lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in membrane remodeling including fission during breakdown of the endoplasmic reticulum (ER) and the tonoplast during leaf senescence and in membrane fusion during vacuole biogenesis in roots.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Vacuole membrane; Multi-pass membrane protein.
Sequence:
MSETSLLIPKTNSPASSENMANTNKSLTGLESLIKLLPTGTLFIYLLLNPVLTNDGECSTGNKVMSSILVALCSFSCVFSCFTDSFKGVDGSRKFGIVTKKGLWTYAEPGSVDLSKYKLRIADFVHAGFVLAVFGTLVLLDANTASCFYPRFRETQKTLVMALPPAVGVASATIFALFPSKRSGIGYAPIAEEVGAEEETKKASVSA
The following text describes a protein:
Function:
Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Has low in vitro and no in vivo activity on D-serine; primary D-serine degradation is performed by the D-serine dehydratase dsd.
Subcellular Localization:
Peroxisome matrix.
Sequence:
MNQNKNNNNKNPKINLLIIGCGCIGLSTGIIALKSGNYKSVSIWAKDLPPNTTSNKAAALWYPFLCNPLDLVGKWSAETMQYYKDHIINDPKSGTITKKVNEIFRRPHPEDPEWKPYIKSFRRARKDELPDGYVDGYAIDDGFVMDTDMYMDYLVDQFKSLGGIIEQRHLVDIREAFVDHDVVVNCTGLGSRELFNDRTIYPGRGQIIVIKNSTDRSIMDEEDHIAYVIPRLTNTVLGGTNQEHDYNTNPTKKDTEEILKRVAMISPRFAKNRIEIQGVKVGLRPARHEIRLENEFFEGGSKLVVHNYGHGGSGFTVSWGCAIEAIKLVDQGLPKLLHFNKLISKL
The following text describes a protein:
Function:
May function as somatic storage protein during early seedling development.
Sequence:
MATARLLLLLTVVAAAAGSCFCSGQEAKPPTPPPPPPYCGSVRTAVEAHNIIGWKTLPADCAKYVADYITGDRYGRDSDVVINEAVAYAESLKLSGSGKEVWVFDVDETALSTVPYQAKHGYGVQPYDHANFLQYVAGGSAPALQGTLRLYQRLLQLGIKPVFLTDRTEDQIAITTHNLLSQGYSSWEKLLLQPIGLQTSTQAFKTSERKKLVDAGYVIIGNIGDQWSDILRSPEGCRTFKYPSPMYYVA
The following text describes a protein:
Function:
Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels.
Subcellular Localization:
Membrane; Single-pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Sequence:
MATARGGSGPDPGSRGLLLLSFSVVLAGLCGGNSVERKIYIPLNKTAPCVRLLNATHQIGCQSSISGDTGVIHVVEKEDDLKWVLTDGPNPPYMVLLEGKLFTRDIMEKLKGETSRIAGLAVTLAKPNSTSSFSPSVQCPNDGFGIYSNSYGPEFAHCKKTLWNELGNGLAYDDFSFPIFLLEDENETKVIKQCYQDHNLGQNGSAPSFPLCAMQLFSHMHAVISTATCMRRSFIQSTFSINPEIVCDPLSDYNVWSMLKPINTSGGLEPDVRVVVAATRLDSRSFFWNVAPGAESAVASFVTQLAAAEALHKAPDVTTLPRNVMFVFFQGETFDYIGSSRMVYDMENGKFPVRLENIDSFVELGQVALRTSLELWMHTDPMSQKNESVKNQVEDLLVTLEQSGADTPQVVLSRLVQSQALPPSSLQRFLRARNISGVVLADHSGSFHNRYYQSIYDTAENINVTYPESQSPEEDLNFVTDTAKALADVATVLARALYKLAGGTNFNNSIQADPQTVTRLLYGFLVRANNSWFQSILRHDLRSYLDDGPLQHYIAVSSPTNTTYVVQYALANLTGKVTNLTQEQCQDPSKVPNESKDLYEYSWVQGPWNSNKTERLPRCVRSTVRLARALSPAFELSQWSSTEYSTWAESRWKDIQARIFLIASKELEFITLIVGFSILVFSLIVTYCINAKADVLFVAPREPGAVSY
The following text describes a protein:
Function:
Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (By similarity). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs (By similarity). Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1) (By similarity). Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates (By similarity). Stimulates exoribonuclease activity of Rat1, allowing it to degrade RNAs with stable secondary structure more effectively (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MNRETFDIQPIGRFYGSNTAIRRPREIACFSYDDQHKFHLGDSSLRYYYPPQLPADLNRGFDTFQKLDDAADEHIDALLDTIAAMEKETGKRCEADIITWRGMMTKILTAPFDDMNGFEMNATCFQGTMCKQLQRQQRMPPGMASQDLMAYWGYKFETISVLDKTWDEASREEIEGRENLVVNNNAQYCSVVRTGIGRTKLVLGGEVDAIWDSKPERKEDPINWVELKTSAEIRKDWDMVKFERKLLKFWAQSFLLGVPKIVVGFRDQGGILRRLEELETANIPNRVRKSGRGTWDGNICINFAATFLEWLKSVIKEGGTWRLRKAEKSSVIEVYQVEESGTGDILSQAFLSWRSTT
The following text describes a protein:
Function:
Has glycerophosphoinositol inositolphosphodiesterase activity and specifically hydrolyzes glycerophosphoinositol, with no activity for other substrates such as glycerophosphoinositol 4-phosphate, glycerophosphocholine, glycerophosphoethanolamine, and glycerophosphoserine. Accelerates the program of osteoblast differentiation and growth. May play a role in remodeling of the actin cytoskeleton (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Cytoplasm. Cytoplasm, cytoskeleton. Note=Colocalizes with the actin cytoskeleton.
