lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Probable transcriptional regulator.
Subcellular Localization:
Nucleus.
Sequence:
MDESFNSILEPENAWLFLFDDVSQLQQLPIVQNNQENFINSIDFNTGDVTTTNISGLNFQSLEESLNSDTSIENKPQIIEQIQFLQQQQQQQHDQIQQQLHNFQQQYQQQYQQRQQQYQQQYQKPYTPPSFIYSEKNDLVPQQQFHLGQENLQQPPQSLQQQQQPPSPSSPPQQQQQPQQQLQQLQQQHQQHQQHQQQPQFQQLPIQHELPQQSQLQHIQIQSQQIPTQPQPQQIQKQIQIEQPQVQVQQQIQPQQQIQPQQHIQLQQHIQLQQPQIQQQQLPPQTIQQKEINKKNQSKQSSNSMPLSQQIFFNTPKLDQHLLSYFQTQKTNNTINTLNVDQKRDNIEKQKENTSPPTPSSPVPTIINSNSTDINQISPSQQQQQQQQQQQQTTDINKILTLQQLEQQQLEYQKQQQQQQQFNLTFDDESKKSIKRINQNIANRNFRQRKKDHIKDIEDKMMELTLENEKLKKENESIRQQEHEGGTMAILKPSPEKKQLMLEIRSIVRQIGEALKEDNEKNLIYLLHMYHGAVAKRYSSIDKDAEQIASPEIQLRLASIGYVLKSTPFLTNIFQGIESDSWFNLFKEKANITSQQSVQLDIIREKYCEYNLKLLDEIHDLDSEVKKFFFQNIFVFQSYSISLKTSKPLDLSQQIEFACKLKLLKNKFFENSCLMFETFSSLSKILTPKQEALLLVEIDIFSCFNLKKFEMITNVWANKSKMKKSSDPFKIGDLSQIFEKP
The following text describes a protein:
Function:
Probable transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MGRKKVEIKRIEDKSSRQVTFSKRRKGLLKKAKELSILCDADVAVVVFSNRDRIYDFSSTNSLTEIVHRYHSHVEAEKESSAEVLDTEHSKYASFMTVGQLLQTVGRQLEEPAVDDLSVTDLVHLENQLPTALMQVRSSKTHLMIESIKSLREKEKLLSEENKHLENKIATTKNKREVKNEMALDFTNLAPASMNCQQQKTTLNFL
The following text describes a protein:
Function:
Catalyzes the transfer of the GlcNAc-1-phosphate moiety from UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate (C55-P), yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP-C55).
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MELIKSGLIAFVASLFCIWLLRPLAIRIGFVDRPNDRKWHEREVPMIGGIAMFFSFCFALLTLSTSLLPYRGMLAGSSILVLMGVVDDFSDLSSKLRLFGQLFAALLMIIWGNVVLSNLGNLFFLGDLKIGLWAIPITVIVVLANINAMNMIDGQDGLAGGVALGQALLLLLVSVKLHQVSDFRLLFILIILLIAFLGFNMRLLWRKEASIFMGDSGSTFIAFLLAWFAIDLSQQNSALIKPMTILWIMAFPLFDLINVIVLRVRQKKSIIVASRDHFHHVLHVAGLNTSLSTLLLCALSLLLGIFGLALNYFTVSDGWQFILWVGALFCYIYIVELTRKPIIDNEIDIIANPEG
The following text describes a protein:
Function:
Receptor for ATP that acts as a ligand-gated ion channel.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MGQAGCKGLSQALFDYKTEKYVIAKNKKVGLLYRLLQVSILTYLVVWVFLVKKGYQDTDTSLQSSIVTKVKGVTFTNTTELGERLWDVADYVIPPQGENVFFVITNLIVTPNQRQETCAESESIPDAWCYTDSDCPPGEPVVAGNGVKTGRCLRVGNMQRGTCEIFAWCPVESKSRPVKPLLGKAEDFTVYIKNFIRFPKFNFSKTNVLDTKDKAFLKSCQFGPKNPYCPIFRLGSMVSWTGSDFQKIAQQGGVIGIQIEWDCDLDKAPSECNPHYSFSRLDNTLSGNSISSGYNFRFARYYRDGAGVEFRTLMKAYGIRFDVMVNGKAGKFSIIPTIINIGSGVALMGAGAFFCDLVLIYLIKKSHFYRDKKYEEVRILQVLPGLAESSQQGGIPEAEEAEHPEAQPRGSSQKGNSCRYQQHLEPTRSSHLGNGKVHMEQLQNLRTAEA
The following text describes a protein:
Function:
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MILPWLILIPFIGGFLCWIAEHSSKTLPRWIALLSMTLVLILSLWIWATGDFQLAPAPGGEPEWTLQFKVLWIERLGISIHLAMDGLSLLMVALTGLLGVLSVLCSWNEIQRRIGFFHLNLLWILGGVIGVFLAIDLFLFFFFWEMMLVPMYFLIALWGHSSDDGKKTRIYAATKFFIFTQASGLVMLVAILGLVFVNFNATGVITFDYATLLKTQLSPHVEWLLMLGFFVAFAVKMPVVPVHSWLPDAHAQAPTAGSVDLAGILLKTAAYGLIRFALPLFPNASAEFAPIAMWLGIIGIFYGALLSFAQTDIKRLVAYSSVSHMGFVMIGIYSGSQVALQGVVVQMIAHGLSAAALFILCGQLYERLHTRDMRKMGGLWSRMPYLPAISLFFASASLGLPGTGNFVGEFLILIGAFKVVPVIIVIATFGLVFASVYSLIMIHRAYFGPSQSDEPILGLDARELSMVLGLAVLLVLLGVYPQPVLDISAASMHGVQQWLGAALSTLAGR
