lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Promotes neurite-outgrowth. May be involved in intracellular vesicle traffic.
Subcellular Localization:
Cytoplasm.
Sequence:
MENDQFTEKQQQVTTSPTQDNQGQSKAEPVPVSQPLSPTNQTSAQPEMATCDISEELNRQLEDIIKTYGSAASLVEKEGTTAETDKPEKEDVGSMEDAECEDVNEESEKDKPAPGDASRAKEPSASKEQKLEKKILKGLGKEATLLMQSLNKLTTPEEKLDLLFKKYAELLEEHRAEQKQLKYLQKRQAQITKEKDQLQSEHSRAILARSKLESLCRELQRHNKTLKEETIQRAREEDEKRKEITNHFQGTLSEIQAQIEQQSERNMKLCQENTELAEKLKSIIDQYELREEHLDKIFKHRELQQKLVDAKLEQSQEMMKEAEERHQKEKEYLLNQAAEWKLQAKMLKEQETVLQAQITLYSERFEEFQKTLTKSNEVFATFKQEMEKMTKKMKKLEKDTATWKSRFENCNRALLDMIEEKAMRTKEYECFVLKIQRLENLCRALQEERNELYRKIKQAQLPEEVNGNDILEEDDDANTNPSSSEQASIELCAADKNMLQELAEAFRVSHKAEETLPSDGSNPETCNVQMCEAISVPELPSHLTSQPEAGNHCEQFSMSTSAPPEHMPAATENMTTLIENMPKPTKSMPMPPEMVPTPTESVPIPTEGVPTPPKIMPATPESVPTLMQNTSAPLGNMPASTKSTPKAVEHVDDIAELFIPDQPAEQKGDTDMEAVD
The following text describes a protein:
Function:
Metallothioneins have a high content of cysteine residues that bind various heavy metals.
Sequence:
MDPNCSCSTGGSCSCAGSCTCKACRCTSCKKSCCSCCPVGCAKCAKGCVCKGASDKCSCCA
The following text describes a protein:
Function:
Appears to function during host infection, and may play a role in suppressing the host immune response.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor. Secreted. Host nucleus. Host cell membrane. Host chloroplast envelope.
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:
MKYSMITLGAFAMMAVAQLSSLPACGQTCISNMLALAPTFGCTANDASCLCSDVNFAYGIRDCSNAACGAEAAGPVIAYGVEYCSSAGVGLSGSATGIDPGLGPATAVVASTPIATDGASAGSLSAITTSEFTSYVISGDSTVSTIVGSTTIYGPAAGSSSAITTSPIVSTVTSGDTSYPTTVGSTTIFGVAGVISTPTASASSALDSLSSSIASEASVITSSASAAVSSLSSRLSSAASPVSTTTSSAGGARQTAFAGLAAAAGFAAIIL
The following text describes a protein:
Function:
Chemokine-binding protein that inhibits neutrophils' chemotaxis.
Subcellular Localization:
Virion membrane; Single-pass type I membrane protein.
Sequence:
MSQGAMRAVVPIIPFLLVLVGVSGVPTNVSSTTQPQLQTTGRPSHEAPNMTQTGTTDSPTAISLTTPDHTPPMPSIGLEEEEEEEGAGDGEHLEGGDGTRDTLPQSPGPAFPLAEDVEKDKPNRPVVPSPDPNNSPARPETSRPKTPPTIIGPLATRPTTRLTSKGRPLVPTPQHTPLFSFLTASPALDTLFVVSTVIHTLSFLCIGAMATHLCGGWSRRGRRTHPSVRYVCLPSERG
The following text describes a protein:
Function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MSRLLLLCSSLLRHRAVLFSKPGHPGRLSHSESPQKKILSPTESAVGIVVFFTTFYIPAAYVLSSLKYFKGE
The following text describes a protein:
Function:
Mitochondrial RNA-binding protein required for the stability of the atp6 mRNA.
Subcellular Localization:
Mitochondrion.
