lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Domain:
Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala/Ser (NPA).
Sequence:
MNGEARSRVVDQEAGSTPSTLRDEDHPSRQRLFGCLPYDIDLNPLRIVMAELVGTFILMFSVCGVISSTQLSGGHVGLLEYAVTAGLSVVVVVYSIGHISGAHLNPSITIAFAVFGGFPWSQVPLYITAQTLGATAATLVGVSVYGVNADIMATKPALSCVSAFFVELIATSIVVFLASALHCGPHQNLGNLTGFVIGTVISLGVLITGPISGGSMNPARSLGPAVVAWDFEDLWIYMTAPVIGAIIGVLTYRSISLKTRPCPSPVSPSVSSLLR
The following text describes a protein:
Function:
Putative sodium-dependent amino acid/proton antiporter.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MGDWLQKEAAAGALAEADPGILASDGYASLSSMMNMVTSLPMGYQGQRLCSSPKRDFDDKEALVSEHKLKEKGNFRQSSAIFNVVNSITGSGIIDFSLILLIKGGVLSGTHSYQALVHKTFGFPGYLLLSLLQFLYPFIAMISYNIITGDTLSKVFQRIPGVDPGNFFIGRHFIIGLSTVAFSLPLSLFRDIAKLGKASLISAVLTAMILIFVIIRAFTLGPYITRTEDAWVFAKPNTVQAVGVMSFAFICHHNSFLIYGSLEEPTVVKWSRVIHISVVISIFISVLFATSGYLTFTGHTQGDLFENYCRNDSLINFGRFCYGITVILTYPIECFVTREVIANVFFGGNLSKISHVIVTTVIITMATLVSLMVDCLGIVLEFNGVLCAAPLIFIIPSACYLKLSEERWIHPDKIMSSVMLLNGVVVMVVGFVMTILYPQDCSHGQEMAYCSFTNASFFNISFSSLDPTIQSSVLNISTFQ
The following text describes a protein:
Function:
May regulate AMPA receptor content at nascent synapses, and have a role in postsynaptic development and maturation.
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein. Cell projection, dendrite. Cell projection, dendritic spine. Early endosome membrane; Single-pass type II membrane protein. Postsynaptic density membrane.
Sequence:
MDGLIEQSGALMHSKISEAGKRNGLINTRNLMAEKRDGLVPVFPTPSYPSHALGSSAAPSQPDGGRSDLVQQLLDPNALPQTVESHYRPNIILYSETVLRAWGDGGASDCCETTFIEDRSPAKDGLDYPDGKFLDLSADDIKIHTLSYDVEEEEDFQELESDYSSDTESEDNFLMMPPRDHLGLSVFSMLCCFWPLGIAAFYLSHETNKAVAKGDFHQASSSSRRALFLAVLSITIGTGIYVGVAVALIAYLSKNNHL
The following text describes a protein:
Function:
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER).
Subcellular Localization:
Cytoplasm.
Sequence:
MVLLSNDEFLSCLHELMLRSKEKGSVYLTMKRCNLLNLCIFPSAGANTNPNISLDAYKQLKSAKKSEDAKSILHSKDTQYQTLMRATFGNKKLSTLVDSSNLVQFTDKYQTVTRLHMDSLKKKDRKDKKEKRKNKNESTNAVVA
The following text describes a protein:
Function:
Essential for Golgi structural integrity.
Subcellular Localization:
Cell membrane; Single-pass membrane protein. Golgi apparatus.
Sequence:
MAGRHQNRSFPLPGVHSSGQVHAFGNCTDSDVLEEDAEVYELRSRGKEKIRRSTSRDRLDDIIVLTKDIQEGDTLNAIALQYCCTVADIKRVNNLISDQDFFALRSIKIPVKKFSSLTETLYPPKGRQASRPSSVQYVPEQQEILPPNDSLSSSESADNFLKEVDRDIEQIVKCTDTKKENLNEVVSALTAQQIRFEPDNKNIQRKDPYYGADWGIGWWTAVVIMLIVGIITPVFYLLYYEILAKVDVSHHSTMDSSHLHSGVTPPSQQREMENGIGPTKGIPFGQHDHKLYSQDSQSPAAQHKT
The following text describes a protein:
Function:
Plays a major role in chloroplast RNA editing. Acts as a site-recognition transacting factor to recruit C-deaminase. Involved in single RNA editing events. Required for the edition of the site 1 of ndhD (ndhD-1 site corresponding to cytidine-2), which is a plastid-encoded subunit of the NADH-plastoquinone oxidoreductase. The interaction with DYW1 is required for its function in editing the ndhD-1 site.
