lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in endocytosis.
Sequence:
MSSKRHKIEVEIIRIRNDGNLLKHKDIIKQLAHKCGDTDPVVKYLDNFVKIHEFFIEHESDTVSALRNSTVLDGFKNKLTEARKQNFDPKDSLVNVFIEASLLLAKLCYSQASFQECVDIYSNVNLAGLENSVTDHYMVIILCEAFAINGLCLERSRLKDPKFKSDVEALGSYETAQKLFMRYIHDHHRLDSTSTSPTSPASHNMDIHIYPAIESCLHRTASLYIKSKTPEKAVSLYKTILTTLPAHIPSQTHQKFLHNLASVLIRGFSKISYKQVSTDTHERSIFFQGVKNVFIPNYIQQEALLLLLITEGLLNLDPVLDMSPEHAESREQTLMKAESLYDDLSVAVASHGQYHIFTESIERSLKYNFDRYHLWNQFALSLCAEGKIDRGVQCLAECCRIDPTISSPDAILASRLCYTKQPPQIDAGLKYAELALEHSDEDHDGLRSRSHLYIGLGCSLKALGSLSKKDRLEYRAKAIKSYTSSHTSDPYDYKPLFHLSFELALSRKVAVAIKKVKQALELQPEACECLHLLALLLSARKLHSEAKVILQSALKLYPSNISLLTTKCRLELCLMEEQDALRTCDEIITLCNRDSTENKLSNSFNQLPVDGVSVANQSTGTELEVGSLLNSVMASRIDRVNSDVESLMGVIHPMLPHMWSGKCTAWVQVADVYLALERYQEAELCVAEAAGLQPLLPDVLYMKGRLCEYNGELDEACSFYNSALTIDPSHLESTEKLAKVLSSNGNICYAKKVLQDAIRLDATSHTVWQQLSDLLAATDEIDQSIECNIFALNLEASSPVLPYTCIVPFI
The following text describes a protein:
Function:
Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Sequence:
MVLDRASDIVTAATTSNDALLSKLSALRAGYLVDPALRAIYTKPSLPRKDPMINRGTWFRFTYIEQMAVAFAAKYAGNCAIVSLGAGLDTLYWRLQLIAQQERSEGKQSYFHVKHWIELDLPSITELKAKKFDLMHGETIDMPMSEDCAVRPFQEGQVILYRPKREHAETTPEALRVDLPGYQLYAANLEMRKTWMPLVRKIVADEKGDTTLPVLFLSEVCLSYLDADSTVGIIRDLPTYFNNFGLVCFEMVNPSDSFGEMMQINMAERQVVMPSFVELGFTAQYRKLFQLSGYEASYAKEAGDVYRSFWPARRREIEQLELFDEFEQWNLIMGHYACIMGWTGIENLEEMLASVGQSADSPDK
The following text describes a protein:
Function:
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Subcellular Localization:
Mitochondrion.
Sequence:
MAQVAASGARQPLLQLLRGPSGHLWEVCIGLEVHAQVLSRSKLMSGAAAATLASARPNRHVSLFDAALPGTLPVLNRECVRQAIRTGLAVDATVHPRSLFERKHYFYCDMPLGYQLTQQRAPVASGGALHFELPASAIVSEHGEGGIEEQETTFDASKYKSRKEKNEALRKRKAKQATKQEDVIPRSVRITRIQIEQDSGKSNHDLEEHNTVVDLNRAGTALLEIVMEPDLRSPLEAGQVMRQLQHLLRHLDVCDGNMEEGSMRCDLNVSVRPTNLGRGADVEMLHHALTSSTAAPFGERVEVKNMNSIRNMMRAAEYEARRQIALIEEEGGEVHRETRSFDAATGETKRMRSKEGAKDYRFFPEPDLPPLVVPETLIQEISENLPELPGALKDRLCAQYDLTPYESSVLVNEPGAAHYFETIAALDSRPSKMVVNWVLNDLFGHLKAANGDIASSPVQATELGALIDLIQDGTISGKIAKDVLELMFYENEAKRTPLQIVEEKGWKQIRDPEEIRALCRAVLDDPVRSAIA
The following text describes a protein:
Function:
Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation. Acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens such as Salmonella typhimurium upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy. Initially orchestrates bacteria targeting to autophagosomes and subsequently ensures pathogen degradation by regulating pathogen-containing autophagosome maturation. Bacteria targeting to autophagosomes relies on its interaction with MAP1LC3A, MAP1LC3B and/or GABARAPL2, whereas regulation of pathogen-containing autophagosome maturation requires the interaction with MAP3LC3C. May play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion.
