lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Probably involved in acid resistance.
Sequence:
MKKKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQVNASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKNGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAALPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNSKLVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKVVIYPMADRSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEPSN
The following text describes a protein:
Function:
Probable transcriptional regulator that may help mitigate the effect of oxidative stress and help mycobacteria survive inside macrophages. Binds to its own promoter region.
Subcellular Localization:
Cytoplasm.
Domain:
Contains an N-terminal domain (NTD), which harbors a winged helix-turn-helix (wHTH) motif that is used for DNA binding, and a C-terminal dimerization domain (CTD).
Sequence:
MALPHAILVSLCEQASSGYELARRFDRSIGYFWTATHQQIYRTLRVMENNNWVRATTVLQHGRPDKKVYAISDSGRAELARWIAEPLSPTRPGRGSALTDSSTRDIAVKLRGAGYGDVAALYTQVTALRAERVKSLDTYRGIEKRTFADPSALDGAALHQYLVLRGGIRAEESAIDWLDEVAEALQEKR
The following text describes a protein:
Function:
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities. The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA. Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B. The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively. The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B. Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties. In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
METLDAIQLPYLGVVGASLIVILGIILLFPLGSDPFITINQHPRDLFQTKAKQQFEYNAAALLNEGLQTGHSAFRLVTNMVTYLILKDQYAEEIKNDSRFGAHEAVDPVLLVDLPGLESMFQGSLHNQVPPMAVRALNKELVHLTPSLSEEAMNCLQTRWTDSTEWHGVSIPETVLALIAQMTTRALLGPELCRNPEWLDIAKSFTTNRAIAVAAVQSWPSFLQPVIHWFLPPCRALRRQIQCARNIILPALERERRAYCSDQPTKREFSNLVFIDQYAKGARYDATMAQLRIIAVAFQTTSDLVEKVIARLCKHPELIEPLREEVVSVVGNRGLHRHSLRKLTLMESVMKETQRLEPAVIIGMFRLAKEKVTLKDGTVVPKGTNIAFANDLRFDPEMYLEPETFDGYRFQRMREDPAKIDLAPFTKTRMSHLAFGHGKHACPGRFLACDEAKLILCHILLNYDIRAVEGSPPELRARGMFVQLDPGAMMSVRRRRGTETAPHG
The following text describes a protein:
Function:
Catalyzes the hydrolytic deamination of adenosine. Plays an important role in purine metabolism and in adenosine homeostasis, and may thereby contribute to cellular signaling events (By similarity).
Sequence:
MIENNKEITLDIIKLLPKAELHRHLDGSIRISTLLELAKEQNVELPTYDQNELAKLIHKDENCSGLVNFLEAFQYTCSVLQHAYAITRVFYEMCEDAVADGVSYLEIRFSPVLHTSFGLSLSEVMEAVCDGMAIAELNLPIKARIIVCGLRHLDPSISKDLAEITWRYRHKGAIAFDLAGPEDGFSSKHHKEAFSIIRNKGINCTLHSGEDSNWTSVADSIHHCGAHRIGHGIAIQQNEELLNHVVNRRIPIECCITSNYQIKAISNASEHPIRKYFDSGAIVSICCDNCTMSNITLSGEYKLAIDTFNFKVEEVIRLIDYSFASSFIDPPLKINIRRESFKKALKIFQTNGYDISGVIENKFYYFEEIGLDVELEIQNNLANNFSLGKNVIRNYPQITLELLENLPKSDLHCRFDGGVSIEQIWNEVQLLGIDKCEKSKQEFLKKLSSKHLACYANFKDFKEFKSLIQSSSHTPQTIRLSKEIINLLLQTPEQINRAFDDIIKVALKDKVQYLELMIRPNSHSRNGLTKEQVLALIIENKDKWEKSSSIKIGLVVFSSSTSDDPIETLDSARLAIANRNSGVIGFGIFGADPISPTESRHFSQTFSLLKENNFNLVQFAGKSDVESLISTIHCSGSTRLSGAFQSHKIPRLMSYLGNYSIPVEISLTEKLKSFTSDDLSFTTPIRHLLDGKCPVVICSFRSSLYPYSRSKMYYKIVKNAKLDFKQVVRLLKNPFAYNFQSHQQRIELVQQFNKLSKEYLNSVNINYSNIII
The following text describes a protein:
Function:
Antitoxin component of a type II toxin-antitoxin (TA) system. Upon expression in E.coli but not in M.smegmatis neutralizes the effect of cognate toxin MazF7.
