lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Sequence:
MFPLLGLFGGTFDPIHKGHLALANELIQKLPSLTEIQFIPSRQPPHRPSPLASPADRLEMIKRAIANQPNLILNDVEIKGNDISYTINTLKILRPLFLTHALCFILSTDAFADFKHWHQSSVILEYCHLIVVNRPNYRLPQQPWLSDLLSHHQTENAEDLGRFQFGKIFFQTLSPRPISATQIRHYLAKGDYEIVAPLLPKTVLTYIKAHKLYQQ
The following text describes a protein:
Function:
Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Microsome membrane; Multi-pass membrane protein.
Sequence:
MADKIKTPRTSELEFGGPMGALLLLFVMPGTVLYLLVTCNTDDASVLRVPGPWPSLDTLWDPSAVILLLAWVSLQALLHILPIGKVTEGITLRDNTRLKYRINALQAMMVTALLVAGAVMFGFPFSYVYDHFLQLAVAAAFIALVLSIFLYAKSLAAPESALAPGGNSGNPLYDFFIGHELNPRIGSFDLKYFCELRPGLIGWCLINLCFMMKEVELRGSPSLSMMLVFGFQALYVADAMKNEEAILTTMDIVHDGFGFMLAFGDLCWVPFTYSLQGYFLVRHPQELGTYTALGIILLNAVGYIIFRGSNSQKNAFRRNPSDPKVAGLATIPTATGKRLLVSGWWGLVRHPNYLGDLIMALAWSLPCGLSNILPYFYIIYFTVLLVHREARDEHQCMKKYGLAWQEYCRRVPYRIFPYIY
The following text describes a protein:
Function:
Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MPDASLHPSDRQAERSWSLPAGMQIAAECRSPVRHPFCQTDARERTNCNPTEPKPTKSMTFAQSQSALDHAGVGAESIAELFWVMLIGGTLIWLIVVGLAVYAMVVPGEHDQKKTRMLVIGGGAVFPTIVLTALLTYGLAMLPELQRPAPEGSQVVEVSGVRWWWRVNYRMPDGKKIETANEIHLPVNEPVEFKLKSEDVIHAFWIPSLGGKVDMMPGRENRLKLHPTRVGVFRGVCAEYCGEAHTQMAFDVIVQSREEFDAWLHQQALPAVSGSDVAEAGREVFEAAGCGACHAIRGTSADGVVGPDLTHFGSRRSIGASVLPNNADNLTRWIKETHRVKPGVEMPAFEAFADDELRSLVRYLGELK
The following text describes a protein:
Function:
May play a role in carrying and orienting carbohydrate, as well as having a more specific role.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MKGFLFLLFTISLLIMIQIQTGVLGNHTISTSKKPRSGSPAFGSLAGGSILFFLTNTLIQLFHLT
The following text describes a protein:
Function:
Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway.
Sequence:
MASTSNQPQSFVAITGSSTSSCGYCHASSDSSHSFGLWAYRLTPSVYQNLIDHGWRRSGKYLYKPTLTTTCCPAYTIRLNAGSSSVSKGQKKVLKKMKRYLNSGKGIVAKDEENEMSKVGPREQFMIPASDIPTAIDTAAWIHADTARSDVSNPKNKTRFEQESAQHLGSTISVLIHETESIANQHSHQLKVVLEVASFTQATFELYKKYQIAVHNDPPSRLNPEQFTQFLVDTPICTELIPETDFKSTTSQLACWNDPTHSIQPQPSYGSFHQKYYMDDKLIAVAVLDILPRCVSSVYFMYDPAFGFLSLGTYSALREIALTKWLSDTMPRGLDYYYMGYYIHSCIKMRYKAAYKPSQILCPETYKWVDLSQATRLLDLRKDTALVDCKNKTEGDTEDAAIQPRPIRDVLHVDIPTNVIEKSVALVGRKLVPLNMLGPKHKLVIQVKEFSTRVNPSTLLDQLVFVAT
The following text describes a protein:
Function:
Transcription activator that acts as a positive regulator of seedling photomorphogenesis. Acts downstream of COP1 and play an important role in early and long-term adjustment of the shade avoidance syndrome (SAS) responses in natural environments.
Subcellular Localization:
Nucleus.
