lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Transcriptional activator that binds specific DNA sequence.
Subcellular Localization:
Nucleus.
Sequence:
MADASAFPYGLRVLVVDDDPTWLKILEKMLRKCSYEGSNLRLLSSSGSRSAWRGGYAVASSPVGVCASVRRLCMSVTTCGLARVALEILRERKNRFDIVISDVNMPDMDGFKLLEHIGLEMDLPVIMMSIDGETSRVMKGVQHGACDYLLKPVRMKELRNIWQHVYRKKMHEVKEIEGHDSCDDLQILRYGFEGFDEKGLFMTVDSDATRKRKDVDHGDQDSSDGATAKKARVVWSVDLHQKFVNAVNQIGFDKVGPKKILDLMNVPGLTRENVASHLQKYRLYLGRLQKQNEERILGSARQDFSTKGPSSENLNLRSSFQEQPSNTSSGYPHASQKIQGQSSVSDSQLEETKRTVPLPAPDRSMNSVSSAAEPQNVAGVSPIGGVLSFKGLPVNQDRKPSETMILECQAWTGGVPAKQFMQYPKHNHARCDLLGDYACLPKPDLEHPTAPGHLFTPPPLISMSCSTEMDARNFSDVKPALLDCIKSFSPALTCTADSVSVQISDSVVTSTDAADRKFSSVEGLPSTKDCYFGQTSNQGSWLRSQEEPSIICGADFASLPEDLPGYPLQGGVSFENVGLSSIDLFHYNDAMILSGLQSNWYDDQDHFSSETTDYPLMDGCLFA
The following text describes a protein:
Function:
Catalytic component of the DNA-directed RNA polymerase (RNAP) that catalyzes the transcription in the cytoplasm of viral DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity). Forms the polymerase active center together with RPB2 (By similarity). Part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template (By similarity).
Subcellular Localization:
Virion. Note=Found in association with viral nucleoid.
Domain:
Lacks the typical C-terminal domain (CTD).
Sequence:
MEAGYAEIAAVQFNIAGDNDHKRQGVMEVTISNLFEGTLPAEGGIYDARMGTTDHHYKCITCSHQRKQCMGHPGILQMHAPVLQPLFIAEIRRWLRVICLNCGAPIVDLKRYEHLIRPKRLIEAASSQTEGKQCYVCKAVHPKIVKDSEDYFTFWVDQQGKIDKLYPQIIREIFSRVTYDTVVKLGRSKNSHPEKLVLKAIQIPPISIRPGIRLGIGSGPQSFHDINNVIQYLVRKNLLIPKDLQIVRGQKIPLNIDRNLQTIQQLYYNFLLDSVSTTATQGGTGKRGIVMGARPAPSIMRRLPRKEGRIRKSLLGSQVWSISRSTICGNSDLHLDEVGYPISFARTLQVAETVQHYNINRLMPYFLNGKRQYPGCSRVYKQITQSVHDIEGLKQDFRLEVGDILYRDVVTGDVAFFNRQPSLERSSIGVHRIVVLENPKISTFQMNVSACAWYNADFDGDQMNLWVPWSVMSRVEAELLCSVRNWFISTKSSGPVNGQVQDSTVGSFLLTRTNTPMGKNVMNKLHAMGLFQTTQTDPPCFANYSPTDLLDGKSVVSMLLKQTPINYQRAPTWYSEVYAPYMHYNKQDISTQIRNGELIEGVLDKKAVGAGSSGGIYHLISRRYGPQQALKMIFATQQLALNYVRNAGFTVSTADMLLTPEAHQEVQEIINKLLLESEEINNRLLHGDIMPPIGLTTHDFYEKLQLNALKFPDRILKPIMNSINPETNGLFQMVATGAKGSNPNMIHIMAGIGQIEINTQRIQPQFSFGRTLVYYPRFALEAQAYGFICNSYIAGLTSPEFIFGEMNGRFDLINKALSTSSTGYANRKAIFGLQSCIVDYYRRVSIDTRLVQQLYGEDGLDARQLETVRFETIMLSDQELEDKFKYTGIQSPLFEEEFSRLKKDRDKYRQIFLNVENFNFSQLLTDVRQVPVNVASIVKNILLSSTSGVLPFDEKSILQKYAMVKTFCKNLPYVFINNIQERLQTPIPVYLKRAAALMRMLIRIELATVKTLNITCEQMSAILDLIRLQYTQSLINYGEAVGILAAQSVSEPLTQYMLDSHHRSVAGGTNKSGIVRPQEIFSAKPVEAEQSSEMLLRLKNPEVETNKTYAQEIANSIELITFERLILQWHLLYETYSSTKKNVMYPDFASDVEWMTDFLENHPLLQPPEDIANWCIRLELNKTTMILKSISLESIINSLRAKHPNTYIMHSVENTASGIPIIIRIYLRESAFRRSTNTRMATDEKIAVNVVDKLLNSTIRGIPGIKNANVVKLMRHRVDAQGKLVRLDNIYAIKTNGTNIFGAMLDDNIDPYTIVSSSIGDTMELYGIEAARQKIISEIRTVMGDKGPNHRHLLMYADLMTRTGQVTSLEKAGLNAREPSNVLLRMALSSPVQVLTDAAVDSAVNPIYGIAAPTLMGSVPRIGTMYSDIIMDEKYITENYKSVDSMIDML
The following text describes a protein:
Function:
Required for 40S ribosomal subunit synthesis. Required for normal export of the pre-40S particles from the nucleus to the cytoplasm. Its subcellular location and association with pre-40S subunitshifts from mixed cytoplasm/nucleus to all nuclear in RPS19 disruptions, suggesting it acts after the ribosomal protein.
Miscellaneous:
MISCELLANEOUS: Present with 1390 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus.
Sequence:
MAGHSHRSSLKNGHKSYKSKHASKGALKRLYKGKVEKEPVGTGKPDKQVSKLQRKNKAKQLRAQRILDSIENRKLFEGKNGAAKIITIVPLVNDLDPLDILYKLLKCADDEGIMVQEVDSKRIFNVHIKKFKSNLKIIIPDMTNFLNILDCAKVADFVVFGLSGVQEVDEEFGEQIIRALELQGIASYIGVISNLSAVHEKEKFQLDVKQSLESYFKHFFPSEERVYNLEKNSDALNVLRTLCQRLPRSINWRDNRGYVVADFVDFVETSPDSGDLVIEGTVRGIGFNANRLVHIPDFGDFQLNKIEKISESSQKRKIIKEKATDSLSLELDLQTVFESNMNRDTLDEYAPEGTEDWSDYDEDFEYDGLTTARYDDHGFLPGREQTSKKAAVPKGTSDYQAKWYLDDVIDANEEEEAEQTNGKDETMMEIDDEMMVEQDNEEVAGDEEYDIEDNEGFEELSPEEEERQLREFRDMEKEDREFPDEIELEPSESAIERLKRYRGLKNLYNCDWQVDEKDPSSPAEWKRLLRIGNYKNTKNRIIKETKNEAQAIAGDRIRMFIRFPKFLLEKIQDPKQLLFAVYGLLLHEHKNAVVNFSLQRWEQYDKPVPSQEPIVVQYGVRRYTIQPLFSQGSNSPNNVHKYERFLHPDTVSVATCIAPVDFTQSPAIFFKPSPTDAKNIELIGHGTFLNADHSRILAKRAILTGHPFRFHKTVVTVRYMFFRPEDVEWFKSIPLFTKSGRSGFIKESLGTHGYFKATFDGKLSAQDVVAMSLYKRMWPMPSLPWNGM
The following text describes a protein:
Function:
Catalyzes specifically the acetylation of the epsilon-amino group of a highly conserved lysine residue in acetyl-CoA synthetase (ACS) and of the universal stress protein (USP) MSMEG_4207. Acetylation results in the inactivation of ACS activity and could be important for mycobacteria to adjust to environmental changes.
