lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in callose synthesis at the forming cell plate during cytokinesis. During plant growth and development, callose is found as a transitory component of the cell plate in dividing cells, is a major component of pollen mother cell walls and pollen tubes, and is found as a structural component of plasmodesmatal canals (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSATRGGPDQGPSQPQQRRIIRTQTAGNLGESFDSEVVPSSLVEIAPILRVANEVESSNPRVAYLCRFYAFEKAHRLDPTSSGRGVRQFKTALLQRLEREHDPTLMGRVKKSDAREMQSFYQHYYKKYIQALHNAADKADRAQLTKAYQTANVLFEVLKAVNLTQSIEVDREILEAQDKVAEKTQLYVPYNILPLDPDSANQAIMRYPEIQAAVLALRNTRGLPWPEGHKKKKDEDMLDWLQEMFGFQKDNVANQREHLILLLANVHIRQFPKPDQQPKLDDQALTEVMKKLFKNYKKWCKYLGRKSSLWLPTIQQEMQQRKLLYMALYLLIWGEAANLRFMPECLCYIYHHMAFELYGMLAGNVSPMTGENVKPAYGGEEDAFLRKVVTPIYEVIQMEAQRSKKGKSKHSQWRNYDDLNEYFWSVDCFRLGWPMRADADFFCLPVAVPNTEKDGDNSKPIVARDRWVGKVNFVEIRSFWHVFRSFDRMWSFYILCLQAMIIMAWDGGQPSSVFGADVFKKVLSVFITAAIMKLGQAVLDVILNFKAHQSMTLHVKLRYILKVFSAAAWVIILPVTYAYSWKDPPAFARTIKSWFGSAMHSPSLFIIAVVSYLSPNMLAGVMFLFPLLRRFLERSNYRIVMLMMWWSQPRLYVGRGMHESAFSLFKYTMFWVLLIATKLAFSYYIEIRPLVAPTQAIMKARVTNFQWHEFFPRAKNNIGVVIALWAPIILVYFMDSQIWYAIFSTLFGGIYGAFRRLGEIRTLGMLRSRFESLPGAFNDRLIPDGKNQQKKKGIRATLSHNFTEDKVPVNKEKEAARFAQLWNTIISSFREEDLISDREMDLLLVPYWADRDLDLIQWPPFLLASKIPIALDMAKDSNGKDRELKKRIESDTYMKCAVRECYASFKNIIKFVVQGNREKEVIEIIFAEVDKHIDTGDLIQEYKMSALPSLYDHFVKLIKYLLDNKEEDRDHVVILFQDMLEVVTRDIMMEDYNISSLVDSSHGGTWHGGMIPLEQQYQLFASSGAIRFPIEPVTEAWKEKIKRIYLLLTTKESAMDVPSNLEARRRISFFSNSLFMDMPMAPKVRNMLSFSVLTPYYTEEVLFSLRDLETPNEDGVSILFYLQKIFPDEWNNFLERVKCLSEEELKESDELEEELRLWASYRGQTLTRTVRGMMYYRKALELQAFLDMAMHEDLMEGYKAVELNSENNSRGERSLWAQCQAVADMKFTYVVSCQQYGIHKRSGDPRAQDILRLMTRYPSLRVAYIDEVEEPVKDKSKKGNQKVYYSVLVKVPKSTDHSTLAQNLDQVIYRIRLPGPAILGEGKPENQNHAIIFSRGEGLQTIDMNQDNYMEEALKMRNLLQEFLTKHDGVRHPSILGLREHIFTGSVSSLAWFMSNQETSFVTIGQRLLANPLRVRFHYGHPDVFDRLFHLTRGGVSKASKVINLSEDIFAGFNSTLREGNVTHHEYIQVGKGRDVGLNQISMFEAKIANGNGEQTLSRDIYRLGHRFDFFRMMSCYFTTVGFYFSTLITVLTVYIFLYGRLYLVLSGLEQGLSTQKGIRDNTPLQIALASQSFVQIGFLMALPMLMEIGLERGFRTALSEFVLMQLQLAPVFFTFSLGTKTHYYGRTLLHGGAKYRSTGRGFVVFHAKFADNYRLYSRSHFVKGLEMMLLLVVYQIFGSAYRGVLAYLLITISMWFMVGTWLFAPFLFNPSGFEWQKIVDDWTDWNKWINNIGGIGVPAEKSWESWWEEEQEHLRYSGKRGIVVEILLALRFFIYQYGLVYHLTITEKTKNFLVYGVSWLVIFLILFVMKTVSVGRRRFSASFQLMFRLIKGLIFMTFIAIIVILITLAHMTIQDIIVCILAFMPTGWGMLLIAQACKPVVHRAGFWGSVRTLARGYEIVMGLLLFTPVAFLAWFPFVSEFQTRMLFNQAFSRGLQISRILGGHRKDRSSRNKE
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 (By similarity). Plays a role in proper central nervous system (CNS) development in vertebrates.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MFPLVKSALNRLQVRSIQQTMARQSHQKRTPDFHDKYGNAVLASGATFCIVTWTYVATQVGIEWNLSPVGRVTPKEWRNQ
The following text describes a protein:
Function:
Ribosomal protein P0 is the functional equivalent of E.coli protein L10.
