lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Required for initiation of chromosomal DNA replication.
Subcellular Localization:
Nucleus.
Sequence:
MVLTTDTKFSEIYDIIKGDSVQGESVLILVARDCDSIAACKILTEILKSDLIAYNIKAVSGYEDLENVNSTLLENEEIKSIIMINCGGNIDITNVFTNLNDQQVAYIIDSHRPYSINNITNESSVLIIDDGTYIEQDELQQLSDDSEEEEEELEEEEAEEDVVEDEAEEAEEAEEAEEAEEAEFDPENEDNPENDEDDGGSENIDENERKSKKKNKKDKKSKRKHRKKKKKKSEKLEKTYYGKSAAVSMYSLSTFLNKQNLDDLLWYAVLGLTDQFIHEKITLDSYEQQYKNFKELILNNYPTDGDDDQEERYRPGNDEDDYDENGDLKRHPSSMFLHGDKIIPSDDFRFMLYRHWNLYESLFNSRYVACKLRVWKAKGRFQLESLFAMMGIPLDQVKQKYNSMNVHYKKQLKQLLAINGPKFGLVNLYFNSFLKKYSNNSEISASDTVYAVTALMESDNLESDQSDQDIWEQNFWEAYDSISNKNIDLLKIGLKQSIQLQKEITRQVTSMIEKRSVILSGPFRYAFITESSDLKYFIHPLALTKLGLFMMDAFISMGKAKRPFLIGALNENKNSYLIVGISGSHSTDIQSNTFGEYFRKSAEYTDATFKYQSFDTSIVEVSKTDLHKFVEHLHGTMQTTQISK
The following text describes a protein:
Function:
Histone methyltransferase involved in di and tri-methylation of 'Lys-36' of histone H3 (H3K36me2 and H3K36me3). Binds to H3 already mono- or di-methylated on 'Lys-4'(H3K4me1 or H3K4me2), but not to H3K4me3. H3K4me and H3K36me represent specific tags for epigenetic transcriptional activation. Positively regulates FLC transcription to prevent early flowering transition. Required for flowering transition in response to vernalization and for the maintenance of FLC expression in late embryos, but dispensable for the initial reactivation in early embryos during reprogramming. Also seems to modulate several traits including floral organ size, root size and dormancy. Promotes apical dominance. Directly involved in the tri-methylation of 'Lys-36' of histone H3 (H3K36me3) at LAZ5 chromatin to maintain a transcriptionally active state of LAZ5, a TIR-NB-LRR protein involved in innate immunity. Required for brassinosteroid (BR)-induced gene expression and histone H3 trimethylation on 'Lys-36' (H3K36me3) in BR-regulated genes.
Subcellular Localization:
Nucleus. Chromosome, centromere. Note=Associates with centromeric constitutive heterochromatin.
Sequence:
MDCKENGVGDASGCNIDANSLASNLAMNTNEDFYEKLSSRGQNLDSVSSLEIPQTASSVNHTIEGQRKCFTEIEQMGYGNSNSQEDAGNTDDDLYVCYNADDTQEQGVVSGELEQSQELICDTDLLVNCNKLDDGKESQDTNVSLVSIFSGSMQEKEAPQAKEDEGYGGTTLPIGGSGIDTESTFVNDAPEQFESLETTKHIKPDEVESDGISYRFDDGGKEGRNGPSSDLDTGSSDDISLSQSFSFPDSLLDSSVFGCSATESYLEDAIDIEGNGTIVVSPSLAITEMLNNDDGGLCSHDLNKITVTETINPDLKLVREDRLDTDLSVMNEKMLKNHVGDSSSESAVAALSMNNGMAADLRAENFSQSSPIDEKTLDMEANSPITDSSLIWNFPLNFGSGGIEVCNPENAVEPLRIVDDNGRIGGEVASASGSDFCEAGMSSSRRKARDGKQCKVVQTKTSARHLRKSSRKKQSERDIESIFKCSKQKRSSLLKTSRSSEWGLPSKTTEIFLQSNNIPYDGPPHHEPQRSQGNLNNGEHNRSSHNGNVEGSNRNIQASSGSCLRLKVKFGKSGGQNPLNITVSKVSGNSLPGNGIVKAGTCLELPGSAHFGEDKMQTVETKEDLVEKSNPVEKVSYLQSSDSMRDKKYNQDAGGLCRKVGGDVLDDDPHLSSIRMVEECERATGTQSLDAETSPDSEVINSVPDSIVNIEHKEGLHHGFFSTPEDVVKKNRVLEKEDELRASKSPSENGSHLIPNAKKAKHPKSKSNGTKKGKSKFSESAKDGRKNESHEGVEQRKSLNTSMGRDDSDYPEVGRIESHKTTGALLDADIGKTSATYGTISSDVTHGEMVVDVTIEDSYSTESAWVRCDDCFKWRRIPASVVGSIDESSRWICMNNSDKRFADCSKSQEMSNEEINEELGIGQDEADAYDCDAAKRGKEKEQKSKRLTGKQKACFKAIKTNQFLHRNRKSQTIDEIMVCHCKPSPDGRLGCGEECLNRMLNIECLQGTCPAGDLCSNQQFQKRKYVKFERFQSGKKGYGLRLLEDVREGQFLIEYVGEVLDMQSYETRQKEYAFKGQKHFYFMTLNGNEVIDAGAKGNLGRFINHSCEPNCRTEKWMVNGEICVGIFSMQDLKKGQELTFDYNYVRVFGAAAKKCYCGSSHCRGYIGGDPLNGDVIIQSDSDEEYPELVILDDDESGEGILGATSRTFTDDADEQMPQSFEKVNGYKDLAPDNTQTQSSVSVKLPEREIPPPLLQPTEVLKELSSGISITAVQQEVPAEKKTKSTSPTSSSLSRMSPGGTNSDKTTKHGSGEDKKILPRPRPRMKTSRSSESSKRDKGGIYPGVNKAQVIPVNKLQQQPIKSKGSEKVSPSIETFEGKLNELLDAVGGISKRRDSAKGYLKLLLLTAASRGTDEEGIYSNRDLSMILDALLKTKSKSVLVDIINKNGPFAGMESFKDSVLSFTEHDDYTVHNIARSFRDRWIPKHFRKPWRINREERSESMRSPINRRFRASQEPRYDHQSPRPAEPAASVTSSKAATPETASVSEGYSEPNSGLPETNGRKRKSRWDQPSKTKEQRIMTILSQQTDETNGNQDVQDDLPPGFSSPCTDVPDAITAQPQQKFLSRLPVSYGIPLSIVHQFGSPGKEDPTTWSVAPGMPFYPFPPLPPVSHGEFFAKRNVRACSSSMGNLTYSNEILPATPVTDSTAPTRKRELFSSDIGTTYFRQQKQSVPPWLRNNGGEKTANSPIPGNLTLEKKLNS
The following text describes a protein:
Function:
Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular Localization:
Cell junction, tight junction. Cell membrane; Multi-pass membrane protein.
Sequence:
MGCRDVHAATVLSFLCGIASVAGLFAGTLLPNWRKLRLITFNRNEKNLTVYTGLWVKCARYDGSSDCLMYDTTWYSSVDQLDLRVLQFALPLSILIAMGALLLCLIGMCNTAFRSSVPNIKLAKCLVNSAGCHLVAGLLFFLAGTVSLSPSIWVIFYNVHLNKKFEPVFTFDYAVYVTMASAGGLYMTSLLLFIWYCACKSLPSPFWQPLYSHPPSMHTYSQPYSARSRLSAIEIDIPVVSHTT
The following text describes a protein:
Function:
Dephosphorylates specifically the 5' and 2'(3')-phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP.
Subcellular Localization:
Mitochondrion.