Sequence:
MRNCVSPLLFAWTKHLRLREFKIPFPNRLVVRSLNQLSVHHEKVTGCRPRQASSDELHKYSKSASNEAFLSSFAENQLFHKCLPSSAGAVLSENDLMYIIRKVSEVYADNKTEKVTVPFDKHKNPFLIYVKKRFAECFDKNPDLCLIVYSKLEVETLAKITPIWINVAKKNKKEDFLVELCLRFLERFRSCNLTEQAILYQNFRENWWSNIKLPQNLKSLYVELCLVYHFHNSHLGMDSSTVSNLKRFCFSESLGHIFAPLRFQNQQLPLQHVYAFLFSIAYRDNQVDTAHFLYKQWSRAGMGPLPKDAFIKFVQLLSKNRNWVLMRDIVQLEEYNSYLLDHRIVSAFLKPLSEKGNYKDILSLISVWQHSVWRPSLAYLQVVYSFSMRALLVNRQYSSAFAFFWKIDPYIRNERLVSQMLQAASQLHYHDLILYVINTYYSGNIMKNLGNKDLICITQSSPPCNISGIKPGSLKLSPTTNTVLAKSICYWLNDAMALLFLLENQLNCKHSLFQRKSLIILLNGILNCPHSSYDLQFRAVSLLTGRIRLNVDFEVSVLASQLVFFVKHRDFKRTLITMKAISKLQKNFDVRIWNYWLVALIQQKLYSRAVKVYSKLICSSAVRNDTTRSLIRLIPKSYFKSYPLLKESETEKKTNSAL
The following text describes a protein:
Function:
Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
Subcellular Localization:
Chromosome, centromere. Nucleus. Chromosome, centromere, kinetochore.
Sequence:
MERSSTAAADLCRYMAEQRAACERQIARGHERTAAAADAFRAAIASARSLADETVAQREKLNRLKDQFRGLEAGLAEALSIQLNKGSECERTSESISSATTTNEQLNNLVMDQRTRRDEYANVISKQLEAVETLEANIDATGEKNLDEAITWYNKFLGFRVVAGEGNESFDNMVNQVSIMSDVSLLFQGVKFVFNKVNMQSPDNEYLFCMKVTKDKYSLIQCDPLLKDSEELVKDLNCTNDLFKFVRIMRARFQAAATKGVHPASSFCPDTSSITASSPPALSVDTTSESTSNQSHSRSRSKNQDMHAKRGRTPRSAASPLATPSSMRRSPRFVAVDAGNRH
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. Ubiquitination leads to cdcD/CDC48 recruitment for extraction and degradation of the incomplete translation product.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MGKDRDKGFRGAKYNPSSSGEANTLMGSQSSGFIGFSAFSSNLTNATDPDYYQVEPEYKVLLKKLQKKDSISRIKGLEELNSKFQKINIEDAEFNISSISPLMNAWEFMYKRLVNDDDRNVRDLASQCLGSIGSRIGKHLGPHVKQLLGPWIVAICDQNDQSINNALLSFQNIFPEKKRKDVFKFGHDEALTYLCENLQETPQTIGDSKSISQEILQERYERCISNSLLAIEYLINNTTATATDSSSSSSTTTTTTTTNNTGNTEIYEKIFESQFFSFFQSKSSNIRKTAYRVLTTVIKKLAGYVEKNFKDFSSKVLGLFSEKDSSTHLYMWDAIISFLQQYGDKAWSNVDVRKHVLPRLWAFLRSGCYGSFELSYPSILPLLTFIPNSIVIGSPSPSPSPSPNTNIDIGFFKELFTNLEKGLEVVDNPRQYGNPNSVDRPSNLLLSCYLECLIYSSKKWGQQYQQINDYLIDTLLFNFYNNHFNLEHSCFSEKLFIEKLLESTIKLANLSNSNLLKIQNLFNSNSFINFNNKENLLNNNEPITTDNNNNNNNNSSPIIKKQEKIIQPISKETLISRLNTFIIVCSNNNNSNNSNNNNVIQVIIKRLFNLACDNLNSNQELSIKILDFILGNYKIDQIISNGLDDIKKIITQLALALNESLLSTGGLNLGVGGDLVSVIVGLLALVPDEDEIKLIWSQILQIFLDSINNNNNNSKKKNNRSNLITNTTNSLVHLINSASNKINRNLLLSTTLFKSIKIQDKKQLQLIKSILFNNNNNNNNEFSPIIPNESVELLIKWVYNKLVDIINTMVQLNLVFNDNDKGGDNNNDDDSDDNDVSIDYLVELSKLLFSSRFKSKSLESLLIEWCKFNIEINNRPSLSGFKSKCNSIDEYLFSTTSNIENDKFILSLLIESIDRNSSTIITNDNLNLNFLSNCAIKLIKSGSYRHDENGDDDDDDDQLYSYFIKEFTSNQLVINSKDQIKISWFRYNRITPFYLLDNYGSNKDNNDSTTFSTDKLLKVLIFNFKVIESFGLEKFIKYSNKENNNSIELLLLNLLFVNGDNQLPPTPTTTTTTTTTITTAVVVSTNEQILEFIENNSTNLLNQFIESLFKFYGDEIFNCNWFNCLVSNVGGDGNNGGIYSVLLALFIDYITSDACLPTSSMKLKSALLNSIKIDNDDNGNSIDSIRQLNLVQILLPILQKESIESYKQWSINQLSQLSSSIPTNFKSISIQLSILSSIVIQRQQQQHQQSQKEQQQITQDDNEILKEKEWLTLLNLIQTIQQWNSKIKSAIIKQQEPELEFLFMKEVELSCLNFILIVIQYISNINSNKSKQPIYLSNNQSQFVQSFLSIWLSNNFTLLSFNKFKSNYYYQQYRNLIEYQSLKIYNIIISNDNIKFIIPGIGDQFQIDHSILILNNWLNRVSNSRSNNNNGNTSDSSYILELYSNTFMKMSNDIKYKISLTKLDNLIELLSTFNYSTSIYNNKGIKKTSYNLLESYFGNENTQLVKSFLLENENNNNNNNNDDGEEKVSFILFSNIFEKILLDFDSTFKPMKKSKDNQLINSISMGQLMCWNLLLLNYSKIDLNRRSILNGWLNDNNIQKVTLFLNQIFPFINKDESPLTTTTTTTDNNGNNYSIEFPFSIIDNDQLITYRMIQKLCSNCFYSLVNYLPSMVRRWADDNSTNSKMNQQIQSYITRFISPIIIQNEIQRVNSYRCTDSDSSDAKFQIKGSTSSKEVTASYEKDEMTISLVLFISDNYPLRVLTVEFSKRVGVSESQWRQWLLSMTSLLLTQDGTVLDACLLWKNSLDKHFQGVEVCPICYSMFHNGTIPKFQCKTCKNKFHAGCIYKWFQTSHKSNCPLCQTDLS
The following text describes a protein:
Function:
ATP-dependent DNA helicase involved in DNA damage repair by homologous recombination and in genome maintenance. Capable of unwinding D-loops. Plays a role in limiting crossover recombinants during mitotic DNA double-strand break (DSB) repair. Prevents crossovers between ectopic sequences by removing substrates for MUS81-MMS4 or RAD1-RAD10 cleavage. Component of a FANCM-MHF complex which promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork (Probable). Binds to flap-structured DNA but not to non-flap nicked DNA, and participates in Okazaki fragment processing by stimulating the endonuclease activities of FEN1 and DNA2. Involved in recombination donor preference during mating-type switching via interaction with FKH1.
Subcellular Localization:
Nucleus.