The following text describes a protein:
Function:
Acts as the second step in ethanolamine degradation by converting acetaldehyde into acetyl-CoA (Probable). Has a very strong preference for NAD(+) over NADP(+) in both catalytic directions. May play a role in bacterial microcompartment (BMC) assembly or maintenance (Probable). Directly targeted to the BMC; Expression of the eut operon allows this bacteria to use ethanolamine (EA) as a carbon, nitrogen and energy source. It relies on cobalamin (vitamin B12) both as a cofactor for the ethanolamine ammonia-lyase (EAL) activity and to induce the operon. EA enhances bacterial survival in macrophages in a concentration-dependent manner, suggesting it is an important nutrient during infection.
Subcellular Localization:
Bacterial microcompartment. Note=Probably located inside the BMC.
Domain:
The first 21 residues target foreign proteins (tested with eGFP) to the BMC in E.coli. The cargo is only detected by Western blot in broken shells, strongly suggesting this protein is normally found inside the BMC and not on its exterior.
Sequence:
MNQQDIEQVVKAVLLKMKDSSQPASTVHEMGVFASLDDAVAAAKRAQQGLKSVAMRQLAIHAIREAGEKHARELAELAVSETGMGRVDDKFAKNVAQARGTPGVECLSPQVLTGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGGPENLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAVVDAARKHTNKRLIAAGAGNPPVVVDETADLPRAAQSIVKGASFDNNIICADEKVLIVVDSVADELMRLMEGQHAVKLTAAQAEQLQPVLLKNIDERGKGTVSRDWVGRDAGKIAAAIGLNVPDQTRLLFVETPANHPFAVTEMMMPVLPVVRVANVEEAIALAVQLEGGCHHTAAMHSRNIDNMNQMANAIDTSIFVKNGPCIAGLGLGGEGWTTMTITTPTGEGVTSARTFVRLRRCVLVDAFRIV
The following text describes a protein:
Function:
Glycosyltransferase that plays a role in cell adhesion.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MLAKNRLPGSGHTTPSPPASPRRSPRYRHGRSKAAAGSRFPTVQPSRTLAHRLSWILLSVLLRRQGIFLFAPLIYISCMLLYMGTVSFDVVPIIQRRPPPGSVYKSPQVYAKLRPEMDADNSTADAITTIWKHSYKGGEWKPYVNKSTGDLPESNGYIYVEANGGLNQQRTSICNAVAVAGYLNATLVIPNFHYHSIWRDPSKFGDIYDEEFFVSTLSNDVRVVDTIPEYLMERFDHNMTNVYNFRVKAWSPIQYYRDSILPKLLEEKIIRISPFANRLSFDAPQAVQRLRCLANYEALKFSKTILTLGETLVKRMKEQSANHGAKYVSVHLRFEEDMVAFSCCIFDGGNQEKQDMIAARERGWKGKFTKPGRVIRPGAIRQNGKCPLTPLEVGLMLRGMGFNKSTYIFLASGEIYDANRTMAPLLEMFPNLQTKEMLASEEELAPYKNFSSRMAAIDYTVCLHSEVFVTTQGGNFPHFLMGHRRYMFGGHSKTIRPDKRKLAILFDNPNIGWRSFKRQMLNMRSHSDSKGFELKRPNDSIYTFPCPDCMSRRNKTTTPESRPPPAT
The following text describes a protein:
Function:
Ensures chromosome alignment and accurate chromosome segregation during mitosis. Promotes proper kinetochore-microtubule (k-MT) interactions during anaphase B. The phosphorylation status of nsk1 affects the proper k-MT coupling, ensuring that it interacts stably only at the correct time during mitosis.
