lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in the biosynthesis of the major light-harvesting pigment bacteriochlorophyll c (BChlc), which confers a significant competitive advantage to green sulfur bacteria living at limiting red and near-infrared light intensities. Catalyzes the methylation at the C-20 position of the cyclic tetrapyrrole chlorin of bacteriochlorophyll d (BChld) to produce bacteriochlorophyll c (BChlc) using S-adenosylmethionine (SAM) as a methyl source.
Sequence:
MSNNDLLNYYHRANELVFKGLIEFSCMKAAIELDLFSHMAEGPKDLATLAADTGSVPPRLEMLLETLRQMRVINLEDGKWSLTEFADYMFSPTPKEPNLHQTPVAKAMAFLADDFYMGLSQAVRGQKNFKGQVPYPPVTREDNLYFEEIHRSNAKFAIQLLLEEAKLDGVKKMIDVGGGIGDISAAMLKHFPELDSTILNLPGAIDLVNENAAEKGVADRMRGIAVDIYKESYPEADAVLFCRILYSANEQLSTIMCKKAFDAMRSGGRLLILDMVIDDPENPNFDYLSHYILGAGMPFSVLGFKEQARYKEILESLGYKDVTMVRKYDHLLVQAVKP
The following text describes a protein:
Function:
Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Sequence:
MWTFLGIATFTYFYKKFGDFITLANREVLLCVLVFLSLGLVLSYRCRHRNGGLLGRQQSGSQFALFSDILSGLPFIGFFWAKSPPESENKEQLEARRRRKGTNISETSLIGAAACTSTSSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIHDQESKSEVQIPYPLSENNQVQSGRAFHHGRFIMSLRKAAMAEPNAKFIEGVVLQLLEEDDVVMGVQYKDKETGDIKELHAPLTVVADGLFSKFRKSLVSNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVLVDVRGEMPRNLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIKLWRKLLKGIPDLYDDAAIFEAKKSFYWARKTSHSFVVNILAQALYELFSATDDSLHQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLVLIGHFFAVAIYAVYFCFKSEPWITKPRALLSSGAVLYKACSVIFPLIYSEMKYMVH
The following text describes a protein:
Function:
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MAARRIGQYVPDWVKIASRVPAEGRADMARFRSIYDNLKSGLDSVPAKAETIDWAFYQKNISKPGMVESFRKAYEAITVPYPKDTQTAKIDVVEKEMAQECEKLMRESRMRIKEYQAEMEKIKSQKSFEDMTVDEYLEMHPELKKQADEEIKKHIWN
The following text describes a protein:
Function:
Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation and accurate chromosome segregation. A member of the RNA-induced transcriptional silencing (RITS) complex which is involved in the biosynthesis of dsRNA from primer siRNAs provided by the RNA-directed RNA polymerase (RDRC) complex.
Subcellular Localization:
Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body.
Sequence:
MEKGIKKYLPSLPFLACISDFPENHGTSRRSATVSLERVHELFTEHWLSNLKNRREKRQELAEEAVYCRSEMLSQRKLLAAVDFPQQLKNSPAKAKATHTSSGVTKEVRASKKYTSSNVEFPLVTDGKEKPVKSKQLRKNSVTEFEKPIETKKSKHRKSRNKFLDKSSGSMEIESWDNSTSDSIIESSSRLHESISLRENDIRSSDSKSVGWDDNSTGFRESSKSLDHTDTSMFMELDSNSDPQFRPKYQAKSSWFAPDDPEASWGNLDDGWGETNGSWSSTDDTKHYKNEWAESINLDNFNRPSQQEDYDKPKNTQVSRSSNHHRRYDSYHPDSRSDSYRSKREHYDNRDTGPRSKHLEKSSYVYNQNFEDRTHLSDHGAHFHLGNANDFNMQGSSRKRKASDRQRESRENELPTKKLNASDSHNPLASLTTDKNDLYINWLKSLSFFQTNSSCAEALVKVIPHYHNKLIDFSQVLQLVFSASEKFPIQENQPLPEQLMFLSNLEKQTPFAKAVGSSIYKLVTGKNLSLDFASQILKEASILEHKNEK
The following text describes a protein:
Function:
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.
Sequence:
MAKRDILPVFPSRANSVIMKQRVLAARRGVGLLKRKRDAIDMKLRELRRIRFDQDMHGDEAMRNAIFSMAKANLLGADFKPQMVSRSHVATVSLRRTEIKIVGVKLNTLELETKGVGAFPLAGLSCGGMQVSRIRDSYTKALKALVEFASLEYQVRMLEAASLQTNMRVNALEHVVIPILQNTYNYICGELEEFEREDFYRLKRSQAKQLEAKMAFTELIKTKNMTDEELETYIKRNINQTRPPAADTPFDQEQFEEREVKRRMREARLSLKQRREQERKEAIKRGEPPPPTSFITTHGASLSFAGRQRDPRASSGDLYSTKRMLLSSGPERKSASNVTERKSDTPPRNSQETQRRSSQMSKDVVNEDPPEES
The following text describes a protein:
Function:
Plays a crucial role in the regulation of neural stem cells (NSCs) proliferation. Enhances the phosphorylation of GSK3B through the PI3K-Akt signaling pathway, thereby upregulating the Wnt/beta-catenin signaling pathway and promoting the proliferation of NSCs. Improves ischemic stroke recovery while inhibiting neuroinflammation through small extracellular vesicles (sEVs)-mediated mechanism. Enhances the secretion of sEVs from NSCs, which in turn inhibit both the MAPK and NF-kappaB pathways in microglia. This inhibition suppresses the pro-inflammatory M1 polarization of microglia, promoting a shift towards the M2 anti-inflammatory phenotype, which is beneficial for reducing neuroinflammation.
