lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs). During G1 and S phase of the cell cycle, the complex functions downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and suppress DNA end resection. Mediates various NHEJ-dependent processes including immunoglobulin class-switch recombination, and fusion of unprotected telomeres.
Subcellular Localization:
Chromosome.
Sequence:
MSQGSQVHIFLGAPVAPLKTTVSQGTASLMSTANAWEKVRLFYKQHSLYLKAGDQEFKNLEDCQVPKGLGPPGLLSGDVLTTSVRRSAQVDEDFKHSASEAQSVKSQVNLSDMTSGQMCGLGDGVQHLPEEEKDQKLQCKNKKITDEQSKNQSDPCVRNFQRDLFALDLKCAAKLDLGCCTEQMSTGTKPEPTGHRERQSQESFSDTRCEPQSEGAVRKASDQRLSAEAEFLSVLTSSQRAFLAQGNDKGQDCINKSTVNMEAEPTGSQGVRRTEGDFSKPGGDFEEESENEQSQVYSLELFSPVCPESESSHSHINPGKNLENTSSQELFSNEENLPPNELCSSHPSTANRSWSCKDDSHHSKALSEVHQVSKKPRMDSNIREAAKAVPQRVMSELKDSKKISLIKNCDSKNQKYNCLVMVLTPCHVKEITIKSGPNSGSKVPLATIVVIDQSEIKKRVVLWRTAAFGALTVFLGDIILLTDVVLYEDQWIGETVLQSTFTSQLLNLGSYSYVQPEKYSNVIANVILQDLLTYVSTKHSYLKDLPQRQPQKMNTVEFVELEQLQPDILVHAVLRVVDVTVLTEALYSYRGQKQRKVVLTVEQAQGQHYVLVLWGPGAAWYTQLQRKKDSIWEFKYLFVQRNSILENLELHTTLWSSCECLFDDDTRAISFKTKFQKNTSSFVKISDLATHLEDKYSGVVLIKAKVSELVFSAAAAQKIALNARSTLQSIFSSLPSIVYAGCAHCGSELETDENRIYRQCLSCLPFVGKKIFYRPALMTIVDGRYNTCVHVGSKMMEQILLNISPDCLNRVIVPSSEVTYGMVASDLLHSLLAVSAEPCVLKIQSLFELDENSYPLQQDFSLLDFCPDSRKLWSPGLSLRAEGTGGIPGKE
The following text describes a protein:
Function:
Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Subcellular Localization:
Secreted.
Sequence:
MKVTAAFASLLLTAFAAPAPEPVLVSRSAGINYVQNYNGNLGDFTYDESTGTFSMYWEDGVSSDFVVGLGWTTGSSKSITYSAQYSASSSSSYLAVYGWVNSPQAEYYIVEDYGDYNPCSSATSLGTVYSDGSTYQVCTDTRRTRPSITGTSTFTQYFSVRESTRTSGTVTIANHFNFWAQHGFGNSNFNYQVMAVEAWNGVGSASVTISS
The following text describes a protein:
Function:
Catalyzes the covalent attachment of ubiquitin to other proteins. Essential for peroxisome biogenesis (By similarity). Required for UBC4-independent ubiquitination of PEX5.
Subcellular Localization:
Peroxisome.
Sequence:
MPNFWILENRRSYTSDTCMSRIVKEYKVILKTLASDDPIANPYRGIIESLNPIDETDLSKWEAIISGPSDTPYENHQFRILIEVPSSYPMNPPKISFMQNNILHCNVKSATGEICLNILKPEEWTPVWDLLHCVHAVWRLLREPVCDSPLDVDIGNIIRCGDMSAYQGIVKYFLAERERINNH
The following text describes a protein:
Function:
Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein; Plays a key role in defense against host by cleaving histatin-5 (Hst 5), a peptide from human saliva that carries out fungicidal activity. The cleavage rate decreases in an order of SAP2 > SAP9 > SAP3 > SAP7 > SAP4 > SAP1 > SAP8. The first cleavage occurs between residues 'Lys-17' and 'His-18' of Hst 5, giving DSHAKRHHGYKRKFHEK and HHSHRGY peptides. Simultaneously, the DSHAKRHHGYKRK peptide is also formed. Further fragmentation by SAP9 results in FHEK product.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor. Secreted, cell wall.
