lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in the biosynthesis of the antibiotic pyoluteorin. Catalyzes the dichlorination of the pyrrole ring of pyrrolyl-S-PltL, generating the 5-chloropyrrolyl-S-PltL intermediate and then the 4,5-dichloropyrrolyl-S-PltL product.
Domain:
Contains an additional unique helical region at the C-terminus. This C-terminal region blocks a putative substrate-binding cleft, suggesting that a conformational change involving repositioning of this region is necessary to allow binding of the pyrrolyl-S-PltL substrate for its dichlorination by PltA.
Sequence:
MSDHDYDVVIIGGGPAGSTMASYLAKAGVKCAVFEKELFEREHVGESLVPATTPVLLEIGVMEKIEKANFPKKFGAAWTSADSGPEDKMGFQGLDHDFRSAEILFNERKQEGVDRDFTFHVDRGKFDRILLEHAGSLGAKVFQGVEIADVEFLSPGNVIVNAKLGKRSVEIKAKMVVDASGRNVLLGRRLGLREKDPVFNQFAIHSWFDNFDRKSATQSPDKVDYIFIHFLPMTNTWVWQIPITETITSVGVVTQKQNYTNSDLTYEEFFWEAVKTRENLHDALKASEQVRPFKKEADYSYGMKEVCGDSFVLIGDAARFVDPIFSSGVSVALNSARIASGDIIEAVKNNDFSKSSFTHYEGMIRNGIKNWYEFITLYYRLNILFTAFVQDPRYRLDILQLLQGDVYSGKRLEVLDKMREIIAAVESDPEHLWHKYLGDMQVPTAKPAF
The following text describes a protein:
Function:
Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
Subcellular Localization:
Nucleus.
Sequence:
MKHPYHIVSLSPDGKTMYAAAARQVDRICLETGECKSTVVEESATRTTTKTGDKPAAAKRTKYLPTSVSHVRSLQLSKGGKYLLATTDETKSLVLLDPTTLEVIKKVQYPKRPSAVATDKEDLNIVLGDKFGDVYGESVEDLLKVEGELKDEPVLGHVSMLTALELGYDSKDRPYVISADRDEHIRISRFPASHVIEQFCFGHQQFVSSLLINDLDASILFSAGGDDEIFVWDWLNGKQLQKLSLREHVESYLNEAHIYVDKKGVATTHKEITVSSLQQIKDTPYLLVNVESTNAIIVLKIVDNKLEVASVFATEAHVISFSVAGNLLVTSEVGSEGVKAYTITDGVVTKSDKEIPFGSCEYEDDSELISLFSTKSLRKRGEF
The following text describes a protein:
Function:
Regulatory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as a vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain VTC4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation (Probable). The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen (Probable). PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase (Probable). VTC5 interacts with the VTC complex to increase the rate of polyP production.
Miscellaneous:
MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein. Note=Localized to the vacuole membrane by the AP-3 complex. Membrane localization is required for VTC5 to promote VTC activity.
Sequence:
MKFEDRILNKSIPEWKFYNINYEKLKVAIKKVTAYDYDNPNDSGMEKLLNQCSVAFDQEFQNVNLFVSLKIKEISTRILSVESSIIDFSKGLNKTSRNRFNLRKLKIINAHVDDCNFELQLLSRFLIIQRIALRKLFKKLLNEFPQDSENPLTASEYVTSIRNSESLRNGHEGISFMKLDLDPYLLEVSLIVDVLHDLENKLEDATEPAVEQRSLNRSDESAHTSSSPEANNSSLPASPRSIPLLSNKKTSKMIDSSLEFDTALIDKAENLGRFLLSSEDIEGLKFMLLNIGFRIIDDSIISTSKEILDTTDNINSAGNKSIRSAKSFNDLQHTLSLSKQKNILPSAVQSNEKYVSISILDTVGNEGSPLLLTDDNINQHPNMIVSSTAEDTCIVMCHVGGLRNHVVTNDLLLRDVKNILSAMRSGNDTKNISALINSLDPSPISKIALEWIQSHRLKTIEPKLDFKRTRFISADNGDIYLIALDESITIGNVSTLPFPILEIKKLSRSSGLSQTAINEDNKFKQLMKSVVTNEFQCSLIPPDLTTWKICLELVHSNELQNDLFQLLLRDQYKLNSDDSLSPDEFFQLGKDRLEEEFDLTGPINNSQGSVDSGRRVRIHKKSKQSDNETKKKPIRYWNEFDEQEEDNLDNAFYIDTNGSRSTTDNEESLLLRNSPPDYGFILFSRNFINRTYDFCEKLRNLIRHDKKTSPDLFQNSKHPHCSSTNYGSVASFGSQSTSASYDDVQRYLQYQQQDIEDSQSIYEYRHDEVVTFLYLSALLTSCIMASVCLGIVLSLFRGQSNNEIDLEIQNILIAIIIISLLVSLILICACLLLLFSRFTLAPIWHYVGCFTMFFSVTGTVCYGMIEIFF
