lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May play a role in mRNA degradation. Endonuclease required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits.
Subcellular Localization:
Nucleus.
Sequence:
MAPTLVEHVVADAGAFLKRAPLQEIGANIYTLRDVVDEIRDKETRRSLAVLPYQLHFREPHPEHVRHVTEFSKKTGDYPSLSATDIRVLALTYQLQLEHEGAEHLREEPLLQVNIQSTPRHPETPVNVPGFHFPSKKATEASNTQTHDHKDGESFNSFQFWREPVAPLDNDLLASLGPEEESHDGRSEAADGEHFNSFQFWREPTPIISDELLALLDEGGASRSDPSAEDRSDDEDKENEPEEEEPDGGGWITPSNIRQVKMESADWTAPADVTVGCLTTDFAMQNVLIQMGLHVLSVGGMVIRQARNYILRCHACFRTTSSMAKVFCPHCGNRTMKKVAVTLNDDGTTKMHFSRNPKVLNSRGLRVRGGVGGAYVVGSHVTCLCLRRSTLCRCLRGGNTETTPTWWRTSASPSSASPGRPGRRPTSSTRTTWRDPPPLARTTSTAALPTCRSETVSAVAAGGGPTPTPPAKSLSRRSDGGSVRLSRTRTFRSPAGCV
The following text describes a protein:
Function:
The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP.
Subcellular Localization:
Cytoplasm. Nucleus, gem. Nucleus, nucleoplasm.
Sequence:
MSEWMKKGPLEWQDYIYKEVRVTASEKNEYKGWVLTTDPVSANIVLVNFLEDGSMSVTGIMGHAVQTVETMNEGDHRVREKLMHLFTSGDCKAYSPEDLEERKNSLKKWLEKNHIPITEQGDSPRTLCVAGVLTIDPPYGPENCSSSNEIILSRVQDLIEGHLTASQ
The following text describes a protein:
Function:
Promotes chloroplast protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MAATTAAAVYRFAVLAPVPSPLSSGRRRPAAPFSRPRGISATPRGRVLCLAASAPASSTDAGQDRLQKVPITNIRNFCIIAHIDHGKSTLADKLLEMTGTVQKREMKQQFLDNMDLERERGITIKLQAARMRYVMNNEPYCLNLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALESNLEIIPVLNKIDLPGAEPDRIAQEIEEIIGLDCSNAIRCSAKEGIGITEILDAIVTKVPPPQDTLKNPLRALIFDSYYDPYRGVIVYFRVIDGSIKKGDKICFMANKKEYLADEIGVLSPNQMQADELHAGEVGYLSASIRSVADARVGDTITHYSKGAECALPGYSEATPMVFCGLFPLEADQFEELREALGKLQLNDAALKFEPESSSAMGFGFRCGFLGLLHMEIVQERLEREYNLNLIITAPSVVYRVNCANNETVECSNPSLLPEAGKRRSIEEPYVKIELLTPKDYIGPIMELGQERRGEFKEMNYITENRAKLIYMLPLAEMVGDFFDQLKSRSKGYASMEYAVVGYRVSDLVKLDIQINGEPVEALSTIVHRDKAYSVGRALTEKLKELIPRQMFKIPIQACIGAKVIASEALSAIRKDVLSKCYGGDISRKKKLLKKQAEGKKRMKSIGRVEVPQEAFMAVLKLEKEVL
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that plays a key role in the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, leading to degradation of nascent peptide chains. ZNF598 is activated when ribosomes are stalled within an mRNA following translation of prematurely polyadenylated mRNAs. Acts as a ribosome collision sensor: specifically recognizes and binds collided di-ribosome, which arises when a trailing ribosome encounters a slower leading ribosome, leading to terminally arrest translation. Following binding to colliding ribosomes, mediates monoubiquitination of 40S ribosomal proteins RPS10/eS10 and RPS3/uS3, and 'Lys-63'-linked polyubiquitination of