Sequence:
MRLNSVALLSLVATALAAKAPFKIDFEVRRGESKDDLSPEDDSNPRFVKRDGSLDMTLTNKQTFYMATLKIGSNEDENRVLVDTGSSDLWVMSHDLKCVSAPNSKRNERSFGHGTGVKLNERELMQKRKNLYQPSRTIETDEEKEASEKIHNKLFGFGSIYSTVYITEGPGAYSTFSPFVGTEGGSGGSGGSNTCTSYGSFNTENSDTFKKNNTNDFEIQYADDTSAIGIWGYDDVTISNVTVKDLSFAIANETSSDVGVLGIGLPGLEVTTQYGYTYQNLPLKLKADGIIAKSLYSLYLNTADAKAGSILFGAIDHAKYQGDLVTVKMMRTYSQISYPVRIQVPVSKIDVESSSGSTTNILSSTTGVVLDTGSTLSYVFSDTLQSLGKALNGQYSNSVGAYVVNCNLADSSRTVDIEFGGNKTIKVPISDLVLQASKSTCILGVMQQSSSSSYMLFGDNILRSAYIVYDLDDYEVSLAQVSYTNKESIEVIGASGITNSSGSGTTSSSGTSTSTSTRHSAGSIISKPVYGLLLSLLISCYVLV
The following text describes a protein:
Function:
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MTFRVAVIPGDGIGPELYEGSKRIIAKLIEKYNLDIDLIEVEAGDVALNKYGEALPRHTLDVIEKADMILKGPVGETAMDVVVKLRQMYDMYANIRPAKSLPNVQSKYPNVDLVIVRENTEDLYKGFEFVTSTGVTIAIKVTTEFASKRIVNVALNYALMRRRKVTCVHKANVMRVTDGLFASVCREILKGKVNFEEMYVDAAAANLVRDPTRFDVIVTSNVYGDILSDEASQIAGSLGLAPSANIGDRKSMFEPVHGAAFDIAGKGIANPTAFLLSVSMMLSRMYELSKENKYILASKSLENAIIETYKSGNKLTEDVGGSAKLKDMVDEIYKYM
The following text describes a protein:
Function:
Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MPKYNVSDFKSKFDKELTNHFNKNGYKQSFVFEDIRLLIAIACIIPAGLAFGIEYVYGFGVLKSYLKYLLPLYFLASCLLTFWSSVVKGSTVYVATKKERHIKISADTFLPLKNKPLITTKFTVLKNRNAVQLEWSVPVAHIFEEDGQISSATFEAEISKYLSQIEN
The following text describes a protein:
Function:
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular Localization:
Nucleus.
Sequence:
GSYRCRAGWASKDDPLLIFRNVTFKQKNKKTLENEILVGNDIINFDQVYNHSRSAFERNVVTQFDIQEQIFDYIFRHLQINSVDSDMPHPLVITEPLSNPNYSRERMSELLFEHYSVPSVQYGVDSLFGLYFNNTATNEFTSDHFIISCGYKTSHLIPIVRGRMMKCRRFNYGGNTIFHINSYSLLHLKYPGHIANITPSRAEHIVQNKCHFAIDFNEKLLKWTNDSYYNKHVIKYQLPFNQVYVVAQKISTEQLKQRHDEQIKRLMGMNLKRRQEKLISEQEKLSHYISLMDIIREEVEENGEYDNDAAILQDNNFSGMQELRAVISKLNNSIEALQDKIMTCTEQVGWLFIHLLFLNATGSMPPLSDTDGRRRWLDQLKADRQRVIDRMNERKNWRNEMMRRRTMASHRRISLISELAKNSKNTDDNFGINDEDWNIYKEINKDSRNSDSENDLDQLEEMEICLQEYDPEFRKIDPSESADLNEYYQIHVALEQIRIPELVYQPSMMGSEQAGLCEGIGHVLRQFNNEQQLRLVQDIFVIGGYASIPNFKSRLEKELLEIRPFESKFKVRMAANPVLDAWKGARLWSINSENLRRYSTNRKDYYEFGGDYLKTCCISNRTSNDFLKNQML
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC).