Subcellular Localization:
Nucleus.
Sequence:
MVEPGQDLLLAALSESGISPNDLFDIDGGDAGLATLTPTPPVQQSVPLSALELNLETEAAVPVKQEPETVSTPALLNVRQQPPSTTTFVLNQINQLPTLGSTIVMTKTPPVTTNRQTITLTKFIQTTANTRPSVSAPAVRNAMTSAPSKDQVQLKDLLKNNSLNELMKLKPPANIAQPVATAATDVSNGTVKKESSNKEVARIWINDVKMRSFSPTMKVPVVKEEDEPEEEDEEEMGHAETYAEYMPIKLKIGLRHPDAVVETSSLSSVTPPDVWYKTSISEETIDNGWLSALQLEAITYAAQQHETFLPNGDRAGFLIGDGAGVGKGRTIAGIIYENYLLSRKRALWFSVSNDLKYDAERDLRDIGAKNILVHSLNKFKYGKISSKHNGSVKKGVIFATYSSLIGESQSGGKYKTRLKQLLHWCGDDFDGVIVFDECHKAKNLCPVGSSKPTKTGLAVLELQNKLPKARVVYASATGASEPRNMAYMNRLGIWGEGTPFREFSDFIQAVERRGVGAMEIVAMDMKLRGMYIARQLSFTGVTFKIEEVLLSQSYVKMYNKAVKLWVIARERFQQAADLIDAEQRMKKSMWGQFWSAHQRFFKYLCIASKVKRVVQLAREEIKNGKCVVIGLQSTGEARTLEALEEGGGELNDFVSTAKGVLQSLIEKHFPAPDRKKLYSLLGIDLTAPSNNSSPRDSPCKENKIKKRKGEEITREAKKARKVGGLTGSSSDDSGSGSDASDNEESDYESSKNMSSGDDDDFNPFRDESSEDDEDDPWLIRKDHKKNKDKKKRKSIDPDSIQSALLASGLGSKRPSFSSTPVISPTPNSAPANSNINSNSSLITSQDAVERAQQMKKDLLDKLEKLAEDLPPNTLDELIDELGGPENVAEMTGRKGRVVSNDDGSISYESRSELDVPVEILNITEKQRFMDGDKRTHRSNQVTAPEYVFLISELAGEQRFASIVAKRLESLGALTHGDRRATESRDLSRFNFDNKYGRNALEIVMKSIVNLDSPMVSPPPDYPGEFFKDVRQGLIGVGLINVEDRSGILTLDKDYNNIGKFLNRILGMEVHQQNALFQYFADTLTAVVQNAKKNGRYDMGILDLGSGDEKVRKSDVKKFLTPGYSTSGHVELYTISVERGMSWEEATKIWAELTGPDDGFYLSLQIRNNKKTAILVKEVNPKKKLFLVYRPNTGKQLKLEIYADLKKKYKKVVSDDALVHWLDQYNSSADTCTHAYWRGNCKKASLGLVCEIGLRCRTYYVLCGSVLSVWTKVEGVLASVSGTNVKMQIVRLRTEDGQRIVGLIIPANCVSPLVNLLSTSDQSQQLAVQQKQLWQQRHPQSIANLSNA
The following text describes a protein:
Function:
Putative 5'->3' double-stranded DNA exonuclease which may also contain a cryptic 3'->5' double-stranded DNA exonuclease activity. May be involved in DNA mismatch repair (MMR).
Subcellular Localization:
Nucleus.
