lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
GRF is released by the hypothalamus and acts on the adenohypophyse to stimulate the secretion of growth hormone.
Subcellular Localization:
Secreted.
Sequence:
MLLWVFFLVTLTLSSGSLSSLPSQPLRMPRYADAIFTNSYRKVLGQLSARKLLQDIMSRQQGERNQEQGARVRLGRQVDSMWADQKQMALESILATLLQEHRNSQG
The following text describes a protein:
Function:
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Subcellular Localization:
Cytoplasm.
Sequence:
MNAYERITRNTAEVVTEEEVRELAEDPEGKRVYVGYEPSGVLHLGHLLTANKLMDLQDAGMEVVVLLADVHAYLNDKGSFEEIRATADQMKAQFLAYGLDEDQTEFVLGSSFQLDEDYELDLHAMQVETSLKRAQRAMAEIQSGETPKVSHVVYPLMQALDIEYLDLDLAIGGMDQRKVHMLAREELPSVGYEKRPVLHTPIIGDLGSGDGKMSSSEGVTISMEDSTADIEEKVTGAFCPQTRDPEGETVNPVLELFQYHVFPRFDEVVVQRPDEYGGDLVYESYEDLADDLESGELHPADAKGALAAALDELIEPGRQRLREIRGE
The following text describes a protein:
Function:
This is one of the chains of the nonenzymatic component (CF(0) subunit) of the mitochondrial ATPase complex.
Subcellular Localization:
Mitochondrion membrane; Single-pass membrane protein.
Sequence:
MRLSSTQARKMLFAAIPSICALSSKKISIYNEEMIVARCFIGFIIFSRKSLGKTFKVTLDGRIQAIQEESQQFPNPNEVVPPESNEQQRLLRISLRICGTVVESLPMARCAPKCEKTVQALLCRNLNVKSATLPNATSSRRIRLQDDLGTKFHLLVRRRFCPQCISKAEKIELIRESLVVLRMVRVGGSLKNK
The following text describes a protein:
Function:
Component of the SMC5-SMC6 complex, that promotes sister chromatid alignment after DNA damage and facilitates double-stranded DNA breaks (DSBs) repair via homologous recombination between sister chromatids.
Subcellular Localization:
Nucleus.
Sequence:
MSDDAVNPKRRRLTSPDKGGAERGASGKEFQILQGYRNFEDDVAHDRATVARTGDISVAVQRLEEVNMLFKQAGDLNLSVNSLFAQDSHAVMSVSELASLSIRNLKLTNAGKLLSPEEFVNGAKRFLLEDYLELNHVSVPGSMYPETDDASNTQNDSIENDGDATSDALDESTNQHADAALRQSMQRNSYLRQFEAYGDFAQFNWFKMGALFQQLGGAPTLVDHMLGPLAVQKKTRVATQRRAVENVGAKTTAEAVTRETLNSNQSETTPEQVKKCFQVLIQKNGYNSISLFRFIIDPSSYARSIENLFYTSFLIKEGRLVLEDDDEGFPAIRPKEPLPQDPAEKELERQRRNDARQKHIIFQMDMATWRKLIDKFHITESFLP
The following text describes a protein:
Function:
Key component of the Ragulator complex, a multiprotein complex involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator plays a dual role for the small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD): it (1) acts as a guanine nucleotide exchange factor (GEF), activating the small GTPases Rag and (2) mediates recruitment of Rag GTPases to the lysosome membrane. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. LAMTOR1 is directly responsible for anchoring the Ragulator complex to the lysosomal membrane. LAMTOR1 wraps around the other subunits of the Ragulator complex to hold them in place and interacts with the Rag GTPases, thereby playing a key role in the recruitment of the mTORC1 complex to lysosomes (By similarity). Also involved in the control of embryonic stem cells differentiation via non-canonical RagC/RRAGC and RagD/RRAGD activation: together with FLCN, it is necessary to recruit and activate RagC/RRAGC and RagD/RRAGD at the lysosomes, and to induce exit of embryonic stem cells from pluripotency via non-canonical, mTOR-independent TFE3 inactivation. Also required for late endosomes/lysosomes biogenesis it may regulate both the recycling of receptors through endosomes and the MAPK signaling pathway through recruitment of some of its components to late endosomes (By similarity). May be involved in cholesterol homeostasis regulating LDL uptake and cholesterol release from late endosomes/lysosomes (By similarity). May also play a role in RHOA activation (By similarity).
