lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the phosphorylation of thymidine monophosphate (dTMP) to thymidine diphosphate (dTDP), the immediate precursor for the DNA building block dTTP, with ATP as the preferred phosphoryl donor in the presence of Mg(2+).
Sequence:
MAGRRGALIVLEGVDRAGKSTQSRRLVEALGAKGHRAELLRFPERTTKIGQLISSYLEKKNNLEDHTVHLLFSANRWEQVPLIKEKLNQGITLVVDRYAFSGVAFTGAKENFSLEWCKQPDVGLPKPDVILFLQLNTSEAAKRGDFGSERYENSSFQEKVLQCYYDLMEDKTLNWKVIDASKTIEDLHNEIKSIVEEAMQEAQHKPIGELWK
The following text describes a protein:
Function:
Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase. Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme.
Subcellular Localization:
Mitochondrion.
Domain:
Forms an alpha-helical dimer with monomers associated via an antiparallel alpha-helical coiled coil, leaving each N-terminal inhibitory region accessible for interaction with an F1 catalytic domain. The inhibitory N-terminal region binds the alpha(ADP-bound)-beta(ADP-bound) (ATP5F1A-ATP5F1B) interface of F1-ATPase, and also contact the central gamma subunit (ATP5F1C). This dimeric state is favored by pH values below 7.0, and at higher values the dimers associate to form inactive homotetramer, where the inhibitory region is occluded, masking its inhibitory activity.
Sequence:
MAVSAVSSRVWLGMWGVRALQTRGFGSERSEDPGSAGSIREAGGAFGKREQAEEERYFRARTREQLAALKKHHEDEISHHIKEIERLQKEIERHKKKIKNLKSDDD
The following text describes a protein:
Function:
ATP-dependent 3'-5' DNA helicase able to unwind duplex DNA or DNA:RNA heteroduplex. Unwinds G-quadruplex DNA; unwinding occurs in the 3'-5' direction, requires a 3' single-stranded end of at least 7 nucleotides. Helicase activity is higher on G-quadruplex substrates than on duplex DNA substrates. Assayed with a catalytic fragment (residues 400-1268). Telomeres and rDNA are notably G-rich; formation of G-quadruplex DNA would block DNA replication and transcription. Acts as an integral component of the S-phase checkpoint response, which arrests cells due to DNA damage or blocked fork progression during DNA replication. Can create a deleterious topological substrate that TOP3 preferentially resolves. The TOP3-SGS1 protein complex may function as a eukaryotic reverse gyrase introducing positive supercoils into extrachromosomal ribosomal DNA rings. Together with topoisomerase II has a role in chromosomal segregation. Maintains rDNA structure where it has a role in re-starting stalled replication forks.
Subcellular Localization:
Nucleus, nucleolus. Note=Localizes to S-phase-specific nuclear foci.
Sequence:
MVTKPSHNLRREHKWLKETATLQEDKDFVFQAIQKHIANKRPKTNSPPTTPSKDECGPGTTNFITSIPASGPTNTATKQHEVMQTLSNDTEWLSYTATSNQYADVPMVDIPASTSVVSNPRTPNGSKTHNFNTFRPHMASSLVENDSSRNLGSRNNNKSVIDNSSIGKQLENDIKLEVIRLQGSLIMALKEQSKLLLQKCSIIESTSLSEDAKRLQLSRDIRPQLSNMSIRIDSLEKEIIKAKKDGMSKDQSKGRSQVSSQDDNIISSILPSPLEYNTSSRNSNLTSTTATTVTKALAITGAKQNITNNTGKNSNNDSNNDDLIQVLDDEDDIDCDPPVILKEGAPHSPAFPHLHMTSEEQDELTRRRNMRSREPVNYRIPDRDDPFDYVMGKSLRDDYPDVEREEDELTMEAEDDAHSSYMTTRDEEKEENELLNQSDFDFVVNDDLDPTQDTDYHDNMDVSANIQESSQEGDTRSTITLSQNKNVQVILSSPTAQSVPSNGQNQIGVEHIDLLEDDLEKDAILDDSMSFSFGRQHMPMSHSDLELIDSEKENEDFEEDNNNNGIEYLSDSDLERFDEERENRTQVADIQELDNDLKIITERKLTGDNEHPPPSWSPKIKREKSSVSQKDEEDDFDDDFSLSDIVSKSNLSSKTNGPTYPWSDEVLYRLHEVFKLPGFRPNQLEAVNATLQGKDVFVLMPTGGGKSLCYQLPAVVKSGKTHGTTIVISPLISLMQDQVEHLLNKNIKASMFSSRGTAEQRRQTFNLFINGLLDLVYISPEMISASEQCKRAISRLYADGKLARIVVDEAHCVSNWGHDFRPDYKELKFFKREYPDIPMIALTATASEQVRMDIIHNLELKEPVFLKQSFNRTNLYYEVNKKTKNTIFEICDAVKSRFKNQTGIIYCHSKKSCEQTSAQMQRNGIKCAYYHAGMEPDERLSVQKAWQADEIQVICATVAFGMGIDKPDVRFVYHFTVPRTLEGYYQETGRAGRDGNYSYCITYFSFRDIRTMQTMIQKDKNLDRENKEKHLNKLQQVMAYCDNVTDCRRKLVLSYFNEDFDSKLCHKNCDNCRNSANVINEERDVTEPAKKIVKLVESIQNERVTIIYCQDVFKGSRSSKIVQANHDTLEEHGIGKSMQKSEIERIFFHLITIRVLQEYSIMNNSGFASSYVKVGPNAKKLLTGKMEIKMQFTISAPNSRPSTSSSFQANEDNIPVIAQKSTTIGGNVAANPPRFISAKEHLRSYTYGGSTMGSSHPITLKNTSDLRSTQELNNLRMTYERLRELSLNLGNRMVPPVGNFMPDSILKKMAAILPMNDSAFATLGTVEDKYRRRFKYFKATIADLSKKRSSEDHEKYDTILNDEFVNRAAASSNGIAQSTGTKSKFFGANLNEAKENEQIINQIRQSQLPKNTTSSKSGTRSISKSSKKSANGRRGFRNYRGHYRGRK
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. 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.
Sequence:
MPDVTLTIDGVQVTVPAGTNIVDAARQAGIAIPVFCYHPRLKPVGMCRMCLVQVGTPKVDPATRQPVVDANGQPVIAMMPKLQTACTTPVSPGMVVKTTTEEVKFAQRGILEFLLTSHPLDCPVCDKGGECPLQNLTMGWGPAVSRFDYNDKVHFEKPVKLGDLIYLDRERCILCGRCVRFQDEIADDPVLGFDNRGRNWMIISKSDPPFNSKFSGNTTDICPVGALTSSDFRFKARVWELQSKPVVCTLCPVGCNLSLDMRHDRLMRVMPRENVAVNDIWICDKGRYGHRFIESPDRLTTPLVRRNGTLVPVSWDEALEFVADQLTIIRARHGGQALAGLAGPQLSNEDLYLFQKLLRELGSENIDTGIGGPTALPPDEIGGWLAPGPATDLSQLGAGTMVLVVGADPEEEAPLYMLRLRGIAQRGGKLVVAGLRPTKLERSASRVVRYAPEGELAFAQGLLKAALAQGAHSPLLERLPGWDKVRSMLDRVSLGDLAAACNLTGDELTQLAKDFLSAGQSLIVYGWEARSAGSALTEMLAALMLLSGRAGTANNGIIALLPGGNSRGAIEMGVRPDAGPGYTPRKQRGLDATGIWNAAQEGKVRAIWLAGVDPAAKLPAARAALEAAEFVVVQDLFLTASAEFADVVLPAASVAEREGTYTNAERRVQRSRQACAPVGEARPDWQIVAAVAQALAMVPIGGGRNGPIPVTTESWSYIVAADVAAEIAAQVPGYTGVTHAALAATGTGGTWGRQFDDAFYYDGTSYTNTEGVGLVLPALVGKGQLHLTFTGAVTRFADDRPLLLLEQVLAYDGDRHLRGSKLQSLIPPGYAAISSVDAAKLNIHSGDRVRLISAAGELVIPARVLADLPAGIVLLPAGLADVMAADIETGPRTRVSLAKVVME
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Sequence:
MRICFVGAGALGSTIGGTLARGGADVWLIDPFRAHVEAINAHGLRMLEGEVESVAKVTACTSAAEVDGVADLVIVLVKSYHTRDAIRAAAPIIGPQTVVMSLQNGLGHEEILSEEVGRGRVMAGKTYVGGVLLGPGHVRSGVIGKETIIGELDGRLTERAQRISDTFNRAGILTLLSDNILGTMWDKLFINVAGGGITAITGLTYGGLYSLPILEDCALAAISEGIAVAQAVGVKISIADPRRAWTMASAGLPAEFKTSMLQSLQSGSLTEVDYIHGSVVRWGAKFNVPTPVNAALVALVKGLEYARSDYPGKA
