lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Mediates C-terminal methylation of the isoprenylated C-terminal cysteine in A-factor mating pheromone and Ras proteins. Does not have a preference for the farnesyl or geranylgeranyl moieties in the model substrates N-acetyl-S-farnesyl-L-cysteine (AFC) and N-acetyl-S-geranylgeranyl-L-cysteine (AGGC) in vitro.
Miscellaneous:
MISCELLANEOUS: Present with 2690 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MHQDFQEDEHEYPDIRRNPLHEVTMTSYILGILLGIFVGLFPQIRFKNFNLFIIALSLFHFLEYYITAKYNPLKVHSESFLLNNGKSYMAAHSFAILECLVESFLFPDLKIFSYSLATKLCTVLGCLLVILGQYTRTIAMHTAGHSFSHIVKTKKESDHVLVKTGVYSWSRHPSYLGFFWWAIGTQLLLLNPLSLVIFIFVLWKFFSDRIRVEEKYLIEFFSAEYIEYKNKVGVGIPFI
The following text describes a protein:
Function:
Essential for the control of the cell cycle at the G2/M (mitosis) transition. Interacts with the CDC2 protein kinase to form MPF. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis.
Miscellaneous:
MISCELLANEOUS: Present with 98 molecules/cell in log phase SD medium.
Sequence:
MMLEGYTVQPPQSTLIGDIEIQDENANQEVKNVLYQGVQKGIKRLEKRQRRVALGDVTSQKANKIHNAIHNKFHQTKNNFEIENIRSSALVKEQQRDVRHEDSDYFLIDSSEGSSTDDEQVNEDAIDDLLSRRVNDQQIQADEVYEDFDGEMQDVIEEDVDSQIEPLSPINNDEIQTELDRAFEKYFRSVPNPLDDDTHDVVMVVEYASDIFYYLRELEVKYRPNPYYMQNQVELTWPFRRTMIDWLVQLHFRFQLLPETLYLTINIVDRFLSKKTVTLNRFQLVGVSALFIAAKFEEINCPTLDDLVYMLENTYTRDDIIRAEQYMIDTLEFEIGWPGPMPFLRRISKADDYDFEPRTLAKYLLETTIVEPKLVAAAPSWLAAGAYFLSRTILGSNDWSLKHVFYSGYTSSQIIPLASLILENCKNASRRHHSIWKKYFDQKHYRCSQIVEEWIVSTEA
The following text describes a protein:
Function:
L-tyrosine transporter that is essential for parasite survival and virulence. May also act as an aromatic and large neutral amino acid transporter. Does not cotransport other charged ions. Involved in amino acid homeostasis by facilitating the net uptake of L-tyrosine and maintaining intracellular pools of aromatic and large neutral amino acids through exchange.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MESTEATMVERKAESPSSGDRARSIELAHQPTGAGASLSSFEVGGAKQGVNKAQDSAVNKGAANTPPRVAFGLSRYVVLVAYCLYCLLSGPSFMNWTTIADSLYKSGAFEWECKPGEIDTSVLPHEPKCPEQEVSVNHLFTVASCSYFVFAMLGGIMLDFAGPKFGALTGLACLITGWTLFGFSSESFRAYVPAMVFMGAGIDMAFFPCLCGANLFPGMVATIIAVYGSFRSISFIVGLSLRTIYINVEGATFRGVMLGYVGAGLGFCLLVALFIIPRRAWPAPDEAPSASAEQDVEAGADALAQKGEKNLTAIQSMKRDFLSLSFLPLFPYFVLVLITILFFAPSAKRLIPSAYEANQIISIFSFVPCIILGGIADRLGIVPVMMICNTCGLLSWILMLIPGIPCFAASQYIVSILISIQMSFLVSQVYCYVTEIFYPENLGKMIGFLCSVGGIISLVTDPMRKYSVDNGFYTMTVLCLIFALINEGLLLFMYVRKRKVPKVL
The following text describes a protein:
Function:
Required for normal Golgi function.
Subcellular Localization:
Golgi apparatus membrane; Peripheral membrane protein.
