lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in cell wall biogenesis. Has a role in the addition of Gal-beta1,3 moeities to galactomannans and their subsequent pyruvylation. Has a role in meiosis.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein.
Sequence:
MFSNSKKKIFLYVLIAGVATFSFAFLVLNRLQAEEHSLAYVENLFLDPFIKQNESLAHANDRPFKLYLGIFSQAKNVDRRNFLRTDYNEYIKEFAVNDTVDVRFILGLPENEQELATIREEQRTYGDLAVLPIPENVDAGKSIVYFQTFLEGYQPFPLFSELADNLIMPSTQFHGSFIYNQSIKTYELPGMKEFQDLGEPKHDYDFIVKADDDSFLNLPRLFEMLKEHVGKSRFYFGRDCTRRELPTAVRDFPYMCGFFYIVSPDMAYEVAKRRNIIIPFEDAQTGYSIYLSGNVKNAEFSKCTLYDLILPNEGFNYRQSYLRIDAIAVHKLKSIPLLSTVSNWFKKMYEHRANCSALIETERLSCLQATIPLPSLDV
The following text describes a protein:
Function:
Probable methyltransferase.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MIGRTFKTDIADYETARPDYPPQITEWLNDEFSVNETSTILELGAGSGKLTPRIIASQPKEIIAVDTYVEMLDVLKKKFPNVDCRVGSAMAIPLEDESVDLVACGQCFHWFANEEALKEIYRVLKPNGKLALIWNIRDNSVPWVEKCSQLLEKCRGGPLNMFEKAAELFPGYGFTELKQSLFTSAKKYSIEDLHRLMNSFSSINRLPVEEKEKMHAELDEIIKTIPRAQNTDQVDFNILTVAYSSEKVPIN
The following text describes a protein:
Function:
Efficient electron donor for the essential enzyme ribonucleotide reductase. Is also able to reduce the interchain disulfide bridges of insulin.
Subcellular Localization:
Cytoplasm.
Sequence:
MSTFNTRCPSCHSLNRVPEERITESPNCGKCQSALLDGAPIEGTEANFSALLQSDKPVVVDFWAPWCNPCVGFAPIFSDVAAERKGQIRCVKIDTEAQQNLAAHFQIRSIPTIMVFKNGQRIDMINGALPKSQFDQWLNQALTK
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins (Probable). Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Displays a preference for substrates with a lysyl residue in the P1 position.
Subcellular Localization:
Cytoplasm. Periplasm.
Sequence:
MTTPTFDTIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGIADALEGKHPAVPVDVVHRALREIHERADAVRRQRFQAMAAEGVKYLEENAKKEGVNSTESGLQFRVINQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGSKWELTIPQELAYGERGAGASIPPFSTLVFEVELLEIL
The following text describes a protein:
Function:
Probable aspartic protease that is responsible for the proteolytic cleavage of the RNA polymerase sigma E factor (SigE/spoIIGB) to yield the active peptide in the mother cell during sporulation. Responds to a signal from the forespore that is triggered by the extracellular signal protein SpoIIR.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Note=Localized to the sporulation septum.
Sequence:
MKIYLDVIWLLNFCFDALLLLLTAFILKRHVKKRRLVGGAFIGSSIVLLMFTPFSPIVEHPAGKLAFSVVIVVVTFGFKRFRFFFQNLFSFYFATFLMGGGIIGAHSLLQSNSIVQNGVMITNQTGFGDPISWLFIVGGFPALWFFSKRRIEDIETKNIQYEERVSVQADLGSQTLHVRGLIDSGNQLYDPLTKTPVMIIYIDKLEPIFGTAETMIIRNTDPLEAIEQLDDSFRFLDKMRLIPYRGVGQQNQFLLCVKPDHVTIMTKEEMISADKCLIGISTTKLSADGEFDAIIHPKMLSGKAVKHVS
The following text describes a protein:
Function:
May be involved in the generation of 28S rRNA.
Subcellular Localization:
Nucleus.
