lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA.
Subcellular Localization:
Nucleus.
Sequence:
MMAHLLDELLLKQPEAFVELVYAEPAAVLSIYQRLSGPARHLLLRFLYQPDATLDKKQFAAYFLKDEDAETVRIELTQRFLLKTMTDGMLTFGSVFLDSLRTALAGRTDAPDQAMPPPKKASEVTPAFLEEHSRVSWEAILSYMTTNAELKNSTMILILQEAQLIVNDQPPISVTPEGFQFLLQDRANQVWLLIVTFLKLLSREEPIPGEGLPMHEALVLLFRIGLGRLNEVSVLEFSAENLTTMQITFLRQLHYMGVVYHRNRKSKRFFLTPYAVMLYHNAELALSQTETGFLLAETNFHVYAYTDSAVKVALLSKFATLTYRLPIMTTAIITRTSVRRALSQGITADQILRFMQRSSLLLRHHDETAPTRPTSPQHATPYSCMLLSPPSFDFFKHGLIQIGACEPHDASQEQEPK
The following text describes a protein:
Function:
This major soluble protein in olfactory sensilla of male moths serves to solubilize the extremely hydrophobic pheromone molecules such as bombykol and to transport pheromone through the aqueous lymph to receptors located on olfactory cilia.
Sequence:
MMNHKELVLFAVVCLSLYQAVEPSQDVVKDMSLNFRKGLDACKKELNLPDTINSDFNRFWNDDHVVTNRDTGCAIMCLSSKLELVSDTGLHHGNTLEYAKQHGADDTVAQQIVDLLHSCAQAVPDLEDPCLKVLEWAKCFKAEIHKLNWAPSAEVMAAEMLAEV
The following text describes a protein:
Function:
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems (By similarity). Binds GTP with specificity. Plays a role in the root morphogenesis by regulation of the cell proliferation. Acts with GB1 in the positive regulation of root waving and root skewing.
Miscellaneous:
MISCELLANEOUS: Dark-grown xlg1-1 xlg2-1 xlg3-1 triple mutant plants showed markedly increased primary root length compared with wild-type plants. Dark-grown roots of the xlg triple mutants also showed altered sensitivity to sugars, abscisic acid (ABA) hyposensitivity and ethylene hypersensitivity, whereas seed germination in xlg triple mutants was hypersensitive to osmotic stress and ABA.
Subcellular Localization:
Nucleus.
Domain:
The helical domain (460-611) is required for self-activation.
Sequence:
MEKKDEGESWKEMVRKMLPPGAPLPEDPSEFDYSIALEYTGPPPVHDIPRVSPVDVNPRVNNPIPLPVSRIAGGVTSSSGGSPASSESVVSVLHNNPESSSGSASVSPVSGHRQNGNQVRRPVVKFKPVDDHDRIEGREAAEEEDNNVEAETERERKVHECTASTKRRKKKKKSECYRCGKAKWENKETCIVCDEKYCGNCVLRAMGSMPEGRKCVSCIGQAIDESKRSKLGKHSRVLSRLLSPLEVKQIMKAEKECTANQLRPEQLIVNGYPLKPEEMADLLNCLLPPQKLKPGRYWYDKESGLWGKEGEKPDRVISSNLNFTGKLSPDASNGNTEVYINGREITKLELRILKLANVQCPRDTHFWVYDDGRYEEEGQNNIRGNIWEKASTRFMCALFSLPVPQGQPRGTVQPSSNYATVPNYIEHKKIQKLLLLGIEGSGTSTIFKQAKFLYGNKFSVEELQDIKLMVQSNMYRYLSILLDGRERFEEEALSHTRGLNAVEGDSGGEEANDEGTVTTPQSVYTLNPRLKHFSDWLLDIIATGDLDAFFPAATREYAPLVEEVWKDPAIQATYRRKDELHFLPDVAEYFLSRAMEVSSNEYEPSERDIVYAEGVTQGNGLAFMEFSLSDHSPMSESYPENPDALSSPQPKYQLIRVNAKGMNDSCKWVEMFEDVRAVIFCISLSDYDQINITPESSGTVQYQNKMIQSKELFESMVKHPCFKDTPFILILNKYDQFEEKLNRAPLTSCDWFSDFCPVRTNNNVQSLAYQAYFYVAMKFKLLYFSITGQKLFVWQARARDRANVDEGFKYVREVLKWDEEKEESYLNGGGEDSFYSTDMSSSPYRPEE
The following text describes a protein:
Function:
SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity.