RPS20/uS10. Polyubiquitination of RPS20/uS10 promotes recruitment of the RQT (ribosome quality control trigger) complex, which drives the disassembly of stalled ribosomes, followed by degradation of nascent peptides. E3 ubiquitin-protein ligase activity is dependent on the E2 ubiquitin-conjugating enzyme UBE2D3. Also acts as an adapter that recruits the 4EHP-GYF2 complex to mRNAs. Independently of its role in RQC, may also act as a negative regulator of interferon-stimulated gene (ISG) expression; (Microbial infection) Required for poxvirus protein synthesis by mediating ubiquitination of RPS10/eS10 and RPS20/uS10. Poxvirus encoding mRNAs contain unusual 5' poly(A) leaders and ZNF598 is required for their translational efficiency, possibly via its ability to suppress readthrough or sliding on shorter poly(A) tracts.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MAAAGGAEGRRAALEAAAAAAPERGGGSCVLCCGDLEATALGRCDHPVCYRCSTKMRVLCEQRYCAVCREELRQVVFGKKLPAFATIPIHQLQHEKKYDIYFADGKVYALYRQLLQHECPRCPELPPFSLFGDLEQHMRRQHELFCCRLCLQHLQIFTYERKWYSRKDLARHRMQGDPDDTSHRGHPLCKFCDERYLDNDELLKHLRRDHYFCHFCDSDGAQDYYSDYAYLREHFREKHFLCEEGRCSTEQFTHAFRTEIDLKAHRTACHSRSRAEARQNRHIDLQFSYAPRHSRRNEGVVGGEDYEEVDRYSRQGRVARAGTRGAQQSRRGSWRYKREEEDREVAAAVRASVAAQQQEEARRSEDQEEGGRPKKEEAAARGPEDPRGPRRSPRTQGEGPGPKETSTNGPVSQEAFSVTGPAAPGCVGVPGALPPPSPKLKDEDFPSLSASTSSSCSTAATPGPVGLALPYAIPARGRSAFQEEDFPALVSSVPKPGTAPTSLVSAWNSSSSSKKVAQPPLSAQATGSGQPTRKAGKGSRGGRKGGPPFTQEEEEDGGPALQELLSTRPTGSVSSTLGLASIQPSKVGKKKKVGSEKPGTTLPQPPPATCPPGALQAPEAPASRAEGPVAVVVNGHTEGPAPARSAPKEPPGLPRPLGSFPCPTPQEDFPALGGPCPPRMPPPPGFSAVVLLKGTPPPPPPGLVPPISKPPPGFSGLLPSPHPACVPSPATTTTTKAPRLLPAPRAYLVPENFRERNLQLIQSIRDFLQSDEARFSEFKSHSGEFRQGLISAAQYYKSCRDLLGENFQKVFNELLVLLPDTAKQQELLSAHTDFCNREKPLSTKSKKNKKSAWQATTQQAGLDCRVCPTCQQVLAHGDASSHQALHAARDDDFPSLQAIARIIT
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; 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 and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription.
Subcellular Localization:
Nucleus.
Sequence:
MDRWGHHGDIMGSREHHGDIVGSLWDQGDFMGTSWGHRGDIVGSRGHHGDIIEMWGHCGVKGTSWRHHGDVVGSLWGQGDVMGTLWGYCGLKGTSWGHHGDVGSLWGHCGVKGTSWGHCRVKGTSWGHCGVIVGSRGHRGDIMGMWGHCGVKGTSWGHCGDIVGSRGRHGDIMGTLWGHCGVKGTSWGHHGDIVGSRGHHGDIMGMWGHCGVIVGSREHHGDIVGSREHHGVKGTSWGHCGVIVGSRGHHGDIMGTLWGHCGVKGTSWGHRGLKGTPWGYHGDMGALWGRGTWGPISAPQRRSRRFYPTRLAIALASGTSGTPPEPDTRGFIVVETNYRIYAYTDSELQIALIALFSELLYRFPNLVVAQVTRDSVQAAIANGITADQIIHFLRTRAHPIMAKQSPVLPPTITDQIRLWELERDRLRFSEGVLYNQFLSQVDFEVLRDHARALGVLVFENPTRRLMVVTPGGHPDVKRFWKRQKHSS
The following text describes a protein:
Function:
Transcriptional regulator.
