lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Transcriptional regulator that functions in sexual development; disruption of asd-4 gene results in agenesis of ascus and ascospore with macroscopically normal fruiting body formation. The GATA-type zinc finger domain binds to DNA sequences from its own promoter region.
Subcellular Localization:
Nucleus.
Sequence:
MATMANHDRETTQPTCQNCATSTTPLWRRDEMGQVLCNACGLFLKLHGRPRPISLKTDVIKSRNRVKTMRPDLAKQKKQQQQQQQQQNLAATADMNGGVGMMDPNNPAAAARRASQKSINGHPVDDNSPVSRTGTPNVYNPHIPIDHSLEYQFQAQQIPGFGVPTASPGRAPSPMNGEHMPQTHEQLLAANASLKTRVSELEVIQELYRGRLHQLETEENIRQASEPGKLEAQLRAQIDAMGEAHQQLQKELEESHRRENMLKRRLDELEVELKDVKDALESQDNGRHKKIRLDENVKTEPYAEVVEPQQPEQQQPAPAEQPIPTPMAIDEATPAPAPAPEAAPEQAPAPAPEPVQEQAQEPEPAPVSEPTEASAPAPAPEADSVVPEPTPAAPESAPTEEPAAPETEASEPPTTAPVEEAPKAES
The following text describes a protein:
Function:
Magnesium transporter that mediates the influx of magnesium into the mitochondrial matrix and regulates magnesium metabolism. Also permeable to calcium, sodium and potassium ions. Required for normal expression of the mitochondrial respiratory complex I subunits. May play a role in maintaining the inner mitochondrial membrane potential.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
KITDASQTALASVVPVFAVVKFDKEGNVTSFERKKTELYQELNLQARDLRFQHLTSISTRNNRIILRMEFLKAVITPECLLILDYRNVNLDHWLFRELAPQLAGDGQLVTYSLPFEFRAIEAILQHRVSTLQARLHEVQPQVFETLESLVNPKMLSVERSKLHVLLQNSKNLSELETDIKVFKESLLKILDEDELIEEMCLTKWTDPQVFEESSLGIDHAEEMELLLENYYRQAEDLANKARELKVLIDDSESVIFINLDSHRNIMMRLNLQLTMGTFSLSLFGLVGVAFGMNLESSFEEDPRVFWLVTGIMFLGSGLIWRRLLSFLGRHLEAPSPPPIPPVLKRSYLNSLRGVDLKSGLRQETFAPSRNPLMNQK
The following text describes a protein:
Function:
Exhibits ATP hydrolysis without substrate. Can phosphorylate D-ribulose with low efficiency.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MLILRQFQISSFELFQSPKQTGFYSSSRSVPLPRTRFYSDFRVMSGNKGTNYEKLYLGMDFGTSGGRFTVIDEQGEIKAQGKREYPPFMKEESMGWASSWKATLFSLLEDIPVTVRSLVSSISLDGTSATTLILNSESGEVLCQPYLYNQSCPDALPEVKSIAPANHTVCSGTSTLCKLVSWWNTEVPNRESAVLLHQADWLLWLLHGRLGVSDYNNALKVGYDPESESYPSWLLGQPYSQLLPKVQAPGTSIGNLKESFTRQFGFPDDCIVCTGTTDSIAAFLAARATEPGKAVTSLGSTLAIKLLSTKRVDDARYGVYSHRLDDKWLVGGASNTGGAILRQLFSDEQLERLSQEINPMVGSPLDYYPLQSSGERFPIADPNLAPRLLPRPESDVEFLHGILESIARIEGKGYKLLKELGATEAEEVLTAGGGAKNDKWIKIRQRVLGLPVKKAVHTEASYGASLLALKGAKQNSGL
The following text describes a protein:
Function:
Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MAEVAAGVGRFKSNYAVERKIEPFYKGGKVQLDQTGQHLFCVCGTRVNILDVASGAVLRSLEQEDQEDITAFDLSPDDKVLVTASRALLLAQWAWQEGSVTRLWKAIHTAPVATMAFDPTSTLLATGGCDGAVRVWDVVRCYGTHHFRGSPGVVHLVAFHPDPARLLLFSSAADTSIRVWSLQERSCLAVLTAHYSAVTSLTFSADGHTMLSSGRDKICVIWDLRSLQATRTVPVFESVEAAVLLPEEPAPELGVKSAGLHFLTAGDQGALRVWEAASGRCVHAQQRLRGPGRELTHCTLAHAAGLLLSVTADHNLLLYDARSLRLRKQFAGYSEEVLDVRFLGPEDSHVVVASNSPCLKVFDLQTSACQILHGHTDIVLALDVFRKGRLFASCAKDQSIRVWRMNKSGEVACVAQGSGHTHSVGTICCSRLKETFLVTGSQDCTVKLWPLPEALLSKGTGHEGGPVFLQAQATQHCHDKDINSVAVAPNDKLLATGSQDRTAKLWALPRCQLLGTFSGHRRGLWCVQFSPMDQVLATASADGTIKLWALQDFSCLKTFEGHDASVLKVAFVSRGTQLLSSGSDGLLKLWTIKNNECVRTLDAHEDKVWGLHCSRLDDRALTGASDSRVVLWKDVTEAEQAEEQAKREEQVVKQQELDNLLHEKRYLRALGLAISLDRPHTVLTVIQAIRRDPESCEKLETTVLQLRRDQKEALLRFCVTWNTNSRHCHEAQAVLGVLLRHEAPDELLTYDGVRASLEGLLPYTERHFQRLSRMLQAATFLDFLWHNMKLPALPTAPAAL
The following text describes a protein:
Function:
Required for autophagy.
