lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Appears to play a role in the switch from cap-dependent to IRES-mediated translation during mitosis, apoptosis and viral infection. Cleaved by some caspases and viral proteases.
Sequence:
MSHYLSKGDRSEAQLRKAGRGSAGHPRAGGGQPIPVKGGGPSPFNSAPSGGGPPQPSSFVASSARPAAVAASINRGGKRANGLPASGGGPPEQGANNKAHQQAALPLHHNNQQQQATGVRQGVGSADANQHSQMGAPQLNSDSKGVTTARTSGNAGTGAPPAIKQLQTSKPPAPPASITTGSGADTPSAAPPPVSQSSQNPISFQFGSFEPSGFGGASTSGKSSVTPYPLRTNSAPPNLDEQRREQARFELRPSSITRVSASGQQHNAQVTTRNVVSGMEPSPTTVPPVQAATSSQGPIPVAPTAQALPPQQLGQSPHYPQHLQVNSLHMPSQHILQIQMQQQQHHQQHQHQHQLHQHQLQQQQQQQQQHQQQPMPPQQGMAQQSLKYPQSMMAAPHHNSQMLGTHPVVNPLPPQPMAQMTHQLGPGQIPSGISVGAYGTTTNQFVTKQRSRAIPIVNPLTHEELKIDLLKKDSVESVPSSSLGTAGRVPSNGPMQQLRAPVGYSPPTHPVYYFPSHPQMYPPSIPKTGTFGGAPLSSSPPVRYSFNPPHPGQGVHAGTTPVPPGAPKVAPQLGPGPPLGSANQVPTSGEILSTPPVAPLIMVGPPSSVTVPGIPAVIGNLRPIPPPLVMNPPIVSNGRPPSLTLPPVSPPAPLTPSSVLPSPNSTVGFKFGDVEASGSTPVATGEASSEGSLNGVIGHASTRVEPNNASGNAPIVGVVASSTSPEASDLVNRPAVTVIPPKPGSGNSNASGISPKIKTPPGTGSAGAFGEKVKSEAVKSSGNPNTRKSSKKDRQRQQQQALAANLPISEGAKTSDQLISPGLGVSGGHKSGLQRTQSGAHGSSAVYTPVKNLGSKPEEPKLPNVNFGSQNSVQDTTKENTESLAVEEVVAGKDEVESVPVRPLHEESKGETPAEIETSLKTDASVLISDGSTASTSSTGLPSLLVKDEPAEVQANELAVVEDDVPEDVRVSVNPSAASSSFDQELVKVETNSIEVEPDTITSEPTFYKASTEMAIENEGVVNDAEPTVADLRKENAGFVEQVDPPSSEADHALTGESAVEWAPDVPDVNEDVSTMKDLPTPLHSESAPGSKGTGGSEVVVIEESGVLAVDINSVEENDVADIQVTSSKYVPEVVPGSPLHSNLDTCMFENKMVSSQQDSATALNTTEETPQAVEVATAEEALQSNPSSGGMMIFTSEEVQSRDSLGPLDSIRGSLENGGEDSRPSEHTESAASNSSKAEDTAPLIVGESRSEVQTTPLLSSTSGMSSTEVIETLNAVESEADSVEPAVVGNPTSGQGEGPKVGSRKKKSRKEFLARADAAGNTADLYNAYKAPEEKKSVEVKQAEVSGAGPSGNDAKDSAITPDKSLPNEVDDWEDAAELPTPTISFPHLVDTGDRKYTRDFLMTFKDQNREFPPNFEIKHDITDVLLDKDKLFSDGLTSPARNLDWQPSGGQRLERRGSGIQLGPDEDRWIRQSGVVPSPGRNQPGDARMGMDIPGGFRPGQGMQSGLISQLPQQWPGMPAQAGFPGLISRGNMPLGHYMTPGPPARSPNGVDGDRWLRQPMSGVKGPGLIPSPRTPLPAIHKAENRYEVGKVSDEEQAKQRLIKGILNKLTPQNFDKLFVQVQEAKIDSATTLTGVISQIFDKALMEPTFCEMYAQFCVKLAADLPEFNENDEKITFKRVLLNKCQEEFERGEREQEEAEKDEEEHVEIKMTPEEREEKRLKARRRMLGNIRFIGELYKKSMLTERIMHECIKKLLGEYHNPDEEDVEALCKLMSTIGRIIDHHKAREHIDAYFRRMESLSNNTKLSARIRFLLKDVMELRRNGWQERRKVDGPKKIDEVHRDAVQERQNASRGDRLGRGPSMGGGGSRGRMGSGPDFVIRGPPSPMYSPGPMGSGPPMGGMRRAPSPQGGMRGGGGFIQDVRMEDRSLMMDARPVPMPLSQRGADEGSITLGPQGGLGRVGVRQLSLSTGRSALSDAVPTSGSDTRRLSLGSILGHAQDRSHYSNRDELPMRPSSAERPRSAERPVLDRPIGADRLSPGLRDFRSTLEQQRLVERSNSLSSSSSTFQPHRTEHTAPFVSVRPSSAPSALSVEELKKKWESTINEYYSVTDLKEAALCVEELKAFKHHPEMVDIWVSESFEKKDRERDLLVKLLLHLHRIDPPFLSRDQIEIGIDRVLSRFTDLVVDVPKAPEFMGVLLGRLICAGVFTLNEVGNLLQVAGESRGEVREEGYALRIFGAMVDTYREEKGEEQMVDAYKRSDLDVENFVSPSEKNRETALQQFLERTNLHKLHPMLPLERYIKDSLDRKVPVMDIIKWIEKNVPSAYSEPSFMRMLMTQVLRRALPDPQSTDISSSNLKVDIKAYAPLLKKCASGGRATANQIQYIIAILLFTNECGHPQGLMTKLFENFSQEEVISKKAYTDWYDDVNDSTPGRDKAIREVSNWLKQKIEEGAEVEDEED
The following text describes a protein:
Function:
Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MLTINLPKTFKVKYLLIALALFYLILVLLLPAIAVFYEAFHKGVEPFIQAMGDRNFQSALQLTVVMALISVPLNTVFGLCAAWVLARNQFPGRALFLSVLDLPFSISPVVAGLMIVLLYGKNGWIGSWFASWDIQIIFSVPGMAIATIFVTLPFVAREVIPVLEELGPEQEEAARTLGAKDWQIFWRVTLPNIRWGLLYGVLLTNARAMGEFGAVAVVSGSILGKTSTLPIFVEQEYKNYQTEAAFGAAVVLALLAVVTLVLKEILEQRTGHHKAV
The following text describes a protein:
Function:
Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.
Subcellular Localization:
Cytoplasm.