Sequence:
MASADDYFSDFEDDELDKLYEKAINKSVKETITRRAVPVQKDLHDNVLPGQKTVYEEIQRDVSFGPTHHELDYDALSFYVYPTNYEVRDYQYTIVHKSLFQNTLCAIPTGMGKTFIASTVMLNYFRWTKKAKIIFTAPTRPLVAQQIKACLGITGIPSDQTAILLDKSRKNREEIWANKRVFFATPQVVENDLKRGVLDPKDIVCLVIDEAHRATGSSAYTNVVKFIDRFNSSYRLLALTATPASDLEGVQEVVNNLDISKIEIRTEESMDIVKYMKKRKKEKIEVPLLLEIEDIIEQLGMAVKPVLQQAIELGIYEECDPSQINAFKAMQQSQKIIANPTIPEGIKWRNFFILQLLNNVGQMLKRLKIYGIRTFFNYFQNKCTEFTTKYNLKKSTNKIAAEFYYHPILKNIKNQCENYLSDPKFVGHGKLQCVRDELMDFFQKRGSDSRVIIFTELRESALEIVKFIDSVADDQIRPHIFIGQARAKEGFDEVKYTRKHAPKGRKKVERLHRQEQEKFLEAERTKRAANDKLERSARRTGSSEEAQISGMNQKMQKEVIHNFKKGEYNVLVCTSIGEEGLDIGEVDLIICYDTTSSPIKNIQRMGRTGRKRDGKIVLLFSSNESYKFERAMEDYSTLQALISKQCIDYKKSDRIIPEDIIPECHETLITINDENEIINEMEDVDEVIRYATQCMMGKKVKPKKAITKKKRVQENKKPKKFFMPDNVETSIVSASTLINKFLVNESGGKQLVTSNENPSKKRKIFKALDNLENDSTEEASSSLETEDEEVSDDNNVFIAEGQNGCQKDLETAIIRTGESLTTLKPLHNFERPNMALFVNDCGLPTKIEKNVKDIRGNQHNLEKEKSCTVDKNNMVLSLDDWNFFRNRYIPEGVSFDVEPNFVQYTKGVKVPHCHKVSKIITLFNDESNDNKKRTIDMNYTKCLARGMLRDEKKFVKVNDKSQVDNNSVNHDSSQSFTLSNAELDDILGSDSDF
The following text describes a protein:
Function:
Primarily acts as an independent SigF regulator that is sensitive to the osmosensory signal, mediating the cross talk of PknD with the SigF regulon. Possesses both phosphatase and kinase activities. The kinase domain functions as a classic anti-sigma factor-like kinase to phosphorylate the anti-anti-sigma factor domain at the canonical regulatory site, and the phosphatase domain antagonizes this activity.
Sequence:
MVRRRPPGRPDRAGGSGRLTLSDWDEAALEVFGTRAADFVGKIENWMKNIHPDDLAPTLSTAERAIRDHTVYEAEYRVRRLDGTYGWVRVRGRATYDEHGEPVRLVGVGWENDESRSARDALSRALRHMSDGFLAFDDEWRIIFANREAERVLGSPEDELLGRVPWALPATRRIPGMEGRLRSAVDMDEPASFDVRMPEGRRYHLRLVPGPGGRTLYITDVTQKRRLQEERQAAERAASERAAHVAKLTAALAKATTSRDVVNALAPRVLAPFAAVGLLVQTVEGESLHTVGAVGYDDGFPSSAEGLSRTSRGPRWAVVASGTPLFLSSVGELVAHSPDAPELPVRPGHESWAFLPLTASGVTFGVCVLSFDRPRLLTDDERTLLTTITALVAQSLERARLYDAEHTRSRELQRGLLPRDLPSVSACTAAARYLPAGQGMDVGGDWYDIIPLSGGQVALVVGDVMGHGLPEAATMGRLRTAVHTLADLELPPDEIMSHLNDIVGGMDEESYVTCLYALYDPTTRVCSIARAGHPPPALVLPDGSVQFPEPAPDPPLGAAEPPFETVELTVPEGSLLVLYTDGLVESSAREMDQGMRTLAGLLTTAYGAAAGEGGARLDLEHLCDTLTAGLLPADQQAADDAALLVARLHATPEEKMARWPLGDDPKTAGLARQHVREQLAAWGMDHLIPATELIVSELVGNVVRHAKGPIVLRLLYDTELICEVYDGSLTMPRIRRATDTDEGGRGLQLITALSRRWGTRYTANGKCIWTEQDLAGAENPRDDPSEALARMFPVVGDFAGDLDALPFGDQEP
The following text describes a protein:
Function:
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM12 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Subcellular Localization:
Membrane. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Sequence:
MSFIIDWNLLNDGVEAERLKLLVNDHFQEVARPSFLGKVTVMQLDFGDIPPEVTIEDICDPLADFYIQEDPAFEYEHDHIQSHSYNSRQNIDTTAASEQISVSDGIGHHGSAIYKEPSLSFDSTNNLRYVQLPPQDTDAQLELNVRYHGNMRLSISTELIVNQPTPAFMVLPLALTLTGFSFDGTAVIAYLGYAINFCFKEPLDGNSILQDMTIESEIGDRNKQVLKNVEKIERFIVQQLKSFFNDFLVFPNFHSIYLTQDDTYTECSSQHSGFNQADTGI
The following text describes a protein:
Function:
Catalytic subunit of the glycosylphosphatidylinositol-mannosyltransferase I complex which catalyzes the transfer of the first mannose, via an alpha-1,4 bond from a dolichol-phosphate-mannose (Dol-P-Man) to the glucosaminyl acyl phosphatidylinositol (GlcN-(acyl)PI) intermediate to generate alpha-D-Man-(1->4)-alpha-D-GlcN-(1->6)-(1-radyl,2-acyl-sn-glycero-3-phospho)-2-acyl-inositol and participates in the sixth step of the glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MQCVQGFVKNETFSRNRILLVAFVARITLVNFTDIDYHVFSDAAKHVSNGGSPFDRATYRYTPALAWILLPVVIFPDFGKILFCVFDILVAFLYFKIMEKDLNETKDEEARDEMEGDQTMNVVMYWLANPLTAVISARGNAESIVSAVVLLNILLLQKGHWMSAALVHGALAIQLKIYPLIYLPCVFLSLSSFGAQKGFVAKLKSLLTNWRGFAYVLVTLISYGLVVLFFYLIYGQLFLDEYLIYHIKRRDLAHNFSPYFYPLYIYEAEPVISQIIGLGAFIPQLMLTVVFAFKHYHDLPFCWFITTFAFVTYNKVCTSQYFVWYIVLLPLLAHKIMMSRKRALTLIGAWFGTQGIWLLTAYLFEFEGHDTFFLMFLASCLFLITNSIILKQIMNHYVWIGKQKTE
The following text describes a protein:
Function:
Probable methyltransferase involved in the maturation of rRNA and in the biogenesis of ribosomal subunits.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MGKEGKAGKERLDKYYHLAKQYGYRARSAFKLVQMNKRYDFLSSAHILIDLCAAPGGWCQVATKEMPVESKIFGVDLEPILPIPRCTTYVGDITTGMCFAEMKKLMKGEHADVVLHDGSPNMGKSWIQDAYTQSELCIAALKFAVTFLKKGGWFISKVFRSQDYYAILFVFEKFFKSVIATKPPASRNTSAEVYLVCKDFLAPSKYDPNLLDPKFVFAKEEETQVPDLFSTKRPKPQGYDTSKALVYNVGNAKEFLQAEDPKAWLATHTAIQFDEGLPVTEDIKGYGSDIRMLGSAELKLLLKWRDIIVKKIKKEQEEADKIKAEEEKMKMEDKILTEQEELQKELEREEEEEREEEIAKNKKTAKQKRAEEKKKRKEQRIKEGGMDIANSSGYDEVDQLFSIDDLKSQQDLDNFFNMTNPVELEEEEEQRKKEEEENEKRAEQERLEQMTYDQRLDEQFEREYKEFLERRGKVKVLAKVGEMKRSVMVQSSLNDGDIIRQADQKPREEVIEEIDDVVHQKGILSSEGKNNKEDLWWSRNGMDDISVQMGILEEVLKKDQAKEEKLKGEVKNEIDDKYEEEVQGEDQVIKEESDKEENEVVVSEDGESDEYEEAEDSNKDNESSEEDDELNWGPHMGKEKLSQALIVAGRIVKDPKQKKRLLEQHISRWTLPEDEDTPAWFRHEEEEHNKLTLPETKEEVAAMRRRLREIDSAPIKKAWEAEARKKKKLQTRMRALEQQASKIEGDGEMNSKEQLRILTKKAKKLNKKFSTHEGVRFVSSKTGKTVGGSSGRMKLVDPRMKKELRAKKRIEKGKAKKGGKGKKSFAKRR
The following text describes a protein:
Function:
Transcription factor that mediates conventional biofilm formation and plays a key role in microcolony formation under both flow and static conditions and to epithelial surfaces. Modulates infection of mammalian hosts.
Subcellular Localization:
Nucleus.