The following text describes a protein:
Function:
Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MTELRQRVGREQPQEGEDKLPYDPQDQDQDQDQDQEQGEAESEVKTDGETASDSESKTDTGGTQQGTPTDDTPEVLNRALANLSSRWKNWWVRGILTLAMISFFFIIIYLGPIVLMMIVMCVQIKCFQEIIMIGYNVYHSYDLPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFALYLTGFCMFVLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLIIHNLFEGMIWFIVPISCVICNDIMAYMFGFFFGRTPLIKLSPKKTWEGFIGGFFSTVVFGLLLSYVMAGYSYFVCPVEFNNETNRFTVDCEPSELFQLQEYHIPAMFHSVISWKTVWMYPFQIHSIALSTFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVNVYIASFIRGPNPSKLIQQFLTLRPDQQIHIFNTLKSHLTENGILANDNGV
The following text describes a protein:
Function:
Pyridoxal 5'-phosphate (PLP)-binding protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5'-phosphate (PLP), the active form of vitamin B6.
Sequence:
MSLEIVQRNLLNILEAVADAVTISSATKRCRLVAVSKTKSAEMIESCFSQGQRHFGENYVQELEEKSAALASKCAEIRWHFIGQVQSNKISKICNSSGIWCVETVESEKHARLFDKEWSKHGASSSPLRVLVQVNTSEEENKGGIKISEAPKLAEFIRKECLNLKFDGFMTIGSHASGVNPDFEKLYTVRQAWSEITGETPESVELSMGMSDDFLQAIQQGSTSVRVGSKLFGAREKKMDDFRSQILKKTRELMLNEQQHEENMKSWNGNETKGFELQFAGMKRGVPQKSGVVGQVFISEDGGFEAIITGYLVKDNLRSISTSFTLTPSSSLKSEITEGLHPLVLAVGSALTLNHVLMLNNVRDEILKLLTPKEVARVASVCKIARAVLTSTAVDNTFWKKHLRADFGAEKVQNTIANGRKFHGVYCEEARARRNQRAAQPHNDNPYLIGVHQPRIDPLRVDPLRVPDRNPMRPIHPDPDAEWFNPQGGFLPPGMPPGNPQVPDLFRGPDHPDLNPLAGGFGLPRGGGSQGRPFMRGPPGSGGSGGGGFL
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular Localization:
Mitochondrion.
Sequence:
MSLSAPTRILRKPTLSRQFSTSLPVLASRGSSKPEGLGARSRPWSVQNVPKFAFDDATSLGWMRMFRIQEGEGLVRKIEEDREALRTANQTKFTPPTAPIRLTSTIDLARPDSRYHTKCVLLVPIAALPLSTPEAVHRFKLLAGPRWTPGKPGRNEFIKDENSDGENGWIKVSEERFESARQNRRSASDILERLVNAANDRESPLPADLPIDTRHLLARHRKKRSRQNTFKWAPGQEFLSRHQEVGGVRGFPVSWLPEELRERVSKK
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MPGEQQTEEEEEEEEMQEEMVLLVKGEEDEGEEKYEVVKLKIPMDNKEVRKLRPRKLEFGDWLKVPSEAPAPPADPARPHACPDCGRAFARRSTLAKHARTHTGERPFACTECGRRFSQKSALTKHGRTHTGERPYECPECDKRFSAASNLRQHRRRHTGEKPYACAHCGRRFAQSSNYAQHLRVHTGEKPYACPDCGRAFGGSSCLARHRRTHTGERPYACADCGTRFAQSSALAKHRRVHTGEKPHRCAVCGRGFGHRSNLAEHARTHTGERPYPCAECGRRFRLSSHFIRHRRAHMRRRLYICAGCGRDFKLPPGATAATATERCPECEGS
The following text describes a protein:
Function:
Involved in the biogenesis of the 60S ribosomal subunit.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MKVIVSADDTGSAKEVICNEGTDTSKQNATQPISIDNCLLEPSSSVKSRIIHFLSFNYQYLIGARLGGQVSVYELSDEESEEKFKLLHNFELPVDAQDKPVALLRVEILDSILVAFESSKVFLIHINDSFDFKPLELVLPEYKPISAFAINPQAENIVALGGKEHDLQILQLFNKNINSTVFKKNNYENEFKPQIIFKAKNVRNDHLELRVPIWITNILFAKAAKGYKLVTSTRYGQIRLYDTAEGRKPRKDYKVTEKPIVTLTFANDEQTEIIVTDTHSLIAKYSLTQVDEKAFKTISASAGEIVKPVPKLLGKFTGGNTGATFGVHAYERIVAFAGLDRYLRVFDLESREILAKVYLGVEVSALLILDDEDTEDEETKKRKRKEEEDDEELWNQLDTKKKTHTI
The following text describes a protein:
Function:
Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication. This subunit is a candidate for the mediation of ATP-dependent binding of ORC to origins. May also be a substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-ORC5).