Subcellular Localization:
Cytoplasm.
Sequence:
MAANEEAVKYVWEGAIPLQIHLHKSEVASHPAPPPALVLAPRIGYLPLLVSLIKPYFKDSLPPGEDSIWFDYKGVPLKWYIPTGVLFDLLCAEPERPWNLTIHFRGYPSNVLIPCEGEDSAKWNFVNSLKEAAYIINGNCKNVMNMSQSDQEDLWTSVMNGDLDAYTRLLPKLKMGNIEDKFSRKADLSSPKSRQGGTEIDVTEQVVKTARIPVRLYVRSVNKDFENLEDVPEIDTWDEISYLNRPVEFLREKGKCYFTLRDAIESLLPEYSGDRAQTSGEEEADGSQETRGEIKLVRIQGIELKLDIPFSWVVNNLMNPEFYLHISVLVIGPQR
The following text describes a protein:
Function:
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Sequence:
MFSTIPNLEGAKAALLELIGRSFSVVSISIGSPPREERNITKSLKKHLALGGLSGNTQKTAFEIESEAYNSSSSRATYDDLCNPTEPNAEASSSETFSAPKSPGITIGPYNNCHHISSGAVSQVYRCDTEEGSYALKVITETHNMEPHSPTREIAILKRLSHPSIISLHTTLYDQESRLVLLLPYMPYTLSDLLSRSSKGLNVGTTKKIFKELLSGLAYLHAEQIIHRDISPSNILLPHDINGKDPIVITDFGTAWHPSISSSTEPTDQKCLEVGTTCYRGPETLFSNTSYTTSLDLWSTGVLLAECLRSPPIPLLESRRGDEDGNQLGLILSMFKTLGTPTEQTWPEAMKWKTNPFQWWNIFPSKSWEELLPDAEDDGRDLVASLVIYESGKRLTAVQALKHSFFLEKLESRD
The following text describes a protein:
Function:
Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
Sequence:
MGKLDVIQAKGTERLKRGFAKMVKGGVIMDVTNAEQARIAEEAGAVSVMALHRVPADIRKAGGVARMAPIEKIQEIMDAVTIPVMAKVRIGHVAEAKILEALGVDMIDESEVLTPSDPFFHIDKREFTVPFVCGARNLGEAVRRIWEGAAMIRTKGEAGTGNIVEAVRHVRLVAEGIRQIQAMTDDQVYAVAEKFAEPYLRLSLNVKEIAGLPQRVLDNEPIYGHYTYREIVDGLYKILLEIKKLGRLPVVNFAAGGVATPADAALMMQMGMDGVFVGSGIFKSSNPPKMAKAIVEAVNHWDEPDVLVEISKEIGEPMRGQDIEELEVRLEERGV
The following text describes a protein:
Function:
Component of a transport pathway that contributes to membrane integrity.
Subcellular Localization:
Cell outer membrane; Lipid-anchor; Periplasmic side.
Sequence:
MKKWLVTIAALWLAGCSSGEINKNYYQLPVVQSGTQSTASQGNRLLWVEQVTVPDYLAGNGVVYQTSDVKYVIANNNLWASPLDQQLRNTLVANLSTQLPGWVVASQPLGSAQDTLNVTVTEFNGRYDGKVIVSGEWLLNHQGQLIKRPFRLEGVQTQDGYDEMVKVLAGVWSQEAASIAQEIKRLP
The following text describes a protein:
Function:
Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence (By similarity).