Sequence:
MAELTEVRAADLAALEFFTGCRPSALEPLATQLRPLKAEPGQVLIRQGDPALTFMLIESGRVQVSHAVADGPPIVLDIEPGLIIGEIALLRDAPRTATVVAAEPVIGWVGDRDAFDTILHLPGMFDRLVRIARQRLAAFITPIPVQVRTGEWFYLRPVLPGDVERTLNGPVEFSSETLYRRFQSVRKPTRALLEYLFEVDYADHFVWVMTEGALGPVIADARFVREGHNATMAEVAFTVGDDYQGRGIGSFLMGALIVSANYVGVQRFNARVLTDNMAMRKIMDRLGAVWVREDLGVVMTEVDVPPVDTVPFEPELIDQIRDATRKVIRAVSQ
The following text describes a protein:
Function:
Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase.
Subcellular Localization:
Nucleus. Cytoplasm. Chromosome. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, condensin associates with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase.
Sequence:
MSCIQIISSSQTSIAGHRKLCNKLFTLRTQEGFETDILRALNIILTVKKGNSNADRVLRFLVTFVNYLQQKDPEIDIVQPILKHILRGLDAKDKTVRYRCCQIIARVVNCVKEIDDDLYNTLKEKLLSRVLDRESIVRLEAVVALSRLQEDTGDEENDVRNILLFLLQNDPSSEVRRSVLLNIEVSNSTLPFILERARDVDAANRKCVYARVLPKIGDFRYLSIKKRVRILKWGLNDRDESVEKAAADMLAYQWIENADNNLLELLERLDVSNNSDVAVLAIKKFFDVRVDSLSQLEFPEQFWLELTAESSLLARTFNEICIEKNYTDLLDKMPEVVQLTYYIERQYVSLRDKSSYDESCFIIEQLLYIGLSQDMVDEIGRRKLLKSLTNSLSTMALPDSLISLHIELLRKLCSSENDFCSLLVEIITEVFEQGHSQNQTEEQGNSNAPELNKNDYEGEEITVSQKSPSPSLPPNELNEPEPDDMDGYKEAFNELRCLSYVQCLFENITSSLNENLYMVDMLKTLIIPAVRSHDLPIREKGLECLSLVCLLNADLAFENVPLYLHCYEKGSVVLKCTAIRTLTDMLIQHGKAKFTEYEDAISSILFEALGEFENAELQTLGAEAIAKLLVILHYRDELFLKPLIIQYFEPNTVDNHALRQVLGYFFPVYAFGAHENQWRIATIFCDALLSLLEIYRDLDEDDVQLSIGHIAQQMLDWTDNEKLYERKTQTGDDYIALNHNVHLHLANMIFESLPNASEGKERKFMISLLGKLKIPTDLPSSDYQRTKRKLETYESHGFTMDSTSLSILAKFERMLLQNEEARSKFEETEEERLMENAEENEHAGAEAISGEIIPDTVEANMEDEEEVYVKQEEDL
The following text describes a protein:
Function:
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MPFTDQPQLLLFFLFASVMILSSLGVIFHPNPITAAVLLVLSFFSLAAIYAVMNAIFIATMQLLVYAGAIMVLVVFVLMLLSLRDDAPRFFIFEKPIKKLLYLGLVMFLGVLLITAVQDGIPSETTVPIGYAQNKDGKFVGYSFQISKNIKQTNTKSTLETPKTTSENQNHVHEKDTDQIILTSGNTAAVGSAMFLRYLLPFELISILLLAAVLGAVVLGKKNLGRNTEGETL
The following text describes a protein:
Function:
Has antibacterial activity against several Gram-positive and Gram-negative bacteria. Is weakly active against yeasts. Acts by a nonpore mechanism.
Subcellular Localization:
Secreted.
Sequence:
MFLMYLLVQTTESSWLSKTYKKLENSAKKRISEGVAIAILGGLRHRRSVAHQEEASLHVKTDELPSPDTVREQL
The following text describes a protein:
Function:
Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. May be involved in the regulation of iron metabolism. Associates with RNAP core during early growth phases, association decreases as cells age.
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Sequence:
MEETFQLLYDTYHQDLYQFLFYMVKDKNQTEDLLQEVYIRVLNSYHTFEGRSSEKTWLLSIARHVAIDWFRKQQTIRQRILGTFDWDTQDVRDQQLLPDELAVQHENVREIYAALDQCTIDQRAVIILRFIQGYSIQETAKALRFSESKVKTTQHRGLKVLRKHMELLREELMDDEVRMERRTDKGVVKSTSGS
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of several pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L-xylulose. Participates in the uronate cycle of glucose metabolism. May play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thereby preventing osmolytic stress from occurring in the renal tubules.