Subcellular Localization:
Lysosome membrane; Lipid-anchor; Cytoplasmic side. Late endosome membrane; Lipid-anchor; Cytoplasmic side. Note=Recruited to lysosome and endosome membranes through N-terminal myristoylation and palmitoylation.
Sequence:
MGCCYSSENEDSDQDREERKLLLDPSSTPTKALNGAEPNYHSLPSARTDEQALLSSILAKTASNIIDVSAADSQGMEQHEYMDRARQYSTRLAVLSSSLTHWKKLPPLPSLTSQPHQVLASEPIPFSDLQQVSRIAAYAYSALSQIRVDAKEELVVQFGIP
The following text describes a protein:
Function:
Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MVYHSSFVDEEGISKACGCPLLPLKSHIRGPAPVSEQDTTDIVDEAITFFRANVFFKNFDIKSSSDKLLIYLTLYINIALKRLEGCRTLAEGTKAIINLGLENVPVPGEAGFPFPSLFSPAQSKKEAELFRNYLKQIREETSGRLLSVAYRPNGTPNKWWSAFSKRKFMNMVLP
The following text describes a protein:
Function:
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
Sequence:
MMLEHVLVLSAYLFSIGIYGLITSRNMVRALMCLELILNAVNLNFVTFSDFFDSRQLKGDIFSIFVIAIAAAEAAIGPAIVSSIFRNRKSTRINQSNLLNK
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. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MSGGPAVRISIESSCEKQVQEVALDGTETYVPPLSMSQNLAKLAQRIDFSQGSDSEEDGAEGESRDREWSKQEPEEEEGAVKFQPSLWPWDSVRNNLRSALTEMCVLHDVLSVVKEKKYMALDPVSHDPSAVKTPQVFQLISKKKSLGTAAQILLKGAERLSKSVAENQENRRQRDFNSELLRLRSQWKLRKVGDKILGDLSYRSAGSLFPHHGTFEVIKNTDIHLDKKIPEDYCPLDVQIPSDLEGSAYIKVSIQKQAPDIGDLGTVNLFRRLQKNKSGTQPWHVKLEAAQNVLLCKEIFAQLSREAVQIKSQIPHIVVKNQIISQPFPGLQLSISLCHSTGDKKNSRSSPEKPKPDDHLYVLEHNLHQMMREFHKQQLSSVVMPHPATAPFGHKRMRLAGPLAYDKAEISSLQHNEGLLEKIIRQAKHIFLRSRTARTIDSLASRIEDPQIQAHWSNINDVYESSVKVLITSQGYEQICKSIQLQLNIGVKQIRVVHRDGRVITLSHQEQELQDFLLSQMSQHQVHAVQQLAKVMGWHVLSFSNHVGLGPVESIGNASAITVASPNGEFAISVRNGPESGCKVLVQFPRSQSKELPKSDVIQDSKWSHLRGPHKEVHWSKMEGRNFVYKMELLMAALTPCP
The following text describes a protein:
Function:
Binds directly to 16S ribosomal RNA.
Sequence:
MANIKSALKRIEIAERNRLQNKSYKSAIKTLMKKTFQSVEAYASDPNPEKLDTINTSMAAAFSKIDKAVKCKVIHKNNAARKKARLAKALQSALPAA
The following text describes a protein:
Function:
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Sequence:
MLRLITQLSEAQTEIKRIAARTHSEQVQHQEATVREILQNVRRQGDEALLRYTLEFDQVRLAPGDLVVGAAELDAAYQRVSTSLLKAIRLAKQRIEQFHRERICKSWVQFQDRGIVLGRRYTPVDAAGLYIPGGRASYPSSVLMSAIPAVVAGVPRIVLVTPPNPEGKINPAVLVAAQESGVHEIYRIGGAQAIGALTYGTRTIAPVSVIAGPGNIYVTLAKKLVYGEVGIDSLAGPSEVLIIADSTANPVFLAADMLAQAEHDSLASAILITPDGRLAERTIEAVDRQLENHPRRTLTEKSLANYGLVIVTADLAEAAALSNLFAPEHLELEVEDPWELLEKVRHAGAIFLGHATPEAVGDYLAGPSHILPTSGTARYASGVGVETFQKCSSLVQYTPQALAEVGEAIDALTAAEGLPSHGDSVRLRLQQYENPHSPTQQQQEE
The following text describes a protein:
Function:
Glycoprotein that plays an essential role in maintaining a well-balanced immune response by modulating complement activation. Acts as a soluble inhibitor of complement, where its binding to self markers such as glycan structures prevents complement activation and amplification on cell surfaces. Accelerates the decay of the complement alternative pathway (AP) C3 convertase C3bBb, thus preventing local formation of more C3b, the central player of the complement amplification loop. As a cofactor of the serine protease factor I, CFH also regulates proteolytic degradation of already-deposited C3b. In addition, mediates several cellular responses through interaction with specific receptors. For example, interacts with CR3/ITGAM receptor and thereby mediates the adhesion of human neutrophils to different pathogens. In turn, these pathogens are phagocytosed and destroyed.
