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:
MAENRTSSISVVLVKVAKVEGQKVTSYDFAGAREAVNSPGVEANGAKTNKWVPQYNRTNLYRDENELVFRRVRGILNKLTPDKFDKLFYELLHVGVETKYILKGVILLVFEKALDEPAYSSMYAQLCLRLSEEAPNFDDPGKTGNSTFRRLLLKQCEEEFNNRSKASQAFDKKDDLTQEEEEERGSTKRKMLGNIRFIGELAKLDMLHETILHKCIKQLLDKKKRASVADTSEDMECLCHLMKTVGSRIDGPKAKPLVDQYFERIYQIRSRSDLPSRIRFMLEGIEELRTNKWIPRKVARDVGPKPINQIRQEAFRDFPPSYPVPHGMLRNSPPHPGPMFCRHPGGGKPAMRQMEPNQGHGFNDVFLRDDPGRARFDDFGGMMDNKAPYGLSYNEDEFDRFTPKDPWAGLANTSIRSSPPLTGSPPSSRHPHYGGSPPSSRNQQYGSRRPPPRPIQLNTDGEISLRPARDSIAAKTLGLNTRPQGKVDPLNRNKAPPIIEKPKPKKPQGPSKADLEKQMTEILKAYLDNKNDTAAIRSIQAMKTNKNGKMQVFHSLEIGLDKNDEERHLICQLLQAMHKEGLTSTDAILQGLQTVLEGKADSDDGHHVKDYIACMAARTIIQGLVTLSDVCKLMDGGSFYPTLLLILKKLEQLNGQEWLMDAFNEAKIDLLSTLPESSRNSCKMMVILEEQSLSFLFPLLRIQAELYKKIEEDPNSSAIYKWIKDNVDASLHDQPEFINAITTCILRYATQQSTLGKGVDISLPPDKDLVEKEIHAIKKLKPLLDKFLLEKIDLQVCALYALQVFCHTNNHPKGLLLRMFMLLYDLEVVDEEAFVKWKEDVNEKYPGKGKALFQVNTWLTWLETADEEGSESEPE
The following text describes a protein:
Function:
Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MMDIYLVIVGFILHLILFASIFDIYFTSPLVHGMTPHSTPDEPPAKRLVLFVGDGLRADKLYELKEDGTSRAPYLRSILKNQGTWGVSHTRVPTESRPGHVAIIAGFYEDVSAVTKGWQENPVEFDSVFNQSRFTWSWGSPDILPMFAKGASGDHVFIHTYPPESEDFADSDASKLDTWVFDKVKEFLSESKEDPSLRSKLNSNRVILFLHLLGIDTNGHAHKPYSKEYLENIALVDAGIKEIVGVLEDAFAHDGKTAYVLTSDHGMTDWGSHGASHPDETLTPLLAWGAGVREARHTTNQQFQDNFLQDWHLEDIERHDVNQADIAPLMSSLIGVPFPLNSVGVLPVDYLNGTEEYKARSLLTNAKQIIAQYEVKENQKFATTFRALFRPFKPLSSGQKELLLKHIHIHMARNRFKQVIAETEKLISLGLDGLGYYQTYDRFFLGSSVTLSYLGWMAYILHILLKYHTSLATPPKPRNHGNTHPGLLPAFCMIAALIAILLALQTSPINYYICALTPVPLWYAVVKRWEVFHQSLVNITTRHSLQEIAGYSVLGVVAIETLVLSLFYREVISVGLVGVALWPLCSGVKHRNKMYSVGWLISCLVLAVFPMLPVVGRDPNITLVVLAGVLLAVSAYILFRHLLKLQSSSSINPLLTWLQIALLLISVMVVYITWIHITNKEGVPLPNKIFSWTMLLAAFVLPSFSSVVIGHRLLGVALSLSTVYMLLSTSHEGLFCLCLCYVMFFWILCESNLNQQQTDKIHQVSFNEEANLEKAPPRNLALTDLRCAWIFVFFILAAFFGTGNIASINSFDPSAVYCFLTVFNPFIMGSLLLMKNVILFLLVACAFQAIHILLRLPTSSLYLVVLLLSDAMALHFFFLVRDSGSWLEIGTSISHYVIVMSMILFIMLLLLLARLITTLSWKRSFKKHHAR
The following text describes a protein:
Function:
Plays a role in the regulation of the early stage of white and brown preadipocyte cell differentiation. Promotes adipogenic commitment of preadipocytes by increasing gene expression of the transcription factor PPARG in a BMP4-dependent signaling pathway.
