lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May play a regulatory role in autophagic activity.
Subcellular Localization:
Cytoplasm. Preautophagosomal structure. Note=The BCAS3:PHAF1 complex is recruited to the preautophagosomal structures adjacent to the damaged mitochondria upon mitophagy in a PRKN-PINK1 dependent manner.
Sequence:
MLDLEIVPEISLGCDAWEFVLGMHFSQAIAIIQSQVGIIKGVQVLYSDTTPLGVDIIINLPQDGVRLIFDPVSQRLKTIEVFNMKLVKLRYFGVYFNSPEVLPSIEQIEHSFGATHPGVYDAAKQLFALHFRGLSFYFPVDSKLHSGYAHGLSSLVFLNGASPVVSKMSLYAGSNVLENRVPSLPLSCYHRQMYLESATVLRTAFGHTKGLKLKLFTEGSGRALEPRRQCFTRELLFGDSCEDVATSLGAPNRIFFKSEDKMKIHSSSVNRQAQSKRSDIFFNYFTLGIDVLFDARTQTCKKFILHTNYPGHFNFNMYHRCEFQFLLQADHPSMSDSGHDLVTPTKQEHVNITAYTKWDAISSALATSERPVVLHRASSTNTANPFGSTFCYGYQDLIFEVMPNSHIASVTLYNTAPPRQPAHSWQQHKMQDIRLTVA
The following text describes a protein:
Function:
Involved in auxin biosynthesis. Belongs to the set of redundant YUCCA genes probably responsible for auxin biosynthesis in roots.
Sequence:
MENMFRLMGSEDSSDRRRCIWVNGPVIVGAGPSGLATAACLREEGVPFVVLERADCIASLWQKRTYDRIKLHLPKKVCQLPKMPFPEDYPEYPTKRQFIEYLESYANKFEITPQFNECVQSARYDETSGLWRIKTTSSSSSGSEMEYICRWLVVATGENAEKVVPEIDGLTTEFEGEVIHSCEYKSGEKYRGKSVLVVGCGNSGMEVSLDLANHNANASMVVRSSVHVLPREILGKSSFEISMMLMKWFPLWLVDKILLILAWLILGNLTKYGLKRPTMGPMELKIVSGKTPVLDIGAMEKIKSGEVEIVPGIKRFSRSHVELVDGQRLDLDAVVLATGYRSNVPSWLQENDLFSKNGFPKSPFPNAWKGKSGLYAAGFTRKGLAGASADAVNIAQDIGNVWREETKRQKMRTRVGHRRCISVA
The following text describes a protein:
Function:
Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination.
Subcellular Localization:
Nucleus.
Sequence:
MDIFQPKTNHFSESIAVICRSNQNRSISAHCRLKQLGYNVSSFGTGVYTILPGATRNFGFQFGIPYKDIKNSLPKDEASVEYYRKNKIYQMLDRNANLKSAPEKFQDCKKEFNIIITLDYSVFMDVLEYFDSRESSTGSLCYVFNLTVMDQLDTAEKGAIEVSEFLKLMESDSDWMNNIDHVIKSFYSKTKINVLHSMQMY
The following text describes a protein:
Function:
Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Subcellular Localization:
Nucleus. Chromosome, telomere.
Sequence:
MASKRKRNHAVTSTGADTGNGNGNDTGLADSNKRQRTSGDGYSKDPPVKQALLNKYYPNVLCLRDYLLSKLPVSSKVRRKKLSSVGRKASANIPYQDGDDDEDEDRVLGDFLDAMKAWPWPHVLSLLGKAGEHVMSDLILDCGVFLQIKNTHGSYYQLSGQPLGEILPITNGKHHGKESGADSGSKKDQQPGILHNPMEINFVRNRMLYAKAALNAQGEVQFGLRHIQVDNRETVQPFKDYTLREEEIDSKYPEAKGIKIPKRLRGKAKDLNRKHEDGNANRIQEEPSFNSTSLKIQSYRKCHSSSILSSSAPSIPARKSTLMDHASSTAEVSAFCRAVLRNIIPHEFWGMGDVQAHNESIFHKNVDNFIGLRRFEVLSLHEVMQGIKETGVRPIMNLRRRAMRKGDKHLLGVSINSVLTPVHNVLTYEKANNLTRLGSTLFSVGDLYQKVKSFKASLNASTKPLYFAKVDVQAAFDTIPQVAVIKLMKTVPSEPEYRFSRHVEIKPTDAYNIDPNAPNKPIRRWKSNAKSMHHLDNFDEDLENDIAIGKKNTVFVENIVNQIRDTNSLLHLLTEHISQNMVKIAHAKRFLKVMHDGIPEYGVGVNPDKTLTNFEVMIYGKKIKRIVGEKMFPYCGNLIDMKTLNIARDRGRGKDLAIQDSLTVEYSRIPGKTFHRKVLNSLTLQTHPMYLDTSHNSLPTVHKNIYTSYLESATKMTSYIKCLPVSKKPKCALIIRTIGDLVALGWCLSRRGGRGRESGDEEGRGEDGRGKYKGYKCEVQKWEMRRLALGAFLEVMRRRQCGYGGVVEWLVRELGGLGGGVVMKR
The following text describes a protein:
Function:
Regulatory subunit of the GMPPA-GMPPB mannose-1-phosphate guanylyltransferase complex; reduces the catalytic activity of GMPPB when part of the complex. Mediates allosteric feedback inhibition of GMPPB catalytic activity upon binding GDP-alpha-D-mannose. Together with GMPPB regulates GDP-alpha-D-mannose levels.
