lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular Localization:
Secreted.
Sequence:
QQHQQIEQQNILCLIWLLICVSWPWRSPGVVSRCCCSWCLSPRALRPRRLTSSASTTTARRARTSRPSSATRWRRSSAPPPASPARSSASISTTASSGYVLRSPASCRVACTAAPLIDRSIDVVFFCNLQGCDASVLLSSTAGNVAERDAKPNKSLRGFGSVERVKARLEAACPGTVSCADVLTLMARDAVVLARGPTWPVALGRRDGRVSAAGEAAASLPPADGDIATLLRIFAANDLDIKDLAVLSGAHTLGTAHCPSYAGRLYNFTGKNDADPSLDGEYAGRLRARCASATDESGMISEMDPGSYKTFDTSYYRHVAKRRGLFSSDASLLTDATTRDYVRRIATGKFDAEFFSDFGESMTKMGNVQVLTGEEGEIRKKCYVINS
The following text describes a protein:
Function:
Transcriptional activator. Binds a GC box motif. Could play a role in B-cell growth and development (By similarity).
Subcellular Localization:
Nucleus.
Domain:
The acidic N-terminal part may favor interaction with the basic domain of transcription factors; The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors. In KLF6, the motif is inactive.
Sequence:
MDVLPMCSIFQELQIVHETGYFSALPSLEEYWQQTCLELERYLQSEPCYVSASEIKFDSQEDLWTKFILAREKKEESELKISSSPPEDSLISSSFNYNLETNSLNSDVSSESSDSSEELSPTTKFTSDPIGEVLVNSGNLSSSVISTPPSSPEVNRESSQLWGCGPGDLPSPGKVRSGTSGKSGDKGNGDASPDGRRRVHRCHFNGCRKVYTKSSHLKAHQRTHTGEKPYRCSWEGCEWRFARSDELTRHFRKHTGAKPFKCSHCDRCFSRSDHLALHMKRHL
The following text describes a protein:
Function:
Structural component of heterochromatin involved in gene repression, including several floral homeotic genes and FLT that regulates flowering time. Required for maintenance of vernalization-induced repression of FLC. As part of the PRC1-like complex, recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me), leading to epigenetic repression. PcG PRC1 complex maintains the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. Transcriptional repressor that binds DNA on GAGA-like motif and 5'-(A/G/T)AACCCTA(A/G)-3' consensus motif in the promoters of target genes. Recognizes and binds histone H3 tails methylated at 'Lys-27' (H3K27me) but depleted in active histone marks such as H3K4me, leading to epigenetic repression. When in complex with LHP1, recognizes and binds histone H3 tails methylated at 'Lys-4' (H3K4me) and 'Lys-27' (H3K27me), mostly corresponding to stress-responsive genes.
Subcellular Localization:
Nucleus. Note=Punctuated distribution and in heterochromatic chromocenters.
Domain:
The chromo domain specifically binds to dimethylated H3 'Lys-9' while the chromo shadow domain is required for dimerization.
Sequence:
MKGASGAVKKKPQVLNEAGEAETAVETVGESRKISGDGGFGSDDGGGGGGGGSGESILREIGDDRPTEDGDEEEEEDEDEDDGGDEEDEEGEGEGGQEERPKLDEGFYEIEAIRRKRVRKGKVQYLIKWRGWPETANTWEPLENLQSIADVIDAFEGSLKPGKPGRKRKRKYAGPHSQMKKKQRLTSTSHDATEKSDSSTSLNNSSLPDIPDPLDLSGSSLLNRDVEAKNAYVSNQVEANSGSVGMARQVRLIDNEKEYDPTLNELRGPVNNSNGAGCSQGGGIGSEGDNVRPNGLLKVYPKELDKNSRFIGAKRRKSGSVKRFKQDGSTSNNHTAPTDQNLTPDLTTLDSFGRIARMGNEYPGVMENCNLSQKTKIEELDITKILKPMSFTASVSDNVQEVLVTFLALRSDGKEALVDNRFLKAHNPHLLIEFYEQHLKYNRTP
The following text describes a protein:
Function:
Plays an important role in the control of DNA replication and the maintenance of replication fork stability. Important for cell survival after DNA damage or replication stress. May be specifically required for the ATR-CHEK1 pathway in the replication checkpoint induced by hydroxyurea or ultraviolet light. Forms a complex with TIMELESS and this complex regulates DNA replication processes under both normal and stress conditions, stabilizes replication forks and influences both CHEK1 phosphorylation and the intra-S phase checkpoint in response to genotoxic stress.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MLEPQENGVIDLPDYEHVEDETFPPFPPPASPERQDGEGTEPDEESGNGAPVRVPPKRTVKRNIPKLDAQRLISERGLPALRHVFDKAKFKGKGHEAEDLKMLIRHMEHWAHRLFPKLQFEDFIDRVEYLGSKKEVQTCLKRIRLDLPILHEDFVSNNDEVAENNEHDVTSTELDPFLTNLSESEMFASELSRSLTEEQQQRIERNKQLALERRQAKLLSNSQTLGNDMLMNTPRAHTVEEVNTDEDQKEESNGLNEDILDNPCNDAIANTLNEEETLLDQSFKNVQQQLDATSRNITEAR
The following text describes a protein:
Function:
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Sequence:
MALQFDEAELLKAYHLDSLEPSAWHTTETGADEKGSASSTAVADEPDPLGLRSSMATFRGLPKDVKTQTSLSSKAFDAKVFLSTIHPDATFADLSHGIQHLKNSIDQRSEALKVLVEENFDRFVAVKATTDGVYREMRDTESGPLQPQADYGVASLNNILANASAKADQVFMPVLENNLKTIKLRSTLGVFERSKFFFNLPGSLSESVEMGRYDVALRDYKKGKYLLDSRPGQLLAVGSATQPESAGGARNDIQQKRVFAKVWDAVEVTMKDMQSRLTAQLREPRRSVEEQERTIEILLELDPTDDPVSIFLESQHEHLRSVMRKTFDGGVARIEAARSAQRASSSAADRDRARDLQKSIRSMRFIDRLDASFDKCTGAETWKATHDLVKSLSKTIAGSLPNFWRVAKNHAEGKFTRAKTRLGGATSATTTSGTTMSAKNKAWAVEALDAYISLVSHLFSLTDMSILIRQPLPTQTPDWVPTGTSSPTAAHYLRKMLTQLVEACNDLASLGITSTSSLRGLLTNARFSFVQVLCVLWQEDAKLLHMLEDWTLNPDEQATTLHLRELAAFHKSNARQAFHLAGGRSAVTPASALEASRKNRNAEQPVAPEFTTRIKASFLDALYAFLDGLVHLAFSDYSPLEPRTALSVQSVPGHPGSAVDVRDPDTRVLVSVTNLSHLSRIVVPSLVKQFGDAYAVKMDEDLATLTEVSTQLDAILFNDYVQRKSAWISEIVSHGILSSGIEWSNIPKPSSVHAFIYQALLSLVQVHAHVRSIAKPLVTRTVTTLVDDLASTTLDSFQRIPRFGLGGMLQATLEIEFLHQTLTNFISPKAEGLLKQVYETISHKYRRVDAREKEQLNSELERVKQILVASRKATALEFLCFRRARRDTAKDEAAPT
The following text describes a protein:
Function:
Required for dimerization of active 70S ribosomes into 100S ribosomes in stationary phase; 100S ribosomes are translationally inactive and sometimes present during exponential growth.
Subcellular Localization:
Cytoplasm.
Sequence:
MQFAIHGKNIEVTEPIRDYVSSKLDKVFAHFDQLTMGVDVYLSVARNPRISRSHSAEVTVQASGTIIRAEEETENLYASIDLVADKLHRQMRKYKERMQKKPKPKTGLAVANQAPISLPNGDEKATALPKEVVRTKYFAMPPMSPEEALDHLALVDHDFFVFRNAESGEINVLYARNHGGYGLIVPR
The following text describes a protein:
Function:
Has peptidylprolyl isomerase (PPIase) and co-chaperone activities. Assists protein folding by catalyzing the peptidyl conversion of cis and trans rotamers of the prolyl amide bond of protein substrates. Inhibits calcineurin phosphatase activity in vitro. Plays an essential role in merozoite egress from host erythrocytes.
Subcellular Localization:
Cytoplasm. Nucleus. Note=During the asexual blood stage, predominantly localizes to the cytoplasm of ring stage parasites and then translocates to the nucleus during the differentiation into trophozoites and schizonts.
