lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Putative phospholipase.
Sequence:
MAAMAHVASFLLLWSLLVCIAAEPLRLSVSISRTESGEIKVSEVPNGGEDHACASGVYQREYTNLGWNFLQITTGASCPDPDQAYAAGFVEGALTWEMTWDHWQNTKDALSASDELPAFLAANDKYVSGEIAAEHLNSSEAFWWQVSLVLEQLKGLAAGYNSYASTSKKLTLDDFLRMNSDGDFYDLIPALKLKKKDSVGGHLARKFGALRQTVERTLGINTGRTEPNVNFDDEDLTLRGQQKCSALVKVMPDFSEIFVAQAAFSGLEELLRIYKLYDFAFHTTAKSADVIPGRRSAFSSYPAHVISGDDFYLISSGIVAVETTIGTFNDDLYRNGITPEGSVFEWLRNMVANRLATSAEQWTSIFSQHNSGTYNNQWLIVDFNLFEPGEPLKDGTLYVLEQYPGYIAAYDATEELRTANYFASYNTPHNKTAYELAGYPAMVTKFGDFYTVENSPRAHLFAREHVKVTDIDSFKHTVRYNDFKNDPLGRCANCTPPYNGEFGISSRGDLNVANGSYPFKAVSHRDHASLDAKVTSGALFKSFSSIVVAGPTCDQQPPFDWSTSDFNYLPHQGHVTEYAFPWVKVDWEGLRGATLTINSTACSAY
The following text describes a protein:
Function:
Component of the ESCRT-I complex (endosomal sorting complex required for transport I), a regulator of vesicular trafficking process.
Subcellular Localization:
Late endosome membrane; Peripheral membrane protein.
Sequence:
MSTSSYAELNPYEEARLYSNNHDRERYENMATLFSLIVALDYLERAYVRESISEKEYAPTCTRLLAQCKTMLKLIVDQEKHSSKPITDLADFMRIYKMNYLAAVHRLTVGVPATVEHASSSSLQSSSDRAKWVAETTQNFITFMDALKLKLRAKDQLHPMLSELMRGYSRSDEVGKDQDASDTRAKLLKWLITLNHMKASDEIDEDQARQMLFDVEGAYNSFFRALQD
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Essential for tRNA synthesis. The RPC53/RPC4-RPC37/RPC5 subcomplex is required for terminator recognition and reinitiation.
Miscellaneous:
MISCELLANEOUS: Present with 998 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MSSNKGNGRLPSLKDSSSNGGGSAKPSLKFKPKAVARKSKEEREAAASKVKLEEESKRGNDKKHFNNKNKRVTGAGGQQRRMAKYLNNTHVISSGPLAAGNFVSEKGDLRRGFIKSEGSGSSLVQKGLETIDNGAESSENEAEDDDNEGVASKSKKKFNMGKEFEARNLIEDEDDGESEKSSDVDMDDEEWRSKRIEQLFPVRPVRVRHEDVETVKREIQEALSEKPTREPTPSVKTEPVGTGLQSYLEERERQVNEKLADLGLEKEFQSVDGKEAAAELELLNADHQHILRKLKKMNNKPERFMVFQLPTRLPAFERPAVKEEKEDMETQASDPSKKKKNIKKKDTKDALSTRELAGKVGSIRVHKSGKLSVKIGNVVMDIGKGAETTFLQDVIALSIADDASSAELLGRVDGKIVVTPQI
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:
MEHNIDTMESSSSCSICQECGKHPFKYRCPGCNVRSCSLPCVNSHKKRLGCNGKRSRTQFVPLSKFDDNILLSDYNLLEETKRIADSTRRMRDDFKSFGYKLPRNLLALCRSAKKRATKVLILSRGMSKREKNRSYYSWSKQSIYWTVEWRFDSTEVVFTDHGIEENRELQGVIEKHLKPGPWNLQVDGKLKPFRKEQLDKLKFLVLKNPKGPKPLFRELDITSPLRHQLIGIMLIEFPVIHVVLPQHAHEFAIDETWVSVPRSRNCPPDEPLHDLPSPKGVYFREEEIQEDDELAQKPQVLDSSNHVSSVEDILNIVGGSIKEVAGEREGYPSSEQEVVREGGDFSLEKQGLRKDVSPVLKSEEMEDYFPSDLEAFEVNNSMDFGFDQVFEDGVSRISPGELYGDDHSFFKGVYFEDDDDREEGEIVEF
