lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Subcellular Localization:
Cytoplasmic vesicle membrane.
Sequence:
MGSTIEIKKTFELRSERVKSIDLHPNAPWVLLGLHSGNVCIWNHESQVTEKTFEIANSRVRSAKFIARKEWIVIGADDGFIRVYNYNTMENIIEFKAHSDFIRSLIVHPSQSYLLSASDDKLVKLWDWENDWKCTKTFEGHEHYVMQLAFNPRDANDFASISLDCTIKFWDLGSMDLRLSINGHTEGLNSVEFFEDDGKLYILAGSDDHTAKVWDYESMTCVQTLEGHTHNVTSFQCVKLDASFIITGSEDQTVRVWNMKTYNLDHVFTSDLGRVWTIEFIEDSSKIILGCDEGILVGQVNSTGY
The following text describes a protein:
Function:
Probable disease resistance (R) protein.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MPLTEIIAGAALGLALQILHEAIQRAKDRSLTTSCILDRLDSTILRITPLMAKVEKLNKESDESLRKVFEDLKHLLEKAVVLVEAYAELKRRNLLGKYRYKRRIKELEGSLKWMVDVDVKVNQWADIKDLMAKMSEMNTKLEKIMGQPIDCIISEDNTNMDIVERVDPSLEAKAGCSNSDSKPKIDIHLRWSKQSKDHGIRFVLN
The following text describes a protein:
Function:
Responsible for microtubule translocation. May be important for the organization of phragmoplast-specific arrays of microtubules. Plays an essential role in stabilizing the mitotic spindle. Required during mitotic cytokinesis.
Subcellular Localization:
Cytoplasm, cytoskeleton, spindle.
Sequence:
MAEPKPGPGPGEGNDGVNVNVLLRCRPLSDKEIAERTPQVISCNEALREATLYIQSVGGKQTSKTFRFDRVFSPESSQEKLFKQAIVPIVQEVMEGFNCTIFAYGQTGTGKTYTMEGGPRRSDDGKVLSAEAGVIPRSIKQIFDTIEANNTDSTVKVTFLELYNEELTDLLSTFDDGKEDGKRLRLLEDRSGVVVQGLEEVVVKSAAEIYQVLDRGTAKRRTAETLLNKRSSRSHSVFSITIHMREVTPEGEDVVKVGKLNLVDLAGSENISRSGAKDGRAREAGSINQSLLTLGRVITALVEHSGHVPYRDSKLTRLLRESLGGKTKTCIIATIAPTVQCQEETISTLDYAHRAKNIRNRPEVNQKISKTAMIKEMSSEMEKLRMELIAQREKNGIYISTDKFQADELERVQLRDTVKALREEMKLEQEEFAATLEQQKSESDKAISRLQSELSAAKADLEYMDARLQEASRSIHERQYIITAQRTAEQDVAEAAEAVRIELAAAAQDVGVLFASLEELSDVHSGDRDTIKHVQSLVAERLGGLGSKLTGAAEGQRRQLAGLGESLASFKAQKAQDLQQLLGRVAAVQDTVAAMRDAVERQAQAAEAAASAALGRINDATGSHVAVAVAAAQGLEAATRGAVDALAQAMEQQSQQLAAFTQQQAASSEAACKALHEAMGRLSGRFEGVQAAADQAGTVVEERTAALGEGMGSFAERYKESCAAQQAVLMAQITALVAAFAEERAGEVAREVTALKQQAVEGGKVVRRQLGGIAGTAASARQEVQEAEASLASGMQSQQGRVQEATTSLTASLRSTHDQARAIHAGVAGQLATSITAQECFNKGMGQACSSGIEAVQGAVRACVTGAYEAAASAAYSATELSRGLEEQAEAAAASTDTWVAACSSLDVNLTDACSQQADGMSALASEAASLLQQRLDVERALPPPAQRDFNVPQASALKELRCAPEEKLLARCHAEFPQVFAAGMAAPSSPRSNTSAASSPPLPSGGENVTPLHPQVAPLVPQTAGQQQATGSVPPSPRTGAGTGLRSRIPSKPSLIPSSPATGKELPPNVTSRQQLADKTNNKQSSILADW
The following text describes a protein:
Function:
In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed.