Subcellular Localization:
Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cytoplasmic vesicle, autophagosome membrane; Peripheral membrane protein. Note=According to PubMed:7540613, localizes to nuclear dots. According to PubMed:9230084 and PubMed:12869526, it is not a nuclear dot-associated protein but localizes predominantly in the cytoplasm with a coarse-grained distribution preferentially close to the nucleus.
Domain:
The MYO6-binding domain is required for autophagy-mediated degradation of infecting bacteria such as Salmonella typhimurium, but not for bacteria targeting to autophagosomes; The CLIR (LC3C-interacting region) motif is required for interaction with MAP1LC3C, but dispensable for CALCOCO2-mediated autophagosome maturation; The LIR-like motif is required for interaction with MAP1LC3A, MAP1LC3B and GABARAPL2, as well as for CALCOCO2-mediated autophagosome maturation; The LGALS8-binding domain is essential for the recruitment to cytosol-exposed infecting bacteria.
Sequence:
MEETIKDPPTSAVLLDHCHFSQVIFNSVEKFYIPGGDVTCHYTFTQHFIPRRKDWIGIFRVGWKTTREYYTFMWVTLPIDLNNKSAKQQEVQFKAYYLPKDDEYYQFCYVDEDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLSYMGLDFNSLPYQVPTSDEGGARQNPGLAYGNPYSGIQESSSPSPLSIKKCPICKADDICDHTLEQQQMQPLCFNCPICDKIFPATEKQIFEDHVFCHSL
The following text describes a protein:
Function:
Plays a role in regulating gene expression in dopaminergic neurons, acting redundantly with homeobox protein ceh-20 in head neurons. May activate dopamine pathway genes in concert with ETS domain-containing protein ast-1, and homeobox proteins ceh-43 and ceh-20.
Subcellular Localization:
Nucleus.
Sequence:
MSEASKSIMDLLSEVVKITDMTMDNEAVNKLKPQIKINPFYRAVQDVLVEQKSKIDLSTKMMKDLEAQENDERLDTMLKAEGVAGPDDSLLRIQEAAGTDQYEYRQQLLKVRRELENETKAFDKHCKKWCEYVEDVLQQQGEFRPITQQSTEKFMNKMSGKFNKVCFVLKQTACEEVIQLKKRYLDARRKRRNFSKTSTEILNEYFLANINHPYPSEEVKQALAMQCNISVAQVSNWFGNKRIRYKKTMAKNEDERRENRKPEDRPPPGAPGAPYSLVPNAFAGMMNPYQMMLPGHQFPIGVAPFNFSMYNPEMMAQYQQSLQNPNQTR
The following text describes a protein:
Function:
Dosage dependent suppressor of PKC1 deletion and MPK1 deletion. Involved in cell lysis.
