lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in pre-mRNA splicing. Binds RNA (By similarity).
Subcellular Localization:
Nucleus.
Domain:
The C-terminal RRM domain and the zinc finger motif are necessary for RNA-binding.
Sequence:
MTSKKQKSSIDTITPTPPNTTTTTTTTSTTATTKDKKKSKKPKSSGLTKVGADIIELQASLLNRPARKQATHVNSRYEDHDTDTTEYNIWYHKKLGNRNWKDRDVSETRCNVLKDCGKTRANKDANFCCYFARGKCINGADCTSLHRIPTPEDDKRLRLTHDIFGRERHKTDRDDMNGVGSFSRDNRTLYIGGIKTNVSGSLEDMVRKNFEEWGRIEYVRVITNRSISFVRYLTRSSAEFAKEAMTDQTLDNGELLNIRWATEDSNPYAKKVDERNLHRVATEVINKRIREMTPDDQSALKYQMTGQYPNTDQQYDQNGQPINASPSTPYQLQYRGSTKYEAHPYARQYNNDLQKRVQSGETVDVAPLNGVGNYYSHSVGTMNQELQKQQYDNYMQQYYQAYGYDYSKLSDDQKLQLQQYFQSYYYGNQQEQQQQETQQIQNNNENNNDNEEEDDDDEDDDDDNEDDDNDNEETKDNKNDKVENKEEENKEVQEKINTESKEDTKNEEQEKKEEKEKTDSDNIVNKED
The following text describes a protein:
Function:
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSLEAIRYRRGSLEILNQLLLPQQSLYEAVGSVRQGWEAIRSMKVRGAPAIAIIGCLSLAVELHNKTTTEESVDNLETFVLDSLSYLVSARPTAVNMAQAAQELGRIVRQEAKREGSTVESLREKVICWAEAMLDQDLKDNRSIGDHGALHLLQQVGQDKVIVLTHCNTGSLATAGYGTALGVIRSLHTMGCLEHVYCTETRPYNQGARLTAYELVYEEIPATLIADSMVSMAMKEKKISAVIVGADRVVANGDTANKVGTYQLAIAAKHHGIPFYVAAPSTSCDLSLEHGGQIIIEERPSQELTDINGVRVAAPGIGVWNPAFDVTPHDLITGGIVTELGVFAPTELLAALTRRANKV
The following text describes a protein:
Function:
Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. L-threo-phenylserine and L-erythro-phenylserine are also good substrates.
Sequence:
MIDLRSDTVTRPSRAMLEAMMAAPVGDDVYGDDPTVNALQDYAAELSGKEAAIFLPTGTQANLVALLSHCERGEEYIVGQAAHNYLFEAGGAAVLGSIQPQPIDAAADGTLPLDKVAMKIKPDDIHFARTKLLSLENTHNGKVLPREYLKEAWEFTRERNLALHVDGARIFNAVVAYGCELKEITQYCDSFTICLSKGLGTPVGSLLVGNRDYIKRAIRWRKMTGGGMRQSGILAAAGIYALKNNVARLQEDHDNAAWMAEQLREAGADVMRQDTNMLFVRVGEENAAALGEYMKARNVLINASPIVRLVTHLDVSREQLAEVAAHWRAFLAR
The following text describes a protein:
Function:
The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular Localization:
Mitochondrion.
Sequence:
MNKRDVRMNVLFCVAALAQTPSGTAVVRLLKGRFGFDLGASLMPVRKYVTRAAAEPFLNGSSSVYVEEMYKAWTKDPSSVHKSWDVFFRGASSGLQPGEAYRSPPSLYMAPGAAPAAARVTSAALTAPAAVPAALPSAQAAPRDIDDHLSVQAIIRSYQVVELLSSHLLFVCLQPLHSVRGHLAAKLDPLGIVTASSNSPLSREELHTPEVVLRNYKLEEKDMDRLFKLPSTTFIGGEEAVLPLREILRRLENVYCGSIGVEYMFINDLDQCNWIREKFESPGVMRLSKERKRLLLSRVVRSTKFEEFLAKKWVSEKRFGLEGCEVLIPAMKTIIDRSSELGIESIVMGMPHRGRLNVLANVCRKPLEQIFTQFSGLEPADEVCYRRNGHNEVDEPMFTQPLMYTKIRKQATALDIYARKLLDEGVVTEKEIEDEKERYDGILAEAYKNAEKEGKSYNRDWLDSPWSGFFGDRDPIKCDPTGVSEEILRHVGVAFSSPPPGNFKIHPGLKRILKSRMEMVEQKQVDWALGEAMAFGSLLKEGVHVRLSGQDVERGTFSHRHHVLHHQTIDKTTYRPLCHLWPDQAPYTVCNSSLSEYGVLGFELGFSMTNPNALVMWEAQFGDFMNTAQCIIDQFISSGQAKWVRQSGLVMMLPHGMEGMGPEHSSARAERFLQLCSEESDVFPTIDEDFAMRQLNDINMIVVNCTTPANYFHVLRRQIALPFRKPLIALTPKSLLRHPEAKSHFNEMTEGTSFLRLIPDEGAVKGNPNAVKRHILCTGKVYYDLTKERKARNLEGDVAISRVEQLCPFPFDLVKQEVDRYPNADICWVQEEHKNQGYWSFIQPRLQTVTANQMPIQYIGRNVSPSTATGSKHVHKKEFEKLLNDSFSV
The following text describes a protein:
Function:
SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity.