Sequence:
MKLVVAIIKPFKLDEVRQALTAIGVHGMTVTEVKGYGRQKGHTEIYRGAEYVVNFLPKLRIEIAVASDVADKAVAVITATARTGQIGDGKIFVTPIDHALRIRTGETDSDAL
The following text describes a protein:
Function:
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Miscellaneous:
MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong mechanism.
Subcellular Localization:
Cytoplasm.
Sequence:
MITSAHIDDIRTQVRAWRAKGETVAFVPTMGNLHQGHITLVKEAAKKCDHVVASIFVNPMQFGQNEDLDAYPRTLEADSQALTAAGAELLFTPTPAIIYPKGLAQQTYVEVPGISDVLCGASRPGHFRGVATIVCKLFNIVQPDIAFFGNKDYQQLLVIRTMVEDLSLPIEIIGIDTIREASGLAMSSRNGYLTAQEKAAAPALKKAIDAMAQGIKQGISIEQVTEEAKASLTAAGFTPDYLEVRHADTLAKAETQDKALVILAAAYLGKARLIDNLRFDR
The following text describes a protein:
Function:
Functions as a GTPase. May act by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm during the 60S ribosomal subunit maturation.
Subcellular Localization:
Cytoplasm. Endoplasmic reticulum. Nucleus, Cajal body.
Sequence:
MGKRKGNTGLGRSIIRDRFGPRGAGGGRHGESYLHTSELSDGYDWGRLNLQSVTEQSSLDDFLATAALAGTEFEAEKLNIKFVNPDVNVGLLTEEEEKEVQKAQEDNRQYISIPRRPAWDETTSADELQRRERDSFLEWRRQLARLQDKEHIILTPFEKNLEFWRQLWRVIERSDIIVQIVDGRNPLLFRCQDLEKYVKEIDKDKMNMILVNKADLLTETQRRVWAEYFGSRGVKVAFWSAMEETDRQGAKDLEEVAEHQEVVEEDDMEEGGTEEVEEPDDEDMASSDSERHQESEDHIRTSPSETELVQELQDVQVLDTERPTVVGVDQTVSNDPQPIRDREEAVARQEDEEEDVQTADSIEDHSALPDSSVEQHSDGNMEATQTEEQLTQETVPLQTGSVDRATASSEQQRDNCSVGNSVEHAVQNSSVLLTGEELLQLFKDLSPQETQEEGVTTVGLVGYPNVGKSSTINALLKCKKVPVSATPGRTKHFQTLYVDETLLLCDCPGLVMPTFVSTKAEMVVSGILPIDQMRDHLPPTSLVCRHIPRHVLERTYGVNLPAPAEGEDPDRLPTANELLNAYGAMRGFMTAHGQPDTPRSARYILKDYVNGKLLYCHPPPGVDPEEFQIWNDQSTGPASTDGHKHSTSKAQQKTKGHQPAPMSKVDKEFFSKHNVRAITKGAQVPQASNQSTNHQSLSGKPWKKHFNKNKKEKARRVFKHLDE
The following text describes a protein:
Function:
Probable transcription factor which regulates lipid metabolism.
Subcellular Localization:
Nucleus.
Sequence:
MYSSIVPSSSNGYYHQSQYQNAHHQHHQQHYHQQSHHHYNGAAAAPVINVHNYHFHTGPVNNQVIEQHYNHHNHVQQTFEENIPQGPHSSFNFSHDFPQQNNSETHLNHMEPSMTPMEHQNSGSSTPYPFEAKLFVPSPAASVSSYSFSSDLSGKDEEDPRIPLKDRGRVYHPQSTEKPKKVPSKRRDKATLDRLRVHKCFYQGCGKVYTKSSHLTAHERVHSGEKPYPCEWPGCSWRFARSDELTRHYRKHTGAKPFACKECSRKFSRSDHLQLHMKRHETDEQDDGMDDFKDFMTFI
The following text describes a protein:
Function:
Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular Localization:
Cell membrane; Lipid-anchor; Cytoplasmic side.