Sequence:
MSSKCTAGIIIIGDEITKGKVADTNSHYVAQKLYALGVDVCKISIIPDQVDVIAEEVALFSKKFTHVVTAGGIGPTHDDITYQAIAHDYDPLNPPTFPCDVETSSFNPALKMALVPASSRLHHSKGLSVFPMIQVYNVYVMPGIPQYLKRCCRHLETLARNPDCVFHSREIYLQADEVGLAPILNAAVKEFASHVSFGSYPVIGHSYYRTKLTMESTDPARLDAAHQHLSAELPADCIVPYDPQAIERAPEVMQDIIDGQGAHHRELHAPISNAYQVIEECLSRYDPSEVCVSFNGGKDCSALLHLIHAAWMTAAARRRSSSSSSFVSGQPLRLRALYIRGQDPFPEMEQFIEDTRQRQLFSPSSFFFFVYDLELWTVAGPVRSGLKIALDEHPEIKAILMGTRRSDPHAANLQAFQMTDDGWPSVMRVSPILDWSYQQVWLFLRRLSLPYCNLYDRGYTSVGNRGNTKPNAALRVVDPGTGLETYRPAYLLHDCMAERQGRL
The following text describes a protein:
Function:
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
Sequence:
MGVLLFQQCNAGAAAAPVNRSKDWRPGTLSCARNQRLITVCCSNGEKSGVAIKVEGDSTPKKRPVLSRAPPRSFGVKDEELVPGKVLTGSVKAIMTFGAFIDLDARFDGLLHISKISDRFVQNVEDVLTVGQQVQVEIESVDLPKRRIQLKRHAVIAQGSKVSSSGTAQVEGTGALAAVPKDTSTGTQAARIRASTNGAPVAGKNGAAASQDDGTNSSRIAGTSTKQPGTRFQSRSSSSTTREEISKEPSSSPLPRLSSRIPPPKTSYQKGQVVSGVVKNYTRRGCFVQLPGNQEGFLHANEIESSREQEPTPVENLVKVGQELKVKVLRIIDGRINLTMKEEVDLKKIKELNENVFATNPFELAFRKNPVIRGYLKETGRLQGSEHGNEERRTRGVEENSSEEKELCKVEFVANVNMFALIGLRFAEGLRVEWSTIPEDVVELTIPHLDMS
The following text describes a protein:
Function:
Electrogenic voltage-dependent transporter that mediates the transport of a variety of endogenous bioactive amines, cationic xenobiotics and drugs. Utilizes the physiologic inside-negative membrane potential as a driving force to facilitate cellular uptake of organic cations. Functions as a Na(+)- and Cl(-)-independent bidirectional transporter. Substrate transport is pH-dependent and enhanced under acidic condition, which is most likely the result of allosteric changes in the transporter structure. Implicated in monoamine neurotransmitters uptake such as serotonin, dopamine, adrenaline/epinephrine, noradrenaline/norepinephrine, histamine and tyramine, thereby supporting a role in homeostatic regulation of aminergic neurotransmission in the central nervous system. Also responsible for the uptake of bioactive amines and drugs through the blood-cerebrospinal fluid (CSF) barrier, from the CSF into choroid plexus epithelial cells, thereby playing a significant role in the clearance of cationic neurotoxins, xenobiotics and metabolic waste in the brain (By similarity). Involved in bidirectional transport of the purine nucleoside adenosine and plays a role in the regulation of extracellular adenosine concentrations in cardiac tissues, in particular during ischemia. May be involved in organic cation uptake from the tubular lumen into renal tubular cells, thereby contributing to organic cation reabsorption in the kidney. Also transports guanidine.
Miscellaneous:
MISCELLANEOUS: Does not interact with nucleosides, nucleobases or nucleotides, other than a moderate activity for adenosine. Mediates the uptake of neurotoxin 1-methyl-4-phenylpyridinium (MPP(+)).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Note=Located to the plasma membranes of ventricular myocytes and vascular endothelial cells. Targeted to the apical membranes of differentiated kidney epithelial cells. Localized to the apical blood-cerebrospinal fluid (CSF)-facing membrane of the choroid plexus epithelium.
Domain:
Glu-206 is essential for cation selectivity and may function as the charge sensor for cationic substrates.