Sequence:
MVTRKKPVKRNAEAAEIQVEQEEDASQPKVAKELMVVAQEVKIIRALACNDVVERNRQIRILRKWFKARAGSSFPFNEDDFMRIWKGLYYTMWMSDKPLVQEELAEKLAQMVDSFGGNTACSLAYFSAFMRTMCQEYFGIDQWRMDKFLMLTRRMVRYLLRFLKQNNWNADLIAAFNSSMQLSVMSEQPKSRGMTMHYLDVFFEELAKAANGEITAAQVNMFLRPFVTYIATQRDAKLVAQCRTRVLYHLMYQSDLGRQYSEKYNAWKQMGFPTASIDDIEKLDSGFDEEDDEVNAEEEQPRATSLDPRAGNVDVHMPELPLNADCVLDELQTQLRTNDFNSKRRKGLRKLIQIFETYQRGEFPLGVRTMPKVEGQTLSEMVEQKVAALDKMEDEVFATGRKLKKLNKSKRKRLLQSINFEEVDEHNYDEVISKALPPELQKKVNYNAKVRSSINNAWVVEEVKEAEPKSKKAKKEEPPQQNKDDQTKVKKKSQLKPKNDQSKPKIEDQPTLKAEKEEPAKRKKLDHSKTKEEQSKPKTDEQPKPTPKVEGQSKAKPTPKTKAAGVDDDAPTNGWDAPLEDGEQDIFVPSRKLQVKQANSKLPQSTPKQPARAEFATPQTGSGKHVRIVTKSNCIYPKSDYYRQLKLSPQVPYDANRLPGKSALKPHWIPGPIHPSYKAKRLFNDTL
The following text describes a protein:
Function:
Involved in the biosynthesis of the antimalarial endoperoxide artemisinin. Catalyzes three consecutive oxidations of amorpha-4,11-diene to produce artemisinic acid, with artemisinic alcohol and artemisinic aldehyde as intermediates products, but is unable to oxidize germacrene A. No activity with limonene, alpha-pinene, beta-pinene, pinocarveol, (-)-alloisolongifolene, caryophyllene, (-)-alpha-gurjunene, (+)-gamma-gurjunene, (+)-ledene, (+)-beta-selinene and (+)-valencene as substrates.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: Reduced production of artemisinic acid (AA) but increased accumulation of artemisinic alcohol (AAOH) and artemisinic aldehyde (AAA), and production of (DHAA) probably due to a lower catalytic activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MKSILKAMALSLTTSIALATILLFVYKFATRSKSTKKSLPEPWRLPIIGHMHHLIGTTPHRGVRDLARKYGSLMHLQLGEVPTIVVSSPKWAKEILTTYDISFANRPETLTGEIVLYHNTDVVLAPYGEYWRQLRKICTLELLSVKKVKSFQSLREEECWNLVQEIKASGSGRPVNLSENVFKLIATILSRAAFGKGIKDQKELTEIVKEILRQTGGFDVADIFPSKKFLHHLSGKRARLTSLRKKIDNLIDNLVAEHTVNTSSKTNETLLDVLLRLKDSAEFPLTSDNIKAIILDMFGAGTDTSSSTIEWAISELIKCPKAMEKVQAELRKALNGKEKIHEEDIQELSYLNMVIKETLRLHPPLPLVLPRECRQPVNLAGYNIPNKTKLIVNVFAINRDPEYWKDAEAFIPERFENSSATVMGAEYEYLPFGAGRRMCPGAALGLANVQLPLANILYHFNWKLPNGVSYDQIDMTESSGATMQRKTELLLVPSF
The following text describes a protein:
Function:
Transcription factor 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. Together with other Obox family members, required in early two-cell stage embryos to kick-start the major ZGA wave by facilitating RNA Polymerase II 'pre-configuration', during which RNA Polymerase II relocates from the initial one-cell stage binding targets to ZGA gene promoters and distal enhancers. Mechanistically, promotes recruitment of RNA Polymerase II from (CG-rich) non-ZGA genes to (CG-poor) ZGA genes at the two-cell stage. Binds to regulatory DNA sequences containing a 5'-ACNCCTTTAATCCCAG-3' sequence motif. Most maternal and zygotic Obox family proteins can compensate for one another.
Subcellular Localization:
Nucleus.
