lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Supplies decaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinones ubiquinone-10.
Subcellular Localization:
Mitochondrion.
Sequence:
MSFPFASLLKRPSAISSLLSLKKPGSWSSILLKAVGVLSRDSRWHSDLLKMLTEEMDSLNGQINTWTDNNPLLDEITKPYRKSSTRFFHPLLVLLMSRASVNGDPPSQQLFQRYKQLARVTELIHAANIIHINIGEEQSNEQIKLATLVGDYLLGKASVDLAHLENNAITEIMASVIANLVEGHFGSRQNGSVGLSNERTILLQSAFMPAKACLCASILNNSSQYINDACFNYGKFLGLSLQLAHKPVSPDAQVLQKNNDILKTYVENAKSSLSVFPDIEAKQALMEIANSVSK
The following text describes a protein:
Function:
Could be involved in resistance to puromycin, acriflavine and tetraphenylarsonium chloride.
Subcellular Localization:
Cell outer membrane; Lipid-anchor. Membrane.
Sequence:
MKNSVQTVGLLHKAAPYFTASLLSAFVLTGCSVPDHYPDLATMWEANELSSTNTFSHQAEMDWPSANWWQRYQDAQLNHLIEEALQHSPSLEMAMARLKGAQGFARQAGAIRSFDLGLAASATESKVSERYQSATPPDGWNDYGTLTLNFQYDFDFWGKNRAAVVAATSELAAAEAESVAARLMISTSIANAYAELARLYANQETVHAALQVRNKTVELLEKRYANGLETLGSVSQAKAVAASVEAELLGIQESIQLQKNALAALVGQGPDRAASIEEPHITLTSRYGLPSEAGVGLLGHRADITAARWRAEAAAQQVGIAQAQFYPDVTLSAFIGYQAFGLDHLFDSGNDAGAIGPAIYLPLFTGGRLEGQLTSAEARYQEAVAQYNGTLVQALYEVADVVTSSQALQARINKTEQAVQQAEQALHIATNRYQGGLATYLDVLVAEESLLNNQRALVNLQSRAFSLDLALIHALGGGFETTES
The following text describes a protein:
Function:
Component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity; Non-catalytic component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MECVLGVVGRDFALVAADTSAVQSILVHKTDEDKVMVLDSQKLMGASGEPGDRVQFTEFIQKNLHLYQFRNTIPLSTAAAANFTRGELATALRKNPYMVNIILGGYDKDVGASLYYIDYIATLHKIDKGAFGYGSYFCLSLMDKLYHPDMTVEEAVDLVDKCIKEIRLRLVVAPQNFVIKIVDKDGAREYARRELVGDNAPAEAATAVVAA
The following text describes a protein:
Function:
Dicer-like endonuclease involved in cleaving double-stranded RNA in the RNA interference (RNAi) pathway. Produces 21 to 25 bp dsRNAs (siRNAs) which target the selective destruction of homologous RNAs leading to sequence-specific suppression of gene expression, called post-transcriptional gene silencing (PTGS). Part of a broad host defense response against viral infection and transposons.
Sequence:
MDNCTRNQKIPMAKTNALFEPHPQLFISQTDIIPSKIIASNPEAYPDIGGSLVDDQHEVEGYLDGLTSGKISNEIVEDLCSSTTESAIENEDAISEEEKGKNVTVTPRTYQLEMLEESLKGNIIVAMDTGSGKTHVAVLRILAELERMEPDKLIWFLAPTVALCTQHNEYLQLNISSVLVKLLVGSDGVDRWTEQRQWDAILKDVKIAVSPYQVLLDALAHGFVRMERLSLIIFDEAHNCLNKAPGAKIMTSFYHPYKSISPLPHILGLSASPVIRSDPQSLSKIEETLDAVCRTPKIHQADLRLRVKLPILSIIEYNPEPEYLMTKTVASLGKVIQDLNISEDPYVLALKSSGSEKSQRELAKLLNNYKTNSQRELRLIYNTGKTILVELGSWAADYYISAVVTKYLKTMKAREVFVVMDLAATERLYIAKALKQVGISPSVFSLADKTSDKVAKLLNIILQQEPPFSAIIFVEERATVFVLADLLSQHPLTKERFKIGTMVGSSSNSKRTQIVGELVDLDKQKDTLSRFKLGKIDILIATNVLEEGIDVRACNLVICFSKPSNLKSFIQRRGRARQQDSKLILLDPLGGKVIDWHELERNMRKMYENEMRELQHISEIETADEQSEDGRVLRVESTGAQLDLDNAVPHLYHFCSVLTAKDFVDLRPDFVYSFDLGTDFVRAKVIFPLSVPETLRVHESRGVWLSEKGAAKDAAFEAYVALYKGGLVNDNLLPLMVHDKVIDELTSKPVDTRASLLEVKERLDPWFDVARAWQEAEHNPGIVRTSIMSLDDLKIELCLPIEPPPIPPLTLHWNSSTELSVEFTNDAEIGTTEDMILRALKDTYLLLSGAFSRRFDIFSRRTVVQFIANRAPASLNLDCVTVTVDEPSRITGFIREFDKLAQPYIFEKWLPSKPPVNEVQHTYLNYSNAPENVPYLALIPVTRRTDFLHKVENQSPSSSKQFSCVLPASVCVQDAMPFQLVQFGMMIPSITHHIEVQLIVDRLCKTILKDLEISDRGLVQTAITHASYSLTSNYQRLEFLGDSILKLCTSVQLISEYPLWPEGYLSAMKDRIVSNSRSSRAAVELGLDEYIITKKFTGSKWRPMYVEDYLKTTEQKSRQMSSKVLSDVVEALIGACMVDGGIPKALKSLQLFFPELNWLPLETRQMSLYQLAADDLHLPIALQPIEQILAYTFTKKSLLVEAMTHPSYINGTQSLERLEFLGDAILDNIIVTAMWSYETELSHFQMHLLRSALVNADFLAFLCMEMSIEQYVTDLTEGKDHQIHETHTRRRFSLVNFLRHSSATFSIYQKQALARHQELREEILAVIKTGDKFPWTLLSRLDARKFFSDMIESLLGAIWIDSGSIDVCTRVVERMGILRYMRRILREGVRIMHPKEELGIVADFEDVKYVLWNRRIGGEDEDDGKDGGGESGIEYLCKVFVGGREIVEVGGGVRKEEIQARAAEAAMEILRGGGREAGFEGGKEGGQGKRKRNEGESEVIGGREGIAQGEKMNLD
The following text describes a protein:
Function:
Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine.