Subcellular Localization:
Secreted.
Sequence:
MMGIFLASVGFMFFSVLYVQQGLSSQAKFTEFPRNVTATEGQNVEMSCAFQSGSASVYLEIQWWFLRGPEDLEQGTEAAGSQVELLPDRDPDNDGTKISTVKVQGNDISHKLQISKVRKKDEGLYECRVTDANYGELQEHKAQAYLKVNANSHARRMQAFEASPMWLQDTKPRKNASSVVPSSVHSSANQRMHSTSSPQAVAKIPKQSPQSACIEFSGAMEARAHERGFQVRSSLGHLRSIS
The following text describes a protein:
Function:
The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.
Miscellaneous:
MISCELLANEOUS: Present with 12000 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MTSIGTGYDLSNSVFSPDGRNFQVEYAVKAVENGTTSIGIKCNDGVVFAVEKLITSKLLVPQKNVKIQVVDRHIGCVYSGLIPDGRHLVNRGREEAASFKKLYKTPIPIPAFADRLGQYVQAHTLYNSVRPFGVSTIFGGVDKNGAHLYMLEPSGSYWGYKGAATGKGRQSAKAELEKLVDHHPEGLSAREAVKQAAKIIYLAHEDNKEKDFELEISWCSLSETNGLHKFVKGDLLQEAIDFAQKEINGDDDEDEDDSDNVMSSDDENAPVATNANATTDQEGDIHLE
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of the 2'-O-methylguanosine corresponding to position 2270 in S.cerevisiae 21S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.
Subcellular Localization:
Mitochondrion.
Sequence:
MIRSRVNLAREVPKKAKAHLSKERRLIKEDSEFVFGTHSVKNALATRKRECRALYVQNADIHSEFEEFLNKLQYKIPIKSVNKEHLNQITACRPHNGVVLEASSLNVPTISDLLFPAGEEYNNKNGQDSPHNDLNEGKSSSSDNYPPLYVYVDGITDPQNMGAVIRSAYILGAKGILLSKKHNTFLSPVVSKASAGALEVFNISHVKNPMVFLRNSVLKGWKVIGTKPALPDNKDQIYTPHKIKTELMNEPKILVLGSEKGLRTNILTQCSHYVSIPGGDKYVDSLNVSVAAGILLYSLVN
The following text describes a protein:
Function:
Odorant receptor.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MGKDNASYLQAFILVGSSDRPGLEKILFAVILIFCILTLVGNTAIILLLVMDVRLHTPMYFFLGNLSFLDLCFTASIAPQLLWNLGGPEKTITYHGCVAQLYIYMMLGSTECVLLVVMSHDRYVAVCRSLHYMAVMRPHLCLQLVTVAWCCGFLNSFIMCPQTMQLSRCGRRRVDHFLCEMPALIAMSCEETMLVEAIHLCPGGGSPPGAALPHPHLLWRDCSRGAEDEVSSRAKESLPHLLFSPHSGLSLLRNHHLRVPEAGQQLLPRSGEVPDSLLHHRHSQHQPPHLHFEEQGCEGDHEETSGVGERGWGASTRGTL
The following text describes a protein:
Function:
Lysosomal proton-coupled steroid conjugate and bile acid transporter. Preferentially recognizes lipophilic steroid conjugates or bile acis as endogenous substrates and seems to mediate escape from lysosomes to the cytoplasm (By similarity). Modulates hepatic cytosolic copper homeostasis, maybe acting as a lysosomal copper transporter and sequestering copper ions in the lysosome (By similarity). Delivers pathogen-associated molecular patterns to cytosolic pattern recognition receptors as part of the innate immune response to microbes. Selectively transports bacterial muramyl dipeptide (MDP) into the cytosol for recognition by NOD2, triggering inflammatory responses (By similarity). Likely acts as a redundant importer of cyclic GMP-AMP dinucleotides (cGAMPs) in monocyte and macrophage cell lineages. The transport mechanism, its electrogenicity and stoichiometry remain to be elucidated (By similarity).
