lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Endoribonuclease that functions in the interferon (IFN) antiviral response. In INF treated and virus infected cells, RNASEL probably mediates its antiviral effects through a combination of direct cleavage of single-stranded viral RNAs, inhibition of protein synthesis through the degradation of rRNA, induction of apoptosis, and induction of other antiviral genes. RNASEL mediated apoptosis is the result of a JNK-dependent stress-response pathway leading to cytochrome c release from mitochondria and caspase-dependent apoptosis. Therefore, activation of RNASEL could lead to elimination of virus infected cells under some circumstances. In the crosstalk between autophagy and apoptosis proposed to induce autophagy as an early stress response to small double-stranded RNA and at later stages of prolonged stress to activate caspase-dependent proteolytic cleavage of BECN1 to terminate autophagy and promote apoptosis. Might play a central role in the regulation of mRNA turnover (By similarity). Cleaves 3' of UpNp dimers, with preference for UU and UA sequences, to sets of discrete products ranging from between 4 and 22 nucleotides in length (By similarity).
Subcellular Localization:
Cytoplasm. Mitochondrion.
Domain:
The nine ankyrin repeats also called 2-5A sensor constitute the N-terminus 2-5A binding domain; The protein kinase domain is predicted to be catalytically inactive. It allows the homodimerization; The ribonuclease domain is located in the C-terminus. A single active nuclease domain in a dimer is sufficient for ribonuclease activity.
Sequence:
METPDYNTPQGGTPSAGSQRTVVEDDSSLIKAVQKGDVVRVQQLLEKGADANACEDTWGWTPLHNAVQAGRVDIVNLLLSHGADPHRRKKNGATPFIIAGIQGDVKLLEILLSCGADVNECDENGFTAFMEAAERGNAEALRFLFAKGANVNLRRQTTKDKRRLKQGGATALMSAAEKGHLEVLRILLNDMKAEVDARDNMGRNALIRTLLNWDCENVEEITSILIQHGADVNVRGERGKTPLIAAVERKHTGLVQMLLSREGINIDARDNEGKTALLIAVDKQLKEIVQLLLEKGADKCDDLVWIARRNHDYHLVKLLLPYVANPDTDPPAGDWSPHSSRWGTALKSLHSMTRPMIGKLKIFIHDDYKIAGTSEGAVYLGIYDNREVAVKVFRENSPRGCKEVSCLRDCGDHSNLVAFYGREDDKGCLYVCVSLCEWTLEEFLRLPREEPVENGEDKFAHSILLSIFEGVQKLHLHGYSHQDLQPQNILIDSKKAVRLADFDQSIRWMGESQMVRRDLEDLGRLVLYVVMKGEIPFETLKTQNDEVLLTMSPDEETKDLIHCLFSPGENVKNCLVDLLGHPFFWTWENRYRTLRNVGNESDIKVRKCKSDLLRLLQHQTLEPPRSFDQWTSKIDKNVMDEMNHFYEKRKKNPYQDTVGDLLKFIRNIGEHINEEKKRGMKEILGDPSRYFQETFPDLVIYIYKKLKETEYRKHFPQPPPRLSVPEAVGPGGIQS
The following text describes a protein:
Function:
Component of the GPI transamidase complex. Required for a terminal step of GPI anchor attachment onto proteins (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSLFTFVQIRVFPFLQRHLFFLQLSLTLIGLSWIFILPRNEIIDRLHVSESALLPGQVNTYFENRYSKTVSSSLTAANTWSHLDASVGTNTMYDDLEQIFTAMGLPTQKQNYSINIPGSEFNGSNFITTLRAPRGDATESLLLCVPWKDHIGQYNEAGVALAISLLKYFQGWSLWSKDIILVIFDDPVYGPSSFLTSYFDQTTPYISYTPLKIRSGSIQAGLSLELVTTENNSDVLEVLYQATNGQLPNLDLFNTISRIFMQHFNYPLRLQGYDFHANSGSSYTSRLKSLWMGMLTQAVSNVTSAHALFPQYRIDMLTLRMKVKDPFSFDMFRFGQAIESTFRSLNNLLEHLHQSFFFYFILDHLHFISIGNYMPSILILAASFMLGAYRHWINHEKKIDLWRPFSFWLFSIFCTIAAYYLVSSSTKITVFIFLYLMLTFIGIIFSTFMTSEDAELVLSYDLMSKSLFISVVSTLNFSLSFVVAILLVPLQFISFRFNRRLSLLFAVLTYFSTFIFLCSLSKILNGPLVPFWLWAKEYELFNSWLMPSVFMILVLPEIIFSVTSFFSLWNEPSVKTKTKTL
The following text describes a protein:
Function:
Controls the rotational direction of flagella during chemotaxis.