Sequence:
MPKNSHHHRSSSVNSTKSRSTESTNKWKIPHYYRRSASGSTQASPDRNSSTGSCSTPVLPTMNVMSSPKKVLLEDPRDNHTKAKKSSRKKSGEMVFVNYTVQDTANENDTDLQTQPVSVPAPKAKLKKKSSKRRMLKIFGSSKNEHIEDIVEEQPMVLQMDSESKPLSGTPISESGIDASSLTTKRSYNSFLKHNRLNGKTPFSGNLSFPSLNMMGNTTDLPIDNNDFCSEKEVVPKSTHDPSLAKPPSRFTESETNSTPNLSSIPLMNTKNTRLKYNKVAPQSSDRQKSQESGLYHSTESFNFKDQNYSNNKSSLSLNSDLSTPHFAKHSPDSPRTSRSFNCGDSQSKVKLPEENDASIAFSKMFTRKRANTGGSTCSLASPTIAQTIQQSNIKVNKLPTQRTTSVGSLSSMSNRYSPIRVASPGRARSATRGSSLYRLSRDLNSLPSVTDLPEMDSTTPVNEIFLDGQPQHKSGSVKGGHRKKQESISDAQRIQHSNSYITTPSSSLVTPPYYMTGYTLPSSASASSTPNVLETHNMNFVPSTSTVTSYRPSSNFSSFDKEYSNENDASGEFSAFNTPMENIPALKGIPRSTLEENEEEDVLVQDIPNTAHFQRRDIMGMDTHRKDDSLDFNSLMPHGSTTSSSIVDSVMTNSISTTTSNATGNYFQDQDKYTLVNTGLGLSDANLDHFIRSQWKHASRSESNNNTGNRVSYSGSTPNNVDTTKTNLQVYTEFDFENPESFFHEQSKLLGEMGHSNNNSNSAINMNEPKSADTYIGNISPDTSATVSLGDLMGSNVSNNSERNFYDGHTFVPQYQANSSVENSNNQNAAPIANNDIDNNLQSFYFDNSN
The following text describes a protein:
Function:
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular Localization:
Cytoplasm.
Domain:
The presence of the iron-sulfur cluster is required for assembly of the RNA polymerase complex.
Sequence:
MSINLLHKDDTRIDLVFEGYPLEFVNAIRRASMLYVPIMAVDDVYFIENNSPLYDEILAHRLALIPFMSEEALDTYRWPEECIECTENCEKCYTKIYIEAEAPNEPRMIYSKDIKSEDPSVVPISGDIPIVLLGTNQKISLEARLRLGYGKEHAKFIPVSLSVVRYYPKVEILANCEKAVNVCPEGVFELKDGKLSVKNELSCTLCEECLRYCNGSIRISFVEDKYILEIESVGSLKPERILLEAGKSIIRKIEELEKKLVEVVK
The following text describes a protein:
Function:
Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens.
Subcellular Localization:
Plastid, chloroplast.
Domain:
The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Sequence:
MDLISVLPSTSKSCVCMHKPLSSSTHKLKPFCRTIRILGMPRPRKSVLMASSMSMSVNTLVSDDDIQRRTGGYHSNLWNDDVIQFLSTPYGELAYRERGERLIDEVRDIFSSMSLEDGEFSDLIQRLWMVDNVERLGIDRHFKNEIKSALDYVYSYWSEKGIGCGTKSIITNLNSTALGFRTLPLHGYPVSADVLKHFRNQIGQFVSCPSETEEDIRSMVNLYRASLIAFPGEEVMEEAESFSEKYLKETLQKIPDCSLSREIGDVLEHGWHTNLPRFEARNYIDVFGQDTKNMESNRKTEKLLELAKLEFNIFQSIQKTELESLLRWWNDSGSPQITFTRHRHVEYYTLASCIAFEPQHSGFRLGFAKACHIITVLDDMYDLFGTVEELKLFTAAIKRWDPSATDCLPQYMKGIYMMVYNTVNEMSAEAQKAQGRDTLNYARQAWEVYLDSYMQEAKWIATGYLPTFEEYLENGKVSSGHRVSALQPMLTMDIPFPPHILKEVDFPSNLNDLACAILRLRGDTRCYQEDRARGEETSCISCYMIDNPGATEEDALNHLNVMISGVIKELNWELLKPDSSVPISSKKINFDITRAFHYGYKYRDGYSVSSVETKSLVMRTLLEPVPL
The following text describes a protein:
Function:
Involved in nucleotide metabolism via production of dUMP, the immediate precursor of thymidine nucleotides, and decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Sequence:
MLISDVGNGIERNYTLQKFILQCYEEQLKNNKNKKVIIIERHPREAIEVFCEIDKTMTEKEREEITNKIYLIEKEYQLEYNKYNTYCISTDYATPNVIARNIFTEWVKRENIENETFHVFLYANEENQKKRIIKRNRGVISEMNFYYVNQINTLYKHYLNEHFTSKENNEETLFIKKLHKDAIIPTRGSDQSAGFVLYSIDDNIIYPHDRCLISTGIAVQIPHSCYGRIAPRSSLAIKYGIDIGGGVIDEDYRGEIKVIVFNHSNTIYKCKKGDRVALLIIEKIKQCKIEEVKEISETIRGEKGFGSTGK
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates 60S ribosomal protein L42 (rpl42) at 'Lys-55'.