Sequence:
MSKVNTDENNFINNNNSNNNINNNDNNDNNNNNIQNVSNQIENGLLSNLPTISSSCESFSSKSHSLTERRSSIKNLLDNFSTLLDILEIPQLMDTCIKNNSFDEALQLESFAKKIYKQYSNNTVIIEIIKEIKVCTRSLISTLQQQLRQDITLTNCIKTIGYLRRLSIYKENELKIIFLHSRDQWLINSLKFDITNSNHVTYLTKLTDSCRTNIFDIVTQYNAIFSNESNDEDQLDDLILYNWIQQKIKVYINIVDSTLNHIKSGSSISYVLENSMYFSMSISRVGIDFRNLLEPIFEKHILNNFLSQITTANHHFLETLKTYKFPLQKSTSPTSSTTSTSSSSSSSSSSQYISPPLSILQHQPLAVLVNLILKSFNELKDCFPISLRSIVILKLKELIISIVGGVTSFYNQLLSNTISNLINSPSTTTTTTTTTITSSFDKVFHSFCKCLAEDFIPFIVKCFDIICSQQLQQQQQINDGSSSSSSSNSIGIDVDSLVLSLKKIYSTETQTIPSTQNNNLPPIPDLVLRGNKNSSPSTTTTPTTPTPTPTPTPTPTPTTPTTPTITHSTPPSPLPSSTTTQLNSNNNNNDNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNTDKKVDERKEENIIKEEEQPISTSTANKNDIAIETITTPSSFSSSSSTNTKSDEEIIDKIVQPDPVVVEKQENEITNILKDDNETTTDILTDNNEATTEIQNNDQSLNPDPIIQEIEDTPSEVIVNNNNNNNDDDDTTF
The following text describes a protein:
Function:
Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion.
Subcellular Localization:
Preautophagosomal structure membrane; Multi-pass membrane protein.
Sequence:
REDWLRMFSSRTRQHYQPIDGEYDEPDLRASGGQGLLPFYNRSYQTGPESAPLIQEASSVSFRPDVRIDMEEHNGPLLTASSSEDRTNWDHITDLDDFFRRIYDYYQGGGFRCIFWHEILSLVQFIFIVFVSTFFIQCVDYEILFNNKAVNIIGNSTDFPRKRQFGDAVDGNCASHLPPLVVACILVATIYWIFRVIRTGVLLLKLTEIQLFYNRALRIDDADLSNLTWESIVRAVCNAQGRIQLLVHDSSISSIHIYHRILRFKNYVVAMVNQDLLPPLISIPFVGDLRFLPEQLKKNLEWMFFLGFCSPFKGSYTLQDEYRDRNRLEEMAENMEKVTTYLGLASLIFSPLVFLYQCLYYLFTAADLTKRDAGALGNRSYTNYGRYRVRHFNELDHELKGRLNRSHAFASAYIAQFSSKLVVVFARKISFMAAAIFVILTGLSVWDEDVVQIEHMLTVITVCGMIALACRSIIPDENLVYQPEVLLNHVTSELHYVPEHWKGNAHDIRTAHEFESLFRLRAINLLEEIFSPFITPFVLLFYVRPGCRSILSFLLDNTERVEGLGDVCSFALLDVAKHGDPSWQKMDEDGGDERGGNHPNRPSRDVAHDGKTEMSCMQFAIRHPDWIPPPATANFIQNLRDKMERDAMAVGQGAGLVRNAFSESIHTILSMPLGGAGMNHLLGGGVSGYPMGGEERGIMSGMERTLEKSLRQSGHESIVDSLREQVGAEMRVSSLYLRGIRADKKKKVYSSMGPADASMFAVPLMETTMAPRSSTFQYPSEDEMERGEAMRRVEEEEEGEDDDDMPPRDFPI
The following text describes a protein:
Function:
DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks. Helicase with 3'-to 5'- polarity; able to unwind over 100 bp of DNA at 50 degrees Celsius. Unwinds forked DNA, preferentially on lagging strand forks; has weaker activity on Holliday junctions. Displaces the invading strand in DNA D-loops. Unwinds short oligonucleotides from dsDNA with 3'- but not blunt ends or 5'-ssDNA tails in an ATP-dependent manner. ATPase activity is stimulated by ssDNA but not dsDNA, protein binds ssDNA, dsDNA with 5'- or 3'-overhangs but not blunt ended dsDNA and replication forks. Replication forks bind both this protein and RPA. RPA does not stimulate the helicase activity of this protein.
Domain:
The C-terminal region (about 633-690) acts as a brake for ATP hydrolysis and interacts with RPA.