The following text describes a protein:
Function:
Receptor for the chemotactic and inflammatory C3a, C4a and C5a anaphylatoxin peptides and also for their dearginated forms ASP/C3adesArg, C4adesArg and C5adesArg respectively. Couples weakly to G(i)-mediated signaling pathways.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MLNDTTSKDYEYEYDQEQYSDLLNVPVDCPAGNCFSNDAYLIVLLGLYSVIFLVGVPGNTLLAWVTWKESRHRLGASWFLHLTMADLLCCVSLPFLAVPIAQKGHWPYGTAGCWLLSSITVLSMYASVLLLTGLSGDLFLLAFRPSWKNADQRTCGVRVVQVSSWMLALLLTVPGAVYRKLLQEHYPPRLVCGTNYGGSVTAEVTITTVRFLFGFLVPLVFMASCHGILQRQMARRHWPLGTAVVVGFFICWTPFHLLRVIIAVASSHSPLLAWALEAEPLVTGLALAHSALNPIMFLYFGRKQLCKSLQAACHWALRDLQDEEESAVTKVSTSQEMVSEMPV
The following text describes a protein:
Function:
Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels. This toxin blocks N-type calcium channels (Cav2.2/CACNA1B). Shows a weak voltage-dependent reversibility. It is noteworthy that ancillary subunits beta modulate recovery from this toxin block. Cav2.2/CACNA1B expressed with the ancillary subunit CACNB2a (isoform 2a) shows a low recovery from this toxin block, whereas Cav2.2/CACNA1B expressed with CACNB3 does not exhibit recovery at all.
Subcellular Localization:
Secreted.
Domain:
The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin; The cysteine framework is VI/VII (C-C-CC-C-C).
Sequence:
MKLTCVVIVAMLLLTACQLITANDSRGTQKHRALRSDTKLSMSTRCKSTGASCRRTSYDCCTGSCRSGRCG
The following text describes a protein:
Function:
Structural component of specialized membrane microdomains known as tetraspanin-enriched microdomains (TERMs), which act as platforms for receptor clustering and signaling. Participates thereby in diverse biological functions such as cell signal transduction, adhesion, migration and protein trafficking. Regulates neuronal differentiation in response to NGF by facilitating NGF-mediated activation of NTRK1/TRKA receptor tyrosine kinase and subsequent downstream signaling pathways. Plays a role in the inhibition of TNFalpha-induced apoptosis. Mechanistically, inhibits the NF-kappa-B signaling pathway by blocking phosphorylation of CHUK. Also promotes the stability of the thiamine transporter 1/SLC19A2 in intestinal epithelial cells leading to an increase of thiamine uptake process.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MSVFTFVKLMMTLVNLLIFLSGITIMALGLWVSLDKNTFLRFLGLFPDKALKFFNIGYYCIATGGWMVLLGILGFSGAKKESKCLLLGFFSIILIIFITQVASAAVVLYYSSAMEILVEWQIPALKNIYGTDVMTTNIWDTAMTTMSCCGFFNYTDFVGSKFEAQNQGNLPPSCCGAGIDLCSCDEAERRLVKASKKHHNHGCYEQILTVLKHNGNIVGAIVASTGGLEVNTQNNQPQLKMLNFYIFL
The following text describes a protein:
Function:
Active during metamorphosis to degrade chitin.
