lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and PABP.
Subcellular Localization:
Cytoplasm.
Domain:
Contains a pseudokinase domain. The protein kinase domain is predicted to be catalytically inactive because some of the residues important for catalytic activity are substituted and it lacks the equivalent of the binding site for a peptide substrate. However, it has retained an ATP-binding site and ATP-binding is required for mRNA degradation, stimulating the activity of the PAN2 nuclease in vitro. The nucleotide-binding site is juxtaposed to the RNase active site of PAN2 in the complex and may actually bind nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active site of the deadenylase and thus increasing the efficiency with which this distributive enzyme degrades oligo(A) RNAs; The N-terminal zinc finger binds to poly(A) RNA; The pseudokinase domain, the coiled-coil (CC), and C-terminal knob domain (CK) form a structural unit (PKC) that forms an extensive high-affinity interaction surface for PAN2.
Sequence:
MQQYSPYPQYSQSLIRNKQGRRNMGSFFMSESLKQDIVHQKQLLYMTLDPNDPRIKNIPPMLNKYHSLYPLDQDGAKENQGKMFGYVTSVYKAICTQDGLPYAIRRIEGFRLSSEYALQAAESWRNLQHPNIVSLKEIFVSKEFGDNTLFFTYDYFPGSETIESKFLSQPNQTSFQPISESVLWSFITQLVSALKTIHSLGLVCRVIHPSKILLTGKNRIRLNGVGIFDVVNYDSPRNLAQFQHEDLLLLGRLILTLACRSAASITAQNLSNSIEYVSNTYSKDLYNLIVYLLTKPVINLPNIDEVVTMISGRLLQENNYLHTYTDDLETELGKEYENGRLFRLVTKLGFINERPLYDMDPRWSETGDRYLIKLFRDYIFHQVYDDGTPVLDFYHVVETLNKLDCGVDEKILLMSRDEQSLLVVSYKDLKKCIELAFSELVSQKSHLN
The following text describes a protein:
Function:
FimB is one of the 2 regulatory proteins which control the phase variation of type 1 fimbriae in E.coli. These proteins mediate the periodic inversion of a 300bp DNA segment that harbors the promoter for the fimbrial structural gene, FimA. FimB switches FimA on.
Sequence:
MKNKADNKKRNFLTHSEIESLLKAANTGPHAARNYCLTLLCFIHGFRASEICRLRISDIDLKAKCIYIHRLKKGFSTTHPLLNKEVQALKNWLSIRTSYPHAESEWVFLSRKGNPLSRQQFYHIISTSGGNAGLSLEIHPHMLRHSCGFALANMGIDTRLIQDYLGHRNIRHTVWYTASNAGRFYGIWDRARGRQRHAVL
The following text describes a protein:
Function:
Positive regulator of phosphatidylinositol 4,5-bisphosphate turnover and negatively regulates signaling through the cell integrity pathway. Involved in rDNA silencing (By similarity).
Sequence:
MSGNSAANAAALAAFNGIGKKKKESTTKLNGTDNNTNHLGVIGSTSNQTKQHQQQQQQPQALRTPLPAHPSRKKSNKFSQLKRLNTAPAMASLQPALQIASPSISPTQPSAPASALDSDPDYFTLSPHTIPSKNEIAKSPQTPQDMIRNVRQSIELKAIPNNAQAKRLSVDYSPQEMLKNLRHSLHSRTKTSPMLTTSDKMGQTMLAEMRDRLENTRRIASNSVASLSLSPNLDFNKSTSDVSNLSHHYDVDTVSTDSFASFNSSINDRHLPHGISIDVTNHDSDEDEIDDREREEDHEPLDNGELKSTNNKVTVSSRLRRKPPPGEDFQMQLNDKSRDTISSGSYSLNPDEVYSFTDPDSYENLVSEVEVGETTRLFPQFPDANHYHQHSSKFRKKHQKVKPINGIYYRDMDSSNTSDTEESTSNLPSRSTTPLLGQPQQQVHFRSTMRKANTKKDKKSRFNELKPWKNHNDLNYLTDQEKKRYEGIWASNKGNYMSQVVIKLHGVNYETQKDPKEEAKMEHSRTAALLSAAAVEDSNYNGNNSLHNLDSVEINQLICGPVVKRIWKRSRLPSDTLEKIWNLIDFRRDGTLNKNEFLVGMWLVDQCLYGRKLPKKVDNVVWDSLGGIGVNVTVKKKK
The following text describes a protein:
Function:
Involved in the biogenesis of the 60S ribosomal subunit.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MANPRQRRKQRSGHARLTRRTANRVKKPKTFGNHFISEAWDKNLTLKQNYQKMGLIVTPNHATGGTEKLYPTPKRDENYEPTAEELEEVKKNLLPGQALIRRNDDGEIIEVVYGKEKTLDDVLDAPIDQAPAKTDLVAKLEREAAERAKPRQKNPLSKYEREYVNRLIAKYGTDDESFEKMARDTKLNPRLHSSAHLKALFKRLDL
The following text describes a protein:
Function:
Required for myofiber maturation.