Sequence:
MGIQGLLPQLKSIMAPIRVEDLRGQTVAVDTYSWLHKGALSCGDRLCKGIPTTRHIEYCMHRVNLLRHHGVKPILVFDGGFLPMKSEQEVKRARSRKENLERAREHEAAGNSRAAFDCYQKAVDITPKIALELIQVLKQEKVDYIVAPYEADAQMTFLSVNKLVDAVITEDSDLIPFGCSRIIFKMDKFGQGVEFQITRLERNRELDLNGFTKQMLLEMCILSGCDYLPSLPGMGVKRAHALIQKLKSHEKVIKHLRYSAVSVPPQYEENFKKAIWAFQFQRVYDPATEDIVHLSGIPHDLSEDDFLGPWLPQAVVKGIALGEIDPLTKEPFEASIPCSAPAADKGYMVKESIIPSNGKKRLELPVQKNILTNYFCLASLEAKRKFRAPKVTPKQKMLNESSLPSPQTEDSGTPDSIEDTSLPMNNIQFSQYSSEHFSSEPPRDDSIDASQCSTGRAFPWGDSDSVSPHCSSHDIGNGPLSRDQHIEDAEVEVSYCNTSAMPISPCLERTSPGIADLSLVSHNTEPSRPVLHYAESYVAPTVRSSYFKKDKRVFTNQVEDQLDDDDDDNAETGTSTLSGVQPGNPGGVVKRRKLWDPQNFEDETLPPTSSHDSPAVDEGCGTDSLDDIDTNSEGRFGCNVSHVNNYSGIAKKSMDKFAALISSFRYAGSRASGLRAPLKDVKNTLSVRSILRPPEQNLRCTAKKTARGHRSQSRSRSDASNSADGPPDLSAFTHSPVFLPDLGKVTDKDAPARSTTGGCPDQSKNTRKAVGTAVSPDLSTFAYTPTTTASRPERSKFSTAIRTADSPDLSTFAYRPTTTASRSERSKLSPTAIRTADSPPDLITFAYKPMKPLDGSRVAGTTLAASGRNSRGKFT
The following text describes a protein:
Function:
Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane.
Subcellular Localization:
Cell outer membrane.
Sequence:
MSCFSRTFLAASISAALFAPQIQAEASVDDNRAQLPNGEQCLVNQPEPTNPGQQPINVEADKLEAINGQKATYSGNVVVVQGKKRIAADNVTLHQQENVVVAEGNVQFSDGEIKTHSTKATNHLNTDEMTLENTRYQFLCEPGRGEAVYVSKTGKAVYEIEDGSITSCPDGDNAWRMRASSIDVDQNEEIATFYNPRLEVQNVPVFYLPYLTVPIGDTRKTGFLYPTASYGSRNGYSFEVPIYWNLAPQYDLETTFNYMQKRGTQLNSVFRYLTDFGAGQIKSEYLADDQLHTELGDRWAFQYEHNGIFQQAWKFEIDYSKVSDINYFSDLDSGVGNREDGQLIQEGRATYRSDNWDSALLVRDFQLLTKDTTSTNLPYRLMPQLSYNYYAPETMKYLDLDLVSHVSRFETDARGKPSATRVHIEPGLKIPFSNTWGNWTTEARVLGTYYQQDLDKTTDAKLEESVTRVIPEIRSVAGIVLERDTVLLDDYTQTLEPKIQYLYVPEKYQDNIGLYDSTLLQTDYYGLFRSRKYSGVDRIESANQVSYGASTRFFDSNYKERLNIAFGQIFYLDSKLNPSNKNPDSTSDKTSYSAWAVEMDFNFADYLFYHGGIQYDIDSQAVQLGNSTLEYRVASGYIQANYRYVAKDYIRNTVGDSITNIDDITRDGISQAGILAGYQLSRKWSASGQYYYDLTTDEALEWLANLTYTSDCWYVGFTYSNQLKSWNGNFVTDPYATPIYENNFSFNIGIIGFGTSIGAGSSMTGVDSAGNSLGYGRPFFLNN
The following text describes a protein:
Function:
Carotene cis-trans-isomerase that converts 7,9,9'-tri-cis-neurosporene to 9'-cis-neurosporene and 7,9,9',7'-tetra-cis-lycopene (also known as prolycopene) into all-trans-lycopene. Isomerization requires redox-active components, suggesting that isomerization is achieved by a reversible redox reaction acting at specific double bonds. Isomerizes adjacent cis-double bonds at C7 and C9 pairwise into the trans-configuration, but is incapable of isomerizing single cis-double bonds at C9 and C9'. Carotenoid biosynthesis is partly required to form the prolamellar bodies of etioplasts.
Subcellular Localization:
Plastid, chloroplast membrane; Peripheral membrane protein.