Sequence:
MWLQAICIYTVFIIIGCGIPTAAEEHSLWRWTCENNRCTKIRNEPENKEPVLSLEACKMFCDDYGLLWPKPTIETNLGNFLSKINMNTIDIQITKQGKSDDLLTAAADRFKTLVSSSVPKGFSAKAAGKSVTVYLVNENPYIREFSLDMDESYELYISSTSSDKVNATIRGNSFFGVRNGLETLSQLIVYDDIRNNLLIVRDVTIKDRPVYPYRGILLDTARNFYSIDSIKRTIDAMAAVKLNTFHWHITDSQSFPLVLQKRPNLSKLGAYSPTKVYTKQDIREVVEYGLERGVRVLPEFDAPAHVGEGWQDTGLTVCFKAEPWTKFCVEPPCGQLNPTKEELYDYLEDIYVEMAEAFESTDMFHMGGDEVSERCWNSSEEIQNFMIQNRWNLDKSSFLKLWNYFQKNAQDRAYKAFGKRLPLILWTSTLTDYTHVEKFLDKDEYIIQVWTTGADPQIQGLLQKGYRLIMSNYDALYFDCGFGAWVGSGNNWCSPYIGGQKVYGNSPAVMALSYRDQILGGEVALWSEQSDPATLDGRLWPRAAAFAERMWAEPSTAWQDAEHRMLHVRERLVRMGIQAESLEPEWCYQNQGLCYG
The following text describes a protein:
Function:
Required for assembly or stability of RuBisCO. Acts at a postchaperonin step to fold and/or assemble the large subunit (rbcL) into RuBisCO. RAF1 binds first to a rbcL dimer (rbcL(2)), leading to a rbcL(8)-RAF1(4) complex formation. In the next step, RBCS displaces RAF1, thus resulting in holoenzyme formation.
Subcellular Localization:
Plastid, chloroplast.
Domain:
Has 3 domains, the N-terminal alpha-helical domain, an extended flexible linker and the C-terminal beta-sheet domain. The N-terminal alpha-helical domain stabilizes RbcL dimers and RbcL dimer-dimer interactions, facilitating RbcL(8) formation. The C-terminal beta-sheet domain probably dimerizes Raf1. The 2 C-terminal beta-sheet domains are swapped and pack against each other to form the dimer interface (By similarity).
Sequence:
MLSLTATTLSSSIFTQSKTHGFFNTRPVYRKPFTTITSALIPASNRQAPPKQQLYQPFRPPPSPIPPKFRSLDTAGKIEVLADRLGLWFEYAPLISSLYTEGFTPPSIEELTGISGVEQNSLIVGAQVRDSLVQSGAKPELIAAFDTNGAELLYEIRLLNTTQRVAAAEYIVDHGFDTKGAGDLARAIKDFPHRRGDVGLGDFDYNLPGDCLSFMLYRKSREHRSPSEIRTTLLEQALETAVTEKAKKAVLRELHGESEEERVKEEEIKIIRVPVVRLRFGEVAGASSVVVLPVCKAEEGEEKLLEAPMEFESGGEFGVVEAEKDWSRWVVLPGWDPVVAVRKGVAVSFSDDREVLPWNGKGEAIMVVIDREKKTVEADNGYYYLVVADGGMKLDRGLVLKEKGVNESLGMVVLVVRPPRDDDDEWQINDEDWD
The following text describes a protein:
Function:
Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
Sequence:
MEGTMPANEYVRHFENAVVLLTGATGSLGGCLLYKLALRLPTKKIYALCRGSVGESVRKWESTMPQQIDEILDTGKVELITGDLSKPGLGLNPAIREEMREEVTAVINTAANISLVEELKDSVRDNCQTAIALFQEVSEFRHVRHFIQFSSLAVNAFLTGGLIEERLYSPPRTVDEEDDRLGLPGADSSKLQYDDRYPWPYVQAKHMLERLLLRQSSSISILIIRPAAIGPAIAEPFPLYGPDKAIPMHSLILCFSVSDLGRVANINRPFEEVPVDLVANCCLLHLASGTTGVVHCASELYVRQTAVELMATARQCITPLEIAELFRTPRASTAILWQNKYRLDNIDDVPVFEVDCSRSEWQKQVTGPLALRPVDHDPQAHLQRRIRRMYRALLGRNRSDNRYP
The following text describes a protein:
Function:
Catalyzes the cleavage of cystathionine to homocysteine, pyruvate and ammonia during methionine biosynthesis.
Subcellular Localization:
Cytoplasm.
