lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Probable lipid phosphatase that specifically dephosphorylates the D-3 position of phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate, generating phosphatidylinositol and phosphatidylinositol 5-phosphate. In association with mtm-9, plays a role in endosome trafficking probably by regulating phosphatidylinositol-3-phosphate levels. Regulates fluid phase endocytosis in coelomocytes. Controls the endosomal localization of sorting nexin snx-3 and the levels of sorting receptor mig-14. By regulating the retrograde transport of mig-14, may be involved in the secretion of Wnt ligands such as egl-20. Regulates posterior migration of QL neuroblast descendants and the anterior migration of QR neuroblast descendants and HSN neurons during larval development. Involved in the formation of correct synapse number in DA9 motor neurons probably in part by regulating the secretion of Wnt ligand egl-20.
Subcellular Localization:
Cytoplasm. Membrane; Peripheral membrane protein. Apical cell membrane; Peripheral membrane protein.
Domain:
The FYVE domain appears to be dispensable for membrane targeting and activity but may be important to increase avidity to membrane.
Sequence:
MRFEDIGISKVDKVCLVDRLGCQENLVGTVHVTTTHIIFRAENGSKELWLATGLISSVEKGTLTAAGCMLVIRCKHFQVITLLISRDKSCQDLYETLQRAAKPVSVNVTELLAFENREPVEDVRGWRRLDWNSEMTRQGITKSQWTESNINEGYTICDTYPNKLWFPTAASTSVLLGSCKFRSRGRLPVLTYFHQQTEAALCRCAQPLTGFSARCVEDEKLMELVGKANTNSDNLFLVDTRPRVNAMVNKVQGKGFEDERNYSNMRFHFFDIENIHVMRASQARLLDAVTKCRDVTEYWKTLEASGWLKHVRSVVECSLFLAESISRGTSCVVHCSDGWDRTSQVVALCQLLLDPYYRTIHGFQVLIEKDWLGFGHKFDDRCGHVGALNDEAGKEVSPIFTQWLDCIWQIMQQKPRAFQFNERYLIEMHEHVYSCQFGTFIGNCDKDRRDLNLSKRTKSLWTWMDARHDDYMNPFYSPTAHVALLDLDTRAARFTVWTAMYNRFDNGLQPRERLEDLTMAAMEHVGVLESHVAQLRTRLAELKTQQNQQITSTNTPTNMVDSGMSSATDDLKNLSLSHPLDPLSSTLPILERATSQESGVMDSSLYYPDEALTKYSLKWQPLRGADRCSNPACRGEFSSTIERRIHCHLCGMIFCRRCLKVSADERERVCDKCKTD
The following text describes a protein:
Function:
RNA chaperone that plays a key role in telomere maintenance and RNA localization to Cajal bodies. Specifically recognizes and binds the Cajal body box (CAB box) present in both small Cajal body RNAs (scaRNAs) and telomerase RNA template component (TERC). Essential component of the telomerase holoenzyme complex, a ribonucleoprotein complex essential for the replication of chromosome termini that elongates telomeres in most eukaryotes. In the telomerase holoenzyme complex, required to stimulate the catalytic activity of the complex. Acts by specifically binding the CAB box of the TERC RNA and controlling the folding of the CR4/CR5 region of the TERC RNA, a critical step for telomerase activity. In addition, also controls telomerase holoenzyme complex localization to Cajal body. During S phase, required for delivery of TERC to telomeres during S phase and for telomerase activity. In addition to its role in telomere maintenance, also required for Cajal body formation, probably by mediating localization of scaRNAs to Cajal bodies. Also plays a role in DNA repair: phosphorylated by ATM in response to DNA damage and relocalizes to sites of DNA double-strand breaks to promote the repair of DNA double-strand breaks. Acts by recruiting the ubiquitin ligase RNF8 to DNA breaks and promote both homologous recombination (HR) and non-homologous end joining (NHEJ).
