lhallee/plat_data huggingface dataset:
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:
MRTSKVEAPEAIAQCVPHYEVRARHVFSGSTTFQGEAVEMPSDGGQKWELRYIGRWERKKMSEHVGSAPLGVPFRSQIAVSVGQNVRAFLGTLGFRHSYRYMRLGTRWQFPNGITIEATRMKALKNEDEKDEYRLVDLENLRVEALLVEIFALTTDEKIDEASQKIRRFAVDLDPYFIERPSEGKEILHSTATLAAEVRRKRPRQ
The following text describes a protein:
Function:
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MFATRSFCLSSSLFRPAAQLLRPAGRSTLRNVWRRSIATEHLTQTEANSRLASQRVHRPNSPHLTIYEPQLTWYLSSLHRITGCVVAGTLYAFAMGYLVAPLAGYSLDTATISGLIQQVPTWIKVPAKFVISYPLTFHIFNGIRHLIWDTTKELSLKGVYRTGYAVLALSVLTSGYFAMI
The following text describes a protein:
Function:
Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Also reduces cellular toxicity and caspase-3 activity.
Subcellular Localization:
Cytoplasm, perinuclear region. Nucleus. Cytoplasm, myofibril, sarcomere, Z line.
Sequence:
MVDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGSHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFDDFFGNRRGPRGSRSRGAGSFFSAFSGFPSFGSGFPAFDTGFTPFGSLGHGGLTSFSSASFGGSGMGNFKSISTSTKIVNGKKITTKRIVENGQERVEVEEDGQLKSLTINGVADENALAEECRRRGQPTPALAPGPAPAPARVPSQARPPTPAPTPAPAQTPAPSVSTRPQKPPRPAPTAKLVSKSNWEDEEQDRQRVPGNCDAPMTSAGLKEGGKRKKQKQKEDSKKKKSTKGNH
The following text describes a protein:
Function:
Involved in proteolysis and elastolysis (degradation of the host protein elastin). Has staphylolytic activity (degrades pentaglycine cross-links in cell wall peptidoglycan), preferring Gly-Gly-|-X substrates where X is Ala or Gly. Enhances the elastolytic but not proteolytic activity of elastase (lasB) and elastolytic activity of other proteases. Degradation of host elastin is likely to contribute to the pathogenicity of P.aeruginosa. While either His-317 or His-356 can abstract a proton in the hydrolysis reaction, the same residue performs both functions in a given catalytic cycle, with the other stabilizing the catalytic intermediate.
Subcellular Localization:
Secreted. Note=Secreted in an Xcp-dependent fashion (a type II secretion pathway).
Sequence:
MQHKRSRAMASPRSPFLFVLLALAVGGTANAHDDGLPAFRYSAELLGQLQLPSVALPLNDDLFLYGRDAEAFDLEAYLALNAPALRDKSEYLEHWSGYYSINPKVLLTLMVMQSGPLGAPDERALAAPLGRLSAKRGFDAQVRDVLQQLSRRYYGFEEYQLRQAAARKAVGEDGLNAASAALLGLLREGAKVSAVQGGNPLGAYAQTFQRLFGTPAAELLQPSNRVARQLQAKAALAPPSNLMQLPWRQGYSWQPNGAHSNTGSGYPYSSFDASYDWPRWGSATYSVVAAHAGTVRVLSRCQVRVTHPSGWATNYYHMDQIQVSNGQQVSADTKLGVYAGNINTALCEGGSSTGPHLHFSLLYNGAFVSLQGASFGPYRINVGTSNYDNDCRRYYFYNQSAGTTHCAFRPLYNPGLAL
The following text describes a protein:
Function:
Plays a role in innate immunity against the oomycete pathogen A.arabidopsidis (Hpa).
Subcellular Localization:
Nucleus membrane; Single-pass membrane protein.
Domain:
The KASH domain, which contains a transmembrane domain, mediates the nuclear envelope targeting and is involved in the binding to the SUN proteins.