Sequence:
MAESPGCCSVWARCLHCLYSCHWRKCPRERMQTSKCDCIWFGLLFLTFLLSLSWLYIGLVLLNDLHNFNEFLFRRWGHWMDWSLAFLLVISLLVTYASLLLVLALLLRLCRQPLHLHSLHKVLLLLIMLLVAAGLVGLDIQWQQEWHSLRVSLQATAPFLHIGAAAGIALLAWPVADTFYRIHRRGPKILLLLLFFGVVLVIYLAPLCISSPCIMEPRDLPPKPGLVGHRGAPMLAPENTLMSLRKTAECGATVFETDVMVSSDGVPFLMHDEHLSRTTNVASVFPTRITAHSSDFSWTELKRLNAGSWFLERRPFWGAKPLAGPDQKEAESQTVPALEELLEEAAALNLSIMFDLRRPPQNHTYYDTFVIQTLETVLNARVPQAMVFWLPDEDRANVQRRAPGMRQIYGRQGGNRTERPQFLNLPYQDLPLLDIKALHKDNVSVNLFVVNKPWLFSLLWCAGVDSVTTNDCQLLQQMRYPIWLITPQTYLIIWVITNCVSTMLLLWTFLLQRRFVKKRGKTGLETAVLLTRINNFMME
The following text describes a protein:
Function:
Inhibitor of protein-phosphatase 1.
Sequence:
MAASTASHRPIKGILKNKTSAASPPVVPSAEQPRPIVEEELSKKSQKWDEMNILATYHPADKDYGLMKIDEPNTPYHNMIGDDEDAYSDSEGNEVMTPDILAKKLAAAEGSEPKYRTREQESSGEEDNDLSPEEREKKRQFEMKRKLHYNEGLNIKLARQLISKDLHDDDEDEEMAETADGDSMNVEESSQGSTTSDHLQHKSQSS
The following text describes a protein:
Function:
Activates YPK1 by phosphorylating of a threonine residue.
Domain:
The PIF-pocket is a small lobe in the catalytic domain required by the enzyme for the binding to the hydrophobic motif of its substrates. It is an allosteric regulatory site that can accommodate small compounds acting as allosteric inhibitors.