Sequence:
MRLLHTSDWHLGRAFHRVNMLGAQAGFVGHLVETVREHSVDAVVVSGDVYDRAVPPLAAVELFDDALHRLAGLGVPTVMISGNHDSARRLGVGAGLIDRAGIHLRTDPAGCGTPVVLGDAHGDVAFYGLPYLEPALVKTEFGVEKAGHEAVLAAAMDRVRADLATRAAGTRSVVLAHAFVTGGEQSDSERDITVGGVAAVPAGVFDGVDYVALGHLHGCQTLTERVRYSGSPLPYSFSEHRHRKSMWLVDLGADGSVTAERIDCPVPRALARLRGTLADLLADPELTPHEDAWVEATLTDPVRPDEPMARLTERFPHTLSLVFDPERAPDEPGVSYARRLADRSDQQIAEDFVTHVRGAGPDDDEQAVLRDAFDAVRADETVREVAR
The following text describes a protein:
Function:
Acts as a dual histone chaperone and heat shock co-chaperone. As a histone chaperone, forms a co-chaperone complex with MCM2 and histone H3-H4 heterodimers; and may thereby assist MCM2 in histone H3-H4 heterodimer recognition and facilitate the assembly of histones into nucleosomes. May also act as a histone co-chaperone together with TONSL. May recruit histone chaperones ASF1A, NASP and SPT2 to histone H3-H4 heterodimers. Also plays a role as co-chaperone of the HSP70 family of molecular chaperone proteins, such as HSPA1A, HSPA1B and HSPA8. As a co-chaperone, may play a role in the recruitment of HSP70-type molecular chaperone machinery to histone H3-H4 substrates, thereby maintaining the histone structural integrity. Exhibits activity to assemble histones onto DNA in vitro.
Sequence:
MPGLRESCEIHFGTSDLYKVLGVRKEAGEGEIRRGYHRVSLKVHPDRVQQEEKENATAEFQILGKVYAVLSDKEQRALYDEQGIVDEETDTLSQDKNWEEYWRLLFKKITVEDIKAYEEKYKGSEEEKNDIISAYMDFEGNMDGIMESVPCADFEDEPRIRHIIQKAIKSKEIPSYNAFVKESKKKREQRNKRAHEEAKEAEEIKKEMGLGDDSDDLKALIQRRQNDRKKEMDSFFDQLEAKYCNTSKKATSKSKAPKKGKK
The following text describes a protein:
Function:
Plays a role in pre-mRNA splicing. Binds to the polypyrimidine tract of introns. May promote the binding of U2 snRNP to pre-mRNA.
Subcellular Localization:
Nucleus.
Sequence:
MASGQPQFRYTQPPSKVIHLRNLPWDCTEEELVELGSPFGKVVNTKCNVGANRNQAFVEFADQNQAIAMISYFASSAEPAQVRGKNVYLQYSNRQEIVNSKSSGEAAGNVLLVSMEGVLPDAVSIDVLHLVFSAFGFVQKIATFEKASGYQALIQFCDTETASSAKAALDGRCIPSYLLPELDVPCTLRINYSAHTVLNVKFQSHRSRDYTNPYLPVAPSAIDGSGPDGKKQEAESNVLLASVENMQYVVTIDVLHEVFSAFGFVQKIAIFEKNSGFQALIQYPDIQTAVAAKEALEGHSIYEGGYCKLHLTFSRHTDLNVKVNNERGRDYTGGNTAPTSNQPSILGPQPVYSGAYNNAPSSATGAVVPPGTTLTPPGAPSHPYTSSEPLPQTPAVPSGGAPLYTSQGILQGPPGVPPAQFPGYGSPQFPPGSAQAQMHQQHPVQGSQQMPGQMNHQPPPGSFMQYPGDGGRPVQDAPGQQAMPFHGHGGGQHLPPGYGGQPQFQQGPRPPMPPQQFPMYGDQQFPPGTGPQMMMPFAGQGGGQQHPFRPYNSH
The following text describes a protein:
Function:
Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity).
