lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor.
Sequence:
MASAGGDECEGAAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMGLLGQNEVEQRQRKVVILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTHSSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVRRGRDLEQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNGDICKWHRGGSNGRSYKRTFSEPGDHPGMLTSGKRSHLESSSRPH
The following text describes a protein:
Function:
Catalyzes the exchange of ADP and ATP across the membrane.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MATWRRDGRLTGGQRLLCAGLAGALSLSLTAPLELATVLAQVGVVRGHARGPWATGHRVWRAEGPRALWKGNAVACLRLFPCSVVQLAAYRKFVVMFTDDLGHISQWSSIMAGSLAGMVSTIVTYPTDLIKTRLIVQNMLEPSYRGLLHAFSTIYQQEGFLALYRGVSLTVVGALPFSAGSLLVHMNLEKIWNGPRDQFSLPQNFANVCLAAAVTQTLSFPFETVKRKMQRRSQSRFPAQSRPAAACRLFPFNMTDAAVSFAKDFLAGGVAAAISKTAVAPIERVKLLLQGIIIYRAAYFGIYDTAKGMLPDPKNTHIVISWMIAQTVTAVAGLTSYPFDTVRRRMMMQSGRKGTDIMYTGTLDCWRKIARDEGGKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYT
The following text describes a protein:
Function:
Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion.
Subcellular Localization:
Mitochondrion outer membrane; Multi-pass membrane protein.
Sequence:
MAEAHQAVAFQFTVTPEGVDFRLSREALKHIYLSGINSWKKRLIRIKNGILRGVYPGSPTSWLVVASATAGSSYYNVDISMGLVNHIQRCLPERYGPYWTPQTRALLSMAVVSTGVWMIGIFFFRQTLKLLLSYHGWMFEMHGQSSRVTKVWAICVRLLSSRRPMLYSFQTSLPKLPVPSVPATIHRYLESVQHLLDDEEYSRKEMLAKEFQEKTAPRLQKYLVLKSWWATNYVSDWWEEYVYLRGRTPLMVNSNYYVMDLVLMRSTDVQAARLGNAVHAMIMYRRKLDREDIKPVMALGIVPMCSYQMERMFNTTRIPGKDTDTLQHLTDSRHVAVYHKGRFFKVWLYEGSRLLKPCELELQFQRILDDPSPPQPGEEKLAALTAGGRVEWAQARQAFFSSGKNKFALDAIERAAFFVALDEESHHYDPEDEASLSLYGKALLHGNCYNRWFDKSFTLIAFKNGQLGLNTEHAWADAPIIGHLWEFVLGTDTFHLGYTETGHCLGKPNPMLAPPQRLQWDIPEQCQAVIESSYQVAKALADDVELYCFQFLPFGKGLIKKCRTSPDAFVQIALQLAYFRDRGKFCLTYEASMTRMFREGRTETVRSCTRESTAFVQAMVEGRRVKADLQDLFRKAAQKHQNMYRLAMTGAGIDRHLFCLYVVSKYLGVSSPFLAEVADDGYGVSYMIAGENTIFFHVSSKFSSSETNAQRFGNHIRQALLDLADLFQVPKADS
The following text describes a protein:
Function:
Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2 at 'Lys-754' leading to its degradation by the proteasome. Plays a role in regulating inflammatory cytokine release and gram-positive bacterial clearance by functioning, in part, through the ubiquitination and degradation of TLR2. Inhibitor of protein phosphatase 1.
Sequence:
MAEAGAGGLSETVTETTVTVTTEPENRSLTIKLRKRKPEKKVEWSSDTVDNEHMGRRSSKCCCIYEKPRAFGESSTESDEDEEEGCGHTHCVRGHRKGRRPTTPGPTPTTPPQPPDPSQPPPGPMQH
The following text describes a protein:
Function:
Exoribonuclease involved in ribosome biosynthesis. Involved in the processing of ITS1, the internal transcribed spacer localized between the 18S and 5.8S rRNAs.
Sequence:
MAAPSNSSRFPPLEKYVALDCEMVQLRNCMGLAKIGIVDAYGNVLMESFVRHHPANVVNYVTRKSGIRPQDLVGAPTYEQIQPQIIELIKDKIVIGHTLFNDLAVIGHRHQYEMMRDTALYYPLRTLVGVRSEGVWPSLRKLAAAVLNMEMHAAGTAHDPVEDARMTMAIFMTVREEYEDALWRGKDVVACLPERYVSCYW
The following text describes a protein:
Function:
Involved in trafficking to the vacuole. Required for cell proliferation and cell expansion, but not for cell differentiation. Acts in low affinity electroneutral exchange of protons for cations such as Na(+) or K(+) across membranes (By similarity). May also exchange Li(+) and Cs(+) with a lower affinity (By similarity).