Subcellular Localization:
Cytoplasm, myofibril, sarcomere.
Sequence:
MASSVEDQQLQQEEAESVKDVQSHYLRCPSPSFSMMSDRFSTVSDRFSVISGSEAESIFMEPIHLSSTIAAKKIISEELPPRPARVSSPPDSALEPAQQLMVEDLYSRVQELLDERSLYNTPCVLDIQRALLRDRLEAPLSPVDEVWPNVFIAEKSVAVNKGRLKRLGITHVLNAAHGTGVYTGPLFYSGMNIHYMGIEVDDFPDADISPHFRSCAEFLDDALLTHRGKVLVDSMMGVSRSAVLVAAYLMIFQNMSIMEALLEIRKKRAISPNEGFIKQLRQLNETLMEERDEDDDETLSQCSVIDARGRLEEQESVFGVKADSIMVEEEEDGGGSVISSVASSAAAAALRAGVQCGSQQPNMQQPADQPSLPGQTREDEDGDVDRMILEWQKRNEKYQSEDWWEAQLLCEDEDDGEDKTQRAVRPDDLESVTSEDVRMVKERIGRRPRRAASLAGSTSSCSSYVDLWKQRLQELEEQAAARHRLQDQDTSSETQQKKIDDDVQSILSDSSSMYNFCKKNKENLTPLERWKIKRIQFGWNKKENAENGEQSEAEPAAAPDLEDVNLTAYQTWKLKQQKKHGGEENKEEILQMSRGEDTATARRRQRREEVLERSRRNLQESQSVCGWETESALSSSIPLSAFCAGAFPSASVCGDDSMSVLSGRSSVLSGRSTRSLPPAVLETPAPPTPVLGPNGEQMVNIANIQNWIASVVNETLQQKQTEMLMGASVAPSRAGSVFSAGRGVDDDKSSVLSGLSASTGLSRSRAESVVSVGAKARSVLSAAGRAESVFSAGGASQLSCGSRKSKITTTSVPLYSLFQDQVNLHKLDTMEKEIKSDMRDKMASYEIKKITEDNKRSTLYKKKKPKEDDEDVDIAKSNGLEELEARTCEKPKPKRDYGRSGILNLPASANNPTSSIDEWLEHVRPPSSKPRVYDGDSGPIRMSRPAYEELQEPSGLDFTSRRSSVSVEVDEEEDYSFRFSSRNCADDDLDPELSYSSRRSPSFNGLSESTSFASRRSYSRYEDEERSSFQNHSIKQKSSVYEDSGRTAGSRRDEEEDEEISAFIAQIKQRARARVAEEMEDDEVLTAWRKQEESKSHDHK
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MKIINIVFLFLVVVGLALSNPHHHNTWVNQDVQRSIDLTTQLSKQILSVKAKSLVDNNKNYQISFDNTYHVSVQAFDDKNNELKVHLSPNSINIKEGFNTFDIELNNKYKINEVLSLKLKVTLMSQMKPYPVEIKQGQTQLVLYNDNHYFTSPYKTETQKTTVKLASGKVESFSEIKPSSLKTNTIVYGPFSNVEAFTVSPMRIHFENSAHFMVLTQLKKEYEVSHWGNLAVETSYYLENQGAHLKGPFSRLDYQRNPGANPSHISEINEAVPLSAADFYYRDSIGNISTSVYQYQSNRINFKITPRFPLMGGWKNNFYTGYNLPIQNFLSVDSADGSYHLNVTFGVGIDNIYVEDHQVKIILPEGATDIKVKSPFPVTETREIRKTYLDTVGRPVIVLNVRDTSFENYRYIQVTYNLSSLSIFHEPLLVIGAVFTFCLFIMFYSRFDLSINKSKVN
The following text describes a protein:
Function:
t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells.