Sequence:
MKSLPPEMRQILGDCYPHIRELNPAQRSAIEAGYLESEDNYIIAIPTASGKTLLGIIAALKTVMEGGRVIYTVPLLSIQNEKIKEFRKLEEHGIRVGKDPRTSDIAVMVFESFDSLTRFSWNILREVDLLIVDEFHMIGEYTRGPVIESAITRARTLNPSVRIVALSATLSNMDEIAGWLDARVVEHDYRPVPLHREVLDTEMFGVREKNDVVLKVLERSLEDGSQTLAFVSTRRFTESLASHLADKISGKIPDDMVESFREVAGKVLEVPKSRGSPPTSTCLKLAECLEAGIAFHHAGLFNRQREIIEDEFRDGNILMITATPSLMYGVNLPSRTVVIRDYTRWTSQGPRRIPVFDYEQMSGRAGRPQYDDAGYSYLIARSHDEAMDLEEYYIRGEVERTTSRIIENRDALYRQIIAQVASGLSGTTEELADFFRNTFYGYQMVEGPFSDSFGMDSIQYEVENATEYLMRNRILYPGPEGFSATEFGLLIAKSNYSVETAIKLHQFASEMDEMDIYRLIYEITRTPDMPLISFKGRKSRDPVRDKLMEHGLFLMDVGNEEATAAALIEWINERTEYEIENAFHVYAASTRRSAYEASKIVKFFGKICEIMGVYRHSSQLEILSARLYYGVKEDAIPLVVGVRGLGRVRARKIIKTFGEDLRHVREDELKRIDGIGPKMAGAIRRYCERF
The following text describes a protein:
Function:
Catalyzes the condensation of three molecules of isopentenyl diphosphate with farnesyl diphosphate (FPP) to yield (all-E)-hexaprenyl diphosphate (HexPP; C30), the precursor of the prenyl side chain of menaquinone-6. Large subunit Hexs-B catalyzes the condensation reaction and the final product chain length is cooperatively regulated by both the Hexs-A and Hexs-B subunits using the whole size of the hydrophobic cleft as a ruler.
Sequence:
MRYLHKIELELNRLTSRYPFFKKIAFDAEIIKLVDDLNVDENVKCAIVAIDTSMRMQDFINEDNKDSFVLSTDVLSALFYKYLSQPFYQHDFLVLTDCVSRINELKSIRATITDEIALHNINKQIHYMFIQPYMNNEKVVSYE
The following text describes a protein:
Function:
Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Subcellular Localization:
Nucleus.
Sequence:
MVRFKNRYLLIQLIYGPHESSTIGSNHQSGPSGTKQVNEKSLIDLIRQSIQLNFGDLGAGEAGADLTVKYYSPTTSNLILRCKRDQVTKVRASLLFINQINPQTPVIFNGIHVSGTIRKTQSFLIEFDRQQILSFD
The following text describes a protein:
Function:
Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the 3'-UTR of mRNAs. In absence of phosphorylation and in association with TACC3 is also involved as a repressor of translation of CPE-containing mRNA; a repression that is relieved by phosphorylation or degradation (By similarity). Involved in the transport of CPE-containing mRNA to dendrites; those mRNAs may be transported to dendrites in a translationally dormant form and translationally activated at synapses. Its interaction with APLP1 promotes local CPE-containing mRNA polyadenylation and translation activation. Induces the assembly of stress granules in the absence of stress (By similarity). Required for cell cycle progression, specifically for prophase entry (By similarity).
Subcellular Localization:
Cytoplasm. Synapse. Cytoplasm, P-body. Cytoplasmic granule. Membrane. Postsynaptic density. Note=Localizes in synaptosomes at dendritic synapses of neurons. Strongly enriched in postsynaptic density (PSD) fractions. Transported into dendrites in a microtubule-dependent fashion and colocalizes in mRNA-containing particles with TACC3, dynein and kinesin. Membrane-associated. Colocalizes at excitatory synapses with members of the polyadenylation and translation complex factors (CPSF, APLP1, TACC3, AURKA, SYP, etc.) including CPE-containing RNAs. In P-bodies and stress granules (By similarity). Recruited to stress granules (SGs) upon arsenite treatment (By similarity).
Domain:
The 2 RRM domains and the C-terminal region mediate interaction with CPE-containing RNA. The interdomain linker (411-429) acts as a hinge to fix the relative orientation of the 2 RRMs. The ZZ domain (509-566) coordinates 2 Zn ions and is probably implicated in mediating interactions with other proteins in addition to increasing the affinity of the RRMs for the CPEs. A continuous hydrophobic interface is formed between the 2 RRM.