Sequence:
MGNRSLTEADHALLSKPLVPTSAEHTQTQEYPRPFVDGSNSQSGSELQASPQGQFGEKALTSTNRFIPLANDDPGMQHEMGLDPSMRRRREEWAERGAAKIVKDVVDPATGELTKHVVKMGIKDFKFGEQLGDGSYSSVVLATARDSGKKYAVKVLSKEYLIRQKKVKYVTVEKLALQKLNGTKGIFKLFFTFQDEASLYFLLEYAPHGDFLGLIKKYGSLNETCARYYASQIIDAVDSLHNIGIIHRDIKPENILLDKNMKVKLTDFGTAKILPEEPSNTADGKPYFDLYAKSKSFVGTAEYVSPELLNDNYTDSRCDIWAFGCILYQMLAGKPPFKAANEYLTFQKVMKIQYAFTAGFPQIVKDLVKKLLVRDPNDRLTIKQIKAHLFFHEVNFEDGSVWDDNPPEIQPYKINAEAMKPLQKVSESDTTVKMANLQLAGNGHADTPLQAPAATSQEHSVISMTAATAAFNKDYTSQPKLGSKSSTSVRSASNNTDREVIQKKVSKNRASVSSPSISTTSRGKDNRSRSSDAFWSRYLQNMDERVLLMKEVALSTRNLEDSPVGLENVALDYKNPLDIEPPTDSAGKFYKKMFLITNLGRALVFVKRRSLSMWEEQEFELQFELELNDVEKIRFISDQVLEIDGSRTIFIGCKERAVLMKLWKLIHNGMTAKPKVVSPKSDHKMFDKFILQKRQNTKKKNQAPPVPQSNRLINGLPDRCILKTPEEGALHTKRPTSLQTRSSSNYSKLLARSTQMRKNMTRTDEK
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MQPHTQPPQPEASSSRAVHIPSDPAPPRPCLTNDAIVSRWQSSPGFQYFWAWIKRRCDRLKGKEIIRGPFDHSAHGIRSLMNMLDQMTSWVEDATPQPQSNQRFGNLAFRTYNKLLQERLPPLIDSWDIPSNLRSQLLPLFINSHAFGHPTRLDYGTGHELAFVLGLWCCVVPGWVGGDNGTEEEEDELILRVFTRYLELTTFLQKTYNLEPAGSHGVWGLDDYCFLPYLFGSAQLLGSNLTPSASLSLALSHHPSATSPPSAPITDLYTLSLHHLTLFKFGASFSEHSPLLYSLSQMPNWVKPHGGLKKMFLGEVVGKRVVVQGIWVGGWCWGEDVPNVEERGDKNEGKGTDAGTKAPWAR
The following text describes a protein:
Function:
Regulator of DNA replication and S/M and G2/M checkpoints. Regulates the triggering of DNA replication initiation via its interaction with topbp1 by participating in cdk2-mediated loading of cdc45l onto replication origins. Required for the transition from pre-replication complex (pre-RC) to pre-initiation complex (pre-IC). Required to prevent mitotic entry after treatment with ionizing radiation.
Subcellular Localization:
Nucleus. Note=Associates with chromatin.
Sequence:
MAPSHNVVLLVDTAESSDKSRLRRVSLRLLNFLACRAGLGQVRWSYRFLNSSGGRCRPPRRSDLRELGPRGWEEFEDELEACWERARNCRPSSTQSSRAQLLQTALMETLADFQWDRPDITSPTKPTLLRSRRGRIVAADEPLKDDSPDNFINPHSRNSIFLLSSCPHSGTELGQFAATSGDFSTQKVMDKLLPKSLQKIVSSKRVRVYWLDTSDWTQFGSSSDHSGYWTMVELMHQVEGRILPSESILGSSCQKAKTLPSFSVPPINIPFESVLNYLIFSEPDYQLWFPRRDGILFLTGKDGTKQLDCAVSLEPVSMIQKLSTSLMTIELKGTMQNCNLPLAGLRVETWLLHNSDCVQLQKLTKELMLKELHMIATVTLEDDVLPRTGILSPLSETAAVLNVICSERTLGLDNLHVQGSVHETDKETFSDLPDIVMSVLNHVYSSEDNTLAPDFPVPEWIKQELSQSSRWTSSVTARWYPLSGVSGASCNLMESFRLINAASSNCDEHLKFDQELTNYLSEFYQKKSVDDAGLGVHRENQKKSGLPRTPVRQKMKTLPRALQMLNAARLNVKAQKADSTLPVPNEKNSQMKRRSSGKQDNKPKQLKPTEFQSEDGLISYIKENYEEAVSLVDHSTMTWARDTLTTIKSYLKSIGSEQIETEAIDKVKLLFKTSKVIRQNYRNNQDKEVKLKECQLQVFLRLEMFVQCPVIQMDSDELELIIEEITDILRIVSLTEDPLFLTKFLEVDVLTQYIASVPKILADIYFSLGTQIPEVLVLVLPSDGDDSIMHEEKSVKSQPSTSRVPSVAPIGAETDQLEDLRTRSAKKRRSTALARHRSVAESSQSFRQIEVPKRQPNKENVQSNAVVVLEKLKLPLPAQPQKDAEAKVRRNLFIQETRSPSKRCSKMPRSQSVSAVESLKRKRSKSHDGSKDHHKLLTKKVSETPVHKQTANRLLLRQIKGRPSESNSNISIVEESPEKEIRDIDLRRSPRIKQLSLTRRNSSSFYASQPKSRNLERVNSATQLQQSRERPGSCLISEVKTPKRLLFGEVLGMISPPTTKRSRRILDMVNPVYKTPGKTPRKTPSKNIPNFEDQSGNMLVKSPCTPYTPRTPSRTPKRLKTPSKGSTERKKAAKNLGKLFSPSKPEEKSPLKLWGRRSERLAQMTPGKDGSPYKQSVCQTLMEVKTPQKLQRLESKDFRTPSRTPTRSNNTTPAKQSMQISNTPRKSDLKHPQEHESRGPSGYILWTPQKRILASVPHTPILQTPQKPISASVPRTPVCRTPQKAILSSVPSTPVCQTPNKAILTSVSRTPVYQTPQKAILASVMSTPVYQTPQKPVLASVPTTPILKTPQRSALASVSHTPSPKKYIMKELTVAITRMRECTPEKVLGSNLSSSATPSSALKSFCSEKTTSVCQTPKKSSIALLKPCDSLEFSGAPERLMDSLCSNKDSTKAETACTVPSQISTQMQNVINAGECTDSLSQTSVSSPSIPFTDKSLSPDLKDALSDVTSSKAEGVTIVSEKLDSSSMDSQEATDSFINSSQTEESIDISEARVVSTEASELKMKVLITRKPSGSGVSYLPTTPKCLGNVCSTSTYGLRCTPDRRQREAAARLGTPEIPAKFSTPKSHCKMIPQSIYEVELEMQESGLPKLRFKRTDSNSTIDMDVNKTPKISRKRKGDESPFNEKWCSKHAVRTEPACVSPSCVRTSHYTPGKSGIQTFICQSYTPNRCLSAAASPSQSDAGVPWTPSPKEKLSTDVINSWPRKKKASALCTNLLKCDKIPEYAEEDGGDFELEGVSKLLEKSPVIEQQSKVDGGTFGLRSRKRVFSLVSPTKETENPVKRVCTFNRHEDSSTATHRHQTKEEMEIFSSDQSRSSYLSSSQQSICDDVFNMSDFTPPSKVPKNPLSACGLLTLTQSPLLYKGKTPSSKRKEKIQDVFSDGDSDHGTPTLKRPTNPAAVSDDSPFRKVNPLRSISKTYSRKKLIT
The following text describes a protein:
Function:
PPIase that acts as a histone chaperone. Histone proline isomerase that increases the rate of cis-trans isomerization at prolines on the histone H3 N-terminal tail. Proline isomerization influences H3 methylation thereby regulating gene expression.
Subcellular Localization:
Nucleus.
Sequence:
MSATPIGFFGLKLVPGKVHRMDVSRDFKITNVSYADQPKSNTKTLVKIHYTHVPGFEDDYDEEEQEKEPKSTDEEEEIEEKVYTLCSLNGANKDHAVVDLQFCQEELIGFSITGDAPVDLVGNYVAPPDFFDQDPSDSELYSDDEDDDEDMYGLDSDDFDDDDDDDMDEDPDRFEELVESSASKPKKAIEAAPLADSKKRAAEKPVKETAAKKLKADASAASAASTPTKAIETKGEKQTKGAKDTKPKSETVEKKTVDKSTSKMTTTKLPSGLVIEEKSAGSGPPCKAGQKVGMRYVGKLTNGKVFDQCTSGKPFYFKLGKGEVIKGWDEGVKGMRVGAERRLTCPPKLAYGNQKIPGIPANSTLVFDVKLVEIK
The following text describes a protein:
Function:
Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration.
Subcellular Localization:
Endomembrane system; Peripheral membrane protein. Membrane, coated pit.
Sequence:
MELARTTLRGLHNFIQEIHRSQNPEEERKSVDKELAHIRMEFKTGKKLKGHGRRKYILKMLYIYILGYDVDFGIPIITELLTSPKFSDKQVGYLAISILLYEEHEATRLVINTLRAELIDSNPLNQCCAFNVISCIGNKEMVETLGPDILNILFSNTIPTVVRKKAALTLKHLYLKNPTIIQLDTEFHDKLLKLLNNPDLCLVSCAVMVLLVIVEKDPTPWEDATSKLLNILSKLMNKDYSSEYNYHSVPSPWLQVRILRTLRYITPKKGAEENYLSDCVKSLIDTCDAKLSENTRNAMFSILFEIIELAPFVEFPENTKSKIVNMLGTYLNATETNLRYLALDAMCSMCAVGCDKEVQKYLSRMIDSLREIDISVKRRALQVLFDVCDNDCCNKILTELLRFLPVSDLAIREEVIVKICLIAEKFAKTPQWYVDIMLQLTAVSGDYIGDQILNRILRIIINNDSVQVFAAKATYKYLQEVAWKDAFIKISSYILGEYGSLVVKDNMKIAQNIFDMLKDKYPLVSYQTQLTMLSAFAKLHATFPCLRDQIKSLFIKYSSSSDAEISDRCQDYLFMTSIEELEPIVFEAIPPWEGAQEGEDGKIVDGEVTVTENSADVVSRNTKETNRDDDLFMLLGVVDPNKKEEVQKNNDLFNILTTPVSSNQQPTSSPLNQPTQQQPSNQSNDVFDFGGSDMNQIQQQPKEEEVNIKPSENTEKYDGCICHNIKEQMENVMINNHNKLILAFEGVLYQDDTIQIGLKSALESPMCKFALFFGNRITEEVELNYIIECPNGLTCNSGEYNGKIGAKSQIQSIAQFTISGFYYQSPIINITYKSSSFKNKIAFSLPLTVNAFLVQEPLEPNIFMQYWNTIGNATEKKSIIQMKQNNPIDLPTVLGGMRFICLDVKPEQIVACSSFPSFQNIYVLLRIEINVTSNKACIYVRAQDPSLAKVIHNLLCYEIAA
The following text describes a protein:
Function:
Involved in the trafficking of vacuolar proteins. May function as a sorting receptor for protein trafficking to the protein storage vacuole (PSV).