Sequence:
MKFLHTADLHLGKIVSGVSMLAEQEYILTQITQIAEEEQVDALILAGDLYDRAVPPADAVKVLNDILVKWNVELGIPIFAISGNHDSAERLAFGSQWYESSKLYMKGKCTSQFDGIPFMDAEVWLVPYHEPAIIRQAFADNSIRSFEDAMQAVTKQIRSKWDTSKAQILVGHAFVSGGIPSDSERQLAIGNVDRVSTDCFDGFTYTALGHLHHPHAIRHPSIFYSGSPLKYSFSEANDHKSVRIVELEGKELISVTERFLTPKHDMRIISGTLAELTENLVENPDDFFQVNLMDEGALIDPMGKLRQFYPNILHLERKKQTLKETQDSFEEIMKKDDLELFGQFFEHVNGTELTETQKQKLADVFEQARKEDAE
The following text describes a protein:
Function:
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAISSSTKERHRRTVLSIAVKSRVLVLTLFFVWRWLADPYDTSAELNRPCLAENSAWSADIDGATDADRWAPRLGRAIEKSVVWDGVYYVKIAECGYEYEQVHAFLPLLPLLMRFVARTFLPKLIPLLGLRATLALAGYLINNVSFVLAAYFLYRLTRALLEDEKLALTAAALFCFNPASAFYSAVYSESLFALLSFTGLVCFVSGAKWPSIVFFGLSSGVRSNGILHAGFFLFQAMHKVFHLASLQRSSMRIVSIVLVAILQSVAVAAPFLAFQTYGYFQLCHDQIRSPPRPWCKSPLPYLYGFVQSQYWQVGFLRYFQLKQLPNFLLASPMLSLAIFSIFTYAKKQPKLLFSLGLAASPSTQSKVAMFSHVDEMTFLAKGKGASKGPGGEDYKVASRGFFSPAAVCFLIQLCFMTAVAMFVMHVQVATRFLSVSPPVYWCGAHLLLNGGARGKTGKLIWSSFLAYVSVGSLLFINFYPFT
The following text describes a protein:
Function:
May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane.
Sequence:
MSDIVPTAPKKPADETENQITSPDPRPGAPPEYSSSFVPGPPGLAIPPPAGYPGGLPMGYYGPHHPSTFPLYMHTGSIRPIQYQPGKYPAPQSSAPVVWMPMPTPIPHCPPGLECLAQLDNIHVLQHFEPLEMITGFETNNRYDIKNNTGQMVYFVTEDTDDYTRNAYRTLRPFVLRVTDCMGREVMTMQRPFRCTCCCFCCPSARQELEVQCPPGVTIGFVAEHWNLCRAVYSLQNEKKEDMMGVLGPCSTYGCGSDSVFEILSLDGVSIIGSITRKWNGVLSAMSDADHFEIHFPLDLDVTMKAMIFGACFLIDFMYFESSPPQHSNIHHH
The following text describes a protein:
Function:
Acts as an important epigenetic regulator through multiple silencing mechanisms. Involved in association with RRP6L1 in the silencing of the solo LTR locus. Controls levels of non-coding RNAs (ncRNAs) from the solo LTR locus. Seems to function independently of the RNA-mediated gene silencing (RdDM) pathway. Functions redundantly with RRP6L1 in the regulation of FLC locus. Participates in the maintenance of trimethylated 'Lys-27' (H3K27me3) at FLC locus via the regulation of antisense long non-coding RNAs (lncRNAs) and the regulation of diverse antisense RNAs derived from the FLC locus. Seems not involved in the exosomal RNA degradation. May be involved in poly(A)-mediated RNA degradation.
Subcellular Localization:
Nucleus. Nucleus, nucleolus. Cytoplasm. Note=Localizes predominantly in the nucleus.