Subcellular Localization:
Nucleus.
Sequence:
MLKQAESMLKWAIEKDNYTTSEKIGLNDYRHVHESLGIGFIALEDIKEDEKLVSFKKDSVLCLTNSDLAQLPEVQSLPSWAALLLVMATENASPNSFWRPYLSIFPTKERITSPFYWDENKKDALLRGTVLESNEDCNEITQLWIDRIEPIIKLYPNRFSQVSYEDFLRMSAVMLAYSFDIEKTKSPISNENEKSAAETSIKEDKNGDAAKKNEGSANQDDEKLHSQSLVGNNCEVNSEDEFSDLESEVDPDELEKAMCPISDMFNGDDELCNIRLYDINGTLTMIATRDIKKGEQLWNTYGELDNSELFRKYGFTKKKGTPHDFVLIKKEHWLPEYIEKLGFEEVEARLELLCREELLYNLEGDFTFSKADLTFKEICLAFVLMEKEKELISVPSKSDIKPKHYRKLLKIIEKRINMYPKISDPKNFDEENAKTLIEGEIDILQNLSAKVKEALTKNRPKKKQKVDH
The following text describes a protein:
Function:
Required for cytoplasmic pre-assembly of axonemal dyneins, thereby playing a central role in motility in cilia and flagella. Involved in pre-assembly of dynein arm complexes in the cytoplasm before intraflagellar transport loads them for the ciliary compartment.
Subcellular Localization:
Cytoplasm. Dynein axonemal particle. Note=Localizes in the apical cytoplasm around the gamma-tubulin-positive pericentriolar region, not in the cilia.
Sequence:
MAGPGRLEELELSSEEAERLQRAFRDERFRALFAEYAAELTDPEQRRLYEEEVTALERERGVEVRFIHPTPGYVLRTSQAGSRRCYLNICSNPHIAPPQARAEPGGHRWELPHSLAPGREELGRAGRRCFVYDVVFHPAALRLAARSARFRRLLSDAAMEAVESRFSAQLDRTNASVLRGTRYKGIPQAPVIRSPLPGGAPRPPSDTDPPLPPPPGPPPGPPPAAPPPAPGPTTPRWSVRHRSYVDLQDYRCGRDSAPGPVPRELVVTVELPLLRSAAQAELEVRPRELRLDSRRPAYRLRLRLPYHVDESAGRAVFDKAKRQLLVTLPVVPPPGPGTPLGEAGGERREEPPPGPELPEEPAAASSPPPRSEAASPSAGPQPGAASPAPSAGSEPAPPGGAPSPCPPEGSPDHMAHSRGGGDSGPAAAVCPPFQCRQDEASLTLLLLVPGIQPQSLSGEVAANRYSVRFSSGAVAYALILQFPAANRLAAPETSVSVGAHNTAILLSKATESTGLWEKYCFGLDASALQERLFVSEENIDGFLRTVLCPSSCTQSDLEAQTLIEVLDVSEDRSQIRLKPREAAGSEHDETNQAVSSSGGDVAAKNNEDHLQPEPEPEHTAAATAEERPTESQRAATSFVTAETIEVDGGSQHCLQQEPSDTGAALPGKPGGKEQALDEAFAGLGLEGGRAGGAGSPAVSPVLQEVGADGSVQSIADHSTHCSIAFQNSVLYELD
The following text describes a protein:
Function:
Involved in chronological cell aging. Extends cell viability after entry into the stationary phase probably through affecting the Pka1-dependent pathway negatively.
Subcellular Localization:
Nucleus.
Sequence:
MDLDFCTVCGATTQDGSLYCSSECHLLDFTKLDTQTTSNISVSSEYQFLVSEHLAHFHRKSMTSADFPTPRFSAYTKLHA
The following text describes a protein:
Function:
May play a role in ribosome biogenesis.
Subcellular Localization:
Nucleus, nucleolus. Nucleus, nucleoplasm.