Sequence:
MAFSLEEAAGRIKDCWDNQEVPALSTCSNANIFRRINAILDDSLDFSKVCTTPINRGIHDQLPDFQDSEETVTSRMLFPTSAQESPRGLPDANGLCLGLQSLSLTGWDRPWSTQDSDSSAQSSTQSVLSMLQNPLGNVLGKAPLSFLSLDPLGSDLDKFPAPSVRGSRLDTRPILDSRSSSPSDSDTSGFSSGSDHLSDLISSLRISPPLPFLSMTGNGPRDPLKMGVGSRMDQEQAALAAVAPSPTSAPKRWPGASVWPSWDLLGAPKDPFSIEREARLHRQAAAVNEATCTWSGQLPPRNYKNPIYSCKVFLGGVPWDITEAGLVNTFRVFGSLSVEWPGKDGKHPRCPPKGNMPKGYVYLVFELEKSVRALLQACSHDPLSPDGLSEYYFKMSSRRMRCKEVQVIPWVLADSNFVWSPSQRLDPSRTVFVGALHGMLNAEALAAILNDLFGGVVYAGIDTDKHKYPIGSGRVTFNNQRSYLKAVTAAFVEIKTTKFTKKVQIDPYLEDSLCLICSSQPGPFFCRDQVCFKYFCRSCWHWRHSMEGLRHHSPLMRNQKN
The following text describes a protein:
Function:
E4 ubiquitin chain-elongation enzyme specifically involved in polyubiquitin chain assembly. Binds to cdc48 and elongates mono- and diubiquitinated ERAD substrates presented by the ufd1-npl4-cdc48 (UNC) AAA ATPase complex to a chain length of 4 to 6 ubiquitin moieties. Delivers these polyubiquitinated substrates to downstream ERAD components, which target them to the proteasome. Enhances ubiquitination at 'Lys-48', but not at 'Lys-29' of the Ub moiety.
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
The U-box domain is required for the ubiquitin protein ligase activity.
Sequence:
MSDLEKIRLKRLAKLQQTNSEANSSKEPKESNIAPEPKKPDLKKRFIGSKATTSNSEQKEISPPVTSGAPKHRLFSKDEWMHFITCQALNITLSETDSSKYYLEGFKKDLEEEGSPLLFNENNVDSALLSRLSTTGNNTFSYLLQSWSFLYQYKKRLPKDENQDFKIHYLSLLKSLLVSYAGIVVMLPDTFNSETIDLAEVLIGAEGIPLEFLSEFVQRFEHENLDELFIPVLESLSLKIGLMNVDTVQMNVMQIILQLVSLKPIALLLPKLPSWNPTNNAGEIEYKTFLGRISSLSVFTQDVASRYFSNSTERSAQNISSSISSLKLTMSTYQDVLFQIFNTLIRTSTSLRESVLDFFAMVVNANHKRQSIQVNHFDITSDACMLNFSHVLSRLSEPFLDIGCSKIDRVQVEYFRRNPRVDIKEETKLNADQKASESFYSKPAEGSNNFISDIFFLNLAFHHYGVNATFKALEQLVQSIRDSEKLKERLETEQQNMSGSFQATRLTAQLSRLDQRLDLDRSFVHCYEIMLTQTSDTSRSFSFLNFVAIWLSRLADGQSSTYPKMPLSLPFNENAPEAFKCLPEYFIETITDYMLSLFKTSSSTLTLHSLEPLCEFCVSFLTQANYIKNPYLRAKLAEILYFGVQTHVGRSELLLDVVRTSKVATRWLLPALMAFYIEIESTGQSTQFYDKFNIRFYICEVFRTIWKQPAYFGKLEQEQKTNLPFFVKFVALMLNDATYLLDEALLKLTEIHNLQSLLADAISNSNSNQNVQESQSNLAAAERQASTYCQLGNETIFMLKLFTSSIPKAFCAVEIVDRLAAMLNYNLQALCGPKCSNLKVEDPTKYHFNAKTLLSIIFDVYLNLCNEPAFVEAVAHDGRSYSKEIFERATSIMTKHNLKSSFDIEAIKEFVNRVEAFRLQEATEEEDMGDIPDYFLDPLMFTIMKDPVVLPRSGISIDRSTIKAHLLSDATDPFNRTPLTLDDVTPNDTLREEINTFLKSKRNKHSRNSE
The following text describes a protein:
Function:
Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Sequence:
MSLQKLENSSNKSVVQEEVLILTELLEDITKNMLAPETFEKIIQLKELSTQEDYQGLNRLVTSLSNDEMVYISRYFSILPLLINISEDVDLAYEINHQNNIDQDYLGKLSTTIKLVAEKENAVEILEHLNVVPVLTAHPTQVQRKSMLDLTNHIHSLLRKYRDVKLGLINKDKWYNDLRRYIEIIMQTDMIREKKLKVTNEITNAMEYYNSSFLKAVPHLTTEYKRLAQAHGLNLKQAKPITMGMWIGGDRDGNPFVTAKTLKQSALTQCEVIMNYYDKKIYQLYREFSLSTSIVNVSKQVREMARQSKDNSIYREKELYRRALFDIQSKIQATKTYLIEDEEVGTRYETANDFYKDLIAIRDSLLENKGESLISGDFVELLQAVEIFGFYLASIDMRQDSSVYEACVAELLKSAGIHSRYSELSEEEKCDLLLKELEEDPRILSATHAEKSELLAKELAIFKTARVLKDKLGDDVIRQTIISHATSLSDMLELAILLKEVGLVDTERARVQIVPLFETIEDLDHSEETMRKYLSLSLAKKWIDSRNNYQEIMLGYSDSNKDGGYLSSCWTLYKAQQQLTAIGDEFGVKVTFFHGRGGTVGRGGGPTYEAITSQPLKSIKDRIRLTEQGEVIGNKYGNKDAAYYNLEMLVSAAINRMITQKKSDTNTPNRYEAIMDQVVDRSYDIYRDLVFGNEHFYDYFFESSPIKAISSFNIGSRPAARKTITEIGGLRAIPWVFSWSQSRVMFPGWYGVGSSFKEFINKNPENIAILRDMYQNWPFFQSLLSNVDMVLSKSNMNIAFEYAKLCEDEQVKAIYETILNEWQVTKNVILAIEGHDELLADNPYLKASLDYRMPYFNILNYIQLELIKRQRRGELSSDQERLIHITINGIATGLRNSG
The following text describes a protein:
Function:
Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis.
Subcellular Localization:
Chromosome, centromere. Nucleus.
Sequence:
MKMGRSREEGVRFKTLVFGHWELDHSFPPSFKSKNPTQGSEPRGQRYEACAVGPGRPPSASRSQPLVFEVEASAPLRPPSSTHAPIPHLRRPAPLLGSARAGGLKAMAESDPLEATFQRSLHIQKLKARDVTEDDVVRCMQKQAKIINGPGIGSDLDAQRREMPCVFLCSRCQRPLGDSLSWEGTDFEGNFFFLNAVSANVYVDKEQKLSTRKNEYGCMIETLSCNGCSLNIGQIYRCTPRHLDYKRDLFCFDVSSVDGYVLGSAENEAVPENEGPVTLDKQDVMESILKKLQVIMHGLELRVSLVESVVSGLCDTT
The following text describes a protein:
Function:
Involved in the intramitochondrial synthesis of acylcarnitines from accumulated acyl-CoA metabolites. Reconverts acylcarnitines back into the respective acyl-CoA esters that can then undergo beta-oxidation, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Active with medium (C8-C12) and long-chain (C14-C18) acyl-CoA esters.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MVARLLLLRARPRGPAGGPGPVCRRLSAGSGPREYLQRSIVPTMHFQDSLPRLPIPKLEDTIKRYLRAQKPLLDDGQFRKTEQFCKSFENGIGKELHEQLVAQDKQNKHTSYISGPWFDMYLTARDPVVLNFNPFMAFNPDPKSEYNDQLIRATNMTISAIRFLKTLRAGLLEPEVFHLNPAKSDTDTFKRLIRFVPSSLSWYGAYLVNAYPLDMSQYFRLFNSTRLPRPVRDELVTDESARHLLVLRKGHFYVFDVLDQDGNIVSASEIQAHLKYILSDSSATPDFPLAYLTTENRDVWAELRERLVSGGNEEALRKVDSAVFCLCLDDFPIKDLVHLSHTMLHSDGTNRWFDKSFNLILAKDGTAAVHFEHAWGDGVAVLRFFNEVFKDSTQAPAITPQSQPAHTDSSAAVRRLNFKLDDAMKASIGAAKDKFDAIVKTLTIDFIQFQRGGKEFLKNQKLSPDAVAQLAFQMAFLRQYGRTVATYESCSTAAFKHGRTEAIRPASIFTKKCSEAFVREPSRHSAGELCQMMAECSTYHGQLTKEAAMGQGFDRHLFALRYLAAAKGIALPELYLDPAYRQINHNILSTSTLSSSTVNIGGFAPVVPDGFGIGCIPGGLPSDSLDSWDLNSGRSQSRTTSNASSPFILLNSSHILSGLPRPSLSHHSVTPQQVPGSLQPLV
The following text describes a protein:
Function:
Component of the chromatin assembly factor complex (CAF-1) involved in chromatin assembly following DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. Required for several aspects of development, including seedling growth and leaf hair differentiation. Plays a critical role in the organization of shoot apical meristem (SAM) and root apical meristem (RAM) during postembryonic development by facilitating stable maintenance of gene expression states. Seems not required to maintain transcriptional repression of heterochromatic genes. Involved in heterologous recombination. May repress endocycle.