Subcellular Localization:
Endomembrane system; Single-pass type I membrane protein. Protein storage vacuole membrane.
Sequence:
MPSVGKSKMKRIVVVVVVIFFLSLSACCSMTSASVVLIGSNVTLSFDDVEANFAPAVKSSGECGALNLAEPLDACSDLRNKVEKASNVSSPYLLIIRGGCSFDDKVRRAQEAGFKAAIVYDNEDDGLLVSMAGNSAGIRIHAVFISKSSGETLKKYAGLSGVEIWLISSFENSAWSIMAISFISLLAMSAVLATCFFVRRHRIRRERPRSSQVREFHGMSRRMVKAMPSLIFTAVQEDNCTSRTCAICLEDYSVGEKLRILPCRHKFHAFCVDSWLTTWRTFCPVCKRDARTSNGELPASESTPLLSSSPASLASSSVLSSFRSTSSLAIQIAPTLSQSPSVSHIPSSRSPSVAHVPLSGTPYVQQSLRSYHQSPSLSVSRSSADLRHASSQRSIASHLISSHSLGYPSISPRTSRYMSPYIPSPSNASPCFLSSSSHQQRPLHCSESAASFSPFASAHSLPEC
The following text describes a protein:
Function:
This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions.
Subcellular Localization:
Cell membrane.
Sequence:
MGDATETFYGVIRRQGITRRSFLKFCSFTAASLGLGASSIAHALETKPRVPVIWLHGLECTCCSESFIRSAHPLIKDALLSMISLDYDHMIMAAAGHQAEAILEETRARYKGGYVLAVEGNPPLNEGGMFCIDGGKPFVEKLTSMAEESMAIVAWGTCASWGCVQAAKPNPTRAVPIDKLITNRPFIKVPGGPPIAEVMSGLVTFITTFGKLPKLDHQGRPSMFYSERIHDKCYRRSHFDAGQFVEEWDDTNARKGYCLYKLGCKGPTTYNACSALRWNGGVSFPIQSGHGCLGCSEDGFWDKGSFYDRLTTIKQFGIEQNADEIGMAAAGVVGLAVAAHAAVTAAKRLRHRPDRPAHKGKPS
The following text describes a protein:
Function:
Radical SAM enzyme that catalyzes the cyclization of dehypoxanthine futalosine (DHFL) into cyclic dehypoxanthine futalosine (CDHFL), a step in the biosynthesis of menaquinone (MK, vitamin K2).