Sequence:
MGRNLGSAFRQELANLDKDPDSHKTAMSNLRSIVKDLDAKVVHVFVAQLSDVKEIGLESGGYTVSLFEDLARAHGVKIAPHIDIIMPAIIRTLSSSEGSLRVQQACSRAVAAMARYGIDPTTPEDKKTNVIHSLCKPLSDSLIDSQHQQHLALGSALCLKSLVDCDNWRSASSEMVNNVCQSLAVALEATSSEAKSHMALVMALSKHNPFTVEAYARLFVKSGLRILDLGVVEGDSQKRLLAIQMLNFLMKNLNPKSISSELELIYQEMEKYQKDQHYVKMAAHETMRQAERLICEADPMFDAENCKPRNSLSGSVKSTSSLREHDGSVYSRQDRSYVNDQDEYDVLFSGVASGRTLVSGSPLVTFGDNNQETGFVIESPRIGDQIQCSGVENGNIESVWFHQRNRSSEFNESVCSRTNRSRSSRRNTKKRQSGDICSKHHRHGFAQDPFTELLDNRQQLLQYSETSSSSSIYDTSGTTTPTNTTEDICEKPKTDLDSEAKLKTVETELDPRLGRSKGVLKLGLSVFSIAVAGFASFMWMYLQDDMMPPHLVPT
The following text describes a protein:
Function:
Dual specificity mitochondrial citrate and methylcitrate synthase with similar catalytic efficiency with both acetyl-CoA and propionyl-CoA.
Miscellaneous:
MISCELLANEOUS: Citrate synthase is found in nearly all cells capable of oxidative metabolism.
Subcellular Localization:
Mitochondrion.
Sequence:
MVQRLLPGAHICRRSFNSSAIIKSSALTLKEALENVIPKKRDAVKKLKACYGSTFVGPITISSVLGGMRGNQSMFWQGTSLDPEHGIKFQGLTIEECQNRLPNTGIDGDNFLPESMLWLLMTGGVPTFQQAASFRKELAIRGRKLPHYTEKVLSSLPKDMHPMTQLAIGLASMNKGSLFATNYQKGLIGKMEFWKDTLEDSLNLIASLPLLTGRIYSNITNEGHPLGQYSEEVDWCTNICSLLGMTNGTNSSNTCNLTSQQSLDFINLMRLYTGIHVDHEGGNVSAHTTHLVGSALSDPYLSYSSGIMGLAGPLHGLAAQEVVRFLIEMNSNISSIAREQEIKDYLWKILNSNRVIPGYGHAVLRKPDPRFTAMLEFAQKRPIEFENDKNVLLMQKLAEIAPKVLLEHGKSKNPFPNVDSASGILFYHYGIRELLFFTVIFGCSRAMGPLTQLVWDRILGLPIERPKSLNLEGLEALTKASNVNKL
The following text describes a protein:
Function:
Has both L-asparaginase and beta-aspartyl peptidase activity. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine (By similarity). May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions.
Miscellaneous:
MISCELLANEOUS: In vasectomized rats, autoantibodies against Asrgl1 are present.
Subcellular Localization:
Cytoplasm. Note=Midpiece of sperm tail.
Sequence:
MATARPSSCGRDSVPATPRASIDVSLVVVVHGGGASNISPGRKELVSEGIAKAATEGYNILKAGGSAVDAVEGAVTMLENDPEFNAGYGSVLNADGDIEMDASIMDGKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGRGAEKFAADMGIPQTPAEKLITERTKKHLEKEKLEKGAQKADCPKNSGTVGAVALDCKGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLGAVSTTGHGESILKVNLARLALFHVEQGKTVDEAATLALDYMKSKLKGLGGLILINKTGDWVAKWTSASMPWAAVKNGKLQAGIDLCETKTRNLPTC
The following text describes a protein:
Function:
High affinity abscisic acid (ABA) transporter that mediates the export of ABA, with a preference for (+)-ABA, through the plasma membrane, especially in vascular tissues (e.g. phloem companion cells), and is involved in the intercellular ABA signaling pathway. Together with ABCG31, export ABA from the endosperm to deliver it to the embryo via ABCG30 and ABCG40-mediated import to suppress radicle extension and subsequent embryonic growth.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSAFDGVENQMNGPDSSPRLSQDPREPRSLLSSSCFPITLKFVDVCYRVKIHGMSNDSCNIKKLLGLKQKPSDETRSTEERTILSGVTGMISPGEFMAVLGPSGSGKSTLLNAVAGRLHGSNLTGKILINDGKITKQTLKRTGFVAQDDLLYPHLTVRETLVFVALLRLPRSLTRDVKLRAAESVISELGLTKCENTVVGNTFIRGISGGERKRVSIAHELLINPSLLVLDEPTSGLDATAALRLVQTLAGLAHGKGKTVVTSIHQPSSRVFQMFDTVLLLSEGKCLFVGKGRDAMAYFESVGFSPAFPMNPADFLLDLANGVCQTDGVTEREKPNVRQTLVTAYDTLLAPQVKTCIEVSHFPQDNARFVKTRVNGGGITTCIATWFSQLCILLHRLLKERRHESFDLLRIFQVVAASILCGLMWWHSDYRDVHDRLGLLFFISIFWGVLPSFNAVFTFPQERAIFTRERASGMYTLSSYFMAHVLGSLSMELVLPASFLTFTYWMVYLRPGIVPFLLTLSVLLLYVLASQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGYYVNKVPSGMVWMKYVSTTFYCYRLLVAIQYGSGEEILRMLGCDSKGKQGASAATSAGCRFVEEEVIGDVGMWTSVGVLFLMFFGYRVLAYLALRRIKH
The following text describes a protein:
Function:
In tachyzoites, required for the cellular trafficking of guanylate cyclase GC and UGO to the cell membrane. May play a role in the folding of the GC P-type ATPase-like domain to sense vacuolar changes in phosphatidic acid and pH levels which trigger parasite egress.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Note=In intracellular tachyzoites, localizes to the apical cap, to the cytoplasm in disperse foci and to the residual body.
