lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Selects the target DNA sites for transposition. Recruits DDE-recombinase A to the target sites and catalytically activates it. Displays non-specific DNA-binding properties. Polymerizes as helical filaments around the DNA. Coating of the DNA by the target DNA activator B might play a role in favoring target-primed replication over integration. Prevents self-integration into an integrated copy of the viral genome. This mechanism is called target immunity and is achieved by two mechanisms: first, the target DNA activator B dissociates from the viral genome ends upon interaction in cis with DDE-recombinase A, which makes the viral genome ends a poor target for new insertions. Second, the interior of the viral genome may also be protected from integration events by the target DNA activator B being strongly bound throughout the whole viral genome.
Subcellular Localization:
Host cytoplasm.
Domain:
The N-terminus region contains a putative DNA-binding region that allows filament-filament interactions and probably favors MuB polymerization and filament clustering. The central region contains the ATPase module. The C-terminus comprises four helices arranged in a loosely packed bundle which can bind to dsDNA.
Sequence:
MNISDIRAGLRTLVENEETTFKQIALESGLSTGTISSFINDKYNGDNERVSQMLQRWLEKYHAVAELPEPPRFVETQTVKQIWTSMRFASLTESIAVVCGNPGVGKTEAAREYRRTNNNVWMITITPSCASVLECLTELAFELGMNDAPRRKGPLSRALRRRLEGTQGLVIIDEADHLGAEVLEELRLLQESTRIGLVLMGNHRVYSNMTGGNRTVEFARLFSRIAKRTAINKTKKADVKAIADAWQINGEKELELLQQIAQKPGALRILNHSLRLAAMTAHGKGERVNEDYLRQAFRELDLDVDISTLLRN
The following text describes a protein:
Function:
Plays a role in the regulation of the cell cycle by phosphorylating the nuclear envelope protein barrier-to-autointegration factor/BAF that is required for disassembly and reassembly, respectively, of the nuclear envelope during mitosis. Under normal physiological conditions, negatively regulates ERK activity along with VHR phosphatase in the nucleus, causing timely and transient action of ERK. Stress conditions activate CDK5 which phosphorylates VRK3 to increase VHR phosphatase activity and suppress prolonged ERK activation that causes cell death. For example, upon glutamate induction, promotes nuclear localization of HSP70/HSPA1A to inhibit ERK activation via VHR phosphatase.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Under oxidative stress, migrates from the nucleus to the cytoplasm.
Sequence:
MISFCPVCGKSVKVSFKFCPYCGKALPVEEDGGTQSAVTPHVSSVPGSRRDLNSSFETSPKKVKCSHTVTSLPLSRHSDCDSSGSDNTLTSPDRATGTRSRPLTPKGSPLSNRQSPQTLKRTRVTTSLQALATGTELTDQNGKHWTLGALQIRDDQGILYEAEPTSAVPSESRTQKWRFSLKLDSKDGRLFNEQNFFQRVAKPLQVNKWKKQFLLPLLAIPTCIGFGIHQDKYRFLVFPSLGRSLQSALDDNPKHVVSERCVLQVACRLLDALEYLHENEYVHGNLTAENVFVNPEDLSQVTLVGYGFTYRYCPGGKHVAYKEGSRSPHDGDLEFISMDLHKGCGPSRRSDLQTLGYCMLKWLYGSLPWTNCLPNTEKITRQKQKYLDSPERLVGLCGRWNKASETLREYLKVVMALNYEEKPPYATLRNSLEALLQDMRVSPYDPLDLQMVP
The following text describes a protein:
Function:
Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors.
Subcellular Localization:
Nucleus.