Subcellular Localization:
Nucleus, nuclear pore complex.
Sequence:
MTDVAREFGIAVSDSSTVFAFLTDKKGFSNKETVLVEKVSQNRQILATPNLRRLVIEMYSVFDKCQKGSSPDAPLDTPTCCTFSRAYRSVLYNAAVSHSSSDFMTDFALWSLYEKLWFGRGDSSICADLISWANQSFTFSRGAMESAVEYLHPGKTIPEEYWKGVAVSLLSCNFSDCVELLELHGGGSECDAFIEALTFFNPENLVDEALANTVNEWKDIMRENLTSGKYGSNENFKYLTKLLLGEERYLVSMASRIFDTWWHFLPFFVLVKNPFAGHVELIELADECRTLFVGEEEEEGAKENDVFWCLISKDDINFQQLIASNPWLAVHLVDLIHKSTLDPEFEVMRKMHMLDYASVLISHSPLWEIGAGYLIACGTEGLLRLETHIEGLHIEDDEMAEQLLEICEEHRLEDAKSCVTNTMTFRYLKQGHWSSTLAWALKTGSKKTIDWTVSRIVGSSSKDELAALRVLSSITNHSVLSLPSLTFLYSYQRFVKMMHCGDVLDCVQHLIPLIMMPDVPTQYYYDLFDYLITIIKEDGRAGIRFSKEILYELSTFLSTFTLDKHRDLNDNYMKKVKVLKKMVMLKLTDSIAKGIACS
The following text describes a protein:
Function:
Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.
Sequence:
MFTGIIEETGTIESMKKAGHAMALTIKCSKILEDVHLGDSIAVNGICLTVTDFTKNQFTVDVMPETVKATSLNDLTKGSKVNLERAMAANGRFGGHFVSGHVDGTAEITRIEEKSNAVYYDLKMDPSLTKTLVLKGSITVDGVSLTIFGLTEDTVTISLIPHTISETIFSEKTIGSKVNIECDMIGKYMYRFLHKANENKTQQTITKAFLSENGF
The following text describes a protein:
Function:
Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRNP70 binds to the loop I region of U1-snRNA.
Subcellular Localization:
Nucleus speckle. Nucleus, nucleoplasm.
Sequence:
MTQFLPPNLLALFAPRDPIPYLPPLEKLPHEKHHNQPYCGIAPYIREFEDPRDAPPPTRAETREERMERKRREKIERRQQEVETELKMWDPHNDSNAQGDAFKTLFVARVNYDTTESKLRREFEVYGPIKRIHMVYSKRSGKPRGYAFIEYEHERDMHSAYKHADGKKIDGRRVLVDVERGRTVKGWRPRRLGGGLGGTRRGGADVNIRHSGRDDTSRYDERDRDRERERERRERSRERDKERERRRSRSRERRRRSRSRDKEERRRSRERSKDKDRERKRRSSRSRERARRDRDRERKEEPRGGPGEGLEPPEPGDGPPDEMLGEPGPDGADGLEEKGRERERDRDRRRSHRGERERRRDRERDRDRDREHKRGERGGGERRGDEGRGGGGGQDNGLEGLGPDGGRDLYMEGEAGDGYLAPENGYLMEAAPE
The following text describes a protein:
Function:
Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moieties on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.
Miscellaneous:
MISCELLANEOUS: The influenza A genome consist of 8 RNA segments. Genetic variation of hemagglutinin and/or neuraminidase genes results in the emergence of new influenza strains. The mechanism of variation can be the result of point mutations or the result of genetic reassortment between segments of two different strains.