Subcellular Localization:
Cell inner membrane. Cell membrane; Single-pass membrane protein.
Sequence:
MAKKEATPADAGAPSGGKSKLKLILLIVVGLLLAIGLSVGGTWFFLSKSLKAEKTEEVASEAAKPGKQPALYEILAPAFVVNFNQNGRQRYMQVGVALMGRDKAQMDALREHMPLVRNKLVMLFSSQSFDSLVTPVGKEMLRQQATAGLQELAKKETGQLAIEQVLFTNFVLQ
The following text describes a protein:
Function:
Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
Sequence:
MGARWCIGTSSNIPLKDNPWVENGSCILTANTGNAQFQTPDAILNTSLFPQVTAYTLVWKGEKSGCYFEQHEQRTTNNKWNKPAPGRMKCNIDVSFSSSLNKVGIALCIRDEDGSYVLAKPGWLLPFCSVEVGEALGLYNANSMIEFSRRQAYGIAHVLVKEAHYMLTPMCSLMYHHAALNIYRCQHRLYTKNISDRIPHLLLHNRTTKELCEITKHQQQNLARLPLQKFMMKNEYSPPMSPSVTFISANEYQNSMKRKSLSGNIEKKKKTKKAITPRSQAQSSKSLCGICLDSVIDSKIFATGSCNHPFCTKCISKNAKVQRKEKMNICNPFYLKKVIVDWESAIYESSIAQRQKIHCPYKNCFLLLVNDGLEGVTSCECPSCHRLFCVQCNVPWHADKNCREFQDFLKSKKGLGEKQLDKKFMQL
The following text describes a protein:
Function:
Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Subcellular Localization:
Mitochondrion.
Sequence:
MKRMMMTIGVVRACERALGRYGARLGNRQRTWRSAAVELSGTLVMPVRHFETGSTTGSVMQETETEVLKSLVGGMMNHARGFPIKGDGVEILGSPSQFYNALLQGVRDAQFRVVIASLYIGTGSLEQELLDAIADSLARKPSLQVTILCDALRTTRPFKESEKYPSSAAMLSNILSSDRVAWRKSTSRDRPKEPLRIGLYQTPMLSKMVKMVLPVRVQEVLGVCHLKAFIFDDNIIMTGANMSTSYFTVRQDRYLCFPNCKNLASYLCSLINTVALHSYNLDESGQLQPRFAHLNPVTESELFATEFSDAVKELTMPSLRTETLEGVDTWVFPTVQMGPFGIRQDEEALLWLLKQLPGGSDIHLSSPYFNLTPEYEDALLKAALEKNVTVLTSSPKANGFYGSSGVSGWIPLAYSLLEQDLHNRAMSIYDKEMNIMSIRNPKGLMIYEYERAGWTFHAKGLWCNLPGAEDGPSVSLVGSSNLGYRSRDRDLEAQVYLFTLAPRLQQQLERERDELFVDASRVTSSIFQGPDRQGGFFASLALRFMKPWL
The following text describes a protein:
Function:
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA.
Subcellular Localization:
Nucleus.
