lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (ManNAcGlc-2,3-diNAcAGlcNAc in M.voltae) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (Probable). Involved in the assembly of an N-linked disaccharide that decorates the S-layer glycoprotein and flagellins.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.
Sequence:
MTENNEKVKNSDSANNQSSKNSKFNFNFEDKKVKCAKTILIIIFLAFLSFQMRAQTADMGFTTNEQYLDVFSDDNGRMYLTALDPYYYLRMSENYLENGHTGDTLKNIDGQQVPWDSYKYGPTGARATFNLLSVVTVWVYQVWHAMDSTVTLMNAAFWVPAILSMFLITPIFFTVRRITSSDIGGAVAAILASLSPSIFVKTVAGFSDTPILEILPLLFIVWFIIEAIHYSKEKNYKSLIYGLLATLMLALYPFMWSAWWYGYYIVIAFLVIYAIYKGISYNSIAKYTKSKNNNHKDKIESEKLEMLNILKISGLFIIGGAVLITALYGVSTTMNALQAPLNYLGLDEVSSQTGWPNVLTTVSELDTASLDEIISSSLGSIHLFAIGLIGIFLSLFRKVLTPVKQISNGLAEKLDIKYALLLIIWFAVTFLAASKGVRFVALMVPPLSIGVGIFVGFIEQFIKNNLDKKYEYVAYPTIAIIVLYALFTIYRADSADLVRMLLPSNYVPIAEGIMLASLAVLIIYKVAELIAESNKKLVMNKIFMILLAIGLITPTIATIVPFYSVPTYNDGWGESLEWINTQTPNNSVVTCWWDNGHIYTWKTDRMVTFDGSSQNTPRAYWVGRAFSTSNESLANGIFRMLASSGDKAYTTDSVLIKKTGSIKNTVDVLNEILPLTKSDAQKALKNSSYKFTDTEVSEILDATHPKVTNPDYLITYNRMTSIASVWSYFGNWDFNLPAGTSRSEREAGSFQGLQTYATNINDTLIVRSLIQQTAEYNIYTLIEVRNETLTGAMMAVTNDGQMQTQQLNMHKVKLMVNENGKSKMYNSLADPDGQLSLLIKVDKNSIIGTDGSNNPVYSSSSWMATANLEDSVYSKLHFFDGEGLDTIKLEKESLDPTANGVQPGFKVFSVDYGNYSK
The following text describes a protein:
Function:
Extracellular signaling peptide that may regulate primary root growth rate and systemic nitrogen (N)-demand signaling.
Subcellular Localization:
[C-terminally encoded peptide 16]: Secreted, extracellular space, apoplast. Note=Accumulates in xylem sap.
Sequence:
MVMAKNLTKFYVVFLVVLMMVVSLLLAIEGRPVKDSSRSLTQMRDSSMFNGSVIMSSFKPVESSVKDLSWLATVKQSGPSPGVGHHRAKGYKMFGRANDSGPSPGVGH
The following text describes a protein:
Function:
Acts as a transcriptional repressor. Corepressor for REST. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Also interacts with MXD1-MAX heterodimers to repress transcription by tethering SIN3A to DNA. Acts cooperatively with OGT to repress transcription in parallel with histone deacetylation. Involved in the control of the circadian rhythms. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation. Cooperates with FOXK1 to regulate cell cycle progression probably by repressing cell cycle inhibitor genes expression. Required for cortical neuron differentiation and callosal axon elongation.