lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Negatively regulates early sporulation-specific genes. Seems to exert its function by positively regulating the Ras/cAMP pathway. Required for growth under alkaline conditions. Acts synergetically with MDS3.
Miscellaneous:
MISCELLANEOUS: Present with 815 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MTVLQPPSSVCYPLNLPIVPNPNLDEATRKKLTLECRTGAAVELARSGVFVHGGLTLPLNLTIINSLQLQKELILYFGKQKDRNADFKTLADWISPEIFFLDLISRTWQRINTTIDTTSENELNNGLSFKERLFHSMCFTESNIYIFGGLMVSPHNGYELIATNELWKLDLKTKCWSLISENPQITRRFNHSMHVLNENNENQDTKLIIVGGLDNMDIPVKKIDIFNLRTSLWESESKSDENPASKGSSKILVNIDGMPISLSHDSNFSVLIENNQAEIPTLALYYPQREANTSRRGTDDGSFSTYAHDLDDKSKLPKHHHHHHGDLKYFESDDADENAVKTLMSPIVILPLLGNSQGARMTSNPTQNNKENSILQVPFHLQYPSGNYFNYNIVVIGFYPDPQPSNLHCFIYNIASGKWIRVNIACTECSISMHRFWKLLIWKSHHQALLLGTRTDDFCSPSVQKFDHILSFSLPMLNGYNKLVNTKHTRTNNGIANSHNLNVNLSLYDHLPYSNSSTIEHTNPYTVTQGYSLDDSGIPRLTSTATSQFENYSRYITVPLEMESTSSIFPPYAMVLGKDALEIFGKTLSDFEFITADGDSIGVPVYLLRKRWGRYFDSLLSNGYANTSFNYEFNGDTSNIISFSPHTASKTTKFGNSSQSSNGSLEKYFSKNGNSKSNSNTSLKKPHSVDFTSSTSSPKQRAISHNKLSPSEPILCADEEDSRSNTLKQHATGDTGLKETGTSNKRPISTTCSSTGMVFRVPFQDMKNSKLGLSEQSGRSTRASSVSPPPVYKKSTNDGNDSNCTLSNTPLVYRRASTVGTTTNSSVDDGFSSIRRASHPLQSYIIAKSSPSSISKASPAEKAFSRRKSSALRFIASPNQSRQTSFASTASTASVVSSTSGRRRNSNQISHLGSSASLPNSPILPVLNIPLPPQEKIPLEPLPPVPKAPSRRSSSLAEYVQFGRDSPVASRRSSHSTRKSSSSDARRISNSSLLRNTLDSQLLSNSYGSDIPYEASIQEYGMNNGRDEEEDGDNQDYGCISPSNIRPIFSTINAININGNFKEGEFFSSKSYINNEKSRRLSYISNPESVESTNSNNNAIIELEPLLTPRSLYMPWSTASVRAFAEFFYTAQINGKWLLAPVTLDLLIMAKIYEIPILYELITEVLYKIISKKEEGLSVTCEALLNLFQQKVSRYCNENEGKIRKQLDSSESYQDTLEIKRSLANIDNGYVDSYLLRNTSMAQSIHYTDDSNGETEIDMHHTGISSIGSLANRAVPTVFAGGPRDSHNSIGSIAFPSNSGVQNIRRSVSLFSPATKKKSSLSRETDPLDTSDQFTDDVPDSGPVSRQQNFPRRSSSFTETVPTEPTRYNYQNLDSSKSNRASDDKEEQNEQATLQDISNFDKYKVETLQKRNSNDGKDLDRTNDPLKNRGTEIPQNSSNLETDPFIRDSFDSDSGSSFRSDSDDLDSQLGILPFTKMNKKLQEQTSQEFDDSIDPLYKIGSSTPGSSRLHGSFSKYIRPNSQREDGSEYVNISSLENMVSPNALPPVDYVMKSIYRTSVLVNDSNLMTRTKEAIELSKVLKKLKKKVLQDISQMDDEMRETGKPIFARGSSSPTLSRQHSDVATPLKQQENTRPALKFASSSPISEGFRKSSIKFSQAPSTQISPRTSVTDFTASQQRRQHMNKRFSTQTTHSTSALFMNPAFMPSAVNTGRKESEGHCEDRSATANRTNRKEDATTNDNDNIAPFPFFGKRR
The following text describes a protein:
Function:
ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. Binds 90S pre-ribosomal particles and dissociates from pre-60S ribosomal particles after processing of 27SB pre-rRNA. Required for the normal formation of 18S rRNA through the processing of pre-rRNAs at sites A0, A1 and A2, and the normal formation of 25S and 5.8S rRNAs through the processing of pre-rRNAs at sites C1 and C2.