Subcellular Localization:
Nucleus.
Sequence:
MDEVSTVNENENRKTMIEPKKLNKRKREPTAIENLTSEEKESQISSLNLEMKGLFDYFREVMDKSKRTDLFSGFSECSSLNSMVALLMEEMSLPLSKLVDEIYLKLKEKTESVTMVAVKSAVVSVGQRVSYGVLNVDADVLEDDSESCLWCWETRDLKIMPSSVRGVLKLRRTCRKKIHERITAVSAMLAALQREETEKLWRSDLSKAAEKLGKILSEVDIRSFMDNMMQKNSSEMAEKDSKREEKLLLKQLEKNRCEAEKEKKRMERQVLKEKLQQEKEQKLLQKAIVDENNKEKEETESRKRIKKQQDESEKEQKRREKEQAELKKQLQVQKQASIMERFLKKSKDSSLTQPKLPSSEVTAQELSCTKHENEIGKVVQAIDNAFSTTCEATVDDIRREHFASWRQLGHLLSSSKKHWGMRRQPKSELFPKLKLSTNSGVTSDGEPNMEKQGDGCEENNFDGRQCKPSSSNRKKSRRVKQLLQFDKSCRPGFYGIWPSQSQVVKPRRPLQKDPELDYEVDSDEEWEEEEAGESLSDCEKDEDESLEEGCSKADDEDDSEDDFMVPDGYLSEDEGVQVDRMDIDPSEQDANTTSSKQDQESPEFCALLQQQKHLQNLTDHALKKTQPLIICNLTHEKVSLLAAKDLEGTQKVEQICLRALMVRQFPWSSLIEISINDIQDEDQEASKFSCSQSTPPSNSKAKIIPDSDLLTVVSTIQSCSQGINRVVETLQQKFPDVPKTKLRQKVREISDFEDSRWQVKKEVLTKLGLSPSPDKGGKRLPKTISTFFSKRCLPPSTKPQPAVEDAAERLENENA
The following text describes a protein:
Function:
Mg(2+)-dependent phosphatase that catalyzes the hydrolysis of the 1-position phosphate from inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate and participates in inositol phosphate metabolism.
Sequence:
MAALLKSLLAASEKAAHIAQLCRQEEALFSLLIEEKRGAEKNKKFLQDFKTLADVLIQEVIKHDVGKEFPELEDHILGEESNKFENGLGETVVVQVCPTQEDTAALLQKILDRNQTAADLLAAAIHQEVVLSDPAVDEMAVEISTENIAVWIDPIDSTNQYIRGRGHVMPVDGIYPSGLRSALVLIGVYDRHSGEPVLGIINEPFFQEDPQTHRWQSKYHWGISYKGTNLSSLSQPPLRTSPRVVLSSNEKPALQKALAPLYGEQLYFASGAGYKMLCVALGLADAYVLSEGSTFKWDSCGPHAILRALGGGIVDFLLSLQAWRAGQHKELPGLTYNKPAEGSVGAERWANQGGLVAYISQEHLKAVMATLVAAKDAF
The following text describes a protein:
Function:
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Subcellular Localization:
Cytoplasm.
Domain:
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Sequence:
MSDLESAYRLEYFEEEGFHRRECVSCGAHFWTRDGDRETCGEPPCEDYQFIDNPGFDASYSLTEMRSAMVSYFERAGHDSIDPYPVAANRWRDDVLLTQASIYDFQPHVTSGASPPPANPLVVSQPCIRMQDIDNVGKTGRHTMAFEMLGHHAFNADEGTDYAYDGEVYWKDTAVEHCEGLLADVGVSLDEVTFIEDPWVGGGNAGAAFEVIYRGLELATLVFMSLERDPDGEYEMKDGHTYAEMDRRVVDTGYGVERWTWMSQGTPTVYEAVYPDTIDFLKEQAGIEHTDEEAELVHRASKHAGNLDIDEVADIEDARAGIAAELGVDAERLTELVAPLEDIYAIADHSRVLAYMFGDGIVPSNVGTGYLARMVLRRTKRLVDDIGADVPLDELVDMQADRLGYENRDTIRSIVRSEVEKYGETLERGGRRVEQLAEEYADRGEPVPTDELIELYDSHGIQPGMVADIAADVGATVDAPDDFYSLVAARHDDGDSGAAGGDGGGDDRLADLPETETLYYDDAYGSEFEAVVLDVFEREGEDGDGAFDVVLDQTMFYPEGGGQPADTGVLTGDDHTVDVIDVQERDGVVLHRTTDNPGKGEFVRGQIDTERRRRLMAHHTATHIVVYAARQVLGEHVRQAGAQKGVDSSRIDVTHYERVDRETVKEIERVANEIVRANTSVQCEWPDRHEAEAEYGFDLYQGGIPAGEQIRLVHVDDDVQACGGTHVARTGEIGSIKILNAERVQDGVERLTFAAGAAAVEHVQGQEDDLRAAAEVLDVTPAEVPETAERFFTEWKDRGKTIDDLKEQLAEARASGGGAGEEVDVAGTTAVVQRVDGDMDELQATANALVDGGQVAVVGSGADGAQFVVGVPDGVPVNAGEVVGELAAMVGGGGGGPPDFAQGGGPDAERLDDALSRAADVLGDAASAE
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MDTLDGRKKLPANESMVDNQHNSLGDNSNVFKQEETPCKIGLVDQSTQKNKDDHCKDIWDEAKNSQDKISSNIDNPKKTYNNRVHVCYDCGKAFTRSSSLVVHKRTHTGEKPYECSTCGRNFTSTSDLTRHQITHTGERPYVCGECGKSYSHSSSLVIHYRIHTGERPFACDECGKRFACRSTLNAHQRRHIDEVTDRLINLKGRKFRSKNVFTKNHESCDAPGDTVANPEERKKIHRSFGILKHNSSLDSTTPCLEDDNFIKQGNSLEKSSCGILKISHSENCNQGHPAKQHTEIPKNTEPPRRIYFRRHQKKEFVRKVHVCDDCGKRFTRSSSLVIHKRTHTGEKPYECSICKKNFPSTSDLSRHQTTHTGERPYVCSQCGKRYTHASSLVIHQRVHTGERPFSCNQCDKSFTSRSSLVTHYKRHTGEMTLLCNVCGKGFLTKFHFALHQRTHTGERPFSCSQCGKRFSSRGALGRHEVIHTGERPYICKTCGKSYTRGSLLSRHERIHMEERSFVKIEPDSHIESTNSTS
The following text describes a protein:
Function:
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis. Over-expression of SigL induces 19-28 genes including polyketide synthases, secreted and membrane proteins. Might play a minor role in regulating SigB.
Miscellaneous:
MISCELLANEOUS: Extracytoplasmic function (ECF) sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning anti-sigma factor is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, Rip1), while cytoplasmic proteases finish degrading the regulatory protein, liberating SigL (Probable).
Domain:
The sigma-70 factor domain-2 mediates sequence-specific interaction with the -10 element in promoter DNA, and plays an important role in melting the double-stranded DNA and the formation of the transcription bubble. The sigma-70 factor domain-2 mediates interaction with the RNA polymerase subunits RpoB and RpoC (By similarity); The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-H) motif that mediates interaction with the -35 element in promoter DNA. The domain also mediates interaction with the RNA polymerase subunit RpoA. Interactions between sigma-70 factor domain-4 and anti-sigma factors prevents interaction of sigma factors with the RNA polymerase catalytic core (Probable).
Sequence:
MARVSGAAAAEAALMRALYDEHAAVLWRYALRLTGDAAQAEDVVQETLLRAWQHPEVIGDTARPARAWLFTVARNMIIDERRSARFRNVVGSTDQSGTPEQSTPDEVNAALDRLLIADALAQLSAEHRAVIQRSYYRGWSTAQIATDLGIAEGTVKSRLHYAVRALRLTLQELGVTR
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MAPPPAPLLAPRPGETRPGCRKPGTVSFADVAVYFSPEEWGCLRPAQRALYRDVMQETYGHLGALGFPGPKPALISWMEQESEAWSPAAQDPEKGERLGGARRGDVPNRKEEEPEEVPRAKGPRKAPVKESPEVLVERNPDPAISVAPARAQPPKNAAWDPTTGAQPPAPIPSMDAQAGQRRHVCTDCGRRFTYPSLLVSHRRMHSGERPFPCPECGMRFKRKFAVEAHQWIHRSCSGGRRGRRPGIRAVPRAPVRGDRDPPVLFRHYPDIFEECG
The following text describes a protein:
Function:
Mediates transmembrane potassium transport.
Miscellaneous:
MISCELLANEOUS: In the Saccharomyces cerevisiae heterologous expression system, a truncated protein containing amino acids 1-1094 localizes to the plasma membrane of the yeast cells, while a full-length protein localizes to both yeast plasma membrane and intracellular membranes.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Host cell membrane; Multi-pass membrane protein. Note=Localizes to the membrane of infected red blood cells.