Sequence:
MQFDKPAHQKKAEYIKKLHGLFRKYHKVAVVTAQNVTSNQLMKIRAGVSGFAEVLFGKNSLMRRAVDELKDEIPSITELEKNLSNGAGLIFTNGSFKAIKEVIDANCLGSAAKPGSIAPCDVFIKPQRTSISPTDIKVLHALNIQCKVFKGTIEITGEKQLIWEGQKVGASEANILGMLGILPFNYTLKIEALYDNGSMYDPSFLSISDDYLAQKFTEGLCNVTCVALGMHYPCVASTPHMIRSAFTDIASIAISINHEMRQIETLQKLLADPEALANLANTAETSGKDKKAEEHHEEEEAIEIGPFSFDFDF
The following text describes a protein:
Function:
Converts sphingomyelin to ceramide. Exists as two enzymatic forms that arise from alternative trafficking of a single protein precursor, one that is targeted to the endolysosomal compartment, whereas the other is released extracellularly. However, in response to various forms of stress, lysosomal exocytosis may represent a major source of the secretory form; In the lysosomes, converts sphingomyelin to ceramide. Plays an important role in the export of cholesterol from the intraendolysosomal membranes. Also has phospholipase C activities toward 1,2-diacylglycerolphosphocholine and 1,2-diacylglycerolphosphoglycerol. Modulates stress-induced apoptosis through the production of ceramide; This form is generated following cleavage by CASP7 in the extracellular milieu in response to bacterial infection. It shows increased ability to convert sphingomyelin to ceramide and promotes plasma membrane repair. Plasma membrane repair by ceramide counteracts the action of gasdermin-D (GSDMD) perforin (PRF1) pores that are formed in response to bacterial infection.
Subcellular Localization:
Lipid droplet. Lysosome. Secreted, extracellular space.
Sequence:
MSYLLFSAGSALLCTFLLLVASPPTSHSDVRTDMEKLDALRRTIQKGRFSEAGSQTNWECELCEVGVTILKKTYGENKFQDEVAAALTQLCILSKLQDKTMCTGFTKEFKHEIVTIIGQTPLSSAEVCGLVVSDCSGPYDPTKFWKVTLPNTPKPPVTPPKPPKPGAPVSRVLFLSDVHVDLLYKPGANAYCGEYLCCRANSPAGKEGPKPAGKWGDYRYCDTPLWTLENLLQHLAQKQSEFDYAIWTGDIPPHNIWNQSRSDQLNALNIVSDMILKYLKIPIYPSLGNHESAPVNSFPPPFVSGKDSISWLYDALAETWTHWTPVSTKSNIERGAFYSVLVRPGLRLISINTNYCYNLNWWLLLNTTDPAGQLQWLTQQLQQAEDKGEKVHIIGHIPPGIDCLSAWSWNYYRIIDRYESTVAAQFFGHTHRDHFELFYDMKNRTRPTNIAYIGPSVTTYQYMNPGYRVYEIDGNYPESSMQVVNQQTYIMNLTEANLTDKPTWQLEYDTKEAYNMSSMTPADWDKFIQRLEKDTELFKTFYRYMYKSQRTDQPFTQKRRTAVICDLKTARSNDPSMCTLTPEVTWKDLQNYRTANRLC
The following text describes a protein:
Function:
Plays a role in the regulatory network through which muscle cells coordinate their structural and functional states during growth, adaptation, and repair.