Subcellular Localization:
Nucleus, nucleolus.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MAIDGEKKKDPRAWDALTPSLAEWILDAIKSMGFEKMTPVQASTIPLFMGNKDVVVEAVTGSGKTLSFLIPVVEKLLRLEEPIKKHHVGAIIVSPTRELATQIHSVLTSLLAFHEPSAGALKPLEEGEKRKPSSTLRVVSQLLLGGTTTPAQDLSRFLKNSPNLLISTPGRLLELLSSPHVHCPQSSFEVLVLDEADRLLDLGFKDDLQKILSRLPKQRRTGLFSASVSEAVGEIVRVGLRNPVKIAVKVKGAGGDKMTPASLQMSYLLTPPTHKFPALLSLLSQLQPTPQKSIIYLSTCAAVDYFQPLLEAVLPKQFALVSLHGKHPPNVRQRNFSKYVAAVSPTILLTTDVAARGLDIPQVDLVVQIDPPSDPKVFLHRCGRAGRAGRKGLSVIFLQPGREEDYIPFLEIRKTPITLFKRPEISTTDDAAKILISKMRKEVLADRALYDKGQRAFVSWVQAYSKHQASSIFRVADLDWTDLGNAWALVRLPKMPELKKWEGDKTLGIKLDMSEYAYKDKVREKARRVAMEEAKNAGPYVPTEEQIARKKQREAWSQKHEKQDLKELKREKKKRKREIERLDKMTDEEKRVEQEKERELQALIEQVKRRKIEDDADEEFEGFAD
The following text describes a protein:
Function:
This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand.
Subcellular Localization:
Nucleus.
Sequence:
MLELPLVKGDPFHHVMEAILDLSDVAHVVCTTRGLNLLAVDTKHLAIVSLLFPAEDFKGYTCDEYISIGIPIRDLVNAIRCGDDKDTITLKVGEENFGTITLSFVSPEKNTVDYEFRLVDAKLERFRLPDRHFLRSKYQGSVKMPSVEFRRICKCLSNFGDEYGVISVTDEDLTYFAKGTDGDVYVEYKQQEEDTTIFKIDVREPVRLAFNPKYLNTFAKVFTLSGQVKLFLSKTHPLMVECKIGQKGRIRCFVAPKVEPEFQGEEEKKEAQKEEVINVGKMESDTDANKNKKRKRKLTDD
The following text describes a protein:
Function:
Subunit of the non-synaptic neuronal acetylcholine receptor (AChR), which may play a role in chemotaxis towards choline. After binding choline or acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Note=Enriched in the sensory endings of sensory neurons.
Sequence:
MLIIIQSLLLATTASLCIADTPVPTQIRLVHDLLDNYDKKAKPMWDNSKPINVSFSMDLYQILELNEPQQYILLNAWIIERWFDEFLYWNPDDYENITELRLPYDSIWLPDTTLYNSLVMKDDDTRRLLNSKLTTDTHRRAALIELLYPTIYKFSCLLDLRFFPFDVQVCTMTFSSWTYDQKGIDYFPYSDKIGTSNYLENEGWYILQTKIKRQEVKYACCPNNYTLLQLTLYLRRKPLFYLVNLIIPTSIITLIAIVGFFTTSSASGMREEKVSLGITTLLSMSILMLMVSDQMPTTSTFIPLIGWFILAMIIVISLGTVVSSVIIAIQKRGSLGERMSKRALKFAKVLAWFTCTSLPPHVEKEHMMEAFDAPTPLVEVRPLQLASVKESVRNKWVSGARRATQRGNSGLALISDKSTDPLIHLSPTAHQPDESISPSAPPVPSSSPLPPPLTPGPADDVVSVASELSSKFLTSRMRPKSQKDNTFAAMQSSIKANRQLAVAEFEWFATVVERTCFVIFVVAFLIITFGINFIGFIHWHQAGVEYGG
The following text describes a protein:
Function:
VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MQSSQWLQPLVLFVMTVILATALKRVDAATGVGIKKSTWEPLCQVSEELDGIAGHVLQEATEMIAATIDFDAAAKRARIFSLKNPMHKWTKAAITIATAYEAKAAAAVRQLKDTYIKQQVEAASRSAYVKGRVDDFLKLLEQTVDGSNNACLLADENADTPVTRSATTKLGQTECKLTQSSITATRRTPTHITTAGYINLVEGTGGDKHQPTAASKECHLTTAHTSKGFAKGEGTAAAVTVMAGYLTIPNSAAELTAATKANLITASEGGIAAWSHAHAAIKLLDRTLPTEYANESGDLTERAALKEAAQNLFGEAKDHQGSDGKKAIEAVFSNTKADTINTIITLIEKEDIPKGAAARPTPAKLGEIKNSIELTNLLSYYQQRLSQDFETLDKRLEESTKHQDPKATEKICGEAKDDEDKCKGLKDKGCSFNEQDKKCELKKDVKEKLEKSNQETEGNDGKRTNTTGSNSILIHKSPLLLVVLLLK
The following text describes a protein:
Function:
Catalyzes the conversion of UDP-glucose into UDP-glucuronate, one of the precursors of teichuronic acid.