Sequence:
MASIFSSQPTDRILEKALDGNRISPEEALALYREGDHLKIMATARSLREKILPHHYASYTMFRVVNYTNYCNVECSFCSFMDEIGNGKGYVLSVEEILEKMDYAVGEGADQMFLQGGVYPDLSFDYYLNVISAVKKKYPHMHIRAFSPVEIINLEKITGLPLKEVLQILKQTGLDSVPGAGAEILTDRMRNIISPKKATTEEWVRAMETCHEVGLPGSANIVFGSEETQEEVIEHLNVVRNLQDRTGGFLSFIPWTFQPQTKRFKVRAVPTQEYLKVLGICRIFLDNILHIETSVMVLGKGVGQLALTSGADDISSVVIEENVLRSYGLKTEKEAVKFLKEGGFTPKRRDLLYNYDRYENELIVDFV
The following text describes a protein:
Function:
High affinity uptake of sulfate into the cell.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MRAWGWVRNKFSSEDDYNDGASNKDYPDRFNEFDNSQNDHNDYTQNNAQFQNAQTTTFGRTISRVKAYYEIPEDDELDELASIPQWFKKNVTSNIFKNFLHYLKSLFPIIEWLPNYNPYWLINDLIAGITVGCVVVPQGMSYAKVATLPSEYGLYSSFVGVAIYCFFATSKDVSIGPVAVMSLITAKVIANVMAKDETYTAPQIATCLALLAGAITCGIGLLRLGFIIEFIPVPAVAGFTTGSALNILSGQVPALMGYKNKVTAKATYMVIIQSLKHLPDTTVDAAFGLVSLFILFFTKYMCQYLGKRYPRWQQAFFLTNTLRSAVVVIVGTAISYAICKHHRSDPPISIIKTVPRGFQHVGVPLITKKLCRDLASELPVSVIVLLLEHISIAKSFGRVNDYRIVPDQELIAMGVTNLIGIFFNAYPATGSFSRSAIKAKAGVKTPIAGIFTAAVVILSLYCLTDAFYYIPNAILSAVIIHAVTDLILPMKQTILFWRLQPLEACIFFISVIVSVFSSIENGIYVSVCLAAALLLLRIAKPHGSFLGKIQAANKYGSDNIANVRDIYVPLEMKEENPNLEIQSPPPGVFIFRLQESFTYPNASRVSTMISRRIKDLTRRGIDNIYVKDIDRPWNVPRQRKKKENSEIEDLRPLLQAIIFDFSAVNNLDTTAVQSLIDIRKELEIYANETVEFHFTNIRSGWIKRTLVAAGFGKPKGHAVDASVCVEVAAPLRDANLSAESSRNLSRIITPIYDDEEGNVSGHIYELDGKNNSDLSMHCQKGSNQVEIEFVEFNSRKYPFFHVDVASAVVDLQHRLLSPQKSDSFGSLKEGGTTTIKKIEN
The following text describes a protein:
Function:
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. 5-bromo-2'deoxyuridine monophosphate is also a good phosphate acceptor.
Sequence:
MNSKFIVIEGLEGAGKTTTRDTVVAVLRAQGINDIVFTREPGGTPLAEKLRDLIKQGIDGEVLTDKAEVLMLYAARVQLVENVIKPALARGSWVVGDRHDLSSQAYQGGGRGIDSQLMASLRDTVLGEFRPDLTLYLDLPPAVGLARARARGELDRIEQESLAFFERTRARYLELAASDASIKTIDASQPIEQVSASISQALAQWLTNQEPV
The following text describes a protein:
Function:
Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
Subcellular Localization:
Cytoplasm.
Sequence:
MTTHEPRTVRAPRGPHKTAKGWIQEAAKRMLMNNLDPEVAEHPESLVVYGGRGKAARNWEAFDHIVATLDRLENDETLLVQSGKPVAVLRTHEWAPRVLIANSNLVPHWANWETFDKLDQAGLMMYGQMTAGSWIYIGTQGILQGTYETFAGAAQKHFGGSLKGTITVTAGLGGMGGAQPLAVKLAGGVSITIEIDPTRIRKRLETRYLDEVADNLQDAIARAEGYKAQGVARSIGVQGNAAELVPQLVEMNWTPDLLTDQTSAHDPMWGYIPPVNADEDAGKLRSEHAEEYRQRAYAAMAAHVRAMLELQKRGAVTFDYGNNLRQRAFEAGVEDAFSYPGFVPAFIRDSFCEGRGPFRWVALSGDPQDIYATDKALLELFPEDERLQSWLTYAADQIAFQGLPARICWLGYKERDRAAKLFNDMVKDGRVKAPIVIGRDHLDAGSVASPYRETEAMKDGSDAVSDWPLLNFGVGIASGASWMSFHHGGGVGLGFSQHSGLVIVADGTDEAAKKLSRALTNDPGMGVIRHADAGYDHALDVARERGIDLPSLGIKDHA
The following text describes a protein:
Function:
Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions.
Subcellular Localization:
Nucleus.