Sequence:
MSTSTTIRVSTQTRDRLAAQARERGISMSALLTELAAQAERQAIFRAEREASHAETTTQAVRDEDREWEGTVGDGLG
The following text describes a protein:
Function:
Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin. Catalyzes in vitro the N-acetylation of tryptamine to produce N-acetyltryptamine, 5-methoxytryptamine to produce melatonin and tyramine to produce N-acetyltyramine.
Subcellular Localization:
Cytoplasm. Plastid, chloroplast.
Sequence:
MQMQAARPRVGVRPRGGIRPFPLPTLSFNNNSNRSACACACAVSVSDSELAARGFAVRRSSTGLDVGALNEVFARVGFPRRQEERLRRALEHSEVVWLEDSASSSAGRPVAFARAAGDGVFNAVVWDVVVEPSCQGLGLGRAVMERLVADLRGKGVSNIALYAEPRVVGFYRLLGFAMDPDAIRGMAFYRSRQQIQNTSS
The following text describes a protein:
Function:
Catalytic subunit of a heterodimer with TRMT112/C04H5.1, which specifically methylates the 6th position of adenine in position 1717 of 18S rRNA.
Sequence:
MPDKKTLWMLNELEGFEKPKIKLEQYATSSELAVSMMEMIDETIGFEGKKLIDIGCGCGMLMTTAATMYELETVLGVDIDDEALKICSRNLETAEVQDRCELLQADILDPESDLPRGTFDVAVINPPFGTKNNAGIDMQFVQIGLQMVRPGGSVFSLHKSSTRDYILKNAKKWDGVGAECCAEMRWQLPATYKFHKQKAVDIAVDLIHFKKLDS
The following text describes a protein:
Function:
Dioxygenase that mediates demethylation of actin monomethylated at 'Lys-84' (K84me1), thereby acting as a regulator of actomyosin-processes (By similarity). Demethylation of actin K84me1 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration (By similarity). In addition to proteins, also demethylates DNA: specifically demethylates DNA methylated on the 6th position of adenine (N(6)-methyladenosine) DNA, thereby regulating Polycomb silencing.
Subcellular Localization:
Cytoplasm. Nucleus. Nucleus, nucleolus. Midbody. Note=Associates with the contractile ring and midbody.
Sequence:
MAAAAEVSLLQECGCKGIRTCLICERQRHRDPPWQICLQKKCCFLYCPDTGWAAGAEGSDLEGWAFPFPGVTLIQDFVTPEEEAEMVRLMDCDPWKLSQSGRKKQDYGPKVNFRKQKLKMAGFQGLPGFSQKVVQRMGLYPGLEDFQPVEQCNLDYSPERGSAIDPHLDDAWLWGERLVSLNLLSATVVSMSPEAPGSLLLCSAPSVRPDAFEDSLVAPSRSVPCQEVEVAITVPRRSLLVLTGAARHQWTHAIHRRHIKARRVCATFRELSSEFLPGGKQQELGQELLQAALSFQGRPV
The following text describes a protein:
Function:
Involved in the detoxification of the Fusarium mycotoxin deoxynivalenol by the transfer of glucose from UDP-D-glucose to the hydroxyl group at C-3, forming deoxynivalenol-3-O-beta-D-glucoside.
Sequence:
MADTASEHSSGGGGIHILLLPYPSQGHINPILQFGKRLAATHPGVRCTLAVTRFLLAETRGAASPGAVHLAEISDGFDRGGFTEAAGDVAAYLARLESAGSRTVGELLRAEAEAGEEHGRQPVRAVVYDAFLQPWAPAVGRRHGAACAAFFTQAPAVDLAYAHAQAGRMHVPVLGIGEETLELPGLPAGLKRADLPTFLTDPSDCPAYLDLLLKQFVGLDSVDHVLVNSFHELQPQESEYMAATWGARTVGPTVPSAYLDHRIPEDVSYGFHLHTPTTAATKAWLDARPPRSVAYVAFGSIAAPSAAQVAEVAEGLLNSGAPFLWVVRASETSKIPEGFADRASEIGMVVTWTAQLEVLSHGAVGCFVTHCGWNSTTEALGAGVPMVGVPQWSDQTTNAKYIQDVWRVGVRALPDGEGVVRKEEVERCVREVMGGEEYRRNAAQWKEKARMSMSEGGSSDRNIVEFLRDLGLGKSQQSTEAL
The following text describes a protein:
Function:
Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G by promoting their ubiquitination and degradation. Acts as a substrate recognition component of an E3 ubiquitin-protein ligase complex: mechanistically, Vif hijacks a host cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex) and the transcription coactivator CBFB/CBF-beta to form an active E3 ubiquitin-protein ligase complex that targets APOBEC3G and APOBEC3F for polyubiquitination, leading to their degradation by the proteasome. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Association with CBFB/CBF-beta also inhibits the transcription coactivator activity of CBFB/CBF-beta. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.