Subcellular Localization:
Nucleus, Cajal body. Chromosome, telomere. Chromosome. Note=Released from telomerase RNA template component (TERC) in mitotic cells coincident with delocalization from Cajal bodies. In response to DNA damage, localizes to sites of DNA double-strand breaks following phosphorylation by ATM.
Sequence:
MKTSEELRLAPDSLPSDLVPAPVLQASPADKNTDSEPVPPPCGGDDQLQVATDAVASSVVSQELQQGDSAPLEVEFNISSELSPRIEEQEVPENASLPVEETNRPELESGEAMEGVSEEPAAVDEGDIFWSYSFSQVPQYLSGSWSEFSTRSENFLKGCKWAPDGSCILTNSADNVLRIYNLPPELYSESEQVDYAEMVPVLRMVEGDTIYDYCWYSLMSSTQPDTSYVASSSRENPIHIWDAFTGELRASFRAYNHLDELTAAHSLCFSPDGSQLFCGFNRTVRVFSTSRPGRDCEVRTTFAKKQGQSGIISCLAFSPAQPLYACGSYGRTLGLYAWDDGSPLALLGGHQGGITHLCFHPDGNLFFSGARKDAELLCWDLRQPGHLLWSLSREVTTNQRIYFDLDPSGQFLVSGNTSGVVSVWDISGAFSDCKQLEPVMTFLPQDDCTNGVSLHPTLPLLATASGQRMFPEPTNSGDEGEPELDLPLLSLRHAHPECQLQLWWCGGGPDPSNPDEDQDEKGQGRTEAVGMS
The following text describes a protein:
Function:
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity.
Sequence:
MSVWLVSVPNEGNSSSETTFLSLKAETASSRHDYADCVRVELPSDLLVGTLDSLMALSDDLNRVDLVIESVVRKIERQFHDLNKGDQALTVDGVPVERYLGFFSWDEAKHPHRRPLPEIVSIIQSSVGKIEEELKQLSTRYSEKKQQLIGLQRKKGGNLMVANLNDVLTPDVVSTSDFVNTEYLQTLVVIVPKNLEEQWLHEYAQIGDQIAEYGPKGSRGNVRGSPVVPGSSRKLMEEGDSAVYTVTLLKGQYQPGFVDKEGNFEPGTTVDYVEDFKTRAKEKRFVVREFSFDPTSHASNEEAIAELEVEVDRLWSALIRWCKAHFGETFIAWMHIKMVRVFVESVLRYGLPVNFVVAMYKPHSGKDKKLRAVLSKKYAHLQPAQFSGLEEGSAGSSQVEYYPYVTNAFQPLSTDQH
The following text describes a protein:
Function:
Fumigatonoid B endoperoxide isomerase; part of the gene cluster that mediates the biosynthesis of novofumigatonin, a heavily oxygenated meroterpenoid containing a unique orthoester moiety. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase nvfA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations. DMOA is then converted to farnesyl-DMOA by the farnesyltransferase nvfB. Epoxydation by FAD-dependent monooxygenase nvfK, followed by a protonation-initiated cyclization catalyzed by the terpene cyclase nvfL leads to the production of asnavolin H. The short chain dehydrogenase nvfC then as a 3-OH dehydrogenase of asnovolin H to yield chemesin D. There are two branches to synthesize asnovolin A from chemesin D. In one branch, chemesin D undergoes Baeyer-Villiger oxidation by nvfH, methylation by nvfJ, and enoyl reduction by the nvfM D enoylreductase that reduces the double bond between C-5'and C-6', to form respectively asnovolin I, asnovolin K, and asnovolin A. In the other branch, the methylation precedes the Baeyer-Villiger oxidation and the enoyl reduction to yield asnovolin A via the asnovolin J intermediate. Asnovolin A is further converted to fumigatonoid A by the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfI that catalyzes an endoperoxidation reaction. The alpha/beta hydrolase nvfD then acts as an epimerase that converts fumigatonoid A to its C-5' epimer, which then undergoes spontaneous or nvfD-catalyzed lactonization. The following step utilizes the ketoreductase nvfG to produce fumigatonoid B. The dioxygenase nvfE further converts fumigatonoid B into fumigatonoid C. Finally the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfF catalyzes two rounds of oxidation to transform fumigatonoid C into the end product, novofumigatonin A.