Sequence:
MGSVGSQRLEEPSVAGTPDPGVVMSFTFDSHQLEEAAEAAQGQGLRARGVPAFTDTTLDEPVPDDRYHAIYFAMLLAGVGFLLPYNSFITDVDYLHHKYPGTSIVFDMSLTYILVALAAVLLNNVLVERLTLHTRITAGYLLALGPLLFISICDVWLQLFSRDQAYAINLAAVGTVAFGCTVQQSSFYGYTGMLPKRYTQGVMTGESTAGVMISLSRILTKLLLPDERASTLIFFLVSVALELLCFLLHLLVRRSRFVLFYTTRPRDSHRGRPGLGRGYGYRVHHDVVAGDVHFEHPAPALAPNESPKDSPAHEVTGSGGAYMRFDVPRPRVQRSWPTFRALLLHRYVVARVIWADMLSIAVTYFITLCLFPGLESEIRHCILGEWLPILIMAVFNLSDFVGKILAALPVDWRGTHLLACSCLRVVFIPLFILCVYPSGMPALRHPAWPCIFSLLMGISNGYFGSVPMILAAGKVSPKQRELAGNTMTVSYMSGLTLGSAVAYCTYSLTRDAHGSCLHASTANGSILAGL
The following text describes a protein:
Function:
Required for the processing of the 27S pre-rRNA (By similarity). Plays an important role in plant growth and senescence by modulating ribosome biogenesis in nucleolus. Associates with ribosomes.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSLEEDIVSDDEMNMIDEDDATDSEAESLSDSDTENEITEKLAEPTKTAIYNRDGLLDKLQDISWPEDVDWTHKLTVEIDQGGAVDVNDDLARETAFYTQALEGTREAFGKLNEMGVNFLRPANYYAEMVKSDVHMEKVKSRLLHEKKQIEESEERRKARDNKRMAKEVQSQKMKERAKEKKDNIESVKKWRKQRQQSGFSDKAGEPELDFESGKSFQRGGGKKRPGVSPGDRSGGKGRPTSRMGNKKREFRDSKFGHGGRKGLSKQNTAETTNDFKGGFRGGKASGNKRQKR
The following text describes a protein:
Function:
May be a carrier protein for lipids.
Subcellular Localization:
Secreted.
Sequence:
MYKTRVIYVLFALCLVEIFAIEMDDDMKELINNLHNTCTGETGATDDQIENARKGNFAEDDSFKCYFKCVFDQMGCMTDDGKVDSEAVIAVMPPELADKIASTVRGCTEVGANPCETAWLANKCYQKSNPDMYFVP
The following text describes a protein:
Function:
Neuropeptide PDF is the main transmitter regulating circadian locomotor rhythms. Required to maintain behavioral rhythms under constant conditions by coordinating pacemaker interactions in the circadian system. Together with CCHa1, involved in regulating intensity and periodicity of daytime activity, possibly by modulating rhythmic expression of circadian protein PER/period in a subset of clock neurons, but not TIM/timeless. Acts on small and large ventral lateral neurons to control sleep and regulates the state transition from sleep to wake.
Subcellular Localization:
Secreted.
Sequence:
MARYTYLVALVLLAICCQWGYCGAMAMPDEERYVRKEYNRDLLDWFNNVGVGQFSPGQVATLCRYPLILENSLGPSVPIRKRNSELINSLLSLPKNMNDAGK
The following text describes a protein:
Function:
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Subcellular Localization:
Cytoplasm. Mitochondrion intermembrane space.
Domain:
The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation; The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine. It is required for correct assembly of the 2 Fe-S clusters; The twin Cx2C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space.
Sequence:
MLQNSTLALTDHEVLSISTVLDAVRKLDNAGVDQCDPLIITQASSLSQLPVESSSLDIVISICRSLEFPCDKLLAEISRVLKPGGTVLIQKTSQSVAGIKDGETSLERKLLMAGFLEAQAIQLKPVVPSEGAQSFGIKAKKPSWKIGSSFSIKKAEKSLPKFQIEDDMDLIDEDSLLTEEDLKKPQLPVDGDCEVGSTRKACKNCTCGRAEEEEKVEKLGLTMDQLNNPQSACGSCGLGDAFRCGTCPYKGLPPFKLGDKVSLSGNFLVADI
The following text describes a protein:
Function:
Key enzyme involved in DNA replication and DNA repair. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA.
Subcellular Localization:
Nucleus. Chromosome.