Sequence:
MGAFRPGAGQPPKRKEFSIEEQHVPTQESEEKNEEKKHVPGAAKLPGPASNLSEIQNMKSELKFVPKGQEQ
The following text describes a protein:
Function:
Guanine-nucleotide exchange factor (GEF) for members of the Arf family of small GTPases involved in trafficking in the early secretory pathway; its GEF activity initiates the coating of nascent vesicles via the localized generation of activated ARFs through replacement of GDP with GTP (By similarity). Also, plays a role in receptor-mediated endocytosis in oocytes and endosomal trafficking. Involved in vesicle retrograde transport from the ERGIC and cis-Golgi compartments to the endoplasmic reticulum (ER). Plays a role in maintaining mitochondrial morphology, network organization and function. May be required for the basolateral cell membrane localization of the serine threonine protein kinase sgk-1 in intestinal cells.
Subcellular Localization:
Golgi apparatus, cis-Golgi network. Endoplasmic reticulum-Golgi intermediate compartment.
Sequence:
MATNGVYIVMGEANCVVALLNKARRQYQLSQVPTLEDTDPLLRNFTDLKEVLNEVADLADMNPQTYLSPFLDVIKAQNTNGPITEAALAAVAKFLNYGLIDASSIKAANAVESIAYAVVHTKFIGGKSTGSDECVLFKILQVLRSLLLSPPGILLSNEAVCDMMQSCFRIVFEQNLSLLLRKAAESTLADMTQLIFTRLPTFVEDTRHPYIRQLVNPTEKRQKRKKKRQLSVHIETKAKEPENVPTEMTKLIGEAAETAETDGAANLGYDVVLTTDPPVDTVTHPDPPIEEIIKLAEPISAGDEADSESEGGGGEEHHERPPVRAHAGLQREIVSDEEEIDTEQTVGGEEKMPYGLPCCRELLRFLITMTNPVDRHNTESMVILGLNLLIVALEAIADFLPNYDILMPLIKNELCRNLLQLLDTNRLPVLAATNRCCFLLFESMRMHMKFQLESYLKKLQSIVLTEEKQHENGGGGTEQKEMALESLVQLWRIPGLVTEMYLNFDCDLYCGNIFEDLTKLLVENSFPTVGGHTASLLSLDALLVVIETIEQNCEDRENGRGEVAKEQEHKDLKKLGLPVLSGYDLAKKMAISTGGKASPMPVSSSIVLRSNRHAPSTELPSMSQIIEQKKRKRLIAEGTELFNQSPKKGIAFLREKGILGHDEQSLVQWLRTNPQLDKKAIADYICNRKHAEVLNAFVKSFPFENTRLDVALRMFLETFRLPGESAEIALVMQHFSEEWFRANNEPFFHVDAAFTLSYAIIMLNVDQHNPQAKRSQPPMTVDCFRRNLSGTNDSRDFDPEMLADMYQAIKTEEIVMPAEQKGTVKEDYMWKVLLRRGETAEGSFYHAPTGWNDHDLFAVCWGPAVAALSYVFDKSEHEQILQKALTGYRKCAKIAAYYGMKEVFDNLCIHLCKFTTLTSMRDGGAGGGADEDVDLSAAALLSHSSSPEAVALAFGENHKAQLATRTLFYLVHENGNILREGWRNLFEALLQLFRARLLPAELTEVEDYVDEKGWVNIQRVHQKELPHTRNDSGLLSWFGLGGGASEADRRKPTQEQLSSMKLASQVISECRPSQIVADSKYLTSTSLAELLSSIAANSAQIVEQAEPQQKTASLSGEDEDALVFYLELIVAITLENKDRLPLVWPHVRRHLEWLLSPRFGRCPVLVERAVVGLLRVANRNLFRDNTVSDDVLHSLSMLLRLSPKALFIFSRQIAFGLYELIRANAANVHKKEHWAVLFALLEAAGAAVLPDDYVMMTTTEKQQQSLRVGGDQQQQRMAYSDVEGASGRGGGAHEERAYTSEGEERRRGGYDSNSDLESRVDSAGSLLGAQKQPADWIHLDHKDAAKATEEALTALGANVVSSKKNFRQFGSLVLRNGLGRHEPAAFLKVCECLAFLLRDAVHVTPDNFESSLQCLRTMVEASLDGGVYAAGPLSGDAQNRLRSNVTDEKAVKKHHHHHHGHKKKELCTDVTEDADESRNEEQQLIGNYQQMSLHLLDLCSQLHSQTPAIFAKWAQGASPAASDLATVAFIWTDIWRPLLQAIGRLSCDCRRGVRAAALTHLQRAFLPANMATLGAAEWQSCFGEVLFPLLTKLLEPFSQMDPIGMEDTRVRTLQIVAKTLLNHLSALSALDSFPDLWMLLLDYMEQYLRVDSCGNLNEAVPESLKNMLLVMDSTGIFAATPRLYDVTVERLNKFMPELIKDTIPNPPRPGQQQSEASEPKKEHASGLEPPPPSSNSTAATSTSDPSIATAQSSISTASSVVGPLVTCPEDAGISAPIPIQHPLTEVIVHSGPTSPIGSPPQTEPPASSPPQHQHSEHQQYEQYRQQQAAAAQQYQQYNQNYPQQQQQQQQQYAYSPEHAAYYQQQYAHQQQQYAEHYANQYQHYQQQQQQQQQHPVNPTSPSVHGQYSVANPLPLPAHPAYHPIVAPSVNSAFTHVYTPPQNNAPALAPSAPTTTSADSPYFTPIPYNPSQQEKP