Sequence:
MAQDLTEKELLKMQIDQLKKEVKNERSMISKTGKELKDYVEAHAGDDPLLKGIPEDKNPFKEKGGCMIS
The following text describes a protein:
Function:
Involved in embryo hatching and implantation.
Subcellular Localization:
Secreted. Note=Secretion into the glandular and uterine lumen may occur as a consequence of progesterone-induced epithelial differentiation.
Sequence:
MFRLLLLALSCLESTVFMASVSISRSKPVGIVGGQRTPPGKWPWQVSLRMYSYEVNSWVHICGGSIIHPQWILTAAHCIQSQDADPAVYRVQVGEVYLYKEQELLNISRIIIHPDYNDVSKRFDLALMQLTALLVTSTNVSPVSLPKDSSTFDSTDQCWLVGWGNLLQRVPLQPPYQLHEVKIPIQDNKSCKRAYRKKSSDEHKAVAIFDDMLCAGTSGRGPCFGDSGGPLVCWKSNKWIQVGVVSKGIDCSNNLPSIFSRVQSSLAWIHQHIQ
The following text describes a protein:
Function:
Part of the ABC transporter complex GltIJKL involved in glutamate and aspartate uptake. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MAIDWNWGIFLQPAPFGNTTYLGWIWSGFQVTVALSLCAWVIAFFVGSLFGILRTVPNRILSGIGACYVELFRNVPLIVQFLTWYLVVPELLPVNLGTWFKSELAPNIQFFLSSMICLGLFTAARVCEQVRAGIQSLPRGQKAAGLAMGLTLTQTYRYVLLPNAYRVIIPPMTSEMLNLVKNSAIASTIGLVEMAAQAGKLLDYSAHAYESFTAITLGYVLINAVIMLLMRLVEKKVQLPGNLGSK
The following text describes a protein:
Function:
Key component of inflammasomes that indirectly senses specific proteins from pathogenic bacteria and fungi and responds by assembling an inflammasome complex that promotes caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria.
Subcellular Localization:
Cytoplasm, cytosol.
Domain:
In an autoinhibited form the C-terminal leucine-rich repeat (LRR) domain is positioned to sterically occlude one side of the NBD domain and consequently sequester NLRC4 in a monomeric state. An ADP-mediated interaction between the NBD and the WHD also contributes to the autoinhibition.
Sequence:
MNFIKENSQALIQRMGIVVIKQICDDLFALNVLNGEEVAIICSHRVEQDAARDIVHMILKKGSAACNLFLKSLENWNYPVYQDLTGHSLFHQNLEEDLDVLAQSLKDLYNSPVFKNFFPLGEDIDIIFNLQITFTEPVLWRKDHRHHRVEQMTLGSLLEALKSPCLIEGESGKGKSTLLQKIAMLWASGMCPALNQFKLVFFIRLSSARGGLFETLYDQLVNIPDSISKPTFRALLLKLHKKVLFLLDAYNEFHPQNCPEIEALVKENHRFKNMVIVTTTTECLRHIRHVGALTVEVGDMTEDSARVLIREVLINELAEGLLFQMQESRCLRNLMRTPLFVVITCAIQMGSEEFQAHTQTMLFQTFYDLLIQKNRRRHSGGTSGDFVRSLDYCGDLALEGVFSHKFDFELEDVCSMNEDVLVRTGLLCKYTAQRLRPTYKFFHKSFQEYTAGRRLSSLLKSREPEEVSKGNSYLKKMVSISDITSLYGNLLLYTCGSSTEATRAIMRHLAMVCEHGSLQGLSVTKRPLWRQESIQNLRNTTEQDVLKAINVNSFVECGINLFSESISKSELSQEFEAFFQGKSLYINSENIPDYLFDFFKYLPNCVSALDFVKLDFYGRATVSQDKTGENSSGVHTEGPSTYIPSRAVSLFFNWMQKFKTLEVTLRDISKLNKQDIKYLGKIFSSASNLKLYIKRCAAVAGRLSSVLRTCKNIHSLMVEASPLTTEDEQYITSVTDLQNLSIHDLHTQRLPGGLADSLGNLKNLLKLILDDIRLNEEDAKSLAEGLRNLKKMRLLHLTRLSDMGEGMDYIVKSLSEEPCDLQEMKLVDCCLTANSLKILAQNLHNLVKLSVLDMSENYLEKAGSEALQGLIGRLGVLEQLSALMLPWCWDAYISLPNLLKQLEGTPGLVKLGLKNWRLRDEEIRSFGEFLEMNPLRDLQQLDLAGHGVSSDGWLSFMDVFENLKQLVFFDFGTEEFLPDAALVRKLGQVLSKLTLLQEARLTGWELDDYDISVIKGTFKLVTA
The following text describes a protein:
Function:
Component of the unc-51/atg-13 complex required for autophagosome formation. Required for the degradation of germ cell specific P-granule components such as sepa-1 by autophagy in somatic cells. This ensures exclusive localization of the P-granules in germ cells. May function downstream of the let-363 (Tor) signaling pathway to mediate sepa-1 degradation. Plays a role in survival during limited food availability.
