lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
As accessory component of the DNA polymerase epsilon (DNA polymerase II) participates in chromosomal DNA replication.
Miscellaneous:
MISCELLANEOUS: In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.
Subcellular Localization:
Nucleus.
Sequence:
MPPKGHKKTADGDFRPVNSAGNTIQAKQKYSIDDLLYPKSTIKNLAKETLPDDAIISKDALTAIQRAATLFVSYMASHGNASAEAGGRKKITPQDVFVALKDVDLAQFVPSVTQSVNEFEQEVAQRKKDKVVRAQDDQDHISSSESETEATEEEGNKRIRTDE
The following text describes a protein:
Function:
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Subcellular Localization:
Membrane; Single-pass membrane protein. Plastid, chloroplast thylakoid membrane; Single-pass membrane protein.
Sequence:
MLNIFNLICICFNSALFSSSFLFAKLPEAYAFLNPIVDFMPVIPVLFFLLAFVWQAAVSFR
The following text describes a protein:
Function:
Catalyzes the stereoinversion of LL-2,6-diaminopimelate (L,L-DAP) to meso-diaminopimelate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Subcellular Localization:
Cytoplasm.
Sequence:
MTTKIKFTKMHGAGNDYIYVDTTRYPIAAPEKKAIEWSKFHTGIGSDGLILIGSSDKADFSMRIFNADGSEAMMCGNGSRCVGKYVYEYGLTAKKEITLDTRSGIKVLKLHVEGGKVTAVTVDMGSPLETEAVDFGDQFPFQSTRVSMGNPHLVTFVEDITQINLPEIGPQLENYHLFPDRTNVEFAQIVGKDTIRMRVWERGSGITQACGTGACATAVAAVLHGLAGRKCDIIMDGGTVTIEWEEATGHILMTGPATKVFDGEMEG
The following text describes a protein:
Function:
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the polyenes aspernidgulenes. The carbon backbone of aspernidgulenes is synthesized by the HR-PKS sdgA, which accepts acetyl-CoA as the starter unit and performs malonyl-CoA extensions as well as regioselective methylation and reduction. The resulting nonaketide offloads the HR-PKS by intramolecular lactonization to yield the 5,6-dihydro-alpha-pyrone-containing hexaenoic acids preaspernidgulene A1 and A2. The FAD-dependent monooxygenase sdgC then installs the first epoxide on the penultimate double bond. Subsequently, the FAD-dependent monooxygenase sdgF presumably generates a ketone intermediate through Meinwald rearrangement involving a hydride shift. Next, sdgC introduces another epoxide on the last olefin of the ketone intermediate after E/Z isomerization. The epoxide hydrolase sdgD then catalyzes stereospecific cyclization of the 5,6-dihydro-alpha-pyrone and opening of the epoxide ring to form an oxygenated trimethylcyclopentanone and an oxabicyclo[2.2.1]heptane unit. Finally, the bicyclic unit undergoes hydrolytic cleavage, either spontaneously or catalyzed by sdgD, to assemble the dimethyl-gamma-lactone moiety in aspernidgulene A1.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MDKRSFKVIVVGGSIAGLTLAHSLDLAGIDYIVLEKHSDPLATVGGSVGLLPNGWRILHQLGLRHQLEQEACPVKVAHMTYPDGFVFSDNFPAAIQERQVPEIQFPIGYMPANDERFGYSLSVLTRQQLIEVLYLGLRDKSKIKVGQRVIKIQHHQNRRGVSVFTESGQEHVGDLVAGADGVHSITRSQMWLQLGQKLDAEKERRQLVAEYSCVFGISSPLKGIPPGEQLIACHDNATVLAFPGKDAHIGWGLIQKLNRPCNSPATTQSSDGETALIMAKSAAGLGLCKDLKFHDLWVNTPKYSFTILEEGLFQIWHHGRIMTPNMAQGANTAIEGAAALANTLRRISQIDKPSEDDINRLLQGYTVRQQKRLRAVHAISRSVTRVHARQGRIKKIIGRYVYPYTPGAALHTFSRIIAPAPCLDYVPMPFPGPGWTRALVSGWSPISGVLLLVIPIIALVYGYSVINFGRDSINN