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:
MQQQQFIQQQQLQQQQHQQQQHQQQPQQPQPQAQKDFNPASLCRFGQETVQELVSRVQECFQLLKNLQPPNGSAQSTSVAVDKKNKLDDQLKMVKVLFKRLRIIYNKCNENSQELDSYPLDSMLPTQSNLVDWKYADRVKSEQYLTAVDEKKELYDQILVKNRHLQDIMEYMRSIIWEINTMLMMRRP
The following text describes a protein:
Function:
As component of a spoke-associated complex, regulates ciliary mobility by mediating a stable and functional assembly of the radial spoke 3 (RS3).
Subcellular Localization:
Cell projection, cilium.
Sequence:
MYSNNQLDNPNHSRSQYRNGDQSGIYAGSDEEFQVLVRKSDLDDVDEVLKIIAQHEREANDLLYDYPNLLSLFEKNYLSVTILNQQQQIIGAAVFNDFPQGLTGQIDFQHENFWENWIFDAFNFDESICITPFNTLWMTFFFVAKDQYKFSQEEELIICQKVFQNVYATLPQLEGILFLKRGETMEDNGAQAQISSILENIFIEVPVKDRDIIKRVRGIHLNSEVFYSPKHACQEIIEIRMAREQDHDDLAEIFNRQSEVLTAQFGEFFIADLIATQNLTRRGTRKFLNNGKAIVGQVRDKAVGLMSISTDIDYKFLAQCFELETYDNLFKPDFMEAIQNKRDDIRRENQYREEDQYQEIVKKMNEERMKSHFIGQRMTLQQHCREKEQEIVMKIDEIINNDAIQKNLTKKQVEEFLDEWLRGYELHQPSDLFYQYPHIFPNTQSIILTPRQLLIETLEFFGLPQHYMNGAGHWKDWVQKKMEEKRIAQLKRPQKKVTKRPKRQKEEDKKEDEFKPPSYFDLTPFQSAFKKFLAVNPEGRTIFRQKIEASMKVIKMMFCNENGEMKEERHVDLNDLGNELNKQKMDIAPEVCENLASFLECFGEIKYEEEIIMVNPPKEDTNQNAKIAQTKKMFASEQTESKPIPKLLKKTSFQEFFDAVYKMKEFDIMMNRLDITKSTTLKAEVSQIVKEEAQQEKAKQEKRRIERSPNPYDDYVKNLKDLDSIPEVPIDAQNAIVINLFCIDENFESRSLDFVEYAFSIFGDRDYIILTQPFTVPETTLLQQFIKIPMKKNSTFDHVLYIYHKDCLLSNTLFIRKSKLEDMQYVAPLFSNLINKQQIYDDTLEAITQTASRKVAFSVFCDQSLIGIYVVSKNVNLDYYISHFCVQDHIILKEHPMTCHTKLIHTALNPLFTKNTRFILKEILRLMNKTCMYFEVQEKTLLPDVFNELVFVRARQFPHFLKRKWDFEHDKEHFERAGDLTEVQDGKRDAFDQEQAPFSLSVITKKMMSSVKVNNNTRIVVVGASDTGISFIESLLSVKDINFTHITLLAPGGIMTMHINLPGDQLKALSTNYTLEELKNLMLDARVNVLDAKMVELDKKGKKIKLDKNAELPYDYLVNTVGLIDTELQNRRLISTGLFSSPYYQQLLDKYGRDRAQIEEGAPPIFGQHPVYGNYVQGVYSIDDPYLYEEFKKTGKKDSNIDLLTRKKRPQSITIYGRTLHTIAFISGMVNRGVHPNRIHYVIPPKVFETQVQFKNNTERLIYEDKRINDPDPFDDPSVEQKIFEFMESKGIQVHKGYNLHQIDVDEETRICQGVVFRKKADNYEEIIQQIEIKKQQILERDANSENADKGFDDTQSRDGDEENQPITLEQEIEELERNKFDDIEITSRFLVTSGLVDIDKEIFYIIHENGLVYNGRLIVKSNFQTTEKDIFCCGKICEFSQRYKRLSIGRSLRLDKYNGRELGQKLAKCLLDSLDLGYLTDQIYSLGELPNLYMPIGIGAFLPGDLFYYHIKKNDYARPSKTMEAEDNRQDIVSDNIDQKQQIGHYIKFKFDNNGIIDQVTYLGTEPVSVQSLVSFVGLSEKCLNQLDVRFKNGLIPNISEFLSENWAIGLYHEWFSEFRHITKMEMLQSENIQQILDEAAKYAQGGGFLDPEFIEKIKAKISPEIISQIQQGTLDFIRENQNHLPMYYVPPKKVNVD