Sequence:
MGRDQVSHKRSQNSNVSEIPDLDSSLHRSEDTLVAEIIEAMTLAGVCVVRNLFTKSLVDQVLKDFEPHVSSTKLFDGYPGNGCHLTGLLSKSEIYAHMVVGNSVFEKVRNHFLSTTFRSWIGGKMMTFTSPPQLDSTICSYINPQSPGEHLHRDDAIHYGWNEAASEYTVGRDISMSMFLALTESTRENGTTRFFPGSHLWDYSQDFPSADDTRIRYAELHPGDCYFMLSSVTHSSTDNRSTNRPRVLAATIVTRSHLRQEENQYLTYDPITVGRFPTWLQRLVGYAPSAPFLGWVDKRDPRCVIDPKAADDHCGGEYYETNEETLN
The following text describes a protein:
Function:
Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MRRIRANAIAILTVAWILGTFYYLWQDNKPHAAASSRSPGSSGSSSSSSGGGHQRSSGKVELHKEERTIPLIASRPPQAEKPGLRGFDEKAYVSSKLLKAGEDPYRQHAFNQLESDKLSSDRPIRDTRHYRCASIHYGADLPSTSIIITFHNEARSTLLRTVTSVLNRTPANLIQEIILVDDFSSDPEDCQLLTKIPKVKCLRNNRREGLIRSRVRGADMATADILTFLDSHCEVNSEWLQPMLQRVKEDYTRVVSPIIDVISLDNFAYLAASADLRGGFDWSLHFKWEQIPIEQKLSRTDPTQSIRTPVIAGGIFVIDKSWFNHLGKYDTQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFRKRHPYDFPEGNALTYIKNTKRTAEVWMDEYKQYYYEARPSAIGKSFGSIADRVDQRRKLNCKSFQWYLENVYPELKVPEKELIPGIIKQGANCLESQGQDSAGNSLAAVGSCKGTANDPAATQEWIFSDPLIRQQDKCLSITSFSTGSQITIEACNQKDGRQKWKMKGSFIQHFVSGLCLESQSSRLVTNICQSDIPGQQWELLQAT
The following text describes a protein:
Function:
Adapter protein with E3 ligase activity that is involved in many diverse biological processes including cell proliferation, migration, differentiation, DNA repair, platelet activation or apoptosis. Promotes EGFR-mediated signaling by facilitating the dimerization of EGFR and downstream AKT activation thereby promoting cell proliferation. Ubiquitinates SMURF2 through 'Lys-48'-linked ubiquitin chain leading to SMURF2 degradation through the proteasome and subsequently osteogenic differentiation. Promotes 'Lys-63'-mediated ubiquitination of CHK1 which in turn activates cell cycle arrest and activation of DNA repair. In addition, promotes an atypical 'Lys-29'-linked ubiquitination at the C-terminal end of IRS1 which is crucial for insulin-like growth factor (IGF) signal transduction (By similarity). Regulates activation of NF-kappa-B in response to signaling through Toll-like receptors. Required for normal skeleton development, and for normal development of the respiratory tract. Required for activation of RPS6KB1 in response to TNF signaling. Modulates TRAF6 functions. Inhibits adipogenic differentiation by activating pyruvate kinase PKM activity and subsequently the beta-catenin signaling pathway (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus. Cytoplasm, perinuclear region. Cell junction, tight junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton.
Domain:
The coiled coil domain mediates homo- and hetero-oligomerization; The MATH/TRAF domain binds to receptor cytoplasmic domains.