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein.
Sequence:
MFNGFRFNGNRIGDRRWFCGGGGEPVTGTNVRAMDRSQEKEAIKSPIPPAIRVRELSFAYGGQTPVLNNLAWQVAPGERLGIIGHNGCGKTTLFLLLCGLLKASAGTIQLLGQALEAGKFLPEVGFLFQNPTDQLFATSVWDDIAFGPQNMGLSPAQVTERVNQAAELTGITSLLDRLPQHLSGGEKQMVAIAGLLAMAPKILLCDEPTASLDIKARRQLINFLGQFQQTLLISSHDLEFVLEVCNRVIIIDQGQIVADGPAQEIMADQTLMESHGLEKPYSLR
The following text describes a protein:
Function:
Has guanylyl cyclase on binding to the beta-1 subunit.
Subcellular Localization:
Cytoplasm.
Sequence:
MSRRKISSESFSSLGSDYLETSPEEESECPLSKLCWNGSRSPPGPQEPNAAGTATAATATATATATATAGARRAQRRRRVNLDSLGESISRLTAPTPQIIQQTLKRTLQYYEHQVIGKAIKIEAWNSKMQAKQMAIVTFLSVMLTSALHLLLGLKFEEMQERFGEEFFNICFDENERVLRAVGGTLQDFFNGFDALLEHIRTSFGRQATLESPSFLCKELPEGTLMLHYFHPHHTVGFAMPGMIKAAGKKIYRLDLEVEQGCENTNITKNLPPGTSQTPADLRISINTFCRAFPFHLMFDASMLVLQLGEGLRKQLRCDAHKTLKFEDCFDIVSPKINATFERVLLRLSTPFLIRTKPEASGSENKDKVMEVKGQMIHVPESNSILFLGSPCVDKLDELMGRGLHLSDIPIHDATRDVILVGEQAKAQDGLKKRMDKLKATLERTHQALEEEKKKTVDLLFSIFPGDVARQLWQGQQVQARKFDDVTMLFSDIVGFTAICAQCTPMQVISMLNELYTRFDHQCGFLDIYKVETIGDAYCVAAGLHRKSLCHAKPIALMALKMMELSEEVLTPDGRPIQMRIGIHSGSVLAGVVGVRMPRYCLFGNNVTLASKFESGSHPRRINVSPTTYQLLKREDSFTFIPRSREELPDNFPKEIPGICYFLELTTGPKQPKPSISSTRMKKVSYNIGTMFLRETSL
The following text describes a protein:
Function:
Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs. Binds the APUM-binding elements (APBEs) in the 3'-UTR mRNA sequence of CLV1, PNH, WUS and FAS2.
Subcellular Localization:
Cytoplasm.
Sequence:
MTTQSAMRMVEGDHVKSWQASSRDTSGIFGSHDMAVEDLRFLMERNRLDSSGSDHTGKIPSRSGSAPPSMEGSFAALRNLLKHQEGSFSRSIENYGSEEEIRSDPGYVAYYLSNINLNPRLPPPLISRENQHLLRHLGGDGNNLSPTASWDDMGIRSSLLASRTALSTHREEPEDEASSGEQLTYASLPGRRKSFADIIQRPHSAGNHPIAEDIHAISSGIASERTRRLPESDVSSVNLLRETDSLSMEAIASEDPFTSELSSQSSTNTQNERSNARVGSREDNNLSAFGASGPSSAASRMRGNQEEPRRMPVQYTPSSYQVQATSPQQMTYPRMGGGTHDMMQNLPRIATGEVHSTFQSPHGLTSPPMYTSTAAYMTSLSPFYNHHNFQSSGMYLPQYNYGGYPPVSGVVPQYMSGYPSHEATVPMPYDISSPSSGYNNSFSRGSFSPTAQNTPLVDPFQLQYYQQAQAEAYAPSFDSFGKQDQQAAGFMAANQEPHSNPLSPSFGLQSPRHMGNYFAVPPGVRVMQQYPGSPLASPVMPSSPVGGGMMSQFGRRSETRYHHQQGPSRNTGIYPGGGWQGNRGGASSSVVDDFKRHSFLDELKSPNARKMELSDITGRVIEFSVDQHGSRFIQQKLEHCSDEEKAYVFSEVLPQASKLMTDVFGNYVIQKFIEHGTPAQREELVKQLAGQMVSLSLQMYGCRVIQKALEVIDVDQKTELTRELDGNVLKCVRDQNGNHVIQKCIESMPASRIGFIISAFRGQVATLSTHPYGCRVIQRILEHCSDDEETRCIIDEILESAFALAHDQYGNYVTQHVLERGRPDERRQIIEKLTGNVVQMSQHKYASNVVEKCLEHADSTERELLIEEIMGKSEEDNHLLAMMKDQYANYVVQKVLEISKDEQREILVQRMKIHLESLRKYTYGKHIVARFEQLFGEESEASEGGAEG
The following text describes a protein:
Function:
Major attachment protein that mediates binding of the virus to cell surface heparan sulfate or chondroitin sulfate. Also plays several roles in host immune evasion by inhibiting the host complement cascade activation, and by providing a shield against neutralizing antibodies that interfere with gB-gD, gB-gH/gL or gD-gH/gL interactions (By similarity).