The following text describes a protein:
Function:
Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. The Tol-Pal system is also required for polar localization of chemoreceptors clusters. The system also appears to be required for the activity of several outer membrane-localized enzymes with cell wall remodeling activity. Is involved in the uptake of group A colicins (colicins A, E1, E2, E3, and K) and in the uptake of filamentous phage DNA.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein. Note=Accumulates at cell constriction sites. Recruitment to the division site is dependent on FtsN activity.
Domain:
Contains an N-terminal domain that anchors the protein to the inner membrane, a central domain (domain II), and a C-terminal domain (domain III), which is the functional portion of the protein. The C-terminal domain is involved in interaction with TolB and Pal, and is also involved in direct interaction with colicins and phages. It adapts its conformation upon binding to various partners.
Sequence:
MSKATEQNDKLKRAIIISAVLHVILFAALIWSSFDENIEASAGGGGGSSIDAVMVDSGAVVEQYKRMQSQESSAKRSDEQRKMKEQQAAEELREKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAELKQKQAEEAAAKAAADAKAKAEADAKAAEEAAKKAAADAKKKAEAEAAKAAAEAQKKAEAAAAALKKKAEAAEAAAAEARKKAATEAAEKAKAEAEKKAAAEKAAADKKAAAEKAAADKKAAEKAAAEKAAADKKAAAEKAAADKKAAAAKAAAEKAAAAKAAAEADDIFGELSSGKNAPKTGGGAKGNNASPAGSGNTKNNGASGADINNYAGQIKSAIESKFYDASSYAGKTCTLRIKLAPDGMLLDIKPEGGDPALCQAALAAAKLAKIPKPPSQAVYEVFKNAPLDFKP
The following text describes a protein:
Function:
Required for survival upon exposure to K1 killer toxin. Involved in the resistance to unfolded protein response (UPR)-inducing agents.
Sequence:
MSTEQVGRKKSYRWVSASQASYDGAGWDSSDEYDYSSEDGTKGSEIHKQKISNLPSLPKLNYTDVNGEHDENTGENKDSNDNNVSKSDISPSDKEVGYLSDGVPKLMASRESVELQAKKSSEHSKSDYLSSTASLKSPSENKKSPHTNRAVNEDLDNLIEQISREMTPEIRQTSDFRRDSDSCDEIQNEAPLGEAVPSSSSPVEEDEKSHSLGVSMDTNEADTTFNTPTRNGNEHLSSDGDVSEQKDDEFKVSERGYLADILPAEKEENLQQEDDGEVESSGALEKKEKSEEKTSIRNRNSTSSGQDKVAKPKPVANETKTSDNGYRNSFFNDYQHSSDSEEDDNNEGNSGSSDDDNRSSVSDKHADINRQSKQLDTTDDDALSYTESIKYSTNETEEEDNEDNESIEDKNEDNESIEDENEDTDSYKFSNREKGSILLTSDEEEEEKGMSSDSDEGSLKAPKSGYFSKMIGNDDKGDSALQPNQIDTIENTNLSNSGSELENSDGSDEEDHINEDKVLEESSVKDSTDVDSWKPDSEALRSGFVQDTANKKAPPGYVIDSNGKLVDLTPASMKPRVVSTYSEMESTWDAFPSKGEDDDLETIRDTKTIYDNNTIYNVPGLIGNQSNLPPLPMDAQEQLNAGNDNSTTDNDNSNNTANDLAARSASFKSENRTVSQGEMTSVHEPSTEEMAKLGQQNNLPKLDMNKLLNSKTSHAGKIEQLRNYKRELDEYDTGIQTWINYTLKSSSNKDKDFIAEEYKQHSHVREAYANADDLSKKHTVINTVASVNQNVTHLRRKVFQHSMKPKDLFASIGKKKL
The following text describes a protein:
Function:
Acts on leucine, isoleucine and valine.