Miscellaneous:
MISCELLANEOUS: Unlike other RNA editing factors, CCR4 does not contain identifiable E(+) and DYW motifs but does contain PPR repeats. Therefore its association with DYW1, which lacks PPR repeats, but does contain E(+) and DYW motifs, is required for its function in RNA editing.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MLVFKSTMECSISSTIHVLGSCKTSDDVNQIHGRLIKTGIIKNSNLTTRIVLAFASSRRPYLADFARCVFHEYHVCSFSFGEVEDPFLWNAVIKSHSHGKDPRQALLLLCLMLENGVSVDKFSLSLVLKACSRLGFVKGGMQIHGFLKKTGLWSDLFLQNCLIGLYLKCGCLGLSRQMFDRMPKRDSVSYNSMIDGYVKCGLIVSARELFDLMPMEMKNLISWNSMISGYAQTSDGVDIASKLFADMPEKDLISWNSMIDGYVKHGRIEDAKGLFDVMPRRDVVTWATMIDGYAKLGFVHHAKTLFDQMPHRDVVAYNSMMAGYVQNKYHMEALEIFSDMEKESHLLPDDTTLVIVLPAIAQLGRLSKAIDMHLYIVEKQFYLGGKLGVALIDMYSKCGSIQHAMLVFEGIENKSIDHWNAMIGGLAIHGLGESAFDMLLQIERLSLKPDDITFVGVLNACSHSGLVKEGLLCFELMRRKHKIEPRLQHYGCMVDILSRSGSIELAKNLIEEMPVEPNDVIWRTFLTACSHHKEFETGELVAKHLILQAGYNPSSYVLLSNMYASFGMWKDVRRVRTMMKERKIEKIPGCSWIELDGRVHEFFVDSIEVSSTL
The following text describes a protein:
Function:
Involved in the determination of cell fates in the dorsal mesoderm.
Subcellular Localization:
Nucleus.
Sequence:
MLNMESAGVSAAMAGLSKSLTTPFSINDILTRSNPETRRMSSVDSEPEPEKLKPSSDRERSISKSPPLCCRDLGLYKLTQPKEIQPSARQPSNYLQYYAAAMDNNNHHHQATGTSNSSAADYMQRKLAYFGSTLAAPLDMRRCTSNDSDCDSPPPLSSSPSESPLSHDGSGLSRKKRSRAAFSHAQVFELERRFAQQRYLSGPERSEMAKSLRLTETQVKIWFQNRRYKTKRKQIQQHEAALLGASKRVPVQVLVREDGSTTYAHMAAPGAGHGLDPALINIYRHQLQLAYGGLPLPQMQMPFPYFYPQHKVPQPIPPPTQSSSFVTASSASSSPVPIPIPGAVRPQRTPCPSPNGQMMSVESGAESVHSAAEDVDENVEID
The following text describes a protein:
Function:
Binds to the consensus sequence 5'-A[AT]T[AG]TTTGTTT-3' and acts as a transcriptional repressor. Also acts as a transcriptional activator. Negatively regulates transcription of transcriptional repressor RHIT/ZNF205. Promotes development of neural crest cells from neural tube progenitors. Restricts neural progenitor cells to the neural crest lineage while suppressing interneuron differentiation. Required for maintenance of pluripotent cells in the pre-implantation and peri-implantation stages of embryogenesis.
Subcellular Localization:
Nucleus.
Sequence:
MTLSGGGSASDMSGQTVLTAEDVDIDVVGEGDDGLEEKDSDAGCDSPAGPPELRLDEADEVPPAAPHHGQPQPPHQQPLTLPKEAAGAGAGPGGDVGAPEADGCKGGVGGEEGGASGGGPGAGSGSAGGLAPSKPKNSLVKPPYSYIALITMAILQSPQKKLTLSGICEFISNRFPYYREKFPAWQNSIRHNLSLNDCFVKIPREPGNPGKGNYWTLDPQSEDMFDNGSFLRRRKRFKRHQQEHLREQTALMMQSFGAYSLAAAAGAAGPYGRPYGLHPAAAAGAYSHPAAAAAAAAAAALQYPYALPPVAPVLPPAVPLLPSGELGRKAAAFGSQLGPGLQLQLNSLGAAAAAAGTAGAAGTTASLIKSEPSARPSFSIENIIGGGPAAPGGSAVGAGVAGGTGGSGGGSTAQSFLRPPGTVQSAALMATHQPLSLSRTTATIAPILSVPLSGQFLQPAASAAAAAAAAAQAKWPAQ
The following text describes a protein:
Function:
With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD.