Domain:
The N-terminal substrate-binding domain adopts a Rossman-like fold and has a binding pocket for GTP or GDP-alpha-D-mannose; The C-terminal domain consists of a series of tandem hexapeptide repeats that adopt a beta-helix conformation (By similarity). The beta-helix forms several protein interaction surfaces involved in assembly of the GMPPA-GMPPB mannose-1-phosphate guanylyltransferase complex (By similarity). Vertebrate orthologs possess a loop extending from the C-terminal domain (C-loop) involved in interaction with other subunits of the GMPPA-GMPPB complex and involved in allosteric inhibition of gmppB that appears to be absent in Dictyostelium (By similarity).
Sequence:
MTTTTTKAIILVGGPSKGTRFRPLSLDVPKLLFPIAGKPMIYHHIEACSKVENMKEIILIGFFQESVLSKFISETSKQLNVAIRYINEEKVLGTAGGLYHFRDIILEGGPSEIFVLHSDICCAFPLNDLLQFHKQHGRSCTIMGTEIESAYANQYGCLVRDEKTAELLHYAEKPETFVSNLINCGVYCFSPQFFDVIGKTMIDLKTSGQNITTDYPEITRKGFDVERLRLEQDIFVPLAGTGFISVYPYVGFWRQIKNAGSSVYCQELYLNHFAKTKPEVLKKGNNIIGNVIIDSTASVDPSAIIGPDVYIGPNVKIGKGVRVIHSIILDQTEIKDHACIIYSIIGWQSLIGVWARIEGIPNYTPFLYSQDKRRGVTIFGAGAQANGEIIVSNCIVMPHKQLDRNYNNEIIL
The following text describes a protein:
Function:
Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
Sequence:
MSLSSHIVNPEDERDVPILKEDQDRINEFARLHAKQTELTDNYKASQDRAEGYNDASEELMLQDDESIPIAVGDCFFMLETDQANELLENGKEAAEAEMEGLREKVGEIDDRLVELKGVLKAKFGNSIQLD
The following text describes a protein:
Function:
Involved in the organization of the mitochondrial membranes and the global structure of the mitochondria. Also required for mitochondrial distribution and mobility as well as for the maintenance of mitochondrial DNA nucleoids structures (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MLESRLAKNIARIVQARKPYLISYHVRASTQNALLKQTVLQSSSFKSFPTLPRLAARNISNSGILSRTTPVIIKQISMVRSYSSGDVENPEILNKNESNQSSGVKRAMPFRVLKKMKSFLFKQNKPLTVDNVTAFFSWWLVSHIVWIVVGTTTFFSLLLYTLNTVSAQELLGRWIGQLMTKNTGFQFVFESAIVPNWRKGLITFNKISVIRRPDTLNGIGAQNPNNKSDYEKEYMALRKRYDSNEEPDTEALSQGNYTQFELSIDKADVSFSFARFLNGKGIVKELQLKGVRGVVDRRFIEWDPSSDPRDYRRKHNWGDFEIEKFKLEDLRVTLLQPKGFRKFPVSVFFCELPRLRKQWLFYDLMNAKTLTGSFDNSMFTIHRLQLRPYSPYLKVGKQLDDMRHSRLRIDNVAIDHLNRGVSGAFGWINDGSVDFLVNISFPSEPSENSFQKAWISLMDKLKKKEKDEDVYKDVHFDVNVQLHNPKAVIPIFTNQVSYINNALIRPIIAYINSTRTFIPILCHVSKPLSDFDGSWTFYDSGVLQEISAQVYESFARDVLNQEIRRKRIQKVGYWSLRRFLHLVLVSLQELAPTTSSISNFE
The following text describes a protein:
Function:
Pre-60S-associated factor involved in the cytoplasmic maturation of the 60S subunit. Involved in the dissociation and recycling of other late pre-60S factors like ARX1, TIF6 and ALB1 before newly synthesized large ribosomal subunits enter translation. Cooperates with the co-chaperone JJJ1 in the release of the nuclear-export factor ARX1. May act redundantly with REH1 to directly promote a stabilizing structural rearrangement in cytoplasmic 60S subunit maturation independent on ARX1 recycling.