Miscellaneous:
MISCELLANEOUS: Vif-defective viruses show catastrophic failure in reverse transcription due to APOBEC-induced mutations that initiate a DNA base repair pathway and compromise the structural integrity of the ssDNA. In the absence of Vif, the virion is morphologically abnormal; MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M (for Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast majority of strains found worldwide belong to the group M. Group O seems to be endemic to and largely confined to Cameroon and neighboring countries in West Central Africa, where these viruses represent a small minority of HIV-1 strains. The group N is represented by a limited number of isolates from Cameroonian persons. The group M is further subdivided in 9 clades or subtypes (A to D, F to H, J and K); MISCELLANEOUS: Required for replication in 'nonpermissive' cells, including primary T-cells, macrophages and certain T-cell lines, but is dispensable for replication in 'permissive' cell lines, such as 293T cells. In nonpermissive cells, Vif-defective viruses can produce virions, but they fail to complete reverse transcription and cannot successfully infect new cells.
Subcellular Localization:
Host cytoplasm. Host cell membrane; Peripheral membrane protein; Cytoplasmic side. Virion. Note=In the cytoplasm, seems to colocalize with intermediate filament vimentin. A fraction is associated with the cytoplasmic side of cellular membranes, presumably via the interaction with Pr55Gag precursor. Incorporated in virions at a ratio of approximately 7 to 20 molecules per virion.
Domain:
The BC-like-box motif mediates the interaction with elongin BC complex; The HCCH motif (H-x(5)-C-x(18)-C-x(5)-H) mediates the interaction with CUL5.
Sequence:
MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLGDARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAIRKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKTKGHRGSHTMNGH
The following text describes a protein:
Function:
Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into several unidentified sesquiterpenes. TPS10 also converts geranylgeranyl diphosphate (GGPP) into the diterpene beta-araneosene.
Domain:
Contains several highly conserved motifs that are important for catalytic activity including the aspartate-rich 'DDxx(x)D/E' motif and the 'NDxxSxxxD/E' motif, both of which are involved in complexing metal ions to coordinate the binding of the isoprenyl diphosphate substrate in the active site.
Sequence:
MEAIKQKRSLISLKESFIYPHEWNHEPCDNKFILECFKESVNLGIFQIDDKKSFSYINSCLSSCAYMWPLCNHSQSLMTGRFIQWSFLIDDYLDSLEIDDKKTDSTVLNVEKALINGTITNKNSKLEEYTVFFRNKLFEYCGRERLDAFNLLINELVICLWTLVPFSKIHSKEKDFYPSYQLYRCIRTINVGIIACCALNFILFKDLDVKLWLNPRFRKILNRASIQISIVNDAVSYAKEILNENAYCNTFYFLQKDSTKFSTFDQVCEYLFNEANTYIKDIITDEPLLLHEFEDVEDRKVVQSLLNHVHYLISGNFVWSIENNQRYQSNIYFINLLQSTGKSIGSSWSNIKTFFR
The following text describes a protein:
Function:
Involved in the presentation of foreign antigens to the immune system.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MEFFVLSLLLLGTLILTETWAGFHSLKYFYTTMSLPELIEPRFTAVVYVDDQQILSFDSDSASQSMEPRTQWIKVEPPDYWERVTRISREDSQCNRMCLQKVSTNYNHSEGDPLSARVTRHTRSDLEVTLRCRAQDFYPAEISLTWLRDGEEEQLQDTEFIETRPAGDGTLQKWAAVEMLSGSEHRYTCQVQHEGLPEPLFLKWEPQFSSIELSAEVIIDLLLTAAIIAVVV
The following text describes a protein:
Function:
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton. Note=Septum.