Miscellaneous:
MISCELLANEOUS: There are seven external glycoproteins in HSV-1 and 2: gH, gB, gC, gG, gD, gI, and gE; MISCELLANEOUS: [Isoform gC]: Membrane-bound gC; MISCELLANEOUS: [Isoform gCsec]: Secreted.
Subcellular Localization:
Virion membrane; Single-pass membrane protein.
Sequence:
MAPGRVGLAVVLWSLLWLGAGVSGGSETASTGPTITAGAVTNASEAPTSGSPGSAASPEVTPTSTPNPNNVTQNKTTPTEPASPPTTPKPTSTPKSPPTSTPDPKPKNNTTPAKSGRPTKPPGPVWCDRRDPLARYGSRVQIRCRFRNSTRMEFRLQIWRYSMGPSPPIAPAPDLEEVLTNITAPPGGLLVYDSAPNLTDPHVLWAEGAGPGADPPLYSVTGPLPTQRLIIGEVTPATQGMYYLAWGRMDSPHEYGTWVRVRMFRPPSLTLQPHAVMEGQPFKATCTAAAYYPRNPVEFVWFEDDHQVFNPGQIDTQTHEHPDGFTTVSTVTSEAVGGQVPPRTFTCQMTWHRDSVTFSRRNATGLALVLPRPTITMEFGVRIVVCTAGCVPEGVTFAWFLGDDPSPAAKSAVTAQESCDHPGLATVRSTLPISYDYSEYICRLTGYPAGIPVLEHHGSHQPPPRDPTERQVIEAIEWVGIGIGVLAAGVLVVTAIVYVVRTSQSRQRHRR
The following text describes a protein:
Function:
Involved in peroxisome biosynthesis and integrity. Assembles membrane vesicles before the matrix proteins are translocated. As a docking factor for PEX19, is necessary for the import of peroxisomal membrane proteins in the peroxisomes.
Sequence:
MWSSIKDFIYRHRRKFITTGVVIGGSVFLLKWLQYKLRELQERQAKEIGEKLKRMQHYECTDRTCNQTILGLSPALSEKVFQSLSTDDILAKLRTNPDNKLELWEELRIVAFTRLITLVYGASMLAVTLRVQINILGGYLYKATVEDSQQQAISLEVQTAYLSLIQHFMRDGIDRLIEIVRKNVTTVMQRYSLKQQLTLADTETLLWSIEMALNNEKGNPIDGIATYTLPNPGASLTGVDGAFSTMFQETLDVLESVESTEVSLANVSIGLAKVMDKLADYYMSSSSGASKQNSKSNLNVESIANINGITISLAKLIPIVNGLASKVAPVPAGANGTVSNGLVPALPEETDLMSSMIVHFLHSEKLRTLGANVYETFCH
The following text describes a protein:
Function:
Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of E2f during S phase. E2f degradation is necessary to ensure proper development. Substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, leading to recruit the DCX(DTL) complex.
Subcellular Localization:
Cytoplasm.
Sequence:
MNIYNKLRAREHGYGNERTYDFALRRLSVAKEDSWRGIAPANYCPDFNPEPPIFSAKFANCDGYRHILAIANEDGKITLQDTTQRNHQPEEQSLVGPQCHFNAVFDLEWAPGQMRFVSASGDHTARLWEVAGSGIRGLNSYVGHTRSVKSAAFKRTDPAVFATGGRDGAILIWDIRANLNMDLTSRVDNCIYSGHTGGPGTPVSQRKQRTRTPKMAGGTTSSSITGLAFQDNDTLISCGAGDGVIKVWDLRRNYTAYKKEPLPRHKLPYAGSSTFRGFTNLIVDASGTRLYANCMDNTIYCYNLASYSQRPLACYKGLLNSTFYIKSCLSPDGKYLLSGSSDERAYIWNLDHAEEPLVALAGHTVEVTCVAWGSSHDCPIVTCSDDARHKIWRIGPDLDGLSEAERAEKYRGTASYVREFGKKAFGPSSGNHKYNLRDLESTPRSLKRLMDQNERTPGSVEKTTTKRSFLEMLGVAGQETEATEQPQKRAKPLESRGRRLFGPSSQETACRHIQLQSINEEDASPSKRQKENSAAEDVSPLHKLLSTPSHSPLSENVNHVYTSPPTTSAAAAAVAADALNPPPISAAIYSPTSNLPNYVLDGEAPHLGIMSPKRKAKEKVDWLTNIRKQKLMSGRAHVTLSEKISEEQQADVLASPRLQSLRQSECSPRIHASPRRRISHTDGGGGTPAGSSSHSHSQSQPKTPTSSRRNSETTLLRFFSIQRSSSVPAEETTTTNAAPSSSDPHPPAVTAPAATPLSMRTPTTAVGSD
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP49 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, and pre-ribosome transport.