Sequence:
MAEGPSLHPKLQVASNIPIEIRSQIPQEPARNLAFQMSQSPLVTPGSTMQSSLSVPERNLLQQESEGSSRQSGSMPLSDKYVNKQTGPMASRKFRKERTVYTKEQQRLLQKHFDECQYPNEKKIMELAVSVGVTKMEIKIWFKNNRAKYRRMNLQNIKQALPESNGISKAVSESTHFPGSIPVVASDNGESMCSGTFGEDSMPKFNCSQESSLYCFQACDGDMCCPQEYLLDGHAPVTAWNSGQSAAVEYQTDIAVAEAPVRLAYAAQAPEDAHNSGPSADELWQRILEDF
The following text describes a protein:
Function:
One of 8 partially redundant surface-active proteins required for efficient formation of aerial mycelium; the short chaplins assemble into a hydrophobic, amyloidal fibrillar surface layer that envelopes and protects aerial hyphae and spores, presumably anchored to the long chaplins. Chaplins have an overlapping function with the surface-active SapB peptide; chaplins are essential on minimal medium while on rich medium both chaplins and SapB are required for efficient aerial hyphae formation. Chaplins are also involved in cell attachment to a hydrophobic surface. Forms amyloid fibrils in vitro probably composed of stacked beta-sheets. A small chaplin extract (ChpD, ChpE, ChpF, ChpG and ChpH) self-assembles into 2 different amyloids; small fibrils at the air-water interface form an amphipathic membrane that resembles spore-surface structures involved in aerial hyphae formation, and hydrophilic fibrils in solution that resemble the fibers that attach cells to a hydrophobic surface. At the air-water interface the hydrophilic surface is in contact with water (probably equivalent to the peptidoglycan layer), while the hydrophobic face is exposed to the air, making the surface of the aerial hyphae hydrophobic. A minimal chaplin strain capable of forming aerial mycelium/hyphae on minimal medium contains ChpC, ChpE and ChpH. The strain also has restored rodlet formation on the hyphae surface. A small chaplin extract applied to a chaplin-deficient strain restores aerial hyphae formation. The small chaplin extract forms an amyloid-like structure similar to that seen on the surface of cells without rodlets (rdlA-rdlB deletions), and is highly surface active, reducing surface tension from 72 to 26 mJ/m(2), which probably allows escape of hyphae from an aqueous environment into air.
Subcellular Localization:
Cell surface. Secreted, cell wall. Fimbrium.
Domain:
Has 2 domains capable of forming beta amyloid structures, both of which are required for aerial hyphae formation while the N-terminal region is not required for rodlet formation.
Sequence:
MLKKVVAAAAATGGLVLAGAGMAVADSGAQGAAVHSPGVLSGNVVQVPVHVPVNVCGNTISVIGLLNPAFGNVCINK
The following text describes a protein:
Function:
The M-Pol II complex possesses alpha-1,6-mannosyltransferase activity and is probably involved in the elongation of the mannan backbone of N-linked glycans on cell wall and periplasmic proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus membrane; Single-pass type II membrane protein. Note=Cis-Golgi. Recycles between endoplasmic reticulum and Golgi (By similarity).
Sequence:
MKANRDFGRDGGPFSITPNRFQPKSSGNPIFRQKTIRTVGIIALTLVLFLFFHRSFFSSFGEFPSFSSTANAPNSDVQEYDLRKVMNAKFTGDYSPKEKVLICAPLRNAAEHLNMFFGHMNNLTYPHELIDLAFLISDTDDNTLEVLKQHLDAIQNDEDESKHFNNVLIMLKDFGAIFGQEFSDRHGFAAQGPRRKLMARARNWLLSAAIQPYHSWVYWRDVDVETAPNTILEDLMRHDKDIIVPNVYRPLPDWLGNEQPYDLNSWAESETALQLADTLGEDDVIVEGYAEYATWRPHLAYLRDPNGDPSVEMPLDGIGGVSIMSKAKVHLEGCEFPAFSFEKHAETEGFGKMAKRMGFSVYGLPHYVIWHIYEPSDDDKRIMAEMERERKEREAAELEEAKKYQTAGFTQPDDQGAEEGPLAHADDHVD
The following text describes a protein:
Function:
Acts as a ribosome collision sensor, splitting the ribosome into its 2 subunits. Detects stalled/collided 70S ribosomes which it binds and splits by an ATP-hydrolysis driven conformational change. Acts upstream of the ribosome quality control system (RQC), a ribosome-associated complex that mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes and their subsequent degradation. Probably generates substrates for RQC; Endonuclease that is involved in the suppression of homologous recombination and thus may have a key role in the control of bacterial genetic diversity.