Sequence:
MSAEQNGSAMTEAQEQLKNFWIKTMDDINNLKSNEFKTQELPLARIKKIMKMDEDVKMISAEAPVLFAKAAEIFINELTLRGWVHAEDNKRRTLQRNDIAMAITKYDQFDFLIDIVPREEIRPAKKEDALETNKMFYVVDQPAPTPQLQVQASQVIPQQIQLLQGSNGVILSQPVIDATHHQLQQQQQQQHPAQQIIQLQAAPQQAAQQTITQTQQQQQLQQQLQQQQLQQQQQQQQQTMQVFTQVVGPNGDVQQIPIQLTPSQLQQIALQMQGKQPGQQIVIHTAGTIDQSNSTNATTIDQSQQQQQQQQQFNTQTIYSQIPMYSQNSG
The following text describes a protein:
Function:
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Subcellular Localization:
Cytoplasm.
Sequence:
MTDSVVTRFAPSPTGFLHIGGARTALFNWLYAKKHGGKMLLRIEDTDRERSTEAAIGAILDGLKWLELGWDGDVIYQFSRAARHREVAEQLLADGKAYRCYATAEELTAMREKARAEGRTRLYDGMWRDRDPATAPSDVKPTIRLRAPQTGETVIEDQVQGRVVWQNENLDDLVLLRGDGNPTYMLAVVVDDHDMGVTHVIRGDDHLINAARQKQIHDAMGWALPSMSHIPLIHGPDGSKLSKRHGALGVDAYRAMGYLPAALRNYLVRLGWSHGDQEIFSTEEMIAAFDLSSVGRAAARFDFAKLENLNGHYIRHADDQSLVKMFEDVLDHVVPSRDELKAKLNDTTRAQLLKAMPALKERAKTLIELIDSAYFIFADRPLELDPKAQALLTPDNRKLIGQLHSALENVETWSGATTEAALRAFAEENSLKLGAVAQPLRAALTGRTTSPGIFEVLDVLGRQESLGRLKDQAKD
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase.
Subcellular Localization:
Cytoplasm.
Sequence:
MTIIADEIPIKRIKLPTDVPFWESTIAYHRVFQTLHLLNDSIKRMSFDSPKIKVTPKIESILKQIEQLSKFIDEIPPVNLEKSRYGNISFRTWHKRVEEYSVDFHKAILPEELYPFISEFHGYLMDSFGSPVRIDYGSGHELHFFCWIVLLVQLKVINEEEYPAIILKVFRNYLYLCRKLQNVYRLEPAGSHGVWGIDDYQFLPFIFGSAQLIKHPYLKPDSILDKSLVSLYEHDNFYFDCVAYIYKVKNRAPFFESSPDLFNISAAESWEKINKGMFTKYHAECLDKYPIVQHFLFGKLLPYELLVRGSTPKHEEVKENAQIN
The following text describes a protein:
Function:
Negative regulator of the osmotic stress response. Acts via the transmembrane protein ptr-23.
Subcellular Localization:
Secreted.
Sequence:
MPAKMLKWLLIHIFLIHSIFCQDAPAQMPFFANSDPMMSKLSQIQFADAPTLKGDKYPDVDAHRIIAPIISPIMEVFDQMKENQRARDQAEKIRKDREDHPLSTSRSLWEMFQRLQRPTTTTTEAPPLIERLFKPYIEPWQKQLDDFSKDMAGITLIPTTTTTPAPTTTTTPNFLEKSLSMFFPSLRRKPQSIPTLPPTTTPTPRLFDPEMFDRLFFKRDKRQATIAPAPKFDIFTVPPPPPLFQEWEKPILSLSNPFTLNPLMKMFTTPSPPQTLAPLPKIPEPNPYEIKKGLPEPQFKLQDPFYNPLFPSRKSKMFDFLAGGEAGRLLG
The following text describes a protein:
Function:
Involved in countering the first line of host defense mechanisms. Specifically inhibits the response of human neutrophils and monocytes to complement anaphylatoxin C5a and formylated peptides, like N-formyl-methionyl-leucyl-phenylalanine (fMLP). Acts by binding directly to the C5a receptor (C5aR) and formylated peptide receptor (FPR), thereby blocking the C5a- and fMLP-induced calcium responses. Prevents phagocytosis of the bacterium.
Miscellaneous:
MISCELLANEOUS: Encoded within a prophage region.
Subcellular Localization:
Secreted.