Sequence:
MENNIIEKDIIKYFQVLPEIAMKSAYKSKWTCSEIFRLLPGMCQSLLLRIIFLTERISINEMYNQFKIPNETMDEVINTIHSIHIIDKEEEDGILYIKLNNDFQSNFKMNLTGSMEPAYKIKEVNEKVSKIIQEKCLKENCIKTFEYFMNKLLQFNSQPNISNNPLRIFKDLELVKEETRQITRKGYQFLFQETKTQLWVIMLSIIGLIQRRISPFINDVFEMTYLKEHIIYNCDHFKKVYGPDPLQLFNDLGIIVYYKEQNVMAITPLMSLLRSNANIPSDLVKKPKTITEINYSVYIYTESQFQVDLYRLFIRKNFQLANLWVGKLNHQSVTEAFAKGITSEMLINFLQPNLPRTIQKQIDLWKKEINRFKEEHVVRYRFYDDAIGRQLFVIVKNESDRLKATILEKEDIRLIFVKYQYGETIRSFMKKKERELLLKQPRPSSTSLPLSLSTDNSKNNIHSGIKRNVPEGIKPKPSKKYIVD
The following text describes a protein:
Function:
Specifically dimethylates a single guanine residue at position 27 of tRNA(Tyr) using S-adenosyl-L-methionine as donor of the methyl groups. Dimethylation at position 27 of tRNA(Tyr) is required for efficient translation of tyrosine codons. Also required to maintain 3-(3-amino-3-carboxypropyl)uridine (acp3U) in the D-loop of several cytoplasmic tRNAs.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MENMAEEELLPLEKEEVEVAQVQVPTPARDSAGVPAPAPDSALDSAPTPASAPAPAPALAQAPALSPSLASAPEEAKSKRHISIQRQLADLEKLAFVTDGNFDSASSLNSDNLDAGNRQACPLCPKEKFRACNSHKLRRHLQNLHWKVSVEFEGYRMCICHLPCRPVKPNIIGEQITSKMGAHYHCIICSATITRRTDMLGHVRRHMNKGETKSSYIAASTAKPPKEILKEADTDVQVCPNYSIPQKTDSYFNPKMKLNRQLIFCTLAALAEERKPLECLDAFGATGIMGLQWAKHLGNAVKVTINDLNENSVTLIQENCHLNKLKVVVDSKEKEKSDDILEEGDKNLGNIKVTKMDANVLMHLRSFDFIHLDPFGTSVNYLDSAFRNIRNLGIVSVTSTDISSLYAKAQHVARRHYGCNIVRTEYYKELAARIVVAAVARAAARCNKGIEVLFAVALEHFVLVVVRVLRGPTSADETAKKIQYLIHCQWCEERIFQKDGNMVEENPYRQLPCNCHGSMPGKTAIELGPLWSSSLFNTGFLKRMLFESLHHGLDDIQTLIKTLIFESECTPQSQFSIHAPSNLNKQEENGVFIKTTDDTTTDNYIAQGKRKSNEIITNLGKKQKTDVSTEHPPFYYNIHRHSIKGMNMPKLKKFLCYLSQAGFRVSRTHFDPMGVRTDAPLMQFKSILLKYSTPTYTGGQSESHVQSASEDTVTERVEMSVNNKAEASGYRRW
The following text describes a protein:
Function:
May function as sodium-coupled metabolite transporter across the chloroplast envelope.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Plastid, chloroplast envelope.
Sequence:
MATAAGGERPKDVDAGATAAGPKAIYCYHAMLATSAGVWLGDNPFRFSLPLLFYQIIIIFVVSNLTHAVLRRLGQPLVISQIVAGLLLGPNFLGRNLWFSRVLFAHRSFQQLQIISIVSTMIFVFVVGVKADLGMIPRVRKKALSIAVLGTLLPYVSVYGMAAALRPQMPPRFANSSIFIILARTWCISSYTVVSCLLRELNLVASRLGRLAMSAILMADFIHVFADACVGTYLMPDTQGAPLNGFSAICSFLGLVVIVMFIMRPLVLWFIRQTPEGALLSGVNFVAVLLMALASGLMTNIFGFHYYMGPFFFGLVLPGGAPLGTTLVDRLETLVTGVLLPVTMAIAGMHTDLTLMADPGQWGWLGGFLVLAVVTKFVGVILPCVYSSMPHRETVTLGLMMISKGIYELGTAVGWRETEIVDSKLYTVLVVSILVLGGGTAPLIKYLYRPEDHYVAHKRRTLQHAMPGDELRVLACIHEQDNVNPVLALLEASGPFHDAPICVYLLHLMQLVGRSDAVLHPYKLKNSSSGSSATALSESDHIVNAFRLFQKQYPDGISVLPYVCISPYSTMHDGVCCLAHDKKATLVIVPFHKHIIADGSISSASSAVQAVNLNILRYAPCSVGILIDHGFSDGGLLVHRVAVYFVGGPDDREALAYGVRMADHAAAELTVVRFLLPKEWRAEGREERIDDRVLMHFQRERVDGKRVVYREEVVKDGEGTVAVIRKTSHEFSLLIVGRRQGEESPVTAGMSMWNEYPELGVMGDMLASTDFGGQASTLVVQQQKRVIRTQSTDDPETTRPRTRTPTPTPTPTPTPTPTGKRVVPREDDDY
The following text describes a protein:
Function:
Together with methyltransferase Trm7-34, methylates the 2'-O-ribose of nucleotides at position 34 of the anticodon loop of substrate tRNAs.
Subcellular Localization:
Cytoplasm.