Sequence:
MKICVVGAGYVGLTLSAALASIGHDMICTDKDVKKIGQLKKGVIPFYEPGLSDAILRCGNLSFSSEVKSSMEECPVIFIAVGTPPRSDGSADTKALQSVIGDLSEAIRSYKTIITKSTVPPGTNENIAKQLIASGVSKNLFNIVSNPEFLREGNALYDMLHPDKTVIGVQEEDHVSAAIVKSIYKHIDTPFIVTSLAGAELIKYANNFFLAAKISFINEMARICEAYQSDISDISRAIGLDPRIGKHFLQAGIGYGGSCFPKDLQALQFAAQEKNTETFLLRAVQHINDTQLGLYIKKIQSFFETLQGKKAAVLGISFKPNTDDIRNSQAVRLMERLAELGCDVHAYDPEAVLPEHLRQHVTQHSQAFDAIEESDFLFLATEWSEFLAFDWKKAADIMKGRLVIDGRNVLKKELIEACGLICTGVGRP
The following text describes a protein:
Function:
Has a role in meiosis.
Subcellular Localization:
Cytoplasm.
Sequence:
MTTPIVFCNPSNIEESLLYINKSLFSKGVIQAEKLRLSHDIRDNCNIVNIIYRLLRATDEERLEKESLLDAIKNNEYEKQRDNNTIKRLKNELELYQNECQLQLNKVRTLERDQAELITQNKGLKDVNAKNELTLKALKNQLSVSLRQHEQQMETLKGNYGLVKARKGRNLNSMLIVKEPIKQNTNAPILPETASFLQQNDENSNFLNSRVNNDEFQLLKGLNNELKKSNGTLLTCLSGTLNSLVEMLSPLYERPNSNPFEVCELNAILLDAKIQNQLLFIRNLLHERKYVSIDELDAILEENEKNKHLINILQKENKRVFEFLTNMHDKF
The following text describes a protein:
Function:
Component of the DASH complex that connects microtubules with kinetochores and couples microtubule depolymerisation to chromosome movement; it is involved in retrieving kinetochores to the spindle poles before their re-orientation on the spindle in early mitosis and allows microtubule depolymerization to pull chromosomes apart and resist detachment during anaphase. Kinetochores, consisting of a centromere-associated inner segment and a microtubule-contacting outer segment, play a crucial role in chromosome segregation by mediating the physical connection between centromeric DNA and microtubules. Kinetochores also serve as an input point for the spindle assembly checkpoint, which delays anaphase until all chromosomes have bioriented on the mitotic spindle.
Subcellular Localization:
Nucleus. Cytoplasm, cytoskeleton, spindle pole. Chromosome, centromere, kinetochore.
Sequence:
MNANGEANGGVDSAALDELIPQIFDQMRTNQLDGSGAAAWGTAAVSTATLLKEMEQLDQIIPVLQQLNESLRRSTGENLSRIRRTCEAVNRVLDTWIKIQSQAGYVGELMDDSEYLSYMEKTRGDEGQQQAYMESLRKQVEELRRKVDERRAVEAAAAAPRAPERTRGASGIPRGGSRITKRGGTTVRGRRMFR
The following text describes a protein:
Function:
Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays a critical role in the assembly of N-DRC and also stabilizes the assembly of multiple inner dynein arms and radial spokes. Coassembles with DRC1 to form a central scaffold needed for assembly of the N-DRC and its attachment to the outer doublet microtubules.
Subcellular Localization:
Cytoplasm, cytoskeleton, flagellum axoneme. Cytoplasm, cytoskeleton, flagellum basal body.