Subcellular Localization:
Membrane; Peripheral membrane protein.
Sequence:
MDLRLAGRRALVTGAGKGIGRSIVKALHAAGARVVAVSRTQADLDSLVRECPGVETVCVDLADWEATEQALGGVGPVDLLVNNAAVAFLQPFLEVTKEAYDMSFNVNLRAVIQVSQIVARGLIARGAPGVIVNVSSQASQRGLTNHSVYCSTKGALDTLTKVMAVELGPHKIRVNAVNPTVVMTPMGQAAWSDPQKAKAMLDRIPLGRFAEVENVVDTILFLLSDRSSMTTGSTVPVDGGFLAT
The following text describes a protein:
Function:
Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
Domain:
Contains a large N-terminal NADP-binding domain, and a smaller C-terminal substrate-binding domain.
Sequence:
MNYIVVTGGAGFIGANVIKRLNELGEEKILVVDNLNKSEKWKNLVDLHFEDYIHKDKFIEEIKNNNFNNSVKTIIHLGARSSTTEKDVDFLMINNYEYTKELAKWSLRNNVRFIYASSAATYGDGSNGFSDEHSLLPILKPLNAYGYSKHIFDLWALKNGILDKIVGLKYFNVYGPKEWHKGEMRSMVLKAYEQIKKDGKIRLFKSYHNDYKDGEQLRDFIYVKDAVEMTLFFIEKTEINGIFNIGTGIPRSWNDLAKAVFESLGIKPQIEYIDMPEEIKGKYQYFTKADMRKMIETGYNKPTLSLEEAIKDYVLNYLEKY
The following text describes a protein:
Function:
Probably specifically methylates an O atom of its substrate.
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Sequence:
MDGTPGHDDMPGQPAPSRGESLWAHAEGSISEDVILAGARERATDIGAGAVTPAVGALLCLLAKLSGGKAVAEVGTGAGVSGLWLLSGMRDDGVLTTIDIEPEHLRLARQAFAEAGIGPSRTRLISGRAQEVLTRLADASYDLVFIDADPIDQPDYVAEGVRLLRSGGVIVVHRAALGGRAGDPGARDAEVIAVREAARLIAEDERLTPALVPLGDGVLAAVRD
The following text describes a protein:
Function:
Central component of stress responses that interacts with poly(A)-binding proteins. Negative regulator of abscisic acid (ABA) responses, including resistance to drought and freezing as well as stomatal closure regulation. Mediates resistance to the bacterial necrotroph pathogen Erwinia carotovora subsp. carotovora and promotes the induction of marker genes for systemic acquired resistance (SAR).
Subcellular Localization:
Cytoplasm.
Domain:
Contains a PAM2-like motif, which seems to be involved in the binding to the PABC/CTC domain of PAB proteins.
Sequence:
MAMVSGRRSTLNPDAPLFIPAAVRQVEDFSPEWWQLVTTSTWYPDYWISQQQQGADGFYDNGENENGGGHIDVADLLPESFDFDDMEDFFDTDAAEFDQGFDGRMYYQAPSEFGFGKNGEMVKKSSGNRSPRSIVEPAKYAEKPAKWGNQRVAAAPRNIHQPR
The following text describes a protein:
Function:
Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane.
Subcellular Localization:
Endosome membrane; Multi-pass membrane protein.