Subcellular Localization:
Virion membrane. Host apical cell membrane; Single-pass type II membrane protein. Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. In the virion, forms a mushroom-shaped spike on the surface of the membrane.
Domain:
Intact N-terminus is essential for virion morphogenesis. Possesses two apical sorting signals, one in the ectodomain, which is likely to be a glycan, and the other in the transmembrane domain. The transmembrane domain also plays a role in lipid raft association.
Sequence:
MNPNQKIITIGSVSLTIATVCFLMQIAILATTVTLHFKQNECNPPANNQVVPCEPIIIERNITEIVYLNNITIEKEVCPEVAEYRNWSKPQCQITGFAPFSKDNSVRLSAGGDIWVTREPYVSCDPGKCYQFALGQGTTLDNKHSNGTIHDRIPHRTLLMNELGVPFHLGTKQVCIAWSSSSCHDGKAWLHVCVTGDDRNATASFIYDGMLVDSIGSWSQNILRTQESECVCINGTCTVVMTDGSASGNADTRVLFIREGKIIHISPLSGSAQHIEECSCYPRYPDVRCVCRDNWKGSNRPVIDIKMADYSINSGYVCSGLVGDTPRSDDSSSNSNCRDPNNERGNPGVKGWAFDNGDDVWMGRTISKDSRSGYETFRVIGGWTTPNSKSQVNRQVIVDSNNWSGYSGIFSVEGKSCINRCFYVELIRGRPQETRVWWTSNSIVVFCGTSGTYGTGSWPDGANINFMPI
The following text describes a protein:
Function:
SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. Substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Inhibits EGF signaling by mediating the degradation of the Tyr-phosphorylated EGF receptor/EGFR (By similarity).
Domain:
The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes.
Sequence:
MAENSESNSKNVDVRPKTSRSRSADRKDGYVWSGKKLSWSKKSESCSDAETVSAIEKTEVPLRSQERKHSCSSIELDLDHSCGHRFLGRSLKQKLQDAVGQCFPIKNCSSRHSSGLPSKRKIHISELMLDKCPFPPRSDLAFRWHFIKRHTAPISPKSDEWVSTDLSQSELRDGQLKQRRNMEEVSCFSHTSVQPCVITSNNSSGRGGPGTDSIVNLASNNSIEDSDMDSDDEIITLCTSSRKRNKPKWEIDEEILQLETPPKYHTQIDYVHCLVPDLLQINNNPCYWGVMDKYAAEALLEGKPEGTFLLRDSAQEDYLFSVSFRRYSRSLHARIEQWNHNFSFDAHDPCVFHSPDITGLLEHYKDPSACMFFEPLLSTPLIRTFPFSLQHICRTVICNCTTYDGIDALPIPSSMKLYLKEYHYKSKVRVLRIDAPEQQC
The following text describes a protein:
Function:
Required for synthesis of the major beta-glucans of the yeast cell wall.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MYNVRGDLNRKTPSDGNVNEIGSMYASRDTSTSSFTNPTDSSTRLLYNNASNATFSSAALAAGVGGTRASGYTHRFSIRPSSQTYNRYPNGGNSAGSDMYSTSPQNNSIVDDIENINKLEAVAFAGPTAGESDFSLSREDKEIDDFLHYPLPAKDAKKLSYFVGGEGLMQLLFLLFLAAGTGMLFIGLPILTYTGHNSLASTRVTGITNHQFRILRLLRYGSLIDPDTPESAYTFDSQDLGTLDLVFSDEFNYPGRAFYDGDDQFWLATDLHYAATTDYEYYDADTPTTANGTLRLRMDAFYNHDLNFRSGMVTTWNKLCFKGGRIEVSASLGGSPYIPGFWPGIWTIGNLVRPGYLATSDGVWPYSYNSCDAGITPNQSDPSGISYLGGQRLNQCVCKGEDHPNVGTGRGGPEIDALEGTFGSGIPYNGSIYLETMPVVSQSAQYAPFDLYMYPNYDFVTIYNQSVSAMNGWAGGVYQQALSCASQLNNSWLSGNAYQKYGFDYKPGSGPDALISWFVGDEYTWTMRQPAVGQNGNIASRPVSEEPMIVVLNFGISPTWIYFYWYELTFPQTMYVDYVRIYQDSSDSSSVLGCDPEGFPTTEYIANHPKAYLNYNATSWSEAGYVRPKNSLMDGC
The following text describes a protein:
Function:
In cyliated cells, dynein axonemal particle-specific protein required for deployment of ODA to the axoneme. Interacts with outer dynein arm (ODA) subunits.