The following text describes a protein:
Function:
Protein mannosyltransferase (PMT) involved in hyphal morphogenesis and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the protein-O-glycosylation activity, while PMT5 and PMT6 may specifically modulate a much narrower spectrum of target proteins. Required for biofilm formation and virulence.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MATGYSTGVSPFDLDENNHNDSIHHRHQNHHSQSHDSSGERDDTEIEDIIQKTSKLNINTSTSTKIKNFFFQSSNRHDSSNSPPLREVFIKTINPLILTAISSFVRLYRIDVANSVVWDEAHFGKFGSQYLKRQFYFDVHPPLGKLLIGLSGYLADYDGNFDFESSNVYPDNVNYVFMRIFNCFFGILVTPLAYKTAVILGYNQFTCWLIAFMVIFEQLSLTLSKFILLDSMLLFFTVLTMYCLVKVHTLAIARVGSNSKTPLTKLEIKWYILTGISIGCVCSVKWVGLFVTALVGFYTIVDLWIKFYQTFAIDKKSPKKMSVVNYLIHWVVRIFTLIIIPMTIYVATFKVHFMVLNHTGPDDGTLSTLLQGSLIGNDLQSGPRSVAFGSLVTIRSQGLSPNLIHSHPHNYPQGSQEQQVTTYGFKDDNNEFLFEFGVDAGLRNQHATLENENSTRNGGNDDDYYHVIIHDGDTVRINHKNTGSYLRANAVGAPITSSSYEVSCFGDVESNDWADEWVIEIQSQDQSPDPMFQDEDPSEIHSVSTSFRLKHKQLGCYLATTGKSYPAWGYQQGEVVCKYSVFSRDKNTWWNIEKHVNNKLPLPATEYVPPKPKFWKEFILLNYAMMASNNALIPDPDRFDKLSSEWWEWPILNTGLRMNSWGDADIKYFLLGNPLITWISTIALIVCPLYLLVVGIKYQRQWILLSATDTSNANPANSQSLSLLAARALLPLAGWVLHYVPFILMGRVKYLHHYVPALYFAIFVAGFIVDAILNLDFSYHNNKFQYIFKVVIYSTLYLVICISFWYFKDLSFGMEGSSVDYRHLRLLGSWMI
The following text describes a protein:
Function:
Catalytic 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 PAB1. 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. May also be involved in post-transcriptional maturation of mRNA poly(A) tails.
Subcellular Localization:
Cytoplasm.
Domain:
Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex; The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with PAN3.
Sequence:
MANTHGLLPRLQGQVTSFLNIGDASPRYTSFPAHHGVPASQLLIHDSGVISLSSKNVRFTSRCGIQRWNKLMSDARCMSFTNTSSQLHVVGSPTTLSVVNMYRGTIVNEISLDEPIVAMKQGKFMAHATESGRVQFLDPRTMEIEHTILAHAGGILSMDIIGNTMATCGYSIRNGALLPDRLIKLYDIRTMRALSPIPFSVGPEHVRFHPKQPSRLLILSKTGAVQICDITSPNYTGVTFIRADMPGMISSMDISSNSDAFAVGDTTNSCAVFSTHETIRYNPYSRQSEYRSMFVDKSTVEIGDDTPLSAVGMPRYTSELLSAWPNSLLINVGRPQPRIPPEVLKNVKMSDFVGYVQDMPLKRNQNLIMSIRASTPTCASPGLSGPKFRSQQQRDRLHRKFKTEGHSAKSSLKSPETNDPSLQESEISEYHWHKIEIKYSKFGVEDFDFEYYNHTVYGGLETHIQNSYCNPLLQILFFNRPLCELVKSHIRTACMKDLCLACELGFLFRMLEDSKGANCQASNFLRAFGATPEACALGLVDAEVSHTDPQSVLTLQYDKLIQTTMRFLLEQLHQELGAKSTKHSQAIDYPPDEYIKTIYGIPLWTLIKCHGNHDHNRDSVPFVIDLHYDHKNLPANFLELLHASINKESSTRAWCDKCQKYQNIKQSRKLTKLPNFLNLNANITNDLESELWRRDTQDGSSCFLLKSFVLRRDADGYLIVDQSGVDVDVDLNSSDVAIYDLKTVVSAIQFENEPTHLVACINVSDDYDAPKWYLFNDFLVQEIFNGEECRFEDWKMPAIIQYIRRTHPDKNEFFLSPVEPDFSILIKHQNINKQKDVCFNYELLTELEIPCISEYICAIDAEFVVMTEAEMEIKSDGSKSIIRPAESGLARVSVIRGIEPRMGVPFIDDYIFISQPVVNYLTEFSGIIASDLDVRTSKLPIVSLKIAYKKLRLLVDIGCIFVGHGLKKDCRTINILIPPHQIIDTVDIYYLKQYSRKLSLRFLVWFFFKEDIHSSSHDSVEDARGALRIYQKYLEAKEQARFDTLLEEIYQEGRKFNFRPPNALTGIANTTQYDMHARTQSSDL
The following text describes a protein:
Function:
May contribute to the regulation of cell proliferation.