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
Subcellular Localization:
Endosome membrane; Multi-pass membrane protein. Golgi apparatus, Golgi stack membrane; Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein.
Sequence:
MSSELQISPAIHDPQGQEKQQQAAGVGILLQIMMLVLSFVLGHVLRRHKFYYLPEASASLLIGLIVGGLANISNTETSIRTWFNFHDEFFFLFLLPPIIFQSGFSLQPKPFFSNFGAIVTFSVLGTFVASMVTGLLVYLGGVMFLMYRLPFVECLMFGSLISATDPVTVLSIFQELGSDVNLYALVFGESVLNDAMAISLYRTMSLVRSHSSGQNFFMVIVRFLETFVGSMSAGVGVGFTSALLFKYAGLDVDNLQNLECCLFVLFPYFSYMLAEGLSLSGIVSILFTGIVMKHYTYSNLSANSQRFVSAFFHLISSLAETFVFIYMGFDIAMEKHSWSHLGFIFFSILFIVIARAANVFGCGYLVNLARPAHRKIPMTHQKALWYSGLRGAMAFALALQSVHDLPEGHGQTIFTATTAIVVLTVLLIGGSTGTMLEALEVVGDSHDTSLGDGFEVVNSRYMTSYDDEDTPPGSGFRTKLREFHKSAASFTELDRNYLTPFFTSNNGDYDDEGNMEQHHEERIPFTRRGNLNNRG
The following text describes a protein:
Function:
Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
Sequence:
MIRPRDELGTATTDSAQKIVLLGSGELGKEIAIEAQRLGVEVIAVDRYANAPAMQIAHRSYVGDMRKADFLFSVVEREKPDAIIPEIEAINLDALFELEKDGYFVVPNAKATWIAMHRERTRETLAREAKVPTSRYTYASTLDELYEACEKIGYPCHTKAIMSSSGKGSYFVKGPEDVPKAWEEAKKKARGSAEKLIVEEHIDFDVEITELAVRHYDENGEVVTTFPKPVGHYQIDGDYHSSWQPAEISERAEREVYRIAKRITDVLGGLGIFGVEMFVKGDKVWANEVSPRPHDTGMVTLASHPTGFSEFGLHLRAVLGLPIPGEWVDGYRLFPMLTPAATHVIKANVSGYSPRFRGLAKALSVPNATVRLFGKPEAYPGRRLGVAIAWDKDVGEAKRKAEMVAHSIELRTRSANWHSQDYEKRKHLL
The following text describes a protein:
Function:
The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. This subunit has 5' -> 3' nuclease activity but not helicase activity.
Miscellaneous:
MISCELLANEOUS: Despite having helicase-like domains, this subunit does not have helicase activity.
Sequence:
MKLLYTDIRTSLTEILTREAEELVAAGKRVFYIAPNSLSFEKERAVLEYLSQQASFSITVTRFAQMARYLVLNDLPAKTTLDDIGLGLAFYKCLAELDPKDLRVYGAIKQDPQLIQQLIELYHEMTKSQMSFLDLENLTDEDKRADLLLIFEKVTAYLNQGQLAQESQLSHLIEAIENDKVSSDFNQIALVIDGFTRFSAEEERVVDLLHGKGVEIVIGAYASKKAYTSPFSEGNLYQASVKFLHHLASKYQTPAQDCSQTHEKMDSFDKASRLLESSYDFSELALDVDEKDRENLQIWSCLTQKEELELVARSIRQKLHENSDLSYKHFRILLGDVASYQLSLKTIFDQYQIPFYLGRSEAMAHHPLTQFVESILALKRYRFRQEDLINLLRTDLYTDLSQSDIDAFEQYIRYLGINGLPAFQQTFTKSHHGKFNLERLNVLRLRILAPLETLFASRKQKAEKLLQKWSVFLKEGAVTKQLQDLTTTLEAVEQERQAEVWKAFCHVLEQFATVFAGSQVSLEDFLALLHSGMSLSQYRTIPATVDTVLVQSYDLIAPLTADFVYAIGLTQDNLPKISQNTSLLTDEERQNLNQATEEGVQLLIASSENLKKNRYTMLSLVNSARKQLFLSAPSLFNESESKESAYLQELIHFGFRRREKRMNHKGLSKEDMGSYHSLLSSLVAYHQQGEMSDTEQDLTFVKVLSRVIGKKLDQQGLENPAIPTSPSSKTLAKDTLQALYPAKQEFYLSTSGLTEFYRNEYSYFLRYVLGLQEELRLHPDARSHGNFLHRIFERALQLPNEDSFDQRLEQAIQETSQEREFEAIYQESLEAQFTKEVLLDVARTTGHILRHNPAIETIKEEANFGGKDQAFIQLDNGRSVFVRGKVDRIDRLKANGAIGVVDYKSSLTQFQFPHFFNGLNSQLPTYLAALKREGEQNFFGAMYLEMAEPVQSLMAVKSLAGAVVEASKSMKYQGLFLEKESSYLGEFYNKNKANQLTDEEFQLLLDYNAYLYKKAAEKILAGRFAINPYTENGRSIAPYVQQHQAITGFEANYHLGQARFLEKLDLADGKRLVGEKLKQAWLEKIREELNR
The following text describes a protein:
Function:
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Sequence:
MRLLEYESKEALASKGIPIPKGILARDPEEAASAVEKLGGRGVLKIQIPHGQRGKAGGIKLVNSPNEAREVAKELFSRTFYGYEVSSLLVEEPVDTATEIYIGGIIDRNSRGMTFISTPYGGMDVEEIAASHPESIEKRTVHPLMGMRSHIARALAKNAAKNVPDKVNEIQRIISSLWDVAVEYDAVMLEINPLALTKDGRLVALDARIEVDDNALFRHMEFEKRYYSSENPRENEARKRDIAYVELDGNIGTMANGAGLAMATMDLVHTFGGKPANFCDVGGGASADRVANALEIILSNPRASVVLINTLCGITSALDVALGVKSIKEKGLLKIPVVVRMSGNQADEGKRILEEIGIKATESAEEAVRYAVELAKRA
The following text describes a protein:
Function:
Bifunctional protein composed of 2 glycosyltransferase domains involved in glycosylating skp1. The N-terminal part catalyzes the transfer of a galactose residue to GlcNAc-skp1 in a beta 1-3 linkage. The C-terminal part catalyzes the transfer of a fucose residue to Gal-GlcNAc-skp1 in an alpha 1-2 linkage.
Sequence:
MNDSPIISVVLPFLIKDNDDKSLNYQGINNLIISIDSIIEQTFKEWELILVDDGSNNEILEQLLSKRYSTDNRIKFIINKENKGIVKSLNDAILNHCSPTSKYIARMDSDDISHPTRLQSQLKYLQSNETIDILGCPIKMFNNNKLIEILNNNNNNNNINNNVKELINIINNEESFKFIQHPDKDILMWSMFFNCCIVHPSVIFKRSIFTIEHCYEENNQFPFIEDYLFWLKSLIMKGLNISNIQSSTPLLYLRKHNNSISFKNIEKQKDSTANASCYYLNILFKRFNIDSEIIQNSSLSMKEIIQFFQLSPSSLSKINNISIELFEFAFKYLELIEKSCTKQQPNYSNSIKDAANEKMGELVSLCLSNYPNNQKSSLLWEKWLSRNPTSQLLSLLSNLNVKSSTTIINNNINNNNNNNNNNNNNNNNNNNNNNNNNNNNNSILNFISGINSNKINTPKSNNNKFKENGIRIICFSKDRAFQLKEYLRTFFKYLKNDDNGNDKFEIIVDVLFTYSNEKFKNSYQLVIESFPQVNFIKEENFTDQLINLVQKTNKLEYVMFSVDDILYYNEFNLKEYCLSLNSEPLALGFYMKLNKNITYCHTCNQDITIPLNSNTISRTENNFKYLKWNRNDNDCKKDWNYPWDLCSTIYRCNDIDSIINGIVKYYGIRNGINHPNRFEFNGNRPIIQKQIYQNKPYCLCLSDHYSPMSVVTINRVQDVYDNPIYDQTLSLDDLDQLLYSNKSLNDEKYKENSLSLNFKSVHIGELFIS
The following text describes a protein:
Function:
Divinyl ether synthase involved in oxylipin biosynthesis. Catalyzes the conversion of (13S)-hydroperoxy-(9Z,11E)-octadecadienoate (13-HPOD) to etheroleate and (13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate (13-HPOT) to etherolenate. Has no activity with the corresponding 9-hydroperoxides (9-HPOD and 9-HPOT).