Miscellaneous:
MISCELLANEOUS: Present with 830 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MSSSGVYTCNSCVLTFDSSDEQRAHMKSDWHRYNLKRRVAQLPPISFETFDSKVSAAAASTSKSAEKEKPVTKKELKRREKQALLEKKKKLLEIARANMLENMQKSQEGNTPDLSKLSLQENEENKEKEEPKKEEPEQLTEEEMAERVMQEKLRNRVDIPLEQCLFCEHNKHFKDVEENLEHMFRTHGFYIPEQKYLVDKIGLVKYMSEKIGLGNICIVCNYQGRTLTAVRQHMLAKRHCKIPYESEDERLEISEFYDFTSSYANFNSNTTPDNEDDWEDVGSDEAGSDDEDLPQEYLYNDGIELHLPTGIKVGHRSLQRYYKQDLKPEVILTEGQGTLVAAETRSFLPAFDKKGVQTQQRVWQTERFDKKRLDKRSAKFVNNQPHYRDQLLQ
The following text describes a protein:
Function:
Plays a regulatory role in neural branching of the tracheae: segment-specific aspects of these neural branching patterns appear to be generated by homeotic regulation of expression.
Subcellular Localization:
Nucleus.
Sequence:
MERPALLQNGEHGAVGSLETKTTTRLMPKPFSIESLIATQTPATVSASASIAASPPSPPEDHEQEQEQELSARAMVASSALGLTQFPLYNPWLHGYFAQNHERLTHLIAGGGCYLGSPVGNPFAGKEPSHPHPPPPHALDKSPLPHPLDTRFLPFNASAAAAAASAATPTDLSYRRLAELMNQDYVHNLSVNARLQHMAVAGRLQEDHPSHSLMHLQEPMLLQANPFSPAKSVSHSPVEPTLDVGVDEDYECSGDSSSDISLTLSPMPRNCNRELDKSRNGAYTNSDSEDCSDDEGAHSHHDASGLGGKDSQGNGSGSSSSKSRRRRTAFTSEQLLELEREFHAKKYLSLTERSQIATSLKLSEVQVKIWFQNRRAKWKRVKAGLTSHGLGRNGSASGTKIVVPIPVHVNRFAVRSQHQQLEKMCLSGPKPDLRKKLSTEAMSGFEKFNGGGLGGSAPSSSTASVGAGSVGMGLALGIGVTTPLSLGRSIY
The following text describes a protein:
Function:
Has a role in the initiation of DNA replication. Required at S-phase checkpoint.
Subcellular Localization:
Nucleus.
Sequence:
MASTPSSSSQLTQIKTRLKTWERQFKAIEGRAPNKADIKANPEIAKMYSTYNSSRKGSKGSDDLPNSSSSHSNSYQRQILSTPKSKTRSESSKAGGRKPSQENHNSSPSKTYAHANSPSKLRKLVEEHSPRKIHYDRLRNSQGRPGTSTKNTPSHLRANPFDLDSGGGKGSPALFADLLLESKRDTPRTKARKFLVGEASPLKPRLHPPEPLYSASQGLSSGLSSFLKSQPIQPHEKPNLESGLDTLNDDEDDELLGPSPFKPTSHNVFQPLFDEPEVESDDHSLSPSKMIKSKWKINSATPFISQSQSHPSGSGSNNNQAPQCAQKDSGQTGKKKNISFGTKRKRLIMPGEEDLSFYEDLPDPETNDPSKNRSSLLNKKKRVERSNNKNQNKKTGDSTTKTTKAQLSIKKRETNSSKNEAMANESEEGSEESGEEKAILPNLPFGNPDQSAVYTELETFTFTTPDETTGADKGKKTSTASGAQSDGKDKGKAKAIDGAPDPKPIKLGTRKVLVRAYRPIEPSQMSQTIDSDYLGDDRLADAERSRKRTRSDRRQLLRERRRERKVRKILDGMTLMEKTLTNRATTPAVGGPVGPGAVSGKAKSAGGGRGKKKTAGPSRLEPARVAGKTEDQEEEDFRFELALDELEIDQQLEDEAVDLDDDWDDEPAGWKNELLDPGVDDDDDDIHSGLNQFVL
The following text describes a protein:
Function:
Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.