Sequence:
MAPTRTRASAIGAPSQPAQSSRKGKKAWRKNIDLTTTESFLEQQSDPLRETSSEVLFVEDRSGQETLAARQARTKRPLKSLEILQNSYGHAALAKPARKHDKKLESQLRKLVGRQRVSTQGDATAIAQKSDDVVKTTLHSVYDVWGSSAKGKSKADDESWIPEQVAKPTIKQPKTLRRDDYQNITSTLPAIDVPHPGSSYNPDLESHEALIQQAYEIEKRLEENEQMAQAEREQWRAKLAIIVAREAELRLQKDDDLKRYRGMEVDVPTDGESDDESERQGMDSDGDAEASEAKRKTRAQRARAKRAHQQQAEAARRKQARIEAAAILHLPALKRRQARLATARAQAAHQRRLQKQTLLAKHGLQGQKLGKHTVPLTRIDVQTSDQLTESLRTLKPEGNLFRDRYQRLQVTGKLEPRVKQSASTKRRKKLKSYETHDYKNFS
The following text describes a protein:
Function:
Non-catalytic component of the proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MLSNKRGIHSASGGIDLRTLREYCLFEDFDVCMPFNPMGVPGGKGNRGSDGAIRGMLPLGDAMGDLFTAGKAGSTKMEDKERFDPYEDNSGTTICLKQGDFIVVAGDTRHSSSMVINSREMSKIFQVGDFLLTGTGFYADTHEVYVKMVYEIRQYEVDDSINIHSAANLLSKILYSKRFFPYYSFCVLSGFEKGKPYVYSYDPIGSFGSVTCVCSGSGRSMIQPLLDSFIDKKNWNNAEETQLSQEDCIRLVVKAFNSAAERDVKTKDNLEVCVMRENQVMRETFPLRRD
The following text describes a protein:
Function:
Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. When antigen presenting cells (APC) activate T-cell receptor (TCR), a series of phosphorylation lead to the recruitment of ITK to the cell membrane, in the vicinity of the stimulated TCR receptor, where it is phosphorylated by LCK. Phosphorylation leads to ITK autophosphorylation and full activation. Once activated, phosphorylates PLCG1, leading to the activation of this lipase and subsequent cleavage of its substrates. In turn, the endoplasmic reticulum releases calcium in the cytoplasm and the nuclear activator of activated T-cells (NFAT) translocates into the nucleus to perform its transcriptional duty. Phosphorylates 2 essential adapter proteins: the linker for activation of T-cells/LAT protein and LCP2. Then, a large number of signaling molecules such as VAV1 are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation. Required for TCR-mediated calcium response in gamma-delta T-cells, may also be involved in the modulation of the transcriptomic signature in the Vgamma2-positive subset of immature gamma-delta T-cells. Phosphorylates TBX21 at 'Tyr-525' and mediates its interaction with GATA3.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Localizes in the vicinity of cell surface receptors in the plasma membrane after receptor stimulation.
Domain:
The N-terminal PH domain allows ITK to be recruited to the plasma membrane by an activated PI3 kinase. This domain also contains a proline-rich region (PRR). The adjoining domain is a SH3 domain, which binds to PRR (from itself or from other proteins). Next, a SH2 domain is required for binding tyrosine-phosphorylated substrates. In the C-terminal region, the kinase domain is required for tyrosine phosphorylation (By similarity).
Sequence:
MNNFILLEEQLIKKSQQKRRTSPSNFKVRFFVLTKASLAYFEDRHGKKRTLKGSIELSRIKCVEIVKSDISIPCHYKYPFQTLVYLQVVHDNYLLYVFAPDCESRQRWVLTLKEETRNNNSLVSKYHPNFWMDGRWRCCSQLEKPAVGCAPYDPSKNASKKPLPPTPEDNRRSFQEPEETLVIALYDYQTNDPQELALRCDEEYYLLDSSEIHWWRVQDKNGHEGYAPSSYLVEKSPNNLETYEWYNKSISRDKAEKLLLDTGKEGAFMVRDSRTPGTYTVSVFTKAIISENPCIKHYHIKETNDSPKRYYVAEKYVFDSIPLLIQYHQYNGGGLVTRLRYPVCSWRQKAPVTAGLRYGKWVIQPSELTFVQEIGSGQFGLVHLGYWLNKDKVAIKTIQEGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDYLRSQRGLFAAETLLGMCLDVCEGMAYLEKACVIHRDLAARNCLVGENQVIKVSDFGMTRFVLDDQYTSSTGTKFPVKWASPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDISTGFRLYKPRLASCHVYQIMNHCWKEKPEDRPPFSQLLSQLAEIAEAGL
The following text describes a protein:
Function:
Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp.
