDNQCLLFDVILPDILRLCNSLLDSTSVLHGSYALTVWSTKALELTKSVTVENTRQQLILPSSTMQQVVGYIWQHWDHPLDGVRHQCREIFRNILKCHVKVSNSPVREDADLLDLTKKVFSEDWHKRGKYIALCCLTEEIGAQEILQLCPQIVTRLLVLMSSEAVTASVHAKELHGKLSKSHKVELTTQFHDEGTSKWQEAWIDPVLDLLCNTSTSVNRQTISDCLSSLLKTSPESMDFIVGRLTTDGGSLSKTSDAKLCGLIACLQTAHSLRMRNLQTHSSATEMMLKKALTHSKDQVRLSSLSLLSESHKQTDPIPGPRLSLVLHFLKYNLNSQSPSFRQQTCSSLKKLFICVRDSSFAAQRSLRQQKKKSACETSPPETPQTEQQLKQYKEFLGKVFEMLFQGIGVGASFARKVTCLSLLSVMLQNLLYHTSSESIAEVFPLSTMFTSRHFHLLLECLADTYEPNKQLGLELLTVVLKNAPNSSVHLKENDPLCAVLYGICETLMESVNPHDSVTAAYILRLLLQHSVDVKEWSLNTGENSDQTLKVAEPSHSTASLEQDVKDHIMINTCNILASLVGKLKPLVEHSKKDLLEVAANCPIYGVIHCIRSLLADVDMTSLVPKLEWGNLLDKIVDVCCEVSSIVSPIVQTAAPEGYIPEGATLVDAAVTQVSLKPVSEDDTTSQEPSSVSSQALLICCWRSLMEISLLFGQFAQKAPMYQEDDDPQGVLSVNQVLKIGHYFTTQLLEARHLGAFEKGKDGFIKLCHRLWRSEIPDLRKLPCDWLKGLLTSLQDYNDSSLCATRRSAGLPLFFECVLTTEPEEHQQAQLKSSMEQLLSLASSLPLPTDSKHTVPVVHALNILKALFRNTKIGEHIFPYIVDGVKVTILGFGSEVWAIRNASTLLFSILMTRIFGVKRGKDEHARRNCMSGREFFARFPSLHSFLLDQLQLAVERIQSCDSSVDLHPSLYPVLIMLAKLYPSPMDGASSALNMSAFVPLVQKCAHSTVMKTRAMAAQALLPLIPAAHAASTIGKLLRQIKDASRIPQNSVHGILLQAQGLIKTYCRKDVPGVTQEDLESEVYPSLQSLSWIGSRSNPCAVTRALYIATVEFLIFDSNVGKGSHPLQELRSTLMATLHTEHQEDSSDICGAAALNVGIATFVLRCLPHSSRVITNNLVEPAGVLLSLLTNKHYEVRQKTLEFLNKSITEQQNCLTASGQTLEAKVDGTVVTVTKGKVSDKLETTASPSNISRDTDIELDERLHPLLGLCTEERIFQQLVIMVMQTERNSEVLPHLLQLMCTVMPLRTFPWVITTPSSKQVTCGDMLQTLVRLGQESTMKPELQAAVVSLSSITANMLYTSSEPQVEMGTTLMQYFADWVGLMLECAQPGKYVEVRQAVAKGLAAVTGILEDGRCLLGDLSFTLWRALLILLQDEDEVTRQTAASSVLLLSNNRQETSISIQPTLALHQAVELLLQSSGKKKWRPCILLLHDLVTGSPDLEDVFPDGQITTEVVFEKGETNTYEEGVELAGVAAQSLTRAVGGSPLVGADVQSNLHADSTTTGHQHPSSTSVQELPIDTSLILALIEKDESLLLDLCRRCSSLKTSPVFVYHTLYGRVCETLYRLVIAMTVLLGCPLLESTFVADTVEKVVEKVAHSTICQQPLPSPLVKQALACLQDLVK
The following text describes a protein:
Function:
Bifunctional enzyme which catalyzes the formation of trypanothione (N(1),N(8)-bis(glutathionyl)spermidine) from glutathione and spermidine. Converts spermidine or glutathionylspermidine into trypanothione. Can also convert aminopropylcadaverine into glutothionylaminopropylcadaverine and homotrypanothione. Also has low amidase activity, hydrolyzing trypanothione, homotrypanothione or glutathionylspermidine to form glutathione and the corresponding polyamine.