Domain:
Two distinct active sites are responsible for anti-C5aR and anti-FPR activity. They might be closely spatially related and might be overlapping.
Sequence:
MKKKLATTVLALSFLTAGISTHHHSAKAFTFEPFPTNEEIESNKKMLEKEKAYKESFKNSGLPTTLGKLDERLRNYLKKGTKNSAQFEKMVILTENKGYYTVYLNTPLAEDRKNVELLGKMYKTYFFKKGESKSSYVINGPGKTNEYAY
The following text describes a protein:
Function:
As part of the nuclear pore complex (NPC), has a role in its assembly and function; (Microbial infection) Required for optimal replication of E.chaffeensis.
Subcellular Localization:
Nucleus, nuclear pore complex.
Sequence:
MRSVIEPDHSIQLNEAIYCYDICTNDFAYNLIAVAFRKHLSLLLVGLPEESGEFGYTRLQDMDLGEKEQRSVSALAFSPDTSLNCTPNNVTLCAANGSQLKLYRTDLGQFTSLQVLRGHGDYVNDVSWVCDGELLASVSDDFTCRFWTTTGGGENVITFGLSSAGMSVKSHPEDPNKVLVAEKKGIIHLYNVTLKQTVISVESPKFPLMSADWAHSNRLFITSLAGGDVVTWDLNRPYVPADVKQVHEDCGRVVRFAPGSSEMVIAMVIGLTLKVFAAKSTVPLLEASLKSYGGMAWHQRLPYISAVSDRKLLFWKVQMK
The following text describes a protein:
Function:
Calcium-independent membrane-associated phospholipase that catalyzes complete diacylation of phospholipids by hydrolyzing both sn-1 and sn-2 fatty acyl chains attached to the glycerol backbone (phospholipase B activity). Has dual phospholipase and lysophospholipase activities toward diacylphospholipids. Preferentially cleaves sn-2 ester bonds over sn-1 bonds. Acts as a lipase toward glycerolipid substrates. Hydrolyzes fatty acyl chains of diacylglycerols with preference for the sn-2 position and of triacylglycerols with not positional selectivity. May also hydrolyze long chain retinyl esters such as retinyl palmitate. May contribute to digestion of dietary phospholipids, glycerolipids and retinoids, facilitating lipid absorption at the brush border.
Subcellular Localization:
Apical cell membrane; Single-pass type I membrane protein.
Sequence:
MRMLKVIIFSLCLHQAYGLDWFDNYMSGLKTQIPMYGLQEFPEKAKNGSSHNEVLICPDMSPSAEVPTTVEKVKPADVKVVAALGDSLTTAIAANATSVLEIPNEYRHLSWSIGGFGNISDVTTLPNILKLFNPNIVGFGKRKTVSYKPAPLEDTGLNLAVTGANTFNLPEQTQHLIDTMKSYPGVNFKEDWKLVTIFIGSNDVCDYCKNKTLFSADSFIHNLTVSLDMLQQQLPRAIINVVQLLRIEELRSVNDKSLGCLLQRSFCSCVAVPNENSTEFQEILDQMTQFQEKLERLFLNSTRFNGKKDFAVILQPFLKHAKPPTDQNGTVDYSYFTPDCFHLTIKGHEQLARALWNNMLQPQGDKYYLKTLSDPIPLLCPSKDHPYFYTRNQASGYSASHHLIGLLVFATLLVYL
The following text describes a protein:
Function:
Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.