Sequence:
MYDKFSRKKLMAARPLWKGQITFGLVNVPVSLYPAVGKTEIHFHLLDSRNMARVRYERVNEETGEEVPWNEIVKAYEYNGGDYVIVEEKELKKAAPESTQSIEIESFIPRRELDCVYFDKPYYLVPVKNGEKGYVILREVLKKTKTVGIARIVIRSKQYLAAVFPYQKGIMVNLLRFAQEFRKTDELNLPTQDIKKYKITPKELSIAEQLVNAMLTQWKPEKYHDEFREKIMKWVEAKIKTGKTISIEKEEAAPVSTNVVDFMQLLKKSIQEKEKTKKHASGSR
The following text describes a protein:
Function:
Serine/threonine-protein kinase, which plays a role in regulating allophagy, an autophagic process in which paternal organelles, including mitochondria and membranous organelles, are degraded in embryos. Phosphorylates the allophagy receptor allo-1, which is required for allophagy.
Subcellular Localization:
Cytoplasm. Note=Localizes to cytoplasmic puncta in oocytes. After fertilization, localizes to paternal organelles during meiosis I and meiosis II. Co-localizes with allo-1 in embryos and oocytes.
Sequence:
MAVSPHKTYPIVITHGEKYTLFNDESIGKGAYSEVYRGRTESGRLVAVKTACKKLEVAAIGIEIEILKKLKGASNIVQYFGSNHTKMAPGSVTSETISFAMEYASSSLEAEMRRPKNHRGLSSNALIDLVVDCSMALSALREHNIAHRDIKHMNILLFPGTPTRGRRSTHLFKLCDMGCSKSLSENSSHEMRTLVGTPNLLHPFLAHEMVDPLMAQNRHNWKTKSAYTSEQCDLWALGCTLYFCATGKFPFEHERNNKSLYHKAVVALTQNPDAIAMVLVQKGRDPGRRTDIFEFQPVTELPAKFTRYPKWLVSTMTCLLRSFFHEPSIEYYAKVADAMRNSKRRTFSSVDQMSIVEHTDMSNVPHLGFSIPSISKCLGYPEGTDILLLSNTSTHYLDSKQKSVDGLPDDLYLVVPQTSHVDMRKILARNIEFHEFDDMTDRKLSEIRIKKCYEGLSMLTEIDEYLALFDRVSTILSTQFSLLVQELSQFERVQTASRFAVYVDMASVPLMLFDEANPETKMISDQCIQQAKRAREELERHAKVSMDIEACAKQLSKDAEDLRLEDMDLPGICEEIESYVFYDKQAILSTQKYSQELVELCLKRRNNIMEQIFNSPDRINKSKLNKAMNLAASLSQLRSNYRKLQDMISECVDLLEKPFQEMKDTVNRYLQAQGCSRNTMQKSMHLLRPEFHESQIRIKKTTKSCRKLIDQLNIELDQLGFVRLGDILIKAESEQTLTRSEEIQETQVVSFFCQAESSPNKEQFPKPEQDSILESSIDEGSTSFESTPPSSPPDVGSNNYFQAVFQYFAKPTSSPSSSAK
The following text describes a protein:
Function:
Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity.
Sequence:
MSSSTSRAQKEKMVTEFRSVTNAIPADASRICKKSGYRLEVAFDLFYNDHLAQQNAERSMQSRSKAIAEAFEGVLNVQFNEFQDPDEPGRMDMNGLMRYLEELSLTPEDPKVLCLCHLLHSPRLGVLERADFLKYWAALLVQATTSPSPPPPIQTADEMTKFQITTLAELDRRLRSELSYFEEVYRYTFDFGRDEGQKSLALSTAIPLWELILPLAPGLDPNVFKPEYLQWWIELLRSRNKSVSRDTWNLFLDFVVQLEDRFANYDELAAWPSLIDDYVTLAREKLGSQGMDVC
The following text describes a protein:
Function:
Catalyzes the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate (PtdIns-4-P).