Miscellaneous:
MISCELLANEOUS: Present with 768 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MNVTTPEVAFREYQTNCLASYISADPDITPSNLILQGYSGTGKTYTLKKYFNANPNLHAVWLEPVELVSWKPLLQAIARTVQYKLKTLYPNIPTTDYDPLQVEEPFLLVKTLHNIFVQYESLQEKTCLFLILDGFDSLQDLDAALFNKYIKLNELLPKDSKINIKFIYTMLETSFLQRYSTHCIPTVMFPRYNVDEVSTILVMSRCGELMEDSCLRKRIIEEQITDCTDDQFQNVAANFIHLIVQAFHSYTGNDIFALNDLIDFKWPKYVSRITKENIFEPLALYKSAIKLFLSTDDNLSENGQGESAITTNRDDLENSQTYDLSIISKYLLIASYICSYLEPRYDASIFSRKTRIIQGRAAYGRRKKKEVNPRYLQPSLFAIERLLAIFQAIFPIQGKAESGSLSALREESLMKANIEVFQNLSELHTLKLIATTMNKNIDYLSPKVRWKVNVPWEIIKEISESVHFNISDYFSDIHE
The following text describes a protein:
Function:
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in gut granule biogenesis.
Sequence:
MTGVDDISSNVHKLVGVTAGMNTAASTGPMNLVLDKCSVVLEELRTIQILTETHSEGLSEQLKMTEKNILEMENLFDQIDQLCLFVQKAKSDLDKLEKLYNVVDRQ
The following text describes a protein:
Function:
Importin beta subunit that functions in nuclear protein import through association with the importin alpha subunit, which binds to the classical nuclear localization signal (cNLS) in cargo substrates. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by importin beta through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, GTP-Ran binds to importin beta and the three components separate, leading to release of the cargo. Importin alpha and beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin beta. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates the nuclear import of histones H2A and H2B. Mediates the nuclear import of transcription factor GCN4.
Miscellaneous:
MISCELLANEOUS: Binds to nucleoporin FxFG but not GLFG repeat regions. Ran-GTP can disrupt the importin alpha/beta heterodimer by binding to the beta subunit and releases both subunits from the docking site; MISCELLANEOUS: The stoichiometric complex between importin beta and Ran-GTP renders the latter inaccessible to Ran-specific GTPase activating protein (Ran-GAP) thereby inhibiting GTP hydrolysis stimulated by Ran-GAP; MISCELLANEOUS: Present with 51700 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus. Nucleus, nuclear pore complex.