Sequence:
MSDGNMDVDESPVSWKVKSLEKLIDGSSFSSTLSRLSSSSRLIPTSRDFHFYYNFDEFKRPIDEITGTSQSTLATIGDSEQVWGKSMKFPGDVDDVYAEDWLCNVNDELIERFDVSVDEFQRIRKKEKEIGRSVVADDGDDGFQMVYGKKKKPVGNVVTGSAAVNGGGSVIDVKMAERDKNSSGKAKVPFHVPTIKKPQEEYNILVNNANLPFEHVWLERSEDDLRAMHPLEKFSVLDFVDKDVNEMEPVKPLPLEQTPFKFVQEVKDLKELVAKLRSVEEFAVDLEHNQYRSFQGLTCLMQISTRTEDYIVDTFKLRIHIGPYLREIFKDPKKKKVMHGADRDIIWLQRDFGIYVCNLFDTGQASRVLNLERNSLEFLLQHFCGVTANKEYQNADWRIRPLPEEMTRYAREDTHYLLYIYDLIKLELQRMAKDDAHTDSPLLEVYKRSYDVCTQLYEKELLTENSYLHVYGLQAAGFNAAQLAIVAGLCEWRDFIARAEDESTGYVLPNKVLLEIAKEMPDSVGKLRRMLKSKHPYIERNVDSVVSVIRQSMQHYAAFESAALSLKDVSPGNVMDKNIEPISEKKDLHTGDVASPSLKENSSQLESTRDLIMGAANTNEGRGLGSGLFGSAKVSAAVRISKKPSSGLGALLGNAASKKKSRTDEKVKEDVKLEQIRSSVNLSFHSFTEKVPDSKSTSETSPKVYGKPEEMSSTMPASVSKEDGVKELKDDSEEASEIVGTSGRVSESKVSSSEMGDIILLENGDEKKVDAEDEPMSLSELSTNFQKCFKSMNKSKKAQKQTEFLNIEPFDYEAARKEVKFGEGHKGRQGKREAAAGQKKGSTQEQSEFGQGKRRQAFPASGNRSMSFKN
The following text describes a protein:
Function:
Catalyzes the reduction of glutathione disulfide (GSSG) to reduced glutathione (GSH).
Sequence:
MATSLSVSPSLSLNTLFFAKALPLSRPSLLSLPLPKSLLSLSTRRRTFAVRAESQNGADAVPAHYDFDLFTIGAGSGGVRAARFAANYGASVAICELPFSTISSETTGGVGGTCVIRGCVPKKLLVYASKFSHEFEESNGFGWRYDSEPKHDWSSLIANKNAELQRLTGIYKNILNNAGVKLIEGHGKIIDPHTVDVNGKLYSAKHILVTVGGRPFIPDIPGNEYAIDSDAALDLPTKPEKIAIVGGGYIALEFAGIFNGLKSEVHVFIRQKKVLRGFDEEIRDFVSEQMSVRGIEFHTEESPQAITKSADGSFSLKTNKGTVDGFSHIMFATGRRPNTQNLGLESVGVKIAKDGAIEVDEYSQTSVPSIWAVGDVTNRINLTPVALMEGGALVKTLFQDNPTKPDYRAVPSAVFSQPPIGQVGLTEEQAVQQYGDIDIFTANFRPLKATLSGLPDRVFMKLVVCAKTNEVLGLHMCGDDAPEIVQGFAVALKARLTKADFDATVGIHPSAAEEFVTMRTPTRKIRKSESSEGKSGSEAKTAAGV
The following text describes a protein:
Function:
Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MTFVSDLFAIALGGSIGAVLRYLITLTVVSAPLSGWLTLHGSVGTTLANLLGCCALGGLFQFSQALVASDWVATGWAASLAHPRTLLAVRIGVLGSLTTFSTLIGETAVFASQGRILASSMLLGINVIAGWCLFWAAAAVVRNWTS
The following text describes a protein:
Function:
Receptor for dopamine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MLSPFDWRRGISSSGTGGTMAAQPLSSTAATTAAATGATAATAATAATTSATLSTAAASTSTTAAPSAGATWINHHLAVEADSSQPANGSDAQAGVEGPTMPAGYLPLYEDVETAAEDAGYALIDDISEWLLGSVGSEAAVGGPENSTNLAVTGANGTLAWLEALNSTQPAQSNSSAEDGERGRYSLRSFVEQQLAGGGAAGAGDGGDAGIALIDSGEEAALDNVADAETDYGMLGGFGDAELLQRTATVARETLGNRTAPSTTSYDGGGSGDVGVAGGLAGTAGGGVGGAGGSGGSTFMLLLENFNDYFPNYNGSTVSGTSTIAPGVAITGSRGSGLLLEQNLTGLYLDGYRLNCTNETLNLTDSCGELRVVDHNYWALILILFPILTLFGNILVILSVCRERSLQTVTNYFIVSLAIADLLVAVVVMPFAVYFLVNGAWALPDVVCDFYIAMDVICSTSSIFNLVAISIDRYIAVTQPIKYAKHKNSRRVCLTILLVWAISAAIGSPIVLGLNNTPNREPDVCAFYNADFILYSSLSSFYIPCIIMVFLYWNIFKALRSRARKQRAARKPHLSELTGGSVIENIAQTRRLAETALDSSRHASRILPDEAATNTASGSNEEEDENAISPDIDDCHVIVNDKSTEFMLATVVEETGNSVVAQITTQPQLVVADPNGNHDSGYAASNVDDVLAGVAPASASAATSAAPRSSGSPPDSPLPSGATLQRSSVSSQRRPTGDDSPKRGEPALRSVGVDNSSVAMKPLSFVRYGVQEAMTLARNDSTLSTTSKTSSRKDKKNSQASRFTIYKVHKASKKKREKSSAKKERKATKTLAIVLGVFLFCWLPFFSCNIMDAMCAKFKKDCRPGLTAYMMTTWLGYINSFVNPVIYTIFNPEFRKAFKKIMHMG
The following text describes a protein:
Function:
Broad spectrum monooxygenase that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including xenobiotics. Catalyzes the S-oxygenation of hypotaurine to produce taurine, an organic osmolyte involved in cell volume regulation as well as a variety of cytoprotective and developmental processes. In vitro, catalyzes the N-oxygenation of trimethylamine (TMA) to produce trimethylamine N-oxide (TMAO) and could therefore participate to the detoxification of this compound that is generated by the action of gut microbiota from dietary precursors such as choline, choline containing compounds, betaine or L-carnitine.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MVKRVCVIGAGAAGLVSVKSCLDDGLEPVCYEFSSEIGGLWNNNERKRNNLSPKAYSTLITNVSKETSAFSDLPMPEEWPAYQTWQQYYQYFHLYADKFDLRRYIHFNVSVEEVVKSENYIETGSWVVQTRDVTTGKEKKEEFDAVIVASGRTGKQIWVTYPGLEDKFRGKVLHSGNYESAEEFKDKSVLVIGASNSGCDVAVDSSSYCKDVFISTRNGFWLVPRIFTHGKPLLMALSNRFKRGLQSFVPGWIINKVFIGMAEVRMNHEALGIRSKFGPMNPRATVTVSDELPLKIYSGLVKVRPEVKSFGEDHVTFVDGKTEAIDLIVMATGFAPKFEFLSKDIIPEQPEDMRLHKWIFPFNLEHPSTLTFVGSCMPVGSGPLNNTHELQARYVTQVLSGKTKLPSADRMQNMWSDQRKEMLKKTGGVFKFKVPIFEYQEEIAGEIGVLPSFFRLLFTDPRLAFNFYFGPLLPYHYRIVGENSKPECREYAL
The following text describes a protein:
Function:
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Sequence:
MIEKIWSGESPLWRLLLPLSWLYGLVSGAIRLCYKLKLKRAWRAPVPVVVVGNLTAGGNGKTPVVVWLVEQLQQRGIRVGVVSRGYGGKAESYPLLLSADTTTAQAGDEPVLIYQRTDAPVAVSPVRSDAVKAILAQHPDVQIIVTDDGLQHYRLARDVEIVVIDGVRRFGNGWWLPAGPMRERAGRLKSVDAVIVNGGVPRSGEIPMHLLPGQAVNLRTGTRCDVAQLEHVVAMAGIGHPPRFFATLKMCGVQPEKCVPLADHQSLNHADVSALVSAGQTLVMTEKDAVKCRAFAEENWWYLPVDAQLSGDEPAKLLTQLTLLASGN
The following text describes a protein:
Function:
Functions in endoplasmic reticulum to Golgi vesicle-mediated transport and regulates the proper organization of the endoplasmic reticulum and the Golgi (By similarity). Plays a key role in targeting to neuronal dendrites receptors such as HTR1A. Plays also a role in primary cilium and sperm flagellum assembly probably through protein transport to these compartments (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein. Note=Shuttles between the endoplasmic reticulum, the intermediate compartment and the Golgi apparatus.
Sequence:
MHATGLAAPAGTPRLRKWPSKRRVPVSQPGMADPHQFFDDTSSAPSRGYGGQPSPGSLGYPTSSSEAAFLAAPMSNMAMAYGSSLAAQGKELVDKNIDRFIPVSKLKYYFAVDTVYVGKKLGLLVFPYLHQDWEVQYQQDTPVAPRFDINAPDLYIPAMAFITYILVAGLALGTQDRMIGGVLTGLLFGKIGYYLVLAWCCVSIFVFMIRTLRLKILAQAAAEGVPVRGARNQLRMYLTMAVAAAQPVLMYWLTFHLVR
The following text describes a protein:
Function:
Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to norspermidine and 1,3-diaminopropane to yield norspermine, and to spermidine to yield thermospermine. It can also synthesize thermospermine from putrescine (1,4-diaminobutane) and caldopentamine from norspermine with a very low activity. The biosynthesis of caldohexamine and caldoheptamine from caldopentamine has been also observed.