Sequence:
MIRLGGWCARRLCSAAVPAGRRGAAGGLGLAGGRALRVLVDMDGVLADFEGGFLRKFRARFPDQPFIALEDRRGFWVSEQYGRLRPGLSEKAISIWESKNFFFELEPLPGAVEAVKEMASLQNTDVFICTSPIKMFKYCPYEKYAWVEKYFGPDFLEQIVLTRDKTVVSADLLIDDRPDITGAEPTPSWEHVLFTACHNQHLQLQPPRRRLHSWADDWKAILDSKRPC
The following text describes a protein:
Function:
Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Together with other chaperonins, contribute to the regulation of gene expression by modulating the spliceosome function on pre-mRNA splicing post-transcriptionally by acting as a co-chaperone of Hsp90 to control levels of LSM8 (By similarity). Required for microtubules (MTs) organization and dynamicity (By similarity). Involved in the process leading to microtubules dissociation in response to gibberellic acid (GA) probably due to the DELLA proteins-mediated translocation of the prefoldin co-chaperone complex from the cytoplasm to the nucleus (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus. Note=In the presence of gibberellic acid (GA) and at room temperature, the prefoldin complex stays in the cytoplasm and is functional (By similarity). But in the absence of GA or in response to cold, the prefoldin complex is localized to the nucleus in the presence of DELLA proteins, which severely compromises alpha/beta-tubulin heterodimer availability, thus affecting microtubules (MTs) organization (By similarity). This changing subcellular localization follows a daily rhythm coordinated oscillation (By similarity).
Sequence:
MADEATRAAFMEIQASMIELTGKLKQVQNQMRNKEGDRKRAFLTLEELRPLPEETNTYKSIGRTFVLEPKTVLEGEQEQKLKDSEAAVASLQTSKEYLEKQVAEVENNLRELLQQEPGIAQQIMSMSM
The following text describes a protein:
Function:
Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm. Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix.
Subcellular Localization:
Peroxisome membrane.
Sequence:
MPGTIAEDRKELFASAVSFLGEPSVQTAPLTKKVEFLQTKGLTEDEIQLALEQAGKADTQGRHEVVQSAGVGAGAVMQDVVYETVPPPLPRRDWKDYFVMATATAGLCYGLYEVTRRYVVPQLLPESRSRLEQDKRQIEDHFEKVDRLLEKLEQEQDEFRDQQVEKLKELDATIIKLQGALEETTKTRNNINFEFRDLKLQVTEMAKKLDEFRQARDHNSQLTALQSDMESLKRLIKNSTLLSSPAPGAGSAPPAVPLAASIPSASEILAKMKSNTRSEDGEAMPSWKIGRKDLSAASIPDWQKTALSSREQSPEDSLANGLSHKLSLDNLSGPE
The following text describes a protein:
Function:
Covalently binds beta-alanine in an ATP-dependent manner to form a thioester bond with its phosphopantetheine group and transfers it to an as yet unknown acceptor via an amide bond. May be required for a post-translational protein modification or for post-transcriptional modification of an RNA.
Sequence:
MTLQELVLRTASVYMDRTAVCFDEGNNQPPVCYSYKALLSAASELSHFLIAHCDFGGIREIGLYCQPGINLPSWILGILQVPAAYAPIDPDSPPSLSTYFMKKCDLKYVLVEKQQLSKFKSSHETVLNYDTVSVEHKDLALFRLHWEDGRVSTVLGDRADQHKVTDREDRVSAESRTPEKEHMDMRHDGCLAYVLHTSGTTGTPKIVRVPHACILPNIQHFRSLFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILFSRHRVTVLQATPTLLRRFGSELIKSTVLSAHTSLRVLALGGEAFPSLTILKSWRGKGNRTQIFNIYGITEVSSWATFYRIPEEILNSAVKHESPVQLGSPLLGTVIEVRDQNGSPVLEGTGQVFLGGKNRVCFLDDEMTVPLGTMRATGDFVTVKDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTWYNQERLILFIVSKVDLVKDCIFKELQKHLPAHALPDDMVLIDTLPFTCHGKVDVSELNKIYLDYISSQPRNELHGKEELWGKLQYLWKSILCLPEDPEDTLKVPANSVFLDSGGDSLKSMRLLSEIERLTGTAIPGLLEVILSSSLLDVYNHIVQAVFTPEDRKANRSYTTKRKFSDADPEEASGKPARLESAWPSNHAGETNSVIALSRGSQVLSLGAGRLLTQLGLCLPVCSLDLIPQTNTQILKSLSPPAPDENLEKPPLFQQGSPVVGAMAMALRERWRSDTGKCVDASPLLVRAAVQDKPSTTVYIGSHSHTVKAVDLSSGETRWEQLLGDRIESSACVSKCGNFIVVGCYNGLVYVLKSNSGEKYWTFTTEDAVKSSPAVDPTTGLIYVGSHDQHAYALDIYEKKCVWKLNCEGALFSSPCVSLSPHHLYCATLGGLLLALNPASGSTVWKRSCGKPLFSSPRCYQQYICIGCVDGSLLCFTHSGEQVWRFAAGGPIFSSPCVSAAEQEIFFGSHDCFIYCCSKEGHLRWKFETTARVYATPFAFSNHPRSDDALLAAASTDGKLWVLESRSGELRSVYELPGEVFSSPVVWESMLVIGCRNNYIYCLDLLCGDKNNQV
The following text describes a protein:
Function:
Selectively catalyzes the oxidative deamination of acidic amino acids. Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors. Protects the organism from the toxicity of D-amino acids. May also function in the intestine.