Subcellular Localization:
Nucleus, nucleolus. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore. Note=Undergoes cell cycle-dependent localization changes, nucleolar during interphase, distributed in the nucleoplasm during metaphase, and increased at kinetochores and the spindle during anaphase.
Sequence:
MAYKLSLSAVEPLLIFPAAPFSTKKEKSTFQNNLISSDVFSSALKPLSPLKSLVADFSTHSNPSKDNQLISPPKINHREFLNEEKESDTQTRYLKQLINICNSPSKNHETSLSPSKSTIDNNERKLDNEIDNYKHDVKYSPYKGQGKTSNPSQGTTKCPGIFEEDNFFSVSPKRRKNLFEKYGKTDLGKPARVPSPKKSLSSTIKSPPSRVKLPTSILSKSPPLKVPNKNRSSTFSPLRTPTSSSKTFVIVDHSTPSPPSIRTKLEAFAPNSTFATQKRLRRLATLESSPALRSTLKSLQSKSSPVKLLKLKEEKAKIKNQLFKSEEEKDPVGKQKLPLESSLSPLDHSSAEKEMQKAPAKNKRRRTGSLETGLYPKESPTPSKKRSKRVLWSLKHIVSPGNREKHSLNSTPESIMKKDTKWPQNLAKNNINSEPNTPTKSNIDTGKAHSARAHKTRKNIQS
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.
Subcellular Localization:
Nucleus.
Sequence:
MHFCKKCGTIMQTPEESNKSFALCYNSKCGHTEPIEASCQETTYELLYNTQQITNKKNDNEEYNRVLGPTIERQCSFCRYRLAAYFTRQMRSADEGQSVFYTCLNCKRVEREDS
The following text describes a protein:
Function:
Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes.
Subcellular Localization:
Nucleus.
Sequence:
MQTSGFFGNHGVGQMVISETPQATLVPWLVGSQLIYGDPLSQLKPLSRDHTDGDDQITSVSRQMNHVIDPRRRPSSGSEIPEKGTNGTVKFSIVPDPKDLGEVQKTQQHYVPFPLQSSLRENPGCFEPGLGQSMVCPSHSYVDQFYGLYATYAAQAMHGRMLLPMAVATQGPIYVNAKQFNAILRRRKARAKAEKKNKSIKVRKPYLHESRHIHAMHRVRGCSGRFLNTKKEGNVGNGGCKVKEWMPPQPANFEASSETLHSGNLKMNSTSSRSSASGSEVTSVCAREDIGDFHIVDNPSPSGFCSHLSMMSGGEGASIGHRWGAAADGCCDPDLLKI
The following text describes a protein:
Function:
Cell surface proteoglycan.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MAVIQRTDCGGMSIRLLFTQGILVLVLTGVWGDPVRSCEQAKNDIEAAKLPKSWLQESPAGGDICGPSSCCSIKSELEMRKTSESLHHFTMSQIFGLSSVVDTRARKFDGLFRSLMNASKLQFHDMFQRTYGKIYLQNSDVFSNFFDKLETYYNRGASRLSDTLDAFFVILYQRMFTVINNQYQFDEKYLDCISDHMADVKPFGDAPRKFTLELKRSFVATRAYFMALATAASAAKKLQSVAIDRECERDLVNMLYCGSCNGMRGLGPCSDYCTAVVGSCLRHHTAFSSDWDNFIDALDKVADRLLGPYNIELVVEPLNVKISEAIMNFQESGTEVSQKIFKMCGQPTLDRKRREANYKDSLEDNPNYEIKRYPPLKRIHGSKKKKTKFSYMNGNETPLEKLVREIKLKLADTRQFWAHLPYQYCNSISAPLSSGQCWNGVSVGEYTGNVTRPPLLLSTVVKDQIYHLQVYTDTLRKAYHGEEVELVDDSDDLLDGSGSGSGDFEIAAPDYAPKAEDIVPKVAEEAPPPSTAGPEVTRPYSGTAKMSLSKALAQFLLPIVLVWFGGAISDLL