Domain:
The PPIase FKBP-type domain contributes to the chaperone activity. Required for the inhibition of calcineurin phosphatase activity; The TPR repeats are important for the chaperone activity. In another study, these repeats appear to be dispensable for chaperone activity. Dispensable for PPIase activity. Dispensable for the inhibition of calcineurin phosphatase activity.
Sequence:
MTTEQEFEKVELTADGGVIKTILKKGDEGEENIPKKGNEVTVHYVGKLESTGKVFDSSFDRNVPFKFHLEQGEVIKGWDICVSSMRKNEKCLVRIESMYGYGDEGCGESIPGNSVLLFEIELLSFREAKKSIYDYTDEEKVQSAFDIKEEGNEFFKKNEINEAIVKYKEALDFFIHTEEWDDQILLDKKKNIEISCNLNLATCYNKNKDYPKAIDHASKVLKIDKNNVKALYKLGVANMYFGFLEEAKENLYKAASLNPNNLDIRNSYELCVNKLKEARKKDKLTFGGMFDKGPLYEEKKNSAN
The following text describes a protein:
Function:
Co-chaperone required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Acts as a co-chaperone via its interaction with HSP90 and is required for the piRNA amplification process, the secondary piRNA biogenesis. May be required together with HSP90 in removal of 16 nucleotide ping-pong by-products from Piwi complexes, possibly facilitating turnover of Piwi complexes (By similarity).
Subcellular Localization:
Cytoplasm, cytosol. Nucleus.
Sequence:
MGGSAPGQSPYQRLSQRMLDISGDRGVLKDVIREGAGELVTPDASVLVKYSGYLEHMDKPFDSNCFRKTPRLMKLGEDITLWGMELGLLSMRRGELARFLFKPTYAYGTLGCPPLIPPNTTVLFEIELLDFLDSAESDKFCALSAEQQDQFPLQKVLKVAATEREFGNYLFRQHRFYDAKVRYKRALLLLHRRSAPPEEQHLVEAAKLLVLLNLSFTYLKLERPTTALCYGEQALVIDQKNAKALFRCGQACLLMTEYQKARDFLVQAQKAQPFNHDINNELKKLASCYKDYTDKEKEMCHRMFAPCDDDSAVGEN
The following text describes a protein:
Function:
Probable gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MAVLYFFREPETVFDCAAFICILQFLMGCNGFGIRRSTFRISWASRIYSMSVAIAAFCCLFGSLSVLLAEEDIRERLAKADNLVLSISALELLMSTLVFGVTVISLQVFARRHLGIYQRLAALDARLMSDFGANLNYRKMLRKNIAVLGIVTTIYLMAINSAAVQVASGHRALFLLFALCYTIVTGGPHFTGYVHMTLAEMLGIRFRLLQQLLQPEFLNWRFPQLHVQELRIRQVVSMIQELHYLIQEINRVYALSLWAAMAHDLAMSTSELYILFGQSVGIGQQNEEENGSCYRMLGYLALVMIPPLYKLLIAPFYCDRTIYEARRCLRLVEKLDDWFPQKSSLRPLVESLMSWRIQAKIQFTSGLDVVLSRKVIGLFTSILVNYLLILIQFAMTQKMGEQIEQQKIALQEWIGF
The following text describes a protein:
Function:
Essential sugar transporter required for the transport of UDP-galactose and UDP-glucose from the cytoplasm into the Golgi and the endoplasmic reticulum, to ensure quality control of protein folding. Essential for pollen development and involved in embryo sac progress.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins.
Sequence:
MEVHGSGFRRILLLALCISGIWSAYIYQGVLQETLSTKRFGPDEKRFEHLAFLNLAQSVVCLIWSYIMIKLWSNAGNGGAPWWTYWSAGITNTIGPAMGIEALKYISYPAQVLAKSSKMIPVMLMGTLVYGIRYTFPEYMCTFLVAGGVSIFALLKTSSKTISKLAHPNAPLGYALCSLNLAFDGFTNATQDSIASRYPKTEAWDIMLGMNLWGTIYNMIYMFGLPQGIGFKAIQFCKLHPEAAWDILKYCICGAVGQNFIFMTISNFGSLANTTITTTRKFVSIVVSSVMSGNPLSLKQWGCVSMVFGGLAYQIYLKWKKLQRVEKKKQKS
The following text describes a protein:
Function:
Has a high affinity for collagen. Affects nematode body morphology and mobility. Essential for C.elegans development and muscle function. The cysteine-rich region could have protease inhibitory activity or may provide the framework for a protein binding module. Probable role in skeletal morphogenesis.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix, basement membrane. Note=In or around the basement membrane.