Subcellular Localization:
Peroxisome matrix.
Sequence:
MKTVRVAVVGAGVVGVSTAVCIAEALPLCSVTLIADRFSPDTTSDGAAGILFAAEFPDVPIATQRRWFRSSFRHLLAIAQSEEAPEAGVTLSSGWQIFKELPETPKPFWWDLVIGFRAMTSGELRRFPGHACGQFFTTLKCECRSYLPWLQRRFRGAGGRVERRRVGSLQELGGDFDLLVNCSGLGSRALLGDMQVEPVRGQVLQVEAPWLQHFIRDGDGKTYIYPGVRSVTIGGTRQAGDWRLGEDQTDTEGIVERCRRLEPSLSRAKVLGCWVGLRPGRRNPRVEKELLQLGGRRVPVVHNYGHGGWGVTLAWGTAVDAVELVRQSLQETPPRSKL
The following text describes a protein:
Function:
Required during maturation of the 40S ribosomal subunit in the nucleolus.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MDSNIAHRPGVLKHPNKSHKTGRHRSKGSISEVTKGKANVKTITKKEKGHLNKHEKRNKLKQLRNQKREEILEQKRNRGTHNTPPFLVTVLPTCKPHINEADVLARLFEGCDDVLVTASHRSCHVSCQRFKQRYEFIFPTSLIDYMDATKVSDCLMLLVPVGQQNGGSAADDDMAVDGEDGGEDGCGRFVDSSAEKILACLFNQGLCSVTLCCSGLKQLPVKKQADKKKDIIKSLSSRFPDEKLLTLDTAQDAIMMLNHIGSQKMNRMSYRDLRAHVFASHVAYVQPDSEVSTAWVGYGAGDYCTLQISGYVRGSRLSPNQLLHLPGFGNFQISMIEELLDPHPLIHKNKQVTLADGDTLKATHRPDPAEQESLECEIEPDEMQNEQTFPTEEELKEAEMNFQKKKVKKLMVPKGLSDYQASWFEQTNEDEEDSDGDEDDDDDDDDDGERKEFNDLVRQRDEISMKVPSVKDDGDAYDNNFDEDEEKRLLEKHKEARMERMFPDEIDTPQDQPARVRFQKYIGLESMNNSQWDRSENLPNEYARITRLNNFKAVRKMLVNEILKKDDNEQEEKKVKPGAYVTIHIAEVPSSILELVNSSRPVVTFALLPFEQKLSVLHFLIRRCPGDKEPIRSKDPMVLHVGCHRFKCRPIYSKHTTAFNHKFEKFFYPDTTLVASVYAPIIISPANVLMFKDGDADDNKLVGTGTLLSVNPDRIIVKRIILSGHPFKINRSSTVVRYMFFNREDILWYKPVNLKTKRGALGYIVEPLGTHGHMKCKFFDKVKSHDVVLMKLYKRVYPKWNDFKQLYN
The following text describes a protein:
Function:
Reversible hydration of carbon dioxide.
Sequence:
MRYINYDEPLYSPDIVNNGHTVQVSAPHDRYHGIRLPHPASTFRFLQFHFHWGNSSARGSEHVVDDNSYSMEMHLVHMNTKYTSVEQASKHGDGLAVVAVLFKVGQVDNLYFDVIVDAVRQVQTGENVHMNVTKPVVLSHLLPKDGVDHFQYFGSLTTPPCSEAVTWIVLRKAVTMSERQVRPCPYEELLFEDKPNSSWNEA
The following text describes a protein:
Function:
Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein stk3/mst2 and stk4/mst1, in complex with its regulatory protein sav1, phosphorylates and activates lats1/2 in complex with its regulatory protein mob1, which in turn phosphorylates and inactivates yap1 oncoprotein and wwtr1/taz. Phosphorylation of yap1 by lats2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis.