Sequence:
MHARPPAHTDDAPAQVRYRQGRTTCVRATASPVLRAPVNPAMAVASPRRGRGRGGAVALLLLPVLLLACRAPAAAGFNTEFEEDKSPKLPRCDNPFQKVKVMYWVDGEQMSALIGMTARFGGMVPDTAAAAPKLPAVIPSSKTGCQKSPQLAGNIAVTERGECTYLEKANAAASSGAKAMVMANDIDDVGKMVCSKNDTALDFKIPVVIVSRSNGLKIFEAMDGAKKVEMQLFSPNKAAFDAAIPFLWLMAVSTTACAAVWTAVVVGEEEKKAPPEGDQEAAKTEEPEIVELQAETAFVFVIVSSCVLLFLFFFNSIWSAWLMVGLFCLGGLQGLHFLASTLIVRACKKCGDTKIKLPAVGNVTAVTLVVLPIALFIVIMWATHQTSPFAWVGQNLMGIGMMILVLQIVQMPNIKVASALLISAFLYDIFWVFISPLIFKKSVMITVAKGTDNGPSLPMVLKMPKEFDVWNGYDMIGFGDILFPGLLVAFSFRFDRSHGKGVGNGYFPYVMIGYAVGLSCTYVGLYLMKSGQPALLYLVPCTLGTIAALGAQRGELSQLWNAKA
The following text describes a protein:
Function:
Transcriptional repressor of genes that require a bHLH protein for their transcription.
Subcellular Localization:
Nucleus.
Domain:
Has a particular type of basic domain (presence of a helix-interrupting proline) that binds to the N-box (CACNAG), rather than the canonical E-box (CANNTG); The C-terminal WRPW motif is a transcriptional repression domain necessary for the interaction with Groucho/TLE family members, transcriptional corepressors recruited to specific target DNA by Hairy-related proteins.
Sequence:
MRLPRGVGDAAELRKSLKPLLEKRRRARINESLSQLKGLVLPLLGAETSRYSKLEKADILEMTVRFLREQPASVCSTEAPGSLDSYLEGYRACLARLARVLPACSVLEPAVSARLLEHLRQRTVSGGPPSLTPASASAPAPSPPVPPPSSLGLWRPW
The following text describes a protein:
Function:
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Domain:
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Sequence:
MSGLCFLTPAKKMVLLRAAGRVHHYPLYRRLASQLSANHILRNSPSEKQKQHVAYVHTSPKTSAGSLRPGQSKDFLQASQVRKKFLDHFQGLNDHVFVPSSSVIPYGDPTLLFTNAGMNQFKDIFQGTIHPDMVQNCYRRVVNSQKCIRVGGKHNDLDDVGKDTTHHTFFEMLGNWSFGDFFKKEACTMALDLLTSVYGLPLENLYFTYFKGNSELQLGADEATRQIWLDLGVPEDRVLPFGMADNFWEMGAVGPCGPCTEIHFDRHGNRNASHLVNLGDPDVLEIWNLVFMQFYRNEAGSLHDLPKHHVDTGMGLERLVSILQGVPSSYDTDLFQPLIKRLEETCPVRPYQGLLGEKDQDHIDTAYRAVADHARMLTVAIADGCRPDSQKRGYVIKRVIRRAVRYATEKLQAPPGALGSLVHLVVISLGNTYPELEEDPVYIADVINNEEEQFLTTLKKGEKYLKKAITELSPRTVLPGDIAWKMYDAYGFPLDLTTLIADENGLGVDIEGFEKSRLESKEITSRGGIKNQQNLSNIKLETTDISHLHELSVKDTDDSYKYNYQHHRRGKYTFPRIHAHILALKTPEGFVESASSGEECAIILDRTTFYAEQGGQQWDEGSFVSADDEELMFSVYDVQSYGGYVLHLGTTAETVSIGDHVTLYVNEERREKLMRNHTGTHILNFALRQVLGHIEQKGSSVAPDRFRFDFNAEKSISDRQLQQISSIANNLISNSLPVHQESIPLQKALAIEGLRTMTGETYPDPVTVVCIGHQDGQLNGDMTKLGMETSLELCGGTHVENTGHIRRLVIVSEKLVSKGVRRLTVVTSNDVMLADYTSNKFLQRLSQLETEVYNASTSNNPEMRDDVIASLESLVEDLEGAHIDLWKKREMNRRVADMQNKLKKADKLNKKSVIKQVAKRLHEEFREKKSEVCLVGVTGDSIDNKVLLKVQQSLEDEFGSTPLMLLSTDKEKAYCICRVPQELVSRGLHASQWMDSVMGEMEGKGFGSETFARGRGLAPSSLEECAKKARSYVVQRLEEDT
The following text describes a protein:
Function:
Single-stranded DNA endonuclease involved in excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Essential for the incision step of excision-repair.