Sequence:
MANQNEVHGLYCDNDLQEGQDETTLFPDNNESSFSNDDSFELASSDLVLLDTVEQNLTLNDTTINPPRPLAISNNHTGGYHNSVPSQCAPSSEAYDDGWDFSSLPNEVEERLDPLFLVIETREEYEEKNDYSFMKKVILLTNIVNRKPSTAILLDEWSDTPVRTGDSLAIYDASEIEGDMIVSNSNGYIIMFPFYLLSATSVADSFTCLRRATFKEWYGSTHYLTKPIVYGNILHRVFQNCLRDPNEFTGLDKLDALLRNSIKLETVNIHFAGLTNDQCLNELRERLPAIRKWMLSITTGDERQPVLIKALIDTEESILSYRFGLKGNIDATVEASITGMRPSVYPLELKTGKVTNTTSHFAQALMYTLLMSEKSGSDIQNALLAYLETSTLTPVKSTVNKLRGIIIARNRLISSIWHHEIPPIVGNVRTCQRCYLSEECFTYNEAFKNEDSEIEPIQSLYQSKLETRDKKDIEFLRKWDRLLLFEEKIISKCKFDMYFLSAEEKEERGDCVNNLKLTKFPLDRGSSLSKRYLYSFFKDESIRTSLNVGDHVLLSSTNGKWTLAKGVITYMERNQVDTELNQFLSPTILNKFNSGDLPFPETDSVDALFRIDKDEYTGGLSLIRSNILKLCILAEHESLRRLIIHLDAPSFTKHKTKPASVVMEQLNSDQRKAIDHVLCADDYALILGMPGTGKTTTIACLIHTLVSNGKSVLLSSYTHTAVDNILLKLKQFNFPILRLGSKSKVLPEVFSFCFGEHDTASDDITVKKIYEEPLIVATSCLGIQHPLFSKRKFDYCLIDEASQIPLPVCLGPLENAHKFVLIGDHYQLAPLVKSSEATENGLGLSLFKLLTEAHPEAVSLLRLQYRMNEDIVSLSNKLIYGGMLQCGSQKTALKRLHISDTDPQKINRLLCSVKIGNSNLPWLHKLLDPAKSVLFFDTDGCSASETKNGRSIENIKEADFIFNSVLALTVLGLEQKAIGVITIYRSQVYCLRRVLSDFPEVEINTADKYQGRDKDVILLSFVRSNPNDSVGELLKDWKRINVILTRAKTKCIMFGSKKTLSSATLFRSLFSFLEEKGWLYLLKEDIGADGTVLTATTNITEHCFRNKKRELKVFDGENVLLKKSKLASFLVDP
The following text describes a protein:
Function:
Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.
Subcellular Localization:
Bacterial flagellum basal body.
Sequence:
MFNTNFYTLKQAMDVALLRQNVHSLNIANVSTPGYKRKYVAFEELLKESEMKLKLSKTNEKHLIGSKNVVEPRVLVDNTTTMRNDGNNVDIDYEMVQLVKNGLRYQVLTRLMSLNIDRYNAVLRGVR
The following text describes a protein:
Function:
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaB. TsaE seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MSREGIRRRPKARAGLTGGGTATLPRVEDTLTLGSRLGEQLCAGDVVVLSGPLGAGKTVLAKGIAMAMDVEGPITSPTFVLARMHRPRRPGTPAMVHVDVYRLLDHNSADLLSELDSLDLDTDLEDAVVVVEWGEGLAERLSQRHLDVRLERVSHSDTRIATWSWGRS
The following text describes a protein:
Function:
Catalyzes the phosphorolysis of N-carbamoylputrescine to form carbamoyl phosphate and putrescine. Is involved in the degradation pathway of the polyamine agmatine.
Subcellular Localization:
Cytoplasm.
Sequence:
MNKKRDFIDTKDFSKEEILFMIEIGRKMKESIKNGHYPQLLKHKTLGMIFEQSSTRTRVSFETAMTQLGGHAQYLAPGQIQLGGHESVGDTAKVLSRLVDILMARVERHQTVVELANTAAIPVINGMSDYNHPTQELGDAITMFEHLPKGKKIEDCKIVFVGDATQVCASTMFMATKLGMDFVQFGPKGFQLREEHLKVAEENCEVSGGSYLITEDVDIALKDADFIYTDVWYGLYEAELSEEERMKTFYPKYQVNKELISKAAPHVKFMHCLPATRGEEVTDEVLDAPYSVVIDEAENRLTAMRALLVYFMNPYVKEAGFAVAEKYDAELELLLRNGAGL
The following text describes a protein:
Function:
Involved in apoptosis. May have a role in rRNA processing and mRNA splicing. Associates with pre-rRNA precursors (By similarity).