Sequence:
MSSTVELASSFIEGAPPGEALTSDGSDIIPSLAPAFERYNEKQLTTVKLPGASQEVIVSEFNKIEGNRYFDVESQTSFGVDHVTQQASGAQSYVLESQNADLIHVEVHSRSNQCSKSLLKSLAKHAAEHYPNCSYGVYPTEDDTAVAILLVANRYSPNNFWNGRFRSIYRVPVSESTTVSGKILVDVHYYEDGNVALNTNKPINIAIPSISAESIISRIAAAERDYQEELNRAFVQMAEGAFKNLRRQLPITRQKVEWEKVGGYRLGQDISGGKGR
The following text describes a protein:
Function:
Implicated in a number of adherence functions. OPA proteins are implicated in pathogenesis and are subject to phase variation.
Subcellular Localization:
Cell outer membrane.
Sequence:
AGEGNGRGPYVQADLAYAYEHITHDYPKPTDPSKGKLSTVSDYFRNIRTHSIHPRVSVGYDFGGWRIAADYARYRKWNDSKYSVSIKNLQRRTSNGNRRDRKTENQENGSFHAVSSLGLSAVYDFKLNDKFKPYIGARVAYGHVRHSIDSTKKTTEFLTTAGARGTDPTVSSPYKNTQDAHQESNSIRRVGLGVIAGVGFDITPNLTLDAGYRYHNWGRLENTRFKTHEASLGVRYRF
The following text describes a protein:
Function:
Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes.
Sequence:
MPLYSVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKMELPCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQFAEKGEQGQYLQQDANECWIQMMRVLQQKLEAIEDDSVKETDSSSASAATPSKKKSLIDQFFGVEFETTMKCTESEEEEVTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVLKDVKFPLMLDMYELCTPELQEKMVSFRSKFKDLEDKKVNQQPNTSDKKSSPQKEVKYEPFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVKRKQDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYGPRRVEIMEEESEQ
The following text describes a protein:
Function:
Lipase that catalyzes the hydrolysis of arachidonic acid (AA)-esterified diacylglycerols (DAGs) to produce the principal endocannabinoid, 2-arachidonoylglycerol (2-AG) which can be further cleaved by downstream enzymes to release arachidonic acid (AA) for cyclooxygenase (COX)-mediated eicosanoid production. Preferentially hydrolyzes DAGs at the sn-1 position in a calcium-dependent manner and has negligible activity against other lipids including monoacylglycerols and phospholipids. Plays a key role in the regulation of 2-AG and AA pools utilized by COX1/2 to generate lipid mediators of macrophage and microglia inflammatory responses. Also functions as a polyunsaturated fatty acids-specific triacylglycerol lipase in macrophages. Plays an important role to support the metabolic and signaling demands of macrophages.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MPGMVVCGRRWGIASDDLVFPGAFELFIRIIWWTGTLVLYSVHKGRFDCKGGGTLHSYLIVLLVLLAAIILSLCALVYASMQGTIMNARPRRSVPALLCVRAVLCAPELVWACLGAVWVSDESLGCERAVVRAVTSAVVASWILLFFTGVAVLLVLDPLGGCRPARPDPGAERDLESSGSAQLLSGARSVAARVWESRLRLLSCCLPRDDSHHAAFSSIAQLLGDFFWDTDLVASDIAAGLSLLHQEQDKMEQYRDPEEVVAHSPPSLPQEDLQGELERAAHWMPFAMAAYGWPLFVYSNPATGLCKLSGDCCRSRSPEYDIVDADHLGCHFTSMLHTTGLQYRDFIYISFHNKIYEIPFFVALDHKKEAVLVAVRGTLSLRDVLTDLSADSESLPVDGVSGACYAHKGIMQAASYIHRKLINDGILNQAFTIAPEYQLVITGHSLGAGAAAVLAVLLRSSFPGLKCYAFSPPGGLLSKSLANYSKDFTVSVVVGKDLVPRLSIPNMEDLKRRILRMVSNCNKPKYQILLHACWYEVFGGDPDDSPTELENRRQEELSRPLLGEESLLLHRSSSYQSLASEDSPGHGSQPPLYLPGRILHVTEEGPARRACFSQVKYRAEWSSEMAFCSVFISPRMLTDHMPDVVLRALQSLTQDSAFSLCPTPHSDTNHLNVI
The following text describes a protein:
Function:
Carboxylate--CoA ligase that may use 4-coumarate as substrate. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester.