Sequence:
MSTAEFAQLLENSILSPDQNIRLTSETQLKKLSNDNFLQFAGLSSQVLIDENTKLEGRILAALTLKNELVSKDSVKTQQFAQRWITQVSPEAKNQIKTNALTALVSIEPRIANAAAQLIAAIADIELPHGAWPELMKIMVDNTGAEQPENVKRASLLALGYMCESADPQSQALVSSSNNILIAIVQGAQSTETSKAVRLAALNALADSLIFIKNNMEREGERNYLMQVVCEATQAEDIEVQAAAFGCLCKIMSLYYTFMKPYMEQALYALTIATMKSPNDKVASMTVEFWSTICEEEIDIAYELAQFPQSPLQSYNFALSSIKDVVPNLLNLLTRQNEDPEDDDWNVSMSAGACLQLFAQNCGNHILEPVLEFVEQNITADNWRNREAAVMAFGSIMDGPDKVQRTYYVHQALPSILNLMNDQSLQVKETTAWCIGRIADSVAESIDPQQHLPGVVQACLIGLQDHPKVATNCSWTIINLVEQLAEATPSPIYNFYPALVDGLIGAANRIDNEFNARASAFSALTTMVEYATDTVAETSASISTFVMDKLGQTMSVDENQLTLEDAQSLQELQSNILTVLAAVIRKSPSSVEPVADMLMGLFFRLLEKKDSAFIEDDVFYAISALAASLGKGFEKYLETFSPYLLKALNQVDSPVSITAVGFIADISNSLEEDFRRYSDAMMNVLAQMISNPNARRELKPAVLSVFGDIASNIGADFIPYLNDIMALCVAAQNTKPENGTLEALDYQIKVLEAVLDAYVGIVAGLHDKPEALFPYVGTIFQFIAQVAEDPQLYSEDATSRAAVGLIGDIAAMFPDGSIKQFYGQDWVIDYIKRTRSGQLFSQATKDTARWAREQQKRQLSL
The following text describes a protein:
Function:
Guanine nucleotide exchange factor (GEF) for Ral-A. Potential effector of GTPase HRas and Ras-related protein M-Ras. Negatively regulates Elk-1-dependent gene induction downstream of HRas and MEKK1.
Domain:
The Ras-associating domain plays a central role in the activation of Ral-A GDP/GTP exchange activity.
Sequence:
MERTAGKELALAPLQDWGEETEDGAVYSVSLRRQRSQRSTPERSGEGQTPIPATDTFLHYRTSKVRALRAARLERLVHELVSGDREQDPGFVPAFLATHRAFVPTARVLGFLLPPPPPPPPPPAGVDSKRTEGQDLNFSKNLRAVVSVLGSWLRNHPQDFRDPPDHQNLGNVRIFLGWAAPGGAEAREAEKLLEDFLKEAKGEQTEEEKRLAWSGPPRIAQTPGSEFAEDCVEEEGPSSEGPELLDFSVDDVAEQLTLMDVELFLRVRSCECLGSMWSQRDRPGAAGISPTVRATVAQFNTVTGCVLGSVLAAPGLAASQRAQRIEKWIRIAQRCRELRNFSSLRAILSALQSNPIYRLKRSWGAVSREPLSVFRKLSQIFSDEDNHLSSRAILSQEETTEDDDCPSGSLPSKLPPGPVPYLGTFLTDLVMLDTALPDTLKGNLINFEKRRKEWEILARIQQLQQRCQRYSLSPRPPILAALRAQRQLSEEQSYRVSRVIEPPAASCPSSPRIRRRISLTKRLSAKLSREKNSSPGGSPGDPSSPTSSVSPGSPPSSPRNREPPPPGSPPASPGPQSPSTKLSLTMDPPGPWPVTLTPSSSRVPLLGQQTSEARVIRVSINNNHGNLYRSILLTCQDKAPSVVQRALEKHNVPQPWARDYQLFQVLPGDRELLIPDGANVFYAMSPAAPGDFLLRRKEGTGHTLSASPT
The following text describes a protein:
Function:
Serine/threonine-protein kinase which phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (eIF2alpha), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis (By similarity). Involved in the unfolded protein response (UPR) triggered by several stresses including mitochondrial, osmotic and oxidative stresses, amino acid deprivation and UV irradiation, probably by phosphorylating and inhibiting eIF2alpha. In addition, leads to the selective translation/transcription of some mRNA including atf-5, pha-4 and gpdh-1 which are part of the UPR. Required for maintaining lifespan during amino acid starvation. Involved in hypoxia-mediated adaptive protective response.
Domain:
The protein kinase domain 1 is predicted to be catalytically inactive.