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MRTEDAAFSSFLAFRWASLTPSKKQILGPSLVLDYVLRMKRRLDEPEAAAYPPQPRRIAESFAHTHRVLAPAPPTYEPPPDAMQPTAGIQYSVAPGYQVSTVPQSSGGHGQASLTAVHSSHHHSSPVPSHGGPAVQSHAHSNPPAAPAPAQGQQFQRLKVEDALSYLDQVKLQFGNQPQVYNDFLDIMKEFKSQSIDTPGVISRVSQLFKGHPELIMGFNTFLPPGYKIEVQTNDLVNVTTPGQVHQISTHGLQPPVPPAPPPSQPPTAQPITPPVHPTPPPPPPKISKPLQSQAHTPTNQQSTPIQYPSPRSPPAQPHTPGPLAHAAPTATAATPTMQNNQPVEFNHAINYVNKIKNRFQGQPDIYKSFLEILHTYQKEQRNAKEAGGNYTPALTEQEVYAQVARLFKNQEDLLSEFGQFLPDANSSVLLSKTTAEKVESVRNDHGGTVKKPQLNNKQQRPNQNGCQIRRHSGTGVTPPVKKKPKILIPKDQSLADANKHGAGAESQFFDKVRKALRSAEAYDNFLRCLVIFNQEVISRSELVQLVSPFLAKFPELFTWFKNFLGYKESSHMESFPKERATEGIAMEIDYASCKRLGSSYRALPKSFQQPKCTGRTPLCKEVLNDTWVSFPSWSEDSTFVSSKKTQYEEHIYRCEDERFELDVVLETNLATIRVLETVQKKLSRLSAEDQAKFRLDNTLGGTSEVIHRKALQRIYADKAADIIDGLKKNPAVAVPIVLKRLKMKEEEWREAQRGFNKIWREQNEKYYLKSLDHQGINYKQIDTKVLRSKSLLNEIESIYDERQEQVSEDNSGISSGPHLTLTYDDKQILDDAASLIIHHVKRQTGIQKEDKYKIKQIVYHFIPDLLFSQRGELSDVEEEEEEETAEAEDGVTKKHNGVGVGGGSSPPKAKLMFGNTAAQKWRGMEDAYNLFYVNNNWYIFLRLHQILCSRLLRIYNQAEKQVEEEMREREWEREVLGLKRDKNDSPAIQLRLKEPMDIEAEDYYPAFLDMVRNLLDGNMDSNQYEDSLREMFTIHAFTTFTMDKLIQSIVRQLQHIVSDEICVQVTELYLSESNTNATGGLLSTQASRNLNEANYQRKAEQLMSDENCFKLMFSQSRGQVQLTIELLDTEEENSDDPAETERWSDYIERYMNCDSTSPEVREHLAQKPVFLPRNLRRIRKCQRGREQQEKDGSGKRALENLESLDKLQCKFKLNSYKMVYVIKSEDYMYRRTALLRAQQSHERVSKRLHQRFQSWLRKWNVEHVSHEMASESRKWLMGEGVEGMVPCTTSRDSEILNFVDINKYRVKYGAAFKTP
The following text describes a protein:
Function:
Key component of the ribosome quality control system (RQC), a ribosome-associated complex that mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes and their subsequent degradation. RqcH recruits Ala-charged tRNA, and with RqcP directs the elongation of stalled nascent chains on 50S ribosomal subunits, leading to non-templated C-terminal alanine extensions (Ala tail). The Ala tail promotes nascent chain degradation. May add between 1 and at least 8 Ala residues. Binds to stalled 50S ribosomal subunits.
Sequence:
MPFDGLLLHKAVRELKELEGEHLRQIYQPTTVDYYFLFRSATVRVCLRPDVSHVAIAEKEEASEKMPSSFTMLLRKELKGAKLLKVEQIGMDRTLRFSFEKFDEIEGIVQKDLYIEIMGIHSNMILVRDRRIIDAHRRIVTKKREILPGREFVIFPSGKVSIFELRELPPESEKTIRNVLLSLLEGFSPVSVEELIHRTGYELDTPWKAVDQRKILEVLEEIKKELELPGVFVYYEASHPVEVSAFRFTMLSLKERYFEKPSEGINEFVRWKEEKSTFENTKNRFIKVVVNRIEDLEDLEEKLSRELSEAEKAERYKKLGDLIVQNLWSIKGKSGEVELTDWETNEKIVVDVGKDPAQTAQKFYNTYKKLQRKKEQVEKRLEEIQREKEYLYQLWQTIEDAEDLETLEEIEEEMREFGLLKERKTKKQKSKKTRFREVYYGGFKILIGRNNKQNDELVRTSSKEDLWFHAHEMPGAHVVVKTEGKKVPQEVVEYAASLAAGYSKGKNSGKVPVDYTFIKYVRKPKGFKPGMVIYKNYKTILVEPRRIEG
The following text describes a protein:
Function:
Transcription regulator that plays a critical role in virulence by positively regulating the expression of multiple quorum sensing (QS)-regulated virulence factors, genes involved in protein secretion, translation, response to oxidative stress and the phnAB operon. At the stationary phase, negatively autoregulates its function through cleavage and translocation to the extracellular space.