Subcellular Localization:
Cytoplasm. Mitochondrion. Nucleus.
Sequence:
IVQCKSNGNRAMWVKVPVDKSYLIPVVFKHGFTYHHAEGNHAMLLKWLPDNVECKVPPYASHQIGVAGIVVNEEENKVLVVQDRQKKPIWKFPGGLSDEGEDIGHTAEREVFEETGIKSEFQSIVLFRQQHKMRSAFNKSDIFVVCRMKPLTSDIILCDDEIAACQWMPINELLVHSDTTPLIKLGAKLVMYGMKYGHEHFDVTATKMRSWVDPTQTFKLYHKPL
The following text describes a protein:
Function:
Methylates ribosomal protein L11.
Subcellular Localization:
Cytoplasm.
Sequence:
MYPAITPLQAGLQWWAVAGRQGVAELWQVQVETAADGADGEVEETLYWYLSELGLPHVERQILAGRLVLRGYLSGETPEGVMERWREHIRERLTQKAEIGWYAVERRDWQAAWREQWRPIFVGERLVIWPVWLPDPPGDRLVIPLDPGMAFGTGEHATTRLCLRALESVPDLGTFADVGCGSGVLTVAALKLGAGRGWAVDTDDLAVVSTRKNLEISGLEERVTVARGSTEQLSGPLDGVVSNILAEVIANLAPEFRRLVHPGGWGIFSGLLLTQAPRVVEALAGQGFALSETLSEGDWACLVGRFSADRPRSAGS
The following text describes a protein:
Function:
May be involved in cell wall organization and biogenesis.
Miscellaneous:
MISCELLANEOUS: Present with 1890 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion membrane; Single-pass membrane protein.
Sequence:
MDWLKNTTIVVLFSHSTDKSNKHKKRQVQCNMRKNTLDMVTIGIACLVGVYTGTRFFEPIVIDRLRKDGNLRTDIPIPEYDEDGNLLKVTPSLSSTPAAPPTPPTPPTPPQQ
The following text describes a protein:
Function:
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Subcellular Localization:
Cytoplasm.
Sequence:
MKARFDKIYKDIVDTIAEKGIWSEGNVRTKYADGTAAHYKSYIGYQFRLDNSDDEAHLITSRFAPSKAPIRELYWIWILQSNNVDVLNELGCKFWDEWKMQDGTIGKAYGYQIAQETFGQKSQLHYVINELKKNPNSRRIMTEIWIPNELSEMALTPCVHLTQWSVIGNKLYLEVRQRSCDVALGLVANVFQYSVLHKLVALECGLEPAEIIWNIHNMHIYDRHYDKLIEQVNRETFEPAKIKINNFKSIFDFKPDDIEIIDYKYGEKVSYEVAI
The following text describes a protein:
Function:
During host cell infection, required for actin-based intracellular motility. Mediates actin tail formation at one pole of the bacteria surface by recruiting host Arp2/3 (ACTR3/ARP3-ACTR2/ARP2) which leads to actin polymerization which provides the propulsive force for intracellular movement and intercellular dissemination of the bacterium.
Subcellular Localization:
Cell outer membrane. Cell surface. Note=Prior to its translocation into the periplasm, targeted to one pole of the bacterium inner membrane in a BimC-dependent manner. Translocates into the periplasm in a secYGA-dependent manner.