Subcellular Localization:
Lysosome membrane; Multi-pass membrane protein.
Sequence:
MKIPFVEPVICLSVFAVTLNSPLTTQYVYRRIWEETGNYSIALESNTSECAKNKSSPIFAFQEEVQKKVSLFNLEMDISGLIPGLVSTFVFLSHSDHGGRKFPLILSSVGALANSAWLCLLSYFALPIQLLIASTFIGALFGNYTTFLGASFAYIVDQCKEKKQRTIRIAIIDFLFGVVSGLTGLSSGYFIRGLGFVWSFLIVTVALFVNLIYILLFLEDSMKESSSQNISVSWTETFKNLFHRTYMLFKNASGEQQSLCCLLLFTMITYFFVTIGVSPIFVLYELDSPLCWDEVLIGYGSALGSVTFFSSFLGIWLFSYCMEDIHMAFIGTFTTMVGMAMTAFARTTLMMFLVRLPFLFTVMPLSVLRSMISKVVHSTEQGTMFACLAFLETLGGITAVSTFNGIYSATVAWCKGFVFLLSAVLLLIPAISLCVIKYVSRNTGSYVLLIQEESSEDTSDR
The following text describes a protein:
Function:
Catalyzes the synthesis of indole-3-acetic acid (IAA)-amino acid conjugates, providing a mechanism for the plant to cope with the presence of excess auxin. Strongly reactive with Glu, Gln, Trp, Asp, Ala, Leu, Phe, Gly, Tyr, Met, Ile and Val. Little or no product formation with His, Ser, Thr, Arg, Lys, or Cys. Also active on pyruvic and butyric acid analogs of IAA, PAA and the synthetic auxin naphthaleneacetic acid (NAA). The two chlorinated synthetic auxin herbicides 2,4-D and 3,6-dichloro-o-anisic acid (dicamba) cannot be used as substrates.
Sequence:
MAVDSPLQSRMVSATTSEKDVKALKFIEEMTRNPDSVQEKVLGEILTRNSNTEYLKRFDLDGVVDRKTFKSKVPVVTYEDLKPEIQRISNGDCSPILSSHPITEFLTSSGTSAGERKLMPTIEEDLDRRQLLYSLLMPVMNLYVPGLDKGKGLYFLFVKSESKTSGGLPARPVLTSYYKSDHFKRRPYDPYNVYTSPNEAILCSDSSQSMYAQMLCGLLMRHEVLRLGAVFASGLLRAISFLQNNWKELARDISTGTLSSRIFDPAIKNRMSKILTKPDQELAEFLVGVCSQENWEGIITKIWPNTKYLDVIVTGAMAQYIPTLEYYSGGLPMACTMYASSESYFGINLKPMCKPSEVSYTIMPNMAYFEFLPHNHDGDGAAEASLDETSLVELANVEVGKEYELVITTYAGLYRYRVGDILRVTGFHNSAPQFKFIRRKNVLLSVESDKTDEAELQKAVENASRLFAEQGTRVIEYTSYAETKTIPGHYVIYWELLGRDQSNALMSEEVMAKCCLEMEESLNSVYRQSRVADKSIGPLGDTCGTERYV
The following text describes a protein:
Function:
Chaperone for NapA, the catalytic subunit of the periplasmic nitrate reductase. It binds directly and specifically to the twin-arginine signal peptide of NapA, preventing premature interaction with the Tat translocase and premature export.