The following text describes a protein:
Function:
Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. 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. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
Sequence:
MGEKVVIVESPAKARTIQKYLGKGYKVASSMGHVRDLPKSGLAIDIEHDFAPSYEIVKPKVVSELSQALRNAEAVYLATDPDREGEAIAWHITQAVKLPKKTPVYRVVFQEITRNAVQQALQQPRQINQNLVEAQQARRVLDRLVGYQLSPLLWDKVKRGLSAGRVQSVAVRLIVEREREIEQFQPQEYWTIEADLLKDAGVAPRDLFRAVLIERDGKKLEKFSIENREQAEAIVADLQGAAYTVVRVTRRDKRRSPAPPFTTSTLQQEAARKLGFSAKKTMTLAQRLYEGVDIGGEDGMVGLITYMRTDSVQVAAEAQTEARDVIGKRFGKEYLPDQPPVYKTKAKGAQEAHEAIRPTSSARLPEQLSGKLENDLWRLYDLIWKRFIASQMAPAVFDSTTVDIAATPVVAGAPAYLFRATGSVLKFPGFLAVYNVSLDEGEEDEDSERRLPPLAEGEALQLVELLPIQHFTEPPPRYTEASLVKELERLGIGRPSTYASILSTIQEREYVEMVDKKLIPTTLGRVVTDLLVEHFGNIVDYDFTSALEQQLDDIAEGSKKWVPVLREFYGPFRSTLEQAQRQMRNVKREEIVTDLDCPKCGQGKLVIRFGRNGEFLACSRYNREGDGESCDFTSDFHRDEQGQIVIDKASAPETSDVLCNVCGRPMVIKKSRFGPFLGCSGYPECNNTRRIGRDGKPVPLPEPTGVQCPKCGEGELLRRRGKFGRPFYGCSRYPKCDYITNTLDEAQAGEAPAEPAKNEPALPSPSRSSKRTRKSA
The following text describes a protein:
Function:
Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MKLSLPLQGYFDLLKHSPGEKKFVCINCGRPVSGLYRQISSTVLKIIDCDKCKKPADKYIEFEVLIILIDLILLSKPAYRHILYNSDCKNLWKIGCILILLEAYCFWTDAFRGITSITYRSHLTDPFLSEKGFYLSTVHFVAGFLLLYGFIYLFTRVLHRSVPKVTGNGKTYPHMLLHGVILASIGKFLFIPIIIWRENSTETGMAIHIVLVLMYFVISLVQIHSVVSDCTRSRSGVIVILAFIVKAYFLTRVSGLLQQFV
The following text describes a protein:
Function:
Rhomboid-type serine protease that catalyzes intramembrane proteolysis. May be involved in TIC22 processing during its import.
Subcellular Localization:
Plastid, chloroplast inner membrane; Multi-pass membrane protein.
Sequence:
MSQLLHLHRLSLPQSSLRFRFPPLHRRRAASSPTNSTQPPLQFRPLTVSRSQITCRFSQSDITPQFELDKAKDNRKPQKRANGIFWIILINLGIYLADHFFQVRGIKSLYLYHNFPAWYQFVTATFCHANWNHLSSNLFFLYIFGKLVEEEEGNFGLWLSYLFTGVGANLVSWLVLPRNAVSVGASGAVFGLFAISVLVKMSWDWRKILEVLILGQFVIERVMEAAQASAGLSGTIYGGYSLQTVNHIAHLSGALVGVVLVWLLSKFPSASMDQDVKKSS
The following text describes a protein:
Function:
May recruit a lipid transfer protein to the forespore membrane during sporulation, thereby aiding forespore membrane formation (By similarity). Required for meiosis.
Subcellular Localization:
Cytoplasm. Nucleus. Prospore membrane; Peripheral membrane protein.