Subcellular Localization:
Nucleus, nucleolus. Note=Localizes in the nucleolar-organizing region during ribosome biogenesis.
Sequence:
MAADEEPDSPSGALQTAAEEEETKTFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELAFQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYLFIPSKFKDTYLVYILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIEHLIGKKLPVFPTQDEEVMMLTERVNEAQRFARMELREHGEKKKRKREDAGDDDDKEGAIGVRNKVAGGKMKKRKGR
The following text describes a protein:
Function:
May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein.
Sequence:
MSNRSSRSSTQGGVPPSAPAYPPVAPPVSQYYEEPPIVVVEKGEKEKMKIAEATLEDEIQAYRQDMLNRDPMKINRDLKVGFNEIFAEPDVTLHSIDCVWTNSYKVFELTKLWWYRFLSVICGLPIAICMGCCFACFSFNIIWCFQPCVRAFRINMLFIKQLWAYTVHIFIRPLTLACGGIFSTIRIHQSNGEYKEESFIV
The following text describes a protein:
Function:
Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant H2A.F/Z leading to transcriptional regulation of selected genes (e.g. FLC) by chromatin remodeling.
Sequence:
MEIDEEEPMVFLDRTTRATRGKRMTKLLDDEVEEDEQFWNQEALKEEEHDDEYEAEREVADEFDSDFNDDEPEPDAVAVNEKELRDLPKKRLIYPGKTASKKKKKKTKVVSQLEYIPGDEKPGEELGNKEQEEKEENEAQEDMEGEKVIRKSTRTSVVVRQAERDALRAAIQATTKPIQRKKVGEEKRMTQEEMLLEAAQTEIMNLRNLERVLAREEEVKKKAIVHKAVYKGPQIRYHSKDGCNYLEFCNGASFNSELSTKSVPYPEKAVCVITGLPAKYRDPKTGLPYATRDAFKAIRERFMDEHDGLRKKMEMGDLFDTLVAKGFATKQKRTKIPKSNKSFSLRSSARFLSSESEEESEEDSD
The following text describes a protein:
Function:
Transcription factor. Regulates neuronal subtype identity. Involved in motor neuron fate determination and maintenance, acting as a transcriptional repressor to counteract gene activation by transcription factor unc-3 in a subset of motor neurons. Probably acts by binding to specific promoter elements. Promotes differentiation of URA sensory neurons and prevents them from expressing male-specific CEM neuronal features. Promotes differentiation of AVD and PVC interneurons and their glutamate receptor expression.
Subcellular Localization:
Nucleus.
Sequence:
MSVRIDEPQLFVSMSKEPTQETVNVGGHHDDSSSNCDERVDDQTEEQKSPPASPDLTANLNVFDLESRQKVVQRLLNSQLNLSNLRAPLNLPPIFQALQGPFSIQQQLLGLASGLTAISPGLDDYDEENTNQGEPEDLTLGGFRKETSVKSEEPSESGINASGPAWSYEEQFKQLYELSDDVKRKEWLDDWLNFMHRIGKPVTRIPIMAKQVLDLYELYRLVVQHGGLVEIINKKLWREITKGLNLPSSITSAAFTLRTQYQKYLYDYECEKEKLSNQSDLQQAIDGNRREAPGRRTAPSFPLPFQLPHAASAAATMLNNQLNGLGMRNDLLDDENTLSLQASGLFGTSYGAEQMAILEAHQRNLERAQRAVQQQVARQSLGLTACSNGNGGNIHNSGRESTSSNDSDIPAKRPKLENDVKTNGASSMRISTKHSDNSKTSMSVSMEINGITYQGVLFALDETVSES
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. Membrane; Multi-pass membrane protein.