Sequence:
MTKENQIVLDERVKENQHLQEEEKLALDAVYLNQITYIKAHWHVWVPTNCHILLKALDSCFLNGDPLGKSKLSVILHVKCSEDYPQRKPAVDLLDPQGLSKEDVQNLLTILRQMADTWEGCVVIAELAHRVREFLTDHTPRPAGSFHDDMLANKVRTEAEKQRKRLDTEQKELELLEEEMRQRNAIEMEKTLNGTRQENETRIIGGRRIVVLSNMPNTQLLISEWTFRFSSNRNPAEGKRKDFAPFLQKLDAVYNEIQKLCEIKGLDQNLVEYAFVHLQKISVSPDQILIQLNVAQKIFSSEENMQDTYELIVQKSNLLRLLAAQAICGLRYLHEASMTHKHLTLGSVWTRNSTGDCVFRFSDFGSMGPLLDLVKMFGDICSGKYVARDEDKEKEYDRRRKDLFQLGTLLDGLILATRGSTYSRVPTPVEGNQNTGTNLLGNFIAKCQEAKNIDQLVEDPFLKEECQSESENIFTPFGGAMSPDGRMLADNVIIRVLGRGGFGDVVLVRNKMDSTDYAIKRIPLNAKSDKLNRKIAKEAKFFAKLNHPNMVRYYYAWAEDLIPIVEETSDDDSSLGAVPIPGKEKIGKKGKLKTGKSLEDKENKANLGGGDSLMPMNLRGLVKDHSIGVDAKEWSTPFGKPEGPKCASRMRQSKRSTPSGGLKHLSECSSDDEDDDDSSEIDWDAESEEVEDEESDDSDEEDEDDGERLVQLNTETSTGADSVFERSTADEDVVFTAESEDLNAKRRESIELMEINTTTTSKSKLAIDVVPVRKPRILCIQMEYCDRATLRQYIDENHCFNAPTEVWRIFSEVLCGLKYMHDMAMIHRDIKPLNIFLTSQNGVKIGDFGLATLEAMSSKGKIVGGAAEKSTSIEAMLSPNGVKSKGSDVHQTRDIGTQLYMAPELFVDELVHKAPYTSKIDIYSAGVVLFEMFYRPLPPSMDRVSTLNNLRDDIKIPSDFGAGLAAPMAGLARRTVEKMLQRNPDERPTADDLLNDEDLPMHTKEDATFRNLCEKVIKKRDGRMNAWLLDKQFKEEVPTSLNYCYDVDICLERAKYNNREVLVETLRAEFCKILKIHSFEKLHTHTLMPVSTALAAASVRTKPVEVLDRSGVPVALPMDLRQNFVRFCVRNSVQRMKRFNFGRVYSQTSANGHPHERWECCVDCIGPQCSSPSLEAELLLVACEMMIGSLPGMKFTLKIGHAQLIEAQIRHLKLSDDVRAELLDALHLISVSDRPHSHKEKMDMLTPKIGAKAANIITKLLIPVEDNFGAFKEKVACFRKKLKVDAARVLVDKAIRDLEEIVGTFKFCRTEAIEQISIVYDSQTCYRPRTFGDGLLFQIQVEKPSTIANNKRGRRQNVLAGGRYDSALLRERHPRDFVYEIPLCISGFGVAMDVVSQIRDSINKSANIPKTPQNHCKVLICSMVQPDGSNLITQKFELAKKLWSMGIEADVFHIPVDDLESLTEHRNRASITHILAVYNTLNEVICKTETSSETMDVDSAISSVWRGVQALDGQSIHMTPCGGGPISSISTPGEAHHHDDHHPGTPVIASKCFRSSVSTTVATTSIRPISATVANLNVILVTSADRFHKVMKEKKRVESQVRNHLTEFVAHFTSKTRIEVLVCDIPADVIKKIVSELTKTSSEAEIDKLFDQLIQKHGKVDLSPLRRQFHITLNGISTGSAQVAILFYRQSDNFYRYLV
The following text describes a protein:
Function:
Phosphodiesterase (PDE) that catalyzes the hydrolysis of 3'3'-cyclic GMP-AMP (3'3'-cGAMP), leading to linear 5'-pApG. Counteracts the function of the 3'3'-cGAMP synthase DncV, and is involved in the modulation of intracellular 3'3'-cGAMP levels. Enhances bacterial chemotaxis and inhibits intestinal colonization in vivo. Thus exerts a crucial role in regulating bacterial infectivity through catalyzing 3'3'-cGAMP degradation. Is specific for 3'3'-cGAMP since it cannot degrade other cGAMP linkage isomers (3'2'-, 2'3'-, and 2'2'-cGAMPs). Is also able to hydrolyze c-di-GMP but not c-di-AMP.