Sequence:
MKIRCDVCDKEEASVFCTADEASLCGGCDHQVHHANKLASKHLRFSLLYPSSSNTSSPLCDICQDKKALLFCQQDRAILCKDCDSSIHAANEHTKKHDRFLLTGVKLSATSSVYKPTSKSSSSSSSNQDFSVPGSSISNPPPLKKPLSAPPQSNKIQPFSKINGGDASVNQWGSTSTISEYLMDTLPGWHVEDFLDSSLPTYGFSKSGDDDGVLPYMEPEDDNNTKRNNNNNNNNNNNTVSLPSKNLGIWVPQIPQTLPSSYPNQYFSQDNNIQFGMYNKETSPEVVSFAPIQNMKQQGQNNKRWYDDGGFTVPQITPPPLSSNKKFRSFW
The following text describes a protein:
Function:
A acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MDPADYRALHESQMENNNGTTAVNVFMHIAPPVFSVFHTVQLIAVASITHVPLRFLVEFCLIVLPFVLLVTVLHRLALNIALTLFVLSAISAVHQIRNRLHLMPFVQVPGKSPQFLTCVRALVNLTTAVCILAVDFHCFPRELAKTETFGYGLMDIGVGLYVFSNGIVYKVRPAEERRLNTARVWKVLISTAPLLLLGFGRFFLTNELDYQLHVSEYGVHWNFFITLACVKFAGTLTMDLVHDPEVIKFVAITLLCCHEMMLHLGVSRYVLSADTQRTTFFAANREGIVSLPGYLALFLASIYIGWVVRPTEEITVAKKFLRRAGKVAIMAAVCWKMIYVCEDMFGISRRLANMGYCFWILAIGASVTALFMFFELFVYFVRFEEPKSPDQIMKTDDFCIPYVPLVLQAINANGLFFFLIANLLTGLVNLVFQTFLLGNGAALTIIGYYMFMLCVAVCFLYVNNVKLKIW
The following text describes a protein:
Function:
Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MSRQDVQRLLEEYQLIGELLSSLQAQHATVAELLEELTTALDGVRLLKGEGGERLVHIGAGLFVKGVFEAKEVLAPLGAGYHAFLDLNNAERILQERIEEYSKLKTSLEENIEKLAERAAQIRQALERLGIR
The following text describes a protein:
Function:
Has growth inhibitory activity.
Subcellular Localization:
Secreted.
Sequence:
MMAPAHDGFCVLCLIFVILSLVLVQTASSLPHQSRRGPHWVECTTPDRALAIQSLTPNRHVGRCPPPPDQIPDDACSQCGCRSDRVCPVEQKCCFNGCQYTCMNPVKPPPAFDWLNEPMRQRTSGNAWLITGPEKTHTVESCSTSTFDEGDGILLECPTGYQCYITYGGDAENNIPNKGICIQIK
The following text describes a protein:
Function:
Functions as a component of the DNA-binding general transcription factor complex TFIID, the RNA polymerase II associated general transcription factor complex TFIIF, and the chromatin-remodeling complex SWI/SNF. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. TFIIF is essential for the initiation of transcription by RNA polymerase II. TFIIF functions include the recruitment of RNA polymerase II to the promoter bound DNA-TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for non-specific DNA, allowing for the subsequent recruitment of TFIIE and TFIIH, and facilitating RNA polymerase II elongation. TAF14 acts as a chromatin reader that specifically recognizes and binds histones that are acylated. Recognizes and binds histone H3 acetylated or crotonylated at 'Lys-9' (H3K9ac and H3K9cr, respectively), with some preference for crotonylated lysine. Component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. Component of the NuA3 histone acetyltransferase complex. The NuA3 HAT complex has 2 functionally distinct forms. NuA3a binds H3K4me3, through the PHD finger of YNG1, and acetylates H3K14 at the promoter region of actively transcribed genes to promote transcription initiation. NuA3b binds H3K36me3 at the coding regions of actively transcribed genes, through the PWWP domain of PDP3, and coordinates transcription elongation. Does not bind DNA.
Miscellaneous:
MISCELLANEOUS: TAF14 is the only non-essential TAF; MISCELLANEOUS: Present with 3100 molecules/cell in log phase SD medium; MISCELLANEOUS: There is no homolog of TAF14 present in the TFIIF complexes of higher eukaryotes.
Subcellular Localization:
Nucleus.
Domain:
The YEATS domain specifically recognizes and binds acylated histones (acetylated and crotonylated). Binds crotonylated lysine through a non-canonical pi-pi-pi stacking mechanism.