Sequence:
MPTLQSLAVPFGCVQGYAPGGIPAYSNKHESYFSGERSIDGNLFCGFKYQCVEFARRWLFERKSLVLPDVDWAVHIFNLKEVSDARTGKPVRCVAIRNGTAAKPVVDSLLIYPSDDYSPVGHVAAITEVGDKWVRIADQNHRFHKWDANYAAELPLIHEKGVWTILDPLEDEVLKPLGWVTFPDTPDRNPNEPLVLHESLHFKRGELPTLRRLTFTPTSREKDWLDLTNEAEAYFADVCGIDVKNPKLEKASYYQMNRELYLDCAKYGNQLHQMFLEATKFVLGSDELLRLFCIPEEYWPRLRHSWETQPHAITGRFDFAFDEDTQQFKCFEYNADSASTLLECGVIQQKWARSVGLDDGTTYSSGSLVSSRLQLAWEMAEVTGRVHFLIDNDDEEHYTALYVMQHASAAGLETKLCVLFDEFHFDENGVVVDSDGVAVTTVWKTWMWETAIADHQKARVQRGNDWRPTPKDEVRLCDILLGPNWDLRVFEPMWKIIPSNKAILPIIYNKHPDHPALLRASYELTVELQRTGYVRKPIVGRVGRNVTVTEASGDIAAKSDGDFSDRDMVYQELFRLPERDGYYAILGGWVIGDVYCGTGVREDKTIITGLESPFSALRVYQGAQRRPLTHEDLDKAEAAAVGGGLKT
The following text describes a protein:
Function:
NAD-dependent epimerase/dehydratase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins. Within the pathway, FUM13 stereospecifically reduces the intermediate 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane. The biosynthesis starts with the FUM1-catalyzed carbon chain assembly from one molecule of acetyl-CoA, eight molecules of malonyl-CoA, and two molecules of methionine (in S-adenosyl form). The C18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain. This step is catalyzed by the pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8. The resultant 3-keto intermediate is then stereospecifically reduced to a 3-hydroxyl product by reductase FUM13. Subsequent oxidations at C-10 by the cytochrome P450 monooxygenase FUM2, C-14 and C-15 by FUM6, FUM12 or FUM15, tricarballylic esterification of the hydroxyl groups on C-14 and C-15 by acyltransferase FUM14, and C-5 hydroxylation by 2-keto-glutarate-dependent dioxygenase FUM3 furnish the biosynthesis of fumonisins. The tricarballylic moieties are most likely derived from the citric acid cycle, and their addition to the carbon backbone may involve FUM7, FUM10, FUM11 and FUM14 (Probable).
Sequence:
MSRGQELVLLTGATGHVGYAVLVKTLQAGYNVRATLRDMSRADAILSSGPVQEALSAQDLDLSFVRVPNFTAPDAFGLVLSNVTHVVHVASALRRGTSTDLKEAIIDVAVQGTRNILRAAHNCPSVRRVVITSSVSAIVDQHPVVSQSPAGRCVTPLDRHADYDAEYYKGDSLKAYTAAKTAALNATDAFLATADGGPTTLPLHFDVINIMPSFVFGPKGLAATPSDVTNGSNIFGIGLVMRHKPWDGIRLEAVCCHVDDVAQVHVNALNDHELLPLKVGAHRDFILGVKFKPEEIGEIVRRRFPREWWESESATFGARGTYDWYHTDYDVGSAERLLGRPFKCLEEQIYDSGSQVMEMLKGMTTRSYN
The following text describes a protein:
Function:
Involved in lipid metabolism and lipid droplet (LD) morphology, number, and size. Supports the formation of small-sized LDs and modulates triacylglycerol accumulation. Induces probably a reorganization of the endoplasmic reticulum into LD-forming domains.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Localized to the lipid droplet-forming sites.