Sequence:
MPGFDYKFLEKPKRRLLCPLCGKPMREPVQVSTCGHRFCDTCLQEFLSEGVFKCPEDQLPLDYAKIYPDPELEVQVLGLAIRCIHSEEGCRWSGPLRHLQGHLNTCSFNVVPCPNRCPAKLSRRDLPAHLQHDCPKRRLKCEFCGCDFSGEAYESHEGVCPQESVYCENKCGARMMRRLLAQHATSECPKRTQPCAYCTKEFVYDTIQSHQYQCPRLPVPCPNQCGVGTVAREDLPTHLKDSCSTAFVLCPFKESGCKHRCPKLAMGRHVEESVKPHLAMMCALVSRQRQELQELRRELEELSIGSDGVLIWKIGSYGRRLQEAKAKPNLECFSPAFYTHKYGYKLQVSAFLNGNGSGEGTHLSIYIRVLPGAFDNLLEWPFARRVTFSLLDQSDPGLAKPQHVTETFHPDPNWKNFQKPGTWRGSLDESSLGFGYPKFISHQDIRKRNYVRDDAVFIRASVELPRKILS
The following text describes a protein:
Function:
Functions as a protein modifier covalently attached to lysine residues of substrate proteins, as well as a sulfur carrier in molybdenum cofactor (MoCo) biosynthesis. The protein modification process is termed sampylation and involves the formation of an isopeptide bond between the SAMP1 C-terminal glycine carboxylate and the epsilon-amino group of lysine residues on target proteins. May serve as a proteolytic signal in the cell to target proteins for degradation by proteasomes.
Sequence:
MEWKLFADLAEVAGSRTVRVDVDGDATVGDALDALVGAHPALESRVFGDDGELYDHINVLRNGEAAALGEATAAGDELALFPPVSGG
The following text describes a protein:
Function:
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNNVPWLSVLWLVPLAGAVLIILLPPGRRRLAKWAGMVVSVLTLAVSIVVAAEFKPSAEPYQFVEKHSWIPAFGAGYTLGVDGIAVVLVLLTTVLIPLLLVAGWNDATDADDLSPASGRYPQRPAPPRLRSSGGERTRGVHAYVALTLAIESMVLMSVIALDVLLFYVFFEAMLIPMYFLIGGFGQGAGRSRAAVKFLLYNLFGGLIMLAAVIGLYVVTAQYDSGTFDFREIVAGVAAGRYGADPAVFKALFLGFMFAFAIKAPLWPFHRWLPDAAVESTPATAVLMMAVMDKVGTFGMLRYCLQLFPDPSTYFRPLIVTLAIIGVIYGAIVAIGQTDMMRLIAYTSISHFGFIIAGIFVMTTQGQSGSTLYMLNHGLSTAAVFLIAGFLIARRGSRSIADYGGVQKVAPILAGTFMVSAMATVSLPGLAPFISEFLVLLGTFSRYWLAAAFGVTALVLSAVYMLWLYQRVMTGPVAEGNERIGDLVGREMIVVAPLIALLLVLGVYPKPVLDIINPAVENTMTTIGQHDPAPSVAHPVPAVGASRTAEGPHP
The following text describes a protein:
Function:
RNA-binding nucleolar protein required for pre-rRNA processing. Component of the 90S pre-ribosome involved in production of 18S rRNA and assembly of small ribosomal subunit. Component of the pre-40S ribosome required for release from the nucleolus.
Miscellaneous:
MISCELLANEOUS: Present with 2930 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MGKTKTRGRRHQDKQRKDEFEPSSNSAKEHIQQEESTYNDEAEIKETQPQMFFGVLDREELEYFKQAESTLQLDAFEAPEEKFQFVTSIIEEAKGKELKLVTSQITSKLMERVILECDETQLKDIFQSFNGVFFGLSCHKYASHVLETLFVRSAALVERELLTPSFDNNEKEGPYVTMENMFLFMLNELKPHLKTMMNHQYASHVLRLLILILSSKTLPNSTKANSTLRSKKSKIARKMIDIKDNDDFNKVYQTPESFKSELRDIITTLYKGFTNGAESRSDISQSTITKFREYSVDKVASPVIQLIIQVEGIFDRDRSFWRLVFNTADEKDPKEESFLEYLLSDPVGSHFLENVIGSARLKYVERLYRLYMKDRIVKLAKRDTTGAFVVRALLEHLKEKDVKQILDAVVPELSMLLNSNMDFGTAIINASNKQGGYLRDDVIAQLIQKYYPEKSDAKNILESCLLLSASTLGNTRDDWPTAEERRRSVFLEQLIDYDDKFLNITIDSMLALPEERLIQMCYHGVFSHVVEHVLQTTRVDIIKRKMLLNILSKESVNLACNVYGSHIMDKLWEFTAKLTLYKERIARALVLETEKVKNSIYGRQVWKNWKLELYVRKMWDWKKLIKEQEFEIFPNSKPLQPKPEKHSRERNNSKEGSAFKKQKHYR
The following text describes a protein:
Function:
P450 monooxygenase that plays a major role in cholesterol homeostasis in the brain. Primarily catalyzes the hydroxylation (with S stereochemistry) at C-24 of cholesterol side chain, triggering cholesterol diffusion out of neurons and its further degradation. By promoting constant cholesterol elimination in neurons, may activate the mevalonate pathway and coordinate the synthesis of new cholesterol and nonsterol isoprenoids involved in synaptic activity and learning. Further hydroxylates cholesterol derivatives and hormone steroids on both the ring and side chain of these molecules, converting them into active oxysterols involved in lipid signaling and biosynthesis. Acts as an epoxidase converting cholesta-5,24-dien-3beta-ol/desmosterol into (24S),25-epoxycholesterol, an abundant lipid ligand of nuclear NR1H2 and NR1H3 receptors shown to promote neurogenesis in developing brain. May also catalyze the oxidative metabolism of xenobiotics, such as clotrimazole.
Subcellular Localization:
Cell projection, dendrite. Endoplasmic reticulum membrane; Single-pass membrane protein. Microsome membrane; Single-pass membrane protein. Postsynapse. Presynapse.
Sequence:
YLFYVHRLYSHIPSPPRDSFFFGHVPYIRRERTRGREIHEVVIEWTNKYGPIIVFWAFHNPVVFVVSPEMVKKVLVTYDLPKSTRVYEKLQFVYNQRCTGRGILTEPDPSAWHKKRTLLNPAFHRKNLMNLMSPFNVICERMIDKLSLISDGKTQVDLADELSRTTLDVIGKVAFDIDLDAIKDDNTPFPSANSSTLMGIQQQFRSPFWRINPFMYPYQQKVIKDIKFLREFGEKVILKRKAAIEKGMDMPKDVLNHILYMCKEDVNVPMEELVDDFVTFFIAGQETTSNLLAFTVFEIGNNPDIEQRIQNEISKVLGSRQFVEYQDLGKLQYLGQTLKESLRLHPPIPGFSRFTPDAIELGGYAIPANTGIAVDVFATHRYPGVWTEPDKFNPHRFGPGSDDTITSSMFLPFANGPRTCIGKMFAEFEAKVIMARLYQEFKIKLVPGQKLLYDLHLTMRPKGGVLCTLDKR
The following text describes a protein:
Function:
Heterodimeric geranyl(geranyl)-diphosphate (GPP) synthase small subunit. The small subunit alone is inactive in vitro while the large subunit GGPPS1 catalyzes mainly the production of geranygeranyl-diphosphate in vitro. Upon association of the two subunits, the product profile changes and the production of gerany-diphosphate is strongly increased.
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Peripheral membrane protein.