Sequence:
MLIWWRGKFRRADEISLDFSLFEKSLQGAVYETLRTYSRAPFAAYKHYTRLKRSADFFNLPLSLSFDEFTKVLKAGADEFKQEVRIKVYLFPDSGEVLFVFSPLNIPDLETGVEVKISNVRRIPDLSTPPALKITGRTDIVLARREIVDCYDVILLGLNGQVCEGSFSNVFLVKEGKLITPSLDSGILDGITRENVIKLAKSLEIPVEERVVWVWELFEADEMFLTHTSAGVVPVRRLNEHSFFEEEPGPVTATLMENFEPFVLNLEENWVGI
The following text describes a protein:
Function:
Transcription factor involved in the regulation of calcium ion homeostasis. Regulates genes encoding calcium transporters, transcription factors and genes that could be directly or indirectly involved in calcium metabolism. Supports especially pmcA, pmcB and pmcC expression encoding for calcium-translocating P-type ATPases. Binds target promoters at motif A[GT][CG]CA[AC][AG]. Plays an essential role germination, radial growth, and asexual development. Also plays a major role in proper chitin and glucan incorporation into the cell wall. Involved in the high-osmolarity glycerol response (HOG) signaling pathway. Required for pathogenicity in an experimental murine model of invasive pulmonary aspergillosis.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Localizes predominantly to the cytosol of the cell in the absence of added calcium and translocates to the nucleus following exposure to CaCl(2).
Sequence:
MASQEMFPELGQSPAPGVKSRGVSRSPHPHQQQQQQQHQQHQGQFTGTVTGLDLDSSIATASSFANSSFDPNSNNVSPSAESYGYTAAGYLSGTPASQTDQNYANSLQIPQSYGTGLVPQFNESRGLPIQQQSQQQHHQQPSLDDNFSDLLNSNATEYDFNTVYQTHSPSSNTAPEYDSSLLLDPQVHQQSHPTQIPSSHSSTSPQISPLEQQQHSSPGPMSTQGSTTVAYYTPQHSRHASLDPATAAFLTSNTHPDWQAVMGNSAAFQGHRRAPSEVSEISSAAPSPYLSQHESFDGVDNNPSPLLAPQNDPSLYDSALGIENFTLSEQHQQHQGFSPAHSPYISPRLMPQQGQEMMPNVPYLSGPAPNTQYPTPPNDMYGNGAEGMMNMSQGTHPSVDIGQASQMAPPSINVEFAPPSRIPSFGPSKPASNLDSLSPPPSSTRSRGRSKSDPYAHPSTSRLRSSSTSSSLDPLAPTTPRSLSPFDSFGRQQQSNPSSRDPSPSRSNRRLSTSSIDSRNYILGLADPQRPGASPNDSKRVQKHPATFQCNLCPKRFTRAYNLRSHLRTHTDERPFVCTVCGKAFARQHDRKRHEGLHSGEKKFVCQGELSRGGQWGCGRRFARADALGRHFRSEAGRICIKPLLDEESQERERSLMDQQQHHLQPLPQQVMVPVDNPHAGNFVLPAALLAQYPALQTLQWDQIAASADDPSDIGGRSSFDASSGNEFGFEDDDSGLSSVSGINAGYSAAGNFY
The following text describes a protein:
Function:
RNA-binding component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Binds to A-rich RNA sequence elements.
Miscellaneous:
MISCELLANEOUS: Present with 6350 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MNRQSGVNAGVQNNPPSRVVYLGSIPYDQTEEQILDLCSNVGPVINLKMMFDPQTGRSKGYAFIEFRDLESSASAVRNLNGYQLGSRFLKCGYSSNSDISGVSQQQQQQYNNINGNNNNNGNNNNNSNGPDFQNSGNANFLSQKFPELPSGIDVNINMTTPAMMISSELAKKPKEVQLKFLQKFQEWTRAHPEDAVSLLELCPQLSFVTAELLLTNGICKVDDLIPLASRPQEEASATNNNSVNEVVDPAVLNKQKELLKQVLQLNDSQISILPDDERMAIWDLKQKALRGEFGAF
The following text describes a protein:
Function:
Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Domain:
The F-box is necessary for the interaction with ASK proteins (By similarity). Interacts with ASK4.