Subcellular Localization:
Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus.
Sequence:
MFTQFGSTAENLSKASTMVFRIGTDAHLYDDPDDVSISPLLDSKFDSEKCEALKRLLALIAQGLDVSNYFPQVVKNVASQRPNEALLSINIFQRDLGDQNPLVRAWALRTMAGIRLHVISPLVLVAVRKCARDPSVYVRKCAANALPKLHDLRLEENATSIIEIIGILLNDNSPGVVGAAAAAFASICPNNLPLIGRNYTRLCEILPDVEEWGQIILIEILLRYVIAKQGLAKESIMASLCPQDEKSDSDPDSNYLEKKKKYEVFSGVNEPELLAMVSRSYLAGQDKYLSNSTTVDVTSSEVDSSRFVSSKSDADLKILLQCTSPLLWSRNSAVVLAAAGVHWIMAPKEDIFKIVKPLLFLLRSSDASKYVVYSLLFQQYYENIKGSRFLQLTQVLCNIQVFTKVMPSLFAPNFEDFFINTSDAYQVKSLKLEILSSIATDESISFIFQELQDYVRDPDRRFAADTVAAIGLCAKRNPQVANTCLEGLLALTSPKSINSTSGSMDDDAVLIQAITSIKDIIKQDPSTHDKAIIYLIRNLDAIKVPVARAIIVWILGEYNSIGNTIPKMVPIILRFLARGFPSESIETKHQILNAAVKVVLNSKGEDFDTAKSILSYVLELAKFDLNYDVRDRSRVLGKLMSCYVSEAQTPENNETTVLLTKHIFGENIKSSNEMMNNRFYLPGSLSQIVLHAAPGYEPLPEPCSLTHVDFEVENSDVVDSGSLNEEGSFDDDSEGSITTDNTHESETESEVDDNTDSLINLSDVGNTQKETGFDSGELMSKGALESWLDENPSSSQNVTGMESVNERNSSARISIGDISGRVKPKTYTLLEPAYGNGLKAVYKYSTDPSTVSPSLVSVEVSFENCSGDQITKISLSDEDSDTNSELQMEEITTLEPGQTTKRIIHVQFHHHLLPLKLNLWCNDKKHLVKLRPDIGYFIKPLPMDINVFLHKESQLPGMFEYSRSCCFTDHLEEVGNEKEEVGDGKIMKDSFLVICESLALKMMSNANVYLVCVNMPVDAKLNDVSGVCLRFSSEILSNSIPCLISVTLDGKCFQPLNASVKINCEETVFGMNLLNRIVNFLGDPPPVTVSS
The following text describes a protein:
Function:
Regulates ADAM17 protease, a sheddase of the epidermal growth factor (EGF) receptor ligands and TNF, thereby plays a role in sleep, cell survival, proliferation, migration and inflammation. Does not exhibit any protease activity on its own.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MRYLTNPRAPEISRSRLVSQTANFFGVGDNCQEDQAKWRRRQSRALSRRHGGIKQGCEPAAPSAEDPFGLPLPHIVDPLARPGRLRDEYDSPRGPLPSQLSTGTATSSILQKQRSQRLIRQRSKRQSVAKMGWELVRNSVKQQPKVQQRPPLIHSRSFAPASMVFDYEDDEEFMDPSQFFSPGVLSDELNDEVFFDFSPKAKRRAPPPSAEPPPIPPPNLRLESDETASEYEEIRERTPRNEDRFRELPRPPPGKLGGFDEVDLAGRPPYKGEYPDPGEDDMYAMPDLPDVYRREPSAGDPLDSRTTNVLQDMIPTGIGWRKPKTEERFKIPPIVSPLPEDLPDGSKPLRRTKIREQIMDMAMDNADRREIGKGLVGRVLNRRYRSRRMDSYVQKQIEEIEDHSRPYFTYWVTTVQIAIMIVSLAFYGFAPIGFSYTQKTGVVLQSNLVMETVGYKEPDNFWIGPRPADLIHLGAKFAPCMHRDEQVFAKIEDAKFIENMTGCCIRSDNAGCVQTSSEECSTRFAMFSKWTPSNPDTNELRTSGPVCGQDPRECKSPSSRPPYEWPDDITKWPICVEPFDSHNQYHTMCEVTGRPCCIGIHGECKIVSRDYCDFVNGFFHEEATLCSQVSCVDSICGLINFFNPDYPDQIYRLWLSLFLHAGIFHCVLSFIMHMTILRDLEKLAGWFRIAIIYIFSGIGGNLTSAILIPYRAEVGPAGAQFGLLACLVVEVFQNWQILRNPCKALLKLLAIIMVLFALGLLPWIDNFAHLGGFICGIFLSFIFLPYICFGEFDRNRKRIQMVVCIVLLVGFFTLGFVLFYIRPITECSWCQYLNCVPITEDFCNDMDVKFEDTVEVQGGIK
The following text describes a protein:
Function:
Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet.