Subcellular Localization:
Cytoplasm.
Sequence:
MSKVPGPIVLMEPLSGKTSLIIKINAIHVSKRSKYQGILIVDTDDYGRTLVLDDYIQSSYYDEIYYHESLVHPAVTTHPRPSDVLILGGGEGATLREVLKHNTVKRAVMVDIDGDVVELSKKYLPQMHQGAFDDPRSEVRIEDGFVYVENALKRGEKFDVVIMDLTDPYSSDIAKQLYTPEFFGKVKRLLREDGIVVTQAGNSFYFPEAYDYVLQGVKGNFPIIAEYSVWIPSFGYAVNFVLGSLKHDPHSLSAEEVDKRLSERGVRAEFYSGKTHIALMNMPVIKKILRV
The following text describes a protein:
Function:
Negative regulator of the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase required for proper mitotic and meiotic progression and cell fate determination. Involved in entry into both meiosis I and meiosis II. Prevents endomitosis by preferentially inhibiting APC/C(CDC20). Required for megagametophyte and endosperm development. Triggers mitotic cyclins (e.g. CYCB1-1 and CYCB1-2) accumulation. Confers immunity to bacterial pathogens (e.g. Pseudomonas syringae pv. tomato DC3000), which is associated with increased expression of disease resistance (R) genes. GIG1 and PANS1 are part of a network linking centromere cohesion and cell cycle progression through control of APC/C activity.
Sequence:
MPEARDRTERPVDYSTIFANRRRHGILLDEPDSRLSLIESPVNPDIGSIGGTGGLVRGNFTTWRPGNGRGGHTPFRLPQGRENMPIVTARRGRGGGLLPSWYPRTPLRDITHIVRAIERRRGAGTGGDDGRVIEIPTHRQVGVLESPVPLSGEHKCSMVTPGPSVGFKRSCPPSTAKVQKMLLDITKEIAEEEAGFITPEKKLLNSIDKVEKIVMAEIQKLKSTPQAKREEREKRVRTLMTMR
The following text describes a protein:
Function:
With EMP70 and TMN2, plays a critical role in the late stages of a nutrient-controlled pathway notably regulating FLO11 gene expression. Acts downstream of RAS2 and TOR. Essential for cell adhesion and filamentous growth. May play a role as effector of cellular copper homeostasis.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MRVRPKRSVITLMAIVVVMLILRNQFYSSRTRGHGQEPVISSSQKNLYDGWITPNFYRKGDPLELIVNKVESDLTQLPYAYYDLPFTCPPTMHKKPLHLSLNEIIRGDRKWESDYKLKFGEDNPCETLCARKTTKEGMQTLDKLVREGYVVQWLIDDELPAATTFISTTDHKKYYASGFPLGFIDPDTDKTYLHNHVMLVIRFHASDNDKNTIVGFEVYPRSVSDYHCPGASKNYEQYEIVIPEDENELTYLPFTYSVYWREEFEVDWNHRWDYFLNAGELSDEQSIQFHWMSLANSVGIVLSISFITLIIYVRVMYTDKSNSKSPKYMINIEGIETEDDLDDDKYGKYSVYTVAKDWIQNGRPNLFGLKVLILLVSFGVQFLFTIIGSLTISCSMNKLHNVRNSVLTMAILFFVLGAFMASFVGTRLSMVTKTKRTKANYLDDNRYLKDYKKFSPIFTILCGSSLPGIVMVSTFLLNSIVWAHDSTSALPFKTIVFFMSIYFIVCIPLSLFGGIVANNIPLPQYWLSGITKDESNSDGNGLFVPKSRAKFNPLVYCGIYLCGIFPLLVIYVEMQYVYKSLWLEKTTFYYFYGFLFLSIILLCVLTMEISIIGSYLLMRFCFEDKVVRNNWRWKCFEMGFSGGVYMELYSLYYIFAVLNIHGFSSILISICYSLIFNVMCSLGLGALSYLTASWFINKIYHQKVNL
The following text describes a protein:
Function:
Putative transcription activator involved in regulating light control of development.
Subcellular Localization:
Nucleus. Note=The nuclear localization is independent of the light treatment.