Sequence:
MDLCFQNPVKCGDRLFSALNTSTYYKLGTSNLGFNGPVLENRKKKKKLPRMVTVKSVSSSVVASTVQGTKRDGGESLYDAIVIGSGIGGLVAATQLAVKEARVLVLEKYLIPGGSSGFYERDGYTFDVGSSVMFGFSDKGNLNLITQALKAVGRKMEVIPDPTTVHFHLPNNLSVRIHREYDDFIAELTSKFPHEKEGILGFYGDCWKIFNSLNSLELKSLEEPIYLFGQFFQKPLECLTLAYYLPQNAGAIARKYIKDPQLLSFIDAECFIVSTVNALQTPMINASMVLCDRHYGGINYPVGGVGGIAKSLAEGLVDQGSEIQYKANVKSIILDHGKAVGVRLADGREFFAKTIISNATRWDTFGKLLKGEKLPKEEENFQKVYVKAPSFLSIHMGVKAEVLPPDTDCHHFVLEDDWKNLEEPYGSIFLSIPTILDSSLAPDGRHILHIFTTSSIEDWEGLPPKEYEAKKEDVAARIIQRLEKKLFPGLSSSITFKEVGTPRTHRRFLARDKGTYGPMPRGTPKGLLGMPFNTTAIDGLYCVGDSCFPGQGVIAVAFSGVMCAHRVAADIGLEKKSRVLDVGLLGLLGWLRTLA
The following text describes a protein:
Function:
May be an inorganic phosphate cotransporter.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MGFEPSEDKARPGGLGVRHWQAVLLFVGMMINYFQRVNISAAIVPMTQSTAGAPFYTWDTSDKSLILSSFFWGYVVSQVPAGLLAKRFGAKLVLGLATAIGGILCFFHPIAAKSGWQSICVLRVLTGLVQGTVYPCVHTLLAKWVPRTERGLLTTGVYSGAQFGTAVILVTSGFIFESSMGWPGLFYLSGGLSLAWALLFFWQAANEPVTASRISKGEVEYIESLTGSNSSSQSMPVPWMSIFRSPAFYGLLAAHCGFTWGFYTLLTEMPTYMSMVLQLNVKSNAFLSSLPYFAMGLLCFVVSPISDLLINRGTISITTARKLFNSIGQWGPMACLIGLGYMTADEKTWAILLLTLAVGINAGCSCGYLINHIDLSPNFAGPMMGVTNGIAGVTSIIAPLVVGAIVSDEEDPSQWRMVFFITGGIYLVCNTIFVIFGKATIQIWNEPPSTSSTMTLRSHQENDSKSIVPTSDKDIRY
The following text describes a protein:
Function:
Trifunctional enzyme involved in UDP-beta-L-rhamnose biosynthesis, a precursor of the primary cell wall components rhamnogalacturonan I (RG-I) and rhamnogalacturonan II (RG-II). Catalyzes the dehydration of UDP-glucose to form UDP-4-dehydro-6-deoxy-D-glucose followed by the epimerization of the C3' and C5' positions of UDP-4-dehydro-6-deoxy-D-glucose to form UDP-4-keto-beta-L-rhamnose and the reduction of UDP-4-keto-beta-L-rhamnose to yield UDP-beta-L-rhamnose. Required for the normal seed coat epidermal development.
Miscellaneous:
MISCELLANEOUS: In bacteria, TDP-L-rhamnose is formed by the successive action of three different enzymes on TDP-D-glucose. In plants, on the other hand, a single polypeptide probably catalyzes all three reactions that lead to the conversion of UDP-D-glucose to UDP-L-rhamnose; MISCELLANEOUS: RHM2 appears to be more highly expressed in cv. Landsberg erecta than in cv. Col-2. Transcriptions factors AP2, TTG1, and GL2 are required for maximum levels of RHM2 expression at the time of mucilage production.
Domain:
The dehydratase activity is contained in the N-terminal region while the epimerase and reductase activities are in the C-terminal region.
Sequence:
MDDTTYKPKNILITGAAGFIASHVANRLIRNYPDYKIVVLDKLDYCSDLKNLDPSFSSPNFKFVKGDIASDDLVNYLLITENIDTIMHFAAQTHVDNSFGNSFEFTKNNIYGTHVLLEACKVTGQIRRFIHVSTDEVYGETDEDAAVGNHEASQLLPTNPYSATKAGAEMLVMAYGRSYGLPVITTRGNNVYGPNQFPEKMIPKFILLAMSGKPLPIHGDGSNVRSYLYCEDVAEAFEVVLHKGEIGHVYNVGTKRERRVIDVARDICKLFGKDPESSIQFVENRPFNDQRYFLDDQKLKKLGWQERTNWEDGLKKTMDWYTQNPEWWGDVSGALLPHPRMLMMPGGRLSDGSSEKKDVSSNTVQTFTVVTPKNGDSGDKASLKFLIYGKTGWLGGLLGKLCEKQGITYEYGKGRLEDRASLVADIRSIKPTHVFNAAGLTGRPNVDWCESHKPETIRVNVAGTLTLADVCRENDLLMMNFATGCIFEYDATHPEGSGIGFKEEDKPNFFGSFYSKTKAMVEELLREFDNVCTLRVRMPISSDLNNPRNFITKISRYNKVVDIPNSMTVLDELLPISIEMAKRNLRGIWNFTNPGVVSHNEILEMYKNYIEPGFKWSNFTVEEQAKVIVAARSNNEMDGSKLSKEFPEMLSIKESLLKYVFEPNKRT
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
Sequence:
MAEVDPETLLEWLQMGQGEERDMQLIALEQLCMLLLMSDNVDRCFESCPPRTFLPALCRIFLDEHAPDNVLEVTARAITYYLDVSAECTRRIVAVDGAVKALCNRLVVVELSCRTSKDLAEQCIKVLELMCTRESGAVFEAGGLHCVLSFIRDNGSMIHKDTLHSAMAVVSRLCGKMEPSDTSLETCVESLSTLLKHEDPHVADGALRCFASLADRFTRRGVDPAPLARHGLTNELLERLANCGQPASFTTTTTPSSTPRPAAGATPDSKSNPNISTVISLLSTLCRGSPTVTHDLLRSDLPASIEKALMGDERCVLDTMRLVDLLLVLLFEGRKALPKSSIAPRLRSSTTGLRRLDSAGERTHRHLIDCIRSKDTDALIDAIDTGVEVNYMDDVGQTLLNWASAFGTQEMVEFLCERGADVNRGQRSSSLHYAACFGRPQVAKTLLRHGANPDLRDEDGKTPLDKARERNDEGHREVMQILQSPGEWMVPVSSATESTITSPEEIKPEDGDREPKGDPEMAPVYLRKMLPIFAQVYNNTMMPSVRKATLALIRKMIHYAPSRLLCEICSGDLLGFTPVLVEVLAAVLDHEDDDEGHLTALQIIQDLMYKGQDLFLDHFARLGVFSKVSSLVGPLDEDREEEGATAQVKREIPDDQHHQLQQQQHHQHMQQQQQQHQQPQLQQQPQTQRMDDSKEVVAGRPYSWKDWCLARGRDCLYIWSDAAALELSNGSNGWFRFILDGKLATMYSSGSPEGGSDSSESRSEFLEKLQRARSQVMPAIQTQPILSIPGPTKLVVGNWTLQCKKEGELVIHNSDGQQQQATVLREDLAGFIFESNRGTKHSFIAETSLGPEFSTGWTGKRGRRFRSKLEQVQQKVKTLARELYEGYFKVAESHPRDVVAKLNSIVMQLEAACDLYNDPIKGIDDEQGWMEEMKGALETLTCLLREENNISAYELHSSGLVQALLYCLSDGYDHVALHDRYIKERVALFKSSFRDNNDEDGGVSPSVMLVRKLVAVLESIERLPLFIYDSAGSSYGLQVLTRRLRFRLERATGETALIDRTGRTLKMEPLTTVASLERYLLKMVAKQWYDYERTSFTFVHRLKEAQSITFRHTHDFDDNGIVYWVGTNAKTAYEWVNPGQYGLIVVSSSDGRGLPYGRLEDILSRDSSALNCHTNDDKRAWYSIDLGLWVIPSAYTLRHARGYGRSALRNWQFQMSKDGISWMTLLTHTDDCSLNEPGSSATWPLEPSTSEKKGWRYIRLQQMGKNASGQTHYLSLSGFELYGTVTGVVEENLSVAPAKVVKDPESSMRKQRKLVRSQVLRQMVMGQRGRSTDWRWREFEGAHQAEGLASSERESLVAAVLKAAAQNEPLPSREPPPLPRMKTVTIPGTRSPSVTSSIPGSTPGATGPILGRNKSNSTPSLSAGEGPDAGSACKDKDHASTSDLSAPSLASAAVVMENQLMRSGLEAVLAETEAVVDGAVSAVLSGGRNKRLATDSEKALSEAIELPPPTAGTGSTPVLPPTTSSMSVSVPNLSSNQDVVSSLADTFPSLMRQSRGSVGSGNSTLSNRTNTFTSSFVRFPYSSSGLPSNNYLSSAQSAPNLPGATTTSMPTSASTVLTSTLSSALATSLTSTSSESDNEFLEPCPTSSLMAELEDEEFPEPEDLDDENEDDSDGEDYDDGTEEEDYDSRGVRRKTWDDEHVLKRQFSALVPAFDPRPGRTNVQQTTDLEIPPPGTPDTSFRDETDSTPTPRLGLFLRGPGLQGVQETEVYCEDLRSTIFRYVQMLYQQTPTGTKHDRLRRIWEPTYTVVYRESRPQDESTSSVENTEGPWTVGFVQRHLGTERLPKTELIMYLQEKADAQFLRRWKLTSNATNIRRTRNSSRLIAAYREFIQLGLARPSSQQRLSQDSGHVLSESDGGSLNAGGKETGACSVDDVLQLLRILYAIATDVGSTDPDGHRFNVPPEEFYSKKITNKLAQQVQDPLVLASLSLPKWCERLTNRCPMLFPFETRQLYFTCTAFGVSRAIAWLQGKREANTERVRTPSTRRDDHHEFQVGRLKHERVKVPRGEQLVEWAINVMRLHCAKKSILEVEFLGEEGTGLGPTLEFYALIAAELQRKSLGMWLTDDEIADDLSRKVDLGEGEKPPGYYIQKASGLFPAPIIQDSEEISRIEQLYNFLGTFLAKCLQDNRMVDIPLSRPFLKLMCMGETGSTHLYYTSTHESYTSPRDSEVFFAEMQQTEASLESMSELISDLAIDSGNESKELILAADPPKPCTPAWFAGVLTWSDFELIDPHRARFLQHLQEMVDRKRQIQLDGSKTEEERNNEIQNLCLETSPGSGVPVKLEDLGLTFQFNPSSKVYGYHSFNLKPNGDDECVSLDNAEEYIELVTDFCLHTGIRRQMEAFRDGFNQVFPIEKLHSFSPAEFQTILSGDQAPSWTRDDILNYTEPKLGYTRESPGFQRFVNVLSAMNGDERKSFLQFTTGCSSLPPGGLANLHPRLTIVRKVDANDHTYPSVNTCVHYLKLPEYSNEDTMRERLLSATKEKGFHLN