Sequence:
MGENSTTGLRGQADVSQFSDAAVEPTLSSPPTGQRQQSLPLFGEETCSISSAPSVGGGGGWPFQRQGSSRLTSRGTSLSSCSDAGSGLGALRQREDSFPEYHGVGLPLGGKYALDGTGLVLAPRVPFIFSHQLPSLTGLDEAGFSDTRKVPSTYQALAARFVHQVHQEAGNGMYPLWSAGVVLRLCLLGALFFVSVGAWLIFEDEQHVECKLNYAEKTLQEGSSRYLLKGISSAHCTREVNELKGEEISVYAEMGHFFQNDAQVLWSRNDRQLAGKIFTDPKDVRECEPLATAVVGNVTKVLHPCGALAWAVFTDKYQFLEGTPEGDNDQVPMKPIPLNQTQAVLLHSWPWQDMYKNPPAEDRAAVLDKVYFWMSPVDNDDGEDMYKTREEARAELLMDRLNYEEAGEMVENGHFIQWMQTAALGTFRKLYGSLEGPLKLPVSAHITVMYDVSSWKGKKAIVLVQKSRLGGRSLFIGIAYLSFGCLLTMLVFYMLWKKWQYRREGEEIRDLRWQTKTRGSKKTK
The following text describes a protein:
Function:
Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Sequence:
MLAGEHSGDLLGGELIRELKKNFSDLETFGVGGERMIEEGFTSIESMEELSIIGFSAILFKYRFLKSLIGRLINLAVEKNCSHAILIDYPGFNLRLAKELKKLGITVIFYVSPQLWAWKFDRIYTIRDNIDLMLVLFPFEKQIYDRYGVPCEFVGHPLAVRLREKIRKEAVIPEPEDKTQFHFTITLMPGSRSGEIRRILNDLLQSAGQLADHYENNNKKIRFLLPNINQKEEVFILEKIELAKSKFPNLTIEYLFDRSLRAIEISDLVLVASGTATLEVAYFEKPMIILYKVSMFTYIIGSLFIQTPNIGLVNILSGQEICRELIQAECSPNNIVEETLALLENKKYRNKIIEDVRKVKEALGSENSSRYASREITKLIKGIAKKTGQELGNPEQQI
The following text describes a protein:
Function:
Involved in biosynthesis of legionaminic acid (5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonic acid)(Leg), a sialic acid-like derivative that is incorporated into flagellin via O-linkage to Ser/Thr. Catalyzes the condensation of 2,4-diacetamido-2,4,6-trideoxymannose with phosphoenolpyruvate (PEP) to give N,N'-diacetyllegionaminic acid.