Subcellular Localization:
Cell inner membrane. Secreted. Note=At stationary phase, gets cleaved and subsequently released in the extracellular space where its transcriptional activity is inhibited.
Sequence:
MPIHNLNHVNMFLQVIASGSISSAARILRKSHTAVSSAVSNLEIDLCVELVRRDGYKVEPTEQALRLIPYMRSLLNYQQLIGDIAFNLNKGPRNLRVLLDTAIPPSFCDTVSSVLLDDFNMVSLIRTSPADSLATIKQDNAEIDIAITIDEELKISRFNQCVLGYTKAFVVAHPQHPLCNASLHSIASLANYRQISLGSRSGQHSNLLRPVSDKVLFVENFDDMLRLVEAGVGWGIAPHYFVEERLRNGTLAVLSELYEPGGIDTKVYCYYNTALESERSFLRFLESARQRLRELGRQRFDDAPAWQPSIVETAQRRSGPKALAYRQRAAPE
The following text describes a protein:
Function:
Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.
Subcellular Localization:
Cytoplasm.
Sequence:
MNTAEELLDVLVVGAGLSGLALAWKLKRAGCTFLVCQAGERVGGAITTAIADGFVCEGGPNSFQESPPLIELLTQLQLEDQIVTADPRLARFVWWENRLRSVPLTPAQLVRSDLLSWSGKARLLWELFVPALGEPREETVAEFVLRRFGEEVLSRLVDPLVSGMCAGDVGQLSIEATFERLVDLERRHGGVLRGLWRTARTRPPFKRLCTLRGGLEQLPQALAQRLQPQILLSHRLEALEHLAGDRWRAVVAGPQGEPVAIAARTVILSGSAHAMASVLRPLDAGLGRALESIYYPPVVSISLAYSKSQVPNAPEGFGHLIPRNQTLRSLGVIWNSSLFPHTAPPNWRLYTCFVGGTTDPATPNLSDTELASLAHRELQTVLGFQAGYQLLRVTRWPQAIPQYALGHPSKQERVERALLGLPGLFLVGNYFGGISLGDCVRHSGAVASRVLQFLTTVASNGSLRPA
The following text describes a protein:
Function:
Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MSNYPTEPNPNSKISAFGTVNCQTISGLPILQLRDTVKTNNGPQFDIVDEAIYHFRTNIFMRDFPAKTGADRLIIYLTFYGMKCLKFIAKNKTNKQKCQLELDGWNLKPFPIPGEGGFIIDSYVTAPANNEKTQLREYFKKLRIEMGNRLLARIFAQGNEADKWWICFANKKFLDKEMAN
The following text describes a protein:
Function:
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
LPKELSLDRKCEACCEITLKRIVYSGFGGLLASLVLFRSPSSRWSAMAFSLGLGAGSAYTDCS
The following text describes a protein:
Function:
Acts as a transcriptional activator that mediates the calcium- and neuron-selective induction of BDNF exon III transcription. Binds to the consensus calcium-response element CaRE1 5'-CTATTTCGAG-3' sequence.
Subcellular Localization:
Nucleus.
Domain:
The N-terminus is necessary for DNA-binding. The C-terminus is necessary for transcriptional activation.