Domain:
The central and acidic (CA) domains are required for binding to the host Arp2/3 complex, Arp2/3-dependent actin polymerization and thus for actin-based motility; The transmembrane domain is required for polar localization at the bacterium inner membrane; The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space. Then, insertion of the trimerized C-terminal translocator domain in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface. The passenger domain is probably exported as a hairpin structure, with all 3 strands of the trimer in the pore simultaneously.
Sequence:
MKYRRLSLAHARQDSGQAASNARSRRFARLLCSSIAPLALGFSADAFAADETMASPFNRGAPNDAHGNLLDEIRRGVPLRHVPASERNTRGAGGSTLADAMRRVIDSRRTAFDSPPATPASPSPSWSDDESPPPTPIATRPASRPESAARSPRHSSPPHSPPASAESPSPRSPDASPSRTPSPTFSFPSPSRTSTPRTQPPSPLRERPERSPAASPRVASPRSAHSRGSTQPPSNLSTPRYEPPTPLQEDPERTPVASPRVASPRSAHSRGSTQPPSNLSTPRYEPPTPLQEDPERTPVASPHVTPAEHAQRRPFLLQKPPQVPSWRKKAPSATLPDSHAPARPGGGQFTTPASGAAKYVAVNSGASDAFAAGVNAVAIGADARAQGQESLATGWRAQADGHRAVATGARAIASGRDAVALGAGSIADRDNTVSVGQRGSERQIVHVAPGAQGTDAVNVDQLNLAISNSNAYTNQRIGDLQQSITETARDAYSGVAAATALTMIPDVDRDKMLSIGVGGAVYKGHRAVALGGTARIGENLKVRAGVAMSAGGNTVGVGMSWQW
The following text describes a protein:
Function:
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Sequence:
MFLIWRLYKTLFLILYIIILQEYVCHSSNHIKSVNRCFIPFISEYIYKQKNRKNNISYDSSNSHYNDKIIPCGNYNKQLKYKINFCRNLYFNNKNEYNRICSRNKLNFHNIQTDNTIYKPKKKYYEVGKVREKIKMYTLFKDDKINTLKCNEEESVTSETINKHDSSVKVKGRRKKNITSNENIMNPNNKSVSSINTNLSDSSNNKNDNSLNSKKNDNTLNSKKNDNTLNSKKNDNTLNSKNNNNSLNSKNNNNSLNSKKSNNSYNDKHIDHIIPEGKNKINNNIDVKHNINNKLNEINEEPYEDTHNKEENSSNKNDNDEKRKEENNNITRRYIKNDQMSYNNINTNSNEYDKNASTLDETYIGKTFEGYVYSVNKNAACIKLKNINKYGLLFKNKANLGDDIEDMNDFFEKDQPVHVKILGINTKKNIFYLGNIIKYNENIKLSKGEYSKGLITKVCDSYCFIKVLKNGSTGYLHKSKLFCMNDKEKKNNDNQNYDNPNNDNPNYDNQNYDNQNYNNPNYDHPNYDNQNYDNQNYNNPNNDYSTSQLYNSDNLQMDFIYKLQFTKIFNIWDIIDVEILGTPQNDYKSNYILTIPRGSKTFKKILNYLNVLKENEDINNIQYKGDYIYSIDNNKNDNIIDSDINNHHINNKKKKKNLYDIQNNMNHSPFNKFHTEDEYLFNDHVQENVHTFYEKNKKYKITYDKENNHKMNKSYYLKKNKELPFNNKFKKIIKNIYDLPNTISLSMLSKTIKIPLASIKKYFIIHENKEYNSSYKINSEQIKRICQHFKIDCNVEQRDDNVVTKVNGTTKDCQEKVFKNVTQDRLKEGEQERVIKVEAKIKNDEMVMQEQKDTKEEKHMDVQFIEEKDINVQHINVQDMDVQDMDVQDINVQDMDVQNINVQDINIQDMDVQNINNSITLNKSTSCQTDESRDAPGGDQNESLDEKDSMEKSKEKKKKKGKSRKKNKDTNLTLKSDSIQKSKTTLDDKKRNVVVTFIGHINHGKTSLFDYICKTNEQKKEYGLITQNIRAFKATVRNNFTFTLVDTPGHEAFMPMRSRGVKISDLSILVISGDEGIQEQTVECIKLIKEFNIKIIIAITKVDIPNVDVDRIINDLLYHDITTELNGGEIQVVECSIYKEESIDKLLDAIYLESEFLNLQTNPDKKHEQAQGVVLDSYIDKNGIVSINLLQNGVLNINDHFYTGSSYGKVKILKDHLNKNIKSAYPSDPIKIIGYNKNSVPVAGDKFYVVENEALAKEIAEHNKNKMLTMEINNFTYDQTNMNRYKDFIISRENKIGGSSGILGENNLKNDIDGNMTRDDNMTRDDNMTSDDNMTRDGNRTNNDNITSDDNMSNDYDKIKETKMYTNNKSFQKDDFLKIHLNNTNENVINMDPSTHIGKNEIKTIYSNYIIKCDKQGSIEVLKNCMLKLQKEDSICKIKNKIIYADIGNVTSSDIKYATSFNATIIAFGVKLSNDIKGSKNSKGSKNHNNYPIIYSNVLYELIENVEKEMEKKLSKKPMGELKGTAQILKVFNISKLGKVAGCIVKKGTISINSNIRILRNDKVIYMGKIISIKIVKEEKTQVTEADECGIGFDNFLDFEPNDIIEAYEN
The following text describes a protein:
Function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
Subcellular Localization:
Mitochondrion.
Sequence:
MSAAQLLRHSRKLRSLRNSVDCERTSLARYFSTGSGSSAVKENGVEKRIGGARFSQYKQPGKELETFKVSLGGANGSSTCRRMLINRVPSAVTGLNGSLSCGRVASARSFSSSADLPPHQEIGMPSLSPTMTEGNIAKWIKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVQGDGAKEIKVGEVICVTVEEEGDIEKFKDYKPSAADAPAAPSESKATPEPAAPKVEEKVPAKAPEPKAPKAEKASRSGDRIFASPLARKLAEDNNVQLSSVKGTGPDGRILKADIEDYLAKGGKSEAFAASGLDYTDIPNAQIRKVTANRLLASKQTIPHYYLTVDTRVDKLIKLRGELNPLQEASGGKKISINDLVIKAAALALRKVPECNSSWMNDFIRQYHNVNINVAVQTEHGLFVPVVRDADKKGLGTIGEEVKQLAQRARDNSLKPQDYEGGTFTVSNLGGPFGIKQFCAIINPPQSAILAIGSAEKRVIPGSADGQYEFGSYMSVTMSCDHRVIDGAIGAEFLKAFKGYIENPTTMLL
The following text describes a protein:
Function:
Catalyzes the decarboxylation of free fatty acids to n-alkanes or n-alkenes in response to blue light. Substrate preference is toward fatty acids with C17 or C18 chains. Saturated fatty acids are converted to alkanes, not alkenes. The decarboxylation is initiated through electron abstraction from the fatty acid by the photo-excited FAD (By similarity).
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MMLGPKTVTRGATKGAAPRSMAARRVGGARRLSVRAAAGPAGSEKFDYVLVGGGTASCVLANKLSADGNKKVLVLEAGPTGDAMEVAVPAGITRLFAHPVMDWGMSSLTQKQLVAREIYLARGRMLGGSSGSNATLYHRGSAADYDAWGLEGWSSKDVLDWFVKAECYADGPKPYHGTGGSMNTEQPRYENVLHDEFFKAAAATGLPANPDFNDWSHPQDGFGEFQVSQKKGQRADTYRTYLKPAMARGNLKVVIGARATKVNIEKGSSGARTTGVEYAMQQFGDRFTAELAPGGEVLMCSGAVHTPHLLMLSGVGPAATLKEHGIDVVSDLSGVGQNLQDHPAAVLAARAKPEFEKLSVTSEVYDDKCNIKLGAVAQYLFQRRGPLATTGCDHGAFVRTSSSLSQPDLQMRFVPGCALDPDGVKSYIVFGELKKQGRAWPGGITLQLLAIRAKSKGSIGLKAADPFINPAININYFSDPADLATLVNAVKMARKIAAQEPLKKYLQEETFPGERASSDKDLEEYIRRTVHSGNALVGTAAMGASPAAGAVVSSADLKVFGVEGLRVVDASVLPRIPGGQTGAATVMVAERAAALLRGQATIAPSRQPVAV
The following text describes a protein:
Function:
Important for the biogenesis of filamentous eisosomes, large cytoplasmic protein assemblies that localize to specialized domains on the plasma membrane to cluster specific proteins at sites of membrane invaginations.