Subcellular Localization:
Dynein axonemal particle. Cytoplasm.
Sequence:
MASPDEDGRPSLPNPWDAILEAVKHQLPSLDSDSSASDCEDEELFIFQRNQTVLIPDLSEELADDPAGAWVTSSGSPPGLAAVPVESAMEPWGEWNAWPRPKESAPLEGRAPSKSSSLLRMSAETPPRQDDDAGGTLNTSASQSPRQGPQGEATRSPQEAGLQTEPLGAASQAQEGSDAASRKALRRERRKMIEKDILHKVTWDGRNPACPDASRGKEKACDAVEVPSEGPPGCLPVLSLQELEEWDLDQVLLSLTGREEDRGDGAPGAAWWAAGRLQGQDHTEPSTQDRLMERLSLLCARQSRETCRAQPGYGTARERVGSSSSSGHLGRRPLGLSCPPARVLSVRRLRPLEIRPGPALG
The following text describes a protein:
Function:
Participates in the epigenetic repression of flowering genes in association with CP2. Functions in the repression of several members of the MADS-box transcription factors family, including SEP3, during vegetative development via histone modification.
Subcellular Localization:
Nucleus, nucleoplasm.
Sequence:
MCNQTPLRSMALDSSGKQPEQQQQQQPRASSGNGEARLKLRRTPNEEHEPENYEDLPLDYSPSLFTSLERYLPEQLLNSTRIDKASFMRDLLLRYSPDTERVRVLRHKEYRDKIMSSYQRLHGEIYTLDPSSFFAPSFLGAFSRKSEPNFRSSMVESYPGIFTFEMFKPQFCEMLLAEVEHMEKWVYDSRSTIMRPNTMNNFGVVLDDFGFDSMLQKLVDDFISPIAQVLFPEVCGTSLDSHHGYIVEYGKDRDVDLGFHVDDSEVSLNVCLGKQFSGGELYFRGVRCDKHVNSDSTEKEVYDYSHVPGHAILHRGRHRHGARATTSGHRANLILWCRSSTFREMKNYQRDFSGWCGGCKLDKQRRQRDSINATKEILARKAAEKTLVELASKSCAE
The following text describes a protein:
Function:
Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids, phosphatidylserines (PS) and phosphatidylethanolamines (PE), from the outer to the inner leaflet of intracellular membranes. May contribute to the maintenance of membrane lipid asymmetry in endosome compartment.
Subcellular Localization:
Recycling endosome membrane; Multi-pass membrane protein. Early endosome. Endoplasmic reticulum. Golgi apparatus, trans-Golgi network. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not TMEM30B. In the presence of TMEM30A, mainly located in recycling endosomes.