Subcellular Localization:
Late endosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein.
Sequence:
MAGERTPILASSSSSYLGSSLPYEVLVDECDADELPPLQFINESGVGFAIKCKVCQKILDLDSRTDFYVIQCDACQEATPVKPAPFGKKYVRCKCKCLLICKAGSKRVACPRSNCKLIMLLSSSGDHQTRPLQNVVRVTCSYCSQQFLFSFVDKRLARCPHCKKISSVGDRHNRKNIIGFLIASLLFLAAGCFLLGFTLNLLPQNKGLIAAYVVLFLVGALLLLRVYFYWRIKVSQIDSTTTSNNIRSPSIGEVIA
The following text describes a protein:
Function:
Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stranded 3'-5' exonuclease activity and single-stranded endonuclease activity.
Sequence:
MRLVHLSDSHLGKAQFNLAEREEDFYSSFSRAIDIAISEKPDLLIYTGDLFDSYRPHPRAFVRAFESLMKLAERGIPIAIIEGNHELGPDVVRKQITSPIANMETLFNRLGYGKLFMRLNAKVERIGDLVVAGLPYKSLGKDVPAMISNLEGKCKSLCNCPSVLMIHQGVKGMIKTFYPELDFSHIASTSFNYVAMGHYHNKVVRRSGNRVFAYPGSTEIVELREAFTSDGSKYILSVDIERDGVDVREIKLETRPFITFSEIIRNTRDLYSLIERIRNEIKGKERPVICGRIQVKGSLKPGFSTGEIKRSLSSDALHIAVKERFEEREEVSDEAPLLGLEDTISQLIGSLKIDEDIKSLAIRIFDIWYREGKRGEDFLNEVMRMVEEP
The following text describes a protein:
Function:
Catalyzes the ferrous insertion into protoporphyrin IX.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MLRPPTNMAAFRAAHRLLGHILRNESSAGLVTQRWSSSAAVASVPKSSDPKPHAQPDKRKPKTGILMLNMGGPETLDDVHGFLLRLFLDKDLMTLPAQSKLAPFIAKRRTPKIQEQYSKIGGGSPIKKWTEQQGEGMVKLLDELSPATAPHKYYIGFRYVRPLTEAAIEEMERDGVERAIAFTQYPQYSCSTTGSSLNAIYRYYNAKGTQPKMKWSVIDRWPTHPLLIQCFADHIQKELNMFPADKRGEVVILFSAHSLPMSVVNRGDPYPQEVGATVQKVMERLGFSNPYRLVWQSKVGPMAWLGPQTDESIKGLCQRGKKNILLVPIAFTSDHIETLYELDIEYAQVLAKECGVENIRRSESLNGNPLFSKALADLVLSHMKSSEICSKQLSLRCPMCVNPVCGEAKSFFTKQQQQ
The following text describes a protein:
Function:
May form an ATP-driven capsule polysaccharide export apparatus, in association with the CtrB and CtrD proteins.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MKALHKTSFWESLAIQRRVIGALLMREIITRYGRNNIGFLWLFVEPLLMTFVIVLMWKFLRADRYSTLNIVAFAITGYPMLMMWRNASKRAVGSISSNASLLYHRNVRVLDTILARMILEIAGATIAQIVIMAVLIAIGWIEMPADMFYMLMAWLLMAFFAIGLGLVICSIAFNFEPFGKIWGTLTFVMMPLSGAFFFVHNLPPKVQEYALMIPMVHGTEMFRAGYFGSDVITYENPWYIVLCNLVLLLFGLAMVSKFSKGVEPQ
The following text describes a protein:
Function:
Required for normal embryogenesis and seed viability. Involved in the first asymmetrical cell division of the zygote. Regulates the number and planes of cell divisions required for generating the normal embryo proper and suspensor, apical-basal axis, cotyledons and meristem.
Miscellaneous:
MISCELLANEOUS: Named LONO after a Hawaiian god associated with fertility, agriculture, rainfall and music.
Subcellular Localization:
Nucleus envelope. Nucleus, nuclear pore complex.
Domain:
Contains FG repeats mediating the translocation through the NPC by interacting with transport factors.