Sequence:
MEKALKILEWEKIISEIEKEAETEGGKAKIRSLKPITDYSIIDRWHLLNEEAFKTIYSFGYPSFSGIRNIEIYIDKAEKGGIVYPDEFEEIVKTLEVWGKLRDYQEKVRKTAPNLWKNTLHNLHDLYIQIRKCVQDGAVIDSASPELKQIRQKKERLNQKVRETLENIIQKEWRGYLQDQIITIRHGRYVVPVRQEFRGKIQGIVHDQSTSGLTVYVEPQVIVELNNQIALLESEEKREIERILTRLTSVLLSYKEEILENLRTSFELDFVYAKVKWAEKYKAITPILEKDKPIVILREARHPFLGDKAVPITLEVGRYFHTLVITGPNTGGKTVTLKTIGLFVLLNQAGIPVPAKEGTTLGIFNQVFADIGDEQSIEQNLSTFSSHMTNIISFIDYLERTGDKKVLVLIDELGAGTDPQEGAALAVALLEYFHEKGTINVIATHYPQLKVIASKYPGMENASMEFDEISLRPLYKVAMGIPGKSNAILISKRLGLPRKILDRAVSLLSENEIKLEEVIGELQKDRRKYQEEIDKINKVKKELQEEKKRILEEREILEKEKEKLKTKYKEELFKDISKIENRLKEIIRRLQEESLSMKDAQSLQEEVKKLKKELVLEEREEPKALSYVPQVGDRVVLRSTKKEGYVIEVDADEKIALVQVGLLKIKVPWTELAPSLKEESQLFSYVKVEKINQESIPREINIRMMTVDEGLEEVKKYLEKAFLAGLKRVRIVHGKGTGKLRNAVHDYLSKVPYVKEYYLAPPNEGGEGATVVILDSSI
The following text describes a protein:
Function:
Catalytic component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling.
Subcellular Localization:
Nucleus.
Sequence:
MSPGDSALDYAKRQAGNVSSQAPSRPSSENDANGTVSTSNEHPSNEAGPSRPRSMGSERSASPQQGTTPKVPTKRRRLNAELAFSSPGPAFQVEQHGSEAQSDSNDSSGRARRPRRSTTLTKSGSNESQDRRSSAHIPKRKEEAGESRNLAESVPKNKLKLNNGKARASDEVELRESSLSLVLPSRSRSRSKSVVKLEPDQDSAFPQEVATPTLQPTRPKPQITPLTALNPQAALSEILARRRSERIALAQSDLEDVHDGHDMLVRELFHLTKFVTMVGYDPDVARTDQSDVFTTFKHAHDLRFSLDDSGSGAEASTAARVTRRRVNARLESLSLKRPDPPSTPSTPSFSKVKVDDDKKSAPEGRRNRRFSSVTGAQPRVNGAHTLETGHSDDTDDSSEEEDSEGSDLDAYSPDGREKGDAKDYNASRKGDAKRARLSSTPHKRHRAKVQDASSNAPVKRTGPRKSKALDELDAFILRQQPRPLPDHPPPLHILAPHQIPAHRRFGGDLDALYESFNMLQDDEGGLEDDDLETYIKLDQRWRAGLPIHPEAGSTTRHAVQKVPRNKSHHDHLLESVTSSYSQMRQYAKLKQQNSRKVARMIAQHWERQLGTSEREKKAEERRLRALAKWTLREVLKQWRLAVNVVRARKAAAEKAEKEKSDKEQLNAILEQSTAMLKKQHEVMTRADSLDDSDDEGSDRTNYGSDGSAESEISDIDDDDNQLIQIQDELPSVSPEQSLDMLTPVPEEADGSKDRVSNTTDHEAATANGDPTVVVESESQPSRRPQRRTARTKTFKARDSKLDADDIEFNDAGNDDEQEDAELERQMLEEDEEDDSEDAGLAADANIPIEELLKRYGYGQEADQDAEDSDAGEDAVSNDDSLENSATKDGSEDVAAVASIKIQEDAEVEEERPVQEDSMPDEAMDLEDDAVSTALNRPSDALLVDDHSDAESAATSGRRSSRRSMTRASSIVSSDRHATRLRQPFLLRGQLRPYQQIGFEWLCSLYANGVNGILADEMGLGKTIQTISLLAHLACDKGVWGPHLVVAPTSVMLNWEVEFKKFLPGFKILSYYGNQKERKEKRIGWNTENSFNVCITSYQLVLADQHIFRRKPWVYLVLDEAHHIKNFRSQRWQTLLGFNSQRRLLLTGTPLQNNLMDLWSLMYFLMPNGATELPGGGAFANMKDFQDWFSNPLDKAIEGGTSMNDETRAMVQKLHAVLRPYLLRRLKSEVEKELPSKYEHVITCRLSKRQRFLYNDFMSRAKTRESLASGNYLSIINCLMQLRKVCNHPDLFEVRPIVTSFAMSRSVVADYEIKDLLVRRRLLQENVWEKVDLDVTNLRITDGEEHLTAIESRDLRRLNAAKKLPHFREAVPEPRELDTWTLEGFERSREQRKLVDRMEKWKHMAYLNQYRCTKRPIYGSGLIKMLTEAGEAARLEPLEQHESDRRGFLTRCDSVLRIVQSRSTRRENMQALIDRFAFVTPRAVAVDMPRWALPGLEAHQRPDMVKREFDTVHPVAVKLHIAFPDASLLQYDCGKLQQLDILMRRLKEGGHRILIFTQMTRVLDILESFLNYHGYRYLRLDGATKVESRQALTEQFNRDARISAFILSTRSGGLGINLTGADTVLFYDLDWNAAIEAQCMDRAHRIGQTRDVHIYRFVTEHTIEENMLRKANQKRLLDNVVIQQGEFNTETLAKRLDWTDMLDESGKIGDVEVVVADQGVGARDVESAFLQAEDDEDRQAALRARHEMFIDDADFEEHQPSTSRPNTASATPLAHTASDGARPDNGAHAADALDAHEIENEHQEQEQEQEQAASIDDYMLAFVESDWPFFA
The following text describes a protein:
Function:
IFN-induced antiviral protein which acts as an inhibitor of cellular as well as viral processes, cell migration, proliferation, signaling, and viral replication. Enhances MAVS-mediated host antiviral responses by serving as an adapter bridging TBK1 to MAVS which leads to the activation of TBK1 and phosphorylation of IRF3 and phosphorylated IRF3 translocates into nucleus to promote antiviral gene transcription. Exhibits an antiproliferative activity via the up-regulation of cell cycle negative regulators CDKN1A/p21 and CDKN1B/p27. Normally, CDKN1B/p27 turnover is regulated by COPS5, which binds CDKN1B/p27 in the nucleus and exports it to the cytoplasm for ubiquitin-dependent degradation. IFIT3 sequesters COPS5 in the cytoplasm, thereby increasing nuclear CDKN1B/p27 protein levels. Up-regulates CDKN1A/p21 by down-regulating MYC, a repressor of CDKN1A/p21. Can negatively regulate the apoptotic effects of IFIT2 (By similarity).
Subcellular Localization:
Cytoplasm. Mitochondrion.