Sequence:
MNEEDTDFAWLHNNSAEHLRFLSHRIFIGPIPSNFIHSTSGFFNKRFQNYTKRQICYNVASPNEPPIDFSFLMHKSTDENPDTPSNLDSPSTQNVGSTNNTRASQSLLRRSSSFFRRRHRKNGTHASTDNNPFSESSTLQPQTAERTSQQAVRSAITETTNPSVSVQNSNSTSTSSAAMIIPHRDSQNSLEIAPLISPESQLSSLHPSSSRRHLISTPHVNRGTQFKRSSSCRNSRQPLLSGVDKHLTSNFTDANLIIKQSVVLARIESTFTVLPSDYNDSAAQRVPRKTISPWSQCLLVARQTDVENSIRLDFISKKLRKRLNGDVVHNLDVPHDKSYKSNYLFSVVLSPHQASWNIYNSFDNSMVLWCPYGKNKTLICLLNFQSSLLSFEWISIISRALLFSPRPSLLISVPAFHIHLRLNFPCFKDTTRPHTNETFVTTDDITQLSRTSTLSLSTASPRLVHDLVMKSWDISEDQFVESCLGVLEVNPEWSGIVKTWSKSHTLGLCWRMYDRLEWINSFSSLKYVGLLAAKDLYQLELRPKLHYPNHVTFRDGSKMDEPTPVEGYLIRLTSSTGRKTRYGRMFHKELYFAIFNNFLFAIQPDSVLPLSMLSKSLNLDDKLPFLSNNENDKYVYEFDPFKIANCRASGLNETIDSSVRESFLLLLQAERKRELDMLTIADSFLDLSRVESVCPVEDVEERNIFEITMTNGMKLVFQSYCERTRNLWINKITEVASYWKQRLFLDLQEYHDVRETNINILHIEQSIEPDVACYLNHWEVAGCVASTLIYHYCSMLGCRVIRMQGTLFKKKDALFEKCFAILIPGQLVFFQDATRTKFGKLCTKTHYRKRYSISLKNAFIYTGLSTMDEFARGPNDPQPHISRLPRCYEDGWQSFDRDDMLSFVIWSSGGVDYDLRPHHSVPDTAYGMAKDKLSKPKRFMFLARTRQERDVWAKRISKEINRGHS
The following text describes a protein:
Function:
Plays a role in microtubule organization and/or maintenance for the formation of primary cilia (PC), a microtubule-based structure that protrudes from the surface of epithelial cells. Plays a critical role in G2/M checkpoint and nuclear divisions. A key player in the DNA damage-activated ATR/ATM signaling cascade since it is required for the proper phosphorylation of H2AX, RPA, CHEK2 and CHEK1. Plays a critical role in chromosome segregation, acting as a mediator required for the maintenance of genomic stability through modulation of MDC1, RPA and CHEK1.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Nucleus.
Sequence:
MAGMAGPAAALRIGDQLILEEDYDEAYIPSQREIQEFARVIGIDPEAEPELLWLAREGIVAPLPAEWKPCQDVTGDIYYFNFATGQSSWDHPCDEHYRQLVIQERERRVDPGGGGGGGGGGGGLRKKPGKQRKDKRKKKGEDILLLKREVQSESGLLPSASFYRTLSPASSSGRASPDLEPQGSLTARQDPFLRVPKGRSSAVLPEPSDPLRLLPAGASGKLQPLSLGKPSRTHQILADVEKILGRASSSSGKHDAGHPPRQDSTAEVRCAAAGAFSDSEPEDTESPRGTQRNRRALKEPPHGAQTDDRSLSPGSPLRGGLLLEVVTLGKDQGDGSALEGRSPVDALPGEKDEDLVPAVAAEVPLVPSVASLRPNRAPEEERGLHSLGNGLRLLDGRRKKGPQATELGKSGRATVEQGPALVAGPVLRVEAEAGARASPESFPSSKADSGGGSVGSSLADHLASQVLGEVDNFSWDLQSSHDTDHAAEPPAAAKRPFLEALHSQAHSSPEEHSESECYSEDQKFYRHVLHMVKRSRGAEPFSQCPGTAQEDSEEAVVSETGSPKGPPSAAEGKEPTPAEKGSRTALAPEGEPDSRKKGVCESVAQEEATEAAAALDLLVPDNRAEKEEESSSEGPRRGARLLRNLHVDLSTLDSGSDNEGEGWLPGEEAGHAKGGVEEEWKQESAEVPKRNAEPEVKPMTPWKEEGSAEDEVKKTSVGKGQALSLQQGKQTSIQNIPKEEEETQGFHQQKEEALRSLKCELEKARREEEQHLREKARQELEELRTQICSETEAEKERVREELESLRQSEEQALREKAHLSLERAKQEAEAAQEAQEAELEQDLQKAVSERKERLRQQKEAALQELEAQFAAETQQQRAAALEVQQKALAALRRQIAEAQQKAETELQEELESAEQQAQRKKHQVAEYERELSDLLREKRQEVEREHARRMEKAQEAHREALAEIQAQHLEEERRQREELQSQLQEERECLRASYEAEVETLRRKQAEQMRDLCRSQKEEEEKAALERELRLQEAQAKAAQLHAQEEAWKRRKQQLFEEEKQLEQQRKEAALALEESRKEQESLAESVRQLLREMAELQEQKAALGSQVERLRKEASELEEAVKSKQGLLSPGEGSSSKPSPKEKEEEEEELRLEDLQESSSVAASRKVEFKAPKDNEESSGLLDQVRHYISAEGSSLKTTKEFLVRQTHSVRKRQTALRAAKLHWSHDLQDPGRSEVLVGVRRSLEEEARQLEEVRSAVRKGQALLRKKEERLAQLESSLAEELSDEDTLKGGACKKVVTFDLSDSEDTSSMMSTNGSPHKRLGLKPDLRLPPLDKIQCLTDSLQRITSELNRVLGLLSTFSTQQPLPFTPGRSPSSPLSTEGVPLATYPSLPRTSAGPHWAWGICSAPVAPSAPAGQSVDNMLTEKWRKYFPGVFPLPCGGPGALSGKLSLVTPDNPVRLLPQPPFRGSEAEKQNIQGMIDANRKWLESVKQDSRVPILLSGPKSPHGPLPGVVQLGLDENNQIKVFHF
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in pre-mRNA splicing.