Miscellaneous:
MISCELLANEOUS: Present with 4760 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
Domain:
Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. FG repeat types and their physico-chemical environment change across the NPC from the nucleoplasmic to the cytoplasmic side: GLFG repeats are especially abundant in NUPs in the central region (lacking a charged environment but are enriched in Ser, Thr, Gln, and Asn).
Sequence:
MFGLNKASSTPAGGLFGQASGASTGNANTGFSFGGTQTGQNTGPSTGGLFGAKPAGSTGGLGASFGQQQQQSQTNAFGGSATTGGGLFGNKPNNTANTGGGLFGANSNSNSGSLFGSNNAQTSRGLFGNNNTNNINNSSSGMNNASAGLFGSKPAGGTSLFGNTSTSSAPAQNQGMFGAKPAGTSLFGNNAGNTTTGGGLFGSKPTGATSLFGSSNNNNNNNNSNNIMSASGGLFGNQQQQLQQQPQMQCALQNLSQLPITPMTRISELPPQIRQEIEQLDQYIQKQVQISHHLKADTIDHDELIDSIPRDVAYLLKSESATSQYLKQDLKKISSFKSLIDEDLLDTQTFSVLLQQLLTPGSKISSNDLDKFFQKKIHLYEKKLEDYCRILSDIETAVNGIDTDLFGAPNNPNSTAITADLGSSEAENLLQLKTGLAAIVSTVIEEFTLFMDIAERIAVLHQKTKTLASLSI
The following text describes a protein:
Function:
GRF is released by the hypothalamus and acts on the adenohypophyse to stimulate the secretion of growth hormone.
Subcellular Localization:
Secreted.
Sequence:
MPLWVFFFVILTLSSSSHCSPSPPLTLRMRRYADAIFTNSYRKVLGQLSARKLLQDIMSRQQGESNQERGARARLGRQVDSMWAEQKQMELESILVALLQKHSRNSQG
The following text describes a protein:
Function:
Converts proline to delta-1-pyrroline-5-carboxylate.
Sequence:
MLSRLLKQACVVRRSHQPSLSIFPSSYFHPSFSIHPSITIHPSISIHSSSASTSSRTPSTSQSALRTLSTSQSAVGFDDPAIAKLDPSFNNPQEAFRSKTNFELIRGYLVFQLCSINYLVDNNKKVMKLARKLVGKNLFEKIMKASFYGQFVAGEDAERIKPVVERNMSFGVKSILDYSAEKDNHVEEARTTELKIKKTNEEKKFNKNKKADDKKFSPSYEFGDRREHVISARTYFYEDEKQCDENMQHFIRGIDAVSGATNATGFAAVKLTALGRPQFLLQLSEVLVRVRRYFDTLAQCYGTGTVTKQDFERHLKSFNLDQEETQRWFTVLDCTKDGSVEIDLLDWHNLLEVNVSLAKLLRVPNLRTGKLEPLVKHLTDVEEEQMKNMLHRIDKILKYAESKDVRVMIDAEQTYFQAAISRLCMEMMRKYNGKKATVFNTYQCYLKDAHNLLCNDLALSKREDFYFGAKLVRGAYIDQEKLRAQTLGYEDPINPSYEATSQMFEKTVGEVMRSINERPKGKIAVMMATHNEDTVRMVLKKMQEYEIKSTDKLICFGQLYGMCDQISFSLGQAGYSVYKYVPYGPVEEVIPYLSRRAIENRGILAKVKKEKKLLRSEIWRRFWRLKWFYKPPRPDILKQHQPQQPHQPQLQKTEQQYKSPSSPSSPRQTPQILRSSAAPK
The following text describes a protein:
Function:
Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI).
Subcellular Localization:
Nucleus.