Sequence:
MSGRTVEEIYQKKTQHEHILARPDMYIGTIEPVTEDVWVYDEADNVMKLRKCTWTPGLYKIFDEILVNAADNKVRDPHGQTTIKVWVDAARGLVRVYNNGEGIPVQRHREHDLWVPEMIFGHLLTSSNYDDTEAKVTGGRNGFGAKLTNVFSTRFEVETVHSRSRKKFFMRWRNNMLENEEAVITPCDGPDYTVVTFYPDFEKFNLEGFTEDMVLIMQRRVYDIAGCTDKSLCCYLNDTRIACRSFPEYVDLYPTMGEERKPSSYSRVNDRWEVCVRVSNVGFQQVSFVNSIATTRGGTHVKYIVDQIIAKVTDQAMRKSKTEVKPHMIRPHLFIFVNSLIENPSFDSQTKETLNTPKARFGSTCDLPASLIDCVLKSSIVERAVEMANSRLNREMAMKMRNTNRKQILGIPKLDDANEAGGKYSQRCTLILTEGDSAKALCTAGLAVENRDYFGVFPLRGKPLNVRDASVKKVMGCAEFQAVSKIMGLDLSQKYTSTEGLRYGHLMIMSDQDHDGSHIKGLIINMIHNYWPDLLKVPGFLQQFITPIVKARKKGRGNNDEGTISFFSMPDYFEWKNAVGEGIKNYELRYYKGLGTSGAKEGREYFENIDRHRLNFVYEDRKDDDDIVMAFAKDKVDERKRWITEFKANTNINESMNYNVRNVSYSEFVHKELILFSVADCERSIPSVVDGLKPGQRKIMFSAFKRNLVRSLKVAQLAGYVSEHAAYHHGEQSLVQTIVGLAQDYVGANNVPLLYRDGQFGTRLQGGKDHAAGRYIFTRLTDIARRIYHPSDDFIVEYRDDDGLSVEPFYYVPVIPMVLVNGTAGIGTGFATNIPNYSPLDVIDNLNRLLSGEELQPMKPWYFGFTGTIEEREKGKFVSSGCATVRPDGVVHITELPIGTWTQQYKKFLEDLREREIVIQYREHNTDVTVDFEVFIHPEVLRQWVAQGCVEERLQLREYIHATNIIAFDREGKITKYLDAESVLKEFYLVRLEYYARRREFLLEQLQRAALKLENMVRFVNEVIDGTFIVTRRSMKDVLKDLKQRGYTPFPPQQKKKMSSTTIVDEEDNDGARKILPDVFEFESVPLCEQVIGKILCTAEPEEINMWKGVLVEYDYLLSLRMVDLTVEMAMYFRTKREQMLNKHNFVLSASSKDLWREDLDLLRSDIEKLFDERRREIALIQCKKLEKRQFFDVSRLRVPLLSDAARKADRSLALRQSNCKREMSSKCASESFALLVDAGVRVSGLTEGSSICDINEARRKYGHSVAGGKRRLVRHDEVSKRGKFSSCGDQRHVSLSDGSDTDDCSIGAPSVSPSDATPATQKSRKISDSSYGFGIEGEVDIFFEDTVGEDFSEPATQANIVRSKSESPVLDFSAEYATEPKSRKRPRSIEDNDENTCPFYVDVVGEDVEYDSDQCIGFDACVF
The following text describes a protein:
Function:
Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network.
Subcellular Localization:
Virion membrane; Multi-pass membrane protein. Host Golgi apparatus, host trans-Golgi network. Host endosome membrane; Multi-pass membrane protein. Host nucleus inner membrane; Multi-pass membrane protein. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs.
Sequence:
MGRPAPRGSPDSAPPTKGMTGARTAWWVWCVQVATFVVSAVCVTGLLVLASVFRARFPCFYATASSYAGVNSTAEVRGGVAVPLRLDTQSLVGTYVITAVLLLAVAVYAVVGAVTSRYDRALDAGRRLAAARMAMPHATLIAGNVCSWLLQITVLLLAHRISQLAHLVYVLHFACLVYFAAHFCTRGVLSGTYLRQVHGLMELAPTHHRVVGPARAVLTNALLLGVFLCTADAAVSLNTIAAFNFNFSAPGMLICLTVLFAILVVSLLLVVEGVLCHYVRVLVGPHLGAVAATGIVGLACEHYYTNGYYVVETQWPGAQTGVRVALALVAAFALGMAVLRCTRAYLYHRRHHTKFFMRMRDTRHRAHSALKRVRSSMRGSRDGRHRPAPGSPPGIPEYAEDPYAISYGGQLDRYGDSDGEPIYDEVADDQTDVLYAKIQHPRHLPDDDPIYDTVGGYDPEPAEDPVYSTVRRW
The following text describes a protein:
Function:
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton. Note=Septum.