Subcellular Localization:
Cytoplasm.
Sequence:
MDDNEWHVCGLVLQAKPARFVQLMDHLLAIPGTEIPTSDPALGKLVVVMQAARSDTLLNHIESARNLDGVLAVSLVYHQQDLQGEEMP
The following text describes a protein:
Function:
Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends.
Subcellular Localization:
Nucleus. Cytoplasm. Mitochondrion.
Sequence:
MVPDKPITSIPPPRDTYLRSRDHPSYPRGATTCCILCALVRRSHSGTRAGQKRRCCYFACHRGLSGRLISQPKSGPLIKALDWPEGRSREEGNAIKILIRWATWNGCRRAFVTVMPKRGKKGAVAEDGEGPKTEPEAKKSKTGTKKNEKEAAGEGPVLYEDPPDQKTSPSGKSATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGEEEHDQEGRVIVAEFDAFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTAYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL
The following text describes a protein:
Function:
Involved in peroxisome biogenesis.
Subcellular Localization:
Peroxisome membrane; Single-pass membrane protein.
Sequence:
MSKRRKNQGYLAIIAAVSIGAAAYLWWRNHSEDDSVSKFNQQDDGTAQDNQIKEKPAIKLGKKRLHRSLCVIISNKLSNLVELDWDEILQEDIVFLILPSVNDFQNSNDIKTDTHKIINCDTELGLWACVRTLKKNELLVCADDIKVPDDIGRYCDKISQIKSSQQLMNYLDET
The following text describes a protein:
Function:
Mitochondrial protein implicated in negative regulation of leucine tRNA levels, as well as negative regulation of mitochondria-encoded proteins and COX activity. Also affects the 3'-processing of mitochondrial tRNAs.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
ILHRLDPLGARWAGGRKGPACSLSQRPLGQGSQKNTGSLSPDLSQPSPAAAQGEEEEESFGTLSDKYSSRRMFHKSTAQLYNLRLKEQSIGEDEEGELEAKSWQGPRNTAYWYFFQCKRLIKEGKLVEALDLFERQMLKEERLQPLECNYTVLIGGCGRTGYLKKAFRLYNDMKKRDLEPSDATYTALFNVCAESPWKDSALQSALKLRQQLQARNFQLNLKTYHALLKMAARCADLRMCLDVFKEIIQKGHAVTEETFSYLLMGCIQDKKTGFRHALQVWRQMLSLGLQPSRHGYNLLLGAARDCGLGDPEVASAVLLRPREELVLLQPPAGGRQARQRAGAEVDHSMSARLHVEALERQLFLEPSQAFEGPPEPQEARSASKAQPGVETKAEPEHTVALSSVAPEPPLQGPEANLLAPGAVSSAVVSFGTVTTPADRLALMGGLEGFLGKMAEHGLQPDIKTLTLLAELVEPGSPAESSLLTLLDTHQVEADLTFFHTLMRKKSKLGDLEGAKALLPVLAKRGLVPNMQTFCNLAIGCRRPGDGLQLLADMKKAGTTPNTHIYSALISAAVKRLDYSYLIDVLRDMRRSGVPANEVVIRQLEFAAQYPPAFDRYKGKNTYLEKIDGFRAYYKQWLKVMPAEETPHPWQKFRTKPKGDQDTVTMADVHRGLGDR
The following text describes a protein:
Function:
May be involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Required in a complex with RAB11A and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Together with RAB11A participates in CFTR trafficking to the plasma membrane and TF (transferrin) recycling in nonpolarized cells. Together with RAB11A and RAB8A participates in epithelial cell polarization. Together with RAB25 regulates transcytosis. Required for proper localization of bile salt export pump ABCB11 at the apical/canalicular plasma membrane of hepatocytes; Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Can hydrolyze ATP in the presence of actin, which is essential for its function as a motor protein. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation.