Sequence:
MRYALAACLLLLAASSFVDAKKKKIADDELGELLDNIDADEEKKSVEPAKNPCEDHQCGWGKECVVGKKGEPTCECISKCPELDGDPMDKVCANNNQTFTSLCDLYRERCLCKRKSKECSKAFNAKVHLEYLGECKKLDECTEEHMAQFPERMADWLFQVMKELKKRRELHKLEWEELLSEAENDDEKKHVYPVIWKFCELDTKPHDKSVSHHELIPITAPVIPMESCIKPFLEGCDANNDGNISIKEWGKCLGLKEGEIQERC
The following text describes a protein:
Function:
Laccase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a structural component of the conidial wall. The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA. The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayg1 though chain-length shortening. 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone. The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN. 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone. Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN. Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin. DHN-melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize. DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins. DHN-melanin also plays a crucial role in fungal virulence, including a protective role against the host's immune defenses. DHN-melanin also protects conidia against amoeba predation.
Subcellular Localization:
Cell surface.
Sequence:
MWYQSASLLGVAAVAQAATVHYSLDLTWETGSPNGVSREMIFVNGQFPGPAIILNEGDEAIIDVTNHLPFNTSIHFHGIEQKNTPWADGVVGLSQWAIQPGQSYTYQWRADTYGTYWYHAHDKAEIMDGLYGPVHIRPRPNRDSPFSMISDDPADIRAMKQAERNGKLVMLSDWDHLTGQEYMKAMEETGYDIFCSDSVLINGRGSVFCHDPEELTQMVPPPELAILNSSLTDKGCLPFVPPIQGNWEHHPDKVPPGLNEGCHPSTTQETIFTVDAAHQWASFHFISAASLKVLVVSIDEHPMYVYEVDGRYIEPQLAHSVKLYNGERYSVMVKLDKEPANYKMRAANDGGNQIVSGFATVTYEGGETSQRPSQPYIDYGSRNTSADVIPLDTNHLPPYPAISPASEPDDFHILMLGRTNSSWEWSLDGAAFLPSNLAALPPAILSPQAPEFADALKITTRNDTWVDIVFQLVVSETTPIQPPHPLHKHSNKGFLLGTGHGKFNWTSIKEAKEASPESFLETPVYRDTFTTSPQGETWTAIRYHVENPGPFLLHCHMTTHLQSGMGLILMDGVDVWPEVYADMITPM
The following text describes a protein:
Function:
Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
Sequence:
MRRGSASRSARSAKIAVCDLLSRLVPLPDQSAPSTYIITPEITSTLHKNLFRHLLESVPSPAVFIPCDPTTSVSQALALLASYGWNLSRAQIEETRQVALARKKGKQAQRAQSPWSTSSAYDDVEDPDLLGPEYSESRRGMPCGHLFQKGEAVYRCRECSLDDTCVQCAPCFQASIHAKHNHDVVFSVSSSNGGCCDCGDPEAWKQDVCCRYHSQSFSNSITANADMELESESQPPHHVISSATQPEAPSVTSEEADGLDQIDAALAALPSQLRDPLLDVISELVMLIVTVFDHAPEFEVVSSLHTPDVVSQLPSLQDGLVSQQSSSTPSKRKSSTTGPRDSDEDMSAVEVDNLVGDSIDEDEQDDEINSHRAWGSRAPRASRSSPGSKYMAEGSSWRSAPHSLDTQPDLTSDNVMAASEMLSASEPWRKFGLDGAKAQVTGDSNSTNRQYAVLLWNDEKHSFSQVIDIVTDATGRSEHDAKGVAERVDKHGREIIEVGSDLRRLHQIARVLHSIDLAVTIRPAFDVFAEEVIQIVLNFLMDLSNCNLYLPSSHGATTLSSSIPLSSWLGQPLKPDAAAFKHIVARSFFTPFHPLKPIEAGSMSPEFFDPRDLTHYEGLLLMDCKLWKSARIDIKALLMSLIARREIKKEVALRFAKIYPKLVETFMIKDREQEYSICFLTVQLFSVPSIATMLVDKVGFLSKLLLLLQSIFAGSLVNEKMDLILPPPTRIQSQANVHLIFLRQSRSYHIFYDIRYLLASEGVQKLIAKAEREHLDYFLACLSLFQAIHPSKRAVSAHVEFESEMWIPVFHISSHLGKAAKMFGEAFAHAQPEKLVAAIVVTIYAIYWSSCKLAIEDPDSWPQTTFHDASYTIGTSAGTKTMSVISFAVESQPISFHHPLHWLLAELIRQISVVGHDALQTWSGSERLDALLRTRVDEDNLLVAIDSPLRVCVKLAQIRCNMWVRNGFVIRSQAHHYRDNSMRAIMYDQDLLLVQAGFAMIDTDRYLLTLLDRFHLLNWFNQTDSPADKPYDTVQGVFLAEELLFLITTCLSEMSSVCAWPIEAQIRREVIHFLALGQGTFTDVTKNIPEKFTDHAAFERILSQVSTFRAPDGTHDFGIFELKDECYAEIQPFFFHYTRNQREKVEEVLRERQKKRLAHSSGRTVSAIKDEELPPWVPSASLHQLRGTLFGRLPDVLSNDILVSLLFKALDQTRSLFAYAPDMLVDAALQIVMIGLVDAADSFADKAASLLISQLEAADDAGAEAEPKPAAEATLVEMLCRVELLEKFKPFKGKITWCLEKLASHSEKARSIVRPHFSATGRGAISADGSGSAASGAPKKKSAEEARRAAAKARQAAIMQKFSAQQKSLLDQLGADDDDDDDDDEGEVDAATSSVGAEGKAPKRTWGSCILCQENLGSDKAFGSLAHIQPSRMMRMTPKQDAPSLQQALEAPLTMDRGSSTGKRIQGTAPMGRSGLPQNAKARQGPAYGSFPQEDHRLGFFASACGHLMHLHCFETYCRSVEQRHTQQIARNHPEDLHRSEFICPLCKSLGNVILPVADVASTTSAEGMFAPFGSVVPDESSLQDWIRKINIDILKHSSKTNVADYQETDHGSGAFLPFFVDHSQSSLQMRLEMANIDRSTGQMIDRLMNVLKPMSHTTKAAREKLQQHTILAPQGRKMYIPEELVAYTIAMLEAAQRGMTPSPSTDCTVPVEQRTVADALNDSTLELLRSLIHCLRVSTLTFHEGSKGPDIIRRGLLKRLLPHWGGDDAVRSPLLLRDPMSILIEAAVVAPDALTQCTALMYYVCLVQTVFGLAQPSIWPQVYGHMGTLFGPSSAPRPGAGLKPGHISKEDVEEARLIFPDVRWTVANIIGFVGYARGNITLGFDNLDDDTLAKMICSYTLPFLRRAAILRRVLGVSRAGLGGADVEAMQVGEGSPAEYRRLLSELHIPLPSEALPVRAEKQTTMASLVEGWIKHAYVPLASLFRPLPIQPAPLGNSLFGGSQASNSAAHDRPSSAAAAIAGVGSASGSASLASGTLGRSSAGLHSLASSYLQAAESHPTLLLEHPHIYELAKLPADLATLLQDTRRRPCKKCGNVPPEPALCLMCGDVVCLQSFCCQSEDDGERGECNQHMDSCGGSVGAYFKIKSNLVLLLYQGNGTFHFLSPYLDSHGEIDVGLRKGRPQKLHQQRYDELRKQIWGHGVANIVARKIEAAMDQGGWQTF
The following text describes a protein:
Function:
Is required to sustain N(2)-dependent growth in the presence of low levels of carbon monoxide (CO). Probably acts by protecting the N(2) fixation ability of the nitrogenase complex, which is inactivated in the presence of CO. Is not required for CO-dependent growth.
Sequence:
MTMDGPAHMPRRYVTFQGVNVEGLSQQLIARILFHVADPAKSNAFWEHFKAKLADADKTLARTADSLCLLCGAIGYIDELFEDNDDEEGLTILRRLEDELC
The following text describes a protein:
Function:
Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm. Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix.
Subcellular Localization:
Peroxisome membrane; Single-pass membrane protein.