Subcellular Localization:
Nucleus.
Sequence:
MALQAPNLFVTEPIPSGHVRFKTSLGPIEIELWPRETPLACRNFVQLCLEGYYEGLIFHRIVPGFIVQTGDPTGSGSGGESIYDEGTFNDEINARLKFTRRGLVAMANLGSPNTNTSQFFVTLDRTEELQDKHTIFGSVIGDTIYNVMKLGEVEIDKNERPIHPPIIKSVEVIDNPFPDIVPRITSAQRKEQAKARKEAKKEKQKEKMLAKHKALGQVESNFGWLLVYVENKGLLSFAEEERLTETSDGSKNRKLKSAHDLEASSQLSQAVLDQRPSLNQLNLPENFKSTLPATIPENPLKVHEALRAVVGRERSGPSESGKTNTKESPVDDSSNKKGKGKHEKKSKESNTELSAADQVKADIIKMQAELKKMSKRHDSDSDSEEDKTKGKTEKTQKRKVTHDGHSLLEEERKKYKARAGDKKTAGRGAASEAESILDSFRRKLREAKPLTKPAEEAERVDGYAGEVDPTQDGVLGDVDGDDDGWMAHTLQFRKDATADLHKVDEYAVIDPLRERKLTLDELEARKNEKRFDNRPQPRNSDRRKKK
The following text describes a protein:
Function:
Catalyzes the dye-linked oxidation of primary alcohols to the corresponding aldehydes and the (subsequent) oxidation of the aldehydes to carboxylic acids. Active with primary alcohols, glycerol, 1,2-propanediol, 1,3-propanediol but not with methanol or sugar alcohols such as D-sorbitol.
Subcellular Localization:
Periplasm.
Sequence:
MRQTGLASLPLKSLAVAVLLSLAGTPALAADIPANVDGARIIAADKEPGNWMSTGRTYDEQRYSPLKQISDQNVGQLGLAWSYKLDLDRGVEATPIVVDGAMYTTGPFSVVYALDARDGRLIWKYDPQSDRHRAGEACCDAVNRGVAVWKGKVYVGVLDGRLEAIDAKTGQRAWSVDTRADHKRSYTITGAPRVVNGKVVIGNGGAEFGVRGYVTAYDAETGKEAWRFYTVPGDPKLPPEGKGMEIAAKTWFGDAYVEQGGGGTAWDSFAYDPELNLLYIGVGNGSLWDPKWRSQAKGDNLFLSSIVAVNADTGEYVWHYQTTPGDAWDYTATQHMILAELPIDGKPRKVLMQAPKNGFFYVIDRATGELLSAKGIVPQSWTKGMDMKTGRPILDEENAAYWKNGKRNLVTPAFWGAHDWQPMSYNPDTGLVYIPAHIMSAYYEHIPEAPKRNPFKSMYQLGLRTGMMPEGAEGLLEMAKSWSGKLIAWDPVKQQAAWEVPYVTIFNGGTLSTAGNLVFEGSADGRVIAYAADTGEKLWEQPAASGVMAAPVTYSVDGEQYVTFMAGWGGAFSTFAGALSLRAGVQPYAQVLTYKLGGTAKLQEPAPRPDTPKPPALSNDTASIEAGAKLYDGYCSQCHGIHAVSGGVLPDLRKLTPEKHQMFLGILFGGRVPDGMPSFADAFTPEQVDQIHQYLIKRAHDLHQEGDTWKQFSAKSSH
The following text describes a protein:
Function:
Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, may regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, and exocytosis. Phosphorylates inositol hexakisphosphate (InsP6).