Subcellular Localization:
Cytoplasm, cell cortex. Cell tip. Note=Localizes to eisosomes.
Sequence:
MSHASKNYNAQLTAAAASTALHGTKKIYNSNENDRAVNSFLGNRTSYGEAVNGSPQYDYMRSRMSTLGSANQPMAPPSLRNRSSVYLPTPAGPPQIPVNTGKRYTLTSSSANYMTKSERQMRPPKSYDFPPSQQVRPSTSRSPSYASYNSEEVNFQSYQDPRLLPRTSQMYMPDNNYSPAVKSPAAQRRSSSYMVPANSRGSPANYNTPYYPTAIPPPIEEYSPSVSLPTSPVAEESYNNVQRSSTVRNNTTQKSVLKKPSRKMSPAYTSSYRQNSPSSQVPPVSKKHVIIYENKEGSSSSESVYEDVFEDFDPSGSNQASLRSTSTIHYTPSSKRISVIPPNTSNIGSRVVSRSGQNNNQPAQPGQYNQQSQPVQSYQSGQSTQHFQPVQPIQPVQSTQYYQPSSPVQPVQNGVPAPPMQPVQSTQYYQPSSPVQPVQNVKPAQPAQPSLEDAAKRRVEEMLRQMDITPTASSTTANNAYASAEPHPSAFPDDMNSVFSDSSFERERDSGRGRSTNLFSKFKSGRSRSKASGEAPYSYPAPPVPSVNNAGARLTLRDSGAAPEATYSLRQPSNHAYSEGRSYTFTGGQPPSVPTMPYGSRFANDSDSMMGSTADFSSKKKGGKFKAFKKFFKMRF
The following text describes a protein:
Function:
Binds to single-stranded sequences.
Subcellular Localization:
Nucleus.
Sequence:
MAYDAFGKPGYGPDFNSAFSPGMGGGAGFNEYDQSSQPSVDRQQGAGNKLRPVTIKQILNASQVHADAEFKIDGVEVGQVTFVGVLRNIHAQTTNTTYQIEDGTGMIEVRHWEHIDALSELATDTYVRVYGNIKIFSGKIYIASQYIRTIKDHNEVHFHFLEAIAVHLHFTQKANAVNGANAPGYGTSNALGYNNISSNGAANSLEQKLAEYSLTPAQMTVMQAIHSAPETNEGVHVRQLAQSVGPGIDLTAVTDFLQQEGIIYTTIDENHFKSVLQDQ
The following text describes a protein:
Function:
Sequence-specific transcription factor. Part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MSTFLDFSSISGGGDGGSGGSCSVRAFHGDHGLSTFQSSCAVRLNSCSGDERFMSNISSQDVINSQPQQAGSYQSPGTLSITYSAHPSYGTQSFCTGYNHYALNQDVESSVSFPQCGPLVYSGNISSTVVQHRHHRHGYSSGNVHLHGQFQYGSATYGNSSDQANLTFVAGCSNPLSPLHVPHHDACCSPLSDGVPTGQTFDWMKVKRNPPKTGKAGEYGFGGQPNTVRTNFSTKQLTELEKEFHFNKYLTRARRVEIAASLQLNETQVKIWFQNRRMKQKKREKEGLLPKSLSEQKDGLEKTEDASEKSPSAPSTPSPSPTVEAYSSN
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.
Subcellular Localization:
Cytoplasm.