Sequence:
MNNDNIGREPIDVVYDKRFSSRIKPKTKKKKRNENRMRLVRIQHYIYNIFTSFLCLFIVILILYASIDISINYGPVIILYILILELGSMLISYILLQFPFFYRKLKNTFMRARNINKYSHQYRPLYYDNNSFTDENESFNISDDEKKEKRKRKHTYSFMSSDGGRKRSNFRRFLSSYKSKKGNEFVNSKTMKNKTKKNTRRKGFLSFNWIGYKNGETNKNRNDNIVNDVYKKYNDDNKYNDDNKYNDDNYNDDDNKYNDDDILNSHSEQDQRKKKKKKKEKRIVVFPRNDTGGNSFKRESIYIDDCNMWMKKTMRKSNRPNFKLTRSLSFNINMNKDDDLMMKDSASLDNIQIFLGHRSSKFLREKNKLQKRKTSIYNKYVPLTFASSYKDDFFKEILKSQTDGIISSSSDYSSSSEDSNKNVYKTIYINNNNNNVDKKGKIDEEDNIVVRNNIHSNENIIIKENPYSLRNAILFHKEKRKYRKNINTLSDDDNKNFAFHSGKKKIKRKEKKRRCFIKLKCFNKIKNLYRFFINYNMKSSKSSNNLYLFFRGFYIYTKHRFVHYLSYEPIWIVAILIRIVLWCIVWIWAASYMERKPKNFEITEWNMKNVPSFYGYIECTFQWCGVFDYFFGLYFSNNKLKYIFSFFSLIDFITTPVSSLIMNFFVQDNINHNYWFLILGPLRFLRLVRAESTISSCFFWLNDVKIIIIGIIILALAILFTFSGIMYILEAPDIERDFVKPLDFVYFGVITMSTVGYGDYTPVTKAGKFLTMFIIITCISFVAAQFKRLKEAMFSPKTVMGIIPKQDDDYILILGPVSPTQLLYICKGINNSFPNSVESIFLFTPLPVVIYRYVYGSIVKNTNIKICISGGNECFICPSIIYDAVINSRALYILNNVDSEKYTLMYQQIFLASNNINFNNHDHQNQRISSDDILHNNIINKYSKDKTKNWKYSDLFSEYKNEINKNNMLNLEMNININNSYSIKEKDDQECLLRFIGTYNICNSLIPITLQLSNNTYEELIKSMNVYNYISIEELKYALLAKSVNCKGLFFLIINFFYKPKAVKSLKKYIIDLKLLMYNGMLRRKNRERLSSSNLKIKQPSQQKSRKGNLINKISLFFKKGQNHQLDAEGISHDEKNNSNTSRTRGNNRNDHMDPQIKGKGVFEMNQKEQKQVMLKEGMNKNMNKNIIKDMEKNMNSNGKDNINDSINESIEKNDLFFLNSLDPNDDRNIHNLSYKNYYYMLEKVNLNMYYYLEGLKYNIYRFQFPECMRGFLFQTASEYLYQKYSAFLIGIITINKEIFLNPVNYIIGEENKYFYTSAFSGIILTTSLDSLIKLSSINNISKKVYEYNKRLIEEKYKSTFSKSWINSDDDHHNSDHKNFVTNTQIKETQIDGDEVKIVLTSHDDSLHPSDRSVKNRKNSMKSIYNQKKSNLGDQKKKNRNQDDRTEHQVDDNNDSDYLQIESVPKKKRNMYYSLVLGICELENYISAYKDAFVDKDKPLLLVCGWPDNIHMFFKYLKRNVYNSSYRNKNNSNIHTYDNNNNNNNNNNIYSKTVKNKKGKRKKMKKLNDDIKYNIIILSLHVPKFNYENDLFNYSENVVFIRGSPLNSYNLIQAGVFYAKRIIILNSNHSLFIDKDAYRIDNEVIIIKNIVNQLFNYISKNKENYFNLLRKTFPKEYIDITINERIFLNDNINNSPNINEMIKGKMSDSSYDSLDDNYSSDDDSSSSNYDDDDEDNDNDEDNVDNNNDHGGESLLLKKKRKKKNMIKLKKRALNVNNIFNINKNPYLICLIKNSESLEYIDGSINLSYENYNDNEKMNKIWENCGEYIYTFELVSANIFVHEMLHNLVSFSLPISKYAIEYSVIYSLIGIDINEYSKNAQKFHKNLNLSTGYVNLVPIPSYFYKKSFYKCFSYFLHNKLSLCIGILRYIDISSLSNKSKKIFVLSCPSRTMKIEPHDQAYVIAHRM