Sequence:
MKIGALAKALGCTVETIRYYEQQGLIPPPKRTSGNFRQYNEEHLQRLSFICNCRNLDISLSEIKSLLNLENASKQQAEEINRVLDKHIKEVATRIHELAHLRMKLIELREKTVSNDEDPMKLLLQHSGVKFVRLK
The following text describes a protein:
Function:
Involved in mRNA export and mRNA coupled transcription activation. Component of the nuclear pore complex (NPC)-associated TREX-2/AMEX complex (anchoring and mRNA export complex) which functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), thereby enabling the export of mRNAs to the cytoplasm through the nuclear pores. The TREX-2/AMEX complex also functions with the transcriptional coactivator SAGA/TFTC complex, to anchor a subset of transcription sites to the nuclear pore complex basket in order to achieve efficient transcription and export of their resulting mRNAs. Within the complex, required for localization of e(y)2 to the nuclear periphery.
Subcellular Localization:
Nucleus, nucleoplasm. Nucleus. Nucleus membrane; Peripheral membrane protein. Cytoplasm. Note=Localizes to nuclear periphery, often in contact with the nuclear pore complex (NPC).
Sequence:
MAEPRPGGYNYKTLLCRNIPELFLDKYVARSHFGRFGTLVNFVLRPRRMTCTVSYASEDEAARALLDGASFQGHLFDISYADNETAPAQKTEEWVDPDIQAELSALQSGWRNEYGSGKPIKKPQNGSSGSGGSSMLPAIPVGPATAPVSRDRTPAQLRDLENMMRRPAHTSEEKFSVLDARDKLLRLNRTQHKLSGATQGHCADMCPEKERVLREFQRQVAYYELQPGSDELICHERALKQYSRSSADQETPLPHELRNETALHMTMSYLMHEIMDISERQDPQSHMGDWFHFVWDRTRSIRKEITQQELCSLGAVKLVEQCARFHIHCAARLVDADPSVFDSKINAENLTKCLQTLKYMYHDLRIKGVPCPKEAEFRGYIVLLNLADANFLWDIGQLPAELQSCPEVRQAIQFYLALQDTNFVRFFQLLADKDTSYLSACILVNYFTRLRVLGLHRLIQAYRSPRKDEVSSLPLSYIAELLSFASEQEAADFVQHYGLQINEAGRVVLSRMHTVETEYKLPRQYELVEVKRVKSVGEVVSGEPLPPRDLYLNHRPHNSFDDYGMLKSIAWTAKDQLAGMQQEEMQPQMPSQPPAVSKHSDTLFKVPMQPDGTAAGFGVFAAAAVPPASSIDGFSFVLPKSRAQEFQEQAPATQQRRAQEEAKHQALQVAIAAAKKREAELMAIHEAKVAEAERVRQQKLRERQEQQRRQQQELEEQRQREQEKLQLEKERQLKLEQLFFVQQQEREAHKQTRTLELYQEIFQDTLAEICQSEFMSHSRACRSYESMLDSITRDLVERQMEQSIYELGVMRVCIRRWRKYRRTQQEKDTLFNQLPLSFGAENPEGVVNKRSMEDSLRLSRRYRLGEPCDYGKLLAGLEEHSWLKLDLWHVLDKCLPVAQPGARRFYKLLISLSGGQEGLQLNCDLDRGLLQQPQSPDARFVDGGYIRGFSQGIGLSVMKIRDDDHDWKATDLAEANGIICLIGLDDIRLLPDRLKPLLQASRCHDVAVIVQHPANTAFVQPDIPLQELCLRSFNIFRLRKSGNNRQRLMIALESAVKFLAKATERKRVGHLHQVETREYLLVNLGSELFRRLKYAAEHDTAIRSDTQLNPQRCVDLFNEAVHRLQLVAGEDLSDWPQFPEELRVFVQPLPIESSLNTNRLEHFEPGWHLPERRQRIVQLLERCKLPKMPVLPRSSSLAEAQCQWVLDYAQISQQEDCVEQIALQAIKILQYDTDDYLNFVEYLAGERMQYILRQERNPPQGIVYNTKTLKRRFLSAWYYEFREPQIYEPVPAEENAQMLEKQPSSQAEVQQLDFDEITSKAEAVLKRFHQRQDERHTLRELNRSHKSRKRRDASDHKHAMSSLVSALKAARSDYQGKSSAVCRLVAQMVEADQVKYQWTPNLTSLIDRKDASTRHQWRPHVNHSTRHARKLPVQSISFLSRCLAKKGEHAGLTSCVLSVKTRYAPKTLHGRELLIWRQSSMRPLLLPSSNLWTGVLSKRHYVPRLRPAEEDEEVERRAVPQLRITKEQSEEEEHQLQRRKDGSRLRNECSEFYLPMGEQDYSEREEENRGHRQAYVPSELMTPELATKWQTTSVTDRDRQLLNLEQQMKTQPSVRMTTQTWFSGNHRRYRSRRSGAKRYHVVSELEGWRRSSNHQPVPVFQGQPGEQEHLRHASHKASARSMPDGQERCQMVWEQKKRSPWHRTEVTNSNKVRMPRIRAAKSAVMMAQEARNKHHRLITKKLVYRPRRTVNAVQAEETEDQDTHHRHHGGGQKMSKRAPERALLKQHLADLLAVSKPEDSFRIGYQPNAPTRQLLEQGKCYVSLRREQFIHLHPVRPNSLILAVNLEVKESPRQPVTTLHRRDGAKRPRLVEDVVKPSLITVIRQSAATWDHNGRKVPAKKSNLVGMPSKEHAYQRRLVRNTSTLEAIVKAQAKPRSEPKSPSSATDYHRVASQKLPHVTSKADISKAADPFKDLDKPRIKEKEVASSWKQAYVVRSKMYDAITPYRRRAYPGKKCITKDKTDGYFLAKRSSAAAAGSSKKVKPPKQPVVSPKVQVPSVLHKKKSRESLGPQTTKTGKL
The following text describes a protein:
Function:
Alpha subunit of a hydrogen-evolving hydrogenase that utilizes protons both as a substrate for hydrogen production and proton translocation. Acts by coupling the redox reaction via ferredoxin and iron-sulfur (Fe-S) clusters to proton translocation across the membrane thereby conserving the redox energy in a proton gradient.
Subcellular Localization:
Cell membrane.
Sequence:
MKKVEYWVKIPFGPIHPGLEEPEKFIITLDGERIVNVDVKLGYNLRGVQWIGMRRNYVQIMYLAERMCGICSFSHNHTYVRAVEEMAGIEVPERAEYIRVIVGELERIHSHLLNLGVVGHDIGYDTVLHLTWLARERVMDVLEAVSGNRVNYSMVTIGGVRRDIGEKQKRLILDMIKYYREVLPQIEDVFLHDSTIEARLRDVAVVPKKLAIEMGAVGPTARGSGIKEDSRWSEQLGVYPDLGIKPVTPEDVTGEKARGDVYDRMAVRIGELWMSLDLLEHALDQMPEGKIKTFPKDNILVAKLKLLGDGEGIGRYEAPRGELVHYVRGQKGRDGPVRWKPREPTFPNLFTIAKALEGNELADLVVAIASIDPCLSCTDRVAIVKEGKKVVLTEKDLLKLSIEKTKEINPNVKGDPTPTGIGCSRGV
The following text describes a protein:
Function:
Possible regulatory or functional link with the histocompatibility cluster.
Sequence:
MSKEQVENNERKEFQKYLEEIYKHHKQSELSYFEHNLETWRQLWRVLEVSDIIVCLADIRHPALHFSPALYEYVLKDLKKKFILVLNKVDLVSPELVTAWKCYFQSKYEHLSVVCFSSFPKAESERNKEQGKVLSKKQRRKKFNSAVGPRELLAACSKLCGDKDEIDQVHEEVETNDALLTLGFVGHTNVGKSSLLNGLVGKKVVSVSRTPGHTKHFQTIFLTPSVRLCDCPGLVFPSLVDKQLQILSGLFPISQVQEPYTAVGYLAARWPLVHMLKLVLPQDLQEDDNKEVDHKWSAWDICEAWAERRGYMTAKAARRDVYRAANSILRLAVDGKVPMYHYPPGFVQERDKWKDHPDTLALAQVQDQKSESRRQREVDEEVSELRMRLKPHSLQPRDFMESADGDDEDETAEEGGLVSNNPFALLADE
The following text describes a protein:
Function:
Functions as a two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction.
Subcellular Localization:
Cytoplasm, cytosol. Nucleus.
Domain:
Histidine-containing phosphotransfer domain (HPt) contains an active histidine that mediates the phosphotransfer.