Sequence:
MAPAPRDERLIRALQARAALASAQNNIRKSASYQKAVEKLTAHRRPITSAMEIGMVKGIGVQIKKLLEKVYNGDVEEIPPEAEEAMEYGDLPIPQGFAYIPGPNTGARAILIAMFGETKRPGYPGFLMKDQIQAAATATGISNTSMYPQPNVGRFYSGWDGIRTLEENGLVLRTKHGMGVKEQFRLTDQGRQLAYFLEGELGLQQGGRQDGGVALPQDFSPAHRRLSGHCQGRQAGEGGFPEVMIGRGREIEMGSNLQQVEEVEAATGEGFRLYKAVCKSSSAVRKKYAVQLHVRVTLARDAEVEQAEALGRVFAGRRPELVARLKEMGFSEDRVLAALAATGADEAAAVQMLVDGASMQRDESGTAAPGGVTQMVVVRSECACPEGRSSHGKCKHAAALFLRVDAHLRSGAELDRPEPGKKKTPRKKRENGDGGLQAKTAPKRRKSGGGAEAPLPREEDRSLGAIAAQLAKSVGSPITPPKHKDVARTPVGASPREMAAQAAFERAAMQASLRKDSPTRAPPVEKGTGQRNVDFVDLEGGLGRAHERHESDQGVRRAVSANKESRSETWKGKEAARDALHGSMLNLGRATPGKGKAVAFVDLDSDCDDPPGQRDADSEEDAALLSVDWKSPRASWGSGWSSAATPASDHREKSGGRRGEEAGRGRSLDLDWLTGDNAPDPAELDRLVDTVTATAEPGSAPSASGRKQGGEVGGVRRVTVVVDETERQTNSNPNSVYLELHRQHEALHAVAGVALAAEKHKLETGDYLWLAETDEGSFVLDTVIERKTMSDLVTRSVTNAHLKQIQKMRASGLPHVCLLLEGEFRTARKFVAVAGQDCRGDVDSAEAVWQLMAELLIGTAKGMDVPQGVPIGSGYGPPPPVRVLQTKDVKGTCKLLTHISAALAARVGGGLEGGEAASAAASRQISLEDFNKEARQRRTKMNKLLKEAEGRAIESRVGDDGLEDPGERRGFADEVQRLSADPDAGVGPSAAQARSGVADASAQGGQPCDECEAQRAALECAECEQALCSDCCASLHSGGARRAHRLTSLPPPWQCEECEGASAAVSCGECEQALCASCSAKIHSKGARARHAVAPLSLAPMQPTSRVSTPPDTHDSVERSGRALMVASSSVYASLRTVDLGPRVALEQTRGERDRGPVEESLYLGLADPGGAAGRAGEREAFWVVLVKGDAFLRGMIQSQVAVSGASSATCPEPDLQAAAVLFLTSLPDPPCPSAHSPGKILILENVLHHCRAMAAAAERARLNGAAGPGEDGDQELRAFLGCHDLNEEMIRWIVRIMFSRGWNVQFTGNQLESSLLFRHLAKAYVK
The following text describes a protein:
Function:
May be involved in the turnover of nuclear polyadenylated (pA+) RNA.
Sequence:
MLLRDEDSDAFRDWLLPKVEKICDADSAVLADYVVALVSANTTERGLKKNCLESLEDFLQDNTAPLVDDIARDESDSHYNAASNGSRPIKQATGRGGIHTLQGGAAAFRPQHALPAFAPMPTAPGFPPVPTTNGLPPRPTASGLPPRPMSNMPTMPNMANLPPPPPGPMPFEMMNNPMAFMSMMAAMSTNMGGIPPLPLVNTQGSHAGGRSRVGKCYNYHEKGFCALGSLCAFEHGDGDDIPQAVPEYDPDQPSLGSNRTRHGGGKAVKARAPFSMLGPSYDHTNTTLVVEQIPTEKLREKDVRAFFSEFGTVVDVQMHTFKSLAIVKFEDNAAATRAYMSPKAVFENRFVKVYWYKQGYGEGAFDGEVEMGDGDGNDFYMQDDRLNPEEIAKRQAEAQKAFEERRKKTQEADAKAAEIERRLKENDVETKQIRQQLAELGVDYDDGMHKEQSPGLANLALEAENLFTLKEAPSMGRGYGFPLRGIRRGRGTRRAGYLGRTSKSSVKRLDNRPRRLAVSDIEKDTPRDEALRQYLMPDVVILTFEYRYQAETFLDNSHQILDVGELVLAWVPNDAFGGLPVSTTTKEPEAAANNEFHVNDDTNGNDDDSDSSATAEEQIKVEAEEDEHVEQDFDVADDADDFL
The following text describes a protein:
Function:
Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with psmg2.