Sequence:
MPASGKEKPLKDVPGSYGVPVVGALKDRLDFYWFQGEVEFYKSRMAKNQSTVFRVNFPPGPPGFPEGHGIVLLDQVSYSVLLDNAKVDKRDTLIGSYMPDLAFTGGYRTLPYLDTAEEKHTTYKSLMFEILHESAQRFGPELSSAFDRTAQEWEAKIAKDGSVESLSTAGNMVIQFLYKTITHQDPMATMGDDPHSVYMAWTGVQFAGIAYTSLPHITEELLMHSFQLPFFPIKKKYEQIVEFFRSAGSGLLDLAVTKYGLDREEALHNLVFSFGINTRLGLLKMFPPILFFIARAGAEFQARLKQEIRGRIKKRKDAASIQALGDLKLVKATVLEVFRLMPSIFVAFGRARQDLEVESHDARYKIKKGELLGTHQYFVMRDPVVFKDPHSFVPDRFMGSEGAALLPHIVWSNGRETDSPTPTNKQCPGKNQAELIAVQFIAEMFLRYDSWEVTQESSVSATKLDVHLCKLVKRS
The following text describes a protein:
Function:
RNA-binding protein involved in post-transcriptional regulation.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MAIGKRKESTEVKKKDGSMNKRVKVAKLPKKVDSFSPKKKKNTTSSGSSESDSMSQNDKKKDSSLNESEDEDFAGFGESASENDELESAESEAENDEESSSQKSNSKESHAQRKKLQKERKAMKPFADTSLKAKSLWDKLRQKTSIKAEERKTIIAELFDLIRTNVKQLVFKHDMSRVVQTCVKFGSKQQRETICAELAGSYVDLCKSPYGKYLAIKIFKYGTPKMKEVILGEMYGNVVKMIRHREAAYVVEDAFREFTNLQQQRALICEFYGPEFQVFKDRTQDIHIDKLLIDHPEKRPSIMQNLWKTIEGSIAKGSIGFTMVHRAMLEFINHADSNEAKELLNLTKELIYEFVHTRDGSQVAMKLFALANAKDRKVMLKSLRPYLIETAKDSYGHLVVVAALDCTDDTIMTGKLLQAEFEGELLKLSADKFARRILLYVLVGWEDARYFSKENRELLRSLDSLKAKTSKKDPIVRRNELKATIGPLLISLISKAAGDMIAESLASQVLVDALLYAPCEKEEAVDATLKAFDGNPEQDNHLIHQIHCSRALKTLVQNGHWSGAEKQVVKAEDDLKVASKLIVIIKKYLVEWASGDGAFVVVAVLEALSDSEKQEFLKILRKHKNQLNKSEFRGTKKLLEML
The following text describes a protein:
Function:
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair (By similarity). Also involved in deacetylation of histones, chromatin assembly and chromosome segregation. May act as a transcriptional oscillator, directing histone deacetylases to specific chromosomal domains.
Subcellular Localization:
Nucleus.
Sequence:
MAVSYKVNERVLCFHGPLLYEAKIVDTEMKGDVTTYLIHYKGWKNSWDEWVEQDRILQWTEENLKTQKELKNAAISTRQKPTSKKSASSTSKHDSTGVKTSGKRSRESSTVTVDGDSHELPSRIKTQKSESPIPQQVKRDGTTDAKNEETTKPENNEKDDFEEEPPLPKHKISVPDVLKLWLVDDWENITKNQQLIAIPRNPTVRAAIAAFRESKISHLNNEIDVDVFEQAMAGLVIYFNKCLGNMLLYRFERQQYLEIRQQYPDTEMCDLYGVEHLIRLFVSLPELIDRTNMDSQSIECLLNYIEEFLKYLVLHKDEYFIKEYQNAPPNYRSLVGV
The following text describes a protein:
Function:
The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.
Miscellaneous:
MISCELLANEOUS: Present with 1520 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MAYNQEDSKRLSDKYKKEGHFDKLKREILSNPWNNTEENSESFEQALRKRVASTVKEMVNEDEELIFKNRGLTSALIESQLVKDNYLKLGSKMEGDNGDGEKKFDLDVYVRSKLQDPKLLEMIKGQLQETLNSYEEEANGST
The following text describes a protein:
Function:
Binds double-stranded DNA tightly but without sequence specificity (By similarity). Incubation with DNA in vitro gives fibrous structures 10.3 +/- 1.1 nm in thickness (naked DNA is 1.83 +/- 0.37 nm). This protein does not significantly compact DNA.
Subcellular Localization:
Cytoplasm. Chromosome.
Sequence:
MAEEHVVYIGKKPVMNYVLAVITQFNEGAKEVSIRARGRAISRAVDVAEIVRNRFLPEVRVKEIKIGTEELPTADGRTANTSTIEIILEKP
The following text describes a protein:
Function:
Regulates the cell cycle in a nutrient dependent manner.
Subcellular Localization:
Cytoplasm.