Sequence:
MVLISDAFGLEISPNGILVGHGDQAVLYSSEPKVELPVQLREGKVRGFAWSSLRKSQRLLLLYSENEYSLIRCTTSSENDLFQLVYEGETRDWINAALFLEDENESEDRKRFVLHTSHSALLYMEYDLTSNADCTVLELARCTDSSILYYTKLHGSSFNKLAIISGNAFGELLVWQTQFPTESDPKSVMKTYPLLLRIEAHNGVIHSIEFDLQSQLLVTTSDDRSVKFWNIQKSGDWTTAEIKPMFSCYGHSSRVMCVVILKIDDRTFVASGGEDSYVCIWSSSGELILKRRQQFGAPIWRLGFSQDAEILYSTSSTGNLVGQNLKEVLNRPKIESTILSSLGDANEFVRNLKFVNNEIIVGLSSLNRLYYTRISPDSSHENKWLMVNDFPSYKRTVLEVFDDIIATCGHRRITLHRYNTNTNDFEQLFDGIRMKGTIRSFQFLSRDRYLVSDNLGYCLLLQTHQLHIESHIALFNNREPWITAALLISEQYLLLGNREGHVMLYCRSSASDDFQLKDSIRYLHGKMGSNFFKLLSLNADNAHVMSGGHEAFLKYLSVRFSDSTLRVSQREGIPLAWVEASPSDDLILGFNDNHIVAWSRRNDILLQLACGGGHRCWDFRLSDGDSQLSIAYVKQKRVYFYRNSLYNAVDNRLKDIEPNNWHVRNCNTLRLITPRNQSDPFILSAGDDNIIKVTQVTNDSLSQRAEMHSHISTVRSLQAIPYKSNGGDSSTWLVFSVGGRSQLCISQLSIDASNKCWISEISSHTLHNVAASKTSTIEARLMAIDVVQHSDGDLFSIYVAGGDGNISHYIWELETPNQLDLKHFVDIQRCPLGIQWIASKGMLLVSTTNGEVYGFDRTLETTYFQLQLHVTGINTIDIYVDRHLLHILSGGDDESIKYTVLNLNNNNVEQKIEYLGLHNAQVNALAIHCPTKSVAASELFAYTCSIDRQIYRIDLSTHKYKRVGYTCIADVKGMLLDEHQRMYFYGCGLQTMSISNIL
The following text describes a protein:
Function:
Probable sugar transporter.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins.
Sequence:
MSLTKKIKNEKSLKQEKQTDQLKSNLRNNNNNINNKSKPKDQNLNTLHYIKTHLKEELFFIFCVGGIYIFYLLYGLVQEQLNVTKFGTEKKVFGFTAFLLALQCFFNMVSAWLVSLVNKEQKDNTPFMKYGFVSMLLVISTFLSNQSIRYISYPTQVLAKSCKPIPVIFMGLLLFKKKYPFLKYIVVIVISLGISLFMLPKATSKKNIQFEGHDHLFGNFILFVSLMMDGVMGPFQDNLVRQYKPSATSMMLNTNIWNLGLFSIMAFARGEVSQAIDFILEYPEVIKLILAFCITSAIGQQFIFLTTNKFGSLNCSTITTTRKFFSILVSIFYFGHSLDNLQWAAICMVFGGLILDLYISYSNKKKGVVLSPIAAPVKHPTATTPLENKKSL
The following text describes a protein:
Function:
Component of the SCF(sconB) E3 ubiquitin ligase complex involved in the regulation of sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor.
Sequence:
MGSHSKAIPPSDKPCTSIPPNLLPSAPASPPTPAPSPTPHQRLPSWRAPEQEEDALLLNTKFFESLSGPRRQQYLEAILSLCSSQQLSFVSSYVAPRLRKDPFRVFPTEISLRVLSFVEDPKTLARASQVSKRWHALLEDDITWKNLCEKHAFTHRRPAEDNQDIIESIHNHRTNSLSGLQRRPNSATIQSRDGFADIPRSLSGDWIASSSIQTRKRRVRPLSYKYHFKQKYMIESAWSKGGRCTQRHISPDQGVVTSLHLTPKYIVASLDNAKIHVYDTNGENQKTLEGHVMGVWAMVPWDNILVSGGCDREVRVWNMATGESIYLLRGHTSTVRCLKMSDKNTAISGSRDTTLRIWDLRTGTCRSVLVGHQASVRCLAVHGDIVVSGSYDTTARVWSISEGRFLRALSGHFSQIYAIAFDGRRIATGSLDTSVRIWDPNTGQCHAILQGHTSLVGQLQMSGDTLVTGGSDGSVRVWSLTRMAPIHRLAAHDNSVTSLQFDNNRIVSGGSDGRVKVWCLRTGQLLRELSTPSDTVWRVTFEEEKAVIMSSRSGRTVMEVWSFSPPPEDTEFDAATIGASSSISEPPPVRDSHPIRPLVLPDLPQRSDGDQVMVDVPP
The following text describes a protein:
Function:
Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that mediates the conversion of QA-mono to QA-di via the elongation of the C-3 sugar chain with a D-galactose.