Sequence:
MDTDLISNLPDDVLGKILSLVPTKLAAATSVLSKRWRNLLPLVDSLDFDETMLFYPDNKDGEDEASSYESGQRRRHSFSHFVDKTLALLSNAPLTEKFSLKCYHEDDGARINRWIRTALERGCLELNLEAANYLPIDSQYFTSNTLVKLTISDGFYPGGHLLPFGGVFFPALKTLTLVSVCFTSVEMINFFIHGCPALEELFLCVWMQYMSSPNVKRVTITSDFDDDIQRPSMVLKTPSLVYLDYSSYVAGNYYVVLDSLVEARLDLRLYEPIIYDEDGLWNAEVFGNITNLIEAIRTIKILHLSPSSLEVFYYCCDLPVLEDLVNLSIESDKEKGWEVMPRLLNKSPNLQTLVVKGLVHRVTYCCGDACACIRMKDREIVSCLSRCRVKVLKILGYGGSFRELKQMRHFLGKLKCLETVKVGVKEGSKKSNYLVANVMALPRVSSKCKIQFI
The following text describes a protein:
Function:
Functions as a receptor binding protein (RBP) and probably mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the KN1-type polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor.
Subcellular Localization:
Virion. Note=Tail appendage.
Domain:
The N-terminus anchors the RBP to the virion (By similarity). The central part and C-terminus probably binds and degrades the host exopolysaccharides (Probable).
Sequence:
MMNQDIKTIIQYPVGDVEFDIPFDYLSRKFVRVYLVSPLNRRQLNNITEYRYVSRTRIKLLVETAGFNLIEIRRFTSASERVVDFSDGSVLRATDLNVSQLQSAHIAEEARDAAMLTISPADDGSLDASGKVIKNVGTPVQSSDAATKGYVDTAVSPLATTIEANFMRTLRTSGRSIRELPGASEVAGMLLGFNGEGDPVPVVAGEGTASDVMLKLAGTTGLSYIGGVGYVTPEMMTVDGKTLVRGLGQDHVRFIQKAIDEGHRRNVPVILSGGYEVYETLHDAPLPRDDGTAYPEWVANGGDSNIRPEEQLYQKAHLRLYNNSVILGAGSQIATIRSTWARSTSAVGLTSPIMWYIEGPLGNRGTVSYVLKGIKTIGAYIGRYVVGISYRSVEDDLEFAGCGIAGVKQGEEQTIHRKIVITAYAGDVTGGWWLQRNNAYGAKYMPPYTDTDVWLLGWCDSSTYEYLSYTGYDYDGRDALVHDWISEWFDTYIFKTANSRKVSEGGRLTYQSANPYPLPTLKGITGRARYITSRYSRQNALNVINTLKTLITIRAPGYMDNSTQSCRILNAMIESVGLIRRTSGANAGNYFGIDVVDKWGADTGVWGLEGTGILEKQLVVFLRPGVPCTNAVVATGAGQIFESWTTTNAQRRLLALRDWNPATQVQTYRYDFRTDYALMRPTRYYTDGPLWNYSKGTSTPTVAVNGSTIAVQKAVTNWYRLGDIMRCNIYVEINSITLQGNSELTVTTPSFNGSWEVAGQGIGKVYLSTLTGGVTLTPVIQQGGNVVRLRKGSSPEVYAFEAGTYNNVVLIIGIDYVPLS
The following text describes a protein:
Function:
Lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum to the cell membrane (By similarity). It thereby maintains the pool of cell membrane phosphoinositides, which are degraded during phospholipase C (PLC) signaling (By similarity). Plays a key role in the coordination of Ca(2+) and phosphoinositide signaling: localizes to sites of contact between the endoplasmic reticulum and the cell membrane, where it tethers the two bilayers (By similarity). In response to elevation of cytosolic Ca(2+), it is phosphorylated at its C-terminus and dissociates from the cell membrane, abolishing phosphatidylinositol transport to the cell membrane (By similarity). Positively regulates insulin secretion in response to glucose. Phosphatidylinositol transfer to the cell membrane allows replenishment of PI(4,5)P2 pools and calcium channel opening, priming a new population of insulin granules (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Cell membrane; Peripheral membrane protein. Note=Localizes to sites of contact between the endoplasmic reticulum and the cell membrane. Embedded into the endoplasmic reticulum membrane via its N-terminal transmembrane domain and associates with cell membrane via its C-terminus. In response to elevation of cytosolic Ca(2+), it is phosphorylated at its C-terminus and dissociates from the cell membrane and localizes to the reticular endoplasmic reticulum. Reassociates with cell membrane upon dephosphorylation.