Sequence:
MIINDKKDQETKVDDTTTLTLTREHLLNCQFSAWYKLYKSITPKTRIIKPLPEDFVNYLSEDGVILPDEEKTSYGSDSGVFEEYSDDEDELDSYVSKLDDFHPKVQAVIDEFGAVAPKLNWSSPQDAIWISPSNSTRCVTVNDVYLLLKSSDYIAHDLTMLDKLGGIPKDFSFELVLRKWININPALEFRCFVKDRELIAVTQRDQNYYEFLIKLKERFLGEIELFFYEHIKDTFPDSSFVFDVYIPEPYDKVWLMDFNVFYPTTDSLIEWSTLVNLDATSPSFDLDLLLIDKELRNASFACQRHSQNKVPMDIVNASMDTEAMVEMLRSQQREMDRLDGDQGGEASATGDTTGDSVANETTAANTTSQDS
The following text describes a protein:
Function:
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Sequence:
MRMRRTILIFTVILIPLTFCFKNALIKHSINIVSKRGNSKNRFSQKVYESKNIDLENDIKENDLIPNVKVMIDVRNMNNISDTDGSPNDFTSIDTHELFNNKKILLISLPGAFTPTCSTKMIPGYEEEYDYFIKENNFDDIYCITNNDIYVLKSWFKSMDIKKIKYISDGNSSFTESMNMLVDKSNFFMGMRPWRFVAIVENNILVKMFQEKDKQHNIQTDPYDISTVNNVKEFLKNNQL
The following text describes a protein:
Function:
Has E3 ubiquitin ligase activity, promoting ubiquitination and degradation of target proteins. Involved in activation of the JAK/STAT pathway. Catalyzes ubiquitination of methylated RBM15. Plays a role in quality control of translation of mitochondrial outer membrane-localized mRNA. As part of the PINK1-regulated signaling, upon mitochondria damage, ubiquitinates ABCE1 and thereby recruits autophagy receptors to the mitochondrial outer membrane to initiate mitophagy.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSRSPDAKEDPVECPLCMEPLEIDDINFFPCTCGYQICRFCWHRIRTDENGLCPACRKPYPEDPAVYKPLSQEELQRIKNEKKQKQNERKQKISENRKHLASVRVVQKNLVFVVGLSQRLADPEVLKRPEYFGKFGKIHKVVINNSTSYAGSQGPSASAYVTYIRSEDALRAIQCVNNVVVDGRTLKASLGTTKYCSYFLKNMQCPKPDCMYLHELGDEAASFTKEEMQAGKHQEYEQKLLQELYKLNPNFLQLSTGTVDKNKNKVTPLQSPIDKPSDSLSIGNGDNSQQISNSDTPSPPPGLSKPNPVIPISSSNHSARSPFEGAVTESQSLFSDNFRHPNPIPSGLPPFPSSPQTSSDWPTAPEPQSLFTSETIPVSSSTDWQAAFGFGSSKQQEDDLGFDPFDITRKALADLIEKELSVQEQPSLSPTSLQNAPSHTTTAKGSGSGFLHPAAAPTNANSLGGSTFPVLPQRFPPFPQHRAVYNSFSFPGQGARYPWMAFPRNSLMHLNHTANPTSNSNFLDLNLPPQHSTGLGGIPIADNSSSVESLNMKEWQDGLRALLPNININFGGLPNASSPSNANHSAPTSNPATTDSLNWDSPGSWMDPAIITGIPASTGNSLDSLQDDNPPHWLKSLQALTEMDGPSAAPSQTQHSNPFSTQIPLHRASWNPYSPPSNPTSFHSPPPGFQTAFRPPSKPPTDLLQSSALDRH
The following text describes a protein:
Function:
Nucleoside permease that transports adenosine and guanosine. Does not show any transport activities towards cytidine, adenine, guanine, uridine, and uracil.
Sequence:
MKLSTLFTLATTISTLTTFTIASPVVVVEKRAINETALAEDIPTTKNNHAQTSYGKPFAIYQPKAFIISMFSLERDPWLKAMDFVHNITIPGLSPVYPDIHCTTNYTICQITTGEGEINAASSISALTLNPLFDLTKTYFLVGGIAGGEPNYTTIGGVTFAKYAVQVGLEYQLAYEDYHKTNPDWISGYIPYGTDDQNTYPGNVYGTEVFEVNEKLRDRAVELASKVHLNNGTEGNAKFRKLYNETAAQGLPKVVKCDSLTSDNYFTGNVLNDYFANFTLLMTNGSATYCSTAQEDNATLEVMTRLAKHGLVDYDRIMIMRTISDFSRPPPSMSAYEYFFNRSDGGISASLENLVIAGTPIIHDIVQNWDKIYESGEKYSSKNYVGDIFATLGGKPDFGKESFDTA
The following text describes a protein:
Function:
Part of the ABC transporter complex CydDC that exports the reduced low-molecular-weight thiols cysteine and glutathione to the periplasm. Export of these thiol-containing redox-active molecules may be crucial for redox homeostasis in the periplasm, permitting correct assembly of various respiratory complexes and formation of correct disulfide bonds in periplasmic and secreted proteins. CydD contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Required for the assembly of functional cytochrome bd-type quinol oxidases and periplasmic c-type cytochromes.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Domain:
In CydD the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.