Subcellular Localization:
Cytoplasm, perinuclear region. Cell membrane; Lipid-anchor. Synapse, synaptosome. Photoreceptor inner segment. Note=Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region. Colocalizes with KCNB1 at the cell membrane (By similarity). Colocalizes with PLCL1 at the cell membrane (By similarity).
Sequence:
MLQLVEESSKDAGIRXLVMLDEQGEQLERVVDEREQMAISGGFIRIMEKMLGSG
The following text describes a protein:
Function:
Implicated in the level of global muscle contraction and cardiac function. Phosphorylates a specific serine in the N-terminus of a myosin light chain.
Subcellular Localization:
Cytoplasm.
Sequence:
CPRRPDPPAEKEADILETIPEGVAASQGPFPVHGDPDLDFQPCGPGRGSGQKEEEEEAPAVPPVTTGGRGGFPRDVTVSAPSDDCPPPPAPFAHRQVSLTAANASSQYSINTKEALGGGKFGEVCTCTEKATGLKLAAKIIKKQSAKDKDMVLLEIEVMNLLNHQNLIQLYAAIESPHHIILFMEFIEGGELFERIVDEDYQLTEVDTMVFVRQICDGVLFMHKMMVLHLDLKPENILCVSSTGHMVKIIDFGLARRYNPKEKLQVNFGTPEFLSPEVVNYDRISEKTDMWSVGVITYMLLSGLSPFLGDNDTETLNNVLAANWYFDEETFEMVSPEAKDFVSHLIVKDQSERMTAAQCLEHPWLNDLAEKARRCNRRLKSQILLKKYVMKRRWKKNFIAVSAANRFKKISSSGSLMALGV
The following text describes a protein:
Function:
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.
Sequence:
MNLQIELYKFQQESLKRSSPERAAIFSDFIQGLSEEFRNRRLLRIGDFAPDFTLKNTKGETIILSEQLKTGPILLKFFRGYWCPYCGLELRAYQKVVNKIRALGGTILAISPQTLVASQKTIDRHDLTYDLLSDSGFQTAQDYGLVFTVPDAVKQIYLQSGCVIPEHNGTEEWLLPVPATFVIDRRGHIALAYANVDFRVRYEPEDAIAILLSLFVGN
The following text describes a protein:
Function:
Required for ciliogenesis. Acts as a tethering factor that facilitates recruitment of vcp/p97 to the intraflagellar transport complex B (IFT-B) in cilia (By similarity).
Subcellular Localization:
Cell projection, cilium.
Sequence:
MHVTRPKSSKGRSRPMITNSSMIYTPSQPSALSPQPPAAAKTKDKSNQSLRSRAILRRSSQPTTDILTEAYDRPPEEPVSLNRYRVLPSIEKKTSTDNQKCSQCVSRHRKCQHTNARLDVVSDSTPPEESDLLLAIRTPCGQRFKRSFRPSDQLKGVLSAAEAEFGDRFDNCIIETMDVPRRTFSNLTMTLAQCGVLNKSVLCISHDDSEMDLT
The following text describes a protein:
Function:
Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.
Subcellular Localization:
Cell projection, cilium, photoreceptor outer segment. Cytoplasm, cytosol. Peroxisome membrane.