Sequence:
MDSESESESNPSTTDEFDRFLDAPDEFYYDCLPIRSNSHQPSSLLRRRKSAHRRDLISSDIETEPSSSSDGFDVGEKSSYVEKNAELRGDIDTSDVIESTKDSIDLSSEKENDLDVISSSGNDMDVIDSGRNRVDPFQEESTVTTVSSDDQGDDDYAGSVPQFREPPNSTEWSLLGFLVGLVIKAIEFQVSFMTSLLTFPPWLLRNCFLFFFDPFSTIRFGRRFLMARVAGISDMIFGYMNPFRLKDTKQMLSIVCKFGWGMFWAVYVGIVLFGLLVSSLMIGGYVINRIADKPFEVKETLNFDYTKNSPEAYVPISSCAGVECEGSCKESNEMSKIRGLRVIPRDQKLDIILSMTLPESAYNKNLGMFQVRVDFLSVDGQTIASIRRPCMLRFRSEPIRLVQTFFKVVPLVTGYVSEIQTLSLKLKGFVEKDIPTACLKIIIEQRAEFRPGAGIPELYDASLSVESGLPFFRKIIWKWRKTLFVWISMSLFITELLFTLVCCRPLIIPRTQPRDRSPSNPTGVWR
The following text describes a protein:
Function:
Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Localization:
Cell inner membrane; Single-pass type I membrane protein. Note=Localizes to the Z ring in an FtsZ-dependent manner.
Sequence:
MENNKMIMLLLLLFLLVVAGAVIFRVRQQSQQATRRRHRREPSIQQSVEKEEEAEIDTDEALGLSQDPQERKEAVRNEPAEAEEIQDIFTLYVMAPKEYPYNGYELLQALLANGLRYGERNIFHRHEIKTGRGRILFSLASVNKPGTFELSKMGNFSCPGLVLFMVLKHTPDPLMAFDTLLETARQLTEDLGGEVWDEERRLLNMDKVAQLRARIRRYEESQRVPDFFES
The following text describes a protein:
Function:
Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis.
Subcellular Localization:
Cytoplasm.
Sequence:
MRGEAGELAVSSGEIATGALSPEKQQEQELMGKLAATGKLPARPASSFLQKKLQQRKFFDSGDYAMDKSKAGTGLGSKPHPLAGGPPPAAPPVVAQRSPAPAATTPSPSASPISQQTNRPSSDRNSDDDNLQIPRPDTVPQRKASIINPSVHCKLSPAPHVQHHDAASPNATSE
The following text describes a protein:
Function:
May prevent inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). May bind to nascent polypeptide chains as they emerge from the ribosome and block their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. May also reduce the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites) (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MPGEAARAELLLPEADRPGPRTDLSCDAAAATTILGGDRREPCALTPGPSHLALTFLPSKPGARPQPEGASWDAGPGGAPSAWADPGEGGPSPMLLPEGLSSQALSTEAPLPATLEPRIVMGEETCQALLSPRAARTALRDQEGGHASPDPPPELCSQGDLSVPSPPPDPDSFFTPPSTPTKTTYALLPACGPHGDARDSEAELRDELLDSPPASPSGSYITADGDSWASSPSCSLSLLAPAEGLDFPSGWGLSPQGSMVDERELHPAGTPEPPSSESSLSADSSSSWGQEGHFFDLDFLANDPMIPAALLPFQGSLIFQVEAVEVTPLSPEEEEEEAVADPDPGGDLAGEGEEDSTSASFLQSLSDLSITEGMDEAFAFRDDTSAASSDSDSASYAEADDERLYSGEPHAQATLLQDSVQKTEEESGGGAKGLQAQDGTVSWAVEAAPQTSDRGAYLSQRQELISEVTEEGLALGQESTATVTPHTLQVAPGLQVEVATRVTPQAGEEETDSTAGQESAAMAMPQPSQEGISEILGQESVTAEKLPTPQEETSLTLCPDSPQNLKEEGGLDLPSGRKPVAAATIVPRQAKEDLTLPQDSAMTPPLPLQDTDLSSAPKPVAAATIVSQQAEEGLTLPQDSVMTPPLPLQDTELSSAPKPVAAATLVSQQAEEGLTLPQDSAMTPPLPLQDTDLSSAPKPVAAATLVSQQAEEGLTLPQDSAMTPPLPLQDTDLSSAPKPVAAATLVSQQAEEGLTLPQDSAMTPPLPLQDTDLSSAPKPVAAATIVSQQAEEGLTLPQDSAMTPPLPLQDTDLSSAPKPVAAATIVSQQAEEGLTLPQDSAMTPPLPLQDTDLSSAPKPVAAATPVSQQAEEGLTLPQDSAMTPPLPLQDTDLSSAPKPVAAATPVSQQAEEGLTLPQDSAMTAPLPLQDTGPTSGPEPLAVATPQTLQAEAGCAPGTEPVATMAQQEVGEALGPRPAPEEKNAALPTVPEPAALDQVQQDDPQPAAEAGTPWAAQEDADSTLGMEALSLPEPASGAGEEIAEALSRPGREACLEARAHTGDGAKPDSPQKETLEVENQQEGGLKPLAQEHGPRSALGGAREVPDAPPAACPEVSQARLLSPAREERGLSGKSTPEPTLPSAVATEASLDSCPESSVGAVSSLDRGCPDAPAPTSAPTSQQPEPVLGLGSVEQPHEVPSVLGTPLLQPPENLAKGQPSTPVDRPLGPDPSAPGTLAGAALPPLEPPAPCLCQDPQEDSVEDEEPPGSLGLPPPQAGVQPAAAAVSGTTQPLGTGPRVSLSPHSPLLSPKVASMDAKDLALQILPPCQVPPPSGPQSPAGPQGLSAPEQQEDEDSLEEDSPRALGSGQHSDSHGESSAELDEQDILAPQTVQCPAQAPAGGSEETIAKAKQSRSEKKARKAMSKLGLRQIQGVTRITIQKSKNILFVIAKPDVFKSPASDTYVVFGEAKIEDLSQQVHKAAAEKFKVPSEPSALVPESAPRPRVRLECKEEEEEEEEEVDEAGLELRDIELVMAQANVSRAKAVRALRDNHSDIVNAIMELTM
The following text describes a protein:
Function:
Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Also acts as an asparaginyl endopeptidase inhibitor. In the human host, inhibits CTSL/cathepsin L, CTSS/cathepsin S, CTSB/cathepsin B and asparaginyl endopeptidase LGMN/AEP which may cause defects in both antigen and MHC class II invariant chain CD74/Ii processing.
Sequence:
MMSTMSIKEGLLVILLSLFLFDTTALIHRREIPHMESKGQMQRGQVLLGGWQERSPEDNEILELLPSVLTKVNQQSNDEYHLMPIKLLNVSSQVVAGVKYKMEVQVARSECKKSASEQVNLKTCKKLEGHPDQVMTLEVWEKPWEDFLQVNILETKVLSSV
The following text describes a protein:
Function:
Probable membrane-associated metalloprotease that may be involved in chloroplast development.
Subcellular Localization:
Plastid, chloroplast membrane; Multi-pass membrane protein.