Sequence:
MMEDGAMGLINNEFEHLMISKRAEDPQFVVETIQEYCAEVKAILSQMKNDIATPDVEFSPLVASCDLVKKKSTRIGCELVISTCMLLIGACDERNKKKFSQTLELLKKDFSTTQSQLETYAWLERRIINVQVDQAESSGF
The following text describes a protein:
Function:
The spt4-spt5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene (By similarity).
Subcellular Localization:
Nucleus. Chromosome, centromere. Note=Centromere and heterochromatin.
Sequence:
MSSSYYVTPSQQRTLRACMVCSLVQLHSKFMRDGCPNCDNVLGLRGNNDAIQECTSQVFEGLITLRDPSTSWVARWQRLEGYVAGTYAVKVTGSLPDDVITNLEDSGVRYIPYVYLPGSCVSGDTDRLVGGMAVRWRRRPEVLELSSEVEVQFAWI
The following text describes a protein:
Function:
Forms a receptor signaling complex with TYROBP/DAP12 which mediates activation of macrophages as part of the innate immune response.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MSPLLLWLGLMLCVSGLQAGDEEEHKCFLEGENLTLTCPYNIMLYSLSLKAWQRVRSHGSPETLVLTNTRKADFNVARAGKYLLEDYPTESVVKVTVTGLQRQDVGLYQCVVYLSPDNVIILRQRIRLAWCQGKPVMVIVLTCGFILNKGLVFSVLFVFLCKAGPKVLQPSKTSKVQGVSEKQ
The following text describes a protein:
Function:
Required for chromosome synapsis and regulates crossover frequency during meiosis. Acts as a transverse filament protein and constitutes the central element of the synaptonemal complex.
Subcellular Localization:
Nucleus. Chromosome. Note=During zygotene in meiocytes, initially localizes onto the chromosomes as punctate foci and quickly extends into linear signals. Associates with chromosomal axes at zygotene.
Sequence:
MQKLGLSGLRGLEGFRSLAGSTSTAAKAPNPKPSSDIGGSTYGSFANLKITAEKLVKEQASVKTDLEMTHTKLRRATEQINLLEAKLQQAVNENAKLKVKQTEDSKLWQGLDSKVSSTKTLCNQLTETLQQLASQTERAEEDKKFFEEILGKNSKAFEEFNCLLHDSSIKLECAEQMIISGKQEMLRIKQEKEEMDQSYKEQLYASDTTIREKNSLIKQLEDSIEQNKARLLYVDSRLECMEQELKLKEDVCICLKENLASTESEKNDLKLRNEGYTLEVQKLSKDNKELNELLSGFTVKVTELDKEHTSISSHVTQLISSFERYDGKVHEEKMLMIKSAKDKFEHLQNQYVNLISENNALQTEIEELKSRIIELQKTQEIVMVQHVEECQVAEDKIRRLESEAEISASNISQLEKVASDLEGRVQKLLEDSRSAENHKQELLQKILKLESDNQELLGRVQSVLNEKSNDTESLQGEIAKRDQQVETLENQVNQLCSIIDEKEQLHTCAVEREKNLEEQKLQVQASLAATESQLTEAKKQYDIMLEGKKIELSKHLKELSLKNDQAINEIRRKYELEKVEIINIEKEKAEKLIKEMENKCNEKISENRQDSERYLMCLKEEHGSMVARIQQDNEHKESTLRAYHKEELQRIQSQAENELRERLSSLRKDHEIQMKSLTKKHEENCQKLQDELELQKSKEEKQRALLQLQWKVMGETQQVDQEVNSKKEYSVSSIKRRDPYIRKEHQLQLVSPETKRKDVNLSGIIQSPITNMLRKVEKGTQDIPKHRKVTHHEYEVETANGRITKRRKTKSTVMFGEPNTQKSLHDTADKDPTKMKKVVAGSHPHPANIGELFSEGSLNPYAEDPYAFG
The following text describes a protein:
Function:
Component of the transcription coactivator SAGA complex. SAGA acts as a general cofactor required for essentially all RNA polymerase II transcription. At the promoters, SAGA is required for transcription pre-initiation complex (PIC) recruitment. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (via core/TAF module) and promoter selectivity, interaction with transcription activators (via Tra1/SPT module), and chromatin modification through histone acetylation (via HAT module) and deubiquitination (via DUB module). SAGA preferentially acetylates histones H3 (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac) and H2B and deubiquitinates histone H2B. SAGA interacts with DNA via upstream activating sequences (UASs). Within the DUB module, the correctly positioned zinc finger domains of sgf11 and sgf73 are both required to fully activate the ubiquitin hydrolase ubp8. Deubiquitination of H2B is required for the maintenance of steady-state H3 methylation levels. sgf11 is required to recruit ubp8 and sus1 into the SAGA complex.