Sequence:
MIGYLRGLAVIVEDVEFARRLYKEGFYGRFLGYDKVKRDEVEKINAPLILGLYEALYLAEKGRLKVMGEDGREVAPEELAALGRERMRNFDEIYKIYKYFRDLGYVVKSGLKFGALFSVYEKGPGIDHAPMVVVFLEPDKGISATDITRGGRLSHSVRKTWTLATVLRQTGEVVLLGFGWARL
The following text describes a protein:
Function:
mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing. Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates.
Sequence:
MTNVSGVDFQLRSVPLLSRVGADRADRLRTDMEAAAAGWPGAALLRVDSRNRVLVANGRVLLGAAIELADKPPPEAVFLGRVEGGRHVWAVRAALQPIADPDIPAEAVDLRGLGRIMDDTSSQLVSSASALLNWHDNARFSALDGAPTKPARAGWSRVNPITGHEEFPRIDPAVICLVHDGADRAVLARQAAWPERMFSLLAGFVEAGESFEVCVAREIREEIGLTVRDVRYLGSQQWPFPRSLMVGFHALGDPDEEFSFSDGEIAEAAWFTRDEVRAALAAGDWSSASESKLLLPGSISIARVIIESWAACE
The following text describes a protein:
Function:
Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone.
Miscellaneous:
MISCELLANEOUS: In contrast to other lysine histone methyltransferases, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones.
Subcellular Localization:
Nucleus.
Sequence:
MFSFFGDESKLPASTVMVSRMTVKKQAVARQQSSGPMAGPSKPSNVTPKHSHGSLKGTPRSASEKGTPKQGPSSSSKSTSKVKQEERIRLSTIPRTPASSSSPGRLKRKTPKVQVVESESSSGSESSDGALDSKPKRPKVTRKETGIDMTPLPGEEVVGRRVFCWDKVDMRGEWGRGWAGFVGCDEVVRGNVQGWANGGGGDGSKNLGKYRAFFPQEGFDRDGDFLPSVEVLYPAKGCREKFVLMVPSSDREFNPIGELRNTLRLILEHYIPPSHRHIFGTLAESLDISNPLSSLPSRMTTPLPNSLVTPPPDPASPSPAFAFEISATSTPAPSTERQETIADLIRKSLAPNRRDGPLFVTAIERYNSAMQAIQEDGTLQQWLDEGMNGGKGIKVREWAALVDFVHDQAYSRVVGGYSHELEHHPKHPEEVSKAISGKEDAYGELRHAFMSKIIEQTKLGPDSVFVDLGSGVGNCVLQASLQAGSRSYGFELLPVPAHCARLQVREVQRRWAMWALKGNLDVEVHEGDFRVHKEVGRRLREADVVLVNNEVFPSSLNMDLADMFLDLKEGAKIVSLKPFVPEGFRMNESNCDSFAAILRSTQHDYYRDWVSWKGEWGNYYVAVIDRSRRIKFEESMKGRASRRR
The following text describes a protein:
Function:
Transporter for ammonium (both charged and uncharged NH3 and NH4) to use as a nitrogen source. The affinity of MEP2 is about twenty times higher than that of MEP1. MEP3 has the lowest affinity. Under ammonium limitation acts as an ammonium sensor, generating a signal that leads to pseudohyphal (filamentous) growth.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
Within the cytoplasmic CTD, an enhancer domain, limited to residues 428-441, upregulates substrate translocation via the MEP2 hydrophobic core, while an autoinhibitory domain, comprised within the 450-485 region and including the NPR1-target serine Ser-457, counteracts the action of the enhancer domain. In between, a linker domain, limited to residues 442-449, appears required for optimal activity when the kinase is present but dispensable when the kinase integrity is altered.