Sequence:
MEQSNDSLRVNHNDGEESKTSAQVFEHLICMDSRDSSFGQNDSPTVLPITTREANNSLISQNIPGPLTQTQTLSAEQFHLVDQNGQAIQYELQSLGESNAQMMIVASPTENGQVLRVIPPTQTGMAQVIIPQGQLVDVNSPRDVPEEKPSNRNLPTVRVDTLADNTSNYILHPQTSFPLPKKSVTGMLEEPLLGPLQPLSSNTPIWACRLRSCEKIGDSYRGYCVSETELESVLTFHKQQTQSVWGTRQSPSPAKPATRLMWKSQYVPYDGIPFVNAGSRAVVMECQYGPRRKGFQLKKVSEQESRSCQLYKATCPARIYIKKVQKFPEYRVPTDPKIDKKIIRMEQEKAFNMLKKNLVDAGGVLRWYVQLPTQQAHQYHELETPCLTLSPSPFPVSSLEEEETAVRDENCALPSRLHPQVAHKIQELVSQGIEQVYAVRKQLRKFVERELFKPDEVPERHNLSFFPTVNDIKNHIHEVQKSLRNGDTVYNSEIIPATLQWTTDSGNILKETMTVTFAEGNSPGESITTKVETNQTRGSLSPEPTHLLSSLSSFQPKIFTQLQGLQLQPRYTSPDESPAVVSVNNQPSSSPSGLLDTIGSAVMNNNSLLLGQSHSLQRDTCLTQNNSTASTMGNLPEPDQNLVAMDELVEVGDVEDTGNLEGTVHRILLGDVQTIPIQIIDNHSALIEENPESTISVSQVKQEPKEPALSMEAKKTVDYKKLSAT
The following text describes a protein:
Function:
Catalyzes the irreversible NAD(P)-dependent non-phosphorylating oxidation of glyceraldehyde-3-phosphate (GAP) to 3-phosphoglycerate (3PG). It is highly specific for D-GAP.
Miscellaneous:
MISCELLANEOUS: GapN is also able to utilize NADP as a cosubstrate but with remarkably different kinetic properties. In contrast to the NAD-dependent reaction, the NADP-dependent reaction does not follow classical Michaelis-Menten kinetics. The saturation kinetics of the NADP-dependent reaction shows an unexpectedly bumpy curve with several more or less pronounced intermediate plateaus, which can be explained by the assumption that the catalytic or binding constants first decrease, then increase with saturation. The first saturation phase is characterized by negative cooperativity. The later saturation phases display sigmoidal shapes indicating positive cooperativity. The negative cooperativity of the first saturation phase could also explain the strong inhibition of NADP on the NAD-dependent reaction if it is assumed that NADP excludes NAD more efficiently from the vacant cosubstrate-binding site than NADP itself.
Sequence:
MRAGLLEGVIKEKGGVPVYPSYLAGEWGGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLFKRGRWSARDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGERVVKVGGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPTYVQPTLVEAPADRVKDMVLYKREVFAPVASAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIVFNYKGKGVWKYE
The following text describes a protein:
Function:
Adapter protein that plays a role in regulating cell-surface expression of adrenergic receptors and probably also other G protein-coupled receptors. Plays a role in NEDD4-mediated ubiquitination and endocytosis af activated ADRB2 and subsequent ADRB2 degradation. May recruit NEDD4 to ADRB2. Alternatively, may function as adapter protein that does not play a major role in recruiting NEDD4 to ADRB2, but rather plays a role in a targeting ADRB2 to endosomes.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Early endosome. Lysosome.
Sequence:
MVLGKVKSLTISFDCLNDSNVPVYSSGDTVSGRVNLEVTGEIRVKSLKIHARGHAKVRWTESRNAGSNTAYTQNYTEEVEYFNHKDILIGHERDDDNSEEGFHTIHSGRHEYAFSFELPQTPLATSFEGRHGSVRYWVKAELHRPWLLPVKLKKEFTVFEHIDINTPSLLSPQAGTKEKTLCCWFCTSGPISLSAKIERKGYTPGESIQIFAEIENCSSRMVVPKAAIYQTQAFYAKGKMKEVKQLVANLRGESLSSGKTETWNGKLLKIPPVSPSILDCSIIRVEYSLMVYVDIPGAMDLFLNLPLVIGTIPLHPFGSRTSSVSSQCSMNMNWLSLSLPERPEAPPSYAEVVTEEQRRNNLAPVSACDDFERALQGPLFAYIQEFRFLPPPLYSEIDPNPDQSADDRPSCPSR
The following text describes a protein:
Function:
Catalyzes the transfer of an acyl group from acyl-ACP to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme can utilize either acyl-CoA or acyl-ACP as the fatty acyl donor.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein; Cytoplasmic side.