Sequence:
MGSNTEATEIPKMPLKIVFLTLPIAGHMLHIVDTASTFAIHGVECTIITTPANVPFIEKSISATNTTIRQFLSIRLVDFPHEAVGLPPGVENFSAVTCPDMRPKISKGLSIIQKPTEDLIKEISPDCIVSDMFYPWTSDFALEIGVPRVVFRGCGMFPMCCWHSIKSHLPHEKVDRDDEMIVLPTLPDHIEMRKSTLPDWVRKPTGYSYLMKMIDAAELKSYGVIVNSFSDLERDYEEYFKNVTGLKVWTVGPISLHVGRNEELEGSDEWVKWLDGKKLDSVIYVSFGGVAKFPPHQLREIAAGLESSGHDFVWVVRASDENGDQAEADEWSLQKFKEKMKKTNHGLVIESWVPQLMFLEHKAIGGMLTHVGWGTMLEGITAGLPLVTWPLYAEQFYNERLVVDVLKIGVGVGVKEFCGLDDIGKKETIGRENIEASVRLVMGDGEEAAAMRLRVKELSEASMKAVREGGSSKANIHDFLNELSTLRSLRQA
The following text describes a protein:
Function:
Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX.
Sequence:
MFQQQLVNHLPYLMALDKSKDLESIGYYLSEHLKVAGGYWTINAIACLNKLDDISEEKKQQLSKWLKECQNQDGGFGGNTNHDSHITNTHYAILLSFLLNCELDYEAAAKYVAARQRKDGSFEGDQWGEVDARFSYCGLSSLTLLNKRDLIDVKKAASYIKKCRNFDGSFGGIPDAESHGAYVFCCVGTLYLCEDLSFNIDELSMWIHERQTSKGGLNGRPEKLADVCYSWWMYSALCLLKREQWINQQALENYILECQDSDGGIADRPNNQADVFHTFFGLAALSLLNGDKYQLNPIDPAFALPKSILKNIPGASRFIQS
The following text describes a protein:
Function:
E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in DNA double-strand break repair by homologous recombination. Is not be required for the stability of the complex. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. Acts as an E3 ligase mediating SUMO attachment to various proteins such as SMC6L1 and TSNAX, the shelterin complex subunits TERF1, TERF2, TINF2 and TERF2IP, RAD51AP1, and maybe the cohesin components RAD21 and STAG2. Required for recruitment of telomeres to PML nuclear bodies. Required for sister chromatid cohesion during prometaphase and mitotic progression.
Subcellular Localization:
Nucleus. Chromosome, telomere. Nucleus, PML body. Note=Localizes to PML nuclear bodies in ALT cell lines.
Sequence:
MPGRSTSSSSSGSTGFISFSGVESALSSLKTFQSCISSGMDTASSVALDLVETQTEVSSEYSMDKAMVEFAMMDRELNHYLKAVQSTINHVKEERSEKIPDLKLLVEKKFLALQNKNSDADFQNNEKFVQFKQQLKELKKQYGLQSDREADITEGVDEDMIVTQSQTNFICPITQLEMKKPVKNKVCGHTYEEEAIVRMIESKHERKKKACCPKIGCSHVDMRMSDLIQDEALRRAIESHKKRRRQSN
The following text describes a protein:
Function:
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in endosomal cargo sorting.
Subcellular Localization:
Endosome.
Sequence:
MPTTQSYYSSYPQNSYPIQVPQKPGYYYPPQHTYGRVSGSPPEAPDSVTTSGVASYEPSAASSNYAGSASDYESTNGATSVDLLDYMGNRLNGSFDPMPLDRSLAKQAQTSGELNAKHRELLELQQLAQRRLMGAQASFAEGMKAAKEVQKDLQWTQKRVDALNDRAARKYPEQFRSAQRRYPAPVDY
The following text describes a protein:
Function:
Transcription factor (By similarity). Involved in development of the hindgut, the male tail, and the excretory duct cell. Involved in modulating function of excretory duct cells. Plays a role in left/right patterning of cell fates in the hindgut.
Miscellaneous:
MISCELLANEOUS: Differences in the regulation of lin-48 expression may explain, at least in part, differences in excretory duct morphology and function between C.elegans and the related species C.briggsae.