Sequence:
MSINLNELVDSLIQSAPPAELKQVSQSLSSLTKGTSTSSTNSLIQDSIEQYAQENIISIDNIIISKYNKDENSSKYIDYVNNKLFNVDWQNQKIIDVESYHDNNNKRGSNYDELIQKLSQYGDDYYPSNFAFTVIPESEDQLRVIIIGQRANHDNFYTGQWKSNYLITEQGIKGNIDLDIHYFEDGNVRLKFNESINSSNNNNNSSTLQSGNLINNASRIVNFINEQENATMVKIIEQFNNLNQKSFKNLRRLLPVTRSKINWGSAIGNYRLGSDVINKK
The following text describes a protein:
Function:
Involved in nicotine degradation. Catalyzes the deamination of pseudooxynicotine to 3-succinoylsemialdehyde-pyridine.
Subcellular Localization:
Periplasm.
Sequence:
MANDKGDISKDGVSRRKFLGGAVIGAAAAAGVGSQILSLSATAQGADKERVGPLQSNVDYDAVVIGGGFAGVTAARELSRSGLKTLVLEGRSRLGGRTFTSKLDGEKVELGGTWVHWTQPNVWTEVMHYGLEIEETVGLASPETVIWVTDNQVKRAPAAEAFEIFGAACTEYYKEAHNIYPRPFDPFFAKKALQEMDGLSASEYLNKLSLTREQKDMMDSWLSGNGHNYPETIAYSEIMRWFALSNFNMPTMFDSIARYKIKSGTVSLLEAMVAESDMEVQLSTPVLKVKQDSHRVLITTEEGTIAASAVVMAVPLNTMGDVEYSPRLSDAKSEIASQGHAGKGVKGYIRIKQDVGNVMTYAPARNDVTPFTSVFTDHVGENGTLLIAFSADPKLVDINDSKAVEKALHPLLPGVEVTSSYGYDWNLDPFSKGTWCTYRPGQTTRYLTELQKREGRLFFAGSDMANGWRGFIDGAIESGREVGYQVASYLKGKNSNA
The following text describes a protein:
Function:
Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
Sequence:
MTCSLSKKDRNSDAKTKAACKISITKLKKIISLPDSNAKEKKPNMMKRKSLSEGYDEKKKKKKKKQDSHEEKEKHNSFSAPLVIKEQSEHDSDAKEKKPHMVKRKSLPDGYNEKKKKKKQESPEKKEKHRSFSAPLVIKEPSEHDSDAKEKKPYMLKRKSLPDGYNEKKKKKKQESPEKKEKHRSFSAPLVIKEPSEHDSDAKQKKLKRKSTSESYDEKMKKPLIIDEEPEEFTTKMLIGESSRSSCGICFDLKTDLDMFKRKSCNHLFCVDCISKYVDSQLNNNVVKVTCPTPNCSAKLLPRHLQHILPKEFIDRWELAKYESKIALEQKTYCAFKDCSVLLVNDNDRGEVLTSCECPSCHRLFYAQCKVPWHAEMNCQEFQDLKHNTNEVDLDDKFLKLAKRNKWQRCPNCSIYVKRRSGCEHMKCRCKCNFCYLCGKKWKHGHLCKKRERLLG
The following text describes a protein:
Function:
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across the thylakoid membrane. Involved in delta pH-dependent protein transport required for chloroplast development, especially thylakoid membrane formation. TATC and TATB mediate precursor recognition, whereas TATA facilitates translocation.
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Single-pass membrane protein.