Sequence:
MKKTLIIAEAGVNHNGDLNLAKKLIEIAADSGADFVKFQSFKAKNCISTKAKKAPYQLKTTANDESQLQMVQKLELDLKAHKELILHAKKCNIAFLSTPFDLESVDLLNELGLKIFKIPSGEITNLPYLKKIAKLNKKIILSTGMANLGEIEEALNVLCKNGAKRQNITLLHCTTEYPAPFNEVNLKAMQSLKDAFKLDVGYSDHTRGIHISLAAVALGACVIEKHFTLDKNMSGPDHKASLEPQELKMLCTQIRQIQKAMGDGIKKASKSEQKNINIVRKSLVAKKDIKKGEIFSEGNLTTKRPANGISAMRYEEFLGKIATKNYKEDELIRE
The following text describes a protein:
Function:
An NAD-dependent ADP-ribosyltransferase (ADPRT). Catalyzes the transfer of the ADP ribosyl moiety of oxidized NAD (NAD(+)) onto eukaryotic elongation factor 2 (eEF-2) thus arresting protein synthesis. Has an LD(50) of 65 ng/ml against the human lung epithelial cell line C38.
Domain:
Domain I (which is divided into 2 non-contiguous regions Ia and Ib) is required for binding to cells, but not for ADPRT activity (Probable). A subtilisin-digested fragment starting about residue 417 and extending to the C-terminus has full ADPRT activity.
Sequence:
MHLTPHWIPLVASLGLLAGGSFASAAEEAFDLWNECAKACVLDLKDGVRSSRMSVDPAIADTNGQGVLHYSMVLEGGNDALKLAIDNALSITSDGLTIRLEGGVEPNKPVRYSYTRQARGSWSLNWLVPIGHEKPSNIKVFIHELNAGNQLSHMSPIYTIEMGDELLAKLARDATFFVRAHESNEMQPTLAISHAGVSVVMAQAQPRREKRWSEWASGKVLCLLDPLDGVYNYLAQQRCNLDDTWEGKIYRVLAGNPAKHDLDIKPTVISHRLHFPEGGSLAALTAHQACHLPLETFTRHRQPRGWEQLEQCGYPVQRLVALYLAARLSWNQVDQVIRNALASPGSGGDLGEAIREQPEQARLALTLAAAESERFVRQGTGNDEAGAASADVVSLTCPVAAGECAGPADSGDALLERNYPTGAEFLGDGGDISFSTRGTQNWTVERLLQAHRQLEERGYVFVGYHGTFLEAAQSIVFGGVRARSQDLDAIWRGFYIAGDPALAYGYAQDQEPDARGRIRNGALLRVYVPRSSLPGFYRTGLTLAAPEAAGEVERLIGHPLPLRLDAITGPEEEGGRLETILGWPLAERTVVIPSAIPTDPRNVGGDLDPSSIPDKEQAISALPDYASQPGKPPREDLK
The following text describes a protein:
Function:
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MANMMMMSSSKALITSSSTIPPSPRFKLSLAQIPFPKLPLPKSPKSHKPLTLPSNLNTISVILASSLAIAPPSLAEEIEKASLFDFNLTLPIMMAEFLFLMFALDKIYFSPLGKFMDERDSAIKEKLNSVKDTSVEVKQLEDQAAAIMKAARAEISAALNKMKKETQLEVEQKIAEGRKRVEAELQEALASLESQKEETIKSLDSQIAALSDEIVKKVLPVSN
The following text describes a protein:
Function:
The phosphorylation of phosphatidylinositol (PI) to PI4P is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3) (By similarity). Undergoes autophosphorylation and phosphorylates serine/threonine residues of protein substrates.
Sequence:
MSRNLDSPVQTQMAVAVFKTPLTGASKMEGKQHHKHQHLQRQSSGRRVFVQTETGCVLGMELDRSDNVHTVKRRLQIALNFPTEESSLTYGDMVLTNDLSAVRNDSPLLLKRNFMHRSSSTPCLSPTGRDLQQKDRSGPIEILGHSDCFSIVKHMVKDIVKAMKMGVEPLPVHSGLGGAYYFRNKRGESVAIVKPTDEEPFAPNNPKGFVGKALGQPGLKSSVRVGETGFREVAAYLLDYGRFANVPPTALVKITHSVFNVNDGVKGNKPREKKLVSKIASFQKFVAHDFDASDHGTSSFPVTSVHRIGILDIRIFNTDRHGGNLLVKKLDGVGMFGQVELIPIDHGLCLPETLEDPYFEWIHWPQASLPFSDEEVDYIQSLDPVKDCDMLRRELPMIREACLRVLVLCTIFLKEASAYGLCLAEIGEMMTREFRPGEEEPSELEVVCIEAKRSVTERDVFSPRSDVVGEAEFQFDLDCDDLESVYSSKIQLTDDYFTKNPFSNGRSSLGKLEESIKEEEEDEEEEEDKTENTVPMIIMKDSFFSSAAFHDKAPSLSKLSTSMKNTHLSDTTRKNPKPLTRGKSENTSSGHKSANEQLPVSASFVKVADMKEDEWVLFLERFQELLGPAFAKRKTATLSKRQRLGTSCQF
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.