Sequence:
MDVHLVEENVSMGNHEIGDEGDVEPSDCSGQNNMDNSLGVQDEIGIAEPCVGMEFNSEKEAKSFYDEYSRQLGFTSKLLPRTDGSVSVREFVCSSSSKRSKRRLSESCDAMVRIELQGHEKWVVTKFVKEHTHGLASSNMLHCLRPRRHFANSEKSSYQEGVNVPSGMMYVSMDANSRGARNASMATNTKRTIGRDAHNLLEYFKRMQAENPGFFYAVQLDEDNQMSNVFWADSRSRVAYTHFGDTVTLDTRYRCNQFRVPFAPFTGVNHHGQAILFGCALILDESDTSFIWLFKTFLTAMRDQPPVSLVTDQDRAIQIAAGQVFPGARHCINKWDVLREGQEKLAHVCLAYPSFQVELYNCINFTETIEEFESSWSSVIDKYDLGRHEWLNSLYNARAQWVPVYFRDSFFAAVFPSQGYSGSFFDGYVNQQTTLPMFFRLYERAMESWFEMEIEADLDTVNTPPVLKTPSPMENQAANLFTRKIFGKFQEELVETFAHTANRIEDDGTTSTFRVANFENDNKAYIVTFCYPEMRANCSCQMFEHSGILCRHVLTVFTVTNILTLPPHYILRRWTRNAKSMVELDEHVSENGHDSSIHRYNHLCREAIKYAEEGAITAEAYNIALGQLREGGKKVSVVRKRIGRAAPPSSHGGGIGSGDKTSLSAADTTPLLWPRQDEMIRRFNLNDGGARAQSVSDLNLPRMAPVSLHRDDTAPENMVALPCLKSLTWGMESKNTMPGGRVAVINLKLHDYRKFPSADMDVKFQLSSVTLEPMLRSMAYISEQLSSPANRVAVINLKLQDTETTTGESEVKFQVSRDTLGAMLRSMAYIREQLSIVGELQTESQAKKQRK
The following text describes a protein:
Function:
Catalyzes the conversion of 2-hydroxy-1,4-benzoxazin-3-one (HBOA) to 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA).
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MALQAAYEYLQQAVGHGAWSSTQTLTLLLIAVPTVLLLLASLAKSTSSSGRGKPPLPPSPPGTLPIVGHLHHIGPQTHISLQELVAKYGHNGFLFLRAGAVPTLIVSSPSAAEAVMRTHDHICASRPWSMASHILRYNTCDVAFSPLGEYWQQTRKLMNTHLLSNKKVYSFRHGREEEVCLVVDNLREAAAKSPSTAVDMSEVLAAYTNDVVSRSVLGSTHRKKGRNTLFREMTMTNVDLLVGFNLEYYIPRWPLTDLLFRLVCWKVTRHLKRWDALLEEVIHEHVEMRKLSGDKEKESDDFIDIFLSRYEEYGFTMDNVKSLLMNVFEAAIETSYLVLESAMAELMNHRRVMKKLQAEVRAYGAEKKLDMIREDDLSSLPYLKASMKEALRLHPPGPLLLPHYSTADCQIDGYHIPANPRVLVNGWAIGRDPAVWEKPEEFMPERFMRDGWDKSNSYSGQDFRYLPFGSGRRICPGANFGLATMEIMLANLMYHFDWEVPNEKEDGCWKVSMDEKFGLMLRRNELLYLVPRASS
The following text describes a protein:
Function:
Cleaves the 2'-5' phosphodiester linkage at the branch point of lariat intron pre-mRNAs after splicing and converts them into linear molecules that are subsequently degraded. It thereby facilitates ribonucleotide turnover.
Subcellular Localization:
Nucleus.
Sequence:
MIIAVEGCAHGELDQIYRSVENLARQKNVKVDLLICCGDFQAVRNESDLQCMAVPDKFRHICTFYKYYNGELKAPILTIFIGGNHEASNYLQELAYGGWVAPNIYYLGYAGVVKFGGIRIAGISGIFKGHDYLKGHFEKPPYTNSTMRSAYHVRSLEVFRLKQLKEDIDIFISHDWPRGVYNYADTRELLHWKPFFRDEIAQNVLGSQAGETLLHELKPKHWFAAHLHCRFAATIQHNEKQSTQFLALDKCLPRRQYLELVEIQHDSTQNLELCYDPHWLAILRSTNHLMSVRPTTQYMPSGGPGCTERWNFNPNEEEIEQVKTIFDNDYKIPSNFSLTAEPFKPRPNYNRNAQQAQAQLNPQTTQFCEKLGIDDPLEKLIGKPIILTAPVVNPDEIALEDDEEEETGDHTEEVAGEDNGIFFVDTKPLKRSKMSLPQPQNEAHEEEPHTAEKEAPLGGILDENDSFAKVADQDVPTIVKKFKRRNQELYMDQESST
The following text describes a protein:
Function:
Cap-specific adenosine methyltransferase that catalyzes formation of N(6),2'-O-dimethyladenosine cap (m6A(m)) by methylating the adenosine at the second transcribed position of capped mRNAs. Recruited to the early elongation complex of RNA polymerase II (RNAPII) via interaction with POLR2A and mediates formation of m6A(m) co-transcriptionally.