Subcellular Localization:
Nucleus.
Sequence:
MDSRVWLPLIGAHLLPRDISVITQMIANNNNTSISRSSTNSSKPEEKNSKKFLIERFLDDDPSPPASILSPSPKAAIPSPIINPAVEFVNGGYGVKNPLAPLISSFETTSIPCSTVSPSSLISSSKDEFQDSLTCHICGKKFGLQRLLNRHIKCHSDLKRYLCTFCGKGFNDTFDLKRHTRTHTGVRPYKCEQCEKSFTQRCSLESHLRKVHGVTHQYAYKERRSKVFVCEDCGYTDEKFEVYLSHIKVVHPFSAAYLRFTQLQKKNSSMKPEQLSKISL
The following text describes a protein:
Function:
Anion-transporting ATPase. Catalyzes the extrusion of arsenite.
Sequence:
MTRIIIFTGKGGVGKSSVAAAHALSSAKSGKKTLLVSADTAHNLGDIFKIQIGSKIAKISENLDALELDSDVVKREIFPEVKNTMLDLMGKSGIGITNLNENFSLPGFENLFSLLKIKEIYESNQYEHILVDCAPTGETLALLKLPELLAWYMEKFFPVGKKIVRILSPISKLAYKVILPSVKTMDTIELIHQKLLELQELLKNNEICSIRLICIPEKMIVEETKRNFMYLNLYKYQVDIVFINRIITDEIENPFMQKWKKIQSKYIKELEEVFFNIPVVKVPWYPKEIVGKSGLKLLCNTIENLPDLFSVKKVTQNEEYFPCEDGYLLKIQLPFVKEEELKIYHHEMDINIKINNVNRCIPLPNVLRKSHIVDTKLENGNLYVHFQLEKKKEEKS
The following text describes a protein:
Function:
Required for vacuolar protein sorting.
Subcellular Localization:
Cytoplasm. Membrane; Peripheral membrane protein; Cytoplasmic side.
Domain:
The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Sequence:
MSLFSAATTAVERTGYGSRYDHIFDMFHPIDGRIPAVCYKRLLETINVSGEDKDRLATLAGSILEGGDGSGGILTSSFTRESWRAALLLANVAQDGLPFDDPSQLVNVDTLTPMDFSEEGERSSINFSASTTGRSQTPLFGDDLDDHSIQSSRSESIIHNNGHSRGHSALDWNPEEQEALQQSQLSQSQLSRSTTPPPLNPQALVPESESGVWTAPPRPDFAPNKADSVTLAIVPEREGMFLFRHVNYSISSVSGTDRITVIRRYSDFSWLQDYLLKKYCFRQVPLLPPKRLAVNGHYLSSDNYFLERRRRGLTRFINQVLRHPVLGQDEAVRTFVTLRNDISGWKKSVFNTAREEFNGRTIDPKFVQQWDEQQATALWAGLIVELDRSHDSVVQLCVLLDRVAKRQEAQAVDSAKIAYNLGAALPPSARVLYSVADDGCVQQITRGLSRASARIETDCQLQQDEARGSQVGVLEEAKKYREALGSMRELFDRLEKYGGNNIPLLEKRIQQNQGRVTLARQRKALMSEIEKLDRAIKMDTEMIAAHKNRTWLIRECITEEIGLFQKTQLQISKLLQEFCVDKIKYAELYSDNWGGLDNDVMDLPV
The following text describes a protein:
Function:
Cytokinin hydroxylase that catalyzes the biosynthesis of trans-zeatin via the isopentenyladenine riboside 5'-monophosphate (iPRMP)-dependent pathway. Can use isopentenyladenosine-5'-monophosphate, isopentenyladenosine-5'-diphosphate and isopentenyladenosine-5'-triphosphate as substrate.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MLLTILKSLLVIFVTTILRVLYDTISCYWLTPRRIKKIMEQQGVTGPKPRPLTGNILEISAMVSQSASKDCDSIHHDIVGRLLPHYVAWSKQYGKRFIVWNGTDPRLCLTETELIKELLMKHNGVSGRSWLQQQGTKNFIGRGLLMANGQDWHHQRHLAAPAFTGERLKGYARHMVECTSKLVERLRKEVGEGANEVEIGEEMHKLTADIISRTKFGSSFEKGKELFNHLTVLQRRCAQATRHLCFPGSRFLPSKYNREIKSLKKEVERLLIEIIQSRRDCAEMGRSSTHGDDLLGLLLNEMDIDKNNNNNNNNLQLIMDECKTFFFAGHETTALLLTWTTMLLADNPTWQEKVREEVREVFGRNGLPSVDQLSKLTSLSKVINESLRLYPPATLLPRMAFEDLKLGDLTIPKGLSIWIPVLAIHHSEELWGKDANQFNPERFGGRPFASGRHFIPFAAGPRNCIGQQFALMEAKIILATLISKFNFTISKNYRHAPIVVLTIKPKYGVQVILKPLVS