Subcellular Localization:
Cytoplasm, cytosol. Cytoplasm. Preautophagosomal structure. Perikaryon. Cell projection, axon. Note=Under starvation conditions, is localized to punctate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome. Recruited to preautophagosomes by lgg-1.
Sequence:
MVNEYDTYNKWLKFFSVRMVQSIIQSRLGDEIESKCVPYSENAVDWFNMRIDELGEISAYLKSNIKSYPPVGTLTLEFLLYTPSGQLLPLEAWILSSSEGTDDCSRNELYHDMSTLLRSAIVSARMTPMHRLYVKKQHLETFVIMYRVFENDISSDMGKGKKTRKIGELVSKFGNISLDLHYRTSMHFEEPEIAPVTPVEDVEEEIDDGEKTVVDENIQTRTVSECVPIADAKKRKASGSVESATSAGSSTSREAAPRFILGQSTSSEDSRHSDVQNSYEEDHKPSLADLRNHSFPFVNLLQSAYNPANGTKKNSSSTCLNSPKSTPEDKEPTIEKVAESFRAAKIDEVVFEEDEDEELPLDSMELSEDSFVHFNQLSDFGGAPSLGNELGDYLKQLKTAPDMTESGDIDICNMDLKTELEKISSQTANFNNFLKHVNSFSDE
The following text describes a protein:
Function:
Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs.
Miscellaneous:
MISCELLANEOUS: Ligation probably proceeds through 3 nucleotidyl transfer steps, with 2',3'-cyclic phosphate termini being hydrolyzed to 3'-P termini in a step that precedes 3'-P activation with GMP. In the first nucleotidyl transfer step, RTCB reacts with GTP to form a covalent RTCB-histidine-GMP intermediate with release of PPi; in the second step, the GMP moiety is transferred to the RNA 3'-P; in the third step, the 5'-OH from the opposite RNA strand attacks the activated 3'-P to form a 3',5'-phosphodiester bond and release GMP.
Sequence:
MAKSRYSRKNKGKKLQRAQQNTVSTEEKPEQEVETIDFNGFQIPKVYDGKFERKPMELEIKKGFVEGMNGDAKIFCNDDLLNLLTFEMIKDISNNYPSCVRQTANAATLPGVVGSLAMPDAHSGYGFSIGGVVAMRLDDPEAVICPGGVGFDINCGVRLIRTNLQREDIEQHKARLADELFKQIPSGVGTQAQIAFSPEDFDSIMKEGLEFLVENGYAWEEDLNHCEEHGKIANADPSLVSNSAKSRGYKQVGTLGSGNHYLEVQVVDEIMDVEAAKAMGITEIGQVCIMVHCGSRGLGHQVCQDYINLCMKSGICNPVDKQLTGVPFNSPIGQQYYSAMNCCANFAFANRGMITYRIRQAFETVLRMKPKKMDMHLVYDVCHNIAKVEEHDVDNKKVQCIVHRKGATRAFPPQHPDISEDYKEIGQPAIIGGSMGTCSYVLVGTQEGMKKSFGSTCHGAGRKMSRTKAMDNLTSKDVINRMKEMGIELRITDPKLAAEEADEAYKDVTEVVETCQAANISKIVLRLKPLIVIKG
The following text describes a protein:
Function:
Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac. The NuA4 complex is involved in the DNA damage response and is required for chromosome segregation. The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) through homologous recombination. Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins. In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively.