Subcellular Localization:
Nucleus.
Sequence:
MAPSGTVADPPQCSTTDSFNSSDTAENDIRPFFVLHKASSGNHNGKLTGIVKSKRRIESPSPKIAKRSEVESVEEEDGQFFSTLRFKVFETVWSKIEKTIEDVLRNSNSKVFSGIHDWIRESFESIISSGALKLSEAVRSYPVLTQASSKQLLTAMVLTRNLEMVDDLLTFEELELHLKSQGCHVAKLSSMDFSAKSGVGGCLRGLLRQFVMPTVDVADVTILASWYRENKNHENPVVIIVDDTERCCGPVLSDLILILSEWAIKVPIFLIMGVSTAHDAPRKILSVNALQRLCATRFTLSSPAERMDAVLKAVFLKPCSGFTVSHKVALFMRSYFLCQDGTLTSFVRTLKIACLQHFSLEPLSIMLEHFCHDGVNQLSGEGTELLTEATMKHAFDLPSVTRNKITRSTFEMLPHFLLDLQRMPNPWSIVVLCLYEAGKFDKLRLLDIFCEILDPEARYLKYFSPSEIVNSQSHNSGRNNVIRRVLRKLRDLSPSQLSSMLKSWENLTAEFTEINDKVIELHPFMRAVEAAGQRQGLPNSPKKHASRSNSKLEKELKAMTDKVATVIEFMLREYMKPVESVPFHEILCFKNVDKLQSALLGDPRGRIQLDLLESHDILHCVCCSQRGTTLLPSMHDTSILYKLAQEHADVINLHDWYQSFKTILIPRSSKAKQKSKSSSKSKKRKEICEEPEAPAEALIQARFCRAVMELQITGLIRMPSKRRPDFVQRVAFGS
The following text describes a protein:
Function:
Negative regulator of the canonical Wnt signaling pathway involved in neuroectodermal patterning. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane and interacting with key regulators of the canonical Wnt signaling pathway, such as components of the beta-catenin destruction complex.
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Sequence:
MDLHYDCAESPAVEQPSGKINKTAFKLFGKRKSGSAMPTIFGVKNKGDGKGTGKIGMVRSKTLDGLADVVLESNKKEELCTETGASQLNPEKSPTVVTINADVSPNSSVAKSHSFFSLLKKNGKSENVKGEQAEQKPGSRQKRGLKGLFNSMRWSKKDKSYKDDKEGASESQPGLILPSSLTASLECIKEETQKPLCEKGKSNEDIPADVPSVEHSRDVNTSAEENPLKASEESLCSTLITEEPQLEDPPVIQHVDNLCQLPDPEVETLPDNKEEDVTGCGDVIADQDDDGGSSTGSKVVPGNGKKVPSNKNTNIVVYQGGGEEMASPEQVDETYVQELFSMVPQSEGASEKTEKVNGTTQVTSREVKCSDSGHDRKGVKPSKLRQVPIYRKERGDQNSKGNEKRQCLRNSDEGYWDSTTPGQEEEEPRSVGKQALARDSCSGDALYDLYTDPDESIHKAQAEDPPVSHSHSKPLSPVTTSCPVKTSSSNKESKIPISIKHLPVHTTNQGTDSGSGSASGHPHPVKSELPRTKIPVSKVLVRRVSNKVITETAAGKRAIHDPTRKYH
The following text describes a protein:
Function:
Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall.
Subcellular Localization:
Cell envelope. Cell membrane; Lipid-anchor, GPI-anchor. Membrane; Lipid-anchor, GPI-anchor.