Subcellular Localization:
Nucleus.
Domain:
The long N-terminal helix forms part of the 'assembly lobe' of the SAGA deubiquitination module; The C-terminal SGF11-type zinc-finger domain together with the C-terminal catalytic domain of UBP8 forms the 'catalytic lobe' of the SAGA deubiquitination module.
Sequence:
MQPASLAGISCTIFENLLKDYTHELTQTVHKNAKLSLQKCPACNKHCRQYCTKPGYDIYGNSVQTPSNVPYYSCLMCKREIAASRYAAHLEKCKGRSLSNATSYSTLFEDDNADEED
The following text describes a protein:
Function:
Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein.
Sequence:
MKGRWAERFAFLLLSAFLILASLLQASARGDECFGPVVELDADGQGPKFGVLGGFGSNLTEPLVSLKLVAANPADACGELAGALAGAAVIVVRGNCTFTEKAAAVQAAGGAAMLLYDSQVGGCVTMGFEPNATSSLTLAAVSIPHELGLQLLGLVAGGGSAGGAGEARVSLRRVSVPLVDSGAVLLWVLAVGTVIAGSVWGGLDHLTHRRTAEDQAPLIHAAHKPASAETVDLTPRAALAFVGLASCMLLLLYFVLNKAFFYVLLVLFCVASVQSQTVLYAAALAQLLPPARKNAHVQLPWLGATPLTVVATLPLAVAVAAVWAVWRNSAWAWVLQDLQGVALMLLVLRTLRVPSLKVACILLPACLAYDVFWVFIQPLLFGGGESVMVHVAQGGSSGEYIPMLLRVPHFGFGGLAGYSLLGFGDVILPGLLVAYTRRADLDLGLAVGASASAAASIQYFLKVSYFPYAVLSYGAGLCLTYAALAFSWFGDQGQPALLYLVPCTLGTVLALAAARGQLGLLWRGAHGPGGRLGAGDHDSDAGEEGARLAGAGLGGAGGGGVVGNGAGQVGPLAGLAAGVADEDGDVEAGGRGIGRAHRSSSAVSAAARARG
The following text describes a protein:
Function:
Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position.
Sequence:
MSLVLFHPEARYILGMTLQRTFEGIICDYTPYYCEENVWKLCERIQQSSKAVIQEFYAVFISNDNKTVALWKQQASDKENGLIVWVVKACLASFALIIYSIGYNNYKHTCDAIICHDYHVILIRKASNLVSVFDFDSQLQFPCTFYDYVTHGLRPDDELQKQFQRLFRVIPALDFLETFASDRSHMKTTKDSNTYLKAPPPYPPIFTKDCSMNLPQFIKMELTSVPGQILNYENFLHFFRSD
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated proteins and mediates their ubiquitination and subsequent degradation.
Subcellular Localization:
Cytoplasm, cytosol.
Domain:
The WWE domain mediates non-covalent poly(ADP-ribose)-binding.
Sequence:
MAEASRKSQLGGPHTKEATEKGDNLECAVCLQNCVHPAQLPCGHIFCFLCVKGIANQSKKCAMCRQEIPKDFIEQPNLLEKPYQREASEGFDGGYQWFYEGKNGWWRYDPRTNEDIEQAFQLNLPLVEILICGEIYVIDITNNWQYCKKTPTRKRRWWQYDERTSREIEAAYKRGEQTSELLIAGFLYIIDLENMLQLRRNEPGRRRKIKRDFATIPKKGIAGLRTPETLDSTEVEVSESSRGPVTPSNTPRSPTSGRESPGEDRELQETIDRITSLQLDTVLYDLH
The following text describes a protein:
Function:
Involved in the biosynthesis of p-aminobenzoate (PABA), a precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate (By similarity).