Subcellular Localization:
Nucleus.
Sequence:
MAPDAGSLNGTTASPALKTPQKPSVTPNVLEVVFGSLLIKPWYPSFYPEQVVGRKLSWDIWAQKACPHRNTPPPGVNVYTKDNYSLYEIDGEKNKMYTQNLCLFAKLFLDTKSVFYDVTTFLYYMLVAHNPTPSIPNTGLGEDGVGQEGQVVGFFSKEKMSWDSNNLACILVFPPWQKQGLAQILMGASYEMSRREGRLGGPEKPLSDLGHLAYEHYWSATLARAILSCPSKKTITVLDLREKTYIVPDDIIATLQAMDVLEHRKKSGAEAVINKAKVRAWAESHRVNLKSLPVDPEAFVLRESSRSVSEE
The following text describes a protein:
Function:
Required for normal Golgi function.
Subcellular Localization:
Golgi apparatus membrane; Peripheral membrane protein.
Sequence:
MAFNQMRSSGSTTDLNRLNSSSISGGGNINISNGGYGNQQLNAILSPIKSSSLSSMSNSSSYSNLNTLSSSKSFNSLTLIENQNDTTTTTSTNNGAISEQYQQLLSMIPKYQTKQYESDVKILFERNTPEQMKQMEFKKRSEIEDMKSQLRNLIGNKYRDLVEGSDAIVKMKKSTELISDNLSLMQSELKQFSEKRNHFRKGVSQDNLKLNKEKEIQKKISIFSKYCKFLIDIPEVIWRSLDSNDYFEVCVFFLKSKYLYSKITNENNLEIKRLLSKLTIIEKQWISMKQFPIKTIGYSKLFLNESTSRIIGTPIEKYIGSLSTLILFEKKSIKETFNEFLLSRRSVLFNSILSKDTNRPIQQTIEKMFQFLKMSIYYIMVLFYPRKYQTNNNNNNDQPEEEEQDDEKLISNDYQSKISKFKSNLQQYTSSLSSMSSTTTTTNSPTFESKMINKPVSEKELNQLPTLNFTSSILESTFNWRSPYLKECLKFYKDVSNGELSINSSGSQQGDDYQDINTNNNNSNNNNSGIDSQDIEYSLIEFDNFNSNFIFKRTSEWIEEIIEDFKLNLVQKFLIDIKSAKELSSLRSEIFDFILDFKNIVPFIQPPQTNSLSSSNSSINSIASPSVSLTSSTSSPIIATTKATVLTTPTPTPTPTPTTPISWNRMFSIICGKDMKYFLNIFEDIFLVKSESIIMDSFSRINLSKIQSDIFSQIKSEDKNFSEFLWFYNQDDPIQSIKNKTNGITPSNELFLTKINQLYNNIKSDFIYLLNDNNINNININNNNNNNNNNNNNNNNNRSMIITSQPKNLIKINEILIKEYMKKSFYKSLNEFTTSTQDRIDQLILLNKNKTTSGTTTSTNLKKDEILFISKLSKIFYKHIVNNPNLYFLNSLNIFDTTNISNCSTSFSKSNSINILDTISSPPQPPPSPTHSSPSIQRHTNNNNNNNNNNNNTSPIINNNNNNSEILKESLPIIDKLKQQFYYGCIVWVNEFVGDYSQILKQDLFNHDWNDSDRIKTWEKHIIQIESNGHNHNNDANDGGGDDDATVNGVNEHSTIIYIPYQTSPFITSYLMSISLEISKFSLNTIDKNILRFIIESITLNLFNIVNDLLSTSSTSTTASTSNLTSNNTTTTIKFNKEGYIQLLIDLKYIGFILFGRELNSSSSKKPTSQPTSNVIIKDSIFKKAKSHYQSIISTKNNVDENIELQKQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQEQLSNNIVYTFNQIIELVEKNLDPIDLAFYNSYIVKFIDQTYSKTLTLFGNFVYLHKSIVKPEKKQSINGGQQSPPLATTSSNGISGGKGIQQQQQQQSDLPNPMQLLKTNTKFQLFSIDTIQTITDAIATAPTTIPSSTSNSIQSSANNSAIASPISTIDYRNQQQQQQNNTNQQSLPSILSPTSASSTINTFSFMGKKISDLMYNTTKK
The following text describes a protein:
Function:
ATP-binding protein, which may act as a adapter in the Toll-like receptor (TLR) signaling.