Sequence:
MDRKKKKVKRELTDEEKKAKAELKALKAAEQRKKRILTKRDNLLKSVSVEQNVSKTNMYKVHMQWRELMRAGKAEQLKASVGPMMEKFENDIKKADRTIVHLMNRLVEADDQYEFAHNNHMQTLNTLIDLHHTRVQIMENDYLKQLNRLETEFNTEREYIINMHTKNEKELLAMMKAMEEEFKETMNEHRQQFEAIREELKNKSTEEYNVAKIGLESQVEDLENQIQETHKAYLASTEAKTIQFKAMVKKDIITSRLVEQRMRKLIRLHESLAYWRARIALNTREWEAMNKALKEEKDRINKHYQDLKRSLNRMHNSEHAKLRAISKASGEVMADLTKKLELAQGILSLGKLNRKLETEYDQIFPCLLSEEGAEFPPRQKELVLRVSQLENPIPEHVREKERLERAHRFSSYALDEYGDEVTEKRYFDNLNRRFNKVMLEKMAINLERKRLKEVNYHLQKRLENYLEMSPMMKHKLKASNMMTDFS
The following text describes a protein:
Function:
Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur.
Sequence:
MREIEISRAIVEAYFNDLLQNLQLDIAIVGAGPSGMVAGYYLAKGGAKVAIFEKKLSVGGGIWGGAMGFNRVVVQESAREILDEFGVDYSQVGNGLYVLDSIELASTLASKAVKAGAKIFNMVEVEDLVVKDGRVSGLVINWTPVMMTGLHVDPLTVEAKFVVDSTGHGAQISQHLLKRGLIKAIPGEGPMWAEKGEELTVEHTREVFPGLYATGMAANALAGAPRMGPIFGGMLLSGRKAALEILQKLGK
The following text describes a protein:
Function:
Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
Domain:
Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin.
Sequence:
MMKCIEEKLKNSILILDGAMGTMIQQEDLTAEDFGGEEYEGCNEYLVETRPDVILKIHKAYIEAGADIIETNTFGATNIVLSDYDLSHLDEELNEEAALLAKQAVKESGKEVYVAGAMGPTTKAISVTGGVTFEELIEAYTRQARGLLKGAVDVVLVETSQDMRNVKAAYIGIQAAFEELKKTVPIMISGTIEPMGTTLAGQTIEAFYLSVEHMKPLSVGLNCATGPEFMRDHIRSLSDLSECYISCYPNAGLPDEDGHYHESPSSLAEKVKRFAEEGWVNIIGGCCGTTPEHIKAMKSALASLRPRDHHEREGHGISGLEALQYDESMRPLFVGERTNVIGSRKFKRLVAEGKFEEAAEVARAQVKKNAHIIDICMADPDRDEIEDMENFLAEVTKVLKVPIMIDSTDENVMERALTYIQGKAVINSINLEDGEERFKKVTPLLQKYGAAIVVGTIDEDGMAVSAERKIEIAKRSYELLTKKYGIRPSDIIFDALVFPVGTGDEEYIGSAAATIEGIRLIKEALPECLTILGVSNISFGLPPAGREVLNSVFLYHATKAGLDYAIVNTEKLERYASIPEEEKRLADALLFETTKETLEEFTNFYRVAKKKDVVVQETLTLDERLANYIVEGTKQGLHEDLSLALEEGRKPLDIINGPLMTGMDEVGRLFNNNELIVAEVLQSAESMKAAVSYLEPHMESSDSAKKGKVLLATVKGDVHDIGKNLVEIILANNGYEIINLGINVRSDRIVQEVQEKKPDIIGLSGLLVKSAQQMVTTAEDLKAANIDVPIVVGGAALTRKFTDNRISPSYKGLVCYASDAMTGLDIINKLQKEEEREKMKQDKKERHLHIVKKEEKKVEIPAVIEPLPKSEVMVPDSTKRIVLRDVPALHLAPFLNRQMLLGHHLGLKGNVKKLLKEGDKRAHELNDLIDELLQEGQSWLKPKAVYQFFPAQSDGQNIVIYDPEDHTRVIERFTFPRQGKAPYRTLGDYLRPIGDEMDYVAFLSVTVGEGVRDIAEELKAKGDYLRSHAIQSLALELAEGLAEKTHMLIRDRWGIPDSPELTMEERFRTKYRGIRVSFGYPACPELADQEKLFRLIHPEEIGISLTEGFMMEPEASVTAMVFSHPEARYFSVL
The following text describes a protein:
Function:
Has a role in transport between endoplasmic reticulum and Golgi.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MAQPGSFPNPNQRQRPTQFQSAPGFNAAPQFPMQPAVGQQRAPQRGPAHQFYQKAQNQTQTPVQDDGFFNSQAPPAFSQDFHQPGMNTVPAPQQQFQQTPAPQQQFQPTTAGFQHRHPTHGSNFGGYGQNPPQQTPPNSNPRPHMQHPQQQQDFINQFSSNPMAGLAMNSAQDFLQKQSEMYLPGAYGVWGSLKYYFTVNNSYVKSRLKILLLPFRHKNWRRMGNGEQDESKPMQYAPPTRDSNAPDLYIPLMGFLTYILIVGYSKGTSNQFSPDVITKDASYCLVMQLVEIGVLAACLYVLNSSISFLDLVSFSGYKYIPLVINTIVFQLLGSIAYYVSLLYTGVAASYFTLNCMKGTVAEPTPENRLFRNYLLFG
The following text describes a protein:
Function:
Involved in the asymmetric conversion of racemic 5-substituted hydantoins to the corresponding L-amino acids. HyuA and HyuB are both required for the conversion of D- and L-5-substituted hydantoins to corresponding N-carbamoyl-D- and N-carbamoyl-L-amino acids, respectively.
Sequence:
MSKIHTDLKKIDPITVQVVLGSLENVAVEMGHKLARMSYSSIIRESEDFGCALVDVRGQQLCESSHSTPLQSGPIPGYIKGIREIMEDRNDTFNQGDVIMHNSPYHGASHGPDVGFCIPVFYKDELIGFSVTTAHHLDIGSSTPGSCGIVDAVDAYAEGLQFKAIKVYDQGVKNRYVWDILKDNIRAPKLVVGDMEAQIAAARIGAQRYIEIIEKYGLDTVQAASEELMNYSEKMMRDAIKKLPDGEYTAEGFLDGYLDSDDPAKKDLRINVTVKVDGSDLTVDLTGTSPQVTDKPINMPLLGTVDIAIYLTLRSILLDSTVYGNFPQNSGLIRPIKIVAPKGTLCNPIFPAPTIARFNSGNAVADTLMKALAQVVPHQVSAGVGNLQVVAFSGQSNENYWVYMDIMEGSYGGRYGKDGMDAVDTLYANTRNNPIEDIESHYPLRVNRYELRDNDSAPGKWRGGIGSIREVSFLADGSFSVEADGHKYAPWGFDDGQDGYVGSLSIRDNETNELVQLPSKLPNRHAQSGSTIQLVGPCGGGYGNPLEREPEKVLSDYLDGFITKEKALVEYGVTITDSEEIDYEKTNELRKV
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. MED8 binds to the consensus sequence 5'-[AC][AG]GAAAT-3' in both the UAS of SUC2 and the DRS2 of HXK2.
Miscellaneous:
MISCELLANEOUS: Present with 937 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MSQSTASLVPEGNQGSLQEDVSFDFNGVPGQALDAVRMRLAQLTHSLRRIRDEMSKAELPQWYTLQSQLNVTLSQLVSVTSTLQHFQETLDSTVVYPLPKFPTTSHESLVTTLLRKKNIPEVDEWMKYVRETSGVTTALLKDEEIEKLLQQDREITNWARTTFRNEYGKHDFKNEESLSEEHASLLVRDSKPSKPFNVDDVLKFTFTGEKPIITGSTSTSSSN
The following text describes a protein:
Function:
Involved in calcium binding and microtubule stabilization.
Subcellular Localization:
Cytoplasm.
Sequence:
MLVYQDLLTGDELLSDSFPYKEIENGMLWEVEGKVRNKFLYFIIWVVQGAVDVNIGANPSAEGGDEDDGVDDQAVKVVDIVDTFRLQEQPAFDKKQFVTYMKRYIKLLTSKLELEKQELFKKHIEAATKFLLPKLKDLQFFVGESMHDDGSLVFAKHV
The following text describes a protein:
Function:
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.
Subcellular Localization:
Cytoplasm.