Domain:
Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity.
Sequence:
MAAPTSMANADGESTRTGYCAATKSFRSLRPPVPLPPPDVPLSFPEFAFSLLPRSSSSSSSSLLPANPALVDAATGEAVSFQAFLSRVRALAGALRSRVGLRGGDVAFVLAPAGLDVPVLYFALLSIGAVVSPANPALTPAEVSRLVSLSGASVAFAVSSTATKLPAGLTTVVLLDSPHFRSLLMDCGQAQGQEPLPVVVVRQSETAAIQYSSGTTGRVKAAALPHRSFIAMVAGFHALRAKAREVRTLLGAPMFHSMGFLFVLQGVALGATTVVVTDAVARAGIRGLVEAAERWAVMDMTASPPVVLGMTKQRCRLPALERITCGGAPLPAPAIERFRRRFPHVDLCMGYGSTEAGGISRMISQEECNHIGSAGRVTENVEVKIVDHVTGKPLPAGQQGELWVRGPAVMTGYVGDNEANATTFNSEGWLKTGDLCYIDQDGFLFVVDRLKELIKYKAYQVPPAELELVLHSLPQIVDAAVMPYPHEEAGQIPVALVVKQPGSKLTEAEVMYNVAKQVAPYKKIRKVLFVDSIPKSPSGKILRRELVNHLRLCELSRL
The following text describes a protein:
Function:
The complex LTO1:YAE1 may function as a target specific adapter that probably recruits apo-RPLI1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery. May be required for biogenesis of the large ribosomal subunit and initiation of translation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAPSSVDSASLCSDIPNSAPPSPSTALSSPARSSPPPQHPPPAESTGLDDIFGSSPPPTAGLSAEPPHTASSSHCEPSDLPSLRRQHVTAGYRDGISAAKHEHVQRGFDAGFPVGAQLGMRVGVVLGVLEGLVRCSPSASSSAPGKRSESGTTAAPSLDILQLYDLAKSELAVQKVFGGVAEIDSEVKPEQDSRLKLEKAGEEVVSKWEETVMRLLGNRS
The following text describes a protein:
Function:
Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome.
Subcellular Localization:
Nucleus, nucleolus. Nucleus, nucleoplasm.
Sequence:
MSSQDEQVAQVQVRFTTRDPDYAVADTPILIPTTLRRYGLSQIVNHLLEKETPTPFDFLVNGKILTTSLDEYIVQNGLSTESVLTLEYIPSTLPPSFLAAFPHEDWISGISLKDDSILTSSYDGIARVWNKSGKVCVTSASLDSSLKSVAWTTDSSFLTASLNQGISLWSYSSADVPMDDDESSAVVADYDCAFVGHENVVERIRTGSSTLFLSAGADKMMGVWDLERSPATGLPTQTVTGKRRKKNTEVLPKNGAKAPLLMCTGHNGPVTDMVFATDTSVAYSVSQDHTIKTWDLITGQLVNSRITRAPLLCIQNIGDLNLLACGSAGRHITLHDPRASAEQTTSITLNGHKNFVSGLACSPENPYMLASVSHDNTTKVWDIRATSGSLYTLSRNVQSKSTWDKLFAIDWNSSTGIVTGGTDKQLQINQSTKGDIASSE
The following text describes a protein:
Function:
Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization.
Miscellaneous:
MISCELLANEOUS: Present with 952 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, actin patch. Note=Cytoplasmic and cortical actin patches. Is associated with cortical actin patches in its dephosphorylated form and dissociates upon phosphorylation by PRK1.