Subcellular Localization:
Cytoplasm.
Sequence:
MAVAELYAQYNRVWIPDPEEVWKSAEIAKDYRAGDRVLRLLLEDGMELEYPVDPGSLPPLRNPDILVGENDLTALSYLHEPAVLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAKQVIKPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFRAGQVAYLEKLRLDKLRQDCIMIQKHVRGWLQRRKFLRERQAALTIQRYFRGQQTVRKAITATALKEAWAAIILQKYCRGYLVRNLYQLIRVATITIQAHTRGFLARRRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIEGKLEEPFSHLNRIREEERMQGRAVEAQSEMHPEGKERLVGAIHEPHEAIKFPKKQPEAEEEVESILQQEASRLSLEKRDLEEELDMKDRMIRRLQDQVKTLTKTTEKANHVHLPSGSREYLGMLEYKKEDEGKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSAINGIKHVVKEHFEDLEMLSFWLSNTCHFLNCLKQYSGEEEFMKYNSPQQNKNCLNNFDLTEYRQILSDVAIRIYHQFIIVMENNLQPIIVPGMLEYESLQGISGLKPTGFRKRSSSIDDTDAYTMTSILQQLSYFYSTMCQNGLDPEIVRQAVKQLFYLVGAVTLNSLLLRKDMCSCRKGMQIRCNISFLEEWLKDKNVQSSLAKETLEPLSQAAWLLQVKKTTDSDAKEIAQCCTSLSAVQIIKILNSYTPIDDFEKRVNPSFVRKVQALLNNRGDSAQLMLDTKYLFQVTFPFTASPHALEMTQIPSSFKLGFLRRL
The following text describes a protein:
Function:
Involved in the targeting and/or fusion of transport vesicles to their target membrane.
Subcellular Localization:
[Isoform 1]: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein. Synapse, synaptosome; [Isoform 2]: Cytoplasmic vesicle membrane; Single-pass type IV membrane protein. Synapse, synaptosome.
Sequence:
MSAPAQPPTEGAEGAAPGGGPPGPPPNMTSNRRLQQTQAQVEEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFESSAAKLKRKYWWKNCKMMIMLGAICAIIVVVIVIYFFA
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Sequence:
MSVENPMRIAIVGVGGVGGYFGGRLAQAGHDVFFIARGDHLAAMRSHGLRVQSIAGDFWLPDVKATDQPAEVGPVDLVIVGVKGWQVREAAYAMQPLIGPETAVLPLLNGVDAPTELAEVLGAEHVLAGLCRIIAYRAAPGVIVHAGVNPPSIDFGELDNRHTPRLARIQAALEGAGIRAFIPENIHVALWQKFMLICAWSGFGAATRAPIGVWRSLPETRPLVERCLQEVVDVAAARGVMLPDNAVSTMMAFIDSMPYEGTASLQRDIMSGQPSELASQNGALVRLARAAGVPVPVNEMLYAILLPQELAARGQLPTQR
The following text describes a protein:
Function:
Stimulates the activity of serine palmitoyltransferase (SPT), and thus plays a role in the biosynthesis of sphingolipids.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MTQHKSSMVYIPTTKEAKRRNGKSEGILNTIEEVVEKLYWTYYIHLPFYLMASFDSFFLHVFFLTIFSLSFFGILKYCFL
The following text describes a protein:
Function:
General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Miscellaneous:
MISCELLANEOUS: The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain.
Subcellular Localization:
Cytoplasm.