Sequence:
MSRVEIEEDTEGDRISTNDYYFERIGEPISIKEDDAQYDLENPPSQPLAISERHAVLFVAHSSGFFVGRTNDVISASKNSNGNGDKVFIQDLSLVDVPVGDVRILSLSADDSILAVTVAADIHFFSVDSLLKKDAKPSFSYSPDESGFVKDFRWRRNDKHSYLVLSNTGKLFHGIDNAPPRHVMDAVDAVEWSSKGSYIAVAQDNSLRIFSSKFNEKRCIALSFDSWIGDSDEDCFVKVDSIRWVRNNCILLGCFQLIEGREENYLVQVIRSPDGKISDGSTNLVALSFSDLFPCSMDDLVPVGVGPHLLFSYIDQCKLAVTANRKSIDEHIVLLDWSSGDDKSAVSVVDIDRETFLPRIGLQENNDDNTVMGLCIDRVSIEGTVNVRSGDDELKELQPYFVLVCLTLEGKLVMFNVASVAGRPASSDTDLASSSDIEDAYTPLIEDDLSKQSSEKHQQLNIAVQNDQKHLNTEKFSTEQRLPNENIFSKEFESVKSSVSGDNNKKQEPYAEKPLQVEDAQQSMIPRLSGTSFGQLPMSLGYDTNKFAGFGPALPVSEKLQKDIFAQSNSMHLQANVESKSTAAFFGSPGLQNAILQSPQNTSSQPWSSGKSVSPPDFVSGPFPSMRDTQHKQSVQSGTGYVNPPMSIKDKSVQVIETGRVSALSNLSPLLGQNQDTNEGVEKIEPIPSIRASQLSQQVKSSFEKSASHQQHKTPLSTGPLRLEHNMSNQPSNINEMAREMDTLLQSIEGPGGFKDSCAFILKSNVEELEQGLESLAGKCQTWKSTIHEQQAEIQHLLDKTIQVLAKKTYMEGMYKQTADNQYWQLWNRQKLNPELEAKRQHIMKLNKDLTHQLIELERYFNRLELDRYNEDGGHPVARRGVPNRSAPSRRVQSLHSLHNTMSSQLAAAEQLSECLSKQMTYLKIDSPVKKNVKQELFETIGIPYDASFSSPDAVKAKNASSAKNLLLSSIPASINQQSRQRQSSAMKNSDPETARRRRESLDRVIFNWAAFEPPKTTVKRMLLQEQQKTGMNQQTVLSERLRSANNTQDRSLLHVKDHASPVVSSNKGIMESFQQDTSEAQSTPFKTRPPMPQSNSPFTISPISASKPSFNWSGNKSSNTTSYAEESAPSQIKDTRTVSQPGGSSFLPKRPVASTVLEQTEKKAGEFKFSEAKANAFVETAAGSVQRLSTTSSGSDFESSKGFGAQFSTMSSGAPASSFSSKSLFGFNSSSSIPGDKFTFPAVTAPLSGTPLDSTSTLFTASSAPVSSSSQDPVPASIPISSAPVPQTFSVTSTSTVSATGFNVPFGKPLTSVKVDLNQAAPSTPSPSPGPTAGFTFNLPALSPSSPEMVSSSTGQSSLFPPSAPTSQVSSDQASATSSLTDSSRLFSSTSLSSTPPITPPDAFQSPQVSTPSSAVPITEPVSEPKKPEAQSSSILSTQSTVDSVANATKTQNEPLPVKSEISNPGTTVTPVSSSGFLSGFSSGTQSSLASMAAPSFSWPGSSQPQQLSSTPAPFPASSPTSASPFGEKKDIVDTQEDEMDEEAPEASQTTELSMGSFGGFGLGSTPNPGAPKTNPFGGPFGNATTTTSNPFNMTVPSGELFKPASFNFQNPQPSQPAGFGSFSVTPSQTPAQSGFGQPSQIGGGQQALGSVLGSFGQSRQIGAGLPGATFGSPTGFGGSNPGSGLPNAPASGGFAAAGSSATGGFAAMASAGRGFAGASSTPTGGFAALASGSGGFAGAAPGGGGGGFGGLGSGTGGFGGFAPQGSSGGFAGAAGGGGFGGFGGQAQGQAGGGGFSAFGGNSGATGKPSELFTQMRK
The following text describes a protein:
Function:
Activates the transcription of the soxS gene which itself controls the superoxide response regulon. SoxR contains a 2Fe-2S iron-sulfur cluster that may act as a redox sensor system that recognizes superoxide. The variable redox state of the Fe-S cluster is employed in vivo to modulate the transcriptional activity of SoxR in response to specific types of oxidative stress. Upon reduction of 2Fe-2S cluster, SoxR reversibly loses its transcriptional activity, but retains its DNA binding affinity.