Sequence:
MVISSPTLSFTSSIPKLPPSLSPSFSSSKSAFFANNATTSFFTYGDHNHSSLLRLTSFRTTTKTTHKGFTCNALFGLGVPELVVIAGVAALVFGPKKLPEVGKSIGKTVKSFQQAAKEFESELKKEPEPTEETSVEKPTSTEAEERQDLKVSNQKETV
The following text describes a protein:
Function:
Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the third and last glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Glc(2)Man(9)GlcNAc(2)-PP-Dol to produce Glc(3)Man(9)GlcNAc(2)-PP-Dol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MDAKQAQLFTSSAAFSAFAASVLLVSDQIKTRVPDPYMDEIFHVEQAKTYCAGQWTTWNNLITTPPGLYIVPSLLHQALPKWFLCSTNHLRWMNAALLCAFPLLISRILSHFRTTPYPPRPGVKPRVRFLIPEDEIILEAIIISCFPITYFSGFLFYTDLGSLFAIIASYDQSLAGRHVLAALLGLWSCLFRQTNIAWVAFIAGSALINHLRQINNTGPSTPKCSQVNHAKRTHRPSQPYDLSLTSASLLDLPRAIRSLVFESFTNFSSTLPIVLPYAGVVVCFVIFVLWNGGIVLGDKSNHITALHIPQLYYFAGFSMAFLVPVSFDLFLIRRTLKSLFGSPRSFFLSCCLFVTILWTIHKFTYEHPFLLSDNRHYTFYVWRRIFKFHRLVKYLFTPGYMICVKMIWERIARSFTMNLLITTFYIIALGLTLIPSPLLEPRYFLVPYVLLRLHIRPVVEETKTWSIRVFTEGCLYALVNLVTITVFLFRPFKGRPGEWEGTWQRFMW
The following text describes a protein:
Function:
Insulin-regulated facilitative hexose transporter that mediates the transport of glucose and fructose. Facilitates hepatic influx of dietary trehalose, which in turn inhibits glucose and fructose influx triggering a starvation signal and hepatic autophagy through activation of AMPK and ULK1. Also able to mediate the transport of dehydroascorbate.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MATIQTDTGMDPDRDRDTAPILGGDGGNRRREQVRNQFLATFVSTLGPLAFGMVLGYSSPALPDLQKETGAVHMDSYHGSWFGSLSAIGAMFGGPLGGWCIEALGRKTSLMTAVLPFTAGWLILAYAQNLAMLYVGRLLTGIAAGMTSLTVPVYVAEISSPRVRGLLGASFQLMVTIGILLVYVFGNFLHWRWLAIVCLVPAVILIIAMAFMPETPRWLLAKGRRPAAVTSLLWLRGPDVDVEDECADIESNLQQQETMSWREFTQPSLLKPFAIGMALMFFQQFSGINAVIFYSVSILEDAGVEGHTGAIIVGAVQVVATFVACLLMDKMGRRILLIVAGVGMAITSVTFGLYFQLEQNNNHNATLTAPTATPAPGPDLSWLSLTSMIVYIIAFSLGWGPIPWLMMSEIFPARARGTASGIATLFNWFGAFIVTKEFNDMVAAFTEQGAFWFFAGICVLGVLFVCFLVPETKNVSLEEIEAYFEGRGRAGSALQRSPFSAPPGEDT
The following text describes a protein:
Function:
Constituent of COPII-coated endoplasmic reticulum-derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Note=Recycles between endoplasmic reticulum and Golgi.