Sequence:
MWRWIRQQLGFDPPHQSDTRTIYVANRFPQNGLYTPQKFIDNRIISSKYTVWNFVPKNLFEQFRRVANFYFLIIFLVQLMIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHNSDNEVNGAPVYVVRSGGLVKTRSKNIRVGDIVRIAKDEIFPADLVLLSSDRLDGSCHVTTASLDGETNLKTHVAVPETALLQTVANLDTLVAVIECQQPEADLYRFMGRMIITQQMEEIVRPLGPESLLLRGARLKNTKEIFGVAVYTGMETKMALNYKSKSQKRSAVEKSMNTFLIIYLVILISEAVISTILKYTWQAEEKWDEPWYNQKTEHQRNSSKILRFISDFLAFLVLYNFIIPISLYVTVEMQKFLGSFFIGWDLDLYHEESDQKAQVNTSDLNEELGQVEYVFTDKTGTLTENEMQFRECSINGMKYQEINGRLVPEGPTPDSSEGNLSYLSSLSHLNNLSHLTTSSSFRTSPENETELIKEHDLFFKAVSLCHTVQISNVQTDCTGDGPWQSNLAPSQLEYYASSPDEKALVEAAARIGIVFIGNSEETMEVKTLGKLERYKLLHILEFDSDRRRMSVIVQAPSGEKLLFAKGAESSILPKCIGGEIEKTRIHVDEFALKGLRTLCIAYRKFTSKEYEEIDKRIFEARTALQQREEKLAAVFQFIEKDLILLGATAVEDRLQDKVRETIEALRMAGIKVWVLTGDKHETAVSVSLSCGHFHRTMNILELINQKSDSECAEQLRQLARRITEDHVIQHGLVVDGTSLSLALREHEKLFMEVCRNCSAVLCCRMAPLQKAKVIRLIKISPEKPITLAVGDGANDVSMIQEAHVGIGIMGKEGRQAARNSDYAIARFKFLSKLLFVHGHFYYIRIATLVQYFFYKNVCFITPQFLYQFYCLFSQQTLYDSVYLTLYNICFTSLPILIYSLLEQHVDPHVLQNKPTLYRDISKNRLLSIKTFLYWTILGFSHAFIFFFGSYLLIGKDTSLLGNGQMFGNWTFGTLVFTVMVITVTVKMALETHFWTWINHLVTWGSIIFYFVFSLFYGGILWPFLGSQNMYFVFIQLLSSGSAWFAIILMVVTCLFLDIIKKVFDRHLHPTSTEKAQLTETNAGIKCLDSMCCFPEGEAACASVGRMLERVIGRCSPTHISRSWSASDPFYTNDRSILTLSTMDSSTC
The following text describes a protein:
Function:
RNA helicase.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MDSSANKCLTTQHFLELEPSLSKKTLDVLDTCGFHLCIPVQRATIPLLCSYKDVAVDAATGSGKTLAFIVPVIEILRRIYEPSKPHQVLGIIISPMRELSTEIYHVAEPFSSTLPNFKAALLVGGSNIKLDVENIEEEGANLLIGTPGTLFDIMERLDVLDFQNLEGQSGFGAVTNVSLNNAFWNIPFIDRLLDMGFQKQITSIMPRLPKLRRTCLFSATQTEAVEELSRAGLRNPVSINVRAEVKAHGELAPLANASFSKTPFGLHIEYLECEADEKPSQLVHFLYFMTCACVDYWGAVLRQLVTLKGCPLIPLHGRMKQTVREKALASFTALSNGIFLCTDVAARGLDIPGVDWIDQEDAYVEFLQKRRVALQERKNSNGPQDITPEIRATVKKDHDVMEKGLRAFVSHVRAYKEHICSYIFRLASLVNLMIHICSYIFRDKAREKQRKKNFSRKQ
The following text describes a protein:
Function:
Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate.
Sequence:
MAAGGDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLDNIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEILSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVVDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQEGGDNDLIERIQADAYFSPIHSQLDHLLDPSSFTGRASQQVQRFLEEEVYPLLKPYESVMKVKAELCL
The following text describes a protein:
Function:
Binds with low affinity to dsDNA and ssRNA, and with high affinity to dsRNA, with no detectable sequence specificity.
Subcellular Localization:
Nucleus, nucleolus. Cytoplasm. Note=Nuclear at steady state, primarily in the nucleolus. Shuttles between the nucleus and cytoplasm when associated with XPO5 (By similarity).