Sequence:
MKWFKYGDGMDLFADMRQEAAGEKERVVMHSQEPWCVLLVDDDEQMHQITRLALTGFKFQNRPLELISVLSGLEARKVMAERSDIALALVDVVMETEHAGLDLVRYIREELQNRQVRLVLRTGQAGQAPEDRVIKEYEIDDYKEKTELTTQKLRTLLYSMLRAYRDLCLIEDQKLGLSHVIEASANVQNTKSLQSYATAVLNQLTSLLKLHASAFYCVATPCPDSEKCNALTVATTAERVELYVESPFKGLPEDVQRRCKEVLSQRTTRDYGDAYVFFKQDERGVDSVLYVGFEQELSELDRKLLEIYMYNIGLTFENINLMVDLRETSKELVYNLANAVEARSRETGAHVQRVALYCERLAHLYGLAESEADMIKNASPLHDVGKVAIPDSILHKPGKLDAQEWAIMQKHVEYGVEILNRSKRRLMQVAKEIAATHHEKWDGSGYPNRLQGDDIPISGRITAIADVFDALGAKRSYKDPWTDEQIREELMAQKGRHFEPKLVELLLEHWDEFIAIRASLPD
The following text describes a protein:
Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion outer membrane.
Sequence:
MVGLTQVMENEAFMAFASYATIILSKMMFMSTATAFCRLTRKVFANPEDCAGFGKGENAKKYLRTDDRVERVRRAHLNDLENIVPFLGIGLLYSLSGPDLSTAILHFRIFVGARIYHTIAYLTPLPQPNRALAFFVGYGVTLSMAYRLLTGRLYL
The following text describes a protein:
Function:
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Sequence:
MEITLFDPIDAHLHVRENALLKAVLGYSSEPFSAAVIMPNLSKPLIDTPTTLEYEEEILNHSSNFKPLMSLYFNDGLTLEELQCAKEKGVRFLKLYPKGMTTNAQNGTSDLLGEKTLEVLENAQKLGFILCIHAEQTGFCLDKEFLCHSVLETFALSFPKLKIIIEHLSDWRSIALIEKHDNLYATLTLHHISMTLDDLLGGSLNPHCFCKPLIKTKKDQERLLSLALKAHPKISFGSDSAPHFISKKHSANIPAGIFSAPILLPALCELFEKHNALENLQAFISDNAKTIYGLENLPSKKARLSKKPFMIPTHTLCLNEKIAILRGGETLSWNLQEIA
The following text describes a protein:
Function:
Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates mRNA stability. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing.
Subcellular Localization:
Cytoplasm.
Sequence:
MTSHVPKHPREPTEDMVKNLKVDPLAKVAASTTSTKNQSEPYYETLETYQGLPCPYGGYYGFYYPSVDGSLGEAKDNGYYGYGTDVQYPVMQGENGSLIYMMPGFQSYDVSPTYMPISPAGVSSQALNSPMYAAQGYYQNQYGYGNVSSPTYLWDPVGENYVYGVASNNQSMKQNISSSSSHNYSNYYSKSKTSFTGHGMGGRPRTPQKSSYAPLPPHNQERGGPLKKKYGASNRDETEKLKARNKENGSSVSENVQEDGECESCLLDGEGKGRSNGVGYVIKRDQYNLPSFQTKYEEAMFFVIKSYSEDDIHKSIKYNVWSSTLNGNKKLDSAYQESQKKVAEKGGTCPVFLFFSVNASGQFCGVAEMTGRVDYEKSMEFWQQDKWTGYFPVKWHIIKDVPNPQLRHVILENNENKPVTNSRDTQEVRLPQGNEVLNIFKNYAAKTSILDDFDFYENRERVMVQKKLRFNPVSKKQEDDLVADMQTMEISDTVKEENTDIIGTLDSLK
The following text describes a protein:
Function:
Functions as actin-binding 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. Seems to contact the mother actin filament.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MSATLQPYLKAVRNTLTAAICVENFSSQVVERHNKPEVEVRTSKELLLTPVVISRNEKEKVLIEGSINSLRISIAVKQADEIEKILCKKFMRFMMMRADNFVILRRKPIEGYDVSFLITNFHTEQMYKHKLVDFVINFMEEIDKEISEMKLALNSRARISAEEFLKRF
The following text describes a protein:
Function:
Neurotoxin that produces dose-dependent hypolocomotion and hyperalgesia in mice. May directly act on the central nervous system, as it is 6500-fold more potent when administered intracerebroventricularly than intraperitoneal.