Sequence:
MTPSSTKKIKQRRSTSCTVCRTIKRKCDGNTPCSNCLKRNQECIYPDVDKRKKRYSIEYITNLENTNQQLHDQLQSLIDLKDNPYQLHLKITEILESSSSFLDNSETKSDSSLGSPELSKSEASLANSFTLGGELVVSSREQGANFHVHLNQQQQQQQPSPQSLSQSSASEVSTRSSPASPNSTISLAPQILRIPSRPFQQQTRQNLLRQSDLPLHYPISGKTSGPNASNITGSIASTISGSRKSSISVDISPPPSLPVFPTSGPTLPTLLPEPLPRNDFDFAPKFFPAPGGKSNMAFGATTVYDADESMVMNVNQIEERWGTGIKLAKLRNVPNIQNRSSSSSSTLIKVNKRTIEEVIKMITNSKAKKYFALAFKYFDRPILCYLIPRGKVIKLYEEICAHKNDLATVEDILGLYPTNQFISIELIAALIASGALYDDNIDCVREYLTLSKTEMFINNSGCLVFNESSYPKLQAMLVCALLELGLGELTTAWELSGIALRMGIDLGFDSFIYDDSDKEIDNLRNLVFWGSYIIDKYAGLIFGRITMLYVDNSVPLIFLPNRQGKLPCLAQLIIDTQPMISSIYETIPETKNDPEMSKKIFLERYNLLQGYNKSLGAWKRGLSREYFWNKSILINTITDESVDHSLKIAYYLIFLIMNKPFLKLPIGSDIDTFIEIVDEMEIIMRYIPDDKHLLNLVVYYALVLMIQSLVAQVSYTNANNYTQNSKFMNQLLFFIDRMGEVLRVDIWLICKKVHSNFQQKVEYLEKLMLDLTEKMEQRRRDEENLMMQQEEFYAQQQQQQQQQQQQPKHEYHDHQQEQEQQEQLQEEHSEKDIKIEIKDEPQPQEEHIHQDYPMKEEEENLNQLSEPQTNEEDNPAEDMLQNEQFMRMVDILFIRGIENDQEEGEEQQQQQQQQEQVQQEQVQQEQVQQDQMELEEDELPQQMPTSPEQPDEPEIPQLPEILDPTFFNSIVDNNGSTFNNIFSFDTEGFRL
The following text describes a protein:
Function:
Transcription factor that is involved in the response to heat shock, oxidative stress, and poor nutrient conditions. Controls expression of oxidative stress response genes such as ccp1, cat1, cat2, sod2; as well as of heat shock genes such as hsf1, hsp30 and hsp90. Negatively controls the expression of the fumiquinazoline (fmq) cluster via binding to the STRE motifs at the fmqA-D promoters. Plays a role in virulence.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Accumulates in the nucleus upon exposure to oxidative stress and heat shock conditions.
Sequence:
MDATYTMAQTPVQGQPSFAYYPTESQSRQQHFTSHPFEMQYYGQVSSYPQQQAQQQHSMPEQQPVYAAQPMLNMHQMATTNAFRGALSMTPIASPQPTHLKPTIIVQQDSPALMPLDTRFVSNDFYGFPSTPPLSTSGSTISSPPSSNGSLHTPINDCFFSFEKVEGVKEGCESDVHCELLANTDWSRSDSPPLTPVFIQPQSLTASQSSDLLSAQIPCPSLSPSPSPDSATFISHPQSILSAEPSGSDFCDPRQLTVESSVGAPAELPPLPTLSCNEEEPKVVLGSATVTLPVHEGLSPSFSSSSEDPLGSLPTFDSFSDLDSEDEFANKLVDFHPIGNTYFQGDKRQRLGTYLLDEDEFLSERSLEDLDDQEAFAQSGLPSVESTDFLAVEGDATQSTEEMSSKKRVTSRRSLKKASTSESSSDSLAKKTQASATSRSGHSDTTSTVQQSTASSRQNSTANTSNSESPAAPVSVNRRGRKQSLTDDPSKTFVCSLCSRRFRRQEHLKRHYRSLHTQDKPFECHECGKKFSRSDNLAQHARTHGGGSIVMGVIDTNSSNTQPAFDEPEPRALGLALYEAANAATSKSTTSESSDGTISDTSSVGGRPAKKRRRDDHV
The following text describes a protein:
Function:
Function on abscisic acid homeostasis at post-translational level, probably through ubiquitin/proteasome-dependent substrate-specific degradation.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MGLSSLPGPSEGMLCVILVNTALSISIVKGIVRSFLGIVGISLSPSSSSPSSVTVSSENSSTSESFDFRVCQPESYLEEFRNRTPTLRFESLCRCKKQADNECSVCLSKFQGDSEINKLKCGHLFHKTCLEKWIDYWNITCPLCRTPLVVVPEDHQLSSNVW
The following text describes a protein:
Function:
Acts as a component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors, like MATALPHA2, MIG1, RFX1 and SKO1. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex.