Subcellular Localization:
Cytoplasm.
Sequence:
MDDNKPLKKLSEESLTKQPDEVFDLLEKLGEGAYGCVFKAIYKEAGQVVAIKQVPVESDLQEIIKEIAIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRRKTLTEDEVATILNDTLKGLEYLHFMRKIHRDVKAGNILLNTNGNSKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYDCVADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPQKPPPTFRDPEKWSETFINFVSQCLVKSPAQRATATTLLQQDFIKNAKPHSNLREMVQEAMEIKRRKLKNGSDSEEDDEEDGDDDVDVGTMVKVSVDHTDGAGTVKVNSLASSISGTMIQHDTDMGLGTMVINDDEEEDTGTMQWRGADTVVKNNDVERPAFMNYFDNVGSSSSESGSSGAPPGGAKKGLPAEEAWKFSKNITEMNFSFLKNLSVSELQIRLGALDPLMEKEIEDLRKRYFEKRQPILDAIDAKKKRQQNF
The following text describes a protein:
Function:
Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase elongates using dNTPs.
Subcellular Localization:
Host nucleus. Note=Requires the presence of the primase associated factor to properly localize in the host cell nucleus.
Sequence:
MTLVLFATEYDSAHIVANVLSQTPTDHCVFPLLVKHQVSRRVYFCLQTQKCSDSRRVAPVFAVNNETLQLSRYLAARQPIPLSALIASLDEAETQPLYRHLFRTPVLSPEHGGEVREFKHLVYFHHAAVLRHLNQVFLCPTSPSWFISVFGHTEGQVLLTMAYYLFEGQYSTISTVEEYVRSFCTRDLGTIIPTHASMGEFARLLLGSPFRQRVSAFVAYAVARNRRDYTELEQVDTQINAFRERARLPDTVCVHYVYLAYRTALARARLLEYRRVVAYDADAAPEAQCTREPGFLGRRLSTELLDVMQKYFSLDNFLHDYVETHLLRLDESPHSATSPHGLGLAGYGGRIDGTHLAGFFGTSTQLARQLERINTLSESVFSPLERSLSGLLRLCASLRTAQTYTTGTLTRYSQRRYLLPEPALAPLLERPLPVYRVHLPNDQHVFCAVASETWHRSLFPRDLLRHVPDSRFSDEALTETVWLHDDDVASTSPETQFYYTRHEVFNERLPVFNFVADFDLRLRDGVSGLARHTVFELCRGLRRVWMTVWASLFGYTHPDRHPVYFFKSACPPNSVPVDAAGAPFDDDDYLDYRDERDTEEDEDGKEDKNNVPDNGVFQKTTSSVDTSPPYCRCKGKLGLRIITPFPACTVAVHPSVLRAVAQVLNHAVCLDAELHTLLDPISHPESSLDTGIYHHGRSVRLPYMYKMDQDDGYFMHRRLLPLFIVPDAYREHPLGFVRAQLDLRNLLHHHPPHDLPALPLSPPPRVILSVRDKICPSTEANFIETRSLNVTRYRRRGLTEVLAYHLYGGDGATAAAISDTDLQRLVVTRVWPPLLEHLTQHYEPHVSEQFTAPHVLLFQPHGACCVAVKRRDGARTRDFRCLNYTHRNPQETVQVFIDLRTEHSYALWASLWSRCFTKKCHSNAKNVHISIKIRPPDAPVPPATAV
The following text describes a protein:
Function:
Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
Sequence:
MVKLPAISKKPREIAKQKIIELAKKMYEDLMKGKRPKITMPIRSLSNAMFDKEKGSFTLVGKEKARTLTVNQAKIFAQTTKMLEFAKQLLETDDFSTLREAYYVSKNWGEARFDDQQASNNVIEDLEAALGVLREHLGFIPEEDGSSVVGPLKIIEETPEGELVVDCTKLGTGAYNIPNDVTKLNLETDADFILAIETSGMFARLNAERFWDKHNCILVSLKGVPARATRRFIKRLHEEHDLPVLVFTDGDPYGYLNIYRTLKVGSGKAIHLADKLSIPAARLIGVTPQDIIDYDLPTHPLKEQDIKRIKDGLKNDDFVRSFPEWQKALKQMLDMGVRAEQQSLAKYGLKYVVNTYLPEKIKDESTWLP
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MVWPFCPDCHNTLTVNASGTVRCSVCNHTTNLSAYSESTLPSRTTTSADRPVPLWAKSDEEQAALRTLSEPKRMVVEEPCVKCGAGEVGFYTVQLRSVDEGQTVFYECPKCSYTWSVNN
The following text describes a protein:
Function:
Component of the ceramide synthase complex required for the synthesis of ceramides. Plays a role in the localization of LAG1 to the nuclear endoplasmic reticulum.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein. Note=The specific interaction of LAC1 and LIP1 at the lumen of the ER may be important for the enzymatic activity of the complex.