Sequence:
MTLDSRYGGEVYGGSKVVKRMEKYRPQNAPKNRQRKLLLPLSYGISSSTLLHILNLQLERQISSGLGRRAYDIHVLNIGTCEQSDSHRLGLFREAYPLHTYTQVPLHSIFKHDTTIKDVISEYGGPEFADDPSKTDQERLDIFRLSLSTATARADIDGILLTRLVVAIAKEQDCDGILWGDSDTRLASKALSNVAKGRGFSVPWDVCDGMSPWGIQFNFPMRDLFKFELSTYASLALPKSLNVVDSERPSVDNLSNKNMSIEDLLAHYVETQGQKYPGVMANIVRTINKLQPQSADTDHKCMLCGMPVDYSGEDPAIIGGQGSSQYTLQDWRERPVAGTLCYGCARTRLDLVPPRSVSS
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:
MVEDKSQVKVKFFTREQDESLHVLDAPLFAPVSLKRYGLSEIINHLLGLAEPVPFDFLIDGQLLRCSLQDYLTRKGLSSEAVLNVEYTRAVLPPSYLKSFSNEDWVSALDVGAERIVSGSYDGVVRTWNLSGKIEKQYSGHTGAVRAVKFISSTRLVSGGNDRTLRLWKTKNDDVKHVDELEGTEEAHTLAILEGHQAPVVSVDVQGDRILSASYDNSIGFWSTNHKDMTAVDPMDSLGDKASSAAKKRRKLTMKDGSVRRRAPLSLLESHKAPVEQVIFASNDSTVAYSVSQDHTIKTWDLVTSRCVDTKSTSYSLLSMVELPKLRLLACGSSARHITLHDPRADSSAKITQQQLLGHKNFVVALDTCPENEYMLCSASHDGTVKVWDIRSSSSIYTITREDQSVEKGINDKVFAVKWAKGVGIISGGQDKKIQFNKGDNIFKN
The following text describes a protein:
Function:
Plays a key role in the control of the eukaryotic cell cycle.
Sequence:
MGYLQYEKIGKIGEGTYGVVYKALVRATKEIVALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLLDVVHSEKRLYLVFEYLDLDLKKHMDSCPEFSKDTGVVKSFVYQMLRGIAYCHSRRVLHRDLKPQNLLIDPRTNVLKLADFGLGRAFGIPVRTFTHEVVTLWYRAPEILLGSRHYSTPVDVWSAGCIFAEMVNQQPLFPGDSEIDELFKIFRVVGTPNEDTWPGVTSLPDYKSTFPKWPPKDLATVVPNLDTAGFDLLGLDTGIEERDGDPHSQLYMITIPGGMQATVKVYQVMF
The following text describes a protein:
Function:
Catalyzes the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Key transducer of G protein-coupled receptor signaling: activated by G(q)/G(11) G alpha proteins downstream of G protein-coupled receptors activation. In neutrophils, participates in a phospholipase C-activating N-formyl peptide-activated GPCR (G protein-coupled receptor) signaling pathway by promoting RASGRP4 activation by DAG, to promote neutrophil functional responses.
Subcellular Localization:
Cytoplasm. Membrane. Nucleus.
Sequence:
MAGARPGVHSLQLEPVKVPETLIKGSKFIKWDEESSSKSLVTLRVDTMGFYLYWTCPNMEVDILDISVIRDTRTGKYAKIPKDTKMREILGFTGPEQRPEDKLVTVVYGNDIVNISFLNFMAVQEDTAKIWTEELFKLAHNILAQNSSRNTFLQKAYTKLKLQVNQDGRIPVKNILKMFAADKKRVETALESCGLNFNRGDSIKPEEFTLDIFERFLNKLCLRPDIDKILLELGAKGKPYLTLEQLMDFLNQKQRDPRLNEILFPPLKRDQVRQLIEKYEPNRQFLDRDQMSMEGFSRFLGGHENSIVPPEILDLSDDMNQPLSSYFINSSHNTYLTAGQLTGNSSVEMYRQVLLTGCRCIELDCWKGRPQDEEPFITHGFTMTTEIPFKEVIEAIAESAFKTSPFPVILSFENHVDSSKQQAKMAEYCRNIFGDALLIDPLEKYPLQPGVALPSPQELMGKILVKNKKRHKVAVKGPEGSVKRRVSEQTSNTYSDSSSVCESSATGLPPSESADVSLTLSNGDEKIEEKPPKYTEPRKSIDHDAYSEEEEEEEPSDPKKSDEGTASSEVNATEEMSTLVNYVEPVKFKSFDAAKKRNKYYEMSSFVETKALEQLTKSPMEFVEYNKKQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTLDLPMQLNVGIFEYNRRSGYLLKPEFMCRTDKHFDPFTENIVDGIVANTVKIKIISGQFLSEKRVGIFVEVDMFGLPVDTKRKFRTKTSQGNSFNPVWDEEPFILPKVVLPTLATLRIAVFEEGGKFVGHRILPVSAIRPGYHYICLRNELNQPVCLPALLVYTEVNDYIPDDHQGYANALTNPIKHISLMDQRAKQLAALMGENEQPFNKDKIDWDPISKPPIRSRDDTPEKIKIPIIPVPSPPAQRDDHIASVLTDIQAPTMEELKSQKSFEKLICRQYRELRQLRRKHLRKVSSLCKEQSTWVTPLQSLRRRKPFGRSHRGVSGADQDAEQKLMDMQRDQQKRLLELREIQHEQERKLKHSHLLQAVQKLQEVAISYHSTQLKKLKEINEKEKKELQKILDRKRHNSITEAKSRERQKKDVELTEINRRHINESVSSIRRLEEAQKRRQEKLQTAHQETLQRIKDEEPKLQAQLDEACQAEFCQLPQEVRRYLQEDGWVGSGSGPPSSSHSSPPSITRSWGSESGEKDSLHSPGDSSDEATRL
The following text describes a protein:
Function:
Repressor of the yfmOP operon. A mutation in yfmP leads to overexpression of yfmO, probably causing a decrease in cellular copper that is eventually responsible for a reduced copper induction of copZA.
Miscellaneous:
MISCELLANEOUS: Binds a DNA inverted repeat of the yfmPO operon.
Sequence:
MEWMKIDQVAKRSGLTKRTIRFYEEIGLIPAPKRTDGGVRLYSEDDMEELEKVISTKEVLGFSLQELQHFMETSRQLELNKEGYLLSLDPKERKEKLEEIQETLNHQLDLIDEKIRTFQSFKERLQGMKGKAERAIQSIE
The following text describes a protein:
Function:
Part of the bacABCDEF operon responsible for the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase. Catalyzes the reductive amination of the C2 ketone of tetrahydro-hydroxyphenylpyruvate (H4HPP), with L-Phe as an amino donor, to yield tetrahydrotyrosine (H4Tyr) diastereomer. D-Phe is not an effective amino donor. BacF associated to BacG converts 3E,7R- and 3Z,7R-ex-H2HPP to 2S,4R,7R- and 2S,4S,7R-H4Tyr, respectively. Given that bacilysin has the 2S,4S stereochemistry in its anticapsin moiety, it is likely that the 2S,4S-H4Tyr is the diastereomer used for the biosynthesis.
Subcellular Localization:
Cytoplasm.
Sequence:
MEITPSDVIKTLPRQEFSLVFQKVKEMEKTGAHIINLGQGNPDLPTPPHIVEALREASLNPSFHGYGPFRGYPFLKEAIAAFYKREYGVTINPETEVALFGGGKAGLYVLTQCLLNPGDIALVPNPGYPEYLSGITMARAELYEMPLYEENGYLPDFEKIDPAVLEKAKLMFLNYPNNPTGAVADAAFYAKAAAFAKEHNIHLIHDFAYGAFEFDQKPASFLEAEDAKTVGAELYSFSKTFNMAGWRMAFAVGNEKIIQAVNEFQDHVFVGMFGGLQQAASAALSGDPEHTESLKRIYKERIDFFTALCEKELGWKMEKPKGTFYVWAEIPNTFETSHQFSDYLLEHAHVVVTPGEIFGSNGKRHVRISMVSKQEDLREFVTRIQKLNLPFGSLQETSR
The following text describes a protein:
Function:
Rho GTPase-activating protein involved in the signal transduction pathway.
Subcellular Localization:
Cytoplasm.