Sequence:
SCPQCREAIQHKQFRPNRQLANVANLVKKLQKKKDLEARMGMCEKHQGLLTLFCKDDGAPICIVCKKFLHRNHNVVPVEEAVQSYKEEFKVFLERLKKEKETLKRLKSLEELRRQEFRKMLELEYKKARVAFDKMRQYLEENQRLWMVHLEEMVKETEKRSDENVTKLSEGIAQVCRLTSEIEERFEQPENKFLQLSMQGHERSLSQLDIWASPATSLQSSNSLIPEARNTQRWFCQFLSLKSMSVTLDPDTAHPYLNLSEDQKVVTWESKKKKREYLKKTMPNNSERFSWETCALGCQKFTSGIHWWVVETLGPGSWTIGIARESMKRKGVLQLSPQEGVWSLRKPFRGAAYFACEILAVVLPEPIVLTLAQEPTKILVALDYEGGRVDFFDGDTNAFIFSFRIESLSGEAIRPFFELREWGFSLQCLS
The following text describes a protein:
Function:
ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Subcellular Localization:
Nucleus, nucleolus.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MAKIDKKTKLKLNKKSVRAPSKPTTEKKPKKYVTADTLTWKPVKTSSFSGIDGGGGMMMLEELEDVGIEWEETDGGRKIAKFVEVESKTSKGKKNAAQEEPNQEGRGDDEKASSASETEEGKKADDKEAVEEDDEEEFPDFAGFAEEDLNAADEEEHPNLDDEPAFNDDLLPEWSSISLHPSLKRSFLASSFTAPTAIQSRAIPAGITGRDVVGVAETGSGKTLAYSLPILHYLLGQRKSKAGIKRPLSALVLCPTRELALQVMDHLNALLKHALATPDGEKPQGPPRVSVGSVVGGLSAQKQKRILERGCDVIVATPGRLWDLIKADDELATSVRTLRFLVIDEADRMIENGHFAELESIVKLTQRSTAQQGPDDDDPVFQAMATLFEESTAREDMQTFVFSATLSKDLQKNLKRRSRSWKGKGKRSSTLEDLVEKLDFRDENPEVIDLSPEGGVVSSLRESMIESTKDDKDLYLYYFLLRYPGRSIVFVNSIDSIRRLLPLFTLLQLPVFPLHSHLQQKQRLKNLDRFKSNPKGILIATDVAARGLDIPQVDHVVHFNLPRTADAYIHRSGRTARAQNEGFALQLVSPDEKSVQRALMKSLERTHELPDLPIEAGFLPSLRERLRVATEIEKAQHRATKATHDKNWLLEAAEAMDIDIDPSMLDGEDDDPDAPYYKPKKQDRGKGKASVENLKMELKALLQEKLVARGVSIRYPTSGSKVIVDDLIKSTGHGMLLGASTSKAYDQVEKTGKRKLGSGRPGAVKKKKVEGR
The following text describes a protein:
Function:
Choline transporter.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MIVPSSDWNLFRSLVGLVDCISCVINISNLQDTLLVLETSREMAVLLLLQNMVYYFMFGGLWKQAFLLALNQFIIGCSVCIWYFNQGPGQSYTGNLFQSIYWAFRYHLGSLAFGSFILAVVQFIRLMLEYAKYQTKQMSGDNKCTKCILDCLSCLVACFERFIEFLNKNAYIQIALTSKSFCPAAKDAFESIWANTMRYSLVSGIGSIFTFIGKLFVGFATVLFSYEIFINVEPYKTDLASPIVPSIVCFIIAYMVAILFMSIYQMACDAVLTCFIYDEELNKQNGGMSAQHCPETLREWFDGTQSS
The following text describes a protein:
Function:
Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis.
Subcellular Localization:
Chromosome, centromere. Nucleus.
Sequence:
MAGSAWLLCSAAEMQSVCGESTVDLEQTNPEVSCRKLNGSSGGPEACVVFLCKNCYTVLGDSLSVCGEERSLAAIACLRVTEDLNVGESVLFVVNGNLKGCAYYPLLCRSCGTNIGFNLYSAPRAYAYLRGLFCLLKEHILCYKLKSSALVPGNEMQFEFPSLEEDVAELKMQLVQLHVKMELISKQLLQQEKNTTACS
The following text describes a protein:
Function:
Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule (By similarity).