Sequence:
MVDAFGLWELNFPCSRVDDDDDEEEQITKEQEEQLCPQFVFSPQFSKDVGKTEPIECSVLVLGVGEVASTFLEVHFLCGNNSSVAAVISDKKTEKNFEYLVKNLRNKRSSLLHQLTRNNDVMVCQISSHVEQDKGFYWTQKIFSHIRPAKVVILTSSPASEYNSDDPSEIKTDFVKMMKTNAWSNSCAGPDITDIQTPNTVKGLAASVLTHCQIYKLPAALFMCYTESMHVDAQAVEAFRCKAPYKQSSMGLESGKL
The following text describes a protein:
Function:
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C bonds of the alkyl side chain (Probable). PynA subsequently forms the amide bond between the acyl chain and L-serine. Although pynA has a terminal reductase domain, it appears to require the thioesterase pynI for the release of the straight-chain intermediate from pynA via the formation of a tetramic acid pyranonigrin J. The methyltransferase pynC then coverts pyranonigrin J to pyranonigrin I via N-methylation. The FAD-dependent monooxygenase pynG catalyzes an epoxidation-mediated cyclization to form the dihydro-gamma-pyrone moiety, followed by pynD-catalyzed oxidation of the alcohol to the ketone and enolization to yield the characteristic tetramic acid-fused gamma-pyrone core of pyranonigrin H. Pyranonigrin H is substrate of pynH for dehydration-mediated exo-methylene formation from the serine side chain to produce pyranonigrin E, before the oxidase pynE reduces the exo-methylene of pyranonigrin E into a pendant methyl to form pyranonigrin G. The FAD-linked oxidoreductase pynB performs the reverse reaction and converts pyranonigrin G back to pyranonigrin E.
Sequence:
MSTQVLIVGGGIGGLTLAAMCRRIGVSCRVLERSAALEPVGAGISLAPNALRALDQIGLYDYVRQEGQPVRKIRVYRNQTQWSEIDFQWLERTFGYPVYSIERHGFHRRLYDAAGGSETVNLGAEVAKVIPPQEEAEGVSVVLKDGRRYTGNVLVGADGVRSVVRRALMATINSPPGQSGAVGEDEDAADVIQFTGRVHLSGYTHPLDHLGPADEGIAYWMLYDRSILTTWPCRDHRQWFVGAVPSKLKDPNRSVWKHADHNTINQVYGSEYHPFAPDFHFRDVVKHAERVVASDVFHQTTFPPMAAGRIAMLGDASHAMTSFFGQGACQAIEDATELASALGMIDVRPTDAETILQGYRHSRERRGRDLVVFSDRFALLHTGRLLGSWGPFVRQMVYTWMPLWGWKWALQWLYGHQPTLVEQRNEAAKKTA
The following text describes a protein:
Function:
Regulates pre-synaptic vesicle recycling at neuromuscular junctions of mechanosensory neurons. Plays a role in maintaining a normal defecation cycle.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MDHRAQAREVFVRAQLEAVQKAITKNEVPLKPKHARTIIVGTHKEKSSGIFWHTVGRIQLEKHPVLTWKFCHLVHKLLRDGHRKVPEETYRYVNRFTQLSQFWKHLNTSGYGPCIESYCKLLHDRVTFHNKYPVVPGKLDLNDSQLKTLEGDLDNMFEMTIDMLDQMDALLVLQDRVYEMMNSLRWNSLIPQGQCMLSPLIIAILDTSKFYDYLVKMIFKLHSQVPPDALEGHRSRFRTIFERTKKFYEESSNLQYFKYLVSIPTLPSHAPNFLQQSDLESYRTPHAYLHSEGSEDGTSLNGHDGELLNLAEAEPQQASPSSQPDPREEQIVMLSRAVEDEKFAKERLIQEARSRIEQYENRLLQMQGEFDHAKREADENREEAQRLKNELALRDASRTQTDDARVKEAELKATAAEERFNKMKGVYEKFRSEHVLALTKLGDIQKQLEASEKSKFDKDEEITALNRKVEEAQREAGRALTKAEGDAGAVDEMRTQLVKADIEVEELKRTIDHLRESHANQLVQSSAEETNKIRLAELEVAKESGVGITQMFDHCEDALQNATSITYPPHLAQSAMNNLVNILSNERLDEPLATKDNVFAGHLLSTTLSAAASAAYTASIESYEGVNDQCKKVLAAAKVAFSDDSALSRADKMKLLRQDIQTLNSLMISLPLQTDIDKDVVGNELEQEMRRMDDAIRRAVQEIEAIQRRARESSDGIRLEVNESILANCQALMSVIMQLVIASRELQTEIVAAGKAGGSPAEFYKRNHQWTEGLLSAAKAVGVAARVLVESADGVVTGKGKFEHLIVAAQEIAASTAQLFVSSRVKADKDSSKLDALSVAAKAVNQNTAQVVAAVKNGQTTLNDEGSLDFSYLSLHAAKKEEMESQVKMLELEQSLNQERAKLAALRKQHYHMAQLVANKEGEEAQE