Domain:
The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
Sequence:
MISGILASPGIAFGKALVLKEEKIVLDTQKITDDQIDAEVARFYEGRNAAVEQLNSIRERALISLGEEKAAIFEGHLMILEDEELEEEILDYLRSNKVNAGVAASKILDQQVTMLSEIDDEYLKERAGDIRDIANRLVKNILGMYIVDLGDIQEESILVAYDLTPSETAQLNLEKVLGVVTDIGGRTSHTSIMARSLELPAIVGTNKVTKLVNTGDYLILDAINNQVYINPTASQIDELKALEAKISEEKAELAKLKDLPAITLDGHKVDVVANIGTIRDCDGAERNGAEGIGLYRTEFLFMDREQLPTEEEQFIAYKQVVEAMNGRLTVIRTMDIGGDKELSYLDLPKEMNPFLGWRAIRIALDRREILNAQLRAVLRASAFGKLAVMFPMIISVEEIRELKAVIETLKAELREEGRLFDNNIQVGVMVETPSAAVNAKFLAKEVDFFSIGTNDLTQYTLAVDRGNEFISHLYNPMHPSVLGLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISVPRIKKLIRNVNFQDAKVLADTALQKPTAAEIDQLIEEFLLENSLN
The following text describes a protein:
Function:
Involved in salt stress tolerance.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MVSDRSCIGYLRSVIAGSVDTHTGHECTITNHAAEEGGGTAAAAAVKVMTVSGSGKRGRYVRQVTGRHNDTDLHVAARGGDAGALRRALDEAAAAVATGEGREALEEVRRAVAAEPNEAGETPLVAAAERGHLEVVRELLRHLDAEGVAAKNRSGYDALHVAAREGRHAVVQEMLLHNRLLAKTFGPANTSPLISAATRGHTEVVKLLLELDDFGLVEMAKDNGKNSLHFAARQGHVEIVKALLEKDPQLARRNDKKGQTALHMAVKGTNCDVLRALVDADPAIVMLPDKNGNTALHVATRKKRAEIVAVLLRLPDTHVNALTRDHKTAYDIAEALPLCEESSEIKDILSQHGALRSRELNQPRDELRKTVTEIKKDVHTQLEQTRKTNKNVHGIAKELRKLHREGINNATNSVTVVAVLFATVAFAAIFTVPGGNANNGVAVVVQAASFRIFFIFNAIALFTSLAVVVVQITVVRGETKSERKVVEVINKLMWLASVCTTISFIASCYIVLGRHFQWAALLVSLIGGITMAGVLGTMTYYVVKSKRMRKIRKKEKMSRRSGSSSWYDNTELSETELNQVYAL
The following text describes a protein:
Function:
4-dimethylallyltryptophan N-methyltransferase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid. DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline. EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine. Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A. Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus.
Sequence:
MTISAPPIIDIRQAGLESSIPDQVVEGLTKEVKTLPALLFYSTKGIQHWNRHSHAADFYPRHEELCILKAEASKMAASIAQDSLVIDMGSASMDKVILLLEALEEQKKSITYYALDLSYSELASNFQAIPVDRFHYVRFAALHGTFDDGLHWLQNAPDIRNRPRCILLFGLTIGNFSRDNAASFLRNIAQSALSTSPTQSSIIVSLDSCKLPTKILRAYTADGVVPFALASLSYANSLFHPKGDRKIFNEEDWYFHSEWNHALGRHEASLITQSKDIQLGAPLETVIVRRDEKIRFGCSYKYDKAERDQLFHSAGLEDAAVWTAPDCDVAFYQLRLRLN
The following text describes a protein:
Function:
Component of the cleavage factor I (CF I) involved in pre-mRNA 3'-end processing.
Subcellular Localization:
Nucleus.