Domain:
The zinc-finger domains are required for binding to dsRNA, and also for nuclear localization.
Sequence:
MEYPAPAAVQAADGGGAGPYNSSELLEGQEPDGVRFDRERARRLWEAVSGAQPVGREEVEHMIQKNQCLFTNTQCKVCCALLISESQKLAHYQSKKHANKVKRYLAIHGMETLKGETKKLDSDQKSSRSKDKNQCCPICNMTFSSPVVAQSHYLGKTHAKNLKLKQQSTKVEALSKRLTNPFLVASTLALHQNREMIDPDKFCSLCHATFNDPVMAQQHYVGKKHRKQETKLKLMARYGRLADPAVTDFPAGKGYPCKTCKIVLNSIEQYQAHVSGFKHKNQSPKTVASSLGQIPMQRQPIQKDSTTLED
The following text describes a protein:
Function:
Mediates the binding and degradation of acetylated low density lipoprotein (Ac-LDL). Mediates heterophilic interactions, suggesting a function as adhesion protein. Plays a role in the regulation of neurite-like outgrowth.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MGLGLLLPLLLLWTRGTQGSELDPKGQHVCVASSPSAELQCCAGWRQKDQECTIPICEGPDACQKDEVCVKPGLCRCKPGFFGAHCSSRCPGQYWGPDCRESCPCHPHGQCEPATGACQCQADRWGARCEFPCACGPHGRCDPATGVCHCEPGWWSYTCRRPCQCNTAAARCEQATGACVCKPGWWGRRCSFRCNCHGSPCEQDSGRCACRPGWWGPECQQQCECVRGRCSAASGECTCPPGFRGARCELPCPAGSHGVQCAHSCGHCKHNEPCSPDTGSCESCEPGWNGTQCQQPCLPGTFGESCEQQCPHCRHGEACEPDTGHCQRCDPGWLGPRCEDPCPTGTFGEDCGSTCPTCVQGSCDTVTGDCVCSAGYWGPSCNASCPAGFHGNNCSVPCECPEGLCHPVSGSCQPGSGSRDTALIVGSLVPLLLLFLGLACCACCCWAPRSDLKDRPARDGATVSRMKLQVWGTLTSLGSTLPCRSLSSHKLPWVTVSHHDPEVPFNHSFIEPPSAGWASDDSFSSDPESGEADEVPAYCVPPQEGMVPVVQAGSSEASLAAGAFPPPEDASTPFAIPRTSSLARAKRPSVSFAEGTKFAPQSRRSSGELSSPLRKPKRLSRGAQSGPEGRDAEESAGPEEAEAPESFPAAASPGDSATGHRRPPLGGRTVAEHVEAIEGSVQESSGPVTTIYMLAGKPRGSEGPVRSVFRHFGSFQKGQAEAKVKRAIPKPPRQALNRKKGSPGLASGSVGQSPNSAPKAGLPGATGPMAVRPEEAVRGLGAGRESSRRAQEPISGCGSPEQDPQKQAEEERQEEPEYENVVPISRPPEP
The following text describes a protein:
Function:
Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the first dolichyl beta-D-mannosyl phosphate derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-dolichol to produce Man(6)GlcNAc(2)-PP-dolichol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MIENKVLPFIKNNQIKCFYTLASFLMIYELCINKIIIDYVKYTEIDWSTYVQQVEVFLKGIYDYTKIEGDTGPCVYPAGHLYVFSLLYNLTENGLNILKAQYIFAAIYILLTFIVFSIYGESIKESIKQITNKSNNNNNNNNNNNNNNNNVFLKIPFYIIIFLCLSKRIHSIFALRMFNDCISMLLFYISLYLIIKGRWNLGCLFFSCSVSVKMNVLLYSPALLFLLLSTFGIWRTIPKLMICGLVQVLLAIPFLMVNPQGYLLRAFEFSRQFLYKWTVNWRFLPEHLFLNKSWALFLLSIHLLFIILFFIKYIKKEQGGISNILKRGSINQNPKLLSVNYILLIMFTINLIGVTFSRSLHYQFYLWYFHTLPFLLWSTNYNLFLKIGFMCITEYAWNTYPSTSTSSLMLFISNFILLIQLYFQPTINSLREDKNNSSGLKKKKTK
The following text describes a protein:
Function:
Endonuclease that cleaves polypeptidyl-tRNAs downstream of the ribosome-associated quality control (RQC) pathway to release incompletely synthesized polypeptides for degradation. The RQC pathway disassembles aberrantly stalled translation complexes to recycle or degrade the constituent parts. VMS1 acts downstream disassembly of stalled ribosomes and specifically cleaves off the terminal 3'-CCA nucleotides universal to all tRNAs from polypeptidyl-tRNAs, releasing (1) ubiquitinated polypeptides from 60S ribosomal subunit for degradation by the ERAD pathway and (2) cleaved tRNAs for recycling. Component of an evolutionarily conserved system for ubiquitin-mediated mitochondria-associated protein degradation (MAD), which is necessary to maintain mitochondrial, cellular, and organismal viability.