Subcellular Localization:
Cytoplasm. Cell membrane; Lipid-anchor.
Sequence:
MAESSLYRQRLEVIAEKRRLQEEIRAARREVEEEKLRVERLKRKSLRERWLMDGAAAVPEPSEDPTSKDPQSPEGQAQARIRNLEDSLFTLQSQLQLLQSASTGAQHKPSGRPSWRRQGHRPLSQSIVEAGSVGQTDLNKRASLPAGLVGTPPESPSEPREDVLGFLPGPRQVPGAAGDSSEANGPCPSPIPTPEQGLSQRAVPSEGRVGEAKGGGVVSVVWEGLRATEDCATGATGPELEAKVEEVVLEAIGDRKGAGSLELPAWVKEDRGIVEVVWEGVGGSDAEAMGEIGRVPEVVQTSSPRLQERLEAAASIEGEDVPQGSPEGDGQGGSGGEEGSFIWVERVTLSEEWEELLVEGLEGPEVAGRERGDESPLGAEGAKTGGGEETWEAEKRKAEESMGIGSEEKPGTGRDEAEMSPVVERKGGEKKLELESRGSAEKLGTEREGGEEPLGIERKVEGHLRAEKEGDEEKRGAEEEEVEEPLGVEKKGGEEEPEATKEPLEAERKGGEETLEAEKRGGEESLETEKTQGTEGDLNLEQGSREGSESQAEEMNEAGPPLEANTETRPEKEGPQPQEKPVGALEEEGVKPQTAAEGQGPLGDATPLLAETPAPEQPAECQPLLQGEGPSANPSAHPVPTYAPARQPEPSAPTEGEEASGPKQKTCQCCAVM
The following text describes a protein:
Function:
Glutamate-gated receptor that probably acts as a non-selective cation channel. May be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells; Glutamate-gated receptor that probably acts as non-selective cation channel.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MVSMFILPAMLHAFSSFGWSMAQNSHHRPHHIHVGAILDMESPVGEMAQQCMTMAISDLNASPSHINHPLKLILHPRNSMGQPLKALSSAVELLENEQVDALIGPQTSEEAELLGELGDRVPIISFSASSPLLSREKNPNFIRMTTNDNSQVGAIAALVQKFGWRELVIIHEDSSYGNGIIPDLLLALHEGNARVAHRTVLPPQARDIYVEAQLYKLMALSANIFIVHMSASLASRFFIKVNELGMMSTGYGWIVTDGIVNELPVMDRSVLDSMQGVIGIRPSIPPSERLHNFSMKWRNNFFTNQHHQIPEVNVYCLWAYDSVWALAKAAYHLGPTTSMQKNDSANELAHLAAIHSRRTGSDLVHTILRGKFTGLSGEIQLKNGQLQQPLAFEIVNVIGRVKRIGFWTQWNGMTQGLNRSNVATQSPSLRKMGSIGWPKSSSAVPKGQRVMPKTGKRMRIGVPIKKGYKELVGVELDPETYATIVTGLCIDVFKAAIDLLPYEVKFDFIPFPNSTTGSYYEDLIYHQYDAAVGDITIAANRSSYVDFTMPSTETEVVMIVPIETSRGTNMWIFLQPLTVDLWLVIGASFVFTGCVVWTIEHGDNNEFKGPLAQQIGMVMCNLSKVVVIVWLFVVLILTSSYTANLSSMLTVHQLQSSTKGESIGFTYSAQYTMFETSYNSTNGFGFVFPKGSPLVPDISASIAKLREDGKLHLISQNWFQNPYLFTNQDSATKVARLDLYSFCGRFLITGITSTGAVTVSYRFRKKESTTAQQHEVADPPVEETFSPFNGDKSTRLEPSEDHRLAHPHTDSGGNTTLTITLFAEKLRP
The following text describes a protein:
Function:
Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.