Subcellular Localization:
Secreted.
Sequence:
MRLSARIIWLILWTVCVAEDCKGPPPRENSEILSGSWSEQLYSEGTQATYKCRPGYRTLGTIVKVCKNGEWVPSNPSRICRKRPCGHPGDTPFGSFRLAVGSEFEFGAKVVYTCDEGYQLLGEIDYRECDADGWTNDIPICEVVKCLPVTELENGRIVSGAAEPDQEYYFGQVVRFECNSGFKIEGQKEMHCSENGLWSNEKPQCVEISCLPPRVENGDGIYLKPVYKENERFQYKCKQGFVYKERGDAVCTGSGWNPQPSCEEMTCLTPYIPNGIYTPHRIKHRIDDEIRYECKNGFYPATRSPVSKCTITGWIPAPRCSLKPCDFPQFKHGRLYYEESRRPYFPVPIGKEYSYYCDNGFTTPSQSYWDYLRCTVNGWEPEVPCLRQCIFHYVEYGESLYWQRRYIEGQSAKVQCHSGYSLPNGQDTILCTENGWSPPPKCVRIKTDCDNLPTFEIAKPTEKKKKSYRSGEQVTFRCPPPYRMDGSDIVTCVNTKWIGQPVCKDNSCVNPPHVPNATILTRHKTKYPSGDKVRYDCNKPFELFGEVEVMCQNGIWTEPPKCKDSTGKCGPPPPIDNGDITSLSLPVYAPLSSVEYQCQNYYLLKGNKIVTCRNGKWSQPPTCLHACVIPEDIMEKHNIVLRWRENAKIYSQSGENIEFMCKPGYRKFRGSPPFRTKCIEGHINYPTCV
The following text describes a protein:
Function:
Plays an olfactory role that is not restricted to pheromone sensitivity.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MIHWSLIVSALGVCVAVLGGYCGWILFPNMVHKKVEQSVVIQDGSEQFKRFVNLPQPLNFKVYIFNVTNSDRIQQGAIPIVEEIGPYVYKQFRQKKVKHFSRDGSKISYVQNVHFDFDAVASAPYTQDDRIVALNMHMNAFLQVFEREITDIFQGFANRLNSRLNQTPGVRVLKRLMERIRGKRKSVLQISENDPGLALLLVHLNANLKAVFNDPRSMFVSTSVREYLFDGVRFCINPQGIAKAICNQIKESGSKTIREKSDGSLAFSFFGHKNGSGHEVYEVHTGKGDPMRVLEIQKLDDSHNLQVWLNASSEGETSVCNQINGTDASAYPPFRQRGDSMYIFSADICRSVQLFYQTDIQYQGIPGYRYSIGENFINDIGPEHDNECFCVDKLANVIKRKNGCLYAGALDLTTCLDAPVILTLPHMLGASNEYRKMIRGLKPDAKKHQTFVDVQSLTGTPLQGGKRVQFNMFLKSINRIGITENLPTVLMPAIWVEEGIQLNGEMVAFFKKKLINTLKTLNIVHWATLCGGIGVAVACLIYYIYQRGRVVEPPVK
The following text describes a protein:
Function:
Structural component of the gap junctions.
Subcellular Localization:
Cell junction, gap junction. Cell membrane; Multi-pass membrane protein.