Domain:
The C-terminal domain probably plays a role in its function.
Sequence:
MSQPTPIITTKSAAKPKPKIFNLFRVCFISLLLIAAVEYFKYGTRINYEWFHCTPIKEPQSGSVIKLWARGGPSCDKRGEYKTIVKRITRDYEPNDEHLSFCIIENDNVPPVHYPIHEDKGEPGYVAYVGYDTDSELVQELCADSTIYHM
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.
Sequence:
MSRSSGKDAPKAFKVMVLQGDHIGPEVMAEVLPLFDVIQSHFGIKVETFERLIGGSCLDQHDCPIQESTLQEASECHAVLLGSVGGPKWDVGDSSRRPETGILRMRKHLNLYANVRPAKIISERQLELSSLKEHVVRGVNIITLRENAGGIYFGRKQEPDPLAHKDLCEYTREEVVRLTRVAAALSLASSHGPLPIISVDKANVMATSRLWRQVVTETIRDEFPQLMDKLSHQLVDSAAMLLAKDPRKLNGVVLTENLFGDILSDLTSVIPGSLGVLGSAEIDGPPIPSQDFRMPMGVYQPVSGSAPDIAGKGIANPIGMFMSFGLMCRWSLGLPKAADAIDSAIKDCLESGQCTRDVGGTLSTQQAGSALRQSIQEFLS
The following text describes a protein:
Function:
Transcription factor. Positively modulates neuronal levels of the ubiquitous Ca2+ sensor calmodulin/cmd-1, probably by direct binding to the cmd-1 promoter, thereby regulating Ca2+ signaling, physiology, and behavior.
Subcellular Localization:
Nucleus.
Domain:
May negatively modulate calmodulin/cmd-1 expression via a negative feedback loop in which the IQ domains bind to calmodulin.
Sequence:
MNNSVTRLLFKRLLTLQLCHHFDIIPHRDQSFDCVQMQQPQNETANNFIPSIQLLWSTDPPQIRPDGTYPQAVELFPCFKDKWNTKEEILNIILAANADPKSNCVTVQSSPRPCSSSQFIYPRLDNAWYKNDGYIWKKRTNGKQNREDHLNLKISGHPHISAKYIHSAIVPTFHRRSYSVPDSDCHVLVHYLNVKTNNKIDDQAEEIARSMIENKVFISLSQLHDQLSPIFLQTLNVNQLVAEINEHLKKKGVNLPTSPLPQEPSSSTSRELERRNSCSSAFRKGLSSVALRRQPSANSEIDANHIGTMLKRFGCNGSSSDRISIIQPTMQNFQSIRSHQNHVAMESRSPSGDGDSRPITFEEDASYQQLSIKSSTNVSTPASAFAEKMKIRSGSQESPMGPPSSSSVTSTSLIPIIEMTPSSSSLKGGQKMLVVGGYYRKGHEYKISFGRGRMMPAVLIHAGVLSCVIPPSAKPEVVQIRVFCNGQAISTASEFTYEPQSAHLIKENDDTLVQIFEKIRIMACAFNAYSSIENIQSSSCMESLLANIVQQIDNEVSSQNLNYKTELLNGSAHFPSKTVLHLVASLDYDRLFEALIDLSRKVPACREFDIFARDNDGSTPLHTACKNSASRIARLIISIDSSAIDVVDDRGRTPVEVAPEHSIDMLSDKNNEEERVNATELWVMTNGKAFTTDKILDGKISRAPIAEKPDDLLREATSSYSIMSEMYEGPMLQAGTSRECDEDCESCCDPDSTQQLHVEIAMDTDVHVPDSPKMARLFHAVTSPGIVVPPNARARMADLARQIIEALPDRIKRNSEVSMCPDEEDPGQNHHGGVEPMFYQQASCSMSTDSPNMMDDYFDMMATETRNDIFTEPRSTETTETSASKSAQLFATHCNFFDDRSFASSSTRANTFESDTLDFDKDLGEFFTIHVDRFVDPIQQRLANLKYNDDEQRDVYEAAMVIQRAYRVYRARSTTRRQEDIERRAALKIQGCYRRYKQFCYFKKLHNAAIVVQKHFRMRKRDDKEEGAVEAVIASVPEHPTLDGQSICIQVPKTNSTMLRERAATTIQVAYRYRHRKRQAAARKIQNFMRQNRNNVNIDDGHTQHLIAENACAKRRRYVACPQTSGDQRNKRDSDGERKRDAHHDAPEFIPIGATPSSTTIPHRPTQRHHPWDQLKPPYGCGTLA