Sequence:
MIYVNGRYMEEKDAVLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEYTVSKHEILEMLDKLLKLNDIKDGNARVRLNISAGISDKGFVAQTYDKPTVLCFVNQLKPESLPLQKEGKVLSIRRNTPEGSFRLKSHHYLNNMYAKREIGNDPRVEGIFLTEDGAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKDIGLELKTGRYELEALLTADEAWMTNSVLEIIPFTKIEEVNYGSQSGEATSALQLLYKKEIKNMIHEKGGRAWRSTQ
The following text describes a protein:
Function:
Acts as a sulfur carrier required for molybdopterin biosynthesis. Component of the molybdopterin synthase complex that catalyzes the conversion of precursor Z into molybdopterin by mediating the incorporation of 2 sulfur atoms into precursor Z to generate a dithiolene group. In the complex, serves as sulfur donor by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. After interaction with MOCS2B, the sulfur is then transferred to precursor Z to form molybdopterin.
Subcellular Localization:
Cytoplasm.
Sequence:
MPADVLSELEAEKAARRQREAQRSAQVAAVIKAEVQSLGSKREVYRSLGSVRLPHARTNRTLRRRAHMRVKVLYFARAREATGSTEESAEIENGTTAKALLETLVRRFPKLQEIRSCLVLAINQEYADGSAVLKEGDEVALIPPISGG
The following text describes a protein:
Function:
Involved in cell size determination. May serve as a chaperone for expansins through the secretory pathway.
Miscellaneous:
MISCELLANEOUS: Unlike the tomato GP1, the BURP domain of AtPGL3 is not cleaved when the protein is secreted to the cell wall.
Subcellular Localization:
Secreted, extracellular space, apoplast. Secreted, cell wall.
Domain:
The BURP domain located at the C-terminus has not been identified in non-plant proteins. It is critical for PGL3's role in cell growth.
Sequence:
MLKQFLLLQSFSFFLFNVVIVGGRTFGGGFSAEENPFTPKASLVRYWNKEIRGQSPRSEFLISKASPLNAVDSATFSKLAAANSLPTRFPDFCSAANLFCFPDLGASLEKHDDDVKFSVYDQKNFTNYGNARAGGADSFKNYSKDGNVVTDSFRRYSRNAAGHDDKFTVYGENSNVVEEGFNSYGTFGTGGAGDFTNYQNNVNNPTSRFTAYSDGGNGRSQTFKTYTHEANAGNGQSFTSYGKNGNGVPNEFTSYGVSSNVIGSGFSNYGESGNAANDTFTSYGSDGNVPQNNFNNYGASGNAAVDTFANYRDKANVGDDSFSSYAKDSNSEKVNFVNYGQSFNPGSETFTGYGKGAEGSKLSFKTYTPNSTFKDYAKKGVAFAKYNVSTTTANTVGDGKTVNKWIEPGKFFRESSLKEGTVIPMPDIKDKMPKRSFLPRSIITKLPFSTSKLGEIKRIFHAVENSTMGGIITDAVTECERPPSVGETKRCVGSAEDMIDFATSVLGRSVVLRTTENVAGSKEKVVIGKVNGINGGKLTKAVSCHQSLYPYLLYYCHSVPKVRVYEADLLELNSKKKINHGIAICHMDTSSWGPSHGAFLALGSKPGRIEVCHWIFENDMNWAIAD
The following text describes a protein:
Function:
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
NENDLGEKWDKCLTDMAVKIGAGIGLGIVFSALAFKRRPWPIAFGVGAGFGMSYANCQHVFKYPEL
The following text describes a protein:
Function:
Involved in translation initiation. May be the homolog of mammalian eIF4B and be part of an RNA helicase. STM1/TIF3 is a non-essential gene.
Miscellaneous:
MISCELLANEOUS: Present with 24000 molecules/cell in log phase SD medium.
Sequence:
MAPPKKTVKKMDLTSFLNDDTFGSSWAEEDVDLNKITIPIETANANTIPLSELAHAKNNSNNTRSGGFGGSFGGRSRLDPALGGGSSDRREEYPVPDAPPYRAVINNIPWDITPEGVQAWVEDGLVKPEAVEEVVLPKNLRDPTRLKGNAFVTLKERADLVAVLKFNGTKLNERTVYVSVAAPRRGGGADVDWSSARGSNFQGDGREDAPDLDWGAARGSNFRGPRREREEVDIDWTAARGSNFQGSSRPPRREREEVDIDWSAARGSNFQGSSRPPRREREEPDIDWSAARGSNFQSSSRPPRREREEPDIDWSAARGSNFQSSSRPPRREREKEEPALDWGAARGAQFGKPQQTKNTYKDRSLTNKKTTDEQPKIQKSVYDVLRTEDDDEDEEAEKQNGDAKENKVDAAVEKLQDKTAQLTVEDGDNWEVVGKK
The following text describes a protein:
Function:
Has an organic peroxide-dependent peroxidase activity.