Sequence:
MLFKSLLTYISLVSTVLAIPAIEVQGNAFWNTETGKRFYIRGVDYQPGGSSELEDPLADTKVCERDIPYFQELGINTIRVYSVDNTKDHDECMDKLAEAGIYVILDVNTPHSSITRSNSECSYNSDYLQEVFASAQMFAQYNNTLGFFAGNEVINDGASLDSAPYVKAVVRDLKTFIKNRGFRTIPVGYSAASVDEYRLASGLYFNCGDDEMARIDMYGINDYSWCGDASMTTSQYSQQMKDFKNFTVPLFFSEFGCNAKKPRPFTEIEAIYSTDMSSVFSGGLVYEYSEEDNEYGLVKLGDDDDDDDVTPNQDFKNLKNEFNKTENPSGDGGASKDLTGGNNCPSKSSLWNVTEEIPDTPGGAIKYLKGVAEPTGHGFDAYVQGNCHGNNDVDDSGNYTSSVGASTRDASATSSSAQSSSGSSSSSSGSTSSGSKENQGVVAATTSVTGVVGLLALIAGFVVV
The following text describes a protein:
Function:
Glycosyltransferase that transfers a galactosyl group from UDP-galactose to soyasapogenol B monoglucuronide in the biosynthetic pathway for soyasaponins.
Sequence:
MEKKKGELKSIFLPFLSTSHIIPLVDMARLFALHDVDVTIITTAHNATVFQKSIDLDASRGRPIRTHVVNFPAAQVGLPVGIEAFNVDTPREMTPRIYMGLSLLQQVFEKLFHDLQPDFIVTDMFHPWSVDAAAKLGIPRIMFHGASYLARSAAHSVEQYAPHLEAKFDTDKFVLPGLPDNLEMTRLQLPDWLRSPNQYTELMRTIKQSEKKSYGSLFNSFYDLESAYYEHYKSIMGTKSWGIGPVSLWANQDAQDKAARGYAKEEEEKEGWLKWLNSKAESSVLYVSFGSINKFPYSQLVEIARALEDSGHDFIWVVRKNDGGEGDNFLEEFEKRMKESNKGYLIWGWAPQLLILENPAIGGLVTHCGWNTVVESVNAGLPMATWPLFAEHFFNEKLVVDVLKIGVPVGAKEWRNWNEFGSEVVKREEIGNAIASLMSEEEEDGGMRKRAKELSVAAKSAIKVGGSSHNNMKELIRELKEIKLSKEAQETAPNP
The following text describes a protein:
Function:
Probably required for the insertion of integral membrane proteins into the chloroplast thylakoid membranes.
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
Sequence:
MAVWRSCLRASSSRHRLSSLFFSHHLKPSSFISHSPPLFSPSPSPSPTCFSPLHRLLSSGPEFPIGSQEIIPTDDSSLPVLAVVDFLEGFHEFTGLPWWMIIASSTVAVRLALLPLLILQLKKLKTISELLPKLPMPIPETPTLKGSIDQFSHFLKESRAIGCPSFLWFFPYLSVQLPCFFLLMASIRKMSLDGHPGFDSGGVLWFQNLSDLPGGSFGPVFPILIATFHYINIQISFDTSTIRQTTGLTGLLMRYYKLYLEILSVPLFFVGYAIPQGSLVYWVTNSSVNIFQQLSLKHPTVGAKLGLLSQGATPGMGHSMEISESVIKYVDSDSKEQTLSLQTLTPEELLSLSVQVLSKGDKETSIQLLRLALEKDPGYVRGLVLMGQALLQKTQLSEATEYLELAISKLLDEDPSDAEDVELLMLASQWAGAAYVQQGKLKSGIIHLERVAKLREPGDPKSKEHYFEALLLLSSALYKEGQSDEAAKILRVVVDHNPAYKPLLEQCEDENELVSDLVSRRKDHF
The following text describes a protein:
Function:
This protein is involved in the repair of mismatches in DNA.
Subcellular Localization:
Nucleus.
Sequence:
MDVNSRAKIRPLDQLVINKIAAGEIIERPENAIKELIENSLDAGSTSIDVLLKDGGLKLLQITDNGSGIQYDDLPYLCQRFSTSKIDNFNDLQHLQTFGFRGEALASISHVAKVTVVTKLSSDIHAWKAFYVDGALAPISPGMSPAPQPCAGKQGTVITAEDLFYNVRSRKSALKNGSEEFRRIMILVQKYAIHNDQVSFNCKKVGDTVASLSLSSRLSKADKIRHIYGPRVASHLRDFSLGEGQSSIVGFSANGFISNADFQDKKSNLILFINNRLVESVELRHALEETYAKYLHKGASYFVYLSLNMSPEQLDVNVHPSKRIVHFLYDQEIATSICDKLGEILERTDTERSYPLQAMIPSISNTKNAESSSQKAVRTYENYLVRTDPRERSIKSMLSDNFLQRSSNNYDNEIIEKVDSANSNKNATNDIKDLQTEEIVEEGNSIDLESIKSLQKQVINSMHVLATNILTEHKYVGLVCPTRRIAAVQHNIGLYVVDYGKLSYHLFYQICLTEFGNYGEFVLETPLSISDLFEIVNGDEDKSESEKFTRLLVSRRDMLKDYFSISVTSGGLLTAVPMLSPKYHPPFEQLPLLISSLTPKFFDWLDEKSCLNGIMKAIAKFYVPLPLSYEESDVKSIRSLESCLEDYLFPEFRRRVICPKKVFEEKCIYQITSLPRLYNVFERC
The following text describes a protein:
Function:
DNA-binding protein that plays a critical role in nucleoid compaction, genome replication and DNA replication and transcription. Binds to both ssDNA and dsDNA with a binding site covering about 15 nucleotides. Displays DNA-supercoiling activity only when associated with the viral DNA topoisomerase 2.