Sequence:
MTVFLGIYRAVYAYEPQTPEELAIQEDDLLYLLQKSDIDDWWTVKKRVIGSDSEEPVGLVPSTYIEEAPVLKKVRAIYDYEQVQNADEELTFHENDVFDVFDDKDADWLLVKSTVSNEFGFIPGNYVEPENGSTSKQEQAPAAAEAPAATPAAAPASAAVLPTNFLPPPQHNDRARMMQSKEDQAPDEDEEGPPPAMPARPTATTETTDATAAAVRSRTRLSYSDNDNDDEEDDYYYNSNSNNVGNHEYNTEYHSWNVTEIEGRKKKKAKLSIGNNKINFIPQKGTPHEWSIDKLVSYDNEKKHMFLEFVDPYRSLELHTGNTTTCEEIMNIIGEYKGASRDPGLREVEMASKSKKRGIVQYDFMAESQDELTIKSGDKVYILDDKKSKDWWMCQLVDSGKSGLVPAQFIEPVRDKKHTESTASGIIKSIKKNFTKSPSRSRSRSRSKSNANASWKDDELQNDVVGSAAGKRSRKSSLSSHKKNSSATKDFPNPKKSRLWVDRSGTFKVDAEFIGCAKGKIHLHKANGVKIAVAADKLSNEDLAYVEKITGFSLEKFKANDGSSSRGTDSRDSERERRRRLKEQEEKERDRRLKERELYELKKARELLDEERSRLQEKELPPIKPPRPTSTTSVPNTTSVPPAESSNNNNSSNKYDWFEFFLNCGVDVSNCQRYTINFDREQLTEDMMPDINNSMLRTLGLREGDIVRVMKHLDKKFGRENIASIPTNATGNMFSQPDGSLNVATSPETSLPQQLLPQTTSPAQTAPSTSAETDDAWTVKPASKSESNLLSKKSEFTGSMQDLLDLQPLEPKKAAASTPEPNLKDLEPVKTGGTTVPAAPVSSAPVSSAPAPLDPFKTGGNNILPLSTGFVMMPMITGGDMLPMQRTGGFVVPQTTFGMQSQVTGGILPVQKTGNGLIPISNTGGAMMPQTTFGAAATVLPLQKTGGGLIPIATTGGAQFPQTSFNVQGQQQLPTGSILPVQKTANGLISANTGVSMPTVQRTGGTMIPQTSFGVSQQLTGGAMMTQPQNTGSAMMPQTSFNAVPQITGGAMMPQTSFNALPQVTGGAMMPLQRTGGALNTFNTGGAMIPQTSFSSQAQNTGGFRPQSQFGLTLQKTGGIAPLNQNQFTGGAMNTLSTGGVLQQQQPQTMNTFNTGGVMQELQMMTTFNTGGAMQQPQMMNTFNTDGIMQQPQMMNTFNTGGAMQQPQQQALQNQPTGFGFGNGPQQSRQANIFNATASNPFGF
The following text describes a protein:
Function:
Essential for vacuolar protein sorting. Required for vacuole biogenesis, stability and to maintain vacuole morphology.
Sequence:
MAPSNPLANWERLGDSFYRKVSLYDAIFDEDVDLDNYIVAGAPYGGAIALHRDESKPYMFRDAHTARSSIDIYSCSGKHINRINWEHGTIRGLGWSEKEELLVITEDGTVRRYFGLYGDFTSFSLGNGAEEYGVRACKFWNNGFVALLSNNQLIAVSNYDEPRPKLLAPCPEGEISSWSLIPPPYTLSRSVEVLLAVDKTIFLIDSSEAEDKVLQNGPFKHASVSPTGRFVALYTAEGQVWVVSSDFQSKHTEYDPQSRVTPRTVDWCGDDAVVIAWEDEIHLIGPNGTAAKYYYDGTVHVIPECDGVRLITNDNCEFLHKVADVTEAIFRLGSTSPASVLLDSVDLLEKKSPKADENIQRIRSSLPEAVDTCVKAAGHEFDVYWQKRLLKAASYGKSVLDLYNSDEFVEMTEKLRVLKAVRDYQIGLPLSYEQYLRLTPEKLIERLVNRHEYLLSIRISEYLQIPADRIYVHWASQKVKVSTVDDEAVCKLIVQKLEGKPGISFEQIAQAAYDEGRAHLATQLLNHEPRGGKQVPLLLKMEEDEVALDKAIESGDDDLIIYVLLHLKSKLPLASFFRMINTRPIASALVEANARGEDTELLKGLFYQDDRPIDGSNVLLSEALNATDLPHKTEKLLLASKLLSDSKDATAVQQHKLLSEASQLLKVQEALDKDIADRAEFVGLSLNDTIYRLIKTGDGKRAHKIQSDFRMPEKTYWWLRLRALVAKRDWGELEEMAKKKSPIGWEPFYNEVLGAGNTKLASLFIPKCTNLPVEERIEMWVKCGMIVKAAEEAHRAKDVNTLEVLRAKASGPAVAEIERMINLLRPRR