Sequence:
MAITAQMVKELREKTGAGMMDCKKALTETNGDMEKAIDFLREKGIAKAAKKADRIAAEGLTFIETNGNDALILELNSETDFVAKNEGFQTLIKELAAHLLTNKPANVEEAMAQTMENGKKVEEHINEAIAKIGEKLTLRRFEIVSKTDADAFGAYLHMGGRIGVLTVLEGSTDEAAAKDVAMHIAAVNPKYIDRDAVTAEEVEHERQVLTQQALNEGKPEKIVAKMVEGRLGKFFEEICLLDQAFVKNPDMKVRQFVESKGGTLKGFVRYAVGEGIEKREDNFAEEVMNQVKGSN
The following text describes a protein:
Function:
Oxidizes L-gulono-1,4-lactone to L-xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate. Can use both cytochrome c and phenazine methosulfate as exogenous electron acceptors, but molecular oxygen does not serve as a substrate. Is very specific for the L-gulono-1,4-lactone substrate, since it cannot oxidize L-galactono-1,4-lactone, D-glucurono-3,6-lactone, D-glucuronate, D-arabinose, or D-xylose.
Sequence:
MSPIWSNWPGEQVCAPSAIVRPTSEAELADVIAQAAKRGERVRAVGSGHSFTDIACTDGVMIDMTGLQRVLDVDQPTGLVTVEGGAKLRALGPQLAQRRLGLENQGDVDPQSITGATATATHGTGVRFQNLSARIVSLRLVTAGGEVLSLSEGDDYLAARVSLGALGVISQVTLQTVPLFTLHRHDQRRSLAQTLERLDEFVDGNDHFEFFVFPYADKALTRTMHRSDEQPKPTPGWQRMVGENFENGGLSLICQTGRRFPSVAPRLNRLMTNMMSSSTVQDRAYKVFATQRKVRFTEMEYAIPRENGREALQRVIDLVRRRSLPIMFPIEVRFSAPDDSFLSTAYGRDTCYIAVHQYAGMEFESYFRAVEEIMDDYAGRPHWGKRHYQTAATLRERYPQWDRFAAVRDRLDPDRVFLNDYTRRVLGP
The following text describes a protein:
Function:
Transcription factor that establishes leaf shape by repressing growth in specific subdomains of the leaf. Negatively regulates knox homeobox gene KNAT1/BP expression.
Subcellular Localization:
Nucleus.
Domain:
The SR/KY and BELL domains are responsive for the interaction between the TALE/BELL proteins and the TALE/KNOX proteins.
Sequence:
MGLATTTSSMSQDYHHHQGIFSFSNGFHRSSSTTHQEEVDESAVVSGAQIPVYETAGMLSEMFAYPGGGGGGSGGEILDQSTKQLLEQQNRHNNNNNSTLHMLLPNHHQGFAFTDENTMQPQQQQHFTWPSSSSDHHQNRDMIGTVHVEGGKGLSLSLSSSLAAAKAEEYRSIYCAAVDGTSSSSNASAHHHQFNQFKNLLLENSSSQHHHHQVVGHFGSSSSSPMAASSSIGGIYTLRNSKYTKPAQELLEEFCSVGRGHFKKNKLSRNNSNPNTTGGGGGGGSSSSAGTANDSPPLSPADRIEHQRRKVKLLSMLEEVDRRYNHYCEQMQMVVNSFDQVMGYGAAVPYTTLAQKAMSRHFRCLKDAVAVQLKRSCELLGDKEAAGAASSGLTKGETPRLRLLEQSLRQQRAFHHMGMMEQEAWRPQRGLPERSVNILRAWLFEHFLNPYPSDADKHLLARQTGLSRNQVSNWFINARVRLWKPMVEEMYQQEAKEREEAEEENENQQQQRRQQQTNNNDTKPNNNENNFTVITAQTPTTMTSTHHENDSSFLSSVAAASHGGSDAFTVATCQQDVSDFHVDGDGVNVIRFGTKQTGDVSLTLGLRHSGNIPDKNTSFSVRDFGDF
The following text describes a protein:
Function:
Hypothalamic neuropeptide which binds to the G-protein-coupled galanin receptors (GALR1, GALR2 and GALR3). Involved in a large number of putative physiological functions in CNS homeostatic processes, including the regulation of gonadotropin-releasing hormone secretion.
Subcellular Localization:
Secreted.