Sequence:
MALAVLRALEPFPAEAPPLAVLLPPGGPWPAAGPAGLVLALRPAGAGPTGPALLVAALEGPGEGPGPESGPDPEPEPGPPELLVSRTLLRLLALGSGARVRARPVRRPPALGWALLGAAPGSGSGTGPRAGPVLVRRGEALPALGPRVLETRPALQGLLGPGTRLAVTELRGRGTKAGQLPGDSHPPLPAPPVVSSFAAPSVPRRLRGILGGTGDALGVSRSCLRGLGLFQGEWVWVTPVREGAQTPRPHLAKMQVQDPRWNLSEKLGPGSPELGEPLADGVALVPANLAFNLSCEPLNIGELSIQRYSEGFRSPENKGSCSVLPGPPFARELHIEIVSSPHYSTSGNYDQALYQHFETPRVVQEGDILCVPTVGQAEILERSPEKLFSTSLGGQKIYSEGSNLAFSGCRGSLLTGTGSVLLRGPPGSGKTTAITAACGRLGLHLFKADCARLCADTSGAVENKLRATFSRARLCRPSVLLLKGVELLGWERDGLGEDAHVVAVLRHLLLNKDPLISNLPLLVVATTNCPQNVPPDVQIAFPHELEVPMLSEEHRLNILQALTARLPLGQEVNLAQLARRSAGFVLGDLCALLAYSSRAACARILTGVMTAGSLSDEDEGELCTAGFPILAEDFGLALEQLQMAHSQAIGAPKIPAVSWQDVGGLQDVKREILETIQLPLEHPELLDLGLRRSGLLLYGPPGTGKTLLAKAVATECSLTFLSVKGPELINMYVGQSEENIREVFSRARAAAPCIIFFDELDSLAPSRGRSGDSGGVMDRVVSQLLAELDGLHSSQEVFVIGATNRPDLLDSALLRPGRFDKLVFVGPSEDRASQLRILSAITRRFKLEPSVNLSSVLDRCPTQLTGADLYSLCTDAMTAALKRRVQDIEDGVEPANSMLLLTMEDLVQAAARLQPSVSEQELLRYKRIQRKFTVS
The following text describes a protein:
Function:
Prion-like protein that has PrP(C)-like neuroprotective activity.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MRQRVACCWVLLLLAATFCQPAAAKGGRGGSRGAARGMARGAARSRHRGLPRYGGALRVAAAAAAAGAAAGAALHQARAETEYHEGNGTAWTSVAPGWVEWGWAMPWLCPLAAILHH
The following text describes a protein:
Function:
Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates mRNA stability. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing.
Subcellular Localization:
Cytoplasm, P-body. Cytoplasm, Stress granule.
Sequence:
MSATSVDQRPKGQGNKVSVQNGSIHQKDAVNDDDFEPYLSSQTNQSNSYPPMSDPYMPSYYAPSIGFPYSLGEAAWSTAGDPPMPYLTTYGQMSNGEHHYIPDGVFSQPGALGNTPPFLGQHGFNFFPGNADFSTWGTSGSQGQSTQSSAYSSSYGYPPSSLGRAIADGQAGFGNDTLSKVPGISSIEQGMTGLKIGGDMTVAVTKTVGSALSSTGMTSIAANSVPVVSSSAPKPTSWAAIARKPAKPQPKLKPKGNVGIGGPAVPPPPIKHNMNIGTWDDKGSMVKAPPTQPVLPPQTIIQQPQPLIQPPPMVQSQLPQPQPQPQQPQGPQQQAPPHQLQQQQQQQLQNRWVAPRNRGVGFNQSNGAGNENYGIGVMPVSSSPSGIEVHPVLEKLKAINNYNPKDFDWNLKNGRVFIIKSYSEDDIHRSIKYSIWCSTEHGNKRLDAAYRSLNGKGPLYLLFSVNGSGHFCGVAEMKSVVDYNAYAGVWSQDKWKGKFDVKWIFVKDVPNNQLRHIRLENNDNKPVTNSRDTQEVPLEKAKQVLKIIATFKHTTSIFDDFAHYEKRQEEEEAMRRKYCFGSNQLVG
The following text describes a protein:
Function:
Forms pores that allow passive diffusion of cations across the outer membrane. Part of a cation efflux system that mediates resistance to copper and silver (By similarity).