The following text describes a protein:
Function:
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MLSSRAAAFTGRRLASTLPPVPRKKSHGVRRLLAKAVVATSLFYAGGLTLSAYNDKANELFVEHVPFGEELVERWEDWTSLRRPGRRMIDARRVDEISRDFRAAATPEATPVVVRPLVQLQLPELQMQGSSPVLEALVNNVNDVVVALNARALELPEDTASALSSVYGEIVHSIQALNASLDQEFATEVESRTGKAISSVQEQLEVEYKQRELALAEQYIQNFEVFKSQLQKATAEQLETELKAHEQALLARHRNEVAQLSIRQVEEFNKIIEKKLDQERNGRLAKLSELNSAVESLAPVLDRLELRAVKNECVTQLSTLISDIQGKLSRGGDEPLDLSSDLQRLTLLADILPRPKRCCSEGPALLDVAMAELQAKAQAPVASNEQLYNRWQLLQPELKTTSLLPPNAGFLGHLTAKLFSMLLFTKEGFSTTQDMDAVTARIAENLRLNKLDCALEEAVNMKGWSRKSADAWVDLARRRLEVLTLLDVIEAEVKTL
The following text describes a protein:
Function:
Specifically methylates the N7 position of a guanine in 16S rRNA.
Subcellular Localization:
Cytoplasm.
Sequence:
MEIILKYFPDLTEEQRKQFAALYDLYIDWNAKINVISRKDIENLYEHHVLHSLGIAKVIQFRPGTKVMDLGTGGGFPGIPLAILFPETKFHLVDSIGKKVRVATEVANAIGLKNVTFRHARAEEEKQLFDFVVSRAVMPLADLIKIIKKNISPKQQNAMPNGLICLKGGELEHETMPFKHKTVIHSLSENFEEEFFETKKVVYSQI
The following text describes a protein:
Function:
Post-transcriptional regulator that plays an essential role in the expression of viral lytic genes and productive viral replication. Possesses numerous activities that promote the expression of viral genes including enhancement of RNA stability, promotion of RNA splicing and stimulation of protein translation often via its ability to interact with different cellular cofactors. Stabilizes polyadenylated nuclear (PAN) RNA by cooperative binding to a 9-nt core of the MRE (MTA responsive element) together with host PABPC1. Functions as a viral splicing factor and promotes expression of intron-containing viral lytic genes. Protects viral transcripts from specific nuclear RNA decay pathways by preventing host MTREX recruitment that promotes unwinding and degradation of structured RNA substrates. Plays a role in the inhibition of host P-body formation by altering the scaffolding activity of TNRC6A at the initial stage thereby enhancing virus production. Also inhibits host stress granule formation by blocking autophosphorylation of EIF2AK2/PKR and its subsequent binding to dsRNA.