Sequence:
MAFFNVFKAVLCAYFISVVFGHGITLKPHQRECFYENLRNNDQMSVTYQTNVGGDQLVSMSIYNPAGQIMHQEVPNSMAQYSFTVKNPGKYMYCFYNDALDGESKEVLFNVHGVIYISDEDLDANNPLLGKVRQLHDTISKVKHEQEYFVARERIHRNTAESTNDRVKWWSILQTVILVSVCVFQIFYLKRLFEVKRVV
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that methylates the delta-nitrogen atom of arginine residues to form N5-methylarginine (type IV) in target proteins. Monomethylates ribosomal protein L12.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSELHDLCKFPTRPIDQSYIDKLTQYLKDGIPATYTIEEAYNYINNIEEEPTTTTTPLHLICSHAPFDITKEEQEIISTMVEKLFEYGAGWSFTDINNQTPGCILISRRKERENKEEDGKWMNDVYQQIIDAGVRAELLLRKVNEFEEIEFIEEDDEQEEKEEEDIPQLVKDEQEIKEEAKQEQTTTTDIKPVVIDDAPDAPSQNQQSYLNTKLEYINDALITKDDKDGVMMAWENDIMKLASDTITSSASSASDSESEQEVNILNIGFGMGIIDAMIQSKLKSHPNAKHYICEAHPDVLQKMKIDGWYEKPNVIILEGRWQDKLNDLLSSSSSSSEASVFFDGIYYDTFSEHYQDMLELFDIIVGLLKPHGIFSFFNGLGADRQIIYEVYKNLLIIDLENYGLNCQFKEFNVPNEKFWNKLQDKSIWDDVKRSYWSCPIYYHPIIKFIDY
The following text describes a protein:
Function:
Acts as a transcriptional activator that mediates transcriptional activation by binding to E box-containing promoter (5'-CANNTG-3'). Acts as a differentiation factor during neurogenesis. Induces photoreceptor cell overproduction in vivo and de novo generation in vitro. May play a role in photoreceptor cell production.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MTKSYSESGPAGEPQAQAPPGWAAGCLSPPADGPEADKKEEDLEALHGEAEEDALRNGEEEDEEDELDEEEEEEEEEEDDEQKPKRRGPKKKKMTKARLERFKLRRMKANARERNRMHGLNAALDNLRKVVPCYSKTQKLSKIETLRLAKNYIWALSEILRSGKSPDLVSFVQTLCKGLSQPTTNLVAGCLQLNPRTFLPEQSADAAPHLPPAGAPFAPPPFPYASPGLPSPPYGTMDSSHLFHLKPPHAYGAALEPFFEGGLPEGAGPAFDGPLSPPLSINGNFSFKHEPAADFDKSYAFTMHYPAGPLPAAPAHAAVFSGAAARCELPGDGLAPYEGHPHHERVLSAQLSAIFHE
The following text describes a protein:
Function:
Methylates ribosomal protein L11.
Subcellular Localization:
Cytoplasm.
Sequence:
MQTTSWLEIAVEVDPEAVETVSEILARYGYNGGVVVEQSWIAGDEGPEFQYDPNRPVWLRTYLPLDAQAEETRQQIEHALWHVHQIRPLGPIQTRTLAEEDWANAWKQFYPVLRVGERTVIVPSWLEYQPQPNDVVLLLDPGMAFGTGLHPTTRLCLHLLERLVQPGQQVLDLGTGSGILAIAAAKLGAGQVLALDNDPIAVRVAHENVERNQVQDLVTVAEGSLGAGQAMGHWLSGDFGPETPDPTLHDNTPQATFDLIAANLIAKVLVLLAPDLATALKPGGLLISSGIIDVKEAEVVAAFAAVGLQQIERHVEGEWVALVHRRPQ
The following text describes a protein:
Function:
Catalyzes the hydrolysis of ATP coupled with the transport of calcium.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MILIALRDLIGVGVQEKFRTALNVQRAALHFHPTAIADPDNVGVRVDGFDIDPDSIASLVHNYDNNGFKKINGVEGIARKLRVSVAAGVREDSLNTRQLYFGFNRYAEKHAKPFLKFVWESMLDSTLIFLMVCSIVLIGGKFATEGLLVNVYDEVGIILGVFFLVVFTSVNDYHQSLKFCEWDRENKNISVKVTRDGKRQKISIYDLVVGDIVHLSIGDQIPADGICISGSNLHIDESSLTGQVDPVYVNQENPFLLSGTKVIDGSGKMLVAAVGMRTEWGKLVEVLNDVGVEETPLQVKLNGVATIVGKIGLSFSLLTLAVLVIQFFVDKATRGDFTNWSSKDAMKLLNYINILVTMIVIAVPEGLPLAVTLNLAFATKSLTNDRALVRHLSACETMGSASYLCLDKTGTVTSNCMVVNKLWISGEVVEMKDNRNGNKLKGKISEEVLNILLQALFQNNASEMVKDKQGKTTILGTSTDSALLEFGLLLGEDDSLVSLPNGGLRVFCKGASEIIIKMCEKIIDCNGESVDFLENHAKHVEHVLKDFASEPLRTISLAYKDINVIPTENNIPDNGYTLIAIVGINDPIRLGVKDVVQTCLAAGVTIAMVTGDDMNIARTIAKECGILTNNGLTIEGQEFRNLSTMHMKVTIPQIQVMARFLPHDKHSIVASLKDMFGEVVAVTGDGISDAPALHEAHIGVAMGLSGTEIAKENADIILMDDNITTIVNIIKWGRAVYINIQKLVQFQLTAIIVALVINFISASVTGYVPLTAVQLLWVNLIMDILCPLALVSEPLNDELMKRPPVGRGEKFITNAMWRNIFGQSIYQVIVLVVLNFEGKNILSISGSNATDVLRTLIFNSFIFFQVFNEINCREIEKINIFKGILNSWAFLVIIFSTVAIQVIIVQFLGNFACTVSLNLELWLISVLIGATSMLIACLLKCFPIERHVSIRRDGYQALSAQP
The following text describes a protein:
Function:
The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MPIMSVCRPLQDVARYSRQRFCMCAQEGAVIHSSCHLFTVEETERCRDRNMAASVKAAHELQSRTRTDDVLISGGVEFSSLLLSKPVLEGLSASGFQRPSPIQLKAIPLGRCGLDLIVQAKSGTGKTCVFTTIALDSLILENATTQVLVLAPTREIAVQIHAVVMAIGSAMEGLECHVFIGGRPISQDKQHLKKCHIAIGSPGRIKQLIEMGALMVSSIRLFVLDEADKLLEDDSSSSFQEQINWIYSSLPANKQMLALSATYPESLAQQLSRYMREPTFVRLNPTDPGLLGLKQYYKIVPSHSLPHKVFEEKVQSLLELFSKIPFNQALVFSNLHTRAQHLADILSSKGLPAVCISGGLSQDQRLEAMWKLKQYQCRVLISTDLTSRGIDAEKVNLVINLDVPQDWETYMHRIGRAGRFGTLGVAVTYCCHGEEENKMMAIAQKCSLDLMHLPDPIPPGIMEEACDHDVIIETLSKPKIPDNFKPEKKKKAKSEQMKSKPSRESHISVVITESVTGDKSCSRAETKTKNHSSKPGRQKQMAPAANLQHDSTITQKQQNDTLPKIPPLSSFKSHTGKRITFDDALVDYETFIREGPGRSVEIIHQYDGFYRSQDKVNGLHDAHDEDEASESYVLEESQSHQDLPPAQEVSELSSEQKTSSESSSESEMEVESESSSSVPSKSTLEALPDNKVSLVRNHSELAELALPSTRVPQQATRSKKRPCQPQSQDTAHHHNLPHKHRTASKSSRRPTGPKRRTRETDETEEEEAGQDYWSSYRAWAEYYNSYYHHSPYNWMTAFYMNSVYIKEMMKH
The following text describes a protein:
Function:
Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.
Subcellular Localization:
Host cytoplasm. Note=The endolysin is cytoplasmic, but can reach the periplasmic space with the help of the holins which disrupt the host cell membrane.
Domain:
LysM domains are thought to be involved in peptidoglycan binding.
Sequence:
MQISQAGINLIKSFEGLQLKAYKAVPTEKHYTIGYGHYGSDVSPRQVITAKQAEDMLRDDVQAFVDGVNKALKVSVTQNQFDALVSFAYNVGLGAFRSSSLLEYLNEGRTALAAAEFPKWNKSGGKVYQGLINRRAQEQALFNSGTPKNVSRGTSSTKTTPKYKVKSGDNLTKIAKKHNTTVATLLKLNPSIKDPNMIRVGQTINVTGSGGKTHKVKSGDTLSKIAVDNKTTVSRLMSLNPEITNPNHIKVGQTIRLS