Subcellular Localization:
Cell outer membrane; Multi-pass membrane protein. Cell outer membrane; Lipid-anchor.
Sequence:
MSPCKLLPFCVALALTGCSLAPDYQRPAMPVPQQFSLSQNGLVNAADNYQNAGWRTFFVDNQVKTLISEALVNNRDLRMAALKVQEARAQYRLTDADRYPQLNGEGSGSWSGNLKGDSATTREFSTGLNASFDLDFFGRLKNMSEAERQNYLATEEAQRAVHILLVSNVAQSYFNQQLAYAQLQIAEETLRNYQQSYAFVEKQLLTGSSNVLALEQARGVIESTRSDIAKRQGELAQANNALQLLLGSYGKLPQAQTVNSDSLQSVKLPAGLPSQILLQRPDIMEAEHALMAANANIGAARAAFFPSISLTSGISTASSDLSSLFNASSGMWNFIPKIEIPIFNAGRNQANLDIAEIRQQQSVVNYEQKIQNAFKEVADALALRQSLNDQISAQQRYLASLQITLQRARTLYQHGAVSYLEVLDAERSLFATRQTLLDLNYARQVNEISLYTALGGGWQQ
The following text describes a protein:
Function:
Acts as a chaperone during the assembly of the 26S proteasome, specifically of the 19S regulatory complex (RC) and appears to have an overlapping role with RPN14.
Miscellaneous:
MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
Sequence:
MSNYPLHQACMENEFFKVQELLHSKPSLLLQKDQDGRIPLHWSVSFQAHEITSFLLSKMENVNLDDYPDDSGWTPFHIACSVGNLEVVKSLYDRPLKPDLNKITNQGVTCLHLAVGKKWFEVSQFLIENGASVRIKDKFNQIPLHRAASVGSLKLIELLCGLGKSAVNWQDKQGWTPLFHALAEGHGDAAVLLVEKYGAEYDLVDNKGAKAEDVALNEQVKKFFLNNV
The following text describes a protein:
Function:
UDP-glucose-dependent glucosyltransferase involved in C-glycosylflavone biosynthesis. Has a strict stereo selectivity and shows a preference for apigenin and luteolin as substrates, but could not recognize flavonols, anthocyanins and xanthones as glucosyl acceptors. No activity with orientin (luteolin 8-C-glucoside) and luteolin 4'-glucoside. Can use UDP-galactose instead of UDP-glucose as a sugar donor, but not UDP-glucuronic acid.
Sequence:
MGSLTNNDNLHIFLVCFIGQGVVNPMLRLGKAFASKGLLVTLSAPEIVGTEIRKANNLNDDQPIKVGSGMIRFEFFDDGWESVNGSKPFDVWVYINHLDQTGRQKLPIMLKKHEETGTPVSCLILNPLVPWVADVADSLQIPCATLWVQSCASFSAYYHYHHGLVPFPTESEPEIDVQLPGMPLLKYDEVPDYLHPRTPYPFFGTNILGQFKNLSKNFCILMDTFYELEHEIIDNMCKLCPIKPIGPLFKIPKDPSSNGITGNFMKVDDCKEWLDSRPTSTVVYVSVGSVVYLKQEQVTEMAYGILNSEVSFLWVLRPPSKRIGTEPHVLPEEFWEKAGDRGKVVQWSPQEQVLAHPATVGFLTHCGWNSTQEAISSGVPVITFPQFGDQVTNAKFLVEEFKVGVRLGRGELENRIITRDEVERALREITSGPKAEEVKENALKWKKKAEETVAKGGYSERNLVGFIEEVARKTGTK
The following text describes a protein:
Function:
Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of DNA damage, involved in the regulation of DNA damage response mechanism. Required for the control of telomere length and genome stability.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Vacuole membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MSQQSTQAFDALNRIVIDLRSRSDEQRKRAALELRELVEVASRDLPQERFLELYNVVNNKITSLISHGDLERTGGIYAVDALVDFEGIDVGQRVTRFGQSLRAVLRGKDLVPMQPAAVALGKMCRPGGSLVSDLVESEIKTALEWLQSDRIEERRYSAVLVLRELGRNSPTLVYTFVGLIFDQIWVGLRDQRLLIRQTAAEAISACFQIIRERDQNLRQTWQAKIYDEAVQGVRQGTVESIHGSLLVIKELLQQGGMFMHEHYPEVCEIVFRHKDHRDAQIRKTVVMLIPELAHYSPTEFAQSYLHPFMVFLSGMLKKDKDRNDAFLAIGNIANAVKSAIAPYLDGVLIYVREGLSLKSRRLGTVDPVFDCISRLAVAVGQTLSKYMEALLDPIFACELSPKLTQALVDMAFYIPPVKPIIQERLLDMLSKVLCGEPFKPLGAPTPNNIAAAPVVPKDSKDPQAYEHRQSEIKLALNTLGSFDFSGHVLNEFVRDVAIKYVEDENPEIREAAALTCCQLYVRDPIVNQTSHHAIQVVSEVIEKLLTVGVGDPDPSIRRVVLAALDQRFDRHLAKAENIRTLFFALNDEVFQIREVAITIIGRLTHVNPAYVIPSLRKVLIQMLTELEFSDVARNKEESAKLLSLLVQNSQKLIKPYVDPMIAVLLPKARDPSPAVAATIMKAIGELACVGGEGMIPYIKQLMPIIIEALQDQSSSAKREASLRTLGQLASNSGYVIKPYLEYPRLLEILQNIIRGEPQRGPLRQETIKLMGILGALDPYRHQQVEERSPEMQLRLESNQMTDISLMMTGLTPSNKEYFPTVVINALLNILKDPSLNQHHAMVIEAIMSIFRTLGLECVSFLDKIIPAFLSVIRTSPVNRLESYFSQLSLLVTIVRQHIRNYLPEIVSVLQEFWNTSAPLQANILQLVEAISRSLEGEFKIYLAGLLPLMLGVLEKDTSTRRLPSERVLHAFLVFGPSAEEYMHLIVPVIVSVFEKPQQPSFIRKAAIETIGKISRHVNLNDYASKIIHPLSRVLAGSDSSLRLASLDTLCALIFQLGRDYLHFAGTINKVLNSHQIQHQNYELLVSKLQKGEALPQDLSAEERYLNQSDEVDFSDVSNKKLDSNPVHLKAAWDATGKSTKEDWQEWMRKFSAAVLLESPNHALRSCAQLASVYPPLARELFNSAFVSCWGELFEGYQDDLIQNIEMAIKSPHVTPDLLGILLNLAEFMEHDDKALPIDIRVLGREAGRCHAWAKALHYKELEFCQDQTSGAVEALIQINNQLQQYDAAIGILRKAQLYKDGITLRETWFEKLERWEEALEFYKRREEDFPDQAETFDVIMGKMRCLHALGEWESLSALAEDKWHTSSLEIKRAIAPLATAAAWGLRKWDLMDDYLSVMKSHTPDRSFFGAILALHRNQFREAALFVQKAREGLDTELSALVSESYNRAYTVVVRVQMLAELEELSIYKQSDDNPKKQEVMRRTWETRLLGCQRNVEVWQRMLKLRALVITPMENMQMSIKFANLCRKSGRMGLAEKHLKTLMGGDESLDVVLPQIVETANGERRLKVSTKHIEAPVQYAILKFQWAVGKQSQALEALKIFTSGLAEKLQQAQVANQGGVANEVHVMNGHNGTNGVMMNGNGYTNGLGANAQSLLTAKGLADHTTLLARCCLKQGEWQVAQKKGNWQYDNVNDILASYKAATHFNPQWYKAWHAWALANFEIVQSIQTELGHDWHNIPTNAVIDHVVPAVRGFFKSIALSQGSSLQDTLRLLTLWFAHGGHVEVNQAVTEGFSSVSVDTWLEVIPQLIARINQPNARVRASIHNLLADVGRAHPQALVYPLTVAMKSAPNTRRSRSAMQIMDSMRQHSPKLVDQADLVSKELIRVAVLWHEQWHEGLEEASRLYFGDHNIEGMFNTLAPLHDMLDNGPETLREISFAQTFGRDLQEAREWCITYQRTKDLGDINQAWDLYYQVFRRIARQLPQLNNLELAYVSPKLLNAHDLELAVPGTYQSGKRIISIVNFESNFSVISSKQRPRKLSLKGSDGNAYVFCLKGHEDIRQDERVMQLFGLCNTLLTSDSESYKRHLNIQRYPAIPLSQNSGLLGWVPNSDTLHVLIREYRESRKILLNIEHRIMLQMAPDYDNLTLMQKVEVFGYALDNTTGQDLYRVLWLKSKSSESWLERRTNYTRSLGVMSMVGYILGLGDRHPSNLMLDRITGNIVHIDFGDCFEVAMTREKYPERVPFRLTRMLTYAMEVSNIEGSFRITCENVMRVLRENKESLMAVLEAFIHDPLLNWRLNGEASPVGPNFRSERRESMISPQVRRPSVMDGNVPPSALTADVGDPIAAPGGPPASRPRARTNSTTQGSQDIEAHENQNTRAVQVLVRVKEKLTGHDFKPEEELPYIQQVDKLLIEATKLENLCQHYIGWCSFW
The following text describes a protein:
Function:
Involved in cytoplasm to vacuole transport (Cvt) and autophagic vesicle formation. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy). Also required for mitophagy, which eliminates defective or superfluous mitochondria in order to fulfill cellular energy requirements and prevent excess ROS production. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes (By similarity).
Subcellular Localization:
Preautophagosomal structure membrane; Peripheral membrane protein.
Sequence:
MGDSKELVWNGSINVQIKLDSRLLVDGVPEGRRLVNIRVPRESHIAIYTPLVLERLRNVLRSDIEELLPKVWYSYKDISLPWSIPFGTLFDIYNGAHKGISGSRDNYINVWKLNLVTDEKFPINVIPIIEGQDQLRKFMMQSWKQCCFILNGSSKRVMSLSLQDSLEVWEGVTERDYAKYSGVIKRILPRTPRRIPVAIHAANGGPIVQTTEPTLTDTSFSQAVEGIVKADFVVCQGIVMYLRDFSDTSLYDVYDKLHSIDGYLHLIANL
The following text describes a protein:
Function:
Regulates the transcription of the copA and cueO genes. It detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations.
Miscellaneous:
MISCELLANEOUS: CueR tightly binds Cu(1+) via a linear S-Cu-S center.
Subcellular Localization:
Cytoplasm.
Domain:
It contains an N-terminal DNA binding region and a C-terminal metal binding region.
Sequence:
MNISDVAKITGLTSKAIRFYEEKGLVTPPMRSENGYRTYTQQHLNELTLLRQARQVGFNLEESGELVNLFNDPQRHSADVKRRTLEKVAEIERHIEELQSMRDQLLALANACPGDDSADCPIIENLSGCCHHRAG
The following text describes a protein:
Function:
Catalyzes the phosphorylation of pantothenate to generate 4'-phosphopantothenate in the first and rate-determining step of coenzyme A (CoA) synthesis.
Subcellular Localization:
Cytoplasm.