Sequence:
MSEVNRESLEAILPQLKCHFTWNLFREGSMSSHMEDRVCNQVEHLNSEEKATMYDLLAYIKHLDGESKAALECLGQAEDLRKSEHNDQSEIRRLVTWGNYAWIYYHMGRLSEAQAYVDKVRQVCQKFANPYSMECPELECEEGWTRLKCGRNERAKMCFEKALEEKPKDPECSSGMAIAMFRLEEKPEKQFSVDALKQAMELNPQNQYLKVLLALKLLRMGEEAEGERLIKDALGKAPNQTDVLQKAAQFYKKKGNLDRAIELLGKALRSTVNNSPLYSLVMCRYREILEQLQNKGDADSSERRQRMAELRRLTMEFMQKTLQRRRSPLNSYSDLIDFPEVERCYQMVISKESPDVEEEDLYERYCNLQEYHRKSEDLAALECLLQFPRNERSIEKEEVKEQT
The following text describes a protein:
Function:
Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSVSTALKLCIFFTGFAGIVAEYSLATLATYLLGNAVLQWSVVISIFLLSMGLGSHASRYIPDDKTPLAFVLAELFLSLLVPFSVPIAYHFANNFLHLQTVIYGLSFVIGSLIGLEIPLAVRINNMYEELKVNISSVLEKDYLGSVPAGLLYAYLFLPKLGLPLTAILAGFFNLISAFLLVKVLKPKKFLKFLAIFTFFLLATYAVGHKRITLYEEQKFYGEEIIHFEQTPYQKIVLTRFGKHYSLYLDGHLQFSTLDEKRYHETLVHVPASFLKRYEKALILGGGDGLALRELRKYPFGEIHLVDLDPKMIEFSKKNLVMRKINENSFYDTRLKVFSEDAFNFVKKTKEKYDFVIVDLIDPRTPSSARVYSLEFYMSLKNKLKEDGIFITQAGDTFYKREVFCSILKTIKKAGFYAYPLVVYIPTFGEWGMVIGSKEPLNFENFELKEKTEFLNRERALAFYTLGKSLECPNVEVNTLLKPVLIYYYYKIQN
The following text describes a protein:
Function:
Positive regulator of brassinosteroid signaling.
Subcellular Localization:
Nucleus.
Sequence:
MAEFTAGFQSFRAQFPVSDIDPNMEIMTNQYAGINPSVLTTPELDFQCFMPFCNHNFFSHQVPEFTGNLAENLLGSVLQEFSQNLVPAQPVMNAAAGNEFHESKKRKSMEKPESSSETSRPQVSETGSKRKNSSGKGKKVKNTLKEEDQKPKEVVHVRARRGQATDSHSLAERVRRGKINDRLRCLQDIVPGCYKSMGMAVMLDEIINYVQSLQNQVEFLSMKLTAASSFYDFSSDSDALETMQRAKAY
The following text describes a protein:
Function:
The soluble GPI-cleaved form, usually released by activated lymphocytes, might play an immune regulatory role by limiting lymphocyte effector functions.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor. Secreted.
Sequence:
MLLEPGRGCCALAILLAIVDIQSGGCINITSSASQEGTRLNLICTVWHKKEEAEGFVVFLCKDRSGDCSPETSLKQLRLKRDPGIDGVGEISSQLMFTISQVTPLHSGTYQCCARSQKSGIRLQGHFFSILFTETGNYTVTGLKQRQHLEFSHNEGTLSSGFLQEKVWVMLVTSLVALQVL
The following text describes a protein:
Function:
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSVGSGGDKTLEAICYRRGSLQLLDQRKLPLETLHLDIHDTNDAWDAIKEMVVRGAPAIAIAAALSLAVEVSNLASFDGTSHDASVFLSKKLDFLVSSRPTAVNLSDSAVKLKEVISKAAAIAKEANSVFQAYIEAAEVMLEDDVTSNKAIGSYGASFIKNYLTDSKNITILTHCNTGRYTPVLVFYFICMVDWFLSYLAWHGFLPYPIILPEIAKYNSVTGLTRTIVIRIRYPDGVILIFLAFLNSLATAGYGTALGVIRALYADGALERAYCTETRPFNQGSRLTAFELVHENIPATLIADSAAAALMNAGRVKAVIVGADRIAANGDTANKIGTYNLAVSAMHHGIPFYVAAPLTSVDLSLSSGQEIVIEERSPKELLHTRGGLGEQVAASGILVWNPAFDVTQAKLISGIITEKGVITKNGTDTFDIAGFVRKTAGNL
The following text describes a protein:
Function:
Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MVDHCTFGWIFSAFLAFVIAFSFFLSPRKNRRGRGTNSTPRRDCLSSSATTNGECRSVDGDADVIIVGAGVAGSALAHTLGKDGRRVHVIERDLTEPDRIVGELLQPGGYLKLIELGLQDCVEEIDAQKVYGYALFKDGKSTRLSYPLENFQSDVSGRSFHNGRFIQRMREKAAFLPNVRLEQGTVTSLLEEKGTITGVQYKSKNGEQKTAYAPLTIVCDGCFSNLRRSLCNPMVDVPSCFVGLVLENCQLPYANLGHVVLGDPSPILFYPISSTEIRCLVDVPGQKVPSISNGEMEKYLKTVVAPQVPPQIHDAFIAAIEKGNIRTMPNRSMPAAPQPTPGALLMGDAFNMRHPLTGGGMTVALSDIVVLRNLLKPLKDLNDAPTLCKYLESFYTLRKPVASTINTLAGALYKVFCASSDQARKEMRQACFDYLSLGGIFSNGPVSLLSGLNPRPLSLVLHFFAVAIYGVGRLLLPFPSPKGIWIGARLVYSASGIIFPIIKAEGVRQMFFPATVPAYYRTPPVFNS
The following text describes a protein:
Function:
Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity.