Sequence:
MADIPSAPPVVQAEEISTTAEVKTPLPDPPATLSAEAAPIVEENLPLREDFIQNAVKFLSHPKVQGSPVQYRRSFLEKKGLNSAEITEAFRRVPDTATAPPAPLPATTTVTTTTTSPAPPAPTASPVAVPPRPAAVLRKPWEQTAQPASAYPAAGQQVAAAPQAQVAPRQGVRWTQMVLALGVLSAAGAGTVIVTKQYLVPRLRAWLRRWLLDISEEVGGVRKLTPVEEAANAAAAAASAAAEATKIMKEAREEVKEVSAEGDRKLEAILGAFQAQTRELTATLGSLKGALEEREEARKEALILGTASHPEGAPPVSLPDLRKELLKFTSVMTGFTGTPPANEAAAAGLSGADVSELKALVLERRAAAVQAPRGPAVDREYEESEDGLNWLQSSQTASQNDLATAPRYDSASKGPVNTSVDRRALGTTAAGRAGPANQGLAMQPASASMEPRYEDANGYQEKGSRPTSANSMPLSQVASGQELPHRPTSSPAQGPDHAPHSQSYMDVLQMLKDGKPIPGIRDIDDKPPNPNQPPTDPKLKPRAKPWEKGFQQVSEKPANGEAPPPFNITNSRSAASPAPVYSSDGQAPWWRKAQPLSQPGVSGPPQGQDGYPPRSTASGAESESFVHPALAGDIDPPRPQAVQSELASGSAPADPSSGPRITEVHSEPVEAQAVEAQPGPSSSRSTSGAGGSQGTERPGLGTGVPAVPSKPAWRPPAVPGFAMPSAAEAIKGKGKVVPVTPMASNGHREVRAAATGEGQGEGSSQSGSVEGTDDRFEKSYAGVVQAGGGSQENEGMEAGGNAE
The following text describes a protein:
Function:
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MRIAQHSKSCQVLQHKKIFTFNDEELINTSESTPNSSGNTEKPQLLVFRNQIMPDSQIARELHEASIQSHWYVETPKEYVDKRVVKLKKQKLEKVVVLDLDETLIYYKPNQTIVRPFCQEFLERLSRICILVLFTAAKKEHAINMLKIIDPNKKYFKAICTSDHNDWQYIVIVENSPKNFVAQINNGIPIIPFEGQQNDNQLELLLSFLEIVLLVDDVRVQLANIFKLQYFYKELNGKQAINKLYNLKKNQ
The following text describes a protein:
Function:
Partially mediates extracellular nucleotide derived phosphate hydrolysis along with NPP1 and NPP2.
Miscellaneous:
MISCELLANEOUS: Present with 1110 molecules/cell in log phase SD medium.
Subcellular Localization:
Secreted.
Sequence:
MFKSVVYSILAASLANAGTIPLGKLADVDKIGTQKDIFPFLGGAGPYYSFPGDYGISRDLPEGCEMKQLQMVGRHGERYPTVSLAKTIKSTWYKLSNYTRQFNGSLSFLNDDYEFFIRDDDDLEMETTFANSDDVLNPYTGEMNAKRHARDFLAQYGYMVENQTSFAVFTSNSKRCHDTAQYFIDGLGDQFNITLQTVSEAESAGANTLSACNSCPAWDYDANDDIVNEYDTTYLDDIAKRLNKENKGLNLTSTDASTLFSWCAFEVNAKGYSDVCDIFTKDELVHYSYYQDLHTYYHEGPGYDIIKSVGSNLFNASVKLLKQSEIQDQKVWLSFTHDTDILNFLTTAGIIDDKNNLTAEYVPFMGNTFHRSWYVPQGARVYTEKFQCSNDTYVRYVINDAVVPIETCSTGPGFSCEINDFYDYAEKRVAGTDFLKVCNVSSVSNSTELTFYWDWNTTHYNASLLRQ
The following text describes a protein:
Function:
Component of the gamma-tubulin ring complex (gTuRC) which mediates microtubule nucleation. The gTuRC regulates the minus-end nucleation of alpha-beta tubulin heterodimers that grow into microtubule protafilaments, a critical step in centrosome duplication and spindle formation.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Sequence:
MFDDLCEALLPAAKTHLARSVNRRGKAEPQEVAYNALSQIFFKNKDPHVVFDLRVVAWPKATVWRALWRRLKQPLPGPLLRGSVFGPPGHSGGSGPLQVLPRKRDTSLTTSMWEKRPYSGYDCDDLSVEMDVQSLISRESWSAMIQETSGYGGCSGTGLPTVGLFSVGDPCGDRSRETPGSRLRALVHSRTIMTGRPTGPAPVPDNADSLAISGGLPFRVASPPSVDQWEDEGFQSSEPSVTPDPALTYEASKRMLDATCCCWNRGCPPWPTEEEPYLRRREEPAFRQVLQRLRQGELQAACLGAVLQAPQPCLCEGVPNVLNVLDCGVVSATFSLLPRVRTAHRPPQWCGALASWLTCLSLRGVGLCSRCFCKHIAYDIYVWGERRINWLKLCCSPALLCWSRPSAVPAGSDCAAYGWGAMERVARHSCLSQELRMEIAKQELIAHAREAASRVLSALSDRQMSERMALDARKREQFQRLKEQFVKDQERRQAARQEELDDDFSYARELRDRERRLKSLEEELERKARQALVDHYSKLSAEAARREQKALWRIQRHRLESARLRFLLEDEKHIQEMLKAVSEAHQPQEPPDVLLSVHPQVTSPGPEHPEGGQGCDSGSAEQHSPAWDGRNRPGLLTPQPLKPLAVGAGGTGLQQAEEARPFSDSLSIGDFLPVGPGAEPSVQTGMVPLLEVALQTINLDLPPSAPGEAPAAASTQLSRPQEYDFSTVLRPAVATSPAPGPLQAAKCSLGSSGLQLWEDSCGKMDACGSTSRETLLPSHPSRRAALEEGSSQPTERLFGQVSGGGLPTGDFASEIAPARPRWNTHGHVSDASIRVGENVSDVAPTRPRWNTHGHVSNASISIGESVSDVAPTRPRWNIHGHVSNASIRVGENVSDVAPTRPRWNTHGHVSNASIRVGENVSDVAPTRPRWNTHGHVSDASISLGESVSDVAPARPQWNTHGHVSDASISLGESVSDMAPTRPRWNTHGHVSDASIRFGENVSDVAPIRSRCNTHGHVSDASISLGEPVSDVVSTRPRWNTHVPIPPPHMVLGAPSPEAEPNTPRPQQSPPGHTSQSALSLGAQSTVLDCGPRLPVEVGPSLSSPSSGCGEGSISVGENVSDVAPTQPWWPNTPGDSVSEELGPGRSGDTEDLSPNWPLNSQEDTAAQSSPGRGEEQAYLAGLAGQYHLERYPDSYESMSEPPIAHLLRPVLPRAFAFPVDPQVQSAADETAVQLSELLTLPVLMKRSITAPLAAHISLVNKAAVDYFFVELHLEAHYEALRHFLLMEDGEFAQSLSDLLFEKLGAGQTPRELLNPLVLNSVLSKALQCSLHGDTPHASNLSLALKYLPEVFAPNAPDVLSCLELRYKVDWPLNIVITEGCLSKYSGVFSFLLQLKLMMWALKDVCFHLKRTALLSHMAGSVQFRQLQLFKHEMQHFVKVIQGYIANQILHVTWCEFRARLATVGDLEEIQRAHAEYLHKAVFRGLLTEKAAPVMNVIHSIFSLVLKFRSQLISQAWGPAGGPRGAEHPNFALMQQSYNTFKYYSHFLFKVVTKLVNRGYQPHLEDFLLRINFNNYYQDA
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Sequence:
MEERTLVILGATGSIGTQTLDVLKKVKGIRLIGISFHSNLELAFKIVKEFNVKNVAITGDVEFEDSSINVWKGSHSIEEMLEALKPDITMVAVSGFSGLRAVLASLEHSKRVCLANKESLVCGGFLVKKKLKEKGTELIPVDSEHSAIFQVMEPEVEKVVLTASGGALRDWKISKIDRARPEDVLKHPVWNMGARITVDSATMVNKAFEVLEAMELFELPFEKIEVKIHREGLVHGAVVLPDGNVKMVVSPPDMRIPISYALFYPRRVALEPFFLRTISLSFEDPDPEKYPAFFLLKEIKDSYALRTAFNAADEVAVEAFLKGRIRFGGIHRVIEKTLEEFQGYPQPRTLDDVERIHFEAIKKAERVTEWLSSTSY
The following text describes a protein:
Function:
An odorant receptor which affects chemotaxis to the volatile odorant diacetyl. Specifies AWA neuronal cell fate via the odr-7 pathway.
Subcellular Localization:
Cell projection, cilium membrane; Multi-pass membrane protein.