Sequence:
MEKKLPRIKALLTPGEVAKRSGVAVSALHFYESKGLITSIRNSGNQRRYKRDVLRYVAIIKIAQRIGIPLATIGEAFGVLPEGHTLSAKEWKQLSSQWREELDRRIHTLVALRDELDGCIGCGCLSRSDCPLRNPGDRLGEEGTGARLLEDEQN
The following text describes a protein:
Function:
Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
Sequence:
MPLDVHEAFSRKNFFLTGGTGFMGKVLIYKIMKEFPDVGYIYVLARGKNSRRLKRYLNPQERVKLEVLSSPCFDPLRKSMGEAAFNALGSRVVAIEGNIVDNRIGLSDKDRQTLINHTHFIVHMAATVNFDERLNIAVETNTLGSLRVLTLAKECKNLEAMVHVSTCYVNYSVQGRPVEECLYSPPFDPQGMCKHILALNDKEIDTVGRDLLKKYGFPNTYTFTKFIGEQLLNENKGNCPLVIVRPSIVGCSLKEPFPGWVDALTAAGGLILTCGLGLVRELVCRQGAIADIVPVDFVVNVILKALFQAKTHFKGNTPKVVNVDEHARERSTAASTAQGLLNPLTAAKQLNGTGKGALKGVYEGNPASIFQQQQQQQNHASNNGGGHINNDNDQGQQQQQQRDTGGPVVAMAGSDVYGTSVPFIYQASTSHSHNHITWRRMSDASIEYWSAKKRHPKALGPVSVQFMESRLLYAMKFFLCREVPSHALAFLADLPEPIGSKSKRENVKKLKRALFRAKDLNRQFVAFTCTEWVFAATNTMSLDEGLSERSRSAFYYDPYLINWWSYCHWYSYGLLKHIVRDTGSFEEPEQPETAAELFRRASSL
The following text describes a protein:
Function:
Acts as a component of the translation initiation factor 2B (eIF2B) complex, which catalyzes the exchange of GDP for GTP on the eukaryotic initiation factor 2 (eIF2) complex gamma subunit. Its guanine nucleotide exchange factor activity is repressed when bound to eIF2 complex phosphorylated on the alpha subunit, thereby limiting the amount of methionyl-initiator methionine tRNA available to the ribosome and consequently global translation is repressed (By similarity). It activates the synthesis of GCN4 in yeast under amino acid starvation conditions by suppressing the inhibitory effects of multiple AUG codons present in the leader of GCN4 mRNA. It may promote either repression or activation of GCN4 expression depending on amino acid availability. GCD2 is also required for cell viability. Its function can partially be replaced by GCN3 under normal growth conditions in GCD2-defective mutants, under AA starvation conditions GCN3 is an antagonist (GCN4 translational activator).