Sequence:
MTDKQLDTKLVNAGRSKKYTLGSVNSVIQRASSLVFDTVEAKKHATRNLANGELFYGRRGTLTHFSLQEAMCELEGGAGCALFPCGAAAVANTILAFVEQGDHILMTNTAYEPSQDFCSKILGKLGVTTSWFDPLIGADITQHIQPNTKVVFLESPGSITMEVHDIPSIVSAVRRVAPEAVIMIDNTWAAGVLFKALEFDIDISIQAGTKYLIGHSDAMVGTAVANARCWEQLRENAYLMGQMLDADTAYMTSRGLRTLGVRLRQHQESSLKIAAWLANHPQVARVNHPALPGSKGHAFWKRDFTGSSGLFSFVLNKKLTEAELSAYLDNFSLFSMAYSWGGYESLIIANQPEQIAAIRPAGGVDFTGTLVRVHIGLESVDDLIADLAAGFARIV
The following text describes a protein:
Function:
Involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles.
Subcellular Localization:
Cytoplasm. Endosome.
Sequence:
MADAHQSPLLLLPLKTTEEVDLGSAVKSLITNSYGEDSKKYSEQTSQLNRARQDAVKGAASDATGRDLLFKWFHMLEMLELRFPELRVPFPWKDAFTQKTISQSSLAYEKASIIFNIAATLSSLASSQPRMPGNADGLKRAYAALRQAAGMLSYINENFLHAPSTDMSKDVVKCLVGITLAQASEVFLEKTIEEKKGAGLISKLASQTAAAYTGLVDDSRENVTKGIFERSWAYLIQVKARHFTSVMQYYKALADDAAGSHGACLVRLTVAETAAKEARNLLTTFSASATASVTADRPSLPSDAASALVAIVNAQVARCTERKESAVKDNDLIYHDILPSESSLPAVDKLVAANPIPIQEIFAAPEVQRVIGPDLFQNLVPLGVHEKASLYSEEKAKIARAESERHDLATGEMQASLDYLGLPSSLQKYRALAQGSGSNAMLDSLADPGPEVMRWSTEEAEGGGGRGADGLGVGATGVDSALQRIESIKSQAANDIDAALAALDDENRECEKQRVRFGHKWSQDPAGLHTKDMRVNLKENKEAMQQASQNDAQIGGLWKSIRQDVQLLVSGREALEAAFAAALTGQTGLYGEGSAPTSLIDTSAEEESASEGEIASVRAKLAQIDEALIKLNKIKKERGEVLADLKEKIQTDDISQVLVLNRRAQNVDSSIFAAELEKFKPHQNRIAVSLHHQQALLAEVETAFKELIELPASKAAGAKWDEKEQARNKLVARLKRARDSNAQVRAGVAKGLQFYADLQEIVKATRQNVNRYVGERKSERSKLVSELEWEEKGSDGLSSSMAGLSGLGGAGGHPAPPTPHRHTSYASAYGGAGAPGPLSPGPPPAALPGVRQTSNSGPPPPPPLPHQQASYQQQPPPAAAAPAHDPYSSMFSSGPFSAALQQPASPQHQRPPTHYGSQLGYACDAPQRAPALPPPPQQFQPSFAPSVASPTQSRYTSPPPVPQGQQTFSGSSGYGMPPAPLQHGGGYGGSQPYAAHDYSSPPPQSPYGVPIGQQQYGGGHAQNQPQYQAYGAPPQQHASQQVYGSRAQPPPPQQQQYQQPSYAQHGGYQGGYQPPY
The following text describes a protein:
Function:
GPI-anchored cell wall protein involved in stabilizing the cell wall. Not implicated in virulence, heme uptake and biofilm formation.
Subcellular Localization:
Secreted, cell wall. Cell membrane; Lipid-anchor, GPI-anchor. Note=Found anchored in the cell membrane as well as a covalently-linked GPI-modified cell wall protein (GPI-CWP).
Domain:
The CFEM domain is involved in heme-binding and contains 8 cysteines and is found in proteins from several pathogenic fungi, including both human and plant pathogens (By similarity). The CFEM domain adopts a novel helical-basket fold that consists of six alpha-helices, and is uniquely stabilized by four disulfide bonds formed by its 8 signature cysteines (By similarity).