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MEHSLSRTASVESTRSWQQLMAGSLPADRKARSSEPETGGDSVGRASVSLPPSGSQAIRQLPQRRASKASDSILDLFGHARSSNSTNSTNGSAIDEVETTPTLEGTRTSSLVPLNALMLPDALRPPPPRPPPDAEVPENKRLSFSSLYSIGSAIYANTRGHSWSGRSSLAGSEFDAKMEGAPHTTTATSSLTVETTRQNGTLGPKLSPTQALFPQEQPASATPSLTPSNASATNLALAAQAGLSTQPRRSRSRTAQRRISGSTATSSSPASRDMREKKPTKGIIGVCALESKARSKPARNIFGKLVEEFDVKIFGDKIILERGRRELGPSFFSDGFPLDKAIAYVRLRKPFCVNDLPMQQVLWDRRLCLGILDKLSVPTPRRIDVTRDGGPRLQSPEFAKSVFERTGLKLQGPEDGTGGGVQPPKHVELVDDGNTILVDGVTLTKPFVEKPVSGEDHNIHIYFHKKDGGGGRRLFRKVNNKSSEKDDTLEVPRSILDPTSSYIYEQFLQTENSEDVKAYTVGPSFCHAETRKSPVVDGLVKRNPSGKEVRYVTKLNEHEAAMASRISEGFGQRVCGFDLLRTDGNSFVIDVNGWSFVKDNGDYYDRAANILKDMFIKEIHRKQRKDAAQSAAADAQKAPEDAATARKSEHRKVFGKIFKSPKISLPPVFDDADLHLEPEASQSEEQIPVPPPASAAQWKLKGVVAVVRHADRTPKQKFKYTFHSKPFVDLLKGHQAEVLLIGQVALQSVNDAVKVAMDEELEDMKKLRELQLYLNKKGAWPGTKVQIKPMFRKRKKEELLPGESLPQDTTDAPRQGSVSGEGKDATSATSDETEIERLKNRSDSMSGVTLSRITAQDNNMVLDKLQLIIKWGGEPTHSARHQTQDMGANFRNDLMLMNRDVLDDVSIFSSSERRVTTSAQIFGASFLDKDQYLEERISVRKDLLDDSNAAKDVMDKVKKKLKTLLRAGTKAPPQFAWPKDIPEPYIVARQVVDLMKFHQRVMNHNFKKIDSEAVSSLTAIQSPPTQPTTPGQSLHQHTNVNHIQSRWCCNEGPELFKERWEKLFKEFADADKVDPSKISELYDTMKFDALHNRSFLEWVFTPDATFVDEDPIVESSKQNSPEQSGKNTPTQSEQPVKSDLRDINKEINPEKPLEHRASLSHRMGFRRKSEIAIKPAPVPSYVNESYFKLYTGLGTAASKAQIDARLVKLREMYHMCKVLFDYIGPQEYGIESEEKLEIGLLTSLPLLKEIVADLEELQASDTPKCFFYFTKESHIYTLLNCILEGGIKTKIERNAIPELDYLSQINFEFLTAHQDWKEVLETLRAKFHTVKLPKSFVAIDLSQDSNGDRRGNGKMKENGDAKSEDGERGRSEERQDEIMLPIAGDVANIASPVSTLDSGEGREGLQPAVLPPPALDP
The following text describes a protein:
Function:
Probable transcription factor. Controls central cell differentiation during female gametophyte development. Required for the expression of DEMETER and DD46, but not for the expression of FIS2. Probable transcription factor that may function in the maintenance of the proper function of the central cell in pollen tube attraction (Probable).
Miscellaneous:
MISCELLANEOUS: Plants lacking AGL80 (mutant fem111) have defects in central cell and endosperm development.
Subcellular Localization:
Nucleus.
Sequence:
MTRKKVKLAYISNDSSRKATFKKRKKGLMKKVHELSTLCGITACAIIYSPYDTNPEVWPSNSGVQRVVSEFRTLPEMDQHKKMVDQEGFLKQRIAKATETLRRQRKDSRELEMTEVMFQCLIGNMEMFHLNIVDLNDLGYMIEQYLKDVNRRIEILRNSGTEIGESSSVAVAASEGNIPMPNLVATTAPTTTIYEVGSSSSFAAVANFVNPIDLQQFRHPAAQHVGLNEQPQNLNLNLNQNYNQNQEWFMEMMNHPEQMRYQTEQMGYQFMDDNHHNHIHHQPQEHQHQIHDESSNALDAANSSSIIPVTSSSITNKTWFH
The following text describes a protein:
Function:
Acts as a cargo receptor for glycogen. Delivers its cargo to an autophagic pathway called glycophagy, resulting in the transport of glycogen to lysosomes.