The following text describes a protein:
Function:
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
Sequence:
MSATETKYVPRLYKKYKEEVVPILQKKFNYKSPMQIPRLQKIVVNMGVGEAVQDIRQLERAVEDLRAITGQQPVITRARKSEAGFKLRKGMPIGCKVTLRKERMWDFLDKLISVALPRVKDFKGLSPRSFDGRGNYAFGIAEQIVFPEIDYDKVDRIRGMDIIINTTAETDEEAFWLLSLLGLPIRSM
The following text describes a protein:
Function:
May be a part of a signal-transduction system that regulates twitching motility by controlling pilus function (extension and retraction).
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MKKINAGNLFAGMRSSSVIAGLFIVLIVSIVLLFANFAYLNTQSNHDKQYIGHAGELRVLSQRIAKNATEAAAGKGEAFKLLKDARNDFEKRWNILVNGDESTSLPPSPEAVKPQMDVVQQDWDGLRKNADSILASEQTVLSLHQVASTLAETIPQLQVEYEEVVDILLENGAPADQVAVAQRQSLLAERILGSVNKVLAGDENSVQAADSFGRDASLFGRVLKGMQEGNAAMSISKVTNAEAVDRLNEIAELFEFVSGSVDEILETSPDLFQVREAANNIFSVSQTLLDKASQLADGFENLAGGRSINLFAGYALGALALASIILIGLVMVRETNRRLAETAEKNDRNQAAILRLLDEIADLADGDLTVAATVTEDFTGAIADSINYSIDQLRELVETINQTAVQVAAAAQETQSTAMHLAEASEHQAQEIAGASAAINEMAVSIDQVSANASESSAVAERSVAIANKGNEVVHNTITGMDNIREQIQDTSKRIKRLGESSQEIGDIVSLINDIADQTNILALNAAIQASMAGDAGRGFAVVADEVQRLAERSSAATKQIEALVKTIQTDTNEAVISMEQTTSEVVRGARLAQDAGVALEEIEKVSKTLAALIQNISNAARQQASSAGHISNTMNVIQEITSQTSAGTTATARSIGNLAKMASEMRNSVSGFKLPEGVEQA
The following text describes a protein:
Function:
Polyamine deacetylase (PDAC), which acts preferentially on N(8)-acetylspermidine, and also on acetylcadaverine and acetylputrescine. Exhibits attenuated catalytic activity toward N(1),N(8)-diacetylspermidine and very low activity, if any, toward N(1)-acetylspermidine. Histone deacetylase activity has been observed in vitro. Has also been shown to be involved in MSH2 deacetylation. The physiological relevance of protein/histone deacetylase activity is unclear and could be very weak. May play a role in the promotion of late stages of autophagy, possibly autophagosome-lysosome fusion and/or lysosomal exocytosis in neuroblastoma cells. May play a role in homologous recombination. May promote DNA mismatch repair.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Excluded from nucleoli.