Sequence:
MVATVKRTIRIKTQQHILPEVPPVENFPVRQWSIEIVLLDDEGKEIPATIFDKVIYHLHPTFANPNRTFTDPPFRIEEQGWGGFPLDISVFLLEKAGERKIPHDLNFLQESYEVEHVIQIPLNKPLLTEELAKSGSTEETTANTGTIGKRRTTTNTTAEPKAKRAKTGSASTVKGSVDLEKLAFGLTKLNEDDLVGVVQMVTDNKTPEMNVTNNVEEGEFIIDLYSLPEGLLKSLWDYVKKNTE
The following text describes a protein:
Function:
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface. Involved in assembly of monomeric PSII from the CP43-less intermediate.
Subcellular Localization:
Cellular thylakoid membrane; Single-pass membrane protein.
Sequence:
MQVNNLGFIASILFVLVPTVFLLILFIQTGKQSES
The following text describes a protein:
Function:
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Subcellular Localization:
Cytoplasm.
Sequence:
MSSKEQKTPEGQAPEEIIMDQHEEVEAVEPNDSAEQVDPRDEKIANLEVQLAEAQTRERDTVLRIKAEMENLRRRTEQDIEKAHKFALEKFVNELLPVIDSLDRALEVADKANPDMAAMVEGIELTLKSMLDVVRKFGVEVIAETNVPLDPNVHQAIAMVESEEVPAGNVLGIMQKGYTLNGRTIRAAMVTVAKAK
The following text describes a protein:
Function:
Phosphorylates the splicing regulator TIA1, thereby promoting the inclusion of FAS exon 6, which leads to an mRNA encoding a pro-apoptotic form of the receptor (By similarity). Required for the biogenesis of some mitochondrial-encoded mRNAs, specifically stabilizes ND6 (NADH dehydrogenase complex subunit 6) mRNA, and regulates its levels.
Subcellular Localization:
Mitochondrion matrix. Note=Colocalizes with mitochondrial RNA granules.
Domain:
The RAP domain is essential for RNA-binding.
Sequence:
MLRILLSAQTSPARLSGLLLIPPVQPCCLGPSKSGDRPFGGGPVQGLQRLLEQARSPGELLRWLSQNPTKVRAHHYPVALRRLGQLLVSQPRPSPVEQATLQDLSQLIIRNCPSFDVHTIHVCLHLAVLLGFPSDGPLLCALEQERRSRLPPKPPSPHRPAIYGGQRLEVALSCPRFLQYPRQHLIRSLAEARPEELTPHVMVLLAQHLARHRLREPQLLEAIAHFLVVQEAQLNSKVVQKLVLPFGRLNYMPLEQQFMPCLERILAREAGVAPLATVNILMSLCQLQCLPFRALQFVFSPSFINHINGTPPSLIVRRYLSLLDTAVELELPGYQGPRLPQRQRVPIFPQPLITDRARCKYSHKDMVAEGLRQLLGEENYRQNLTVPPGYCTDFLLCVSSSGAVLPMRTQDPFLPYPPRSCQQDQANFNSTTQDPAQRVVLMLRERWHFCRDGRVLLGSRALRERHLGLMGYQLLPLPFEELESQRGLPQLKSYLRQKLQALGFRWGPEGG
The following text describes a protein:
Function:
Transfers mannosyl residues to the hydroxyl group of serine or threonine residues.
Subcellular Localization:
Endoplasmic reticulum. Membrane; Multi-pass membrane protein.