Sequence:
MATLFNTIVSTVPFIQSKFQRRTRSDFKINNSQADRLNTRFTVMLLAVTSALLGSAHVWGQPITCWTPAQFQPHWSVFVDQGGESRYCYTHGTYFVPFEDDLTQDSSVRHQYRINYYQWVPYILGVQALLFCIPHLLRKFIKSYLEYDVPGVIEHVEGFWASIKVVPELPMQITAFENGPAIFVWEGLRLSRRHRCLNLARCHALATLVQAVIAWMLASVLHFLWLDYVFGGPLVILDVIVGKDWLVTGHFPRTVHCDFQRRALASSQLETVLCMLHLNIYYEKVLLFLWLWVQVLDALCCHYLYGVDLHQTGIGFKGANISFFTTNSEIIQGRAKVFKLLEFAAEGESTPSTDRFIRVLGSDGLFVLQQIALNLGNLPASYLAAAMRNCCKRYENEDKMEPKLLEV
The following text describes a protein:
Function:
RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient 3'-end histone mRNA exonuclease activity and degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Required for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs (By similarity). Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA (By similarity). Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs. In vitro, does not have sequence specificity. In vitro, has weak DNA exonuclease activity. In vitro, shows biphasic kinetics such that there is rapid hydrolysis of the last three unpaired RNA nucleotides in the 39 flanking sequence followed by a much slower cleavage through the stem that occurs over a longer incubation period in the order of hours (By similarity). ERI1-mediated RNA metabolism plays a key role in chondrogenesis (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus. Nucleus, nucleolus.
Domain:
The SAP domain is necessary for binding to the stem-loop structure of histone mRNAs and to form the ternary complex with SLBP, but not for 3'-end histone mRNA exonuclease activity.
Sequence:
MEDERGREHGGDAAQQKTPRPECEESRPLSVEKKQRCRLDGKDTDGSKFITSNGGDFSDPVYKEIAMTNGCINRMSKEELRAKLSEFKLETRGVKDVLKKRLKNYYKKQKLMLKESNAVDSYYDYICIIDFEATCEEGNPAEFLHEIIEFPVVLLNTHSLEIEDTFQQYVRPEVNSQLSEFCIGLTGITQDQVDRADAFPQVLKKVIEWMKSKELGTKYKYCILTDGSWDMSKFLNIQCQLSRLKYPSFAKKWINIRKSYGNFYKVPRSQTKLTIMLEKLGMDYDGRPHSGLDDSKNIARIAVRMLQDGCELRINEKLHGGQLMSVSSSLPVEGAPAPQMPHSRK
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors (By similarity).
Subcellular Localization:
Nucleus, nuclear pore complex. Nucleus membrane; Single-pass type II membrane protein. Note=Central core structure of the nuclear pore complex.
Sequence:
MVTRVASSERPRPLVPESIVDAPTQRLYAIGVFVALQAYKIYDLLKLETSSISDVPKSGFLVKWIIIDAIYLRLLPKFRIPWLSFQPAATLLQIAIFAAINLLLSSLSSLKWISIGSILLPYFKKKELSISEHKINPNNVIHNSSRILGQYTLQVLPEGTAKINPLHENYCLNSLRKDQYVDLAIQFNSTIPKYIQYSHVDLETKEETLVEVSGRSLRKLLSSSSKNPKEPRLQTIYLKTNKRGLYTLKHVVDKSKLDVRIFRSEAVVVSCPTATFASRQSGGRLRERCVGDTDNAELKVTGVAPLQVTYRNWDGKHFNTHIIDSTIPDDFHPPAVVLSSNPKDIVFYKGIDIQWARSSEIFVPINTLLKAPGQWIYAVTQVTDALGNSQQFPSNDQFLLRFAHGYTEADGESHSLPENVYSVFVHQRPDIQFRGCSIESPANLFPNKETSLSLYSSFSEYNSLEVGVDRYELGLDPQNITVPPLSHKTYQISPRSSANINVKKPGIYVLSSVSSQYCSGEVLEPNTCLVVTPPEAKVSVSFEEISDQCAGSIGARADLELEGTPPFTIAYRMTKDNEASRIQYVTTDRTRYQLNFTPKKAGKYRYIILGIQDANYGYRELSGSSFYKDQTVFPLADASFEERRNGDLSTVVKTSCIGDTMSLPVLLTGSAPWTLEYEIFRNNKREESHVVESKDPRYILEVPMLVHGSQYTITLVSVKDSNGCKRSLNTADTVIKVRRQRPTATFYSSDNTYTLKSVEGALMKIPLRLAGEKPWYVEYSHTSGLNKVSHHKEVLNDPNSYLTVRKSGTYTLLSVSDSSCPGTIQNVEQKYQVEWLPRPFLSIPSLESSVKGKTRYYEQNAVCAGDSSAFEVQLSGSGPFLLKHDKILVDEKSKTYPKQKSELSTVQNTVLVKADTAVPGVYHYEFTKLSDSLYSDSDAVTIVNNQSYQAVVLQRVNSLPKASFMNVEKLYTFCINTDVTQSNAQLIAIQLQGASPFSLVIGIKNELTGSVSKYTLNDIHESVYKFAFPQEQLTLGKHVVRLLQVRDANGCAASITKTQPAAKVSVVEMASLAPLGSRQYYCVGDRLSFALQGLPPFDVEYEFNGVTQHATSDSHILTRLIELPGVVAMKSISDHGSHCKSYINPPIEQIVHDIPTVRISNGKDVIENIHEGDQAEISFHFTGTPPFSFSYARRALGKKRPGKVLETHTVTGINEYEYKVLSSVEGVYTVLSVQDKYCRYPQDSTSSSNI
The following text describes a protein:
Function:
ATP-dependent annealing helicase that catalyzes the rewinding of the stably unwound DNA.
Subcellular Localization:
Nucleus.
Sequence:
MVLTDEQRQAIAKKREEAIRRAAAYREREMQAAANATASTSSAAPPAPPKPVIPVMFSQNRQNFQPMKPTMNNSTKQSTINNYIKQVQKPEPTSLIKPTIGVKLKLDIGDRIKIEFYPFHSAVIDLIKQVPSRNYDPAKRSWTVASSDHITISNILKNATAVKVELEPLPQNIIGLTNFKPKAAPSDLNTVMDPSLIERLFPYQKEGVIFALERDGRILLADEMGLGKSVQALTIARYYKADWPLLIVCPASVKGAWKKQLNTFFPIIHRIFIVDKSSDPLPDVCTSNTVAIMSYEQMVLKHDILKKEKYRTIIFDESHMLKDGKARRTKVATDLSKVALHVILLSGTPALSRPSELFTQIRLIDHKLFTNFHEFAIRYCDGKQGRFCFEAKGCTNSEELAAIMFKRLMIRRLKADVLKDLPEKRREVVYVSGPTIDARMDDLQKARADYEKVNSMERKHESLLEFYSLTGIVKAAAVCEHILENYFYPDAPPRKVLIFAHHQIVLDTIQVEVNKRKLGSIRIDGKTPSHRRTALCDSFQTDDNIRVAVLSITAAGVGITLTAASVVVFAEIHFNPGYLVQAEDRAHRVGQKDSVFVQYLIAKKTADDVMWNMVQQKLDVLGQVSLSSDTFRTADKMHLRFNDAAQPGIAEYLKKTPDTTIDEWEDPVEEKEDDDLEIICDSPAPKRIKN
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. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MDIITQLQDQLDEMAVLAVNTFGTLQRDAPPDRLSSSYPDPLNPNPKPEDDSKPQVQAQPGAPPPPPAQAQAQAQPPAPDLTEQPKAMSRALVLAAKKFDALVAAVPLSSEEDQVKRIQELQAENEVVGLELQKQLEAAGNTIPTVSRVLTIICLITDVIALQKGS
The following text describes a protein:
Function:
Cystine/H(+) symporter that mediates export of cystine, the oxidized dimer of cysteine, from lysosomes. Plays an important role in melanin synthesis by catalyzing cystine export from melanosomes, possibly by inhibiting pheomelanin synthesis. In addition to cystine export, also acts as a positive regulator of mTORC1 signaling in kidney proximal tubular cells, via interactions with components of the v-ATPase and Ragulator complexes. Also involved in small GTPase-regulated vesicle trafficking and lysosomal localization of LAMP2A, independently of cystine transporter activity.
Subcellular Localization:
Lysosome membrane; Multi-pass membrane protein. Melanosome membrane; Multi-pass membrane protein.