Sequence:
MSYNFTGTPTGEGTGGNSLTTDLNTQFDLANMGWIGVASAGVWIMVPGIGLLYSGLSRKKHALSLLWASMMASAVCIFQWFFWGYSLAFSHNTRGNGFIGTLEFFGFRNVLGAPSSVSSLPDILFAVYQGMFAAVTGALMLGGACERARLFPMMVFLFLWMTIVYCPIACWVWNAEGWLVKLGSLDYAGGLCVHLTSGHGGLVYALILGKRNDPVTRKGMPKYKPHSVTSVVLGTVFLWFGWMFFNGGSAGNATIRAWYSIMSTNLAAACGGLTWMVIDYFRCGRKWTTVGLCSGIIAGLVGITPAAGFVPIWSAVVIGVVTGAGCNLAVDLKSLLRIDDGLDCYSIHGVGGCIGSVLTGIFAADYVNATAGSYISPIDGGWINHHYKQVGYQLAGICAALAWTVTVTSILLLTMNAIPFLKLRLSADEEELGTDAAQIGEFTYEESTAYIPEPIRSKTSAQMPPPHENIDDKIVGNTDAEKNSTPSDASSTKNTDHIV
The following text describes a protein:
Function:
Seed storage protein.
Sequence:
LSTLNTHNLPLLRLVYLEREDLVAVHVDDLNNQANQLDQKLDGGLLPQGHAPHWLMNAHSLFYLTRLLVAQCRAPKGMLVVLPAGVAHWCLNDGKHYLDNPR
The following text describes a protein:
Function:
Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II (By similarity).
Subcellular Localization:
Nucleus. Chromosome.
Sequence:
MGDEIVIDKTAFFNRLSSFYAAWKADKRSTNSVFGGAGSIIILMGKTDEANSYQKNNAIHFWLLGYEFPATLFVFTPEVMYVVTTAKKAKHLEPLKGGKIPVEILVTTKDQEEKTRLFEKCVDIIKSAGNKVGILPRDTTTGPFVEDWKRVYGKISGDVEEVDISPALSAACFSVKDTDELVSIRNASRACSGLMSDYFVDEMSRLLDEEKQMTHKALSMRIDAKIDDAKFFNKLAKLPSEFDPQQIDWAYGPVIQSGGKYDLKLTAVSDDNNLEPGIIIAGFGIRYKTYSSIIGRTYLVDPTKSQEANYSLLLSVHEAVLKEARDGVVAKELYNKAIGIVRARKPELESHFVKNVGAGIGIELRDSNMILNGKNTRVLKSGMTFSITVGLVDVEEPSVKDKKKNVYSMMITDTVRVGEQGPHVFTKDAGIDMDSVSFYFGDEEEPQKPAKEKKETKSSAIASRNVTRTKLRAERPTQVNEGAEARRREHQKELAAKKTKEGLDRFAGTTGDDNGVTQKKFKRFESYKRDNQLPAKVKDLTVYVDHKASTVIVPVMGRPVPFHINTIKNASKSDEGEYAYLRINFLSPGQGVGRKDDQPFEDLSAHFLRNLTLRSKDNDRFAQVAQDITELRKNALRREQEKKEMEDVVEQDKLVEIRNRRPVKLPDVYLRPPLDGKRVPGEVEIHQNGLRYVSPFRNEHVDVLFSNVKHLFFQPCAHELIVLIHVHLKTPIMIGKRKTRDIQFYREATEMQFDETGNRRRKHRYGDEEEFEAEQEERRRRAALDREFKAFAEKIADAGKDEGVDVDIPFREIGFTGVPNRSNVLIQPTTDALVQLTEPPFLVISLNEIEIAHLERVQFGLKNFDLVFVFKDFHRAPVHINTIPVENLEGVKDWLDSVDIAYTEGPLNLNWTTIMKTVVSDPYGFFADGGWSFLAAESDSEDGSDEEEESAFELSESELAADESSEEDSDYDDDASADDDFSADEDESGEDWDELEHQAKKKDRESGLDDEDRGKKRKR
The following text describes a protein:
Function:
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Sigma-S contributes to the protection against external stress, thus playing a role in cellular fitness and survival.