Sequence:
MNKLRQKYLQKWLRAQQEPIKKLMRANIVLATLSSFILVAQTYFLATLLDKLIMQNVPRDELIPYFLGLIIGFGMRAIILWAREKIGFQSGQLLRNHIRQKILDKIHLVGPATINQKPAGSWASIMLEQVENLHNFYARFLPQQSLSAIVPVVIFIAVFPLNWAAGLILMITAPLVPLFMIIVGIAAADNSQKNMDTLSRLSAQFLDRLRGLETLRLFNRTSEQTEHIENATEDFRETTMDVLKLAFLSSAVLEFFTSISIALMAVYFGFSYLGQIEFGTYNAPLTLFTGFFCLILAPEFYQPLRDLGTYYHDRAAGIGAADAIVDFLESDYLTVHQNEKTISLESAVEISAENLVVLSTQGSALTKPLNFQIPANHNVALVGQSGAGKTSLMNVILGFLPYEGSLKINGQELRESNLADWRKHIAWVGQNPLLLQGTIKENLLLGDVQANDEEINQALMRSQAKEFTDKLGLHHEIKDGGLGISVGQAQRLAIARALLRKGDLLLLDEPTASLDAQSENLVLQALNEASQHQTTLMITHRIEDLKQCDQIFVMQRGEIVQQGKFTELQHEGFFAELLAQRQQDIQ
The following text describes a protein:
Function:
May be required for normal outer mitochondrial membrane dynamics. Required for coatomer-mediated retrograde transport in certain cells. May recruit other proteins to membranes with high curvature. May promote membrane fusion. Involved in activation of caspase-dependent apoptosis by promoting BAX/BAK1 activation. Involved in caspase-independent apoptosis during nutrition starvation and involved in the regulation of autophagy. Activates lipid kinase activity of PIK3C3 during autophagy probably by associating with the PI3K complex II (PI3KC3-C2). Associated with PI3KC3-C2 during autophagy may regulate the trafficking of ATG9A from the Golgi complex to the peripheral cytoplasm for the formation of autophagosomes by inducing Golgi membrane tubulation and fragmentation. Involved in regulation of degradative endocytic trafficking and cytokinesis, probably in the context of PI3KC3-C2 (By similarity).
Subcellular Localization:
Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Mitochondrion outer membrane; Peripheral membrane protein. Cytoplasmic vesicle, autophagosome membrane. Midbody. Note=Association with the Golgi apparatus depends on the cell type. Following starvation colocalizes with ATG5 and LC3 autophagy-related protein(s)on autophagosomal membranes.
Domain:
An N-terminal amphipathic helix, the BAR domain and a second amphipathic helix inserted into helix 1 of the BAR domain (N-BAR domain) induce membrane curvature and bind curved membranes; The SH3 domain is required and sufficient for the interaction with UVRAG.
Sequence:
MNIMDFNVKKLAADAGTFLSRAVQFTEEKLGQAEKTELDAHLENLLSKAECTKIWTEKIMKQTEVLLQPNPNARIEEFVYEKLDRKAPSRINNPELLGQYMIDAGTEFGPGTAYGNALIKCGETQKRIGTADRELIQTSALNFLTPLRNFIEGDYKTIAKERKLLQNKRLDLDAAKTRLKKAKAAETRASSEQELRITQSEFDRQAEITRLLLEGISSTHAHHLRCLNDFVEAQMTYYAQCYQYMLDLQKQLGSFPSNYHSNNNQTAVAPVPSASSNVIGSSALTSTSSLVITSPSNLTDLKECGGSRRARVLYDYDAANSTELSLLADEVITVFSVVGMDSDWLMGERGNQKGRVPITYLELLN
The following text describes a protein:
Function:
Required for the initiation of meiosis II and progression through anaphase II.
Subcellular Localization:
Nucleus.
Sequence:
MLSMLLPFGNSGVYASDVDREDRPEIAKLVQAFPTIEEDYHVVKLVGAGSFSSVFKAVDRHFDSYDNSYWISSQIEDQMPHDKTKRPKNHFVALKRIYATVLPSRIQTELEMLHELRGSDCVLNMITAVRHQDQVLIVLPFIQHAEFRDFYMKYSLPEIGAYLRDLLKGLAHIDAKGIIHRDIKPGNFAWNPYTQRGVILDFGLAQWQEADAPTENCCVDKLRKLKQEGKYYDYFPFEKTIADPPEGYLLHDPRPTKRADRAGTRGFRAPEVLFRCQNQTSSIDVWSVGVILLCFLTHRYPFFRCEDDIDAIVELAHIFGRNGMSNCALLHGQIWSDNIPTLLDQKHNWLDLIASITKNDENLILETSSDYQVALAIDLLDKLLELHPSKRVKAKTALQHEFFNACGVTRSGFEAENPFRSDFPSTVEQ
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase.