Sequence:
MLFSGSAIPLSSFCSLPEKPHTLPMKLSPAAIRSSSSSAPGSLNFDLRTYWTTLITEINQKLDEAIPVKHPAGIYEAMRYSVLAQGAKRAPPVMCVAACELFGGDRLAAFPTACALEMVHAASLIHDDLPCMDDDPVRRGKPSNHTVYGSGMAILAGDALFPLAFQHIVSHTPPDLVPRATILRLITEIARTVGSTGMAAGQYVDLEGGPFPLSFVQEKKFGAMGECSAVCGGLLGGATEDELQSLRRYGRAVGMLYQVVDDITEDKKKSYDGGAEKGMMEMAEELKEKAKKELQVFDNKYGGGDTLVPLYTFVDYAAHRHFLLPL
The following text describes a protein:
Function:
Acts as a regulatory factor of isoprenoid biosynthesis. Could bind RNA.
Sequence:
MSLLSADALGLLLKNAISASSMRLGRVVHARIVKTLDSPPPPFLANYLINMYSKLDHPESARLVLRLTPARNVVSWTSLISGLAQNGHFSTALVEFFEMRREGVVPNDFTFPCAFKAVASLRLPVTGKQIHALAVKCGRILDVFVGCSAFDMYCKTRLRDDARKLFDEIPERNLETWNAFISNSVTDGRPREAIEAFIEFRRIDGHPNSITFCAFLNACSDWLHLNLGMQLHGLVLRSGFDTDVSVCNGLIDFYGKCKQIRSSEIIFTEMGTKNAVSWCSLVAAYVQNHEDEKASVLYLRSRKDIVETSDFMISSVLSACAGMAGLELGRSIHAHAVKACVERTIFVGSALVDMYGKCGCIEDSEQAFDEMPEKNLVTRNSLIGGYAHQGQVDMALALFEEMAPRGCGPTPNYMTFVSLLSACSRAGAVENGMKIFDSMRSTYGIEPGAEHYSCIVDMLGRAGMVERAYEFIKKMPIQPTISVWGALQNACRMHGKPQLGLLAAENLFKLDPKDSGNHVLLSNTFAAAGRWAEANTVREELKGVGIKKGAGYSWITVKNQVHAFQAKDRSHILNKEIQTTLAKLRNEMEAAGYKPDLKLSLYDLEEEEKAAEVSHHSEKLALAFGLLSLPLSVPIRITKNLRICGDCHSFFKFVSGSVKREIIVRDNNRFHRFKDGICSCKDYW
The following text describes a protein:
Function:
Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule. Involved in mediating assembly of both ODAs and their axonemal docking complex onto ciliary microtubules (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium axoneme.
Sequence:
MEGERRAYSKEVHQRINKQLEEIRRLEEVRGDLQVQISAAQNQVKRLRDSQRLENMDRLLKGRAQVQAEIEELQEQTRALDKQIQEWETRIFTHSKNVRSPGFILDQKVKIRRRIRILENQLDRVTCHFDNQLVRNAALREELDLLRIDRNRYLNVDRKLKKEIHHLHHLVSTLILSSTSAYAVREEAKAKMGLLRERAEKEEAQSEMEAQVLQRQILHLEQLHHFLKLKNNDRQPDPDVLEKREKQAGEVAEGVWKTSQERLVLCYEDALNKLSQLMGESDPDLLVQKYLEIEERNFAEFNFINEQNLELEHVQEEIKEMQEALVSARASKDDQHLLQEQQQKVLQQRMDKVHSEAERLEARFQDVRGQLEKLKADIQLLFTKAHCDSSMIDDLLGVKTSMGDRDMGLFLSLIEKRLVELLTVQAFLHAQSFTSLADAALLVLGQSLEDLPKKMAPLQPPDTLEDPPGFEASDDYPMSREELLSQVEKLVELQEQAEAQRQKDLAAAAAKLDGTLSVDLASTQRAGSSTVLVPTRHPHAIPGSILSHKTSRDRGSLGHVTFGGLSSSTGHLPSHITHGDPNTGHVTFGSTSASSGGHVTFRPVSASSYLGSTGYVGSSRGGENTEGGVESGGTASDSSGGLGSSRDHVSSTGPASSTGPGSSTSKDSRG
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III (Pol III) which synthesizes small non-coding RNAs including 5S rRNA, snRNAs, tRNAs and miRNAs from at least 500 distinct genomic loci. With CRCP/RPC9 forms a mobile stalk that protrudes from Pol III core and functions primarily in transcription initiation. Pol III plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF-kappa-B through the RIG-I pathway; DNA-dependent RNA polymerase which catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular Localization:
Nucleus.