Sequence:
MSKIADDQNFNDEEENFAKLFKKELEKEETLEKGTIKEGLVVSINENDGYAMVSVGGKTEGRLALNEITDEKGQLLYQKNDPIIVHVSEKGEHPSVSYKKAISQQKIQAKIEELGENYENAIIEGKIVGKNKGGYIVESQGVEYFLSRSHSSLKNDANHIGKRVKACIIRVDKENHSINISRKRFFEVNDKRQLEVSKELLEATEPVLGVVRQITPFGIFVEAKGIEGLVHYSEISHKGPVNPEKYYKEGDEVYVKAIAYDAEKRRLSLSIKATIEDPWEEIQDKLKPGYAIKVVVSNIEHYGVFVDIGNDIEGFLHVSEISWDKNVSHPNNYLSVGQEIDVKIIDIDPKNRRLRVSLKQLTNRPFDVFESKHQVGDVLEGKVATLTDFGAFLNLGGVDGLLHNHDAFWDKDKKCKDHYKIGDVIKVKILKINKKDKKISLSAKHLVTSPTEEFAQKHKTDSVIQGKVVSIKDFGVFINADGIDVLIKNEDLNPLKKDEIKIGQEITCVVVAIEKSNNKVRASVHRLERKKEKEELQAFNTSDDKMTLGDILKEKL
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MSGANSAANGASLEDCYTNLFAVADLSGIRWRHYSWIRPTEPVAPLEDPVLQSYAKCIKANILSVWRCHNTVRADLFAGSETQIQSKELWIYWYGDEPNFEDLIAPEIQDAVQAQGVWDNCMSYECRTLLFKSFHNSIERCLLSGGYVRLGRWFVKPFASYPIPGENLSDHHSVSFSFFLHGEKTVCSNVEVGLHQPVCRLTADHLAIAQGSATAVPVILSPYGLSGFLTGQAYKSTHQTAQRILYEWKLFYPIKQQQTSKGEHDRHHHHHHHHHHHHHNQHHPHHYHPGYRDEEEDNTVPAVVEVHVGSYLTDGYLTGGIRMLYPSCYVLVPQSEFSHHHAMAVQAGGYIPPPSMGLGHGKINGPATPGLSSVALTPPTSPPDQQLPPGDGSGALYTGGSTLDPSLGDDGDDSCTGALIHKVTSKVWSQWLTETAPPTPPSGGAGGGGTLPNGSMASTPGTITNTSGNTGTMSSQQSSLEPCSISTEDNNSSLETKPSLVPPPQPSPTANQITWQFHDPSSKTDCACSRRKWRDLKRQKVLKLKSRSKSPSSTGSTHSGHSGIGNPAFSGSVHRQQRSQRPSTPFHHRATHTDDLIGVDQELSSRLAPIGVATTPLSSVGPVSQESKPSNNALPKPSPAAFRTPGSTDPVLTESPPSVAPSPLIPPPTGSGLNPSERDRTMPTLSPYPPPRNGETGMPQASSGPVGSSMGRNCDMGHSMDHVGLIGDLKVERDLLTGRTIGHREPVKQEEDKVWQNFRLPSEHQMDSKRPLLPLLSYEKREENENMFDSLYDPANNDEIFCQPHKKLKEEKPVQPVASVLDFPAEMDVGLRHNRPPSPEKDPYEFMENETSPTQGGRMPISGRGRMKPNGRTRGGPRRPSIKKNKVKDDEVQRRAEEEKPRPETLTADGQSNVFNTDPSKAMGAAANKALPNKGETKRLMHTDDIKVTGVGDLERLFESSSSDDDDTGFDDMVSQVIHRGEESSTKPFGNSLHSSTGMPGSSQTGPDLARMYPTPPSLEQQNSAFSPVNQPCHDYINHGSVQGITQLEHSAGGDFNEIEADENMGSPKPEQIQDWSFVYKVPPTERFVGPSMYAPLKALPSSKQPPLKIPEMCHYRPSWQLPLSPKPDLLPVAKDSLVLEMEMNMNQPIVFNAPGPTLMQSPAAYPGSQEPRSAANMDLQSPASEASSYVRNINSIEAPTPASNIPEAHGLLVNLTLSDSLLNIYKDRNFDSSVMCVCNKNMCQCGFSAVMNRRYAVGSGLFAEDESEITGQPADAALWTFHKDNPMLAGMPDRKPLLSVEEPSSEKDGKEVSRTAKCVLRLIQEQCNSPYATLARLAGCVHKRGINSSGPLARSQIEINDGCDACFAALDLGRLLMDGTAGSKMDDTLKSSCLHSWPYSPAMARSTMSSQDVVRTLSSLQPLLQDAIQKKRTTRLWEKPYTVQGPLTWQVFFNIGARGPAETPEPLPIPRLMIGHDKDWLSSSPFALYYWEKLMLEPYSSARDVAYIALVPENKYILRCATMFFKELTAVYEGCRLGRHAPIAKTFQDGIMKIGKKYAQKLSNEPVDVWFTDVAHLPEADKLKLYAQFCRAYVAPFLNQEQPDASMFRTSRHHSSSSGASSGSNVPGSGSYPSSSSSSSYVVGSSNTSGSQGGAMHEQGSQGSDTSSASMPAPSSTPSRPANRQDSKDGSSASSSENKENLPKVTALETVTPRDSEQPPAVVVYIVDPFRRGEDAEEEGEVSVATLGLMHCFAEIFDKLQVSLQRNIAFQIIPLHQVLQVANSEVSSRFLNQLKSVAFSVFSQCRRFQSPTIPGRSLTGFGPAADLDRTIITKNAEHNEDRLYAPPFILAPIKDKQTELGESFGGLRQACGELFCSYCLSHDQRWLLVSCTDSKGELMETQIINVDVQNSKRRKKVSVRNIALYCLWDFLMGVISKASIPWRLVIGRLGRLGQGELKDWSMLLSRKNLAHYSRKLREQCSMCSVPGTLDFPCILSACLVSTEPEPGLSIMADMVAADKCSKNSQRDQPSCQLHTPDDASCTHIMVFPTSATKQAAATNMPQDQADLTFNSELRLDDEDPFLVDDLLLNIFMNTSNMMPDPSNIQLSDLDQEPIPTDGGPAPAAQGPGNPTTRQQPNQEPGIPAEPEDVLRGILQQPLALGYFISTAKTGPLPKWFWSACPEAENSCPVFLKAALHVHNPSEQPDDILQTKHSHPLDSDRTPEVLRYVLETYNSLSWLTVDPSSGDRRSCLPVHMVVLVQLYNTIASLQ
The following text describes a protein:
Function:
Cysteine protease that may play a role in regulating cell morphology in response to stressful conditions which likely cause oxidative damage. Appears to catalyze its own cleavage, which probably leads to its activation.
Sequence:
MAIINKDKATELILKQGFSGSYQSEQVTFLLKRTHIEPTDTAEKERLIQSGEKHYSQMISLENAPTARHLELFEQAMQQGQQRLAQEVQQLAQTLVVEFNEPIVLVSFVRAGVPLGVLLYHAIQDLGRDCVHYGISIIRDRGIDFAALETIIARHGHASIVFVDGWTGKGAIRQELQRSLGNDTRFIGKPLPLVVLSDIAGCAWLAASGDDWLIPSGILGSTISGLISRSICEGETLSADEITAENIDQWHRCIEYHHLKEFDISQQFIQRINQIRLKLNPQSNAVWAETQQQAQQDQSQQVVHKLAQEYDIQNINRIKPSIAEATRAILRRVPDLVLLRDADDEDTRLLRHLTQITKTPVQVVGDQIAPYRAITLIQKLGKG
The following text describes a protein:
Function:
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins.
Subcellular Localization:
Nucleus.