Sequence:
MALTVPLIVLAVLLSLMESPASAPVHRGRGGWTLNSAGYLLGPVLHPPSRAEGGGKGKTALGILDLWKAIDGLPYPQSQLASKRSGETFAKPDSGVTFVGVPDVVPWKRIRPGTTRFQVRSLALLSGLRIQCCCELWCRLQMWLGSHIAVAVV
The following text describes a protein:
Function:
Water channel required to facilitate the transport of water across membranes. Involved in freeze tolerance, osmotolerance and cell flocculation in liquid cultures (By similarity). Is non-functional in most laboratory strains.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell 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 (NPA).
Sequence:
MSNESNDLEKNISHLDPTGVDNAYIPPEQPETKHSRFNIDRDTLRNHFIAAVGEFCGTFMFLWCAYVICNVANHDVALTTEPEGSHPGQLIMIALGFGFSVMFSIWCFWWGFEPSRFSLFVFGQSHLTSQMCSDVVSSDHCWDGCWWCR
The following text describes a protein:
Function:
Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis.
Miscellaneous:
MISCELLANEOUS: Present with 2800 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MAVLCGVCGIKEFKYKCPRCLVQTCSLECSKKHKTRDNCSGQTHDPKEYISSEALKQADDDKHERNAYVQRDYNYLTQLKRMVHVQKMDARMKNKRVLGPVGGHNSNFKKRRYDIDEDDRDSTECQRIIRRGVNCLMLPKGMQRSSQNRSKWDKTMDLFVWSVEWILCPMQEKGEKKELFKHVSHRIKETDFLVQGMGKNVFQKCCEFYRLAGTSSCIEGEDGSETKEERTQILQKSGLKFYTKTFPYNTTHIMDSKKLVELAIHEKCIGELLKNTTVIEFPTIFVAMTEADLPEGYEVLHQEPRPLEHTSTLNKFIDNAREEEDAEEDSQPTEEPVQKETQDASDSDSDSDDDYNPGLSMDFLTA
The following text describes a protein:
Function:
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MINLIITLIINTALSTIIVLIAFWLPQLYLYLEKSSPYECGFDPLGSARLPFSMKFFLIAITFLLFDLEIALLLPLPWAMQLPTPNLTLILAYCLIILLTAGLAYEWIQKGLEWSE
The following text describes a protein:
Function:
Zinc metalloprotease that mediates intramembrane proteolysis of proteins such as ATF6, ATF6B, SREBF1/SREBP1 and SREBF2/SREBP2. Catalyzes the second step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2: cleaves SREBPs within the first transmembrane segment, thereby releasing the N-terminal segment with a portion of the transmembrane segment attached. Mature N-terminal SREBP fragments shuttle to the nucleus and activate gene transcription. Also mediates the second step in the proteolytic activation of the cyclic AMP-dependent transcription factor ATF-6 (ATF6 and ATF6B). Involved in intramembrane proteolysis during bone formation. In astrocytes and osteoblasts, upon DNA damage and ER stress, mediates the second step of the regulated intramembrane proteolytic activation of the transcription factor CREB3L1, leading to the inhibition of cell-cycle progression.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein.
Sequence:
MDVTTVFGSVILLHTFFYYLDRYLKGKNSQRYASFLNRFPVQIDFMNVRWTTSMFNKALSSWAMMRLRFLSKWYNIGTVITLLLCIPSLILLGSTALVSFENMMDSKKEEAMLQPVVPGVNLPSYDLPYYLITLLVCTVVHEAGHAIAAVSDQVPLVSVGLILWLIIPAAFVELPTSNVVGLSPWKQLKIYCAGVWHNIVLSAMAFAVLMMLPILLIPLFQSGAGVSVVNLNAYSTDGHHDFQVGDQLTQINDCRVTGVESWRLCLTAVLLESSGFCLDNSYLASSSSSDQLGCCNDSEFSRSHLCFLSSPDLVPKKYHCLRAREVSQLSSAWCSNHKGCSAVNQSCLMPSFHSESVNETDSSRLIIVKRKSADPVLFAGLPNEIYLSVYVSDYVPRIFIGSQFINFIEHLLKYISSFSAGLAVLNVVPCIFMDGHHIVGALSEIVFEGRGSISMKRQTQYALVFLGTSLVVINIAFGVLTLFL