Sequence:
MHFSRTSLILFAAGLASAQLPNVPGCSLDCFVAALSADGCSSLTDFACHCQKPELVSNITPCVQSACNIADQSSVSVAVVSQCSAAGHPISVPPVGAASTTASETATTTESSTQTTTGTSSTASKTSSSAASSTPSSSSASSSHHHSSSSALTTRTLTSTEPSSQSTSASAAATTTLSGNAGSEKANVAGVVAVAAAALYLL
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MESEKRVPADKDSPAKSLITALHLKYVEKPWSETINLVCRCMEKRKKDSNVPSKQLLDCLERLHKALNATSFTDMVTRLEIIAKHKGLGSHLSPSEDVCYITSDIFYLEVLFQPAGEVADVKVAHHGEAPVSSEMLCNLLRLKNFEEFGKELEGLSSLFNTSGDSETNMKMFSALQFVEKDLLKMFQIPRPVSSGDPWLDNVLHGRIGNVTPRNNGIRYPMSIEYYISPYDLLEEKMKPESRSCGNKVFVTAEVTNTIQRLPSASVIADSPQMTNEGFPVHATLDDLVSMELSACLFLKFPRPVPILSCFIEEFHRLTAGISVSEDLKQVPFYELLMKTKMNVTTWGSDSCCFLVTLPGHHRQGYVISQQWWLKPWEGALVHKIPFTHPGHVPSLLSLLRHQTAFSTLIASCVTGNEQALHLSMLNELDFHFEILPYTGTSFSLSFQHPVTGSMASLFVNVVDSNHISCKLFPPEVPDPSIDDWISKVMKRCMSIPVTMRAIFRKIASRETPTASETGAAPENTSEITATTSSSLPIAQENTQSANHCPGALVMFFLQNL
The following text describes a protein:
Function:
Essential component of the nuclear pore complex (By similarity). The N-terminal is probably involved in nucleocytoplasmic transport (By similarity). The C-terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of Nup62 to the pore complex (By similarity). Binds to transcriptionally active genes. Negatively regulates chromatin attachment to the nuclear envelope, probably by preventing chromatin tethering by Nup154.
Subcellular Localization:
Nucleus. Chromosome. Nucleus envelope. Nucleus, nuclear pore complex. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Central region of the nuclear pore, within the transporter (By similarity). Associates with chromatin.
Domain:
Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited.
Sequence:
MVFQLPTTTAAPTGGATSSFSFGLSTGTPAAAPASGAATTAPATKTTFSFGTPAPTAGIGGGDADNSKAQAPPAFGFGLGSGTASAPLTLGTQAAANPASTTSATATGTSAAPPAFGGFTAQPAASVVPTIATSAPNTAATTTGLLGGSGLGAPKTTAAASTTLTAAPSAIASTQGAAPAPTLSTGGAFANLTTETKTTDSSAVSTASQLSYHQLEEHINKWTLEFEEQEKVFTEQATQINAWDKLLISNNGKIVELNDAVKKVKTDQQVLDQELEFIATQQKELEDSLGPLEKEFVNLPRVDMERSQTYLMVENLDTQLKQMSEDLKEIIDNLNEANKGQDTTDPIIQIGKILNAHMNSLQWIESQSTNISKKLEDIGKIQDSQKRDIFRAPF
The following text describes a protein:
Function:
Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Has an essential role in mediating growth by negatively regulating insulin signaling. It also has a role in maintaining presynaptic function in the neuromuscular junction synapses of third-instar larvae.
Subcellular Localization:
Nucleus.