Subcellular Localization:
Cell membrane, sarcolemma, T-tubule. Endoplasmic reticulum membrane; Single-pass type III membrane protein. Preautophagosomal structure membrane; Single-pass type III membrane protein.
Sequence:
MGAVWSALLVGGGLAGAIFVWLLRDGGEGDSERQDAAPGGARRGGGGLSCGPPGREPAASPEHLQESNGCLVSETKGHGNLQEAARRLQSPSGKDSGCNSSREHVPSGGFPATESLAASETGNSRGYSEVSRNESLESAIREWGFQKGQETLANVASCFAEKLYSSNLVIDRAKEVSLAQLSNQDRADNEDWEMVSRHSSWGDAALGGSLEAPVVSPNQEMDCGRSTLMEPRGQEVDVKRKKVVAVVSGSQQVSIRFQIHYITSTGKQCIAITGDHKSLGRWSTYLPLQYSKDGFWCRSVSLPADTVVEWKFVVVENGEITRWEECSNRFLETGREDKVVQKWWGIP
The following text describes a protein:
Function:
Functions as a ribosomal silencing factor. Interacts with ribosomal protein uL14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation.
Subcellular Localization:
Cytoplasm.
Sequence:
MIDVLRKILKKISEKGGENPVVLDMRKTPVPTDYFVIFTANSYTHMRAMRDELIDLIKELSLPLIYYDKGEEYEWLIIDAGSVVIHIFTEKGRDFYDLEGLWIDADRISV
The following text describes a protein:
Function:
Catalyzes the dephosphorylation of different sugar phosphates.
Sequence:
MAIKLIAIDMDGTLLLPDHTISPAVKNAIAAARARGVNVVLTTGRPYAGVHNYLKELHMEQPGDYCITYNGALVQKAADGSTVAQTALSYDDYRFLEKLSREVGSHFHALDRTTLYTANRDISYYTVHESFVATIPLVFCEAEKMDPNTQFLKVMMIDEPAILDQAIARIPQEVKEKYTVLKSAPYFLEILDKRVNKGTGVKSLADVLGIKPEEIMAIGDQENDIAMIEYAGVGVAMDNAIPSVKEVANFVTKSNLEDGVAFAIEKYVLN
The following text describes a protein:
Function:
Substrate-binding subunit of tRNA (adenine-N1-)-methyltransferase, which catalyzes the formation of N1-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA.
Subcellular Localization:
Nucleus.
Sequence:
MSQNSLQNDSIQNPRVTWEGCSVLLDINDGDRLVFARLSASATLKIGNKNCSLQPLIGCPFGSLFQVDNGPRGPYLSRVTPSAEGNDLQETQDCQLKDEPKDNRAIVDNNKAQSLTGEDIDEMRRQGATGDEIVEALISNSATYEKKTSFSQEKYRLKKQKKYSPRVLLRRPFCRSICEAYFKKYPARIGFLRVDTLSLLLSMANIAAHSDVLVVDMVGGLLTGAVAERLGGTGYVCNAYLGDTPYPMDIVRIFNFSSEICKRIVRSPVDGLRSIQDGTSEQFFQHKGVSNSEIQSNEQMSSQDSFPHSISTEETTLSSENGMLDLIPQMVTASPPQVAKTCKATKAGENASLDAINLWKENGFSSLLIAAPELDVWSIVQEFLPFLSYSASFAIYHQYLQPLATCMHNLQLGKMAIGLQISEPWLREYQVLPSRTHPCMQMSAFGGYILSGTRICSSDSQIQK
The following text describes a protein:
Function:
As part of a SNARE complex may be involved in endoplasmic reticulum membranes fusion and be required for the maintenance of endoplasmic reticulum organization. Also plays a role in apoptosis. It is for instance required for endoplasmic reticulum stress-induced apoptosis. As a substrate of RNF185 interacting with SQSTM1, might also be involved in mitochondrial autophagy.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Mitochondrion membrane; Single-pass type IV membrane protein. Note=Localization to the mitochondrion is regulated by RNF186.
Sequence:
MAAPQDVHVRICNQEIVKFDLEVKALIQDIRDCSGPLSELTELNTKVKEKFQQLKQRIQELEQSAREQDKESEKQLLLQEVENHKKQMLSNQTSWRKANLTCKLAIDNLEKAELLQGGDSLRQRKTTKESLAQTSSSITESLMGISRMMSQQVQQSEEAMQTLVSSSRTLLDANEEFKSMSGTIQLGRKLITKYNRRELTDKLLIFLALALFLATVLYIVKKRLFPFL
The following text describes a protein:
Function:
O-mannosyl-transferase that transfers mannosyl residues to the hydroxyl group of serine or threonine residues of proteins. Specifically glycosylates the IPT/TIG domain of target proteins, such as MET and MST1R/RON. TMEM260-mediated O-mannosylated residues are composed of single mannose glycans that are not elongated or modified.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein; [Isoform 3]: Membrane. Note=Shows perinuclear localization.