The following text describes a protein:
Function:
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MIVGQSLQKGNLVKHNVQKEHTRVFPFIWGSIEEEGKNLTSSVTPYSSITSVYERRPLQHLKSPFMRPPSVRFNSLSVIILKDSEASLRASILFCFHPTSIFFSSIYSESLYAVLSIGGIYFLISGANLLALSSLAFSVLSRSNWVLNACYIGFQTIHRAYDVLPIKVLIYVIMRRLFVFCSICWISSIWISQGAGFLKYFQLKQLPNFLLASRILSIAIWLITHYVKLQPEAFFSLGFQVAPKSNVVDRNNTRISTTTQEYQTLKRRKHSTKEEEVPTPSVP
The following text describes a protein:
Function:
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MESKEKIVSCLNILKRLPPTQIQKNAAALASLIPDYAEELYQKIDKPLDIGQDEKGNQFIQSEFNRDGDSFRSYLTNSYYPAIDDAVYPSEALRKLEIKANAVFDEYRRLYYEGGLSSCYFWDKEDGGFATAWLIRKNVEKSKGIEDGSWSSINVIDIKTDGKSKWTYKITTSVVLEMNIIENQDVGKFNITGTLTKQKEESFEAPAGNKDLDLFHIMKIGTLVEDVESYLRSQLDSVYFGKTKDIVFQTRFSEGQKHFLQQRQELAGEFKQKYG
The following text describes a protein:
Function:
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Subcellular Localization:
Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it.
Sequence:
MSFRHLKTIAIPPSERVKCVELHPTEPMLVVALFDGNVQIYNTNDWTILRTIHVSPTKPVRCVRWMTSINAVITSGDDLSISAYDYNTGTLIATQKDAHADYIRSIAVHPSQPLILSASDDTKIKLFRIENNSFKEEHEYTGHKHFVMDVKFNPKDPNQFASASLDNTIKFWGINESAPRFTLSGHIAGVNCIEFCPSADKTILVSGSDDFTIRFWNLQNNKEIHRLASNNPNDTNFHTGNVTSLRFHPKFPLLFSTGEDNKFFIWNTTTYKREMSFNTNKGRGWTIDSNDTTIALGCDEGLSIMQFENTTALVSTDTQGRTYWALNNEIKYTNLAQGKNPEDGKLVDLKIEDRATVDFYPAYTSINPSEKNVALCGEGNYYIYSMIGFRVKESGSANEFAWGSGDYFATRLGKQVTIHKLKGNPQKLTHGVNVTSIFGGHLLGLASNESIFFYDWQFLNLIRQIDVKATNVWWCGANKVAIATDDTLYVLVYTQPKKEDDYENAFFVESQIEVSVKSGCWYENAFFYSDGRSVSFIMEDRSEVIARFDKPYQISGYAKNTERIYLYDRDVNFISYSVPISLLKAYKKVLRFDEEEENEEEEEENLDIDETAIPSNWLLRFTSLLEEKGQFRRALKFAETDDKIFELALKIPDFNLAISIARKTKSLVQWHQISTIALKEGQIDLLEEALKVSGDENGLLLLHSACKRKKQMKELAESVSNAKNVSFAAYFSLGEYSKCIDILLETGREPEAALMARTYLPRRINECVELWQKKLRERGDHRLADSIASPKEYPNLFGIEDQQQEEEQQQEEEEKVEIPKVDSKKEEAKEEKVEEEEEELDVDDLLAGIDTGAEEDI
The following text describes a protein:
Function:
Binds the phosphorylated C-terminal domain (CTD) of the largest subunit of RNA polymerase II and functions as a scaffold for RNA processing machineries. May be involved in pre-mRNA splicing.
Subcellular Localization:
Nucleus.