The following text describes a protein:
Function:
Major constituent of messenger ribonucleoprotein particles (mRNPs). Involved in the regulation of the stability and/or translation of germ cell mRNAs. Binds to Y-box consensus promoter element. Binds to full-length mRNA with high affinity in a sequence-independent manner. Binds to short RNA sequences containing the consensus site 5'-UCCAUCA-3' with low affinity and limited sequence specificity. Its binding with maternal mRNAs is necessary for its cytoplasmic retention. May mark specific mRNAs (those transcribed from Y-box promoters) in the nucleus for cytoplasmic storage, thereby linking transcription and mRNA storage/translational delay (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSEVEAAAGATAVPAATVPATAAGVVAVVVPVPAGEPQKGGGAGGGGGAASGPAAGTPSAPGSRTPGNPATAVSGTPAPPARSQADKPVLAIQVLGTVKWFNVRNGYGFINRNDTKEDVFVHQTAIKRNNPRKFLRSVGDGETVEFDVVEGEKGAEATNVTGPGGVPVKGSRYAPNRRKSRRFIPRPPSVAPPPMVAEIPSAGTGPGSKGERAEDSGQRPRRWCPPPFFYRRRFVRGPRPPNQQQPIEGTDRVEPKETAPLEGHQQQGDERVPPPRFRPRYRRPFRPRPRQQPTTEGGDGETKPSQGPADGSRPEPQRPRNRPYFQRRRQQAPGPQQAPGPRQPAAPETSAPVNSGDPTTTILE
The following text describes a protein:
Function:
Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates.
Subcellular Localization:
Cell inner membrane; Single-pass type II membrane protein.
Sequence:
MRLGRRTSKQEEAQIDLTSMLDIVFIMLIFFIVTSSFVRESGVEVNRPTAAHAVSQKQAGIFVAITAANDIYIDKRQVDVERVQATLEHLLLDQPDASLVIQADEHAFNGTVVKVMDAAKGAGVKSIALAAEKP
The following text describes a protein:
Function:
Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis.
Sequence:
MVDAGSKRALDDGEAPSQLQATTDEGVACFGCGKSDVKYRCPRCERITCSLQCCLEHKKQASAASFDCNGKRDRTKFVGIKKFTDADLSSDFFFLEEVSRSTNSAVRSRSQLNANARRYTSNKKRKVATDKRSPSAPINPDIPADWLARFPIAVQLFAEHSAKRGVALTLLAPGMSKRGRNSSYMDTKKNTLYWRVEWAFPSAEVPVNHFEERANEKDTLFALLGKFLTPNQENVAIRGKLKKYAVHDWEKHILLLLRKEFTPASQPQYHRLDGNQSLESNLKRKAVVEFPVITVALVADADEYPVAHDVIETVASMETHKDDQLAETEKPKDMEVEESDGGTSSELLEVEATDTTAKLFSISEEEPAAEGEAPVLPKCVMIQELDVTG
The following text describes a protein:
Function:
3'-5' RNA exonuclease that trims the 3' end of oligo(U) tracts of the pre-U6 small nuclear RNA (snRNA) molecule, leading to the formation of a U6 snRNA 3' end-terminated with a 2',3'-cyclic phosphate.d. Participates in the U6 snRNA 3' end processing that prevents U6 snRNA degradation.
Subcellular Localization:
Nucleus.