Sequence:
MSPHGDGRGQAQGRAVRVGLRRSGGIRGGVAVFAAVAAVFTFTLPPSVPGGDSGELITAAHELGVAHPPGYPLFTLVAKLAITLFPFGSIAYRVNLLCGLFGAVAASLLFFTVFRLSGSSAGGILAAGVFSFSRLTWQWSIAAEVFSLNNLFVGLLMALTVHFEEAATAKERSKVAKIGAFCCGLSLCNQHTIILYVLCIIPWILFQLLKKKELSLGSLLKLSLYFSAGLLPYVHLPISSYLNHARWTWGDQTTLQGFLTHFLREEYGTFSLAKSEIGSSMSEILLSQVTNMRTELSFNIQALAVCANICLATKDRQNPSLVWLFTGMFCIYSLFFAWRANLDISKPLFMGVVERFWMQSNAVVAVLAGIGLAAVVSETNRVLNSNGLQCLEWLSATLFVVYQIYSNYSVCDQRTNYVIDKFAKNLLTSMPHDAIILLRGDLPGNSLRYMHYCEGLRPDISLVDQEMMTYEWYLPKMAKHLPGVNFPGNRWNPVEGILPSGMVTFNLYHFLEVNKQKETFVCIGIHEGDPTWKKNYSLWPWGSCDKLVPLEIVFNPEEWIKLTKSIYNWTEEYGRFDPSSWESVANEEMWQARMKTPFFIFNLAETAHMPSKVKAQLYAQAYDLYKEIVYLQKEHPVNWHKNYAIACERMLRLQARDADPEVLLSETIRHFRLYSQKAPNDPQQADILGALKHLRKELQSLRNRKNV
The following text describes a protein:
Function:
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function.
Subcellular Localization:
Cytoplasm, perinuclear region. Nucleus.
Sequence:
MTELVKMKRSKAPTTRRAEIQQLYQCYSAGMTSLPSSALLKFLHKEQMELTADEDTAESLIDRYEIEETARENRSMTFEGFLRYMESKVCCVFNQAHTSVYQDMDQPLTSYFISSSHNTYLTGDQLIGKSHLDAYVWALRKGCRCLEIDTWDGPDMEPIVYHGYTLTTKILFKDVITTVAQHAFEVSPYPVILSLENHCSQQQQEVMAQYLVSILGDMLLTAPLDHLAGGELPSPNDLKCKILIKNKKKKPRIKTEQATEESADEGEEDYDDLEDEEDDEDHQTKTKFWSPRKAGPKKEEKKVVIAEALSDLVIYTRSVKFIGFSHSRDHQSYFENTSMAEKKARKLASGSGLNFVQHNQRFLTRIYPAGSRMSSSNYNPQEFWNVGSQLVALNFQSLGLPMDLNDGRFQDNGGCGYVLKPAVLLPSDRSFDPICSRHRLKPTHLLLKVISGSNLPVSRSNKGLDPFVRVEIHGIPSDSRKKNTQTVKNNSLSPHWDSDMNFIISVPELCLIRFCVRDQTGLLSSEFVGQYTLPFTSMMKGYRWVPLRSRDGCSLDPASLFIFVCVVAPPAGRIPAVHQDQFAPSSRINHLSSSRSSLSSLIMASARSLLFFCFLFFTFTSSTIPYINGTFLYTSCEEKTDMRPLKHTRTTHCIERIWP
The following text describes a protein:
Function:
Catalyzes the conversion of ribonucleotides into deoxyribonucleotides, which are required for DNA synthesis and repair. Can reduce each of the four common ribonucleoside triphosphates.
Miscellaneous:
MISCELLANEOUS: The glycyl radical is involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical. The ketyl radical gains an electron from a cysteine residue and a proton from formic acid, forming 3'-keto-deoxyribonucleotide and generating a thiosulfuranyl radical bridge between methionine and cysteine residues. Oxidation of formate by the thiosulfuranyl radical results in the release of CO(2) and regeneration of the thiyl radical.