Sequence:
MSMTAGNVVFVGNIPYDVSEQQMTEIFNQVGPVKTFKLVLDPETGSGKGYGFCEFFDSETTAMAVRKLNNSELGPRKIRVEFPSNDPRRNQSYEYTERTDRYMEQQNAHESSYNSRFIPPVLHSTSSLPASQGGGMPSPAIYSSSMATNLNKNINSTSVPAYNFHNSMTSDFDSASQPHTDAYNARTFQYNKSSQNKGDYTSGTSISNPTSIPLAPSVVQVLSTFSAQELLNMLSKLQTVVHIAPEEARRLLIANPALPYAAFQAMLLMNLVDANVLQQVVVAVKNKNMHQPASATSSPPSVPQKIPSSNHKSQQANGSDQGNEGKRMALIQQLLALTPEQINALPPAQRDQILSIRRQHFRQ
The following text describes a protein:
Function:
Probable FMRFamide-like neuropeptides. Binds to neuronal receptors such as dmsr-1 to promote sleep in response to cellular stress also known as stress-induced sleep (SIS). Plays a role in behaviors associated with SIS, acting in concert with the FMRFamide related peptide, flp-24 and neuropeptide-like protein nlp-8; AADGAPLIRF-amide: Inhibits muscle tension in somatic muscle. Acts as a ligand for the npr-22 receptor in vitro. Acts as a ligand for isoform a of the dmsr-1 G-protein coupled receptor in vitro; APEASPFIRF-amide: Inhibits muscle tension in somatic muscle. Potent inhibitor of the activity of the dissected pharyngeal myogenic muscle system. Acts as a ligand for isoform a of the dmsr-1 G-protein coupled receptor in vitro; [ASPSAPLIRF-amide]: Acts as a ligand for the npr-22 receptor in vitro. Acts as a ligand for isoform a of the dmsr-1 G-protein coupled receptor in vitro; [SPSAVPLIRF-amide]: Acts as a ligand for the npr-22 receptor in vitro. Acts as a ligand for isoform a of the dmsr-1 G-protein coupled receptor in vitro; [SAAAPLIRF-amide]: Acts as a ligand for the npr-22 receptor in vitro. Acts as a ligand for isoform a of the dmsr-1 G-protein coupled receptor in vitro; [ASSAPLIRF-amide]: Acts as a ligand for the npr-22 receptor in vitro. Acts as a ligand for isoform a of the dmsr-1 G-protein coupled receptor in vitro; [AMDSPLIRF-amide]: Acts as a ligand for isoform a of the dmsr-1 G-protein coupled receptor in vitro.
Subcellular Localization:
Secreted.
Sequence:
MMTSLLTISMFVVAIQAFDSSEIRMLDEQYDTKNPFFQFLENSKRSDRPTRAMDSPLIRFGKRAADGAPLIRFGRAPEASPFIRFGKRAADGAPLIRFGRAPEASPFIRFGKRASPSAPLIRFGRSPSAVPLIRFGRSAAAPLIRFGRASSAPLIRFGRK
The following text describes a protein:
Function:
Required for 3'-end cleavage and polyadenylation of pre-mRNAs. Also involved in chromosome segregation where it has a role in chromosome attachment to the mitotic spindle (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MSYEPRGDHDKGYGGGGGHDGLPPRNRGRRPVTDYGASVVHYMRHRQPRYRGSYAGEVERPSPSYIVDMLPPYARVTNPADSVPSRHLHSSLNKIKHPINVVRWTPEGRRLLTASSSGEFTLWNGTGFNFETIMQAHDSAIRALVYSHSDDWLVSADHDGIIKYWQPNFNNVESIRGHTDPIRDLAFSPNDTKFVTASDDQTLKVFDFAGGSTDMTLTGHGWDAKSCDWHPSRGLIVSGSKDHLVKLWDPRTGRCLTTLHGHKNTITKTLFERVQGNCLATSARDQTARVFDLRMMRDIALLRGHEKDISTLTWHPVHSNLLSTGGSDGSLFHYLLDEPNTAPDGSVMPIPAVYDTADPSSAPAQPIYPAHKIPYAHDFAIWSLDWHPLGHILASGSNDRITRFWSRARPGEAPESFNDRYHIGEAAAEAQGTWDRRGGRHMRQVEEEQELEDEMDGLVDQKMPIKGQPGVGGGGMMPGLSFPSIPGLPLQQVPSSGPGGSGFIPPPPIIPGVGGATGVPPPLPFPIPGMPGLPAGVVPPPLPGLDLKNPPDFSALAEMMKKAGYQPPPPPGSAGAPMPPPGILPPGLIPPPGAAGFPMPPPGFAPPPLIPGAGGPPGGATHPDGGNDQYDSSGRRRAPLPSQEESLRMEQSKGNYTRVR
The following text describes a protein:
Function:
Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Subcellular Localization:
Cytoplasm.