Sequence:
MFVLVEMVDTVRIPPWQFERKLNDSIAEELNKKLANKVVYNVGLCICLFDITKLEDAYVFPGDGASHTKVHFRYVVFHPFLDEILIGKIKGCSPEGVHVSLGFFDDILIPPESLQQPAKFDDTEQVWVWEYETEEGAHDLYMDTGEEIRFRVVDESFVDTSPTGPSSAEATSSSEELPKKEAPYTLVGSISEPGLGLLSWWTSS
The following text describes a protein:
Function:
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across the thylakoid membrane. Involved in delta pH-dependent protein transport required for chloroplast development, especially thylakoid membrane formation. TATC and TATB mediate precursor recognition, whereas TATA facilitates translocation.
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Single-pass membrane protein.
Sequence:
MQDRPRRGPTVCGIFGLGVPELVVIAGVAAVLFGPKQLPELGKSLGKTVKSFQQAAKEFEGEIKKNAEELKEEAQNSVDEFKNEVKKEK
The following text describes a protein:
Function:
Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity). May regulate negatively the transition to flowering time and confers flowering time delay.
Subcellular Localization:
Nucleus.
Sequence:
MWNLNDSPDHHEESDSRGNPVGHVSNGMSQSATWLPFVLPVTRNFFPAQSMEPGVRWSGFNSVGKSDPSGSGRPEEPEISPPIKKSRRGPRSRSSQYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAHAAARAYDRAAIKFRGVDADINFDIEDYLDDLKQMGNLTKEEFMHVLRRQSTGFPRGSSKYRGVTLHKCGRWESRLGQFLNKKYVYLGLFDTEIEAARAYDKAAIKCNGKDAVTNFDPKVYEEEEDLSSETTRNGHNLGLSLGESSSEEFRLKSDIASIRSRIRDEERLLGSDLSLAMMTTTVRSEKQQSDGGGNRVVGMAASSGFSPQPSPYRIPRTFHFSRP
The following text describes a protein:
Function:
Accessory subunit of DNA polymerase gamma solely responsible for replication of mitochondrial DNA (mtDNA). Acts as an allosteric regulator of the holoenzyme activities. Enhances the polymerase activity and the processivity of POLG by increasing its interactions with the DNA template. Suppresses POLG exonucleolytic proofreading especially toward homopolymeric templates bearing mismatched termini. Binds to single-stranded DNA.
Subcellular Localization:
Mitochondrion matrix, mitochondrion nucleoid.
Sequence:
MPGYSSDRDRGFGSPRFGGSRGGSLGGKKFGNPGEKLTKKKWNLDELPKFEKNFYQEHPDVARRPMQEIEQYRGSKEITVKGHNCPKPVMNFYEANFPANVMEVIQRQNFTDPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKEYVHINIGALELSANHNILQIVDVCHDVEKDDKLIRLMEEIMSEKENKTIVFVETKRRCDDLTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLREANQAINPKLLQLVEDRGSGVLEHYVECLELVNKRLPFGAAQIGTCFHAVATNEKENNVRTGERMMSILVWYSSGRTAGQWLDYWLRQRLQWWRKFAICPSNFSSSHHHDEEGRRGSNLYYSFPWGKELIETLRSLGDNELLKMYPGKGSQLHGRDGRKSMVPHILSVSGNLDSGVLAYLFDGFQLGENAVTRKKTQQRKVLKLHPSLTPIKVALDVARGPTTELRQVCQGLFSELLENGISVWPGYLETMPLTLEQLYTKYDEMSILFTILVSEATLENGVVQLRNRNTTMKEMMHISRLKDFLTKYISAAKNV
The following text describes a protein:
Function:
Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid.