Sequence:
MSAFKKKNVFVNPFYQDGVGRRTGIVVKKDVRKDSDGFEVFDDYWSESENDATMHTTLAAEKENKDGTMKKRSLRSMPSFTPQEASSDREASKVELPQDVSQAAENASALEADITGSIIKGRAPSLEPSSALSKFKTRQRLSFSEATTSEESQTSEGENSVGDEGESQESGSSSEGTVKAPSSQSELSQEEGDEQTETEEDDASGPVEHDDQQSSRTTSEPSSPQEEVPEPQAKATSPSDEGTTAQTRGSKRRSTRPDGDLSGPVPRETRSRKSISQSKNIVENEEIDEREAEKAVETRGRRSTRQSNASVLNENELQKDNEKSAKKGADTRRRKSTRQSKANEGKVDKDAVNDKEIDTNIKNSSRRSRSIKPSNVSVNKGNDIEIDLEKQEEKAGGTRRRKSTRQSKANDAVDDIEIDTNTQNGSRRSRSLKPSNMSINKGSDTEMELEKQEERAGGTRRSKSTRQSNVSIKDVQEDIVGDKETDDVTSNLRKSPHQSSRLEREIKRIHDRSIRRSKGVEDLKDDVEKETQVVKSRRKSKQQSNAPPGKEVEEEKGEEEEDEGTEDEVAPETDAETAGETEGEKVEGTKEEEVLETETESEFVTETEEEEGERNIEEPESEEAVDTEVDEIKKTEEENFRKAIKQKEKTVVASKSDVVEDEDDDTEKVFFSLRASFAVPSVHEVEDEFEFADADSQEYGLLDDTQKGNRKKAGRTNRKTIAKGGKKNDKEVVQKEKPEKLPKSTRRPTQKDKQESKMGKGQKKKASKRGSEIGRDDDQKKLKESPNESLSGDGHDSKLAMGGKKSRGKKSNQQKKQLQRSQRSSESTSQASSSDADADSQVDDDQAAAVDLPQKNQRKRRQKKPSNQKASSSDADAGSQVDDDQAAAVDLPQKKQRKQRQKKSSDHPAEVSNSSKTASDETLGVDEDGPSTGKAGSSSSAFRSRRSSVHFTTKDMISVGGDISIHQVSSAEDKSSDNKDAPPTTATLSKDHKKSRRSSKGRSSGGGAKTRDKANEDDTKNVEEHLSGQSSHESTAESDRETADQGQSRRGRKKGAKAKKPSKRPSSKATSTTSEDSLKTDEEDGVRRTKRHRAPPREYWHDSIEHTEDHTDTTQVLVAHHDANQNQSDQSIDQSTDQPTDQSPKGPTPPGKSPSTSSGGARSITSTGSILKVSRNWDKRPKNKKNKYSILYTEKPLRKAYIIKPDEEDGVRRTRRQRVRPLEYWRNERPLYERRKSGGLALAGIISPGAPEERVSVRSMRQPAKPKGHLPVTPSHISIHASPPVGTSKVCQPTINVVNPDTKQEVAIDAVATSKMLKFTGPSGLPAKPDDAITISKALSQKAFAAGILTIRPFGEKGSQLVRRDTMIFYVVRGKVAMTLHETSQILQSGDWFFVPKGNVYNITNLRRDEAKLTFFQLKSS
The following text describes a protein:
Function:
Component of the FERRY complex (Five-subunit Endosomal Rab5 and RNA/ribosome intermediary). The FERRY complex directly interacts with mRNAs and RAB5A, and functions as a RAB5A effector involved in the localization and the distribution of specific mRNAs most likely by mediating their endosomal transport. The complex recruits mRNAs and ribosomes to early endosomes through direct mRNA-interaction.
Subcellular Localization:
Early endosome. Secreted.
Sequence:
MQYDVNNCSYRLASPNNLIFSLGYSTSNPCGVHSSGSDIPSSLEDPGEPCPTPSLAQISAWVVAMASERLPSRPACLLVASGASEGVSAQSFVHCFTLASAAFNLQVATPGGKAMDFVDVTENNARWVQDFRLKAYASPAKLESIDGARYHALLIPSCPGALTDLASSGSLARILQHFHSESKPICAIGHGVAALCCATNEDRSWVFQGYSLTGPSVYELIRAPGFARLSLIVEDFVKDSGAGFSASEPDAVHVVLDRHLVTGQNANSTVPAVQNLLFLCGGRK
The following text describes a protein:
Function:
Functions as a multifunctional transcription factor that may exhibit positive and negative control on a large number of genes. May antagonize YY1 and function in development and differentiation.
Subcellular Localization:
Nucleus.