Subcellular Localization:
Nucleus.
Sequence:
MAATKETGRAAAPSGKRRRGLRHPASDSQTLARLAAGPWLPGVLTCSKRTRGDAATRSARPPVLPPPPRPPQRRCRHLVSRAGTLRCACVGTASEGPRHGRAAILSVAMLAGSPDRDCFLPPPPQLPIFRSFSVSLVVLKRRKSSFALLEM
The following text describes a protein:
Function:
Malate-sensitive anion transporter permeable to chloride, nitrate, sulfate and malate. Involved in dark-, CO(2)-, abscisic acid- and water-deficient-induced stomatal closure. Belongs to the R-type anion channels.
Miscellaneous:
MISCELLANEOUS: Malate functions as a gating modifier as well as a permeating substrate.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Note=PubMed:20626656 also indicates a not confirmed endomembrane localization.
Sequence:
MSNKVHVGSLEMEEGLSKTKWMVLEPSEKIKKIPKRLWNVGKEDPRRVIHALKVGLSLTLVSLLYLMEPLFKGIGSNAIWAVMTVVVVLEFSAGATLCKGLNRGLGTLIAGSLAFFIEFVANDSGKVLRAIFIGTAVFIIGAAATYIRFIPYIKKNYDYGVVIFLLTFNLITVSSYRVDSVINIAHDRFYTIAVGCGICLFMSLLVFPIWSGEDLHKTTVGKLQGLSRSIEACVDEYFEEKEKEKTDSKDRIYEGYQAVLDSKSTDETLALYANWEPRHTLRCHRFPCQQYVKVGAVLRQFGYTVVALHGCLQTEIQTPRSVRALFKDPCVRLAGEVCKALTELADSISNHRHCSPEILSDHLHVALQDLNSAIKSQPKLFLGSNLHRHNNKHQNGSISNNKHHQRNSSNSGKDLNGDVSLQNTETGTRKITETGSRQGQNGAVSLSSFRTDTSALMEYRRSFKNSNSEMSAAGERRMLRPQLSKIAVMTSLEFSEALPFAAFASLLVEMVARLDNVIEEVEELGRIASFKEYDNKRDQTADDVRCENPANVTISVGAAE
The following text describes a protein:
Function:
Catalyzes the GTP-dependent phosphorylation of 5-hydroxy-L-lysine.
Subcellular Localization:
Cytoplasm.
Sequence:
MKPVASVRPALSKEDVLGILSERYCLQGVLEVKELPSYEDRNYYVKTEKEQPNEFVLKIMNSSDSTRIHVDGEIEFQKVLNLKGFCCPEHMQDVNGNYKSYIQLGDSRHMVRLLTYLPGTVLGGIIRSPDVLVAIGKYVADVHNATKDFRHPCLRDNPEYIWSLENVPKLHMYLDYISDDGGKDLVREAIKLFEKNVIPNMNLFEHGTIHGDINEGNLIVLANSVTKQGIQINRETMGLIDFNESNISCLIFDLTCAVTYMMIENKGVLEDFVDAGGYVIGGYLKNRPISELEISLLPYCVLGRYAQTLSISTYTQTLDPKNQHIFTTSHSGWEQLEILIKKGADEILRRWREIASSTT
The following text describes a protein:
Function:
Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MEKKTKIPPLMNAVKDEKITEITPSSSSSSHQRETNLIDLTIDIQINILTRLSMKSLFQFRSVCKSWRTLLLTREIAVHLDQVSDKIYTLTTNADELWLRGIRRFKIPIELQSLEFMLLEPVNGIICIIGPVSSHVTFAYLWNPLTNEFKHLPKPNVQMGYVAVGFGFGFAPKSNDYKVVRVVQHERKFDSHAEVYSLNRGSWRRVKDDSCSSSSAWMNRILQGVVTVDLENEVTTEEERMSFDHKNHQADHSFSKLLHISLCFASNVMGSIEHRTHNGMIVTSALIIWKALMCVTGSESPVVVVLSGSMEPGFKRGDILFLHMSKDPIRAGEIVVFNVDGREIPIVHRVIKVHERKDTGEVNVLTKGDSNLEDDRLLYAQGQLWLQRHHIMGRAVGFLPYVGWVTIIMTEKPIIKYILIGALGLLVITSKD
The following text describes a protein:
Function:
Uses geranylgeranyl diphosphate to catalyze the cis-prenyl chain elongation and produce polyprenyl diphosphate with a chain of 35 carbons.