The following text describes a protein:
Function:
Probable methyltransferase involved in the maturation of rRNA and in the biogenesis of ribosomal subunits.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MGQKKKKLAKGRLDKFYYLAKEQGYRSRAAFKLVQLNKKYNFLGSAKACLDLCAAPGGWMQVASKYMPVQSLIVGVDLVPIRQVRNCISLAEDITTQKCRTEIKKALKTWKVDVCLHDGAPNMGTSWVQDAYQQAELTLHALKLATEFLATGGWFVTKVFRGADYNSLIWVFNKLFRKVESTKPQASRNASAEIFVVCQGFLNPKKIDPKLLDPKFVFKEVQEGPKKVDVLSEKKAKRNRSGYEDGVTMLRKKGFISDFIESSQHLLDLASFTEYEFDENAQIFKQHPSTTPEIIECFRDLRVLGKNDFSKIIKWRKAMAEYKEKLDNPEEEETKEPEPERELTQEEKDALLDTELEQLKENLEKKRRKEKKKANEKKRLERKRIELTMHIPGDKIEEGADDDLFVMKGKQDFQDDVVAEHGDSDSDDSDSDDSEVEPDRRTQEEAEMDNDEFMEQQLEDQYKQYILRVSNRAKEFDVKVKKDKLSQDAEFDDQDDDEMEQEEEDHPLYVGKAKPIEKDADMFFDNDLFGGVEYRTEDDEPSEDEQEEEDEDSKPIDISKLKLQKAQPVATKSKKQKTTKGGSEKGGKKHQKMPSGEESDDEDIVQEMDMEEVPMEEDVEYSSDSDEEIDDKIKTKALGEFLLRKKSRNDLVDDSFHRFAFNDNRDGMPQWFIDDENRHHKPQTPLTKDMVDEIKRKIKEIDSRPIKKIAEAKARKKMRLGKKMEKVKEKSSSIMDNADMSNKEKSRAIEKLYAGTDKKNQKPKKIIMIAKKSKTGGGGTGKYKIVDKRMKKDLRAMKQKQKTVGRSAASKKANKKK
The following text describes a protein:
Function:
Predominantly catalyzes the biosynthesis of ganglioside GD1alpha from GM1b in the brain, by transferring the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc sequence of GM1b. GD1alpha is a critical molecule in the communication and interaction between neuronal cells and their supportive cells, particularly in brain tissues, and functions as an adhesion molecule in the process of metastasis. Also shows activity towards sialyl Lc4Cer (N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-enine) generating disialyl Lc4Cer, which can lead to the synthesis of disialyl Lewis a (Le(a)), suggested to be a cancer-associated antigen.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MKTLVRHGLAVCLALTTMCTSLLLVYSSLGGQKERPPQQQQQQQQQAAATGSAQRSAESSPPPRPEIPAGPRPLEGYLGVADHKPLKMHCRDCALVTSSGHLLRSHQGPQIDKTECVIRMNDAPTRGYGRDVGNRTSLRVIAHSSIQRILRNRHDLLNVSQGTVFIFWGPSSYMRRDGKGQVYNNLQLLSQVLPRLKAFMITRHKMLQFDELFKRETGKDRKISNTWLSTGWFTMTIALELCDRINVYGMVPPDFCRDPNHPSVPYHYYEPFGPDECTMYLSHERGRKGSHHRFITEKRVFKNWARTFNIHFFQPDWKPDSLAVNHPENKPVF
The following text describes a protein:
Function:
Required for the proteolytic cleavage of the transcription factor RIM101 in response to alkaline ambient pH.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MFKAFIALLILLIVCWVIQLLPVIAVPFTTPDANIYLSYYNNYKFGVFGICNVERHICSKPSIGYPSTNSTFYAYDNDESFGTGGIVLPSDVRYTISKLLVVHVVAFCFSSLLLIVIFGLIIILFFKYIKTKKDLEGIQLNDSSHEITIHSDEEDNNNNNIDNTNHNNKRASVTINKTIFDLTPFLNLMLVFTFFSVLTTLLAFLADILLFTPNLSYLGWLQLIPIVSMALVTSMLCFIKRSISSRKFFESEYRYANDDMRIMRKTYVDEFWNDNASDDGFYVYTDGFYTRNGDNVQQPTSNTAGSLLSEHHDVSIVEPRTFLDTDDSRRGSSPHEFIELQNLRPV