Sequence:
MRRKSSPTFGKQQKAGAPQPHHTPAGFPVADYFAVALTAAAVFANSLNGDFVYDDHQAIVTNPDVVSPSFSLTNDFWGGPISSKGSHKSWRPLTTLSFRANYLLHGLKPFGFHFVNVILHVVCSMLVLRLVQRTVKGRGARLFAALLFAVHPVHCEAVAGIVGRADLLATLCVLTGLAVDRSLPYTAALTVVGLACKETAIVLPVLIGVRKVIDRRKLSSIAPLAVLTLLLCYARLSIQGFEQPTFSLADNPAAHHPSFVVRSLTFWTLPMLHSWLLVWMTSRHWSEVSLPIVVHILKLISNNLQELSFDWSMDAVPLVLTPLDYRFILSLIAYGILATVTLRALRNLTAGDRQDTSPDGLLFSLSILVLPHALLSSNLLTYVGFVIAERVLYLPSVGFCLVAGMGVEWILKRYPKSTSSVLVLLAVLLSLLAARTVARNEEWSDDVRLFDSAVDINPAKAFANLGHVLARRGRSDEAEEAYLKALSRRPNMAETHYNLGVLFFERGNLSAAVGYYRQAIRLRPSFAVAHLNIGIALQSLGRKAEAAAAFKVCSRVDATSSKAAVTQMSALSSCSFNLGSLLAANGDHRAAVNAFKLALSTAPPSYSSLPSIWTMLGESYAELGLDRQAESCYADALASDPHHSPALITAAQLRLRQNRSSDALSLLQRAATTAPNSSAVHLHLGLALQKAVLSTLAAQLHLNKNYAEAETLYDEAIRLDPSDAVSRENREKLRRILAKLMSWLVGVVSTGSLVFVALSMVYIASMVNDVQSLQEEVTVNMDEFKVMAEDTWSRLVKMHVNPTGSSDAPPTFATLLGRNKRQANSQCNCGPSSRGCPAGPPGPPGQPGERGRDGNPGQSGRPGANGIALAVTFDTPGGCVKCPPGPPGPDGEPGFPGPAGQPGQPGLAGPAGNPGRDGQPGAPGNNGEKGRDGQPGRPGSDGQPGVQYTPGEAGRDGAPGRPGPQGPAGQPGQDGAPGQDGQPGENGRDGQPGQDGQSGQPGEQGSDGLPGADAAYCPCPSRTSSYSEPVHAAPVETAYPAPAPGYRA
The following text describes a protein:
Function:
Catalyzes the CoA-dependent transfer of an acetyl group to the 6-O-methyl position of a range of galactosides, glucosides, and lactosides. May assist cellular detoxification by acetylating non-metabolizable pyranosides, thereby preventing their reentry into the cell (Probable).
Subcellular Localization:
Cytoplasm.
Sequence:
MNMPMTERIRAGKLFTDMCEGLPEKRLRGKTLMYEFNHSHPSEVEKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVIREINDRDKHYYFKDYKVESSV
The following text describes a protein:
Function:
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer (Probable). Important for hyphal growth and conidiophore development but not pathogenicity.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Cell septum. Cell tip.
Domain:
The N-terminal myosin motor-like domain (MMD) does not seem to have motor activity but is indispensable for polarized cell wall synthesis via binding to actin that ensures the proper localization to the hyphal tips and septation sites near actin structures.
Sequence:
MAAPSPAGGAPSHAQSSLPSLPAHLQSDTHLTAHLASRFHVGLPTARLSSQALISLNTYTTSTKGPDGGKEGSAMGEAEDLAKRAFTRLGARGENQAVVFLGESGSGKTTIRSHLLSAFLSFSSTPLSSKLSYAAFLFDTLTTTKSLTTQTASKAGLFLELQYDGSSSVNPTLIGGKIIDHRLERSRITSVPTGERSFHVLYYLLAGTSPAEKAHLGFDKAVHVSTSSGAIGHKRWRYLGHPTQLKVGVNDVEGFQHFKTALRKLEFPRSEIAEICQILATILHIGQLEFASGQATTTHAEESGGYSHEGGETVTIVKNKDVLSIIAAFLGLSVEDLENSFGYRTKTIHRERVTVMLDPKGARQNADELARTIYSLLVAYVIEAVNQRICAAEDSVANTISIVDFPGFAQACATGSTLDQLFNNAATELLYNFCLQSFFDRKADELEREEVSVPATSYFDNTDAVRGLLKHGNGLLSILDDQTRRGRTDNQLLESLRRRFENKNPTIIVEGSKRTSLISQNARSAFTVKHFAGEIDYSVNGLIEENGEFISGDLMRLMKSTKSDFVRELFGQAALQTVTHPKEKTAIMQAQVSSKPLRMPSMARRKTSPSSRLAFDAGDADEVESQAESIAKDSSSGRRKSAMLTSGIQGAAGQFLSSLDIVNKCLSSTNLNPYFIFCLKPNDRRIANQFDSKCVRAQVQMFGIAEISQRLRNADFSVFLPFAEFLGLAEIGNIVVGSDKEKAEVVLDEKRWPGNEARVGSTGVFLSERCWADLAKVGERVVPVYAADMSDEGGDGLLHPRSTGYGDSKVRLLNPADQSPGAFIYGDEAKQGYFGSRDLDGRSDAGNSAFNSGDMFRNHETREQMLEKGNEKKMEEVDDAPISGSRKRWIALVYLLTFYIPDFAIKLFGRIKRKDVRMAWREKFAINLIIWFSCGVAIFFIVAFPGLVCPTQHVYSAAELSSHNGKDGHSSFIAIRGVVFDLDKFMPGHYPHIVPESALKKYAGVDATGLFPVQVSALCQGKSGSVDPMVLLDYRPTNISGSATTISGTDTNSVYHDFRHFTNDSRPDWFYEQMVMLKANYLKGYVGYTPKYLNTLGKKSQSIGSINGKVYDLTSYIAGGRLTKAPPGETVPSDVDTDFMDNSVVSLFQSLPGQDLSKHWENLKIDPALRRRMQLCLDNLFFVGHVDTRNSAQCEFARYFILAISVLICSIIVFKFLAALQFGRKNVPENLDKFIICQVPAYTEDEESLRRAIDSMARMRYDDKRKLLVVICDGMIIGQGNDRPTPRIVLDILGVPESVDPEPLSFESLGEGQKQHNMGKVYSGLYEVQGHIVPFLVIVKVGKPSEVSRPGNRGKRDSQMVLMRFLNRVHYNLPMSPMELEMHHQIRNVIGVNPTFYEFILQVDADTVVAPDSATRMVAAFLNDTRLIGVCGETALTNAKNSAVTMIQVYEYYISHNLTKAFESLFGSVTCLPGCFTMYRIRSAETAKPLFVSKEVVDAYAEIRVDTLHMKNLLHLGEDRYLTTLLLKHHSKYKTKYISSAKAWTIAPESWTVFLSQRRRWINSTVHNLIELIPMQQLCGFCCFSMRFVVFVDLLSTVIQPVTLAYIIYLIYWLVKDTSTIPYTSLILLAAIYGLQALIFIIRRKWEMVGWMIVYLLALPVFSLALPLYSFWHMDDFTWGNTRIITGEKGRKVVISDEGKFDPASIPKKKWEEYQTELWEAQTSRDDRSEVSGISYGTKSYHPAQSEYGFPGSRPMSQLDLPRFGSRMSLAPSEMMSRHADMEMENLSHLPSDDAILAEIREILRTADLMSVTKKSIKLELERRFGVNLDLKRPYINSATEAVLAGAL
The following text describes a protein:
Function:
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Domain:
Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
Sequence:
MYFKQEDIDKLLDNLRIEEVVGEFIELKKVGSSYRGLCPFHADTNPSFFVTPEKKICKCFVCGSGGNAINFYSKIKNISYTEAIRELSQKYRINIKEYKNTNTNENYEKFYQIMEDSHNFFMEKIFSQDSRGALEYLSNRGLDTNLIKEHQLGYAPPKWSELYELLNAKGYSDEDLLALGLIKKSEEGRIYDAFRNRIIFPIFSPSGRIIAFGGRTLEKDTSVPKYINSPDTPIFKKGKNAYGIERAVNIKNKNYSILMEGYMDVLSANIYGFDTSIAPLGTALTEEQAQLIKRYSSNILLSFDMDKAGISATERASFILKSQGFNIRVLQFEESKDPDEFLKKNGREAFLKVVENSLEIFDFLYNLYSSEYDLNNNIIAKQNFVERFKDFFSNVDNDLEKEMYLKKLSEKIDISIDVLRKTLVEQNKKHVTRKDYLDENQEKIEKKEFKQANNLEMAIVKMLLRKPEYYNFFKKEKLESDIANKIFKFFNQKIKENLFFDSNIIMKEFKKYVEESNDFSQYEKNNELARIIMDYILIPNKIEEERENIELFKSYLRVKLKLRDKTKDNIAKKIEFGKLKKEIAKAKSVEEFIKVYNSFKYLF
The following text describes a protein:
Function:
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Sequence:
MTDVRGELLQQIKDKAVVHGKVTLSSGLEADYYVDLRRITLDGEAAPLVGQVLLDLTADLEFDAVGGLTMGADPVAASMLHAAAARGRRLDAFVVRKTAKAHGLQRRVEGPEIKGRRVVVVEDTSTTGGSPLTAVEAVREAGAEVVAVATIVDRATGAGEKIQDGAGVPYLYAYGKDELGLD
The following text describes a protein:
Function:
Involved in beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Sequence:
MHHLNRLDTKMALLEVKDLQVRVEEREILHGLTLTVNEGEVHAIMGPNGSGKSTLSHVIAGKPGYEVTGGQILFKGEDLLEMAPDERAAKGVFLAFQYPVEIPGVATMTFLRTALNAQRKARGESEYSTPDFLKKVREVSKSLNIPQDMLKRGVNVGFSGGEKKRNEVLQMALFEPSLCILDEMDSGLDIDALRIAADGVNALRAPKRAMVVITHYQRLLNYIVPDFVHVMSKGRVVKSGGKELALELEDSGYAQFEDA
The following text describes a protein:
Function:
May regulate the transcriptional function of androgen and estrogen receptors.