The following text describes a protein:
Function:
Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MMEEIKELIDYGIMGTLLFMSFVALAVGIERYLSIRSTKVENFKSKAQLEKELTKRLYIIATVASNAPYVGLLGTVLGILLTFYIIGEKGIVNTKEIMVGLALALKATALGLIVAIPSTILYNFLVRKVREKLLDWEAIHGECSSSHE
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:
MADKQEDTALLPVDDKIDLFDDTMSWEKLSVPESIMELLHASGFHMPTKTQVAAIKPILCDRKRSGLLEAPTGTGKTISFLTVAMSHITPDKSLPQAVIIAPTKILCRQIYGVAENLAKGSNIRVSLCFAKDELNEGELNPTAHIVIGTIHSLLNNFSGKIVVKGKTRIAERATFDCTAINTIIIDEADYFIENKHEISKFIEIAPKKTRRYLYSATMPSEVVDTMVKEWLDVDNPYFVERVNIYLGNSVQFSLCCTEADKTVALDKVINLEIYKKGAQSIIFCKTRKFVDECYRVMKNAGYSCSRYHSDMSKEAKMAEFEKFRKRETNCLITTDGLARGIDVATIRLVVNYNPPVKWVNNGDEVADPTLYTHRIGRGGRFGKATVSITLYEKDTEEVYMNKIIEHIDEKYATQKRTEHVITSLDSVDEIKEKVESIVRKVDDEISREIDEQNKKTEKRNEDGRAERRDDVEGLEL
The following text describes a protein:
Function:
May be involved in the transport of sterols.
Sequence:
PVYFNEPLSSLQKCFEDLEYSNLLDRAYEYGSRGNGLMRILYVAAFAVSGYASTDSRPCKPFNPLLGETYEADYPEKGIRFFSEKVSHHPMVMACHCEGKGWKFWGDSNLKSKFWGQSIQLDPSGVLTLQFDDGETFQWSKVTTTINNLIIGRVYCHHHGTMNISGNRQYSCKLTFKEQSFLDRNPRQVQGLVTDANGTKVAFLMGKWDESMSCIIGDDASKVNSRNANQSTGATLLWEKNVPPANPTRYNLSSFAITLNELTPGLKEKLPPTDSRLRPDQRHLENGEYEKANSEKLRLETRQRMARKMQESGWKPRWFQRDTEDGTFRYVGGYWEAREQRKWVGCNDIFGNNVSTLCTSASI
The following text describes a protein:
Function:
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Sequence:
MQRYFIYLAYDGTNYHGWQIQPNGSSVQECLMKALSTFLRRDVEVIGAGRTDAGVHASLMVAHFDHEDVLDTVTVADKLNRLLPPDISVYRVRQVKPDAHARFDATARTYKYYVTTAKYPFNRQYRYRVYGSLDYERMNEAARTLFEYIDFTSFSKLHTDVKTNICHISHAEWTKMEGEDTTWVFTIRADRFLRNMVRAIVGTLLEVGRGKLTVEGFRKVIEQQDRCKAGTSAPGNALFLVNVEYPEDIFSEETKKSVLSTLLPEGGEC
The following text describes a protein:
Function:
Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
Subcellular Localization:
Nucleus.
Sequence:
MEIDLMNEIACKCIHEWGAMVTADREILLNSRANARILIDERVNSGMTIDLKKGIESIVRQELEDEACLNVLLKWACLQRGDSLIEIFNGAEFVGWQGTFRRIAVSFMSMDSMGIIAVKMDGVIFLSETEKRYGEHDSRWDEEEPFYEGFSKFKMTQIMVRSELVNSSMNETIPLFVGSSVEALTKQKQSNTIHKAAKFWKKNGKDGAIFRNLNCLLRCDLTDLKWIIFGARDNDFILSKTKTRGRDEFEELINGVEKMYLRLFDILKGIKRFLNEVDVSSCVVEFPVDTEEGTVIQITEATASETNGLLTQQFKQRFNIE