Miscellaneous:
MISCELLANEOUS: ORF50 and ORF57 are the earliest genes expressed in the lytic cycle.
Subcellular Localization:
Host cytoplasm. Host nucleus. Note=Distributes in host nuclear splicing speckles.
Domain:
Binds viral intronless RNAs.
Sequence:
MVQAMIDMDIMKGILEDSVSSSEFDESRDDETDAPTLEDEQLSEPAEPPADERIRGTQSAQGIPPPLGRIPKKSQGRSQLRSEIQFCSPLSRPRSPSPVNRYGKKIKFGTAGQNTRPPPEKRPRRRPRDRLQYGRTTRGGQCRAAPKRATRRPQVNCQRQDDDVRQGVSDAVKKLRLPASMIIDGESPRFDDSIIPRHHGACFNVFIPAPPSHVPEVFTDRDITALIRAGGKDDELINKKISAKKIDHLHRQMLSFVTSRHNQAYWVSCRRETAAAGGLQTLGAFVEEQMTWAQTVVRHGGWFDEKDIDIILDTAIFVCNAFVTRFRLLHLSCVFDKQSELALIKQVAYLVAMGNRLVEACNLLGEVKLNFRGGLLLAFVLTIPGMQSRRSISARGQELFRTLLEYYRPGDVMGLLNVIVMEHHSLCRNSECAAATRAAMGSAKFNKGLFFYPLS
The following text describes a protein:
Function:
Controls stomatal patterning.
Subcellular Localization:
Secreted.
Sequence:
MKRSVCVASIAIILCCVPVVVTSARHVRRLQIHHSQAHESQPSTGEGIVAKPNSYWERTRPMMKRKGSDTLQIAGSSLPDCSHACGLCTPCRLVMVSFVCASLEEAETCPMAYKCMCNNKSYPVP
The following text describes a protein:
Function:
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Subcellular Localization:
Cytoplasm.
Domain:
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Sequence:
MRLVMLGGPGSGKSTQSHNLSQELKLPVISMGGILREAIANATPLGIKAKPYVERGDLLPDPMMIEFIQQRLVQEDGGQGWILEGYPRTAFQAEELDFLLEDLGQPLDWALYLKIDEATMVERSLNRSLFDDHPEAITTRIGKFHEYTVPLLEYYAAKQNLLTVNAYPEVDQVTKLILARL
The following text describes a protein:
Function:
Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of E3 ligasew complexes, leading to modify the Ubl ligase activity. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. Csn5 is essential for growth or survival.
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
The JAMM motif is essential for the protease activity of the CSN complex resulting in deneddylation of cullins. It constitutes the catalytic center of the complex (By similarity).
Sequence:
MSKNGAADALKTFELENNIQTIDHDQLFKYDPQQYQQFLQSKPWSKDPHYFKHVKISAIALLKMVMHARSGGKLEVMGMLMGKVENNTMIIMDSFALPVEGTETRVNAQVEAYEYMVEYLELIKQTGRLENALGWYHSHPGYGCWLSGIDVGTQSVNQQYSEPWLGIVIDPTRTVSAGKVEIGAFRTYPQGYKPPNEGPSEYQSIPLSKIEDFGVHCKQYYSLEITYFKSSLDQQLLDKLWNKYWVNTLSSSPIFSNRDYITGQINDLSEKLEQAETQLSHSRSSILDKKKEESLLSKVSKDSSKVTIEQVQGIMSQVFKNSIFNECQTTKQ
The following text describes a protein:
Function:
Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies.
Subcellular Localization:
Late endosome membrane; Peripheral membrane protein.
Sequence:
MNNASDRRDSVEAPITEVCVVSGKERCPQGFKLLGETEDGKDGDLWTDKFFGKKVTRYICFNRAYANVGGNVLADVALLGERDIVPTGYSQITATADTGEVALKKRILCIKMLPRNMTDSAICDIKLLAKTKRPPPGFTFVGEVNSISVSYKMGPVQRTPGPGRPAPGPPQMSRQQSQPLTEQPVPASPSYAPDVQRQYHTLPADIHRQRADVIPLTRQMSTVKIATAVDGIPFEINKKLGADSIKDFSLPEMQYQTEQEIENKYKYDFTAERTAAARIPPNF