Sequence:
MAPSEDPRDWRANLKGTIRETGLETSSGGKLAGHQKTVPTAHLTFVIDCTHGKQLSLAATASPPQAPSPNRGLVTPPMKTYIVFCGENWPHLTRVTPMGGGCLAQARATLPLCRGSVASASFPVSPLCPQEVPEAKGKPVKAAPVRSSTWGTVKDSLKALSSCVCGQAD
The following text describes a protein:
Function:
A probable intramembrane site-2 protease (S2P) that cleaves type-2 transmembrane proteins within their membrane-spanning domains. Cleaves PbpB (PBP3, FtsI) near 'Ala-102' and 'Ala-103' in response to oxidative stress; cleavage is inhibited by Wag31-PbpB interaction. Probably also cleaves anti-sigma factors RskA, RslA and RsmA but not RsdA; Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal (possibly oxidative stress) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein (includes anti-sigma factors RskA, RslA, RsmA, and PbpB in M.tuberculosis) is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, this entry), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein (ECF sigma factors SigK, SigL and SigM).
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MMFVTGIVLFALAILISVALHECGHMWVARRTGMKVRRYFVGFGPTLWSTRRGETEYGVKAVPLGGFCDIAGMTPVEELDPDERDRAMYKQATWKRVAVLFAGPGMNLAICLVLIYAIALVWGLPNLHPPTRAVIGETGCVAQEVSQGKLEQCTGPGPAALAGIRSGDVVVKVGDTPVSSFDEMAAAVRKSHGSVPIVVERDGTAIVTYVDIESTQRWIPNGQGGELQPATVGAIGVGAARVGPVRYGVFSAMPATFAVTGDLTVEVGKALAALPTKVGALVRAIGGGQRDPQTPISVVGASIIGGDTVDHGLWVAFWFFLAQLNLILAAINLLPLLPFDGGHIAVAVFERIRNMVRSARGKVAAAPVNYLKLLPATYVVLVLVVGYMLLTVTADLVNPIRLFQ
The following text describes a protein:
Function:
Catalyzes the conversion of chorismate to isochorismate.
Sequence:
MKQLSGLLGELRQKLCAGFPEQAGIQQLIFPAPGLVGRQLLEWLTAQTHFPQFYWRHRDNHEEAAVCGQTRSFADMKDADDFIQQNPDANGLRIWGLNAFEPVMVFGQLTDNGLVSGKNAQASFLFLPRLEILRRGKKTSLTLNLSSETSLQKDALQAITFIDQLMAARALPVLNARIQHSSHTPGYPQWRNLIQQALNDIEQQKLDKVVLARTTTLTLNKPLSCAAFMAASRQVNHRCYHFMLRFDDRQAFLGSSPERLYLRQQLHLETEALAGTVSNLDSDPQAAVLADWLMHDEKNQRENLLVVDDICQRLQGGVTAVDVMPPEIIRLRKVQHLRRRICAQLSRASDTDCLQRLQPTAAVAGLPREAARQFIAKHELFSRGWYAGSAGYLSLKRTEFSVALRSARVDGQQIHLYAGAGIVAGSDAEQEWQEIDNKSAGLQSLLEHEAQPVKA
The following text describes a protein:
Function:
Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has also a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides. Involved in lifespan determination in a ubiquinone-independent manner.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MERVVGVVFRRLGSSSRVFRRGQGEQLQSLPVNITTVRWCSASIVVDNEEKAMLDRIIRVDHAGEYGANRIYAGQMAVLGRSTAGPIIQHMWNQEKEHLKKLNELMVSNRVRPTILMPLWNVAGFALGAGTALLGKRGAMACTVAVEASISEHYNSQIRTLMESDPEKHQALLQTIKKFRDEELEHHDTGLEHDAEQAPGYFLLKNAIQLGCRAAIFLSERV
The following text describes a protein:
Function:
Involved in the maturation of specific proteins in the endoplasmic reticulum. Required for maturation and transport of active lipoprotein lipase (LPL) through the secretory pathway. Each LMF1 molecule chaperones 50 or more molecules of LPL (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAAPRESLRRRKAGAGDPEPEAPPGQGRDLKGRPARLRAGTFWLTRIVLLRALAFVYFVAFLVAFHQNKQLIGDRGLLPCRAYLQSVQRHFGGRVSWDALSYAPTILWLLDWSHMDANLDALALLGLGISSFILVSGCANMVLMAALWVLYMSLVNVGQIWYSFGWESQLLETGFLGIFLCPLWTLSALPRGTPTSWVVMWGFRWLIFRIMLGAGLIKIRGDRCWRDLTCMDFHYETQPVPNPVAYFLHRSPWWFHRFETLSNHFLELVVPFFIFLGRRMCIVHGALQVLFQVVLIISGNLSFLNWLTIVPSLACFDDATLGGLFPSGPGRLKDQVLKIQEEETRGARAPRTRGSVARGTVNLALGILVAWLSIPVVLNLLSPRQVMNSSFNPLRIVNTYGAFGSITRERTEVILQGTASANASAPDSAWEDYEFKCKPGDPRRRPCLISPYHHRLDWLMWFAAFQTYEHNEWIIHLAGKLLANDAQALSLLARNPFEGRDPPRWVRGEHYRYKFSRPGGRHAAEGKWWIRRRLGPYFPPLSRQDLRGYFTSRQWPYPEPE
The following text describes a protein:
Function:
Potassium channel regulatory subunit that modulate the delayed rectifier voltage-gated potassium channel activity of KCNB1 and KCNB2 by altering their kinetics, expression levels, and shifting the half-inactivation potential to more polarized values. While it does not form functional channels on its own, it can form functional heterotetrameric channels with KCNB1 and KCNB2. Each regulatory subunit has unique regulatory properties that can lead to extensive inhibition, significant changes in kinetics, and/or substantial shifts in the voltage dependencies of the inactivation process.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTRLSLRDLSETDFEDNEISINVGGFKKKMRSNTLLRFPETRLGKLLSCHSKESILELCDDYDDTKNEFYFDRNPELFPYVLHFYNTGKLHVMGELCVFSFSQEIEYWGINEFFIDSCCSYSYHGRKMEPDQEKWEDNSDQESTTSSFDEILAFYNDAAKFDNQPFGKIRRQLWLALDNPGYSVLSRIFSVLSIVVVLGSIITMCLNSLSDFQIVNKKGDLEEDPRFEIVEHFGIAWFTFELVARFAVAPNLLKFFKHALNLIDLVSILPFYITLIVNLVVESSPTLANLGRVAQVLRLMRIFRILKLARHSTGLRSLGATLKYSYREVGLLLLYLSVGISIFSVVAYTIEKEENRALETIPACWWWATVSMTTVGYGDVVPVTTAGRLTASACILAGILVVVLPITLIFNKFSHFYRRQKQLESAMRSCDFGDGMKVVPSVNLRDYYAYKVKSLMASLTNMSRSTPSELSLNDSLH
The following text describes a protein:
Function:
Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Capable of regulating both type I apoptotic and type II autophagic cell death signals. The former involves caspase activation, chromatin and mitochondrial condensation while the latter involves caspase-independent cell death in conjunction with accumulation of mature autophagic vesicles, plasma membrane blebs, and nuclear condensation without DNA degradation. Mediator of anoikis and a suppressor of beta-catenin-dependent anchorage-independent growth of malignant epithelial cells. May play a role in granulocytic maturation (By similarity). Regulates granulocytes motility by controlling cell spreading and polarization.
Subcellular Localization:
Cytoplasm. Cytoplasmic vesicle, autophagosome lumen.
Domain:
The autoinhibitory domain sterically blocks the substrate peptide-binding site by making both hydrophobic and electrostatic contacts with the kinase core.
Sequence:
MVQASMRSPNMETFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVCREEIEREVSILRQVLHPNIITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDTQQAMVRRESVVNLENFKKQYVRRRWKLSFSIVSLCNHLTRSLMKKVHLRTSEDLRNCESDTEENIARRKALHPRRRSSTS