Subcellular Localization:
Virion.
Sequence:
MGRKDPRKIDGVLKYHPQLVTMGQSVDLDGIAYIMKDKSSLSLGDIQSVLTNYVEAMRAALFDGKSVNIRDFGVFSLSAHTLGATTKEECTVKNIKSIQINFRPSSSVRPNLTSTRAGDKIEFLDLEAPKKKKGDGSGEDNTPGGGGNEGGGGDEEAPDPTV
The following text describes a protein:
Function:
DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities. Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Subcellular Localization:
Nucleus.
Sequence:
MFKDHSFVFLPNGSTPRARIVAQVLRRHGGSLQEGAGDSPITYLVPDQYLTATGEVKNRELFELEEQRPGTWRKGAVRLSWVSDCVKAGQLLNKENYAVKPPQRAEGKRLGKRRRESEHSAAAAAARPATPLEGNAKVACALQQLAERCRLQGEAFRNRAYLLAREAVLELPYSIQTYEQARSLPNVGDGIAQKIALLAAGGSVPGLELELTPDERIVRYFAACHDVGPGRAQQWRALGFESFADVLRASPQWRLPWAMLYGMRFYEDWQLRIPRDEVGEHAAVLEQCAPAGMSVVIAGSYSRGSTTCGDIDVVLYREGCDDPEVLADDLTALVQRLVSIGYVECPLHLSKRLQPLFDPAVHSLARGLGVSVSGRLSEKDTLARFYSGVRLPGKAPVPPGAPAIPYVAQDRELFAPHASGSARPCRRLDLLTCKWSERGACLLYFIGNDTFNKALRTRASAQGMTLNQHGLFDKSSGACVESADEYRIMELLGFPRLEPTDEQRNRRI
The following text describes a protein:
Function:
Required for vacuolar assembly and vacuolar traffic. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion.
Miscellaneous:
MISCELLANEOUS: Present with 1170 molecules/cell in log phase SD medium.
Subcellular Localization:
Vacuole.
Sequence:
MTTDNHQNDSVLDQQSGERTIDESNSISDENNVDNKREDVNVTSPTKSVSCISQAENGVASRTDESTITGSATDAETGDDDDDDDDDDDEDEDDEDEPPLLKYTRISQLPKNFFQRDSISSCLFGDTFFAFGTHSGILHLTTCAFEPIKTIKCHRSSILCINTDGKYFATGSIDGTVIIGSMDDPQNITQYDFKRPINSVALHSNFQASRMFVSGGMAGDVVLSQRNWLGNRIDIVLNKKKKKKTRKDDLSSDMKGPIMGIYTMGDLILWMDDDGITFCDVPTRSQLLNIPFPSRIFNVQDVRPDLFRPHVHFLESDRVVIGWGSNIWLFKVSFTKDSNSIKSGDSNSQSNNMSHFNPTTNIGSLLSSAASSFRGTPDKKVELECHFTVSMLITGLASFKDDQLLCLGFDIDIEEEATIDEDMKEGKNFSKRPENLLAKGNAPELKIVDLFNGDEIYNDEVIMKNYEKLSINDYHLGKHIDKTTPEYYLISSNDAIRVQELSLKDHFDWFMERKQYYKAWKIGKYVIGSEERFSIGLKFLNSLVTKKDWGTLVDHLNIIFEETLNSLDSNSYDVTQNVLKEWADIIEILITSGNIVEIAPLIPKKPALRKSVYDDVLHYFLANDMINKFHEYITKWDLKLFSVEDFEEELETRIEAASEPTASSKEEGSNITYRTELVHLYLKENKYTKAIPHLLKAKDLRALTIIKIQNLLPQYLDQIVDIILLPYKGEISHISKLSIFEIQTIFNKPIDLLFENRHTISVARIYEIFEHDCPKSFKKILFCYLIKFLDTDDSFMISPYENQLIELYSEYDRQSLLPFLQKHNNYNVESAIEVCSSKLGLYNELIYLWGKIGETKKALSLIIDELKNPQLAIDFVKNWGDSELWEFMINYSLDKPNFTKAILTCSDETSEIYLKVIRGMSDDLQIDNLQDIIKHIVQENSLSLEVRDNILVIINDETKKFANEFLKIRSQGKLFQVDESDIEINDDLNGVL
The following text describes a protein:
Function:
Verruculogen synthase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities. The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA. Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B. The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively. The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B. Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties. In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Sequence:
MTVDSKPQLQRLAADADVDRMCRLLEEDGAFILKGLLPFDVVESFNRELDVQMAIPPPKGERLLADKYPPHFKYVPNVATTCPTFRNTILINPVIHAICEAYFQRTGDYWLSAAFLREIESGMPAQPFHRDDATHPLMHYQPLEAPPISLSVIFPLTEFTEENGATEVILGSHRWTEVGTPERDQAVLATMDPGDVLIVRQRVVHAGGGNRTTAGKPRRVVLAYFNSVQLTPFETYRTMPREMVESMTVLGQRMLGWRTMKPSDPNIVGINLIDDKRLENVLQLKAADSPA
The following text describes a protein:
Function:
Transport of aldohexuronates such as D-glucuronate and D-galacturonate. Under anaerobic conditions, can play a critical role as a D-glucose transporter in the absence of sugar-PTS system.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MRKIKGLRWYMIALVTLGTVLGYLTRNTVAAAAPTLMEELNISTQQYSYIIAAYSAAYTVMQPVAGYVLDVLGTKIGYAMFAVLWAVFCGATALAGSWGGLAVARGAVGAAEAAMIPAGLKASSEWFPAKERSIAVGYFNVGSSIGAMIAPPLVVWAIVMHSWQMAFIISGALSFIWAMAWLIFYKHPRDQKHLTDEERDYIINGQEAQHQVSTAKKMSVGQILRNRQFWGIALPRFLAEPAWGTFNAWIPLFMFKVYGFNLKEIAMFAWMPMLFADLGCILGGYLPPLFQRWFGVNLIVSRKMVVTLGAVLMIGPGMIGLFTNPYVAIMLLCIGGFAHQALSGALITLSSDVFGRNEVATANGLTGMSAWLASTLFALVVGALADTIGFSPLFAVLAVFDLLGALVIWTVLQNKPAIEVAQETHNDPAPQH
The following text describes a protein:
Function:
Regulatory subunit of glucosidase II (By similarity). Essential for stable accumulation of the receptor EFR that determines the specific perception of bacterial elongation factor Tu (EF-Tu), a potent elicitor of the defense response to pathogen-associated molecular patterns (PAMPs). Required for sustained activation of EFR-mediated signaling, but not receptor FLS2-mediated signaling elicited by the bacterial flagellin flg22.
Subcellular Localization:
Endoplasmic reticulum.
Sequence:
MRVVVISSFVSVSLQLSFLLLLASAIRSSSSPPNDPFLGISPQDEKYYKSSSEIKCKDGSKKFTKAQLNDDFCDCSDGTDEPGTSACPTGKFYCRNAGHSPVILFSSRVNDGICDCCDGSDEYDGHVSCQNTCWEAGKAARENLKKKIETYNQGLVIRRQEIEQAKVGLEKDAAELKKLKSEQKILKGLVDQLKDRKEQIEKVEEKERLQKEKEEKEKKEAELAAQQGKGDAEEKTDDSEKVEESSHDEGTPAVSQHDETTHHDEIGNYKDYPSDEEPAAEGEPTSILDEATHTNPADEHVVERKEESTSSEDSSSPTDESQNDGSAEKEESDEVKKVEDFVTEKKEELSKEELGRLVASRWTGEKSDKPTEADDIPKADDQENHEHTPITAHEADEDDGFVSDGDEDTSDDGKYSDHEPEDDSYEEEYRHDSSSSYKSDADDDVDFSETTSNPTWLEKIQKTVKNILLAVNLFQTTPVDKSEADRVRKEYDESSSKLNKIQSRISSLEKKLKQDFGPEKEFYSFHGRCFESKQGKYTYKVCAYKEATQEEGYSKTRLGEWDKFENSYQFMSYTNGEKCWNGPDRSLKVKLRCGLKNELMDVDEPSRCEYAAILSTPARCLEDKLKELQQKLEKLMNQDKPQNHDEL