Miscellaneous:
MISCELLANEOUS: [OCT+] is the prion form of CYC8. [OCT+] is the result of a conformational change of the cellular CYC8 protein that becomes self-propagating and infectious. [OCT+]-aggregates sequester soluble CYC8, resulting in increased levels of iso-2-cytochrome c, defects in sporulation and mating, higher levels of invertase derepression and increased flocculation, reminiscent of a partial loss of function of the CYC8-TUP1 corepressor complex. [OCT+] can be cured by GdnHCl and by inactivation of the molecular chaperone HSP104, which is required for [OCT+] propagation. It is speculated that prion properties of transcription factors may generate an optimized phenotypic heterogeneity that buffers yeast populations against diverse environmental insults; MISCELLANEOUS: Present with 3890 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Domain:
The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble form, and which forms a parallel in-register beta-sheet in its amyloid form.
Sequence:
MNPGGEQTIMEQPAQQQQQQQQQQQQQQQQAAVPQQPLDPLTQSTAETWLSIASLAETLGDGDRAAMAYDATLQFNPSSAKALTSLAHLYRSRDMFQRAAELYERALLVNPELSDVWATLGHCYLMLDDLQRAYNAYQQALYHLSNPNVPKLWHGIGILYDRYGSLDYAEEAFAKVLELDPHFEKANEIYFRLGIIYKHQGKWSQALECFRYILPQPPAPLQEWDIWFQLGSVLESMGEWQGAKEAYEHVLAQNQHHAKVLQQLGCLYGMSNVQFYDPQKALDYLLKSLEADPSDATTWYHLGRVHMIRTDYTAAYDAFQQAVNRDSRNPIFWCSIGVLYYQISQYRDALDAYTRAIRLNPYISEVWYDLGTLYETCNNQLSDALDAYKQAARLDVNNVHIRERLEALTKQLENPGNINKSNGAPTNASPAPPPVILQPTLQPNDQGNPLNTRISAQSANATASMVQQQHPAQQTPINSSATMYSNGASPQLQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAHAQAQAQAQAQAQAQAQAQAQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQLQPLPRQQLQQKGVSVQMLNPQQGQPYITQPTVIQAHQLQPFSTQAMEHPQSSQLPPQQQQLQSVQHPQQLQGQPQAQAPQPLIQHNVEQNVLPQKRYMEGAIHTLVDAAVSSSTHTENNTKSPRQPTHAIPTQAPATGITNAEPQVKKQKLNSPNSNINKLVNTATSIEENAKSEVSNQSPAVVESNTNNTSQEEKPVKANSIPSVIGAQEPPQEASPAEEATKAASVSPSTKPLNTEPESSSVQPTVSSESSTTKANDQSTAETIELSTATVPAEASPVEDEVRQHSKEENGTTEASAPSTEEAEPAASRDAEKQQDETAATTITVIKPTLETMETVKEEAKMREEEQTSQEKSPQENTLPRENVVRQVEEDENYDD
The following text describes a protein:
Function:
Acts as a translational activator of mitochondrially-encoded cytochrome c oxidase 1.
Subcellular Localization:
Mitochondrion.