Sequence:
MSIQNISFLGAGSIAEAIIGGLLHANVVKGEQITVSNRSNETRLQELHKKYGVKGTHNKKELLTDANILFLAMKPKDVAEALTPFKEYINNNVLIISLLAGVSTDSIRKLLQKDVPIIRAMPNTSAAILKSATAISPSKHATAEHIRTATSLFETIGLVSVVEEEDMHAVTALSGSGPAYIYYVVEAMEEAAKKIGLKEDVAKSLILQTMIGAAEMLKASDKHPSILRKEITSPGGTTEAGIEVLQEHKFQQALISCITQATKRSHNLGKTLEQLTKEK
The following text describes a protein:
Function:
Catalyzes the conversion of xanthine monophosphate (XMP) to GMP in the presence of glutamine and ATP through an adenyl-XMP intermediate.
Sequence:
MDPKNVKSDLVLILDYGSQYTHLITRRIRSLSVFSLCISGTSSLSTIADLNPSVVILSGGPHSVHTPDSPSFPDGFLQWAQSNGVTVLGICYGLQLLVQRLGGDVRVGDKQEYGRMEICADKPSALFGPEKVGKRQVVWMSHGDEAVALPDGFHVVARSDQGAVAAIENPPAKLYGLQYHPEVTHTEDGMETLRRFLFDVCGVGAGWKMEDVMEEEIKVIKETVGPDEHVICALSGGVDSTVAATLVHKAIGDRLHCVFVDNGLLRYKERERVMETFEKDLHLPVVCVDAVNQFLTKLKGVVDPETKRKIIGKEFICIFDAFAQELEGKLGKKPSYLVQGTLYPDVIESCPPPGTGRTHSHTIKSHHNVGGLPKDMKLKLIEPLKLLFKDEVRQLGRILDVPVAFLRRHPFPGPGLAVRVLGDVTEGNALDILRQVDEIFIQSIKDAGLYDSIWQAFAVFLPVRSVGVQGDQRTHSHVVALRAVTSQDGMTADWYYFEHKFLDDVSRKICNGVRGVNRVVQDITSKPPSTIEWE
The following text describes a protein:
Function:
Component of a complex that catalyzes the oxidation of glycolate to glyoxylate.
Sequence:
MATVISKTVFDDVETLKKELIRCMKCGNCMSACPIYNVEKKESSVARGKIALGEAVLSDEINIDDETLVKLIFNCLVCKSCMLACPSGVRYDRIILGLRAAIAKKKGIPFVKKALFGLLKNPELFDKGMKAFATMQGLFLREEGEKIRTPKRFLKGISPRFDEQFILPELSRESFRDRVNETVEAKSSQATVIFFTGCSVNYLYPEVGDDLLYVLNKNNVSVITPKKQNCCGMPVMVHGDIDTARELARKNIDIFEQTNAQYIVTVCGSCGSALKHEYPLILEGTEHVEKAKKWAERVYDISTFLLKVINLEPPKGKVELKVTYHDSCHLKKSMKVFNEPRQLLKMIPGLTLIEMKKPDACCGSGGSYHLTHADTSIKIAKAKAEDIKATGADTVCTGCPACMMEIFESMHRFDGQCNVTHTVSLLAQSYKAEEKENV
The following text describes a protein:
Function:
Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity).
Sequence:
MEILDKQAFFETREKLYTLSRSLNIIKQRIQIAENDRKKCLITINELESLSSETKTYKAVGKMFVISPMTSLKTELKQQVQKDEEDVKGLINQSKYIDAQITDTERSLNELVRKK