Sequence:
MSNTQSQDTKQQEASQQPQQQKPTVLEEDDEFEDFPVDDWPENETEQATANGNNVHLWEESWDDDDAAEDFSKQLKEELKKVDASSS
The following text describes a protein:
Function:
Within the ovary, required for the organization of somatic cells and oocytes into discrete follicular structures.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MEWGSESAAVRRHRVGGERRDGPGATPQPEREAPAQDSLADSCGGGARTRKRSGAGSALSEAPAALGLALYLLALRTLVQLSLQQLVLRGAPGHRGEFDAGQARDYLEHITAIGPRTTGSPENEILTVHYLLEQIKLIEVQSSSLHKISVDVQRPTGSFSIDFLGGFTSYYDNITNVVVKLEPRDGAQHAVLANCHFDSVANSPGASDDAVSCSVMLEVLRVLSTSSEALHHAVIFLFNGAEENVLQASHGFITQHPWASLIRAFINLEAAGVGGKELVFQTGPENPWLVQAYVSAAKHPFASVVAQEVFQSGIIPSDTDFRIYRDFGNIPGIDLAFIENGYIYHTKYDTADRILTDSIQRAGDNILAVLKYLATSDMLATSSKYRHGNMVFFDVFGLFVIAYPSRVGSIINYMVVMAVVLYLGKKFLQPKHKTANYTKDFFCGLGITLISWFTSLVTVLIIAVFISLIGQSLSWYNHFYVSVCLYGTAAVAKIIFIHTLAKRFYFVNASGQYLGEVFFDVSLFVHCGFLIALTYRGLCSAFISAVWVAFPLLTKLCVHKGFKQHGAQGKFIAFYLLGMFIPYLYALYLIWAVFEMFTPILGRSGSEIPPDVVLASILAGCTMILSSYFINFIYLAKSTKKTMLTLTLVCSVTFLLVCSGTFFPYSSNPASPKPKRVFLQSCSSQHVTRTFHDLDGNIVKRDSGIWINGFDYTGMSHITSHIPEINDTIRAHCEESAPLCGFPWYLPVHFLIRKNWYLPAADVSPRDPAHFRLVSKERTPWDSVKLTFEATGPSHMSFYVRTHKGSTLSQWSLGNGTPVTSKGGDYFVFYSHGLQASAWQFWIEVQVLEEQPEGMVTVAIAAHYLSGEDKRSSQLDALRDKFPDWTFPSAWVCTYDLFVF
The following text describes a protein:
Function:
Required to establish and maintain the arrest of oocytes at the second meiotic metaphase until fertilization. Acts by inhibiting the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase. Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. Plays a vital role in modulating the ubiquitilation of CCNB1 and CDK1 during gametogenesis.
Sequence:
MLASKNSRFTDETEILKMSERHSGEAGTGAGNEVDSPIVRVKSSSFGDLCSTSSFQDSGYSELLKSCSFDNTDKELFGKKERGSTLIHEYPETSSLALTYSLESPIQRKRFVFLRKENDKTPELCETPKVSRKKHLLRRRLDISFSLLDRDVESHSSSLESCTSQVPNLEKNIPSSASGFPRQGNFSSSVTSTLRTGEVTSSSQKLRLDFSQQKTSTVDDSKDDCGLFEVECISPIQGSNFKDSITHDFSDSSLCINNENTYPELLGSSVGGTSCRTDEDIFVTPISNLVPSVKFNASRRFSPSAGVRRNISTPEDSGFNSLCLDKSEDSLSEQEGSFQELLQKHKGTLKVRDTIKKSRRLGRLRRLSTLREQGSQSETEEENQTYLSSSESTPATTSDVSESQPSSDNKSEDLSFKNLSKTPALQLVHELFMKSRRKRFQQNGAHELLEERDGGKIAVLQRVLAGLIGKKMGIEKLDILTELKYRNLKHVLAMVLDSLTAESLCSVWKVSRNWREIIVQDKKANRRRKLHITQLKTNSECFSIQMPDSPSTRTGILLCGAILNVEDAATRLHLLNRSALRSVQAQARTPGFQKEQASTFSPWGEVLTPIASSSVTHLSSKQEEYVKVAKTLFIDEALKPCPRCQSPAKYQPYKKRGLCSRTACGFDFCVLCLCAYHGSEECSRGAAKPRNRKDVLPGSAQSKRNLKRL
The following text describes a protein:
Function:
Substrate-recognition component of the DCX(DCAF15) complex, a cullin-4-RING E3 ubiquitin-protein ligase complex that mediates ubiquitination and degradation of target proteins. The DCX(DCAF15) complex acts as a regulator of the natural killer (NK) cells effector functions, possibly by mediating ubiquitination and degradation of cohesin subunits SMC1A and SMC3. May play a role in the activation of antigen-presenting cells (APC) and their interaction with NK cells.
Sequence:
MAPSSKSERNSGAGSGGGGPGGAGGKRAAGRRREHVLKQLERVKISGQLSPRLFRKLPPRVCVSLKNIVDEDFLYAGHIFLGFSKCGRYVLSYTSSSGDDDFSFYIYHLYWWEFNVHSKLKLVRQVRLFQDEEIYSDLYLTVCEWPSDASKVIVFGFNTRSANGMLMNMMVMSDENHRDIYISTVAVPPPGRCAACRDASRAHPGDPSAQCLRHGFMLHTKYQVVYPFPTFQPAFQLKKDQVVLLNTSYSLVACAVSVHSAGDSSFCQILYDHTTYPPAPPSPPGPQSPELPPVLPSLCPEAAPAWPSGPPDPSPAIAKAKEFVADIFRRAKEAKGGTSEEVRPPPCPGPSGSRCRLPSEPLGPGGEAVPRDSPPAAEAPAPEPGYVNYTKLYYVLGSGEGTEPEDEFEDDKISLPFVVTDLRGRNLRPMREQAVVQGQYLTVEQLTLDFEYVINEVIRHDATWGHQFCSFSDYDIVILEVCPETNQVLINIGLLLLAFPSPTEEGQLRPKTYHTSLKVAWDLNTGIFVTVSVGDLTEVKGQTSGSVWSSYRKSCVDMVMKWLVPESSGRYVNRMTNEALHKGCSLKVLADSERYTWIVL
The following text describes a protein:
Function:
Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively. Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also functions as the substrate recognition module for the DCX (DDB2-CUL4-X-box) E3 ubiquitin-protein ligase complex DDB2-CUL4-ROC1 (also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1). The DDB2-CUL4-ROC1 complex may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. The DDB2-CUL4-ROC1 complex also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. The DDB2-CUL4-ROC1 complex also ubiquitinates KAT7/HBO1 in response to DNA damage, leading to its degradation: recognizes KAT7/HBO1 following phosphorylation by ATR.
Subcellular Localization:
Nucleus. Chromosome. Note=Accumulates at sites of DNA damage following UV irradiation.
Domain:
The DWD box is required for interaction with DDB1; Interblade loops of the WD repeat region mediate most of the interaction with DNA. A hairpin between blades 5 and 6 inserts into DNA minor groove and mediates recognition of lesions and separation of the damaged and undamaged strands (By similarity).
Sequence:
MAPRKRPENQKTPEVVVRPKSKRNRSPRELEPEAKKLCVKGPGSSRRFDSGLWAGLASLRVPPLCSSIVRALHQHKLGTAAWPSLQQGLQQSFLNSLASYRIFQKAAPFDRRATSLAWHPTHPSTLAVGSKGGDILLWNFGIKDKPTFIKGIGAGGSITGMKFNPLNTNQFFTSSMEGTTRLQDFKGNTLRVFASSDTCNVWFCSLDVSVKSRVVVTGDNVGHVILLNMDGRELWNLRMHKKKVTHVALNPCCDWLLATASVDQTVKIWDLRQVRGKSSFLHSLPHRHPVNAAHFSPDGAQLLTTDQKSEIRVYSACQWDCPPSLIPHPHRHFQHLTPIKASWHPRYNLIVVGRYPDPNFKSCSPHELRTIDVFDGSSGKIMYQLYDPESSGIMSLNEFNPMGDTLASVMGYHILVWSPEDAGTQK
The following text describes a protein:
Function:
O-methyltransferase; part of the gene cluster that mediates the biosynthesis of griseofulvin, an important antifungal drug that has been in use for a long time for treating dermatophyte infections. The first step of the pathway is the formation of the heptaketide backbone by gsfA which is initiated by priming with acetyl-CoA, followed by sequential condensations of 6 malonyl-CoA units. The resulting benzophenone can undergo a spontaneous dehydration to form norlichexanthone. However, the true precursor for the griseofulvin biosynthesis is not norlichexanthone, but the heptaketide benzophenone that is O-methylated at 3-OH by gsfB to produce griseophenone D which is further methylated at 9-OH by gsfC to yield griseophenone C. Griseophenone C is then substrate of halogenase gsfI which is responsible for the regio-specific chlorination at the C13 position to form griseophenone B. The cytochrome P450 gsfF catalyzes the coupling of orcinol and phloroglucinol rings in griseophenone B to form desmethyl-dehydrogriseofulvin A which is further methylated at 5-OH by gsfD to yield dehydrogriseofulvin. Finally, gsfE performs stereospecific reduction of enone 18 of dehydrogriseofulvin to afford the final product griseofulvin.