Sequence:
MGTALVYHEDMTATRLLWDDPECEIECPERLTAALDGLRQRGLEERCLCLSACEASEEELGLVHSPEYIALVQKTQTLDKEELHALSKQYNAVYFHPDTFHCARLAAGAALQLVDAVLTGAVHNGLALVRPPGHHSQRAAANGFCVFNNVALAAKHAKQKYGLQRILIVDWDVHHGQGIQYIFNDDPSVLYFSWHRYEHGSFWPFLPESDADAVGQGQGQGFTVNLPWNQVGMGNADYLAAFLHVLLPLAFEFDPELVLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLAGGRICAVLEGGYHLESLAQSVCMMVQTLLGDPTPPLLGLMVPCQSALESIQSVQTAQTPYWTSLQQNVAPVLSSSTHSPEERSLRLLGESPTCAVAEDSLSPLLDQLCLRPAPPICTAVASTVPGAALCLPPGVLHQEGSVLREETEAWARLHKSRFQDEDLATLGKILCLLDGIMDGQIRNAIATTTALATAATLDVLIQRCLARRAQRVLCVALGQLDRPLDLADDGRILWLNIRGKDAAIQSMFHFSTPLPQTTGGFLSLILGLVLPLAYGFQPDMVLMALGPAHGLQNAQAALLAAMLRSPVGGRILAVVEEESIRLLARSLAQALHGETPPSLGPFSKATPEEIQALMFLKARLEARWKLLQVAAPPP
The following text describes a protein:
Function:
Nitronate monooxygenase that uses molecular oxygen to catalyze the oxidative denitrification of alkyl nitronates. Acts on propionate 3-nitronate (P3N), the presumed physiological substrate. Probably functions in the detoxification of P3N, a metabolic poison produced by plants and fungi as a defense mechanism.
Miscellaneous:
MISCELLANEOUS: P3N is a potent irreversible inhibitor of the key enzyme succinate dehydrogenase in the Krebs cycle and electron transport chain. P3N has been shown to be a toxic metabolite to bacteria, plants, fungi, mammals or any organism that uses succinate dehydrogenase.
Sequence:
MNEFMKKFSLTKPIIQAPMAGGITKPRLASAVSNQGALGSLASGYLTPDLLEQQIKEIFELTDAPFQINVFVPLGLEMPPKDQIKKWKENIPLANQVNQFTSVQEEWDDFYQKIDLILKYKVKACSFTFDLPPEDAVKELKTAGCCLIGTASTVEEALLMEERGMDIVVLQGSEAGGHRGAFLPSKGESAVGLMALIPQAADALSVPVIAAGGMIDHRGVKAALTLGAQGVQIGSAFLICHESNAHPVHKQKILEANEADTKLTTLFSGKEARGIVNKWMEENEQFETQTLPYPYQNTLTKAMRQKASLQNNHDQMSLWAGQGIRSLTEEISVKQLLNQLCQEDIKI
The following text describes a protein:
Function:
Functions as a two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction.
Subcellular Localization:
Cytoplasm, cytosol. Nucleus.
Domain:
Histidine-containing phosphotransfer domain (HPt) contains an active histidine that mediates the phosphotransfer.
Sequence:
MDIKALHLKLQEMRQSFFNEGYLNCQYTQIEALEKDSSPYFIVEIITLYFRDSPNVIAALEHEFIGAIKINNELEKANILLQAGNVEGMKEAVRRIKKEHSELRAKFETYFQLMRRAGPTEQAVNSS
The following text describes a protein:
Function:
Component of the nexin-dynein regulatory complex (N-DRC) a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. May play a role in the assembly of N-DRC.
Subcellular Localization:
Cell projection, cilium, flagellum. Cytoplasm, cytoskeleton, flagellum axoneme. Note=Detected along the length of the sperm flagellum.
Sequence:
MAAPNLITPLRDICVKVVAANFEGCPTFGPLPDKYVKRIIDILPLDLPLELVGSLIADEDYWRRRSQARWKNCEVAAHGYSWKQLFFERNLMEFLEQYDPAVTDLSSLKRLLTYSRRFVQTVHIRQLPSHLDLQILFECMVNTPSSLALSYNLKEVGMDYDRSLFGMKLSDCRALAKALEHTETLTHLDLSNNSLDDDKVRMLASGLVENLSITHLNLSHNKIADRGVRALAKLLDGHSVISLLELHDNQIHTEGAESLARAFKSNQCLLSVNLRLNRMGDEGCKAVVESVRGSPTLQRLNISANAAGPGTAAAVVALLRLNNTLTELDVSCNQFGEDACGNVRRALEQNGSVRLMDVRMTGINPDDEMAIAENLRARQERVDKARVLGK
The following text describes a protein:
Function:
Lectin involved in innate immunity. Agglutinates all types of human erythrocytes, Gram-positive and Gram-negative bacteria. Has a stronger agglutinating activity towards Gram-negative bacteria than towards Gram-positive bacteria. Specifically recognizes acetyl group-containing substances on agglutinated cells. The hemagglutinating activity was inhibited by EDTA, acetyl group-containing mono- and disaccharides, N-acetyl derivatives of amino acids, other acetyl group-containing substances, propionamide and benzamide. Enhances the antimicrobial activity of big defensin against Gram-positive bacteria but not against Gram-negative bacteria.