Sequence:
MLKPHSEARAAFIQTQQLHAAMADTFLEHMCCLDTDSPPITAWSTGIICTMGPASPLLEMLKKTIKSGMNVAHLNSHGAHEYHTETIKNVRTATESFASDSILYQPIAVAPDTKGPEIPAGPVKGSGTAEVELKKGNILWRDYKNICKVVEVGCKIYMDDGLISLQVKQKDAHFLVTEVENGGSLGSKMGVNLPGAAVDLPAMLEKDIQDLKFGGEQYVDMMFSSFICKTSDVHEVRKVLGEKGKNSKITSKIENHDGGWRFDEILEASDGIMGARGDPPQAIPAGKVCLAQRMMIGWCSQAGKPMLEDVIKKLHPTWAEGSGVANAVLVEADCIMLSGETAKGNYPLEAVHMQHLIACEAEATIYHLQLFAEFCHLAPITSDPAEATAVGTVEASFKCCSGAIIVLTKSVARYCPRAPMIVVTWNPQAARQAHLYHGIFPVLCFFKKDDVVIVLTW
The following text describes a protein:
Function:
Involved in a cysteine salvage pathway from S-alkylcysteine. Catalyzes the reduction of N-acetyl-S-hydroxy-L-cysteine (N-acetyl-L-cysteine sulfenic acid) to N-acetyl-L-cysteine. This pathway is likely important in the catabolism of alkylated cysteine generated by proteolysis of alkylated glutathione formed in the detoxification of a wide range of electrophiles.
Sequence:
MSDVVNIVVWSKKGCSYCEEVKNYLNEKGFPFQNIDVSEKEKLRDILQVKYGVRHVPVVEIGRGNQYQGITEIGIEHLDLALANHAQIKEAKR
The following text describes a protein:
Function:
Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
Subcellular Localization:
Nucleus.
Sequence:
MAAVNKPNQPRTSKETLLEKRAAVEAAFRKKKESERRALGLVEHMVENSAVDTQWLADKAKFINPQYYQDTIEERAIAKQCGFPVCHNLIEKELKQKYRIDLKTKKVFDVTQRKNFCSDVCFSASNHFKDQLLTSPLWMRHKEKIPRFEINHTPKKSLKGDEFVLIAVAVPDEENNTEEDVEVIKEKTALKPKTLRKIVSEPVVNPCKLVSKIVQQWFTMRTFKWLRNVKEEFIDNGVDSIQEKLLQMNINNPNVKEEGINLPRRQFQPQTEDRHSLKQFRAFLAGKTEYAVEKDDCSIIKDNTGDVIENKEETVSIIIPLANVSAQKNLRKKIVMDYVEKGFPQLTTITGLEFRRYQRDLIQLVSTFSLTADTITFRSHEIPFLCFILITCLATRDSAVKKRLTREPVKTEVSSFLADYERTMEQLEEYVIDLCKPFENSPN
The following text describes a protein:
Function:
Multifunctional dioxygenase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA. 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN. Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A. Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE. Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4. The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide. Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol. Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation. Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional.
Miscellaneous:
MISCELLANEOUS: In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives.
Domain:
Residues at positions 150 and 232 are important for the type of reaction catalyzed, using identical substrate. Both ausE and prhA accept preaustinoid A1 as a substrate to form divergent products through dynamic skeletal rearrangement. AusE (containing 'Leu-150' and 'Ser-232') first desaturates at C1-C2 to form preaustinoid A2, followed by rearrangement leading to the formation of the spiro-lactone in preaustinoid A3. In contrast, prhA (containing 'Val-150' and 'Ala-232') first desaturates at C5-C6 to form berkeleyone B, followed by rearrangement of the A/B-ring to form the cycloheptadiene moiety in berkeleydione.