Sequence:
AAVHLTLPPVVTLENGSSTNVSIQLSGPLDTALVITFNMTFSSKNRTIIELPNEVAVPAAQTESSFVVKSKAVGQVTIYLQSNNSNQTGPRIRFLVIHSNFVGIINQLIGWIYFVAWSVSFYPQVYENWRRKSVVGLSFDFIALNLTGFIAYSVFNIGLFWVAYVKEQFLHQHPNGVNPVDSNDVFFSLHAVALTLVVIVQCFLYERGDQKVSPLAIGFLVLSWTFVFIVLGVAAAGVITWLQFLFCFSYVKLAVTLVKYFPQAYMNFRRKSTEGWSIGNVLLDFTGGSFSLLQMFLQSFNNDQWTLIFGDPTKFGLGLFSIFFDIVFITQHYCLYRRKSGYEQVN
The following text describes a protein:
Function:
Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration (By similarity). Its substrate specificity is still unclear: may act as a protein kinase that mediates phosphorylation of coq-3 (By similarity). According to other reports, acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway, as suggested by its ability to bind coenzyme Q lipid intermediates (By similarity).
Subcellular Localization:
Mitochondrion.
Sequence:
MAAKRPPASTLKWCQQEMGPICEGIGMVVRSQIGYDGRRIEKQIRRKALQTVVMGGQDVDPLKEPNKTNAPLLSPTLPSTNEALQRARVVAAGIETFAKLMSQGTYPGSAGFTVSETGERKYMKQTSPVQSNIVANLMATADKLSKGVISLAPFPLPTITKLGTWVIANPTAQLPIPPQLKSAIPAIGQIETLIQSILGVQGPVSSVSRAPRKLKLEGVTDQVVLEPETIHATVDVEPIDKTLTKEEAEFLIKAARSVDDDNAETAIFGTQKAKPKVYRPELPKNFEVNLEMGNVHTLTRSNESSVPATRIGRLATFGQLAFGLLGGATAEVTRRTFGIGKRLQEEGIPKNPFLSEANADRIVATLCRVRGAALKLGQMLSIQDSSTVPPALLQIFERVRQSADFMPIKQVHRQMKDAFGDDWREKFEHFDDKPFACASIGQVHKAVLKDGRNVAVKVQYPGVAEGIDSDIDNLVSVLSVGGIFPKGMFLDAFVGVARRELKQECDYEREARAMKKFRELIADWQDVYVPEVIDELSSSRVLTTELVYGKPVDACVEEPQVVRDYIAGKFIELCLKEIFLWRFMQTDPNWSNFFLGKHPKTGEPRLVLLDFGASRAYGKKFVDIYMNIIKSAYDGDKKKIIEYSREIGFLTGYETSVMEDAHVESVMIMGETLASNHPYNFANQDVTMRIQKLIPVMLEHRLTSPPEEIYSLHRKLSGCYLLAAKLKATVSCGGLFHEIHENYVFGEDGIDINID
The following text describes a protein:
Function:
Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process; dATP also allows positive supercoiling. Increases the linking number in steps of +1. Only this subunit binds DNA, in isolation it does not hydrolyze ATP. Hydrolyzes ATP only in the presence of DNA. Transiently cleaves a single DNA strand and remains covalently bound to the 5' DNA end probably through a tyrosine residue. It changes linking number in steps of one, and nicks DNA preferentially at 5'-CNNN | 3'-sites with a strong preference for 4 pyrimidine residues. There are about 1000 heterodimers per cell. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication (By similarity); Reverse gyrase activity is reconstituted after incubation at 80 degrees Celsius for 5 minutes, positive supercoiling requires ATP and Mg(2+). In the presence of ATP it binds and nicks substrate but does not make closed product.
Miscellaneous:
MISCELLANEOUS: Starts on a TTG codon; MISCELLANEOUS: This enzyme is the only unique feature of hyperthermophilic bacteria/archaea known and seems to be essential for adaptation to life at high temperatures. It may play a role in stabilization of DNA at high temperatures.
Subcellular Localization:
Cytoplasm.
Domain:
Introduction of positive supercoils requires the cooperation of both the helicase-like and topoisomerase domains of the 2 subunits. The helicase-like domain probably does not directly unwind DNA, but more likely acts by driving ATP-dependent conformational changes within the whole enzyme. A beta hairpin in the 'latch' region of the N-terminal domain plays a regulatory role in the enzyme, repressing topoisomerase activity in the absence of ATP and preventing the enzyme from acting as an ATP-independent relaxing enzyme; it also helps to coordinate nucleotide hydrolysis by the ATPase domain with the supercoiling activity of the topoisomerase domain.