Miscellaneous:
MISCELLANEOUS: Present with 10300 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MSESEAKSRSATPPSKAKQATPTTTAAANGEKKLTNKELKELKKQEKAAKRAAMKQANGISIEQQQQQAQMKKEKKQLQREQQQKREQKQKNANKKKQNERNVKKSTLFGHLETTEERRATILALTSAVSSPKTSRITAAGLMVPVVASALSGSNVLTASSLMPVGPNASSTVSASAPASTTTTLPASSAALSAGTSSASTNTPTAIQQEIASSNASDVAKTLASISLEAGEFNVIPGISSVIPTVLEQSFDNSSLISSVKELLLNKDLIHPSILLLTSHLAHYKIVGSIPRCIAMLEVFQIVIKDYQTPKGTTLSRNLTSYLSHQIDLLKKARPLSVTMGNAIRWLKQEISLIDPSTPDKAAKKDLCEKIGQFAKEKIELADQLIIDNASTQIEESTTIVTYGSSKVLTELLLHNAISLKKNIKVIVVDSRPLFEGRKMAETLRNAGVNVMYALITSLDTIFNMDVDYVFLGAHSILSNGFLYSRAGTAMLAMSAKRRNIPVLVCCESLKFSQRVQLDSVTFNELADPNDLVNIDYENPVERRGNKGALLNQFIKERKFEKKKLAMENKPKGNKIGGKKGSEGESKDASNEEDSNSKNILDGWQELPSLNIVNILYDLTPPEYIKKVITEFGALPPSSVPVILREYKGSA
The following text describes a protein:
Function:
Polyketide transferase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2). Within the pathway, the polyketide transferase af380 catalyzes the transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy-seco-sesquiterpene to produce prefumagillin. The pathway begins with the conversion of farnesyl pyrophosphate (FPP) to beta-trans-bergamotene by the membrane-bound beta-trans-bergamotene synthase af520. The multifunctional cytochrome P450 monooxygenase af510 then converts beta-trans-bergamotene into 5-keto-demethoxyfumagillol via several oxydation steps. 5-keto-demethoxyfumagillol is then subjected to successive C-6 hydroxylation and O-methylation by the dioxygenase af480 and O-methyltransferase af390-400, respectively, to yield 5-keto-fumagillol, which is then stereoselectively reduced by the keto-reductase af490 to 5R-hydroxy-seco-sesquiterpene. The next step is the polyketide transferase af380-catalyzed transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy-seco-sesquiterpene which leads to the production of prefumagillin. Finally, oxidative cleavage by the monooxygenase af470 converts prefumagillin to fumagillin (Probable).
Sequence:
MNREDVEFPTCDGLILRGWLYPGTIRGPAIVMNQGFNTPKEILLPDVAVWFQQQGVTVLLYDNRCIGASDGEPRNDVKPAKLVEDFHDALTFMARHPMVDEDKIILYGYSFSAMTALVAAGLDHRVGAAISVTPIANYDFREKEKNNVMALAMQDRVSTLAGNDPVYIPFVGDDGYNPAGWGNQYNMEQFRAFLGTSFFTNRTTVQSYYHVLAWQPYGAMRLIKGTPVMMVTPAEDTISSPADQRAVFDMIPEPNKEFDLVAGRGHMDVINGEGAEEVLQRQLAFMRKHLDF
The following text describes a protein:
Function:
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Subcellular Localization:
Cytoplasm.
Sequence:
MAQKKQFYLVVRGRNPGLYQQWSGEDGASAQVTGFPGALYKGFSTIAAAHEWVRSLPATEQTLALQLLADYEHAPHAEAEPDQNTQQPLSRPATSPSEDASSSSTNGIVMMYTDGSALGNPGPGGYGVVLRYNDHYQELTGGFRLTTNNRMELMACIVGLRALKRPVSVRLHSDSRYVVDAFRKGWIHRWQAQNWMRSETEPVKNADLWAELRLLCEGHQVEFVWVPGHQGVPDNERCHELAIAAAARPDLPPDVAFEMQWSRT
The following text describes a protein:
Function:
At the onset of mitosis, forms a medial ring structure before the arrangement of the medial actin ring. Essential for the central positioning of the division septum before the cell divides.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MSKSAFTSKSQLKGIDGSFNDPFRQPSMNLPTPPHDDGLPSIPRSTALPNLSNRLSPYSHRNYLPIPEADSRNLEVLNSISLTTGSVVNQINKLYQRSCDNANYLQDLRSLILQTPTAEANATQVTESLNQIQKILQEASSKDREQIVQVIKELNKGNSLEVRRELGNCLAHLKKGTLNIDNALQASLQKYWKELQYFNVSKDKLLSLEESIKLLSARLEETDTPSSTHWIEINAGFKEVGDELSENFQRKQEILSGLQNNVILRTNNRKPVGSDGSNSNFNGGEEQMDSKDQEEIQDYLNSLLSVHEKDGVLLQKFHNSYVQYQKLAVALSKYENFDADKLFQQMNLAKQSNETLLQTLTEQTDQLLSFKETMDSFKFILGPSMENQALQQGILAEQQDLVAQLRDIVLRSETLAENPSNMPGSCLPGASSNTADEFTEQLNLLKNEVARLSAICPSPNSGINASVLTNADNLEKENLLLVNNNAFKVDDRSVSSVALDDHNRQLQMNVEELEGKKADLTSKINRLDKDFVKLNTTYSLLTDQVKTKQLALQEIESRVIRLEERLNMLQKLSMQPAISSSSEFVPIESHPSSSAVVPIEEPKNSIIEKKRVPHNAARNSVNLEVTLPNSKKRFSSFSGSSSKLPVRPSTALTDKRKPSWSRRLAAAIGFSSGSPEKKHVITSSDAGHQRSKSRSFSSKM
The following text describes a protein:
Function:
Component of the phosphoenolpyruvate-dependent nitrogen-metabolic phosphotransferase system (nitrogen-metabolic PTS), that seems to be involved in regulating nitrogen metabolism. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein NPr by enzyme I-Ntr. Phospho-NPr then transfers it to EIIA-Ntr. Could function in the transcriptional regulation of sigma-54 dependent operons in conjunction with the NPr (PtsO) and EIIA-Ntr (PtsN) proteins.