Sequence:
MASNTSRSAHLAQIITENTANIETYRREQGLPPLSLGPDAPLDVKYPPNVEKCRRAVIDATLELGELATGPVELRLVPGWAIMTMFGVTQFICDFDIARQIPLAGDISYEDLSKAINVAVPVLRQVLRAGMPYHMFYESRPGHVAHTATTKVMASESLISDWTSLYTDVLFPASAGLSKALREEPTASDPSKTGFMVTKGDGESGMYMYFEKHPEEARRFAGVMEAFQKDEAYAVRHLTDSWPSDSQTGKLVDLGGSTGAVAFALAEKFPGLEIVVQDLPGALEAAHVREGKNVSFMPHDFFNEQPVKDADVYMFRWILHNWPDGHVQRILRALVPSLKPGAKVIVFDEIMPPAGTLPLSIERYQRNIDFGMLTLFNSKIRDIVEWKEIITQSDQRFNVTGVRYPENSRLSLIEIVWQP
The following text describes a protein:
Function:
Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramides/GlcCers (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) into free ceramides (such as N-acylsphing-4-enine) and glucose. Plays a central role in the degradation of complex lipids and the turnover of cellular membranes. Through the production of ceramides, participates in the PKC-activated salvage pathway of ceramide formation (By similarity). Catalyzes the glucosylation of cholesterol, through a transglucosylation reaction where glucose is transferred from GlcCer to cholesterol. GlcCer containing mono-unsaturated fatty acids (such as beta-D-glucosyl-N-(9Z-octadecenoyl)-sphing-4-enine) are preferred as glucose donors for cholesterol glucosylation when compared with GlcCer containing same chain length of saturated fatty acids (such as beta-D-glucosyl-N-octadecanoyl-sphing-4-enine) (By similarity). Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl 3-beta-D-glucoside to ceramide (By similarity). Can also hydrolyze cholesteryl 3-beta-D-glucoside producing glucose and cholesterol (By similarity). Catalyzes the hydrolysis of galactosylceramides/GalCers (such as beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine), as well as the transfer of galactose between GalCers and cholesterol in vitro, but with lower activity than with GlcCers (By similarity). Contrary to GlcCer and GalCer, xylosylceramide/XylCer (such as beta-D-xyosyl-(1<->1')-N-acylsphing-4-enine) is not a good substrate for hydrolysis, however it is a good xylose donor for transxylosylation activity to form cholesteryl 3-beta-D-xyloside (By similarity).
Subcellular Localization:
Lysosome membrane; Peripheral membrane protein; Lumenal side. Note=Interaction with saposin-C promotes membrane [?]association. Targeting to lysosomes occurs through an alternative MPR-independent mechanism via SCARB2.
Sequence:
MAARLIGFFLFQAVSWAYGAQPCIPKSFGYSSVVCVCNASYCDSLDPVTLPALGTFSRYESTRRGRRMELSVGAIQANRTGTGLLLTLQPEKKFQKVKGFGGAMTDATALNILALSPPTQKLLLRSYFSTNGIEYNIIRVPMASCDFSIRVYTYADTPNDFQLSNFSLPEEDTKLKIPLIHQALKMSSRPISLFASPWTSPTWLKTNGRVNGKGSLKGQPGDIFHQTWANYFVKFLDAYAKYGLRFWAVTAENEPTAGLFTGYPFQCLGFTPEHQRDFISRDLGPALANSSHDVKLLMLDDQRLLLPRWAEVVLSDPEAAKYVHGIAVHWYMDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVTGWTDWNLALNPEGGPNWVRNFVDSPIIVDIPKDAFYKQPMFYHLGHFSKFIPEGSQRVALVASESTDLETVALLRPDGSAVVVVLNRSSEDVPLTISDPDLGFLETVSPGYSIHTYLWRRQ
The following text describes a protein:
Function:
As a likely component of a histone deacetylase complex, together with saeg-1 and hda-2, functions downstream of the cAMP-dependent kinase egl-4 to regulate the expression of genes required for egg-laying and foraging.
Subcellular Localization:
Nucleus.