Sequence:
MNQENDQELNGVNNDNRNERDHLEGFNPSAAHRFDYTLQDNENRENYKNEAKLVDYGTNWFPICGVSAVCFPEQQLPMKFDEDEQELYDRLVASARANGFVVLFPSDIRECDTLPYVATLSKVVQANPQTFSMELMGVHRCKVLSYNLENGEAFVQLLPEVEIPALLPKHLPKYSRRYSMYERRSLATRITGYPFDSLRDISRNQAEQCCLELKGMIGEEILQQALNRGLTYFSYFISQQIFSNRETEYSLLKEDSANTRIAAALKYCKVSIGKCRRCFAPIFLNENIMRLPEQTMTHVIAHGFVHKITLLSSITNYVRASAPSYEFTWFPDYAWIIIQCVGCHQHLGWEYMSMTREPQRFFGIQREGVQFENDIAEERDDDNSDPTESSDSLSDEESD
The following text describes a protein:
Function:
Non-catalytic component of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP), which catalyzes pseudouridylation of rRNA and is required for ribosome biogenesis. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs. The H/ACA snoRNP complex mediates pseudouridylation at position 93 in U2 snRNA; Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ("psi") residues may serve to stabilize the conformation of rRNAs.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSFRGGGRGGFSGRGGGFGGRGGGRGGFQQSFGPPDQVLEMGTFMHACEGEMVCESINPKIPYFNAPIYLENKTPIGKIDEVLGPINQVYFTIKPQEGIVATSFKPGDKVYIGGDKLLPIEKFLPKPKPPPGAKAKKAVGARGGGRGGRGGARGGGFRGRGGAPRGRGAPRGGSFGFRGGAGGRGGGRGGPRGGFRR
The following text describes a protein:
Function:
Member of the two-component regulatory system RprX/RprY. May activate RprY by phosphorylation.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MKKSTIWILGIIMGLSFLSLLYLQVSYIEEMVKMRKEQFNTSVRNALFQVSKDVEYDETQRWLLEDITEAERRALAQSSSTTEQKNGLIQQSERYRFKSPDGTLYSEFELKMITTEPSKVPKAMISERHGRNTIPQTSRSLTDAIKNRYMYQRFLLDDVALRMIYKASDKSIGERVNFKKLDNYLKSNFINNGVELLYHFSVIDKDGREVYRCSDYEDGGSEDSYTQPLFQNDPPAKMSIVKVHFPGKKDYIFDSVSFMIPSMIFTIVLLITFIFTIYIVFRQKKLTEMKNDFINNMTHEFKTPISTISLAAQMLKDPAVGKSPQMFQHISGVINDETKRLRFQVEKVLQMSMFDRQKATLKMKELDANELITGVINTFALKVERYNGKITSNLEATNPVIFADEMHITNVIFNLMDNAVKYKKPEEDLVLNVRTWNEPGKLMISIQDNGIGIKKENLKKVFDKFYRVHTGNLHDVKGFGLGLAYVKKIIQDHKGTIRAESELNVGTKFIIALPLLKND
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of 2-oxoglutarate and 2-oxobutanoate, leading to the respective 2-hydroxycarboxylate. Cannot use NADH instead of NADPH as a redox partner. Do not catalyze the reverse reactions.
Sequence:
MPHNPIRVVVGPANYFSHPGSFNHLHDFFTDEQLSRAVWIYGKRAIAAAQTKLPPAFGLPGAKHILFRGHCSESDVQQLAAESGDDRSVVIGVGGGALLDTAKALARRLGLPFVAVPTIAATCAAWTPLSVWYNDAGQALHYEIFDDANFMVLVEPEIILNAPQQYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNAQAIRDVLLNSSEQALSDQQNQQLTQSFCDVVDAIIAGGGMVGGLGDRFTRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLGQDDVLAQLTGAYQRFHLPTTLAELEVDINNQAEIDKVIAHTLRPVESIHYLPVTLTPDTLRAAFKKVESFKA
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). Involved in osmotic and oxidative resistance, yeast to hypha transition and the ability to damage and invade oral epithelial cells.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MRFTPILRQIPKLKLSEVLVKAGDGVPTGLAGIYKHPNPRPALVTLYNETLKTLKENFPADSVYRQSTEALTQNRLMIVESEEIVENIENQIGGGLIEEIVIQAADELSLASQLGGLKVWEELEEKPLDDQWVYFGKKI
The following text describes a protein:
Function:
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Required for cell growth, osmoresistance and expression of GPD1.