Subcellular Localization:
Nucleus.
Sequence:
MGVTGLWTVLQPCARPIKIETLNKKRLAVDASIWIYQFLKAVRDKEGNALRNSHIVGFFRRVCKLLFIGIKPVFVFDGGAPVLKRQTINNRKSRREGRREDAVRTAGKLLAIQMQRAAEEEEKKRKEAVRHPRNQEEQEAIPENLVYAEEILQSQQERTENRKFKKKDQYHLPDLGKSMNEMGGADDPRVMSLEELEEYARQFDRGEDINVYDFSKIDFEGHFFQSLPAADRYNILNAARLRSRLRMGYSKEQLDTMFPDRMAFSKFQIERVRERNELTQRLMNLNGMNDDMVGVGGANRVAGERGREYVLVKNDGVEGGWALGVVTNRDEGKAHKPIDVDLPPPAEEDEDWEEDEDFEDVPIEGLNRLPKPKPGLSAEDKEGREFISNELAKRRRKFYNSRKPRPTQPRPRKVSPVNQDPDSLFLAEENEDEEWENVPAADDAELFEDAGDDVEDDMLQQAIALSMQPNGDEEQVAEQSEDDPVREVFQQKRAADANPFAGVKGRGLAIARLANQRSSKLAPKGPFEGSDSEEDDMNLQAALAESRKSKRPVKPRNSILGKKKMEKIEAENAGGFEKKLDQDKKDAAPLPPWFAGERDLGNDLQAQREEEKQQWEEAKQEEKARFQFQELPTIRKQDTREVIDLDAPPSQAQSQEVVAIDSDEEDALMEDAPAVDAEVRIGDLADKLRAEPPKPLSPQQGSPPRQNPALVKKTPFADDSDDEPVDWSESEPEDEKRAQATVKAAEVAEQPAPREPTRSPSEEFEDVPMDNPKTTNDLPKVSSPQTNGQHTAETVAQPAKSPSPDFEDVPIRTEPPSRPKRRHRSPSPAELQGPDDLDIPIVPYGGIAEDTAHLDIPGNDSDQYSDPEDAELFASLAAEAEEHERFAKEVTNNAATKVNFDEELKSLRAQQKKDRRDADEVTQSMITECQHLLTLFGLPYITAPMEAEAQCAELVHLGLVDGIVTDDSDTFLFGGTRVYKNMFNAAKFVECYLANDLVSEFSLTRDKMIAIAQLLGSDYTTGIPGIGPVTALELLAEFPDLQDFKDWWTGVQNNTIPKDADKNSAFRRRFRRGQATKLFLPPGFPDQRVADAYLHPEVDSDPEPFQWGVPDLAALRTFLSSQIGWSWERTDEVLVPVIRDMNRREKEGTQANITRFFEGGVGAGAFAPRVRGAEGPSGKKKGKGAAGKRLGAALSKLAEREGARGGVDDEGEGEVQPKSLAGAAAEEESVTATRKKRKGGSKATSVADEDDFAAEEEEDEAYEEPKKKRARKTRKGKAA
The following text describes a protein:
Function:
Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation.