Sequence:
MGSATPSRLQKFPATAPADEIYAAFKEDGCVIIEGFVPPDQMARFSQEIQPAMEKIQVQVTNDGNSNDRVKRFSKLVTTSPTFRHEILENDLMHELLQRVFSKPGEGMGYHFNDTMVIEVQPGAPAQRLHRDQELYPWWNSMGPDAPECLVNFFCAVTPFTVENGATRLVPGSNRWPELTLINATDCPQYGKIDSVPAIMQPGDCYMMSGKVIHGAGHNATLSDQRRALAFSTIRRELRPVQAFPLWIPMQIATELSPRTQAMFGFRSSTQHCDVDTVHFWGNDGKDIGEHLGLISSA
The following text describes a protein:
Function:
Repressor of jasmonate responses.
Subcellular Localization:
Nucleus.
Domain:
The jas domain is required for interaction with COI1.
Sequence:
MGLTVKQEILEEPATDPAGSTSSAMHWSFSNKAHPQYHLSFKGQENNNNNKPKIGFESLASAGLVTITTTTDIVDTIHRPYSTQIGAHHVPTRNGVVGTTELRSAPRTSPGPAQLTMFYAGSVCVYDNISPEKAQAIMLLAGNAPISTTIRNFPSHDHNNNNTNETTITRSIRVLKSPSNTTEVSKIESRQPPSHNLSAVPQARRASLARFLERRKERVVNASPYGNGKQSSQHMMNFTINSSGSSTPLPATN
The following text describes a protein:
Function:
Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.
Subcellular Localization:
Endoplasmic reticulum lumen.
Sequence:
MKIFQFVIAGLAALSLVSAGDPEQDDVIPPSDVVVLTSDTHDAFIAEHPLTLVEYFAPWCPHCKSLAPEYASAAAELKELDPPISIASVDCTTENVICDKLSIQGFPTLKLFRSGVADDYKGERTAKSIVTTIKKQLLPAVSDVSPESFENFIISEKVVIVGFFDEKSAAERKIFTEIANVQRDSFLFGAADGSKTFKGHKHTTPSIALFKKFDEGLAVLSEDLTSENIKDFISKTSMPIMDEVGPDNYEFYVKRGLPIGFFFYGSAEQREQVGKVIEPVAKEFVGKISFVYLDSAKFGAHAPNLALKEEWPAFGFQDGLRKWPLDQSKPITEEAVRALAKGVLDGSIASTLKSEPVPETQDEPVITVVGDSFDKIVLDTKKDVLLELYAPWCGHCKKLVPTWDTLAKTITSDKIVIAKMDGTTNDIPPSTKVDLQGFPTILLFKAGSSEFMTYQGDRSLASLSAFLKENAVHGSEVPEIDDSAEQDPDLLHEELDLEELEPEVERDEL
The following text describes a protein:
Function:
Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Required for cell surface integrity and cell separation during budding.
Subcellular Localization:
Secreted. Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MDLVIMNFVFLLYLTSVVKCSIKLDFNKVSTPSKYTKRDALPMPLINDKILYTTELEIGSNKDKVSVSIDTGSYDLWVMSNDAVCYKVSEFQTEGAPQLPDIFNDIDQDYSCTFNGTYNSKSSKTFKNTSEDFSIGYVDGSAAQGVWGYDSVQFGQYGVTGLKIGIANRSSVSDGILGIGIANGYDNFPVLLQKQGLINKIAYSVYLNSSNSTTGTILFGAIDHAKYKGALSTVPVDSKSQLSVNVTNLKTKNGNVASGGHSILLDTGSTFSIFPDEWIDALGHSLNATYDEDESVYEIECDGYDEHFFGFSIGDSDFSVPIQDLKTEKDGQCYLAIMSNSVIGGGGILFGDDILRQIYLVYDLQDMTISVAPVVYTEDEDIEEILNPNEDQNEVPTSTSFTQSASSSGSQPSSTISGENMDKNTTSSSSGNCQTRSWIAILSALFLVYIHII