Sequence:
MTESAIDDQRFNLTKELQRHSCRDQGKITQKDDALDFISYSSFQSSFNTDQKSANNGSTVRRSIRSIFRRAAELPRVHMGPLTYSHGINELVNKKLRKDCDLSTLCRVLQRGIRMIRMTRRRRKFYEFKLINNNGQIIWKDGSKYLELDSVKDIRIGDTASTYQEEVDPKRLRSDSKLWIAIIYKVSNKLKALHVVALNELDFNTFLSCICGLVKLRRELMESILLPDNSQFARIHWQITVSEKEEDEKKDTLSFADVKKLCDKFHIYVSTGQLLEFFQLADINHNGLLNYFEFEKFIKILKNRKEVNMIWSKFTKPPHSHLSFENFFQFLITEQHEQVDRQTAWSYFIKYREPTQLTMGQDGFTKFLKEQPYLVEVKEELYSKPLNHYFIASSHNTYLLGKQIAETPSVEGYIQVLQQGCRCVEIDIWDGENGPVVCHGFLTSAIPLKTVIRVIKKYAFITSPYPLIISLEINCNKDNQKLASLIMREVLAEQLYFVGTRTDKLPSPRELKHKILLKSKKTSEATRGLSVNEPFPSSFSSSYESANEQELRMKDDSTNSSSATNSSSMQRIKRIGLKKHADIINDVSNISGIHGIKFRNFSLPESKTIAHCFSLNERKVEYMIKDKHLKLSLDKHNRRYLMRVYPHVLRYKSSNFNPIPFWKAGVQMVATNWQTNDIGQQLNLAMFQILDHQPDGSFKSGYVLKPKKLLPVVTKAKMIPLIYEHFENGSDPVTVKIRILSTQLLPRLNDTSPSRNNTNSFVKVEFHTDDEPTMPISIDKGTRISATEASTKSSQGNGFNPIWDAEVSITLKDTDLTFIKFMVISEETQIASVCLKLNYLRMGYRHIPLFNMEGEQYIFCTLFIHTQIL
The following text describes a protein:
Function:
Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI).
Subcellular Localization:
Nucleus.
Sequence:
MPNSHNERIASYIERRWPQRFPEFCAALRRYPLPISSGAAGTQLHGSCPEAVRATEAFCAMLAPRHGREVLGDDNSTNDEMLARDGEVSVAALRRSVSFPFSPFRCFKMQRTEGGPPLLSGQPAVWSGNSDWHFDQLHNSRGEAGTSLMHSSTTGCQSGEPLPEEKLSWRELRDRCLSKGLLGSGTKVHLIARLRKHGASKLAETSPKPRYVPDSQAEVLSHLREDSERCSRSMSSAGHTSTVSDMIRHGQRLRTLFRSPNTDIAPTTSLAEGGSEPQGRLLGTPKEFVASQQRERKLVHSTPSMPTNTTDIDADENETPKEEGCSNNYSWHLLVDNRERIKGAHENLIEVCSRAGAPSVSCTLPCGDFMIGINSPNVGCSANSANVPDYQCRNAAGCTVLREGAMYGQTQKISFLVVERKTVKDLCASITSSRYYEQRQLLSSSPFRSVVWVVEGTMESITVEERRRVLSACASLASLPRFRVVWTRHLSETATFLRSLGKSVGSILCKTKMEQCPETLVTNCTECLQYINKIRKDIQARTTFPRMLMCIRGCSAPLAIQLASKYGSLLGLWRRLKYQGVDACDADPDIHRLTKPQKEVYLCLTKFILTRSYC
The following text describes a protein:
Function:
Transcription factor required for transcription of 5S rRNA by RNA polymerase III.
Subcellular Localization:
Nucleus.
Sequence:
MSESDETKSISSLISSSSSSRPKKYICTYEGCDKAYNRPSLLEQHLRTHSNDRPYKCTVEDCDKAFFRKSHLETHIVSHSEKKPFHCSVCGKGVNSRQHLKRHEITHTKSFKCTFENCQEAFYKHQSLRHHILSVHEKTLTCKQCNKVFTRPSKLAQHKLKHHGGSPAYQCDHPGCFKNFQTWSVLQFHIKQSHPKLKCPKCGKGCVGKKGLSSHMLSHDDSTMIKIWTCDYCDVGKFAKKNELVEHYNIFHDGNIPDDLLKETEVKKLENLLDQGSKLNNLHELETEKLKVEEDEEDEEDSLDEKRSDVRSDSMSAQRSIKSFTASLEGSKSVSKLISNSGKKINCPKNNCDRMFSREYDLRRHLKWHDDNLQRIESFLNSIEKEETPEGEPLVKKARMDLLPNETSVISR