Domain:
Modulators bind to two classes of sites, one that binds ATP and dATP and regulates pyrimidine ribonucleotide reduction ('pyrimidine site'), the other that binds dATP, dGTP, and dTTP and regulates purine ribonucleotide reduction ('purine site').
Sequence:
MTPHVMKRDGCKVPFKSERIKEAILRAAKAAEVDDADYCATVAAVVSEQMQGRNQVDINEIQTAVENQLMSGPYKQLARAYIEYRHDRDIEREKRGRLNQEIRGLVEQTNASLLNENANKDSKVIPTQRDLLAGIVAKHYARQHLLPRDVVQAHERGDIHYHDLDYSPFFPMFNCMLIDLKGMLTQGFKMGNAEIEPPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPFVTASYNKHRKTAEEWNIPDAEGYANSRTIKECYDAFQSLEYEVNTLHTANGQTPFVTFGFGLGTSWESRLIQESILRNRIAGLGKNRKTAVFPKLVFAIRDGLNHKKGDPNYDIKQLALECASKRMYPDILNYDQVVKVTGSFKTPMGCRSFLGVWENENGEQIHDGRNNLGVISLNLPRIALEAKGDEATFWKLLDERLVLARKALMTRIARLEGVKARVAPILYMEGACGVRLNADDDVSEIFKNGRASISLGYIGIHETINALFGGEHVYDNEQLRAKGIAIVERLRQAVDQWKEETGYGFSLYSTPSENLCDRFCRLDTAEFGVVPGVTDKGYYTNSFHLDVEKKVNPYDKIDFEAPYPPLANGGFICYGEYPNIQHNLKALEDVWDYSYQHVPYYGTNTPIDECYECGFTGEFECTSKGFTCPKCGNHDASRVSVTRRVCGYLGSPDARPFNAGKQEEVKRRVKHLGNGQIG
The following text describes a protein:
Function:
Controls heterocyst differentiation. Dimerization is required for DNA-binding. Has both a protease and a DNA-binding activity; Controls heterocyst differentiation; increased expression leads to more heterocysts than usual. Has protease activity. Binds the promoter regions of hetR, hepA and patS and is required for their expression. Dimerization is required for DNA-binding, DNA-binding is inhibited by the PatS6 peptide. Binds the inverted repeat 5'-GTAGGCGAGGGGTCTAACCCCTCATTACC-3' found in the hetP promoter, required for expression of hetP.
Miscellaneous:
MISCELLANEOUS: In Nostoc filaments, approximately every 10th vegetative cell terminally differentiates into a heterocyst specialized for nitrogen fixation under nitrogen deficiency.
Domain:
Has an N-terminal DNA-binding domain that inserts into the DNA major groove, a central flap domain and C-terminal hood domain. The hood domain binds the PatS6 peptide. Upon PatS6 binding the flap domain probably moves considerably.
Sequence:
MSNDIDLIKRLGPSAMDQIMLYLAFSAMRTSGHRHGAFLDAAATAAKCAIYMTYLEQGQNLRMTGHLHHLEPKRVKIIVEEVRQALMEGKLLKTLGSQEPRYLIQFPYVWMEQYPWIPGRSRIPGTSLTSEEKRQIEHKLPSNLPDAQLVTSFEFLELIEFLHKRSQEDLPPEHRMELSEALAEHIKRRLLYSGTVTRIDSPWGMPFYALTRPFYAPADDQERTYIMVEDTARYFRMMKDWAEKRPNAMRALEELDVPPERWDEAMQELDEIIRTWADKYHQVGGIPMILQMVFGRKED
The following text describes a protein:
Function:
Probably involved in the diffusion of protonated ethanolamine (EA) into the cell at low pH. At low pH most EA is protonated, and this permease becomes necessary.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MGINEIIMYIMMFFMLIAAVDRILSQFGGSARFLGKFGKSIEGSGGQFEEGFMAMGALGLAMVGMTALAPVLAHVLGPVIIPVYEMLGANPSMFAGTLLACDMGGFFLAKELAGGDVAAWLYSGLILGSMMGPTIVFSIPVALGIIEPSDRRYLALGVLAGIVTIPIGCIAGGLVAMYSGVQINGQPVEFTFALILMNMIPVIIVAILVALGLKFIPEKMINGFQIFAKFLVALITLGLAAAVVKFLLGWELIPGLDPIFMAPGDKPGEVMRAIEVIGSISCVLLGAYPMVLLLTRWFEKPLMSVGKVLNMNNIAAAGMVATLANNIPMFGMMKQMDTRGKVINCAFAVSAAFALGDHLGFAAANMNAMIFPMIVGKLIGGVTAIGVAMMLVPKEDATATKTEAEAQS