Sequence:
MASLVRSLSNKVKKRPADEPTIPTPEQQILEEQSVAIDGDPVVRRSALSEHLMATYYDDVTTAYEGFQRGCRIAGDLPCLGKRGDKIGMYRWLSYNEVRERAHSFGSALVHLGCHPSQRTFVGIQAKNCVEWVLTDLACQMFSMVSVPIYDTHGPDACLFIINHADVETIVCNHTKVPFILKNIKRIPHLKCIIQIGELVKEEERKDAKVSGIELLSFSIAEEIGRKNIKVVNPPKPNDIFTICYTSGTTGTPKGAVQTHSNVIADVSGVIRQYNTCGIDVHFSYLPLAHAYERTGVICMLQSGCRIGFYRGDPQLLFEDIQELKPTFFASVPRIMNKVYDKVMAQVSESKFKSWMFQKGLHAKKADMNKNVFRSNTIWDKVVFKKVQMLFGGRVRAITSGAAPLSPKVMTFFRCAMGDCRIMEGYGQTECTACASLQLPQDMQAGIVGPPLTCNYIKLVDVPEKSYSTKDLKGEVCIKGPNVIPRYHKNPEKTAETLDEDGWLHTGDIGMWLENGALKIIDRKKDIFKLAQGEYVAPGKLENIAQRSPFVAQAFVHGESLKTFVVAILVPDGEVLKKWAAQKNIQGDLKTLCEKEEVRQAVFEDVVRVCKEAELFSFEQVKAVHLHPEAFSVENDLMTATFKIKRPQIIKAFHDVIESLYHEVETKGERPRNEVNLNLEMKGKAGNESNVYTDAR
The following text describes a protein:
Function:
Plays a role as a transcription factor. Mediates positive transcriptional regulation of several chaperone gene during the heat shock response in a HSF1-dependent manner. Mediates negative transcriptional regulation of CDC25B expression. Plays a role in the dephosphorylation of the heat shock factor HSF1 and ribosomal protein S6 kinase (S6K) by the protein phosphatase PP2A. Involved in the regulation of cell proliferation and resistance to thermal stress. Involved in the cell cycle checkpoint and survival in response to ionizing radiation. Associates with chromatin to the CDC25B promoter.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Predominantly cytoplasmic. Translocated in the nucleus during heat shock.
Sequence:
MEFKLEAHRIVSISLGKIYNSRVQRGGIKLHKNLLVSLVLRSARQVYLSDPCPGLYLAGPAGTPAVPPPQQPGEPVAGPPSGWGEPPPPVARAAWPEPEPQPQPQPQRPSVCHTPGAGSSEPVAAVAGSGEALRGGEEDSAAAAWGRVERPRAASSGGGSDACPEGPRAVRRPCGCPPAVEERSSEDGSPAPPAPCPRKRGAAGVGGGRASCSAPGSTPLKKPRRNSEEQPVTGEDDTDEEMETGNVANLISIFGSSFSGLLRKSPAGGREEEEAEEGGPEAAEPGQICCDKPVLRDMSPWSTAIVAF
The following text describes a protein:
Function:
Subunit 8, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). Part of the complex F(0) domain (By similarity).
Subcellular Localization:
Mitochondrion membrane; Single-pass membrane protein.
Sequence:
MPQLDTSTWLLTILSMLLTLFVLFQLKISKHSYSPNPKLVPTKTQKQQTPWNITWTKIYLPLL
The following text describes a protein:
Function:
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Subcellular Localization:
Cytoplasm.
Sequence:
MNDQIILALDVGERRIGVAISDADARIAAPLTTINAHPPERAIAQIVRLVQERGVSRVVVGLPLTMRGERGPQAEVVQRFADTLSSALSCPVEMFDERLTSVAAEQMLRNLGLKPAKIKAQIDQVAASIILQDYLDARRSNPNRSHELPHSSD
The following text describes a protein:
Function:
mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
Subcellular Localization:
Cytoplasm.
Domain:
The RNA gate region regulates mRNA cap recognition to prevent promiscuous mRNA-binding before assembly of eif3d into the full eukaryotic translation initiation factor 3 (eIF-3) complex.
Sequence:
MSSFNLVGVINNRTWGPDSKNEELVNYCMPDIKKYQFEPSMKFERIGKVCDFTMNSYQKNTKDINKNSNDVNAFEEELQFQTVDLRTGQKQKGSIFNKKKIHNKQNTTQAFTQKQQEEDNLYSSRIKTAEQKKQKLLQQAKTARINARHRIFTEWSIEPTPLWTVECEIMFNELPKKIIKIDNLKVEDLFFKGKSLFYDKKIENINVKNPPLLFHHTKEGINLIPKTKEDHNLINILNNENKNKIISNEEDPNNINNIIVISTDQILSCLMSCVQSKYSWHLLIKKKGNQIIIDKDDDSIIDLLTVNENSIDAPTQDNENKINSLQALGIEAVKINQRFRKQVILKNDIAEEFEPGNFNIKNIKINDILYRYRKFQIPPLVQSNNKKTYTLITRGEIHSQIKGLNKSYVYVCALNEYDIKSHKNWRSQIENQKGALLANEIRNNTSKLQKFISQALLSGCDDVKLGFISRKNANDPDNHHILSIQSHKTKDLSTQIGLKYDNMWGIFRFVIDNLADKPNGNYVILKDPLKPLLRLYCTHEDSN
The following text describes a protein:
Function:
Together with the cullin protein ANAPC2, constitutes the catalytic component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins. May recruit the E2 ubiquitin-conjugating enzymes to the complex.