Domain:
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence:
MSGWPRIYYKLLNLPLSILVKSKSIPADPAPELGLDTSRPIMYVLPYNSKADLLTLRAQCLAHDLPDPLEPLEIDGTLLPRYVFIHGGPRVFTYYTPKEESIKLFHDYLDLHRSNPNLDVQMVPVSVMFGRAPGREKGEVNPPLRMLNGVQKFFAVLWLGRDSFVRFSPSVSLRRMADEHGTDKTIAQKLARVARMHFARQRLAAVGPRLPARQDLFNKLLASRAIAKAVEDEARSKKISHEKAQQNAIALMEEIAANFSYEMIRLTDRILGFTWNRLYQGINVHNAERVRQLAHDGHELVYVPCHRSHMDYLLLSYVLYHQGLVPPHIAAGINLNFWPAGPIFRRLGAFFIRRTFKGNKLYSTVFREYLGELFSRGYSVEYFVEGGRSRTGRLLDPKTGTLSMTIQAMLRGGTRPITLIPIYIGYEHVMEVGTYAKELRGATKEKESLPQMLRGLSKLRNLGQGYVNFGEPMPLMTYLNQHVPDWRESIDPIEAVRPAWLTPTVNNIAADLMVRINNAGAANAMNLCCTALLASRQRSLTREQLTEQLNCYLDLMRNVPYSTDSTVPSASASELIDHALQMNKFEVEKDTIGDIIILPREQAVLMTYYRNNIAHMLVLPSLMAAIVTQHRHISRDVLMEHVNVLYPMLKAELFLRWDRDELPDVIDALANEMQRQGLITLQDDELHINPAHSRTLQLLAAGARETLQRYAITFWLLSANPSINRGTLEKESRTVAQRLSVLHGINAPEFFDKAVFSSLVLTLRDEGYISDSGDAEPAETMKVYQLLAELITSDVRLTIESATQGEG
The following text describes a protein:
Function:
Repressor of the treBC operon. It is able to bind trehalose-6-phosphate.
Sequence:
MQNRLTIKDIARLSGVGKSTVSRVLNNESGVSERTRERVEAVMNQHGFSPSRSARAMRGQSDKVVAIIVTRLDSLSENLAVQTMLPAFYEQGYDPIMMESQFSPTLVMEHLGMLRRRNIDGVVLFGFTGITEELIAPWKASLVLLARDAQGFASVCYDDEGAIHILMQRLYEQGHRNISFLGVPHSDITTGKRRHDAYLAFCKKHKLHPVAALPGLAMKQGYEHTASVIMPDTTALVCATDTLALGASKYLQEQRIETLQLASVGNTPLIKFLHPEIVTVDPGYAEAGRQAASQLIEQINGRCDPRRIVIPSTLA
The following text describes a protein:
Function:
Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit.
Subcellular Localization:
Cytoplasm. Nucleus, nucleoplasm. Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner.
Sequence:
MDMDSGSMGVAFQPSEPIASTILCCECGVPTPPNAAAMCMDCIKMTTDITSGIPRESTVNHCRECERYMQPPNNWMIAPLESRELMAICLKKLRGLNQVRLVDANFIWTEPHSRRIKVKLTVQKEAFTNTILQQSFQVEFYVNNTQCPDCARTYTPHIWKAVCQVRQKVLHKRTFLYLEQIILKHKAHMNTVNIKETKDGIDFYFGQRAHAIKMVEFLSAVVPIRYKGSEELISEDFKSNTANYKFTYSIEIVPICKDDLVCLPKTVAKAHGNIAQLVVCTKVGPTIRFLDPLTLQTCDMLPSIYWRTPFPALADIPELTEFIVADVDLLGPTNGKYALADVELIKSSDGSTHLTRTHLGGILNAGNTVLAYHLAVTNFNNEVYDTLREDSIPEVVIVKKTYPQTKKKNRNWRLKTIGMQKAEDVKKQDIERQERDYELFLQNLEEDPELRQGVNLYKAPVKAIAVADTDMDEEDEVDEDIPQISVDELLDDVEAMHI
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that methylates the delta-nitrogen atom of arginine residues to form N5-methylarginine (type IV) in target proteins. Monomethylates ribosomal protein L12.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MADNDSISVRISEDCPPEIQRMLTAAWAHDVDTVKKLIDTPEVARGQDPKTGESPLHAAIRSCGAPSEDDTPEDHEKAKATVSELLMWGAIWNDVDNNNETPGCVAARLNRPELYELCVNAGVRAEMLFGLMDGYEALDSDDEDDEEMAEGEEAQAEDGEEAPELVAAEEATQTAEEETPAVFQPPAVNLEEQVTSDKYLRSTVAYSDGKLVDDAGNGVMMAWETDIMRRSVDALLPNKEPGKRILNIGFGMGIIDGMFAETKPAVHHIIEAHPEVLEYISTPESKFDSTWEESGPAPGAYRVWEGKWQQIGLQLLEEGHVYDAIYFDTFGEDYGQLRMFFTEYIPGLLDSNGIFGFFNGLGADRQICYDVYTKVAEMHLADAGLDVEWKEIPVDMKELAEADKDGWEGVKRRYWTLDTYRLPVCTFLG
The following text describes a protein:
Function:
Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U16 and U17 in cytoplasmic tRNAs. Also able to mediate dihydrouridylation of some mRNAs, thereby affecting their translation (By similarity).