Sequence:
MASGDTLYIATDGSEMPAEIVELHEIEVETIPVETIETTVVGEEEDDDEDDEDGGGGDHGGGGGHGHAGHHHHHHHHHHPPMIALQPLVTDDPTQVHHHQEVILVQTREEVVGGDDSDGLRAEDGFEDQILIPVPAPAGGDDDYIEQTLVTVAAAGKSGGGSSSGGGRVKKGGGKKSGKKSYLGSGAGAAGGGGADPGNKKWEQKQVQIKTLEGEFSVTMWSSDEKKDIDHETVVEEQIIGENSPPDYSEYMTGKKLPPGGIPGIDLSDPKQLAEFARMKPRKIKEDDAPRTIACPHKGCTKMFRDNSAMRKHLHTHGPRVHVCAECGKAFVESSKLKRHQLVHTGEKPFQCTFEGCGKRFSLDFNLRTHVRIHTGDRPYVCPFDGCNKKFAQSTNLKSHILTHAKAKNNQ
The following text describes a protein:
Function:
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins. Within the pathway, the FAD-dependent monooxygenase asqG catalyzes the epoxidation of the terminal C7'-C8' olefin to produce the intermediate [(1'E)-5'-(3',3'-dimethyloxiran-2'-yl)-3'-hydroxy-3'-methylpent-1'-en-1'-yl]-quinolinone B. The first step of the pathway is catalyzed by the nonribosomal peptide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin. 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ. AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin. The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI. 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B. The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene. The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain. The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin. Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (Probable).
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MAAFTVIIIGGSISGLTLANVLEKYGIKYILLEKRPSIGPQLGATVVVHPSGLHLLSQLGLRERVEELATPVELQKAIGPDGTFVLNIAATNQCDRTIADALSTGYMPMFIARQDLIKVLYDNLQDKFRVHASLGLRELEWAGDKVKVTTTDGTSVVGDIVVGADGANSRTRAEIWKIADVEDPSYGSQQLAKSIACTYRCVFGMVDDGDSSLARTAYLAFQYNRAYTYLPTDSGRAYFLAFFKNPAKTVNDAIPRYSDQDEDADVAAHANDIIVPGLTFGDLYKRRTRCTLVPLQEYLLDKCFYKRVVLIGDAVHKLNPITGRGANLAIEGAALLGDLIKHALEKSLQPTDEMLQTAFFTYQQCTKSRAPSQIDDAHRVQSLAALENPLLKFMSLKLLKRATADKLALGVAVDFSTGHSMRYLPQLPQRGMVPLNKDVVANPEHRPASSTVLWIILMLGMASLGAVWQKHQRAEEDQPIHGYTLLTLSTFYNLMILFASAVHGSLGRRAVNLSFSDDSGMVPFYAVGHAPDKYRPTTPSRRVGLLVPGPSYLGSGGHFNGLLEVA
The following text describes a protein:
Function:
Extracellular proteinase found in the pitcher fluid of carnivorous plants. Digest prey for nitrogen uptake.
Sequence:
MALEPLPKLSSLTVLLLSLIPLSSGAFAGGVRVELTHVHANAGDSEAKLIQRAVASSRHRLSTLVDRAPLHAGKTEYIVDIAIGTPALAFSALVDTGSDLIWTQCKPCSNCYWQSSPVFDPSKSSTFGTIACDSMLCKALDQHSCNASCHYSYMYTDHSYTEGVLGTETFTIGSTSVPGLAFGCGNSNDGVAFAEAAGFVGLGRGKLSLISQMGLTEFSYCLTPFGSRKKSTLSIGSLPNPNATAHPVMSTPIVRNKSWPSFYYITLNGITVGGTVVDIPSSTFAINGDGSGGMIIDSGTWLTYLEYSAYDKVADAFTAQIKNMNTTDQSLFDLDLCYELPPKSTPDTLNLPKLIFHFQGADLELPPGNYFGVDSDTSSICLMMAESSGLSVFGNFMQQNMQVMYDLGNDVLSFYSAECG
The following text describes a protein:
Function:
Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Sequence:
MQIIIVGTFVHTPSISNLEIFDGTVGVNNGLIVFLERSTMEETVRQAKLLPGMADSMVLRLSPLEFVCPGMIDTHIHAPQYANCGLGIDLPLLEWLDKYTFPLEKSMTKLETAFRSFSQVVHRTLEHGTTTASYFSSLHAHSSALLADLCYHHGQRAFIGKCNMDTLAPDDYRECSAEASVDATQDLIRFMSKLDPSRTLVSPIITPRFAPSCSEQLLCECAALAKTHNLPIQTHVSENKGEVDLVKRMFPNNTSYTDVYDQAGLLTPRTILAHAVYLTSNEVSTIAARGSGVSHCPTSNAILSSGLANVRYMLTNGVKVGLGTDVSAGYSVNMLDSIRQAAMTSRQLSVLHSNNQIALSLAELFFMATLGGAQLLNLGDRIGSFALGKTWDALLVDVGGSNAGATIDVFGTETKEALVSKWVFGGDDRNLRRVWVNGVCVAGTDLLSSKCEKCEHCLQHTKAIEVPVTRTVAEQASAFAKPVSTTDNEKEQISIQSKA