Sequence:
MIIINAVTPLPSRHSSEGIFFVSSRSALSLCLCLSLSLRPPLFRQSCTSPAFFFFLLLLLLLRREARAASQGLGGTERKAGRGKRATGNERPALSEGRRNKRPGAMGERLRGQAAGSFPSASSSSPSLAAAAAAAPAPPAPGCSLHNGLLLHNGFHPLPGRNGEAAPHPLLFGSPPAKKGSRPRRRVDSGRKNRPPFPWFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAMHRFIQMGSEKNFSSLHTTLCATGGGAYKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGQPECYYFENAADPEKCQKKPYCLDNPFPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKDIYGGDYERFGLQGSAVASSFGNMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNEVRVFINRLSNLPLCYSKTHRYLIYVTYMTDGNN
The following text describes a protein:
Function:
Plays an important role in the formation of lipid droplets (LDs) which are storage organelles at the center of lipid and energy homeostasis (By similarity). Directly binds to diacylglycerol (DAGs) and triacylglycerol (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MERGPTVGAGLGAGTRVRALLGCLVKVLLWVASALLYFGSEQAARLLGSPCLRRLYHAWLAAVVIFGPLLQFHVNSRTIFASHGNFFNIKFVNSAWGWTCTFLGGFVLLVVFLATRRVAVTARHLSRLVVGAAVWRGAGRAFLLIEDLTGSCFEPLPQGLLLHELPDRKSCLAAGHQWRGYTVSSHTFLLTFCCLLMAEEAAVFAKYLAHGLPAGAPLRLVFLLNVLLLGLWNFLLLCTVIYFHQYTHKVVGAAVGTFAWYLTYGSWYHQPWSPGIPGHGLFPRSRSMRKHN
The following text describes a protein:
Function:
Component of the exocyst complex.
Sequence:
MERPLAGEGLDLDAMEFKEELVEMRQHLRGLVAEFCVGASGNVTAPDRWLSELNVAWLLHLSELGASARGSFISRQLQQLVQSWILALRKINTSMIWACFSGFSSQEKATVAPPAAPEFVCFIEATLWKMFIFAGTIAGTIAAPLNFDDTNCQEHIVSRAAGELRALLDMRDALSSVSEHIMMSFRSSPYVQSTIHKDITDDMGGLLSAELGKLDEAVRDARYRIRTAAMSSLDDDDSSAEAGGTTQTTLKSSPDIHKVTRSVINCIKVLSANHTHGYQDGLIMEMATSLEEKLTRVSQSFPDQSLRFLFLINNTHFIRQQLHHDLTHKINTYIESYLQVSWAPMLKCLNNTTFHCFKRNSPLPKFESEFQMTYAVQKLWKVPDPWLRKRLREAIIEIVVSDLTKYLEDNNRITPGITPQEVEEMLQELFEG
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.
Miscellaneous:
MISCELLANEOUS: This protein may be expected to contain an N-terminal transit peptide but none has been predicted.
Subcellular Localization:
Mitochondrion.
Sequence:
MKLFYFFLLSFLSSYIIAFSFKSTQSAHFILSVGRCNENYGNNIKKNRLYSTNNDHLKLLKYVREVTNASIQLCNKALKECNNDVDKAIEHVRKNTKSSTFVSTNIKVKKEGLVASQIKDDKIVLLELLTDSDFVARNKMFVQFVYSLLNVTLDNDLSVGNCKNAGDNKNSEDGYTTSGNILSNNNIMDEILSLPYVDEENKSNSTMREQLNYLRNIFREDIKIGRFSKYSKKNPNEFLHYYIHNKLDDHVGLSGVLLVLHINNLDEILKTKKEDIVNFANDLSMHIISAKPASVSIDTLNPKITKKEMDIIRDGLKDMKKPENILNNMIQGKMKKFYSSIVFLEQEYMLDETKRKVSQVIKDFGKDHNINISVNHFNYFAIGEKNVLME
The following text describes a protein:
Function:
Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine; Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine.
Sequence:
MNRTPTLRAPDLAGVPDCLVIVGGSMAAVKAPTALRRLREGGASTAVIATRAALAFITPLSLATAGNCEVATDETWFAPQPIAQHLSLARARVTVVLGASAELLAAAAHGHADTLATATLLSAEGQVLWVPAMNERMWLHPAVQANAERLRGWGHLFLGPETGAFGTPGEGSGTGRMAEPEAIAARALALLNEQDAEAEAAPQDLAGLKVVVSAGPTREYLDPVRFISNPSSGKMGFAVAEEARTRGAEVVLVTGPVNLPDLSGVQTVRIETALEMQAAIMEAAGDADMVVMTAAIADYRAAAPKSEKEAKTPGDVTIHLTPNPDILAGLGAEQAAHPGRVLVGFAMETHAGVERAALKAQRKNADFILLNYPTREGTAFGGDDNQVTLVRADGTHADWPRISKREVARRLLDEARQIRERR