Sequence:
MAAAAAALASSPLVHLTAAARLRLPRPRPSPAASSRWGYPRGAYLDWRPLRRCDRMRRFSVDEGGGGGEDGEKRGEEEAAAPVEAKVGAAEELGSERSRSGSFSSSSSPSSATPGVSSEPPLLSFSVDNIDTVKLLELLGPEKVDQADVKAIKEKFFGYTTFWLTREEPFGDLGEGVLFVGNLRGDREEIFGKLQRQLRELTGDKYNLFMVEEPNSEEDDPRGGPRVSFGLLRREVSEPGPTTLWQYVISLLLFLLTVFSCIELGIASKISSLPPDIVSYFTDPNATGPPPDMQLLLPFVESALPVAYGVLAIQLFHEVGHFLAAYPKNVKLGIPFFIPNFTLGTFGSITQFKSILPDRKTMFDVSMAGPLAGAALSFSMFSVGLWLSSNPAGATDLVQVPSNLFQGSLLLGLISRAILGYSALHAATVSIHPLVIAGWCGLTTTAFNMLPVGCLDGGRGLQGAFGKDALFGFGLTTYSLLGLGVRTPEKPCLDDVSDVGTWRRGALIASVFLVVLILIPLWDELAEDLGVGLVSSF
The following text describes a protein:
Function:
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Domain:
Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
Sequence:
MTDEAEDSGPGGYAAARLRLLTEGARSGPPRRRALAELTDGWLAGLFGAATEEHTGISLVAVGGYGRGELSPRSDLDLLLLHDGRDDKAVAALADRLWYPVWDLGIDLDHSVRTPQQARKTAGQDLKVHLGLLDARHLAGDLGLTASLRTAVLADWRNQAPKRLPELRDLCAERAERQGELQFLLEPDLKEARGGLRDATALRAVAASWLADAPREGLAEARRRLLDVRDALHLATGRATDRLALQEQDQVAAELGLLDADALLRQVYEAARVISYAGDVTWREVGRVLRSRSVRPRLRAMMNGRNGGKPVAERSPLAEGVVEQDGEAVLARTARPERDPALPLRAAAAAAQAGLPLSRHAVRRLAATARPLPTPWPAEAREQLVTLLGSGRPTVQVWEALEAEGLVTRLLPDWERVRCRPQRNAVHLWTVDRHLIETAVRAAGFTRRVHRPDLLLIAALLHDIGKGWPGDHSVAGETIARDVAARIGFDGADTAVLATLVRHHLLLVETATRRDLDDPATVRAVAQAVGTEHTLELLHALTEADALATGPAAWSSWRGSLVADLVKRVSGVLAGEPQPEAESAAPTAEQERLAVEAFRTGGPVLALRAQTEPPADSAPAPSSPSSPSFPSPLSSPSSPSSADGPEPLGVELLIAVPDQAGVLPAVAGVLAMHRLTVRTAELRSVPLPDGVEGSVLLLDWRVAAQYGSLPQAARLRADLVRALDGTLDIAARLAERDAAHPRRRGVEPPPPRVTVAPAASRLATVIEVRAQDAPGLLFRLGRALEAAGVRVRSAHVSTLGANAVDAFYVTRGEGTPLPGDEAASVARGLEESLRT
The following text describes a protein:
Function:
Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MLRSGAASASSGGGRGPSSSLSSVKRSKHDDTRLPEAYQQERPPWRPPLHPTAARRHVPDLFPTKSGQPEDDMSQISVRKGFAPRTYVHNEYFCAHDAIHTRLLSPDALDTLSDWMDEVMQRRRELDRASIATNQYKPPSRVTLNDAKLANYVKDLADPTVPLMRLSRSVPHGFRGEKLFEMLWVGGALPSTATAATTTVNYFHSRIAGPPSASSASASASASASTSAPRKSVDIPRAVWFIRALGAAELSSLRNKSAATIIPEITSNLCAWMAKQVAELNLVHTAESNSTATASPAPVSPSTHLPRTPSAAPSSLSRSVAAAHFARTPSNLNPASSPSLAPAKEVCYVLQNDADEERWIAKWSYSLSLARHLHAQNLLDRSVLVRWIVDAFSASNLVQLPFLLELVQEVLLLVLRRRCFVKPFLTALLVQIPNVDARLDPSSSGGLRTKLVLLFRIVCENSPESLISPRLWFEHSASLTQLLNELNAETPLPLSHQAFEFVEQTVRPRVDRLLLRPHSGNTTQNASLETQETLSSPLQHHLDIQALDSFDMTTIDRVFLQNTSATHRYAKHDRDDTVWATRIDTILTWACTDRRSGVVRQYLAATLIEKIRFGVPWEESSEETDQVSLPAFDLEHNTTKTRKINVEPMLIKWLGDVETSLNQKLDESSTQTRVSLLATVDVGAIVVLLGELARRGVFSYTKYLQRLIARGMTAPSASSATEQHQNPDGSVQTPSSVSASRDSLHLRLLRSLPLYDQPASVYQQRRQAIYGDRTKETYEDAAQRRALRQLQSFLPFAFAQEVQAEASRIAVSPSPSTPDPVHALSRLWSASRFVRCRLFRSELLPAVTARVERLNGDQLSQISAVLVMADDFEGLAQLLATLLLRPLSDNLARAAFNMVIEYSLVWRSMDIMATLNQLVRQQLNHSSSIRNDRQAVMASTTLLRLRTLIENVPSRISASALDPGADHDALQQHVQALRPNVDALLDRFAKLTRSSVESDGSIASSSTPVEGSDMLTPFRSLFVQPDAMSDEMIERTIVDSVFARSDTSLVPSAVRLIDQLYLEASLEIDERHARWLSNLVLSIEQGTHSDASMKALLSLLTRLIAHGTLNLQLAMDTFLLPYLLSSVRRLTDPATRNTEVPMHIGSIVSSLGEIFASSLGETVPATSYEDMRAFGAQTKLLFAQVNLPSLLRAATCLISAFDETSTVPASEKAQIESFCNALLQSQPMQIAFRQEPRLCILAIKDTCKSMWGCNPSRVIDLAMACLDPTSLLLRDVGTIDAASVKNRLDGWDTAVVATELVEIFERLQLVESSFQTRADSKTKALASGIFDDLFVQLPDIGAQLVRDCQSSGLVSRFTDIGIKILSDKVKAASTDADKTPRRMDNSHKGMTNFGPDDGADAPAQAKTAADAAKHGPCVGEQQVESTLRSVVRMCEQQHSFIFNATDADSCAQLLLHVVTSLEDALGSMAAASHQDKVARLVTVLHGSMTFQLMHLVLRFGCLWNGTMRALALRLVKALLELTRQAGEKTECGGSFALLLDSLSFVLDELPPTLLSTCLPELETQLQTIELATQERSDKLQQLSFRLDNATTANAWLVASSAGAALKKGWFTSGGLNPWECAEYLEAPPAANPAAAGAAGAAGAAAGGNARAGVVETGRSGVNSRAAVESPGAVTVNDAETCNSLPGARTGWTGKLWLNTAIPLSMLGVRVTRDLVPNYASPASPGGVSVGSNDASSQPWTTGGGASAIGVGTCSAMDMDAKEALAALPMFVESERTYGERSAGEPAYSRDLRRGLLVEPNLPCRTRDERGETSQEPARATMDPAGAHTSVTSSATHDPSHVIDLTWDADEEMPLSTHPHHPAVATTSRKRRLSKRD
The following text describes a protein:
Function:
Involved in the targeting and/or fusion of transport vesicles to their target membrane.
Subcellular Localization:
Vacuole membrane; Single-pass type IV membrane protein. Prevacuolar compartment membrane; Single-pass type IV membrane protein.