Sequence:
MYAIFGCFLALETRSLLIKGERGIFDGGPGQGWCWDGMLGILLNGSRYYYNKGTRTSKWRIPDEVKLAREKDIISHASDFGSIPVVKTSSPGVDGSLLSAHVEMKNSSEPSSPTVANSEKIGIAVTLGNSVSPPVSETTSAQDAVVYGDGFSLENREKDAALTEIGGATPSNEKTVELGPLVYESKAEAKSAFKTLLQSANIGSDFTWDQAMRAVINDWRYGALKSIGERKQAFNEYLSQKKKLEAKERHVKQKKAREDFRIMLEASSQWRKVQDRLETDERCSRLEKINCLEIFQEYIRDLESEEGEQRKLWMIKDFAAYLVVSSNTSGSTAKDLFTDVMDELEKQVLRRSLGVQILSRVYRQGCLRVQLVSLLCFGRPSHLDRQKAFRAFGLGNAHHGNGGGGSVMVEWLLVASVADGGGKGGDTSVVMVSKECVEVDDVLVVVNDAWKLMMC
The following text describes a protein:
Function:
Transcription factor expressed after fertilization required for zygotic genome activation (ZGA), a critical event in early embryonic development during which the developmental control passes from maternally provided mRNAs to the expression of the zygotic genome after fertilization. Binds and activates expression of key ZGA marker genes, such as NANOGNB, ZSCAN4, DUXB, KLF5 and DPPA3. Binds to regulatory DNA sequences containing a 5'-TAATCC-3' sequence motif.
Subcellular Localization:
Nucleus.
Sequence:
MQDPGHLQGPPLALDPPRRQRQERTVYTESQQKVLEFYFQKDQYPNYDQRLNLAEMLSLREQQLQVWFKNRRAKLARERRLQQQPQRVPGQRGRGARAAPLVPVAAASFPGGPEFPQGRGSWISPQPGPWGVLPAAEPKIYSLPRTWGGPECGTQEGLKAVPAPGPGPIPAPIPGPAQIPGPVPGPAPNLGPMSGPLSVSIPGPIPAPISCPGPIPDPVLGRTLMPGPGSLPTPAPGALWPQSPYASNLSPDTQLYPDFTKLLPLLDRFEESSLSTTTSQYKEEDGFVDKNHSVPRSLLDL
The following text describes a protein:
Function:
Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. All amino acids serve as attractants in B.subtilis, they appear to cause an increase in the turnover methyl groups, leading to methylation of an unidentified acceptor, while repellents have been shown to cause a decrease in methyl group turnover. The methyl groups are added by a methyltransferase and removed by a methylesterase. McpC is required for taxis to cysteine, proline, threonine, glycine, serine, lysine, valine and arginine and for aspartate, glutamine, histidine and glutamate. Primarily mediates response to positive stimulus of PTS carbohydrates. Greatly influences the duration or magnitude of the response to negative PTS carbohydrate stimulus.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane raft; Multi-pass membrane protein. Note=Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion.
Sequence:
MFKKLHMKIAVFVSIMLIITVVLLMLSSYLTLKPMITEDGKNTTQNVTQSLEQNIELQLKSYAISLSRLANGELTHTFVTKPSKEASRLFHDDIKQIKDNDDYVAMAYIGTAKKEMFTYPKADFAEDYDPTSRPWYKLAAETPDQVVWTEPYKDVVTGDMIVTASKAILDRQKVIGVASYDLKLSAIQSMVNKQKVPYKGFAFLADASGNLLAHPSNQGKNISKDQTLQTIASEKKGIQDVNGKMVVYQTIGETGWKVGTQFDTDQLMWISDKMNRANLWISLIALIITIILSYFLAKTITGPIQQLIVKTKAVSAGDLTVRAESKSKDEVGILTRDFNLMVENMKEMVEQVRLSSGKVSDTSEQLTAVAAETNETSGQIAKAIEEVAAGASEQASEVETINEKSESLSTKIRQIAEEAGGIKERSKSSEDASYKGLDALGQLLMKSNEANMETKKVETMLLDLENQTKNIEEVVTAISNISDQTNLLALNASIEAARAGESGRGFAVVADEVRKLAEQSALSTKHISETVKLIQLETKEASHAMVEASRMNDEQNSAIHETGEVLNTITAEMQSLVQGIDHIYAEIQRMSEEQLAISEAIQSISAISQESAAAAEEVNASTDEQLVTLDKVKHSTETLKHASQELMNTIAKFTL
The following text describes a protein:
Function:
Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein. Cytoplasmic vesicle, COPII-coated vesicle membrane; Multi-pass membrane protein.
Sequence:
MQNYDKKEVGSVPGAMPDFRGNDGSLVSVLKTLLFFTILMITLPIGLYFTSKSLLFEATLGYSSNDSYFYAAILAVLAVHVVLALFVYVAWNEGSRQWREGKQD