Sequence:
MNATLRIRNRPVAESTYTSLRGAKAEVVRVEREEREIHPKPPFETGTMLQAATRRLRLSSERVMQLAQDLFEGGLITYHRTDSTRVSEEGKRVARDYIRANFDPEDYNPRTWEPEAEHVEGAHECIRPTRPADAEELRTMVREGAIQTTVTLTSHHLRLYDLVFRRFVASQMKPAKVLYQEAVLEVEVKGVPVAELELSGVLEIVEPGFTKVLTEYDLPAYGIRETPELEEGDRLEIGDVEVLERHEEYPYDQSELVEDMRERGLGRPSTYAQIVEKLFRRGYVYEVPQRRWIFPTTRGEAVYEYLSTHYERFVSEETTRDLEERMDAVALGKAEYQEEMEKLYLELERVVEMPDPEP
The following text describes a protein:
Function:
Receptor for glutamate that functions as a ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein.
Sequence:
GTHHPKIHHTVLNTWKCSTCDFVIRNPVYLSCFRGPQPWVRSPWGSCSRAPLPQSIHLSFLRTVPPYSHQSNVWFEMMRYYKWNHIILIVSDDHEGRAAQKKLETLLEEKESKAEKVLQFEPGTKNVTSLLLEAKELEARVIILSASEDDATTVYTAAAKENMTGPGYVWLVGEREISGNALRSAPEGLIGLQLMNGKNESAHIRDAVAVVAQAVHDLFEKENITDPPRGCVGNTNIWKTGPLFKRVLMQTKYADGITGRVEFNEDGDRKYANYSVMNLQNNKLVQVGVYNGSHFLPNDRKIIWPGGETETPQGYEMSTKLKIVTIHQEPFVYVKQTQQDGKCEARHNSTGGLVQQVLCTGPNETMPGEAQLGFCTVASVEYVCIAFSRQVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLAILKSVSRGVREGTGGLRPPCSLALTFLLLSGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKATFRSITSTLASSFKRRRSSKDTVRGRKTIMPSFSFFLSFLSFSLSLSLSFSLSPPLFCHPINYHTPIPKLPV
The following text describes a protein:
Function:
Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. Promotes assembly, stabilizes and maintains the activity of mTORC1 and mTORC2 complexes, which regulate cell growth and survival in response to nutrient and hormonal signals. May be involved in telomere length regulation.
Subcellular Localization:
Cytoplasm. Membrane. Nucleus.
Sequence:
MVQSLLGYLALDSQRRPLLIQVLKELLETWGSSSAVRHAPLEQQCYISKAILVCMAHLGESELQDVRDELLASMMAGVKCRLDSSLPPVRRLGMVVAEVISSRIHPEGPPLKFQYEDDEMSRELLALAAPGPASDCSLEARGPSPAPVATEPPVETPEKTMESDVHPAQPQGSDSELDSDDEFIPYDMSGDKELKSSKEPLYIRDCVEALTTSEDIERWEASLKVLEGLVYRNPQATREVSVELAKVLLHLEEKTCVAEFEQLRQRALVAVTVTDPEQVAKYLTSQFYGLNYSLRQRMDILDVLVLAAQALSRPRSLQRLSQHSSPASGTSRSPALAISQPDWQVVVEERIRSKTRRFSKGCPRREVSGVPNEFNSVAGYFFFPLLQHFDRPLVTFDLLGDDQLVLGRLTHTLASLMYLAVNTTVAVPMGKALLEFVWALRFHVDIYVRRGLLSAVSSVLLSVPTERLLGDLPDELLEARSWLADVAERDVDEDCRELAVRSLLLLERLKDKLLSSCSPQP
The following text describes a protein:
Function:
Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ("psi") residues may serve to stabilize the conformation of rRNAs.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MKKDKDFENFVGLQLGGGYRDKGPPSEVVEKIPYFNAPIYLQNKIQIGKVDEIFGPINESLMEGIVATSYAEGDKFYIDPAKLLPLARFLPQPKSCEPLDFLEESCACQGEGGGEPPKGSLGGAIDTHFGSLKVLVKKMSAEGAALQGSGWVTNSLRSLWLTLDTTANQDDDKAAILVPSLLCSDLFVFVFHCSPLLPDKTLTRLVRSLLFHFSVT