Subcellular Localization:
Secreted.
Sequence:
MPAKWISTLVLIGFFAMINGVLSVDSHDKGSVRSSLNEGLSMAEVRTAINRAMSGKDSRMPTPRDILSANVSGTTLKNPILDFTESFNVGKSCYDILVTQNASQSGLYLVHPPNIVQGPWKVYCDQESEGGGWTVFQVRDDVEPHENFMRNWEDYKLGFGDFDREFWLGNILLWALTNSNDNKKYELAVNLEDWSGNKRFARYKGFRIGPESDKYRLYFTKMFLGNAGDSLFSHNGLAFSTFDVDNDNREGEDFAERSCARLYKGGWWYGNCHDSNLNGWYLGGPHRSFADGINWYTWSGYNYSLRRTMMRFRPLSDNYTSNGPSIGLSVPNSYSPIKPDSYLPMRGFRNIEDSSAELKDNVEPEPGLNQSKSNV
The following text describes a protein:
Function:
DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (top2) active site tyrosine residue. Hydrolyzes 5'-phosphoglycolates on protruding 5' ends on DNA double-strand breaks (DSBs) due to DNA damage by radiation and free radicals.
Subcellular Localization:
Nucleus. Nucleus, PML body.
Sequence:
MSSSDNDEPKVVEISDDEMECEGVVEVNNEQSDEAKMREFAEITATDEIMAQSILQDVGWDLKRALDVFFGSDAFKETRNEAVMGPSSSAVGNQPVMTAEDLKGFELSLMSWNIDGLDGRSLATRMKAVATIVKKVNPDILFLQEVVDRDLEPIDKLQSLYKIYYSNKGCQYYTAILVSKMFEVEKHDVVHFQNSGMYRTLQIVEGSIGGMKVFLVNTHLESMRDHRAQRMAQFSFCMDRCAEIIANNPGCFLFFGGDLNLRDEEISSIPDGVLDAWVSAGCDTKTKWTWDTYKNDNKQGFNGAKMRFDRIYWHGPFNQVHFSLEGRQRIRSCLCFPSDHWAINATFSAV
The following text describes a protein:
Function:
Involved in the regulation of gamete interactions during the double fertilization and to prevent multiple-pollen tube attraction; mediates the redistribution of the gamete fusogen HAP2/GCS1 to the cell surface after secretion upon sperm arrival.
Subcellular Localization:
Cytoplasmic vesicle. Secreted.
Sequence:
MGLKHVFFILALTCLIMANIANATSRNDRLNNNMKPDYDLATRLEASGGLTNPECCRAIDIITRNCWPAMLTSLGFTVEEGNILRGYCDASSPPSPGGLPMIYLPQVSKFWLRQGASMALLFLWC
The following text describes a protein:
Function:
Involved in spore and ascus formation. Required for the efficient assembly of the precursors of the prospore membrane to a continuous prospore membrane.
Subcellular Localization:
Prospore membrane; Multi-pass membrane protein. Endoplasmic reticulum. Note=Localizes to prospore membrane, and accumulates in the endoplasmic reticulum in vegetative and sporulating ERV14-deleted cells.
Sequence:
MLFPKRLIVWGVLLILSLSQFVLYLPATTCTNSKGLRLCAPQFTITVIGGSSTANEFIASVREFLRLISYLTIDMGWSNEFTDPSVYEDENLVDTFQPDKVFELNYFGFCKRSNKSKVYCTSNENYGMDVLEVLVRDVGIQLGNISTTRSNETKKFGDSLVLTYRLALTSIRDFLKHDKHTGNALSKALIGSPDPNVKGVSPTKNYLKGVNLAFILMMFNGMVFYFAVLEIIVGFLSICVVSAFGGALSVGKRHRLFPMLLKSSSSILVVIATLTILCNIVYLIALKTLEPEEVTDVGSDNAAVHTTGWELLKVNVGSGFIMGLARYAIQWVLLVLAFLAANHYKAKPKKSDKYTEDTSNSPSPDLMEK
The following text describes a protein:
Function:
May contribute to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity (By similarity).