Sequence:
AGHSHWKNIKETKELKDAQKQKTFSLVIRKIKIAVQGNGSTNPKLNSFLAKVLEEAKAKDIPSSTINTALQRFKGPQFFVEGRALSGCSVIVESFSDKPKWFRQSVQHILKTYGGRIADAGSCCHMFDYKGVIYVPGTSTDNSRVLNYDKAFELAIEAGAEEVVEDSDENDEKIFKFICETKELHQVRKSLIDLSLHPYEARLEHIPHTFVNIEKENVDVALKLVGDLEALEDASQVFHNIQVAQT
The following text describes a protein:
Function:
Binds medium- and long-chain acyl-CoA esters with high affinity. Can interact in vitro with palmitoyl-CoA and linolenoyl-CoA. Binds phosphatidic acid (PA) and phosphatidylcholine (PC) in vitro. May play a role in the biosynthesis of phospholipids.
Subcellular Localization:
Endoplasmic reticulum.
Sequence:
MELFYELLLTAAASLLVAFLLARLLASAATASDPRRRAPDHAAVIAEEEAVVVEEERIIEVDEVEVKSARARECVVSEGWVEVGRASSAEGKLECLPEEEEAPAKAARELVLDAVLEEREEEGQVGEERCDLAAAVAEVVGVKPHELGVEAAPGEVSDVTLEEGKVQDVGVEQHDLVAEAAPREALDTGLEKQGVPIIEAVEIKRQDDLGAEVAPSDVPEVEFEQQGVRIIEAIDVNQHHRVALAAPAEVVDAGLEERVQAIEAGSSGLTSETVPEEVLDELSEKQEEQVIEEKEHQLAAATAPVAIPGVALAETEELKEEQSSEKAVNVHEEVQSKDEAKCKLHLVDQQEGSASKVELVGRNTDNVEISHGSSSGDKMIAELTEEELTLQGVPADETQTDMEFGEWEGIERTEIEKRFGVAAAFASSDAGMAALSKLDSDVQLQLQGLLKVAIDGPCYDSTQPLTLRPSSRAKWAAWQKLGNMYPETAMERYMNLLSEAIPGWMGDNISGTKEHEAGDDAVGSVLTMTSNTINQHDSQGNEDNTGMYEGHLTSSPNPEKGQSSDIPAE
The following text describes a protein:
Function:
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance.
Miscellaneous:
MISCELLANEOUS: Present with 1400 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion.
Sequence:
MISIKGTGRFLLDNYRIWQRRAFNRPIQLRKGYKVLAIETSCDDTCVSVLDRFSKSAAPNVLANLKDTLDSIDEGGIIPTKAHIHHQARIGPLTERALIESNAREGIDLICVTRGPGMPGSLSGGLDFAKGLAVAWNKPLIGVHHMLGHLLIPRMGTNGKVPQFPFVSLLVSGGHTTFVLSRAIDDHEILCDTIDIAVGDSLDKCGRELGFKGTMIAREMEKFINQDINDQDFALKLEMPSPLKNSASKRNMLSFSFSAFITALRTNLTKLGKTEIQELPEREIRSIAYQVQESVFDHIINKLKHVLKSQPEKFKNVREFVCSGGVSSNQRLRTKLETELGTLNSTSFFNFYYPPMDLCSDNSIMIGWAGIEIWESLRLVSDLDICPIRQWPLNDLLSVDGWRTDQL
The following text describes a protein:
Function:
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments.
Sequence:
MATTVHPIPPPFFSPYLDDQCNKINAKPVPWEGYQRAKLLSADELSLLKSLSKLPSAQRPTVLATQGPQYAKLYIDLLRKLQRVDTVQAVLVSISDMLADNSTIPYFHNLASPEHPDDPYGPIVKCLSMDEEFPVLGSLRILSLLIATDPKPFPNDLVPTLLSSLQKLLNGSRLPLWEVAAQVLGAVLGTKQFRKFVWNEENCLSGLIKSLKTNPNPQAQYWAITCLWQLSFEKEVAENLDKKYDVVAILTDIAKAAVKEKVTRVVVATFRNLLAIAPSQNLPSMFVTKLLPFIVSLQSRKWSDEEIVEDLDYLKDELKSRLDGLSTYDEYVKELESGHLVWSPAHETDDFWKENGIRIGQEEGGKAVKRLVELITTSKDPLVLAVATHDIGQFVKYGGDRSKQIIDNLHGKTRVMELMSHENADVRYQALMTVQRLMSQHWSK