Subcellular Localization:
Plastid, chloroplast. Note=Localizes in punctuate patterns inside the chloroplasts.
Sequence:
MLSLGFSLPPPSDNKLIITNNNQYNYRTNLANVCSNNNVNAVGDQLVTLPEGLKHVAVIMDGHRRWAKNKGLTVKQGHRAGGEKIQVLTRLCSQWGVKVLTIFAFSTENWVRLEEEVDFLMKLFLELIGSQEILDEWTRDGRRVSFIGDKSIFSKSLQEALAVMEERTKFNSGLHVIIAINYSGRQDILQATKSIAIKVKNGDLTVKDIDQSLFEQELDTHCTEFSEPDLLIRTSGEKRVSNFMLWQLAYTELYFANKLFPDMEEADFIEALTSFKSRQRRYGGKKI
The following text describes a protein:
Function:
Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport. Binds 2 molecules of cholate per subunit.
Subcellular Localization:
Cytoplasm.
Domain:
Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Sequence:
MAFSGTWQVYAQENYEEFLKALALPEDLIKMARDIKPIVEIQQKGDDFVVTSKTPRQTVTNSFTLGKEADITTMDGKKLKCTVHLANGKLVTKSEKFSHEQEVKGNEMVETITFGGVTLIRRSKRV
The following text describes a protein:
Function:
Cysteine protease. In the mosquito midgut, required for parasite development.
Miscellaneous:
MISCELLANEOUS: Able to cleave native host hemoglobin; however, hemoglobin is likely not to be the physiological substrate.
Subcellular Localization:
Membrane; Single-pass type II membrane protein. Cytoplasmic granule. Note=Localizes to punctate structures, likely dense granules, at the apical end of merozoites.
Sequence:
MVAIKEMKEFAFARPSLVETLNKKKKFLKKKEKRTFVLSIYAFITFIIFCIGILYFTNKSSAHNNNNNKNEHSLKKEEIELLRVLLEKYKKQKDGILNESSNEEDEEKYTLNSETYNNKNNVSNIKNDSIKSKKEEYINLERILLEKYKKFINENNEENRKELSNILHKLLEINKLILREEKDDKKVYLINDNYDEKGALEIGMNEEMKYKKEDPINNIKYASKFFKFMKEHNKVYKNIDEQMRKFEIFKINYISIKNHNKLNKNAMYKKKVNQFSDYSEEELKEYFKTLLHVPNHMIEKYSKPFENHLKDNILISEFYTNGKRNEKDIFSKVPEILDYREKGIVHEPKDQGLCGSCWAFASVGNIESVFAKKNKNILSFSEQEVVDCSKDNFGCDGGHPFYSFLYVLQNELCLGDEYKYKAKDDMFCLNYRCKRKVSLSSIGAVKENQLILALNEVGPLSVNVGVNNDFVAYSEGVYNGTCSEELNHSVLLVGYGQVEKTKLNYNNKIQTYNTKENSNQPDDNIIYYWIIKNSWSKKWGENGFMRLSRNKNGDNVFCGIGEEVFYPIL
The following text describes a protein:
Function:
RNA-binding protein involved in regulation of mRNA stability. Binds AU-rich regions in the 3'-UTR of mRNAs and promotes their stabilization by recruiting a MKT1-containing complex. Stabilizes chaperone mRNAs during stress that causes an accumulation of misfolded or unfolded proteins in the cytoplasm.
Subcellular Localization:
Cytoplasm.
Domain:
The zinc finger domain binds AU-rich regions in the 3'-UTR of mRNAs.
Sequence:
MSTATSAPVVESMSDTVVCPQLSRHSTSLEELYTIGYNRSHSPSCFSSAGCEEEEGQKNVLAERYKTKLCKNFVQYGTCPYDIRCMFAHGEEELRTAEMNIMDGLVTKDAITSFQKLWHRAVSASSGSKHHSSHVANRRGVMTTATTTTTAGGSTDAAMHICRRMQRVVAAAAAAVPCGGRRVVSGSIRIRGCVRHNPYCHNILPTVSRYYSTMPDVFTRPYSKSDSCGNEAITEGNAWTYANEEGNEKETPAMISSGVPELTAWKRFNYVAERSQCTSVPEQNLPCADFAAIKESNNTGGNASGVDVENVDDAEHSTCSSVGNESGYFCRASRSASCGEQSQSHLKREGNEGRGEGLHMFLSL