Sequence:
MTEPALSSANNALMQKLTGRQLFDKIGRPTRIVAPMVDQSELAWRILSRRYGATLAYTPMLHAKLFATSKKYREDNWSSLDGSSVDRPLVVQFCANDPEYLLAAAKLVEDKCDAVDLNLGCPQGIAKKGHYGSFLMEEWDLIHNLINTLHKNLKVPVTAKIRIFDDCEKSLNYAKMVLDAGAQFLTVHGRVREQKGQKTGLANWETIKYLRDNLPKETVFFANGNILYPEDISRCMEHIGADAVMSAEGNLYNPGVFNVGQTKNKEKIFPRVDKIIREYFQIVKECQESKASKTAMKSHFFKILRPFLPHHTDIRSTLATMNAKATWEEWEEQVVKPVEKVVQEIFEQPDIAIKDEITIGEKQSWGGSYRTVPYWRCQPYFRPVNGITGDKRVMQGLIDESVNKKRKADVPLESADKKKDVKA
The following text describes a protein:
Function:
May play a role in the organization of actin filament arrays within muscle cells.
Subcellular Localization:
Cytoplasm, myofibril, sarcomere, Z line.
Sequence:
MPQTVVLPGPAPWGFRLSGGIDFNQPLVITRITPGSKAAAANLCPGDVILAIDGFGTESMTHADAQDRIKAAAHQLCLKVDRAETHLWSPQVSEDGKAHPFKINLESEPQEFKPIGTAHNRRAQPFVAAANIDDKRQVVSASYNSPIGLYSTSNIQDALHGQLRGLIPSSPQNEPTASVPPESDVYRMLHDNRNEPTQPRQSGSFRVLQGMVDDGSDDRPAGTRSVRAPVTKVHGGSGGAQRMPLCDKCGSGIVGAVVKARDKYRHPECFVCADCNLNLKQKGYFFIEGELYCETHARARTKPPEGYDTVTLYPKA
The following text describes a protein:
Function:
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP42 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation.
Miscellaneous:
MISCELLANEOUS: Present with 7110 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus.