Domain:
The SMP-LBD domain is a lipid transport module, which binds glycerolipids with a preference for phosphatidylinositol (PI).
Sequence:
MDPDWGQRDVGWAALLVLFAASLITVLGWMLQYARGLWLSRADGGRDSRPASAAEPGGSLRELGVWRSLLRLRATRTSTPEEAGVRGLLASLFAFKSFRENWQRAWVRALNEQACRDGSSIQIAFEEIPQLPPRASISHVTCVDQSERTMVLHCQLSAEEVRFPISVTQQSPAAVSMETYHVTLTLPPTQLEVSLEEIPDEGLLVSWAFTDRPELSLKVLPKLQTRERDEEQPELSTVEELIKDAIVSTQPAMMVNLRACSAPGGLVPSEKPPTMSQAQPSIPRPTRLFLRQLRASHLGSELGGTEELCCAAELDNPMQQKWTKPMRAGPEVEWTEDLALDLGPQSRELTLKVLRSSSCGDAELLGQATLPVGSPSRPMSRRQVCPLTPGPGKSLSPAATVTAELHYEQGSPRNLGTPTSSTPRPSITPTKKIELDRTIMPDGTVVTTVTTVQSRPRVDGKLDSPSRSPSKVEVTEKMTTVLSESSGPSNASHSSSRESHLSNGLDPVAETAIRQLTEPSGRAAKKTPTKRSTLIISGVSKVPIAQDELALSLGYAASLEASMQDDAGTSGGPSSPPSDPSATSPGPVDALSSPTSVQEADETTRSDISERPSVDDVESETGSTGALETRSLKDHKVSFLRSGTKLIFRRRPRQKEAGLSQSHDDLSNTTATPSVRKKAGSFSRRLIKRFSFKSKPKANGNPSPQL
The following text describes a protein:
Function:
Factor that stimulates resuscitation of dormant cells. Has peptidoglycan (PG) hydrolytic activity. Active in the pM concentration range. Has little to no effect on actively-growing cells. PG fragments could either directly activate the resuscitation pathway of dormant bacteria or serve as a substrate for endogenous Rpf, resulting in low molecular weight products with resuscitation activity; Reduces lag phase and enhances the growth of quiescent (1 month-old culture) M.tuberculosis; works best between 8 and 128 pM. Increases the number of bacteria that can be recovered from a 3 month-old culture. Stimulates growth of stationary phase M.bovis (a slowly-growing Mycobacterium) as well as M.smegmatis cells (a fast grower). Binds N,N',N''-triacetylchitotriose (tri-NAG). A fragment (residues 194-362) hydrolyzes an artificial lysozyme substrate 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside (MUF tri-NAG). By itself has little activity on cell wall, in combination with RipA is active against cell wall extracts from a number of Actinobacteria; this activity is inhibited by PBP1A (ponA1). Sequential gene disruption indicates RpfB and RpfE are higher than RpfD and RpfC in functional hierarchy.
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Subcellular Localization:
Cell membrane; Lipid-anchor. Note=Localizes to the septa upon expression in M.smegmatis.
Domain:
An expressed fragment (residues 194-362) hydrolyzes an artificial lysozyme substrate 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside (MUF tri-NAG).
Sequence:
MLRLVVGALLLVLAFAGGYAVAACKTVTLTVDGTAMRVTTMKSRVIDIVEENGFSVDDRDDLYPAAGVQVHDADTIVLRRSRPLQISLDGHDAKQVWTTASTVDEALAQLAMTDTAPAAASRASRVPLSGMALPVVSAKTVQLNDGGLVRTVHLPAPNVAGLLSAAGVPLLQSDHVVPAATAPIVEGMQIQVTRNRIKKVTERLPLPPNARRVEDPEMNMSREVVEDPGVPGTQDVTFAVAEVNGVETGRLPVANVVVTPAHEAVVRVGTKPGTEVPPVIDGSIWDAIAGCEAGGNWAINTGNGYYGGVQFDQGTWEANGGLRYAPRADLATREEQIAVAEVTRLRQGWGAWPVCAARAGAR