Subcellular Localization:
Cytoplasm.
Sequence:
MTVKQTVEIKNKLGMHARPAMKLFELVQSFDAEVMLRNDSGTEAEASSVIALLMLDSAKGRQIEVEATGVDEIQALAAVIELFNSGFDED
The following text describes a protein:
Function:
Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine and small amounts of phosphatidylethanolamine from the lumen to the cytosolic leaflet of the trans-Golgi network and ensures the maintenance of asymmetric distribution of phospholipids. May be involved in transport from early endosomes to the trans-Golgi network (TGN) (Probable).
Miscellaneous:
MISCELLANEOUS: Present with 4510 molecules/cell in log phase SD medium.
Subcellular Localization:
Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein.
Sequence:
MGLILRWKEKKQLSSKQNAQKSRKPANTSFRQQRLKAWQPILSPQSVLPLLILMACVFAPIGIGLVVSTISVQRLVVNYTECDALAPAKHFETIPSEYVDYHFSKKVAVQPQWMVLTDPELGNQTCRIQFEVPNHIKKSTYVYYRLTNFNQNYREYVQSLDLDQLKGKALIGNDLDPNCDPLRTVENKTIFPCGLIANSMFNDTFGTTLTGVNDTADYLLTTKGIAWDTDSHRYGKTEYNASDIVPPPNWAKLFPNGYTDDNIPDLQNWEQFKIWMRTAALPNFYKLAMKNETNGLGKGIYIADIELNYPVRSFYGTKSFVLTTNSIIGAGNEALGIVYLIVAGIATLFAILFLIKVIFKPRPMHDHSYLNFENSDTPFDESSVVSIPLREIL
The following text describes a protein:
Function:
Involved in protein precursor import into chloroplasts. Part of the motor complex consisting of a co-chaperone (TIC40) and a chaperone (HSP93) associated with the import channel (TIC110). Causes the release of bound transit peptides from TIC110 and stimulates ATP hydrolysis by HSP93. Involved in reinsertion of proteins from the chloroplast stroma into the inner membrane.
Subcellular Localization:
Plastid, chloroplast inner membrane; Single-pass membrane protein.
Sequence:
MMVNMMDNLALNVSSQNKLVSGFTANPRTDATTISNKPLFCPFKIPKRSGAIYKSKSSISTPRAINKLNDAKDCFARISSSSGQHSSSQAGSIMFWVGVGVALSPVFSSAASYLKKYAMTMIEKTDTQNNKSATATATATSPRAKQCKLTIVVPAGFEIEVTQANKSETSQGSSATSAVTVDVPPTKTKPIESNDDNESIKEPKKSGAKSNGVTVEALEKAIDDPTVLKMVYPNDMGGNPEWNNRVMDSFKDIDLDLNSPEVKEQFDQIGLNPEEVVSKIMANPEVAMAFQNPRVQAAIMDCSQNPMGIIKYQNDKEVMDLFDKISELFPGVTRAE
The following text describes a protein:
Function:
Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.
Subcellular Localization:
Nucleus.
Sequence:
MQGDILERRVLITYDQKENAGTTTGGEALHLRHPKTAVPSLYLLIREKLQEVHWFKQQLASWFIGESVSEDGSLYLSSPVDPLFIALPLLEQARMKKGDSPGMFRGLEEMLEVEGFPGYQKLFDVFEKTLDMVCEVREAGDTKYYRLDDFKALAWLCCKVEQASAALKMKGGKAFHGLSDDELRTYSIGLLSEYLPAATWMKRLSDHYGVDLDAAKKARVLLPVQPLPCAPPPPPPAKTVPVAKGRASSLAKKGPQPGDRKITSFFARPR