Subcellular Localization:
Secreted.
Sequence:
MAANLKFLIVVAAAAATVSVSDAQLSSTYYDGTCPTVFDMVKSVVRSAINREKRVGASIVRLFFHDCFVNGCDGGLLLDDNLPAFESEKNALPNKNSARGFEVIDKIKAATENVCKGVVSCADILAIATRDSVVELGGPSWQVLVGRRDARTANKQAADTDLPPFSANLTLLINMFQQKNFTARELVALSGAHSIGMARCTTFRDHLYNNTNLDPIATTDLKANCPQSGGDDNLVGLDHQSPNRFGNNYFQGLMKKRGLLNSDQVLFNAGSTDDVVRTYGDNAQMFSDEFASAMVKMGNMNPLTGSNGEIRTNCRKIN
The following text describes a protein:
Function:
Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
Sequence:
MMDYAEEGQPRKRQRIRRGAAGVAGRGAAAEPAAGGTRAEPRPQYPYQMRDGVIYAPWRTEPAAADFGGGGGSGGIGGAVTGGGAGGGVTGGGAGGRTGGGVTGGGGSRRPERRPDPDGGRAAKEVIVVSDSSDENGDEEEAERGAGRGRRRLPPGLERYGPPRIRVHVVERGESEIHKKIAAALRAHGHDAAGVDVKPAIPAAAAAAAAAAAAAAPVGAAAGGGAGDGAGGGAGGGAGGGAAAAAAADAGAAADGPATRTRLHTRTSSRMAAAAITNAAIGAKRAARSARAQAGGGGGGGGGGGGGGAAVPGAAGAAGAARAAAGAAGAAGAAGAAAVNDGAGPSSAGAAAAAAAAAAAAAAAAGGSAGAAAAGGGAGPSGRGGAGGSGAAGGSGGSGGAGGSGPLQTCGICLDEQPPSEFHTISACGHRFCRGCLSRHVQLAARERVFPVRCPQPGCRGPGVGVAEGMALLTEPADRDKLQMLEVESSLPAHLKFYCPNPACSLLMVLDEDPPVENLPVRCHGCRKQLCARCRVVWHSGLSCAQHRALEEAQGAAGGGGGDTAALGALAGERGWKPCPQCRALVELAHGCNHITCKCGAEWCYKCGALWRRPAAGAAGGSRVRAMPTCSCRLWDDSNRQLEAEFRQRWYERHGLAPDAARRRAVNELQNMGILPRAAAAAAAAGGAAGAAAVPAAAAPAAAAAAGGGGGGGGRQVVHIRIPRDVRWLGGAPDGGGGHVPAELEARLRRLGVYDMLMEVAGDVRRQLRQEQQAAVGGGAAAAAGRRVLGRRTRVGVVKQEPGLEEQGQPGPGGGAAAAAGGGGGGAGGAGGAGGGGGGGGGGRANDALDDAAVEAAVRQLINGYRFLVVAAADALERGDGPGHVAVARMRQHGRWVIERALRRAALMAPPPPPVGLQAAAAAAAAGAAAAAAAAAGEGAQARRADAGGARGFDLAQAMWDLFVEPVEADTDGDNVIARYNRRREPAAAAAGAAAATGAAAAAAAAGPARARAAAEVEAAEAKAANAQDRYRRAVQELEDPEPLPRIRGRADVAGGAAAAAAAAERKQRALAALEAARRRAAAARLGKQELEDPEPLPRIRGRADVAGGAAAAAAAAERKQRALAALEAARRRAAAARLGKQGPAAAAAAAAPQTRAAESVNGPGARRAAAAAGGGGAAAAGSAGEVMQTRRPARPVPAGLGAGAGLGERPRRRRGGGGGGGGGGGSDSDGGGWLEWGFEDVCLQLEVAERAGRTAAGDAGGTSRAGAEGDSRTAAAAAAGRRSAAAAAAAAAHGSAGAARHGVKQEQQSAAAAGAEQGPNRFVDFLAGMLFQDAGNAARRGGGGAGAAAGAPAAAVPPAQPPPAAAAAAAAAAGAAAKSAAARRRRRSPAPFSAAAALPARVRHDARAGRPGAAGGGAGGPGGAGGSGGGSSNSSSEDELGRMLRLIGDTSSSDDDGNDGAGAGGAGGAAAAAAGGAKRTQFVPLPAPAAGGGPGDRRRRRRAIRRGAAGGDTALDAIPVYGSDDDDDALLGGPGAPELAAAAPPPPPVQNPAAAAAAPPPAAAAKARGGAAGGGGGGDGGADGEARDDDGGVAAGQRSLARAQAAVADAHARARERHQAIAEQMRARVEVLLEAAARARAEAERVRVEAETVRAEAHGVRAEAHGVRAEGLRAGRQLHRASPAAANTRGSAGKGAECGAGLAAPGAPAAAAAAANDIPPPQPAPDVLPLLNVPLPPPLPLPHGGIGDEFDDALNAFQEAVAAPAAGGVQGMFDQFDRMMEEARVEGEALLQADVAALQQQLWGPLPGRLLAQPPPPPAAAAPAAVAQPPPAAPAAPQAPAAPPARPAAAGAAQAAAADDGSRPRDEVMERRKRWMEEQAGQRAAAREAQVQLARQQAAAQAAGVGARAAAAVRERMAKLAGGAGAPAAPAVPAAGGGAGGAGEGGRGAAGGQLPRAGAPHIRLRGPDPALDVFMHWRGSGPGVAVRVGAGARPGAAARVGAGAGAGAGAGAGAGAGGVAGGAAAGNTAAAGGAAAAGGAASTGGAAAAGGAPAAGGAPAAGAAAAAGGAAGGAAAAGAAGCVPALLGFWRDDRAVRMRLREAWNRIGFPDIHDIGGDEVWETGRSGAAAAPAAAAGAPPPPNAAAPAAGGDENAERAAKRRRLNPGAAAAPAPAAAAAAPAPVVLQVVVQVVHPGGVAGIAPEALAALQEQLQGLLQQLQTQGQGAAAAAGSGAAAAAGAAGLPGGGNGAAGSGGVLVAPVLVLPPAPQPAVQGPQPAMQGPQPLLLVPPPAAPAAAAEAGAGASATAAPAAAGAAVAPAAVAEPQPNEAVAAAPAAAAAAAAAAGFGAGDGAEQSHP
The following text describes a protein:
Function:
Required for the proteolytic cleavage of the transcriptional repressor RIM101 in response to alkaline ambient pH, which is necessary for sporulation and invasive growth.
Miscellaneous:
MISCELLANEOUS: Present with 784 molecules/cell in log phase SD medium.
Sequence:
MSLLRLWNKESRAPSKIKSHGIVGSYGNSMLAHNNVKQFRIDIDEPHRVWKPNESITGEAVIDIKRDITNVAIKLSLVCEVRVKTGNSPTSKNKRIEKTLEKSTFLYGQDYVKTAFSAKEKKPHVDKTTILNGLSKGEHRFPFRIRIPRGRGMLSSIKFERGSITYFLSCTLESLNNINGLKKPEARCEREFAVIVPLDVSRLPKPKTKTVVLQSASMVQNKKNKSTEDESSSYTQLTQKSTTSNSSSSSVNSKTSPLPNKTVTISVDIPQAGFMIGEIIPIDVKIDHYKPFYAPAGLTTTLVRICRVGGAGKDDPMETFRKDICQSISPIYINPETLQFQSRVYLKVPLDAFSTLTTVGKFFSFQYYIEVMVNLSKKNVVYTESNRIIGTPIGEQNGLGVENNINRIQRKMLRMVNPETLENDSEGYESSIFFKDMVNVEKLKRLRNVTGMSIETVIGTTRSEQQQSDASIPSQSSITAPQNSPSNLRDWLAPLNAYDSDDVPVPKYSPNDKVSVPSEDKQELEQKRLQQLESDPPPCDDY
The following text describes a protein:
Function:
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Endomembrane system; Multi-pass membrane protein.
Sequence:
MNIIGKLFMLFISASLINNIVFMRFLALCPFVGMSTQIETSIGMGAAVTFVMVMASVVTFFIYYYILVPLNLLFLRTISFILVIAVLVQLVEMVIKKFLSSLYKAMGIYLPLITTNCAILGVTLLNINYGHNLIEAIVYSLGVSLGFTIALILLASIRDRLSYSEIPEFWKGYPIVFISAGLLALIFLGFQGLAH
The following text describes a protein:
Function:
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs, the first step in 5-carboxymethoxyuridine (cmo5U) biosynthesis. May be part of an alternate pathway, which is able to bypass cmo5U biogenesis in a subset of tRNAs under aerobic conditions.