Sequence:
MSSAAKKEAILRQFRQLTNATPQDANRILKAHGYRIEPATDAFFNNEQAQINASISSSTLDRKSEREVKERLNALFDRFRDAGADSDEEDDEASQPEDRDLISIGGALKMCEALEVSPEDVVFLPLSYYLKSASMGTFTREGYINGWKMLDLSDTIDKQKKTLEKLRQELLDNKPLRLERIAQEKSNPATASGANKGLYEKVYEYTYAFARREGQKSLALENALAFWDLVLPASPTFQRAGSQGTFTQAQLDLWKRFLSEQTRGRAVSKDTWMQFLDFTKEINSDFSNHDFDAAWPSIIDDFVLWVRDNMPASDGMDTS
The following text describes a protein:
Function:
Involved in lipid catabolism. Essential for sterol esters biosynthesis in leaves and seeds, but not in flowers. Plays a role in controlling the free sterol content of leaves. Catalyzes the transacylation of acyl groups from phospholipids to a variety of different sterols. Prefers phosphatidylethanolamine over phosphatidylcholine as an acyl donor. Not active toward neutral lipids. Highly specific for position sn-2, which in plant lipids is essentially devoid of saturated acyl groups. Broad sterol specificity (cholesterol > campesterol > sitosterol > stigmasterol), but no activity with lupeol or beta-amyrin.
Subcellular Localization:
Microsome membrane; Single-pass type II membrane protein.
Sequence:
MGANSKSVTASFTVIAVFFLICGGRTAVEDETEFHGDYSKLSGIIIPGFASTQLRAWSILDCPYTPLDFNPLDLVWLDTTKLLSAVNCWFKCMVLDPYNQTDHPECKSRPDSGLSAITELDPGYITGPLSTVWKEWLKWCVEFGIEANAIVAVPYDWRLSPTKLEERDLYFHKLKLTFETALKLRGGPSIVFAHSMGNNVFRYFLEWLRLEIAPKHYLKWLDQHIHAYFAVGAPLLGSVEAIKSTLSGVTFGLPVSEGTARLLSNSFASSLWLMPFSKNCKGDNTFWTHFSGGAAKKDKRVYHCDEEEYQSKYSGWPTNIINIEIPSTSVTETALVNMTSMECGLPTLLSFTARELADGTLFKAIEDYDPDSKRMLHQLKKLYHDDPVFNPLTPWERPPIKNVFCIYGAHLKTEVGYYFAPSGKPYPDNWIITDIIYETEGSLVSRSGTVVDGNAGPITGDETVPYHSLSWCKNWLGPKVNITMAPQPEHDGSDVHVELNVDHEHGSDIIANMTKAPRVKYITFYEDSESIPGKRTAVWELDKTNHRNIVRSPVLMRELWLQMWHDIQPGAKSKFVTKAKRGPLRDADCYWDYGKACCAWQEYCEYRYSFGDVHLGQSCRLRNTSANMLLQYI
The following text describes a protein:
Function:
Thiolesterase that catalyzes the hydrolysis of S-D-lactoylglutathione to form glutathione and D-lactic acid. Involved in the metabolism of methylglyoxal, a toxic compound for yeast proliferation, by converting methylglyoxal to lactate via S-D-lactoylglutathione by sequential enzyme reactions catalyzed by glyoxalase I and glyoxalase II.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSFHITPIWMWKGTGNNYAYLLTCDKTKITAIVDPAEPESVIPVIKEKTAKKEIDLQYILTTHHHYDHAGGNEDILSYFPSLKVYGGKNASGVTYTPKDKEIFKVGEVQVEALHTPCHTQDSICYYVSSPSKRAVFTGDTLFTSGCGRFFEGDAKQMDYALNHVLAALPDDTVTYPGHEYTKSNAKFSSTIFSTPELTKLVDFCKNHESTTGHFTIGDEKKFNPFMCLGLESVQKAVGSSDPITVMKKLRDMKNAA
The following text describes a protein:
Function:
May function as transcription factor capable of interacting with purine rich repeats (GA repeats).