Sequence:
MSLPPPSPHRARSPVVPLLGIAAIAGGIAIAFAWTAGWIGGDRLTAARMTDTIESSGPPHPGFRRAHTKGVCVSGQFQSSGKATWVSSARIFSQASTPVLGRMSIGGGDPHGADGAARVRSMALQLRSDDGQEWRTAMNSFPFFVVATPAGFQALNVASKPDPATGKPDPAKLAAFGKQYPEAAKFQQWAKTAPWSDSWANTQYNGVNAFRAVAADGRERYIRWSMRPHTPFKGLSAEQRAQADGDFLATDLDARLAQGPLRWDMVLTVAEPGDPVDDPSQPWPASRRQIVAGTLSLDHAQPQASGPCRDLNYDPLILPKGIAASNDPILAARSSVYSQSFNRREREIASGKGGAATGQGAHP
The following text describes a protein:
Function:
In complex with rde-11, required in the endogenous and exogenous siRNA pathway for biogenesis and accumulation of secondary small interfering RNA (siRNA) intermediates, such as 22G-siRNAs derived from ergo-1 targets.
Sequence:
MSNHRSNFRDYQREGIRANNAGTSGDAVRQNGNPISVAKHVDGKKSVYMLFLRQIGQKKFLTEQGHRYNQNDQADKDIMTRYYHGMCPDLKQKFEREVAEHNGNRGLVIKTKHQRAQRNREMRHRNPDEFQQLRRAHLETLSQTPSVIALPRDINHVLHITEDLDAFCLANRKKAKRIMTSYIAQRSDDPGNPLLCEDYTMQIVSVFPVAYAFKPSINKLSSYPAEISVTTFNLKNGIIQNESRFVKFDAAWFYPDADDIGHEELSRKAMADELGISPNGPADGCEPYEVFEWLQHLLKQHPKSPILCDRAQFNFVYYGIKTLATYTGINAITFFQEVIIPSILSIQDFTSVILEKAPTDVPRVWRDVDICNQFQYHFLIPRTELNLFCSFHENKPSPTKYNCVKAHNARLLDNFFTVIKGNRLQGFVISPPVHEICIQDGSDTSLPQTILARTISRNDAEVYAARQRDTDEQYDVHQEGPSNHDQYEFASEPLDFEEDSDEENYNEQLDVPYSYNDHFISSSSVREPEHPSARSRDVAPNVQQESVVVPAPRRLSPQRAPRPSQNSPNAYSERKSFSAFPSEDPSEDYETPIISHIMNRNEADQYFNILDSVKPGQKYKIIKFDDF
The following text describes a protein:
Function:
Intrinsically disordered protein acting as a chaperone (By similarity). Ensures leghemoglobins (e.g. LB120-1) protection from denaturation under thermal and drought stresses to delay root nodule nitrogenase inactivation and subsequent nodule senescence, thus supporting symbiotic nitrogen fixation (SNF).
Subcellular Localization:
Cytoplasm.
Sequence:
MSQYQQGYGDQTRRVDEYGNPLTSQGQVDQYGNPISGGGMTGATGHGHGHHQQHHGVGVDQTTGFGSNTGTGTGYGTHTGSGGTHTGGVGGYGTTTEYGSTNTGSGYGNTDIGGTGYGTGTGTGTTGYGATGGGTGVGYGGTGHDNRGVMDKIKEKIPGTDQNASTYGTGTGYGTTGIGHQQHGGDNRGVMDKIKEKIPGTDQNQYTHGTGTGTGTGYGTTGYGASGVGHQQHGEKGVMDKIKEKIPGTEQNTYGTGTGTGHGTTGYGSTGTGHGTTGYGDEQHHGEKKGIMEKIKEKLPGTGSCTGHGQGH