Sequence:
MPVLHNRISNDALKAKMLAESEPRTTISFYKYFHIADPKATRDALYQLFTALNVFGRVYLAHEGINAQISVPASNVETFRAQLYAFDPALEGLRLNIALDDDGKSFWVLRMKVRDRIVADGIDDPHFDASNVGEYLQAAEVNAMLDDPDALFIDMRNHYEYEVGHFENALEIPADTFREQLPKAVEMMQAHKDKKIVMYCTGGIRCEKASAWMKHNGFNKVWHIEGGIIEYARKAREQGLPVRFIGKNFVFDERMGERISDEIIAHCHQCGAPCDSHTNCKNDGCHLLFIQCPVCAEKYKGCCSEICCEESALPPEEQRRRRAGRENGNKIFNKSRGRLNTTLCIPDPTE
The following text describes a protein:
Function:
Promotes the transport of cholesterol across mitochondrial membranes and may play a role in lipid metabolism, but its precise physiological role is controversial. It is apparently not required for steroid hormone biosynthesis. Can bind protoporphyrin IX and may play a role in the transport of porphyrins and heme. Was initially identified as peripheral-type benzodiazepine receptor; can also bind isoquinoline carboxamides.
Subcellular Localization:
Mitochondrion membrane; Multi-pass membrane protein.
Sequence:
MRLKRRRDLPAAPAESARRGAVRWPSGEGAAAGRPARARARGRQRPEAGAPGPAGLWAARPGLPAKPGGAGRAGQGGPREGLPPPAAQCPSWSRVLVVAELSGTAAAAAMAPPWVPAVGFTLLPSLGGFLGAQYTRGEGFRWYASLQKPPWHPPRWILAPIWGTLYSAMGYGSYMIWKELGGFSKEAVVPLGLYAGQLALNWAWPPLFFGTRQMGWALVDLLLTGGMAAATAMAWHQVSPPAACLLYPYLAWLAFAATLNYRMWQDNQVRRSGRRLSE
The following text describes a protein:
Function:
Probable FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of 5-hydroxy-2-hydroxymethyl-1,4-pyrone, also know as kojic acid, a by-product in the fermentation process of malting rice that acts as a chelation agent. Glucose might be converted to kojic acid by a combination of dehydrogenase and dehydratase reactions involving kojA and probably additional enzymes. Improves the antioxidant capacity via the accumulation of kojic acid that is also a strong oxidant.
Sequence:
MRVATQLRVGIVGGGWNGCHLALELKKQGHRVSLFEQKPDIFQGVSGNFGIRLHKGPHYPRSKATRDSCREALVKFCETYPELVVHHESAIYAHGEADALGNPSKVSDEAFRDVCYESPECTAVDPKANGFQGLISAYNLDEPSVAIGDRLRNTFKEKLGRAGIYVHLNATVDRIIHTEDTNRIQTGDGQYVFDVVINATGYTSLLPQNIADALPVDIGITYQTCIALVYEDQQPQEKPLSFIVMDGWFPCVMPAIDTNEPLQKKYILTHGSYTILGSFDRHEEGQELLDSLDEEAIAARIKPHCEREITRFWPGFLDRFQYRGWKGSVLAKLKTTSEFRSSLTFEKDGVIHIFPGKVSNVVTAAEEVVPLINDIARRRHGVVREWNGVRFTVSSAFHTHSKEIGDKPGLGEHHTSNLQTYVSLVTAN
The following text describes a protein:
Function:
Forms an efflux pump with AaeA. Could function as a metabolic relief valve, allowing to eliminate certain compounds when they accumulate to high levels in the cell. Substrates are p-hydroxybenzoic acid (pHBA), 6-hydroxy-2-naphthoic and 2-hydroxycinnamate.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MGIFSIANQHIRFAVKLATAIVLALFVGFHFQLETPRWAVLTAAIVAAGTAFAAGGEPYSGAIRYRGFLRIIGTFIGCIAGLVIIIAMIRAPLLMILVCCIWAGFCTWISSLVRIENSYAWGLAGYTALIIVITIQPEPLLTPQFAVERCSEIVIGIVCAIMADLLFSPRSIKQEVDRELESLLVAQYQLMQLCIKHGDGEVVDKAWGDLVRRTTALQGMRSNLNMESSRWARANRRLKAINTLSLTLITQSCETYLIQNTRPELITDTFREFFDTPVETAQDVHKQLKRLRRVIAWTGERETPVTIYSWVAAATRYQLLKRGVISNTKINATEEEILQGEPEVKVESAERHHAMVNFWRTTLSCILGTLFWLWTGWTSGSGAMVMIAVVTSLAMRLPNPRMVAIDFIYGTLAALPLGLLYFLVIIPNTQQSMLLLCISLAVLGFFLGIEVQKRRLGSMGALASTINIIVLDNPMTFHFSQFLDSALGQIVGCVLAFTVILLVRDKSRDRTGRVLLNQFVSAAVSAMTTNVARRKENHLPALYQQLFLLMNKFPGDLPKFRLALTMIIAHQRLRDAPIPVNEDLSAFHRQMRRTADHVISARSDDKRRRYFGQLLEELEIYQEKLRIWQAPPQVTEPVNRLAGMLHKYQHALTDS
The following text describes a protein:
Function:
Gustatory and odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. Gr21a and Gr63a together are sufficient for carbon dioxide detection and avoidance behavior. It is possible that the CO(2) receptors Gr63a and Gr21a activate the TRPC channels through Galpha49B and Plc21C. This innate olfactory avoidance behavior can be inhibited by inhibitory interactions of the odors such as 1-hexanol and 2,3-butanedione with Gr21a and Gr63a.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MRPSGEKVVKGHGQGNSGHSLSGMANYYRRKKGDAVFLNAKPLNSANAQAYLYGVRKYSIGLAERLDADYEAPPLDRKKSSDSTASNNPEFKPSVFYRNIDPINWFLRIIGVLPIVRHGPARAKFEMNSASFIYSVVFFVLLACYVGYVANNRIHIVRSLSGPFEEAVIAYLFLVNILPIMIIPILWYEARKIAKLFNDWDDFEVLYYQISGHSLPLKLRQKAVYIAIVLPILSVLSVVITHVTMSDLNINQVVPYCILDNLTAMLGAWWFLICEAMSITAHLLAERFQKALKHIGPAAMVADYRVLWLRLSKLTRDTGNALCYTFVFMSLYLFFIITLSIYGLMSQLSEGFGIKDIGLTITALWNIGLLFYICDEAHYASVNVRTNFQKKLLMVELNWMNSDAQTEINMFLRATEMNPSTINCGGFFDVNRTLFKGLLTTMVTYLVVLLQFQISIPTDKGDSEGANNITVVDFVMDSLDNDMSLMGASTLSTTTVGTTLPPPIMKLKGRKG
The following text describes a protein:
Function:
G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
RYDIMNFQRSNETGYEFVLVGTWGDDGLRMISEPQWRDAQDGVPVSRCSTPCPKGHLQESTLNLCCWKCIECGDYQYVATPYRCLDCEEGMWPNANHDGCDSIPQKYLQWTETASIIVMVVCSFVMLSTGAVATIYIRYITTPLIKASSRELSFVVLLGILCATASTFAVLAKPTPIVCAIERFMPAFGVATIHAAIFTKTNRIARILAVKESKMFSRKRRFMSTTSQLVITGLLILGQAIVSGTMLAIEPPGAQDFFAAPNQVSLICNTSELANFLGLSYDFLLILLCTVWAVKTRNVPENFNEAKMIGFAMYATVVIWIAYLAVYCGSERNRELSLCLAMNVSSFMVLMFLFIPKIYIVLFHPEKNV
The following text describes a protein:
Function:
Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein; Intermembrane side.
Sequence:
MLRTILRPSTSTFHNKNPLQLILLNSRRRQPYSVQQQPQPPTNPTVISQYRDRQQAEFRARNRSLLLYAISIGVVTLGLSYAAVPLYRAFCSATGYNGTPSTSSSRDGTGKFAPDRIAQPVGQKTITVRFNADKSDTLDWKFWPCQKSLTVKPGETVLAFYKAKNLSDHDLLGVATYNVTPGQVAPYFAKVECFCFDEQRLLAGEEVDLPIFFFIDKDFVEDPLMKDIDDIVLSYTFFKAKRNSYGFLEPDIPANSPHLSGFGNHPTAAPATPSPHIRPSNPTNNTTSTLTKP