Sequence:
MSLSVAEKSYLYDSLASTPSIRPDGRLPHQFRPIEIFTDFLPSSNGSSRIIASDGSECIVSIKSKVVDHHVENELLQVDVDIAGQRDDALVVETITSLLNKVLKSGSGVDSSKLQLTKKYSFKIFVDVLVISSHSHPVSLISFAIYSALNSTYLPKLISAFDDLEVEELPTFHDYDMVKLDINPPLVFILAVVGNNMLLDPAANESEVANNGLIISWSNGKITSPIRSVALNDSNVKSFKPHLLKQGLAMVEKYAPDVVRSLENL
The following text describes a protein:
Function:
Probably involved in transport through the plasma membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MSNNPPQPQYQPIYGQQGGQPSYPQPPQPPYAQQYGQQPSYPQPQQPPYAQQYGQQYGQQPSYPQPPQPPQYQQPTYNQQASYQQPNMPPPSQPYQQSQQYGATQQNYSSSGIASTDGLVPKKDGRFRKDSPYKDVWATIAFLICLAGFIAVSAFGVTKLDLKNTSSGVSTSNVRNRATTGNTSSNRTATPIEIYIPAADIGGILVSNVAVGLVLSLAYFLLMQRFAGKMIYASGILSIMFTLALAVVFAYFRMYIPAVLYVVFAALFAWMFYSWRHRIPFAKLMLKTVTKITAKYPATLIVGIFGVIFSAAFSVLWVVGLVGITNFLNAEKTSPGLSYFMMVFSLFVFYWTNQVIQNTVHITISGLFATYYFMGVADSQGNVTVNIKNPTAAAAKRALTTSFGPNCYGSLLVAIIQTLRAIVRMASENNDNPAIAIILCCIQCLLSCIQGMAEYFNKYAFTQVAIYGKDYCTAAKDTWELIKSRGIDAIINDDLIGNVLNVGAFFVGLVTGVVGFTYIQLSPTIPHYTANYIVIVFVSFFIGIVEFSVLSSVIDSGVATTFVCLAEDPSALARTKPDLYHKIAEVYPQALIQF
The following text describes a protein:
Function:
Involved in the recognition of invading microorganisms. Binds specifically to beta-1,3-glucan and activates the phenoloxidase cascade (By similarity).
Subcellular Localization:
Secreted.
Sequence:
RCARVCAVLFLFIQISYGQYQVPQVTVQALKPRGFKASIPDSPSVSLFVFQGNINRAISKSDIGTISGEILKAKDGRWTFEDPNVELKVGDVVNYYVVVVSNRGGYIKDNLSFTVSALEDPSSTGTGTDPVPTPTTCRPTATKLRSGVACAGQTIFEENFNTFREDVWQIEQYIPVYSTEFPFVSYQHLSQDPTVAVTGGNLRITPKLQQRMPGFTDSSIYSGSLNIFSGCTAPAEACMKDAWGASILPPVVSGRITSKAFAFTYGTVFVKAKLPQGDWIYPEILLEPFLKKYGSTHYSSGVIKIASARGNRELTSGYTDYSNKMLFGGPVMNLQCYDTLLESKASSNGRQWGDDFHEYVLRWAPERITLSVDGVEWARVEPTASGLSGRFPQTCSKLPRTFLAAGTKMAPFDDHFYLTLGVAAGSITEFPDGVQTSGSRPKPWTNTGSKAMLHFWEDMDSWFATWNQPQLLVDYVKVVAL
The following text describes a protein:
Function:
Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain.
Sequence:
MEDIVIAGMSGRLPESNNLQEFWDNLIQGVDMVTEDDRRWKPGLYGLPRRNGKLKELDKFDAAFFGVHPKQAHTMDPQLRLLLEICYEAIVDAGINPNELRGTNTGVWVGVSGSEAGEAFSRDPEELLGYSMTGCQRAMFANRISYFFNFKGPSLSIDTACSSSLLALENAYKAIQHGQCNAAIVAGVNVLLKPNTSVQFMKLGMLSPDGACKSFDASGNGYCRSEAAVAVLVTKKSLAKRLYSTILNAGSNTDGFKEQGVTFPSGAVQQELLISLYKEAGIQPSQVEYLEAHGTGTKVGDPQEVNGIVGVLCDSTREPLLLGSTKSNMGHPEPASGLAALAKVILSLEHGVWAPNLHYKTPNPDIPALQEGLVQVVTEPTPVKGGIVGINSFGFGGSNVHIILKPNEKKPSGVASVEVPRLVLACGRTEKAVETIIQQSREPTADNTFVNLLNDISGIPPSSMPHRGYTLVKTDSDIKEIQQAQVSGRPLWYICSGMGTQWKGMGHSLMKLDIFHQSILRSDEALKGTGLKVSELLLNADDKTFEDTLHAFVGLAAIQIAQIDMLKAMKLEPDGIVGHSVGELACGYADNSLSHSEAILAAYWRGRCIKEAHLPPGGMAAVGLTWAECKIQCPEGVVPACHNSEDTVTISGPKDSVREFVADLKSKGVFAKEVQSAGVAFHSYYMEAIAPSLLSALKKIITPKPRSSRWISTSIPESQWNSDLAKFSSADYHVNNLVSPVLFQEGLQIIPENAVVVEIAPHALLQAVLRRSLKPTNTILPLMKKGHSNNLEFFLTNIGKVYMNGINVEANNIFPRVEYPAPAGTSLISPLIMWDHSQTWDVPKAEDFPAGSGGSTSTTVYNIDMNPDSPDIFMNGHCIDGRVLYPATGYLVLAWRTLARSLGVVMEQTPVIFEDVTIHRATILPKTGIIQLEVRLMPASKRFEVSENGNLTASGKISVMEENVLNNFQNQLMDSLDKDEDIDSELPLSDKDIYKELRLRGYDYGPSFQGIIESNSRGDKGKLLWNGNWVTFTDTMLQMMVLGLKGRSLRLPTRILSVGIDPTVQKDHVFLHKGDREAVHVAVNSCLDRIVAGGVQILGLHATTAPRRQQQQTPPILEKFVFSPYFEEECLSDNNYLHYQLQQCSGKIHELESKVAQHGLKLEIPELKAPEPTKGVPKADALNKGLLHVLSEICNLELNGNLQSDLELMLIKEKDQLRNDPLLNGLLDSPQLKTCLDIVLENGNPQQMKIVEALAENGRLFSYVPALLNTQPMLQLDYIATDSASEVLSSLEENLKEFGGSVEQWDPMGTAPSTLTNADLLVCNNSLHHLRNPQQAFINMTATVKEGGFILLHTLLKGDMLGETIKFLNTQNAQQKEGLLSQTEWKEVFDSASLNLVAMKKSFYNSIIFLCRRQVPEQTPLFLSVEDMTCPWVKSVQEAMADSGERTIWLTSEHQTNSGIVGMVNCLRQEPGGKRIRCTFNADAETNTLSEKEKQQRLKSDLVMNVYRDGKWGCFRHIPFQKDGIQDETAFAFVNILTRGDLSSLSWVASPLQHFQPSSPSVQLCKVYYASLNFRDIMLATGKLPPDAIPGDLALQQCMLGMEFSGRDPAGRRVMGLLPAKGLATVVDADKHFLWDVPESWSLEEAASVPVVYATAYYALVVRGRIRKGESVLIHSGSGGVGQAAIAIVLSMGCQVFITVGSSQKREYLQNRFPKLDANCFANSRDTSFEQHILNRTGGKGVDLILNSLAEEKLQASLRCLARHGRFLEIGKYDLSNNSPLGMALFLKNVSFHGILLDALFEDQNKEWEDVSALLKEGIKEGVVKPLKCTVFERDDVEPAFRFMAQGKHIGKVLIKVRDEEVEQQYGSDMLQISAIPRTSFPSTKSYIITGGLGGFGLELAQWLIERGAKNLVLTSRSGIRNGYQAKQIQTWKGMGIKVLVSSKDVGSVEETVLLIEEAGQLGPVGGIFNLAMVLKDAMIENLTTQLFQDVNKPKYDGTLNLDRVSREKCPELDHFVAFSSVSCGRGNAGQSNYGFANSTMERICEKRRQDNLPGLAVQWGAIGDVGVVLETMGSNDTVIGGTLPQRIGSCMDVLDQFLNQPHPVMSSFVLAEKTLSVKSKGSSQQDLVEAVAHILGVRDINSLNPDTSLADLGLDSLMGVEVRQTLERDYDIVMAMREVRQLTINKLRELSSKPSNMEDAKTTQKSSVPPELSILDLTNLLVNPDASTTTKLNNVESAERPLFLVHPIEGSIAAFHSLASKLTIPCYGLQCTRAAPLDSIYSLASYYNQCIKQIQPEGPYLIAGYSFGACVAFEMCSQLQAQREVSQAPDSLFLFDGSHSYVAAYTQSYRAKLTPGSEAEAETEALCAFIQQFTGMEYNKLVEALLPLKDLETRVIAAVNLIIQSHKDISQEALQFAASSFFYKLKAADQYIPKNKYMGNVTLLRAKTRTEYGEGLGIDYKLSEVCDGKVSVHVIEGDHRTFLEGTGVDSIIGIIHSSLAEPRVGVREG