Sequence:
MPVQASEVAKNVDHLYLFLLVSSLISFVILIGGMTWFIFKYRRKTDSDKTAYITHNTLAEFLWSFIPLVIMIVIFWWGWRIFADLRSVHEKGDIEIHVTARQWQWTFKYPNGVTIVSPNATEKLNTLFQPNGIYVPVGKTVRLVMTSQDVLHSFYVPAFRNKMDAIPGRYTTLTFTPTEKGDFVVYCTEFCGTSHSNMLSAIRVVDNETFDKWYAEAGNVDLSKIPPTELGKKLYAEKACAGCHSTDGSRLVGPSYKGLFGSTREFESGPGVIADENYIRKSILQPTAQVVKGYPPAMPSYQGQLSDDEINALIEYIKTLK
The following text describes a protein:
Function:
Bifunctional enzyme that catalyzes the last two steps of purine biosynthesis. Acts as a transformylase that incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-AICAR (FAICAR). Also catalyzes the cyclization of FAICAR to IMP.
Subcellular Localization:
Cytoplasm, cytosol.
Domain:
The IMP cyclohydrolase activity resides in the N-terminal region.
Sequence:
MQALLSVYNKSGIVEFSKILSSKGFNLISTGGTAKSLVDNGLKVQQVSDVTEYPEMLDGRVKTLHPKIHGGLLARPELAHHQADLNKYNIKPISIVVVNLYPFVETVSKESTTLEEAIENIDIGGHTLIRASSKNFQNVLIIVDPSDYKWIGERIQSSTDSTNVLSSITLEERKKLALKAFQHGCSYDAAVSQYLSKVELTNATTIQGVKGTDSASVNVEFPQTFLPLYEKKNDLRYGENPHQKAALYQCPGTGGIANAQLLHGPALSYNNILDGDAALKAVREFDRCACVVIKHTNPCGLSVGVNDSEQAEVYKRAFNGDPKSAYGGILGFNRTLTLETATALKSVFYEVIIAPDYTEDALALLSKKEKLRILRIPEAANQIQFTQPDIRTITGGALLQSPNPIIRGDLAEATKNWKVVTENKPTEQQMKDLLFAWRVSKHVKSNAIVLSKDETIVAIGAGQPNRSQSVDICMKVGGDKVKGSVLASDAFFPFADSIDLAHQGNIACIVQPGGSIRDQEVIDAANKYGIPMVFTGNRNFLH
The following text describes a protein:
Function:
[CLE17p]: Extracellular signal peptide that regulates cell fate. Represses root apical meristem maintenance. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2.
Subcellular Localization:
[CLE17p]: Secreted, extracellular space.
Sequence:
MTHVLVRRQGQGKKRRWDVNMTMCFFLFFFVFYVSFQIVLSSSASVGYSRLHLVASPPPPPPRKALRYSTAPFRGPLSRDDIYGDDKRVVHTGPNPLHN
The following text describes a protein:
Function:
RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex and disappears during maturation of the complex and is replaced by GAR1 to yield mature H/ACA snoRNPs complex. Acts as a competitive binder for CBF5 probably required to prevent non-cognate RNAs from being loaded during transport of the particle by inducing a non-productive conformation of CBF5.
Subcellular Localization:
Nucleus.