Sequence:
MELCTTNIQCLGIKDSAHKKKIFNSSSNTKVLEFQVRYENPENDEDKPPSEPIIFQTTQSAINKLITEIYNVNLPLSNFSIGSSSALSDISLLCQCISSTPKIQKSLAFVNFIETENNLCKSSTFLYEFIKDSNISGVLTKTKNKNKRTKKERLCAIKYNRILYYFSNNDKKCKGLKFLDDCKVLGKSFNTFQLSFGSNETYLFTTPTTEECEKWVSTINSCIEHIQKSTFQVSGQVQGTLVRGRNLAIKDIGGLSDPFAIIKAERQQYKSHTIYKTLNPTYNENFHFDISKHNSYLYLFLWDEDKFKTDFMGEIIVPLSALPANQEVQLWLPLAPRNSKDKVSGDLLLKLRYFYAPDTLEVSPNAIYGNSLESLKNRPNVCKNSVPIILYQFIEFFEKHGLNEEGIFRICGNSIEIKSIKSQIDQNFESVIFNAPSVHAFAGAFKLFFRELPEPLFTFAQYDNFINLSKQKNFEIQAVIDIMKTFPQSHIATLKLILPFFKKISDNINTNLMGNYNLSIVFGPALLRPQVEDNTNLMEMIVVNEITKFIFDNSQQILKSL
The following text describes a protein:
Function:
Acyltransferase that catalyzes the formation of ester bonds between fatty alcohols and fatty acyl-CoAs to form wax monoesters. Shows a preference for medium chain acyl-CoAs from C12 to C16 in length and fatty alcohols shorter than C20, as the acyl donor and acceptor, respectively. Also possesses fatty acyl-CoA retinol acyltransferase (ARAT) activity that preferentially esterifies 11-cis-retinol, a chromophore precursor of bleached opsin pigments in cone cells. Shows higher catalytic efficiency toward 11-cis-retinol versus 9-cis-retinol, 13- cis-retinol and all-trans-retinol substrates.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MFWPTKKDLKTAMEVFALFQWALSALVIVTTVIIVNLYLVVFTSYWPVTVLMLTWLAFDWKTPERGGRRFTCVRKWRLWKHYSDYFPLKMVKTKDISPDRNYILVCHPHGLMAHSCFGHFATDTTGFSKTFPGITPYMLTLGAFFWVPFLRDYVMSTGSCSVSRSSMDFLLTQKGTGNMLVVVVGGLAECRYSTPGSTTLFLKKRQGFVRTALKHGVSLIPAYAFGETDLYDQHIFTPGGFVNRFQKWFQKMVHIYPCAFYGRGLTKNSWGLLPYSQPVTTVVGEPLPLPKIENPSEEIVAKYHTLYIDALRKLFDQHKTKFGISETQELVIV
The following text describes a protein:
Function:
Plays a role in the regulation of circadian rhythms. Transcriptional repressor which inhibits Clock-mediated transcriptional activation by binding to E boxes in the promoters of Clock target genes and repressing their transcription. E box binding activity is time-dependent with higher binding activity seen in the early morning (zeitgeber time 2) than early evening (zeitgeber time 14) and is dependent on the presence of the circadian protein per. It is likely that per binds to Clock-cycle heterodimers, reducing their affinity for E box binding and allowing cwo to bind instead. Negatively regulates its own expression.
Miscellaneous:
MISCELLANEOUS: The name 'clockwork orange' is based on the Anthony Burgess novel of the same name and derives from the potential clock function and the presence of an Orange domain.
Subcellular Localization:
Nucleus.
Sequence:
MEPYWNETNGHAAHPVKYESEAAVSSFPYCTESSLNFSTSATAYSEDDAEYATGRRNKTSRQDPLSHRIIEKRRRDRMNSCLADLSRLIPPQYQRKGRGRIEKTEIIEMAIRHLKHLQSECQQKESDYRSGYMDCMKEAAKFLYDVHMQDFCHRLLGRLQEHIDEMFKTDCYKSTRSCHMPDNVSASSGSPHQAYHPPLCHLRDMLATSASDVEHSQDHNDVKDLSFRNHLNQLQRSQQAAAAAAVAAAAVAVANGSSPASNAGVDSKVPLTNGGGTGGAPPAADNVPSNSTGSGSAAACAGGNSNSSGSNSSNAASSTICPPAGGSCPAKVTPLAAHQQPHQAPVITSTAPHHHHHHTDSSHHDFESSREPILHTDTSNMHSPPPRDLLLQQHPHLAHSHHTQDSLMSVRMRNYSESSHEIEHNNNYKYKNHIKERFVHELHDEETSSEHCPVAAHLQSDHSHLQALSEHSKDGTEPEIAPIMAKKRKLAEAAANGEIPLEVHTESSNAGASSANRLDKPSPSFNFSDIKDIKAELHNGNSNSSPLLAKLSAVAAAGGQLSTPSSTTAPLPPRHTFTVPIFALHGQGNYYVPLNVDYNALVPFLNGMDLLEKSYTSMPVVHPININVNFMPSSPSASLLAAAAAAAVAVGKQQQQQAVVAAGAGLPLSTNSAAAQAAAVAAAAVAKAKLEQAMNQSW