Subcellular Localization:
Nucleus.
Sequence:
MSLVDLGKRLLEAARKGQDDEVRTLMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVELLVRNGADVNAKDMLKMTALHWATERHHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEILVILQEAMQNQVNVNPERANPVTDPVSMAAPFIFTSGEVVNLASLISSTNTKTTSGDPHASTVQFSNSTTSVLATLAALAEASVPLSNSHRATANTEEIIEGNSVDSSIQQVMGSGGQRVITIVTDGVPLGNIQTSIPTGGIGQPFIVTVQDGQQVLTVPAGKVAEETVIKEEEEEKLPLTKKPRIGEKTNSVEESKEGNERELLQQQLQEANRRAQEYRHQLLKKEQEAEQYRLKLEAIARQQPNGVDFTMVEEVAEVDAVVVTEGELEERETKVTGSAGTTEPHTRVSMATVSS
The following text describes a protein:
Function:
Antitoxin component of a type II toxin-antitoxin (TA) system. Labile antitoxin that binds to the MqsR mRNA interferase toxin and neutralizes its endoribonuclease activity. Overexpression prevents MqsR-mediated cessation of cell growth and inhibition of cell proliferation. Initially reported to act as a cotranscription factor with MqsA. Following further experiments, the MqsR-MqsA complex does not bind DNA and all reported data are actually due to a small fraction of free MqsA alone binding DNA. Addition of MqsR to a preformed MqsA-promoter DNA complex causes dissociation of the MqsA-DNA complex, probably causing derepression of MqsA-repressed transcripts. MqsA binds to 2 palindromes in the promoter region of the mqsRA operon activating its transcription. Binds to other promoters, inducing mcbR and spy and repressing cspD among others. Binds to and represses the rpoS promoter, the master stress regulator, resulting in decreased cyclic-di-GMP, reduced stress resistance, increased cell motility and decreased biofilm formation; in these experiments 5 TA systems are missing (lacks MazEF, RelEB, ChpB, YoeB-YefM, YafQ-DinJ). An earlier study showed overexpression alone increases biofilm formation, perhaps by repressing cspD; in these experiments the 5 TA systems are present. Represses the csgD promoter. In the presence of stress, when this protein is degraded, the promoters it represses are derepressed, leading to biofilm formation (Probable). This TA system mediates cell growth during bile acid deoxycholate stress by degrading mRNA for probable deoxycholate-binding protein YgiS; bile acid detergents such as deoxycholate are important for host defense against bacterial growth in the gall bladder and duodenum.
Domain:
The Zn-binding N-terminal domain (residues 1-65) binds to the MqsR mRNA interferase toxin and makes contact with the DNA phosphate backbone, while the C-terminus (residues 70-131) binds the promoter in a sequence-specific manner. They are linked by a short flexible domain.
Sequence:
MKCPVCHQGEMVSGIKDIPYTFRGRKTVLKGIHGLYCVHCEESIMNKEESDAFMAQVKAFRASVNAETVAPEFIVKVRKKLSLTQKEASEIFGGGVNAFSRYEKGNAQPHPSTIKLLRVLDKHPELLNEIR
The following text describes a protein:
Function:
Orphan nuclear receptor.
Subcellular Localization:
Nucleus.
Sequence:
MEQIPQEQKTEPFLASFTTTEKLGTETPTTSITPNTQFRGRYEKPNCAVCNEVGDGLHFGAEACRACTAFFRRSVALSKKYECRAGRNCEVSSNIRCMCRSCRYDKCIEVGMNPECVQNRRENDTPKADLQFDTSKTEIRRPIPNFNIVPQASAVPSTSNFMDFSIFKDTPISNFSAFSPASLPGLSSSPSLETMPLLERMRINYDKMENARNVIHRREGENIFQQKVPRAITFREATEVTTKEVSLVADWIEWCFDDFGLLPVDQKTILFQNFFVFFCMLERAFMTVKSGRDGIVVMASKDYIDYDNLEGFFKECNSGTGGTPAEIAKLIRPSFELQKRSLINLMRLENVDSYEFFALCVMLFWDFGLEGQSDECNEVGRRVKHRVTREMTFYLRNVKKHEEPLYRMASVVSILPSLQRAVRRFQEDIEMANIFNIYALPENFVNIINGKFN