Domain:
The longin domain is essential for the vacuolar and subcellular targeting.
Sequence:
MAILYALVARGTVVLSEFTATSTNASTIAKQILEKVPGDNDSNVSYSQDRYVFHVKRTDGLTVLCMAEETAGRRIPFAFLEDIHQRFVRTYGRAVHTALAYAMNEEFSRVLSQQIDYYSNDPNADRINRIKGEMNQVRGVMIENIDKVLDRGERLELLVDKTANMQGNTFRFRKQARRFRSNVWWRNCKLTVLLILLLLVIIYIAVAFLCHGPTLPSCI
The following text describes a protein:
Function:
Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand.
Sequence:
MPTWLNVAEKPSVAKEMAQSLSGGNCRTVPSQSRFNPVYEFKFEGKTMLVTSVAGHLMEDQFPPNTKNWSTYPFQGLFSAPITKYVRADLEPVKKNLEALAGRADTLVLWLDCDREGENICFEVMQVVQSKRPQVQVKRAHFSALTARDLLNAVHNLKLPDKRLSDAVEARQEMDLRIGAAFTRYQTVKFRHLFAAIPGVLSFGPCQFPTLGFVVRRYWQQQGFVPEDFFTLQLQHGDTKFHSSRGSMYDQVAATLIYEDMLLAAAAEGHKGRITNVQQRPSHRRPPVPLATVVMQKLAATHLRIPSERCMALAESLYQEGLISYPRTETDSYTFQESELLELVRVQISNADVAEYATAMLADIATRVRPPLRGGRDDKAHPPIHPTKAWNATQDERGRLYNLIVRHFLASLSPDAVAATTQVSAEFGGELFSTGGTTILQRGWLDIFPYERWNSTCIPNYQIGDAFQPTAVPLKKGCTSAPPHLTETHLISLMDSNGIGTDATIAQHIKTVLDREYVKREGQSLVPTTLGIALASAYESLGLASLLQPQLRAQMELAMGDIANGAATKEQVVAAAVQLYEEIFSRLMANTNAFYEELKRYLQPEVETDACAVQATVVKANFIPCGTCGRLMDLVERAGERDREVWSVRCHACNKMHRVPNGRLNTLEPVSPPHTCPLCGFLALRVANREKQTSYHVCPHCFGSPPKAWSVTTYGCVGVAASLPDVEAAAEFRCFQCTADCPLAKGLEAIGITTCIACRQHELRLRSGANGFFLSCRGYPSCQLRVSLPAAASVKPSPSQRCPACSAVLLTFDFSGRQGVPGLNMLDTICVRCDARIKDYIAVKGMPTSGANSSAVPSAAASVASTASGTYTLPSVKPSARRSVRGGGQRGGRGGDAAAANTPSGGVDPVCGCGTPAKQLVSRKEASRGKRFLTCANRQCSFFQWLD
The following text describes a protein:
Function:
May play a role in growth regulation and in negative regulation of cell cycle progression.
Subcellular Localization:
Cytoplasm.
Sequence:
MKGFPSLEQSTEAFKLLKQLKLHAEQEANYLPRGAGLSLIESTLENASSISVKLRDAKVEDLWSLTNFFRYRTQTFVLAVNLLDRFLAMMKVQPKHLPCIGVCCLNIAAKVVEEECNIAATHELIRISQCKFTVSDLSRMEKIISEKLKFQFQAVTALTFLHLYHAVALSHTSDRKEMLNLEKLEAQLKACLCRLVFSKARPSVLALSLLTLETEALQXMAVFTILQSKRIKEYIYIADRELQYWRELVAKCMTEYSSPECSKPDNKKLVWIVSRRTAQHLHSSYCSIPELPTIPEGGWDESESEDSSEDMSCGEDSLSSSPGSDGEGRFFPELFRLQAKQRPT