Subcellular Localization:
Endomembrane system. Endoplasmic reticulum membrane; Single-pass type IV membrane protein.
Domain:
The RING-type zinc finger domain is responsible for E3 ligase activity.
Sequence:
MAGDEAAEGSGRMHMDLNLHVGLPPLPQPRVQLDTSTASSSTLMPPNLTGATPEAPTTGEPEESLAPAATTFSPSNTTLFALEEHPMLDPIVYSWLDGNSASGEEYTDAPEPSAPAPVDGLLVARSVRPSRVAAATGMEMVNTSTLGQQSTQGAAATTIELRFLRMIQISQQHNIVRPGSANLTQSSFEAARGPNPDGGDNSSFECTICLELARQPVVTSCGHLFCWPCLYQWLHAQSSSFECPVCKGEVLTGDITPIYGRGGEEEGVSTATTNPNLPPRPQAHRRESLRQQLQMAGRDGNTREMVRVLRQLIQDENQGWDAIPARVETTWVPAARQRAGARRQQRQDRNAAPAQVVLAAPQQPSSMEQLLTSSTAAAIVAGEPGPSSRSRRPSESPTIRRTRRRPQ
The following text describes a protein:
Function:
Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MDRELAQPASVLSLPVVCGHAIMGSSVYITVELAIAVLAILGNVLVCWAVWLNSNLQNVTNYFVVSLAAADIAVGVLAIPFAITISTGFCAACHGCLFIACFVLVLTQSSIFSLLAIAIDRYIAIRIPLRYNGLVTGTRAK
The following text describes a protein:
Function:
Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.
Subcellular Localization:
Cytoplasm. Secreted, cell wall.
Sequence:
MTEQMLDYFIVGAGLGGVAFAEVALQHQKSIFVFAGDKPPSSVAAAGVYNAVILKRFTLVSQAQEQINLLKVFYPEIEKRIQKNIIFDLPTYRRLASVEEQNNFIVASDRPLFQLFLSPKIISDKFKAVISPFGFGLMKQTGYVDTKLLLQSYRNYLQQNGCISAETFNYAELIIHPDFVEYKGQKAKQIIFAEGFQMKHNPFFKDLPLEGAKGELLVIRSENLDVNVLLKAGVFVLPIGNDLYKVGATYNWTDKTNKPTQSAKDELISELKELISCDFEVVEHLAGIRPTVKDRKPLVGRHPFHKNIYLLNGLGTRGVMLAPYLSYKLFDFIESDLPLDSSISIERYYNSITSSNK
The following text describes a protein:
Function:
Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase.
Miscellaneous:
MISCELLANEOUS: It can potentially be a fungicidal target. Inhibition of FAS2 by cerulenin impeds the growth of wild-type and heterozygous strains.
Sequence:
MKPEIEQELSHTLLTELLAYQFASPVRWIETQDVFLKQHNTERVIEIGPSPTLAGMASRTIKAKYQSYDAALSLQRQVLCYSKDAKEIYYTPDPAEPPAAEEPKAETGKESAPAASAAAAAATQPAAAVAPPPQSAGPVESIPDEPVKASLLIHVLVAQKLKKPLDAVPMSKAIKDLVNGKSTVQNEILGDLGKEFGSTPEKPEETPLEELAEQFQDTFSGSLGKTSTSLIGRLMSSKMPGGFSITNARKYLESRFGLGPGRQDSVLLTALCNEPASRLGSEGDAKSFLDTMAQKYASHAGISLSSPSAGGASSGAGAAVVDSAALDALIAENKKLARQQLETLARYLQVDLTKGEKAFIKEKEATTVLQQELDLWEAEHGEFYAKGIKPVFSPLKSRTYDSYWNWARQDLLSMWFDILFGKLTSVDRETINQCIQIMNRANPTLIKFMQYHVELCPTYRGETYKLGKRLGEQLIENCKQILGQSPVYKDVSRITGPKTTVSAKGDIVYEEANKESVRKFEQYVFEMAQGGSMTKMKQSSIQEDLARVYKAISKQASRDSKLELQKVYDQLLKVVEGSTEIETEQTTQDALAIPTGSNTPTEEDELSTASDDDEIASLPDKTSIAQPVSSTIPNKTIPFLHIQSKSESGNWEYDRKLSSIYLDGLESAAINGLTFKDKYVLVTGAGAGSIGAEILQGLISGGAKVIVTTSRYSKKVTEYYQNMYARYGAAGSTLIVVPFNQGSKQDVDALVEYIYNDQKKGGLGWDLDVIIPFAAIPENGNGIDNIDSKSEFAHRIMLTNLLRLLGAVKARKTTDTRPAQCILPLSPNHGTFGFDGLYSESKISLETLFNRWYSEDWGTKLTICGAIIGWTRGTGLMSANNIIAEGIEKLGVRTFSQKEMAFNILGLLTPEIVNLCQEEPVMADLNGGLQFIDNLKEFTSKLRNDLTETADIRRAVSIESAIEQKVVNGDNVDSNYNKVTVRPRANMKFDFPTLKSYDEIKQIAPDLEGMLDLENVVVVTGFAEVGPWGNARTRWEMESKGEFSLEGAIEMAWIMGMIKYHNGNLKGKPYSGWIDAKTQTPVDDKDIKAKYEEEILEHSGIRLIEPELFNGYDPKKKQMIQEVVIQHDLEPFECSKETAEQYKHEHGDKCEISEIEESGEYSVRILKGATLFIPKALRFDRLVAGQIPTGWDARTYGIPEDTINQVDPITLYVLVATVEALLSAGITDPYEFYKYVHVSEVGNCSGSGMGGVSALRGMFKDRYADKPVQNDILQESFINTMSAWVNMLLLSASGPIKTPVGACATAVESVDIGIETILSGKAKVVMVGGYDDFQEEGSYEFANMNATSSAIDEFKHGRTPKEMSRPTTTTRNGFMEAQGSGIQVIMSADLALKMGVPIHAVLAMSATATDKIGRSVPAPGKGILTTAREHHGNLKYPSPLLNVKYRKRQLSKRLDQIKSWESSELNYLQEEAHLAKEEFGEEFSEAEFLRERTEEIYRESKRQVADAKKQWGNAFYKSDPRIAPLRGALATFNLTIDDIGVASFHGTSTVANDKNESATIDSMMKHLGRSEGNPVFGVFQKYLTGHPKGAAGAWMLNGAIQILESGIVPGNRNADNVDKVLEQYEYVLYPSRSIQTDGIKAVSVTSFGFGQKGAQAVVVHPDYLYAVLDRSTYEDYAKRVTARNKKTYRYMHNAITRNTMFVAKDKAPYSDELTMDVYLDPLARVSKTKNEFVFTKKSVQSDKSYVSNIANSTAKALSSLNKSSKGVGVDVELLSELNIDNETFLERNFTPEEIKYCQNSANPQASFTGTWSAKEATFKALGVSSQGGGASLKEIEIVRDGNGAPQVVLNDNAKAAAKAAGVKNVNVSISHDDFQATAVALSEF
The following text describes a protein:
Function:
Involved in growth and development through its role in cytokinesis and polarized cell expansion. Required for plasma membrane internalization. May function in clathrin-mediated membrane trafficking, including plasma membrane endocytosis, essential to both cytokinesis and cell expansion.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Cytoplasmic vesicle, clathrin-coated vesicle. Note=Colocalized with clathrin at the plasma membrane.
Sequence:
MDRRRAGSPVYGRQWSESSNSTEATSPAMSPAHRKQLGGIGGFSTVKRTQNVAAKAAAQRLAKVMALQNKDNGDEDDEDEDEDLSLRFASASLKPARHAPSSISSTGSNSSNGNNNLPAVSFAPRTRSPSPALGRNFAEQVPSSVRSASAGRPSMSARSTTPTPIPNLMPPSRVSVKTPVSIPPLDPPTRSRDKRFFADVPSVNSKEKGDQREASALRDELDMLQEENENVLEKLRRAEEKRVEAEARAKELEKQVASLGEGVSLEAKLLSRKEAALRQREAALNVAKQKKSGKDEEIVSLRSELENLKDEATTAAERLQEAESEAKSLRTMTQRMILTQDEMEEVVLKRCWLARYWGLAVQHGICADIAPSRQEHWSKLAPLPFELVTSAAQKAKELSWDKGGNDRSKAARDLSDLTGEGNIESMLSVEMGLRELASLKVEDAVVLIFAQQRKLSLVRHTVSDSKGHGESRFIDAYELGEAEQEDVAFKQAWLMYFWGRAKLHGVEDDIAEERVQLWISRSSGKSQTTSHDALDVERGLIELRKLGIEQQLWEASRREIDQLPSPTSSNHDLDADS