Sequence:
MSLVCYESSSSGEDDDETISDNPRMLKVPKLQESFHELYKKKPKTFDSPEFHEGRIRGQKHIEGLWFVQTYLEVDLSKKVKKGIREFLNSQSRFQSLLCSEHNVPRRLHLSISENYRINYSTKNQLVHKWEQYTNNLNYRTLKFRLGKMCLLFNDEKTRMFLAFECKFSDENYKDLISHASDCMKEFTNRNLREDFLLHISFASSLTNEDEYQNWVSQDRESHFFKTMNEIINTKIQKDQFSESFIVDSLKLSIGHLIFTFPFCK
The following text describes a protein:
Function:
Promotes the exchange of Ras-bound GDP by GTP.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MGNINSICLNNNGKYRIDSISCSLEGCKLNSKELVENMVALVDKYPLTQLLIIRECKLKQIPVNITNLSNLSELILSDNKLSQLPWSLPPPFKPNTLLSMASITNENLVRLDLSNNRFTEFPSSVFVLPNLKQLILCNNQLTNMNVTLCGGTSNNNGAHQPHIACQLEELKLSNNNFTIFPSIIGDQLTTLKSLDLSGNTITSLPNSFSNLVSLTSLNLKSNKFTCFPPSLCTLDKLVHLNLSCNQILVSPSDHTLGVSLLPSLEKLELQHNRFAHFPMDILEIVSLRVLKLQDNDIDKIPDKIGNLLNLNELFLSENKITQLPSTIGELINLRKLYLEYNKIGSLPQEFSKLSKLNILILHNNDLKFVPDQLHSLSQLLRLSLDENQLSSSDQKLIKSEGSLALIKRKNKLNYGSTMNGTGTTSSSGSASTSTHGSINKTTDILLSSVTLNNSILNQINNNNNNNNNNNNNNNNNNNSSNNNSGTNSLSSTPNGTGKSKKKLTHLTISRSLFRGNSSNLESEKEDFINKKQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQLGSTASPSTASPITSHITVNSTVLDFEDDIQKMQLGLEALSNLETSIGSNNSGGGDSMNGSGGNINNSGGSGSGCGTISGSTTKQRRGSVFLPPTNAFKLSPNVVSSSYNTLPASVMSGLLQQQNLENGGVGSGSGSGSPIISANSICNSNSSSSNSLLKPPIINTTNLSTSPNLLSQSSTSFLNLPPLNQSSTNSFLPPQHQHHHHHSNLSQSLSINNLAHRLPTSLSSSSLSSNNTYDSLQFQQQQQHHHHNHNNHQNSNQPLATIVPSFSKFKNSFDQLLEEQDFSKKKRETLQKLSKEQKWNLLLQYRNSTLNMLNMKEHSNNSNNNQSIKNSTIIASTTTTTTTNGESLDGSSIQQQITKNSNFQSSRFYIDNLTSKTDISLVKEVHDFLKESGPEVSIFIGMGGIESLLGILQFNLDNAQLQFDEEKVGYCLLCLKILVECTAKSVITTNNSLNLVTMFLTSASKYIIDIIIDIYDELLRLQVIGVSVVLDSLINFQKVKGLSSPYVPLVALLRNPIIEMPTKTTVFKIINFLIYSFSVLEERFSVICSLLKVGILEVIGMFRALPHTSYSLRFELDLFEEVLDSDESELVKKIGRKEVLKRMSNEDNDLSKQSSKQSMDFVRVVMVSAGYGDLKIDLDERTSYANVIDFIQSNYQIKYSIDRYGLFVPAIGSLVLDGSILQSSGSQSRWVDPSKSLIDNGLSNEIVEFKMKPMQIQVLQSVVVVVATNHQKEDIIKEFTIDPQLKCFEIVQYLRTRLDSSSPAFQRKISVLTEDEDEDYESDIYGVYCFSSLESYDQGSWYPLNSRFLDFNPTNTPTIIDVKLMERPLRVLFSGTEKLMKFNPYVPVSELIKEIKNEIHLKINIEDYGISYVPNVSSSNLSSLIIEETWLDPTKTLLDHNDMKCSVVQFKFKPRTVSVMVLVESGIEIPTTDTPYQFVNTNSISEIIEKICTPHQLNPLSHSLYISDCQGQKIKLLSRQNCLRDQQVNNGDHLIITSKQKDLPSDFNVWDEPNDSSETITYSKDRRVSSVTLNKLIEKLTSPEYTQDSEMKTIFLSSYRSIITPSVLLSKLMERHTIPTLVDKERGKLIQRKTRLLIKSWLELETTKNREEVITLLVQNMPAQSIEDDGLKELTELFVDLSTKSYSSILPIVIGELPKCKIPKIIDSYVTFADMDEIEIARQLSLLTFPLYSRIETSELLNQRWSKPGGGPNIMSVVGLFNKISNWVSFTIVNQPKLRDRAVVYGKMVKIANAFYELRNYHLLMAIISGLNASPVLRLKYTKGKLSKNLKDNLDTLEELMSTQSSMKNYRADLAAASPPAIPFMGFHLSDLVFIDEGNQQLCDSRINFKKLEMYKKTIATLQNFSLFPYQFTPVPIIQNYFLDYKIVADKPIYEMSLSAEPRNAERYDIQ
The following text describes a protein:
Function:
Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Sequence:
MDYPQQHIKPYNEDGKKTEQVERMFDNIAHAYDKLNHTLSLGIDRSWRRKAIAWLRPFRPQHIMDVATGTGDFAILACRELNPDELIGTDISEGMMNVGREKVKKEGLSDKISFAREDCTSLSFADNRFDAITVAFGIRNFEDLDKGLSEMCRVLKPGGHLVILELTTPDRFPMKQLFAIYSKVVIPLLGKLLSKDNSAYHYLPDTIKVFPQGEVMKGVISKTGFGEVHFRRLTFGICTLYTATK
The following text describes a protein:
Function:
Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Sequence:
MAQEISNLVKKYNVTWQQTMLRIYDPKETVEFYEKNFGMINIHTYHFNEYNFSLYFLITPPYDEEERKKLPEPNTKESEKYLWNLNTVCLELTYNHNSQEKLSNGNNENDRGFGHIAFNCNDVIEQCDNLFKKNVKFHKLPHETKMKTIGFALDPNNYWIEIVKRSNQVKWKNYKNITNFSQTMIRVKNPEKSLYFYIHILGMKLIHVKHCSDFSLYFLKSNYACAENNKEMIEDQSNKNTNEIYDFNSLKNSYQTDEDYENFKQSWEPVLELTHNHGTEDDDNFSYHNGNTEPRGFGHIGFLVNDLENYCKELETLNVTFKKKVTEGLMKNIAFIYDPDNYVIELIQRDTSFIAK
The following text describes a protein:
Function:
Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MPILITALIYLIFFLSGATALVYEVVWVRKLSLVFGGSHLAVTTVLAVVMGGLALGSWLFGRRVRTTRNLLRLYGALEIGIAFFALLFIALLNLYSLMPAYSFESLTEHSHQLPRVALLTLRIVLAAIALIVPTTLLGGTLPVLAAFMVRGRRAVGRGVAYLYALNTFGAVAGCFGAGFYLLGRFGVSNTMAGAITVNVLLGIACFALQGPAARYLEAGEDEAPAPLSAVTLPEEKARIGLVVWGIGVSGFCALGYEVLWTRVLGIVIGTNVYGFTLMLAAFLTGIAAGSGAYGLWARRLRPPEEGGCPVSKLIGGFGVVQIVIGLSALLVTILIRDLPTRVFFLQDLFLSQSTDLFRARQFANFALVFSYLFIPAFFMGVAFPLAGTLDACRRRKVGHAVGEVLTCNTIGAILGTVVSGFVLIQVFGIERSLYLLATVNAGFGLLILARLLRGTPRRLATAGTVLAVVGVMAVAGTMPRIWDAKYFAIYRTNQPEVFRTPDLIAEAKRHTDVLYYAEGIQSIVSSIRIRGGYQAFLRNGRIEASDHNESLQNQYALGHLPMLLHRNPRKVLVIGAGSGITLGAVSLHPSVSEMTLAEVEPKVLGVTRSFAAYNHGVLGDRRLRVAFSDGRNYLATTGERYDVITADPIHPWLSGAGYNYTREYFELAAEHLRAGGIMCQWLPLYDLSADDLRSVVRTFRQAYRHVLVWMTQGDAMLIGSNAPILLSEDELAARIAVPAVAADLARVQMGSATDLLSYFVMGTAGADRFSRTGRINTDDNLYLEFSVPRSTGKSALPEVNVNALARHRESVLAYLDDSVPPADRLARENRWMRLDRAAALALEARAIFLGGRYDSPRFGLLVSELEGNYAAFAPWRFLRSEYLEEMASSPLPLDQLALALLDESGRRVVVNVAAVMSRVSRELTVVDFVDSDERVIIGQADINGRGRDGSAKRLAAEVMEAVRLAYNEELSGAEARGKPLPDQAEFVRRMREIIATMTGRQHGNPYPAQGRPIKESA
The following text describes a protein:
Function:
Likely involved in U12-type 5' splice site recognition.
Subcellular Localization:
Nucleus.
Domain:
The CHHC region interacts with the 5' splice site of the U12-type intron.
Sequence:
MEGEPPPVEERRRLQEELNEFVESGCRTLEEVTASLGWDLDSLDPGEEEAAEDEVVICPYDSNHHMPKSSLAKHMASCRLRKMGYTKEEEDEMYNPEFFYENVKIPSITLNKDSQFQIIKQARTAVGKDSDCYNQRIYSSLPVEVPLNHKRFVCDLTQADRLALYDFVVEETKKKRSDSQIIENDSDLFVDLAAKINQDNSRKSPKSYLEILAEVRDYKRRRQSYRAKNVHITKKSYTEVIRDVINVHMEELSNHWQEEQEKAEDDAEKNEERRSASVDSRQSGGSYLDAECSRHRRDRSRSPHKRKRNKDKDKNCESRRRKERDGERHHSHKRRKQKI
The following text describes a protein:
Function:
Has antimicrobial activity in synergy with other peptides. Strongest activity observed against E.cloacae.
Miscellaneous:
MISCELLANEOUS: Not induced by bacterial challenge in imd mutant flies. Level of induction reduced by over 90% in 18w mutant flies. Toll loss-of-function mutation has no effect on induction by a mixture of E.coli and M.luteus; but strongly reduces induction by E.cloacae.
Subcellular Localization:
Secreted.
Sequence:
MSKIVLLIVVIVGVLGSLAVALPQRPYTQPLIYYPPPPTPPRIYRARRQVLGGSLTSNPSGGADARLDLSKAVGTPDHHVIGQVFAAGNTQTKPVSTPVTSGATLGYNNHGHGLELTKTHTPGVRDSFQQTATANLFNNGVHNLDAKAFASQNQLANGFKFDRNGAALDYSHIKGHGATLTHANIPGLGKQLELGGRANLWQSQDRNTRLDLGSTASKWTSGPFKGQTDLGANLGLSHYFG