Sequence:
MKYDLTTQDSTIKRNNAINDKDFEKLVMDLQPLIIRRIKTFGFNHYDLEDLYQEILIRMYRSVQTFDFSGEQPFTNYVQCLITSVKYDYLRKYLATNKRMDNLINEYRVTYPCAIKRFDVENNYLNKLAIKELICQFKYLSAFEKDVMYLMCEQYKPREIAQLMHVKEKVIYNAIQRCKNKIKRYFKMI
The following text describes a protein:
Function:
Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. Involved in the pre-rRNA processing steps leading to small-subunit rRNA production independently of its RNA-modifying catalytic activity. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome.
Sequence:
MGQHILKNPLIVNSIVEKAAIRSTDTVLEIGPGTGNLTVKLLQKAKKVIACEVDPRLAAELQKRVQGSPVSTKLHIIVGDVLKTELPYFDVCVANLPYQISSPFVFKLLLHRPLFRCAVLMFQREFALRLVAKPGDKLYCRLSINTQLLAKVDHLIKVGKNNFRPPPKVESSVVRIEPINPVPPINFKEWDGLTRIVFARKNRTLSASFKTQGVQTMLEKNFRIHCSIHNQAIEEDINIAEKVDTILKSVNANARRARSMDMDDFLELLHAFNSNGIHFA
The following text describes a protein:
Function:
Polynucleotide 5'-kinase involved in rRNA processing.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSEAENKLPFIPEEWSNAASSVSCSSLQPVIALVCGPKNSGKSTFSRNLVEVLLQRYKRVAYLDTDVGQPEFTAPGFLSLTIVDKSILESDWTVPCVKTPERCFFYGDVSSKRDPKAYLRYVYTLFDYYQLHFCKSSENKTELPLVINTPGWVKGIGYELLVDVLRYVSPSHVVKINISAYNKNLPAGLFWLDGNDDETAHLIEIQSAYQDRYNQSILIHKDARLMRDMRIIAYFRQCFKGKEVNTIKELTHELASHIPYEVPISSLTINHLHCQIPSSEVYYSLNASIVGLGISTEVFEDLPSCVGLGIVRGIDTERGILYVITPVPENLVEKVDLLLQGYIQLPTCLLEVKDYRSPYLSANVLAST
The following text describes a protein:
Function:
Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Is involved in the demethylation of trimethylated 'Lys-9' on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. Also catalyzes the hydroxylation of 60S ribosomal protein L27a on 'His-39'. May play an important role in cell growth and survival. May be involved in ribosome biogenesis, most likely during the assembly process of pre-ribosomal particles.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MATDATRHPVGAGLRVMLILLACLATVATSTSSPDMPDLPQVSAVDHHLLRQMLGDAITPTAFLQHYYRQDLLHIPAIATKKSADLWASDSWFEDLKHVDALLAETLVQFHDDDNVFVLRNNKARSQTINTTDWSVQGPRFYAEGQSAVIRREFQDVPQSPFEHMLLDVFGASEVTAHAYISAPHALALPPHTDQYDVVVVQVFGHKEWTICTGTNDSSADWPEATPAQLAQIYELEISNPEGCRNWAIKDLERMHCRQLTLRENDILYLPKALIHFATTNDNITSAHVTYSIDRDEASWRDVIETACWQSQHPLCAVVSQVLAGLDHSALGLPWIQLAHEPMGGLETSCATANDLVRSYHPYSLRSLMKAQTFSALPAYVTPHDMNMFLARLADCNATMGVDEKGHPVSMTQLIINRKALDLLHPTPSRNRRDVAWTAPCNSKGGVCTGCNGRSCDDSCNSGETCDNYGCDSSCNSGDDSCDNSCDGTCNTCTGGCDTYACNTAACAAGYYKFTNDITNQGCQVCQTGKYQEATHNSWSCKNCAAGTYASTTGRTSCTACPGGQFQTATGQSSCKSCSSYGTVCDSGQYQGGCTGSTPGSCYTCSSGTYQNANSHRAASCKTCAACGIGKYYGCTITAGTTCSVC