Subcellular Localization:
Nucleus.
Sequence:
MKVKIKRFHSGRWVGVATWKWMANDDNCGICRMPFDGCCPDCKVPGDDCPLVWGRCSHVFHMHCILKWLNSQLHQQLCPMCRQEWQFKE
The following text describes a protein:
Function:
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MNQRNKIQGCCSNLSLPQLTKKTDENCAKTLKQITPTNTLKKIGDFQGCGRSTSQLNNAILNNLYDQASQKSKVGDKPRKDMCSRAHTIYQQQQNDDQLRKQIQYNDYFIGGIKEILGKEICAQNLKQMCIDQLNQIYKNVTCKDQTFISKKQLPNIVLTKKYSIAIDLDETLVHSEELKPNRRYDFQNLQFGTFIRPYCLQFLQLLNKHANLFVFTSSNIKYATTIMQILDPQKDLFQGLFFRDHCTILQDNSQVKDIKIISSDLTKIILIDNNPQCFIPEPFNGIPIVPFLDNKADKELLILSQFIEREIFTSEDVQHVIKRFFQFQQFRQFENGMQAYQILYN
The following text describes a protein:
Function:
Single-stranded 3'-5' DNA helicase that plays a key role in homology-driven double-strand break (DSB) repair. Involved in different DSB repair mechanisms that are guided by annealing of extensive stretches of complementary bases at break ends, such as microhomology-mediated end-joining (MMEJ), single-strand annealing (SSA) or synthesis-dependent strand annealing (SDSA).
Subcellular Localization:
Nucleus. Chromosome. Note=Localizes to sites of DNA damage.
Sequence:
MNRTPIRRCKSAEIEEDPFSPIPKFSRLRTPRTSREYVCPLKSTSPQSPSSSTENEPPPVSVTSPPARKRALEESTVTPIQQKIGPPVLKRSSLSKLADGFRTAAYLNNESENDDDPFGLSFRNEQVLMSKCAPAPEKRPETLTLDPSKCLPERDMEMYRKIKKLDKFYDWQQECLSDKRLLDGENCILSLPTGAGKTLIAEVLMLREAIVRKRNAILVLPYVAIVQEKISALAPFEDAFGINIEEYASNKGRFPPIKRRKRVSVYVATIEKANMLINSLITQGQLDRVGMVVVDELHMIGDGGRGAILEQLLAKFLYKGTGQIVGMSATLPNIDDLKFALRAFVYSTNFRPVELTEFVKIGQTMHQVSENGDLNPAGDLPTNNLKSTDPDGICQLLAKLIPKNSAVIFCPNKKNCENVAVLIAKTLPAHIRQAKRAESDAFLQSYLSDNDDERMDAVLKQCILSGVAYHHSGLTQDERKCVEAAFMEGLIYVVCATSTLAAGVNLPVRRVIIKAPMVGRERLGKAQYLQMAGRAGRAGFDTKGDCITIIKAGEEERWFREMLKSDIPRCMSSLSSEESMGSFILDCVVLKLAENIEEIMTAVRYSLFYAQESPENIRKLVESSVKRLEEHYFITIEPLEQDVASEPSAQASSIPRVPGKISPSDLGNAVFNAGFDPDEATRLHADLVSSLNQGVIFASHFHLLFIITPYEQVCNINWDLFLLMYNALPSSERKLLAECGLEEKFILEAIITRVDLTAGTPRMRLYIALMLQKIWNHEPMYTVAERFGVEKGWLQATLQSSISQAASIAKFSEKITTMWPLRKLLPELVQRLSEAAQPELLPLMTVDGIKKARAAILFKAGYKTVGMIARANPLKLVQELGTIRMAQANSIIASARMVLRDQVDEKMEELDVWGVATDSFNYF