Sequence:
MSETGSNLDPANVDATTLPPIGVPEAPAQAASPHLATEEPSPDTVQLAAVDEVDHQQTASIATSAASQLPIMEPAVMDAGSEAAQVDVMAVDANEPASNLGDPAADSRPIANGETTQTNMANLDPPQNEVRTMANGETMAVTYADLGGPSDEINSEPAKDIKTAADGETIAASSANLGPEESAQTVEPVAEIMVEPAQIKTAIDGEITAETSADLGGVADSAGTVKSVTDGETLASTSADLGGPAEGNLEPANVNIATDGETIASTSADLGGPAADVNMADVKTATDGETKGESEGKIDPDTERKEQPGDIVVDTGDAIDRALAEEAAEASDSSSDSSSDDSSSDDSDSESDGDPEETNVAGEEEEDSTGPLKTANEQIDEPIPQLPEGFAISEKTAIEHVGTLQSVTNRTAVIKATVSGEFRVLGDDTIFCFEDKTIVGVLFETFGLVKMPFYSVRVSSDEEAAALKEKVGSPIYYVAGHANFLYTDRIKSIKGSDASNNYDEEVPEEEQEFSDDQAEMEVKSARKKKKKAKKRADGGENEDAPKEVKRQRNDRYKERTDNRQGGGNNYNSDSRYHNNNHGSGYSNSNNQNNNNQMYPLMPGGMSFPGMGMGMGMPPMPPMPGMSPLPGMPPMPGMPMMPPGMPFMAPDQMLQMQQHFAQMQQQQQQQAMSQGMSQQQMQQWQLQQLQMQQAAMFPPPNNSNNRHNDQGQGHQDRNNPRPYS
The following text describes a protein:
Function:
Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Dispensable for SPC enzymatic activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSDQLLEQVRDAFEGQIDFEGQRLAEMLTTVLLGAAGIIAFLVGYFTQDIRMTLYVGLAGTALTFLVVVPPWPFYNKNPEDWLPASNAKQSFNVDVDGQKVG
The following text describes a protein:
Function:
Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis. This subunit may play a central role in organizing the structure.
Subcellular Localization:
Cytoplasm.
Sequence:
MHPMLTIAVRAARKAGNVIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTDQDVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKAKQYATTYINIIGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGGHNYMMTGNIVAGNPRVVKAMLANMRDELSDALKR
The following text describes a protein:
Function:
May control cell-cell adhesion, cell migration and proliferation, cell morphology, and protects renal epithelial cells from oxidative cell injury to promote cell survival.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Cytoplasm.
Sequence:
FPRAATFGSVLSVNGKTENYILDTEPGLQESLKCAVQNHIRDEELLWYREDGRVDLKSGNKINSSSVCVSGISEDDNGITFTCKLQRNQSVSISVVLNVTFPPLLSGNDFQTAEEGSDVKLVCNVKSNPQAQMMWYKNNGILNLENHHQIQQTSKYFQLSITKVKKSDNGTYSCIANSLIETKTKDFHLIVKDKGSTVPIEPIIAACVVVFLTLVFGVIARRKRIMKLCRKDQGPQCRTAL
The following text describes a protein:
Function:
The main replicative DNA helicase, it participates in initiation and elongation during chromosome replication. Travels ahead of the DNA replisome, separating dsDNA into templates for DNA synthesis. A processive ATP-dependent 5'-3' DNA helicase it has DNA-dependent ATPase activity.
Sequence:
MIADNKFDGPHRGKKKKEVSTIEILARQQPFDREAEMGVIGSVLLMPDICDEIASLKADDFYDEANQIIYRHLRDMFDSGEKIDITLLVSRMRTAGDFEKVGGAAYLAQLGGSVANAAHAAFYGEIVREKAMFRRLIESGTEILRDAYEQNSTAKELCAQAEQKVFAIMEGRSGNSVWAISDVLHQAMDRMEARMRDDYVEGGAETGLTDFDQMTGGLHHGELIILAARPSMGKTALAMNIAEHCAIVQREPVLFVSLEMSAIELADRMLCSLARVNGHRLRNGTISSDDRDRLVSKANDISQAPLFVDDSPSRTVSEIAAAARRIKRKEDGLGLIVIDYLQLIEPDNSRDPRQEQVAKIARRLKGMARELEVPLLCLSQLNRQAEDGKDHRPKLSHLRESGAIEQDADVVMFVHREEYYHRGEDKAQFAGQAEIIIAKQRNGPVGDVELTWEGDFTRFSNRAAEHHSEFDDYREFTSPGGF