Sequence:
MRIVILDELLSREMDGSNDGSSARVNSLKHVIKRNKMDMADDAPSSLDLMRRIFQAEISREIHQIMERHTRTTLLPAIENLRKNGHVVDESVLNGLYCNILEAAKKPYQKDPEPMPPICTNGNGFLDINSQEHENNLKRGYESDSSDVSGVSHCSDAKRRRGRPRKDEEAYRLEMTPPTMNEVIRWNPDRIDVNTRFITATKIAQVMGMPPSILFNKYPRMFRYSCDEDDKNILHEQNLLIRAPGRCYLLVAEDARQLVPSTYFQDVLNVSFLISEPLLSKIRQKAASTYEKYKVFLPTQPNNYL
The following text describes a protein:
Function:
Probable metalloprotease involved in proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Accompanies the pre-60S particles to the cytoplasm (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MELDPSDSNSRVVDASQFSKYRDAGALVSKAFHQVASRCVPGASTREISSYGDNLLHEYKSSIYKSQRFEKGIAEPTSICVNNCAYNYAPGPESVIAGNDNSYHLQVGDVTKISMGLHFDGYTALISHTIVVTPPPQPGMGPYIGPGADAICAAHYASKAVANLLATNNSDDPITGSRLRKIVDDIASQFRVSVCPGSRIRRISRFLVGQPTIDRLEEDQNTKHAVEWPAPEEETRKADVTNSLDPANVLSTELNTWHVMPKEAWLIDISMSSQPISSLKEHPDLKPTLYIHDVNVSYMLKLKASRSLLSEIKKEKSVFPFHFGSLSSERNLLGLRELTDRHILVPMPVLISSPSNVIAREELTVITQPNPSSDLLCLTVPTPPSYVKSDFSLEDGTDAALICEGINVNIKSININV
The following text describes a protein:
Function:
Glutamate-gated receptor that probably acts as a non-selective cation channel. May be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells; Glutamate-gated receptor that probably acts as non-selective cation channel.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MAGESRARSHPLFLLLLLLTFAAFLPATSRAQQPSAPAEVKVGLIIDAASPVGKIARTTIPMALEDFYSAFPNSSARVKILQHDSRGDVVAAASAALQLMTSQGARAILGPQSSVESAFVAGLATRAEFPVVSFSATSPSVSPAAARFFARAATSDAAQAGAIAALATHFGWRRVVPVYQDDDYGAAFVPFLVDALTTGDARAEVPYRCALPAAATRDAIAAALYRMESEQTRAFVLHTRPELARRVLASAVETGMMAEGHAWVITDGLTGLLGSIEPPQGVIGLAPYVPVTPRLRDVRKRWAHRYMRDHRDDEPAQAEMGCYAVWAYDAAWAVAHAAERLSSSDLSSPPGLVGGKGGPTEIAGLGKSVTGDKFLRAINDTRFDGLGGRFELINGELAVPAFRVINIMDNGKERGVGFWTPQHGLSRHSDRRSDESNGELAPVIWPGESTVQPRGWVQPTNARKLQVAVPGSVADGYKAIVHLDVDLVTNQTTASGFVIEVFEAAVRLLPYALPFEYVKAESMPYDKLVEAVGNGSFDAAVADITITANRSEHVDFTLPYTATAIAMVVPVRDERGSKRTWVFLKPLRYDLWLVSAAFFLFTGFAVWAIEHRVNDDFRGPPSYQVGTLLYFGFSTLVFAHRENLRSNLSRFAVVVWVFVVLILQSSYTASLTSMLTVPQLGPTVADYGALLRAADQKVGIMNNSFMRGAMGKAGFTPDRLVPYRNPQEFQEALLNGTIAAVVNETPYLKIFLKAYRGNFTMVAGQRNKTGGFGFAFPKGSPYVTDLSRAILELTESDEMNMIERKWFGEEDDGAAEGGGFTSNSLSFGSFWGLFLITGATSLLCCAVHLATFVAANRREITPHLSWKDRVRKMAKLFDDKDPSAHTFRIKDYGGAVGVASRNGAVGSPPVTLGGEAGSPVSVPYTSEWSVEMESPETCEIELAAGGQEREEVRAPPMPTDQERMVELQ
The following text describes a protein:
Function:
Cytotoxin and helminthotoxin. MBP also induces non-cytolytic histamine release from basophils. It is involved in antiparasitic defense mechanisms and immune hypersensitivity reactions (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MKFPLLLALLVGGASALHLSSETSDSKSPLMDENLPRDAEISGPEGEECPPGEELMPLEGEKEEGSGSEGVPGDEGAVSGQDVTDVDLQCPKEEDTTSLMGDSGCKTCRYLLVRRAECFDKAQSVCRRCYRGTLASIHSFSVNFGIQSAVRGINQGQVWIGGRIKGWGRCKRFRWVDGSSWNFAYWAAGQPCPGGGRCVTLCTQGGHWRLSHCVKRRPFICSY
The following text describes a protein:
Function:
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein.
Sequence:
MATFNLTIVSAEQKIFEGEVKQIQVTGVEGELGILPGHTPLLTAIKPGIVKFTLKDGNEEVIYVSGGFLEVQPNIVTVLADIAIRGSELDADRIHEAKRKAEENIVSRGSDADHDLLVAKLSKELAKLRAYELTEKLLKTRR