Sequence:
MPTQELIPVTEKVKIWFLDVSAFFAISINFALIILILTKSPQSLGTYKYLMIYIALFELTYAALYVAEKPEIFTKDSAFLILTNTKDSVFPKTISIFVDVLFIGFYGLTISLLAIHFIYRYLAISSNDWLDTFQDWKLILWLLFPIANGGVWCFAAAVIFAGKEDSDRFLREFYLPLVQNKTSFEDVYYGGPFYYLNDAHGNSYINWISFQGTLVVLSLIIISFITMIYFGVKGYNSMKDLMRHASISDKAKSLQSQLFKALVLQTIIPVFLMHIPATAIYVTIFFNVSSEIFGEILNLSIALYPALNPLPTIFIVSSYKQAVIDLLCCKKKIDPHSGTQGNSQLMTQHPLNTISHTLS
The following text describes a protein:
Function:
Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2).
Sequence:
MIVIDEKRIFQEIEEKNPASVSLNGPDGILPQVQETAKNITKKFGIPAYVLADTTWGTCDLNSNGSKVLGAEIQFNIGHTINTETYEKNLILIDAYDDVEFDSVAKKCAELLKGKVISLVTDSQHLHQVDKVEKILTENGITVKIGKGKGQLNDGQVFGCEFYPATDLKKEVDAYVFLGQSNFHASGIALSTNLPTYVLDPYFNEVREVTDFAQKLKKKATLAIYKAAEAKTFGVIVGLKEGQLSKVFALKIKEELEAEGKEVQLFALTDITNDRLRNLKGIDAFIQVACPRISTDNQFDKPVLSSPQANALLKILRNESIEGYLEIPHWL
The following text describes a protein:
Function:
Metallo-phosphoesterase involved in phosphate metabolism. Acid phosphatase activity with phosphoenolpyruvate, inorganic pyrophosphate, phenyl-phosphate and p-nitrophenyl-phosphate as the most effective substrates. No activity with phytic acid, phosphocholine or bis-p-nitrophenyl-phosphate. Has a peroxidase activity at alkaline pH.
Subcellular Localization:
Vacuole.
Sequence:
MNHLVIISVFLSSVLLLYRGESGITSSFIRSEWPAVDIPLDHHVFKVPKGYNAPQQVHITQGDYDGKAVIISWVTPDEPGSSQVHYGAVQGKYEFVAQGTYHNYTFYKYKSGFIHHCLVSDLEHDTKYYYKIESGESSREFWFVTPPHVHPDASYKFGIIGDMGQTFNSLSTLEHYMESGAQAVLFLGDLSYADRYQYNDVGVRWDSWGRFVERSTAYQPWLWSAGNHEVDYMPYMGEVTPFRNYLQRYTTPYLASKSSSPLWYAVRRASAHIIVLSSYSPFVKYTPQWHWLSEELTRVDREKTPWLIVLMHVPIYNSNEAHFMEGESMRAAFEEWFVQHKVDVIFAGHVHAYERSYRISNVRYNVSSGDRYPVPDKSAPVYITVGDGGNQEGLAGRFTEPQPDYSAFREASYGHSTLDIKNRTHAIYHWNRNDDGKKVATDEFVLHNQYWGKNIRRRKLKKHYIRSVVGGWIAT
The following text describes a protein:
Function:
Transcriptional repressor which acts as a downstream effector of Notch signaling.
Subcellular Localization:
Nucleus.
Sequence:
MDHNMHVNAPSLHHWGYAAGPGVVMPGATATTPQSHWVPPPQSHHSAHSNHSHGHSQGHSHGIGSLKRTLSESDCDDLYSEESSKEQISPSEPGSCQLMSRKKRRGVIEKKRRDRINSSLTELKRLVPSAYEKQGSAKLEKAEILQLTVEHLKSLQSKTLDSLSYDPQRVAMDYHIIGFRECAAEVARYLVTIEGMDIQDPLRLRLMSHLQYFVQQRELSAKSCASPGGWSPAAPSSSGYQPNCAAAPYQSYAAPANPGAYVSSYPTLSASPSQQAQQLGGRTSVSRTSGSAVTESLPSHDLHSDSSSQQQQQQQQQQQQQQQHQQQQHQQQQQRTQTTPQPTQQQHYTHDHSAVHSEQQVPTYIELTNSNRPAAIGSDSLSYSAAPQYPVSGLPGQDYNNSSVLQYATPNGAKPYRPWGAEMAY