Miscellaneous:
MISCELLANEOUS: Present with 3930 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Mitochondrion. Endoplasmic reticulum membrane; Peripheral membrane protein. Note=translocates from the cytosol to mitochondria upon mitochondrial stress.
Domain:
The VLRF1 domain mediates binding to the 60S ribosomal subunit.
Sequence:
MNSQKASKMTGSLKKNDLYIFDLSEQLLNSLKLMSFDSTLREVEVEKTSDNDRNKESGDLQIARKKVTSNVMRCSVCQMSFDSRNEQKAHYQTDYHLMNVKRNLRGLDILSVEEFDALISKEHGIKSEDENSGGEQTSSDHEESEEASDRDPDLQTNNYMETIIENDLQKLGFQKDESDAISHINTQSPYIYFKSKYLQKNEVLAIYKSLFNKRSLSNPNEALTFWNSQENPMAISALFMVGGGHFAGAIVSHQRLNVKGNAHKKDETLIEQAVNFLEHKTFHRYTTRRKQGGSQSAMDNAKGKANSAGSALRRYNESALKTDIQGVLKDWEPYLSKCDNIFIRARNVSDKKIFTDNTVLNKGDERIKSFPFTTNRPTVLELKKAWCELSYLKILPKPEPLAVKETVQKLEVSNKKDEFKEKQEPLLEEIQTEEIISLLKKGRAPLLISFLKKNKLDGNFRLKPESKYSLTPTMLHYASQQGMKQMALILLSNIKCDPTIKNRLGRTAWDLNRNDDVRHAFQIARYNLGESFTNWDETHIGQPLSREQVDEINEKKKAIENEKAEKLIKLELEAAKEKQRFAKDAERGPGKKLTNIPSIQQQNLNSLTDEQRRRLMREQRARAAEERMKKKY
The following text describes a protein:
Function:
Member of the two-component regulatory system BasS/BasR. BasR induces the transcription of the ugd, ais, arnBCADTEF and eptA-basRS loci, all involved in resistance to polymyxin. Represses the transcription of pmrD. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well.
Miscellaneous:
MISCELLANEOUS: The activity of the BasR protein is controlled at a post-transcriptional level by the PmrD protein, under low Mg(2+) concentration conditions.
Subcellular Localization:
Cytoplasm.
Sequence:
MKILIVEDDTLLLQGLILAAQTEGYACDGVSTARAAEHSLESGHYSLMVLDLGLPDEDGLHFLTRIRQKKYTLPVLILTAHDTLNDRITGLDVGADDYLVKPFALEELHARIRALLRRHNNQGESELTVGNLTLNIGRHQAWRDGQELTLTPKEYALLSRLMLKAGSPVHREILYNDIYNWDNEPSTNTLEVHIHNLRDKVGKSRIRTVRGFGYMLVATEES