Subcellular Localization:
Mitochondrion outer membrane.
Sequence:
MSQSRARKVLIVGAGPVGALTALSLHRRGWEVEVWETRDDPRGQDAAPSNLRSINLAISSRGLEALRSVDPSIAENFLEEAIPMKGRMIHHTDGKQESQLYDPIGGQSINSISRPILNQRLVQSLPEAVKLRFNTKLKHIDFKNRVAYASHKQETSLLPGEESEKDKKQNTEDEDGTAFDLVIGCDGSWSKVRTAMMRAERIDFSQSFIPHAYIELHMPSDPAFPGGYAMDKNHLHIWPRHAFMLIGLPNKDGSFTLTLFIPFSSLELLDTRESAAAFFREHFPSAVDIVGEKVLLDDFEKNPRGNLVTINCTPSAWSSHAILLGDASHSMVPFYGQGLNCGLEDVRVLSSILERHHISPTTTLALGETDPELELALKAYSDERQGDLKAICELALQNYTEMRSHVLSPLHHLRRQVDKVFTTLFRSAPQATLSLMEPFPTKKVRGWTSLYEMVTFRPDVGYSEALRKERWQKDVVGYAGWIGGVVGVGAAGVFAATMAKKWLERR
The following text describes a protein:
Function:
Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro (By similarity). Aminopeptidase that binds to the auxin transport inhibitor N-1-naphthylphthalamic acid (NPA) (By similarity). May play a negative role in the regulation of PIN auxin transport proteins (By similarity). Involved in the coordination of the symbiotic nodule developmental program; prevents the formation of root nodules by regulating the expression of the nuclear transcription factor Y subunit (NF-YA1), a key nodulin (Ref.1).
Subcellular Localization:
Nucleus. Cytoplasm. Cell membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Sequence:
MENTLSALRSLMASHSPPLDALVVPSEDYHQSEYVSARDKRREFVSGFSGSAGLALITKDVALLWTDGRYFLQAEQQLSDEWKLMRIGEDPAVDTWMADNLLKEASIGVDPWCISIDTAQRWERSFAEKQQKLVQTTKNLVDEVWADRPPAEINAVVVQPLKFAGRSVADKLKDLRKKLVQEQARGIIFTSLDEVAWLYNIRGNDVAYCPVVHAFAIVTSNSAFLYVDKRKVSAEVKSHLEENGIEIREYTAVSFDVALLATDELDTTSTAKDTLAEITKQAEKFVSETNKSVNGKHQAKENSNNLIWADPGSCCYAVYSKLNPDTVLLQQSPLALAKALKNPVELEGLKQAHIRDGAAVVQYLVWLDKQMQDIFGASGYFSEGNTVKKEELSQSLKLTEVTVSDKLEGFRASKKHFRGLSFPTISSVGPNGAVIHYSPKAETCAELDPDKIYLFDSGAQYLDGTTDITRTVHFGKPSAHEKACYTAVLKGHIALGNAVFPNGTNGHALDILARIPLWKNGLDYRHGTGHGIGSYLNVHEGPHLISFKPRNVPLQSSMTVTDEPGYYEDGAFGIRLENVLIINEADTKFNFGDKGYLSFEHITWAPYQTKLIDLNLLTPDEINWLNSYHSRCRDILQPHLDDAAENEWLKKATEPVGV