Subcellular Localization:
Cytoplasm. Note=Localizes to mid-cell in an FtsZ-dependent manner. Localization does not require FtsA, ZipA, ZapA or ZapC.
Sequence:
MQTQVLFEHPLNEKMRTWLRIEFLIQQLTVNLPIVDHAGALHFFRNVSELLDVFERGEVRTELLKELDRQQRKLQTWIGVPGVDQSRIEALIQQLKAAGSVLISAPRIGQFLREDRLIALVRQRLSIPGGCCSFDLPTLHIWLHLPQAQRDSQVETWIASLNPLTQALTMVLDLIRQSAPFRKQTSLNGFYQDNGGDADLLRLNLSLDSQLYPQISGHKSRFAIRFMPLDTENGQVPERLDFELACC
The following text describes a protein:
Function:
Small GTPase that cycles between an active GTP-bound and an inactive GDP-bound state and mainly functions in vesicle-mediated endoplasmic reticulum (ER) to Golgi transport. The active GTP-bound form inserts into the endoplasmic reticulum membrane where it recruits the remainder of the coat protein complex II/COPII. The coat protein complex II assembling and polymerizing on endoplasmic reticulum membrane is responsible for both the sorting of cargos and the deformation and budding of membranes into vesicles destined to the Golgi.
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus, Golgi stack membrane; Peripheral membrane protein. Cytoplasm, cytosol. Note=Active at endoplasmic reticulum exit sites (ERES) where it inserts into the membrane and recruits the remainder of the coat protein complex II/COPII.
Sequence:
MFLVDWFYNMFLWLGFFKKEAKIVIIGLGNAGKTTLLHLLVTGSLKSHIPTLRPNAESFTYGNVNFKAYDLGGQQNLRFLWKQYVPDSKTIIVFMVDSSDYNSIIESKSEIHDILGDEHLSQSPLLILGSKCDAKGHHNRENLIDLLDIRRFELGLNNSNNVPFDLIMTSSITRYGITDMLNWLDKCTDIIKNN
The following text describes a protein:
Function:
Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MELGYGGQATFQPQQTQGYVLCCLCGTNILPNPSNMCVNCIRSQVDITEGIQKQCTILWCKECGRYLQPPKHWVTAELESKELLTFCIKKIKGLSKVKLVDAGFIWTEPHSKRIKVKLTIQVFNGAILQQTFVVDYVVENNMCPDCNRQNANPNSWIACVQLRQHVYHKRTFLFLEQLILKHDAAAQCVKVRDIHEGIDFFYANRSHAQKFIDFLQSVVPIRFRADKQLVSHDTHNNTYNYKFTFSVEIVPLCKGLARVPASTACSAEIVPLCKDDLVFLPPKMAASAGNLGPFVLVSRITNQISLVDPANMRTHTMDAPVYYRHECLALASQRSLISFIVLDIEPIRAGNSSKSGSATPAGGAGGGGGGYGQGGGPGGGGGSGRYQLAEAQIARVSDFGKNDTVFYVRTHLGNILHPGDTVLGYDLTTAQLTGIDYDNHMSAGGRVPEIILVRKSYDEKRRRRAARGGAGGAARPWKLKTLEMEVDDAATGQRGRNEAALEADRERFMQELEEDADMRARINIYKDAQGLAQVQLAAARTQAAAAAPAVPAGLMEGEDEEDDDDEDLPQIPLEELLDDLEGLALDPDADGEEEDPSAGQASGAGAGDMDMD
The following text describes a protein:
Function:
Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Subcellular Localization:
Cytoplasm.