Sequence:
MVELKIACKLDGSCEKPRYRKYKCKVCGWVYDPLKGDPSQNIPPKTPFEELPDTWICPVCRGKVGKESFEPLDEWVEFDE
The following text describes a protein:
Function:
Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Can play two different roles depending on the source of dihydrofolate: de novo synthesis of tetrahydrofolate or recycling of the dihydrofolate released as one of the end products of the TS catalyzed reaction. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.
Sequence:
MIAASVGCRPLVHLVGAGLDSCYLLMLNLSRCVECVRVGGSSVARIRSLQIRRDCQARACVRVQARRWRTGTAVESKSRTFSTDRTAARIQLLLSSSSCLFSEAVACRSSVVDSLPLWSGGVACSRTWSNLFLKSRHPWKAQSTTGIAYFANKSEEDQAMETVEAPTRSFQIVLAVSRNWGLGVNGDLPWHLPLDLKHFTKVTTETRSSSKRNAVVMGRKSWDALPKKYRPLKRRFNVVLSRTSKQVDDDSGSTVVCESVHSALTLLATPQYASEIETVFIIGGGQILRETMSASLCDAIHLTEVDAEVECDTFSPPVDRSIFTPWYASAPIVENNLRYSFVTYVRRGGSLTKVDVQQNVNVATSGAKQETGVASKADERIKDFVSLLPPSLAHRHEEYQYLDLIKDIIQNGTVKGDRTGTGTISKFGCQMRFNLRKCFPLLTTKRVHWRGVVEELLWFISGSTSAKVLQDKDVHIWDGNSTKEYLSSIGLTEREEGDLGPVYGFQWRHFGAKYTDMHADYTGQGFDQLADVIHKIRTNPNDRRIILSAWNPADLQLMALPPCHMFAQFYVANGELSCQMYQRSCDMGLGVPYNIASYSLLTYMIAHVCDLVPGDFVHVLGDAHVYTNHLEPLKEQLKNDPKPFPVLKIKSSKRDIDSFTADDFELIDYKPNRRIFMKMAI
The following text describes a protein:
Function:
Required for the proteolytic cleavage of the transcription factor RIM101 in response to alkaline ambient pH.
Sequence:
MPTPCLEQFLHHLEKSHLYLSIDNTKQAKKECLESIKILNSIAKTTPLPEIKVLSQYTLNHYESLDKPRTISDKLEWISSKLTQETFFPPVIQFNENFTSHNELFVDTISPIQDNDNKIFEKLPNKLAKFEYIEISNWDNDITHLKNLYQDILPNCSFVSSFLAIIDANIPIIDTITPQKSSQKYKVSLRFNGALRNVIVDSKFPIMPNSRNLIIKSYSDTELYWPALIEKAYLTIMGNGYNFSGSNMANDAYVLSGWLPQIIKLSNGQLPSNIDDLWRLRTQGKVTMGIGTGTLSKQLSSQLHLVSGHDYVIDNIKDGVITVKNPWLDPKDRVVEIKNFNHFKYLYVNWKPDHKPYQHYFLYQAKPNTYNQPQFTIKCMEETWILLERHLSETSSSPSPHWMDMNVFETEYKIITPSQYKKYLSVETNNRLQLIKLKPGVFTIVISSNKPCRFTLSSFNAMFSKSKYKYDYTETVNGEWNSDINGGNWAMSTYINNPQYDIIAKQTTELIMGMHGQGQINFHLFHSSSDSMGERIQNFDKTKLINYQNYNASYQSSSYRLTPGHYKLVVSEYYRSIGTYQLVLNSSEPITITKIPPFLGLYNISKSFNWDNTNRFKLKFETTGYNSKVKIKIAYFNGESDFELQTSYRPAMRASLFNSQTKQPIQINEQFNDSLYGVFLHEILPSPEEYILLIERFEIGYGRCVVEIGCNNKVILK
The following text describes a protein:
Function:
The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAGTGYDRQLTIFSPEGRLYQVEYALKATKCESLTTVGVCSDEAACIITQKKLPDRLVDPSTVTHLHRISKHVGCCMSGIYADGKVIAQRSQYYASKFQLDYGYEMPVSLVAKKTADFAQMLTQHAYMRPFGVSSMFIGWDEVSGPQLWRSDPAGSVAAFRGCAAGEKEQEAFNNLEKKKITKELTVDQVVCQALDCLQTVTSSEFKATDIEIAIVTKDNKLFHLLSQQEIEHYLVLASEKD