Sequence:
MSQIRLCVQHCEFFPGKILELSNEDRKYLFNVLRCHPGDTLSIFNGKGKSFHAKIIDLKTIEILQEEELHTEDVFSITLCQALLKGEKMDMIIQKATELGVKKIIPFVSDRCIVRHTRKIGRWEKIAKEASEQSHRSIVPEISNVINFSELIKNIDNGILFWEKATSPLIQTISEVNHDKNIFLLIGPEGGFSQEEVSQAEKMNIKTASLGKRILKAETASIVSVALVSFLLQWKL
The following text describes a protein:
Function:
NodD regulates the expression of the nodABCFE genes which encode other nodulation proteins. NodD is also a negative regulator of its own expression. Binds flavonoids as inducers.
Sequence:
MARINSRQVEAFRATMLTGSVTEAAALMTVTQPAVSRLLRDLQALLKMELFERRGTGLVPTAAAMALYTEVERSFVGLERITAAAEEIRGRRTGSLRIAALPALSNGYLPRLAGHFLKERPNLNLAFFGVISPIVVDWVLNNQCDIGFAEVPIAHSGLPSLRLPALARVAVLPTGHRLAEKEVLEPRDFEGETFISLSAGSSSRHLVDQVFHRHDVRRVLRVETTLSEIMCGMVSSGLGVAICDPFTAQEFSTRGVVVRRFLPRIDFEFSAVFPAQRSPSPVALDLVETMRKSLAEFED
The following text describes a protein:
Function:
Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase OPG063 that creates mRNA's poly(A) tail. In the presence of OPG102, OPG063 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.
Subcellular Localization:
Nucleus. Virion.
Sequence:
MNPGAGYESRTDLPFETILRPDAPAVPYRRRKNERKSVIHWGQRKLLLCEIEFLLLHGDKAPLVVYAGAAPGPHVKILMGMFPKHSFVCVDPAPFSKQLVENDRLILRQEMFTDDVAREFADRDVLFLSDIRSADPDIMDEKEVDSQVVADQEAQMRWHLLMKAKASLLKFRLSWKEGITNYLKGDIYLPIWGPMTTTEARLLVEGTEMQGYDNQKYEQQMFFFNTVARVARYEHDVKAVGIDFCYDCRAEVEVLRRYIKQERTADLSAEELAERVGRLSERISRELGHRTLADGNSDPGVRKQGIIQRQYIAGKPAYAKRKQHEAQYSNTAQRLMAGMGYKQGKGLGREAQGAAEPILESSQIGRRGLGFSLAGHRFDAEKEGAVNHDQNLDESGEKPAKTAKPMAFELAGQTLSTVGQVASDLSTGEPPAQRTKIQNEHETEASEQGASGDDAKPLSPSHSQAETAKKEDGEI
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Miscellaneous:
MISCELLANEOUS: Present with 1350 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1.
Sequence:
MSSLLKLHCIRPLPQRSVWLSGYKQKARCIHSSAANGDFMSWFKRKKQEEHQEPVKDTKQLIKDIEEGTNEASSQSSSNNKNRLELIPENFIGEGSRRCKRQKELKLAVSSAPFNQWLSRDKITSDNQLDDMILQATEKTLGKVDQDVQFSDLVAKFQFTKFLQSKSGYLIPDYELTTLSTPLQFKRYIKEKILPSANDPKLAYKEAEPNAIHPFSDNYASPNIYVVNDVTSKEQKSKYDTIMKEIQKLEDDATRKALETARSA