Subcellular Localization:
Cytoplasm.
Sequence:
MKTVRIETFGCKVNQYESEYMAEQLEKAGYVVLPDGNAAYYIVNSCAVTKEVEKKVKRLIKSIRNRNKNAKIILTGCFAQLSPDEAKNLPVDMVLGIDEKKHIVDHINSLNGKQQVVVSEPGRPVYEKVKGSFEDRTRSYIKVEDGCDNTCTYCAIRLARGTRIRSKPLEIFKEEFAEMVMKGYKEIVITGVNLGKYGKDMGSSLAELLKVIEKVPGDYRVRLSSINVEDVNDEIVKAFKRNPRLCPHLHISVQSGSDDVLKRMGRKYKISDFMRVVDKLRSIDPDFSITTDIIVGFPGETDADFQRTLELVEKVEFSRVHIFRFSPRPGTPASRMEGGVPESKKKERLDVLKEKAKDVSIRYRKRIIGKERKVLAEWYVMKGVLSGYDEYYVKHEFVGNRVGEFHSVRVKSLSEEGVISCRADMVEGKVPARG
The following text describes a protein:
Function:
Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
Subcellular Localization:
Nucleus.
Sequence:
MPSYLPILSYPSSAQDENASKLTTEYGKAFISGNENGTASTKRVEENVVISPIIKSVNAAGKNEPAGKKGGKKAVKKKHRAGGDRASKVTPVRDVSVNGDGTSSNIPDENKVDEVVMKAKSHAQALHAVKRAVLEIQLFLLDGVRTNVQLESCSALLTQSEYQDVVVERSIDKRCGYPLCEKPLVPESKRKGRFRISVSEHKIYDTRETGLFCSQTCLMTSKTFALSLQVDRDALIQQDKLAAIVRSVRDLKVAGASKVGKKSVDQPSDRSKDSILAEVKERLDVGIASFEDAGPSDAIEGYTPVTSIRDWRLRRNVQQQASVSVAGVLGNPESAVRDSGNVTTTNDGRPSLVKSSPSNDLSPSKGKSALTLHTGNLSGSLQDAPILKSILKKCQSESPVKRSVSWGDQKAKGELSHKVEAQVKQKSGSKARRQVKVLPQPSKSAAATSSSASVESGALRTEAESNRTQVESKADQSQITQRLSSAEQVLSTTQKTVVADGKSNPAKSGHVDIQPAQEAPAPKDATACSLPDSSSNCEISTFEAKDSKAPFTDAEAQIAERLASAKDLAAALMEAADATATGDFESSEAVARAGLSILSLDETREESFPANTRSEAASQVEETARLGLKWPPVDPQEEEDEEVSSSKGGWHDTAPKNFKLEISMFGTIWMALEEWISAATIAFIYGKEADCEHDFLSVNGREYSLQVVCEDGLSAEISKAFSTGIARVLPDVVQALRLRIPVSTLEQACGRMLRTMSFVEPLPALGVNHWRMLVMLFLEALSVDQVDSIGVHLSEHSSLFRQLLVGTGTSEAEYDIFRGLLLPAGRLPSVSTLNGG
The following text describes a protein:
Function:
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Sequence:
MGNPKIHVNIVVIGHVDSGKSTTTGHLIHKLGYIDNHVIESLFKLKGYFISGFERDNLVEPSTNLGRYDGPTLIEALDHLKLPVSMREIHKPLRIRIHGFYKVGGIGNVPVGRIVTGYLTPGMVMNFAPTGLQRKVKSVKIDGEVLLSVAFPGDFVGLDVEDVAAKDLQPGYVASNSNNDPAMGAADFTSYLIITKDPGMIQTGYTPVLDCHTSHIAVEFSGKEIMIPAKPMVVEAFSQYPPLGCFVARDMRQTVAFGVITYVTKLTSIEEDDQSI
The following text describes a protein:
Function:
Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSTIDKEKFQFVKRDDFASETIDAPAYSYWKSVFKQFMKKKSTVVMLGILVAIILISFIYPMFSKFDFNDVSKVNDFSVRYIKPNAEHWFGTDSNGKSLFDGVWFGARNSILISVIATVINLVIGVFVGGIWGISKSVDRVMMEVYNVISNIPPLLIVIVLTYSIGAGFWNLIFAMSVTTWIGIAFMIRVQILRYRDLEYNLASRTLGTPTLKIVAKNIMPQLVSVIVTTMTQMLPSFISYEAFLSFFGLGLPITVPSLGRLISDYSQNVTTNAYLFWIPLTTLVLVSLSLFVVGQNLADASDPRTHR
The following text describes a protein:
Function:
As the sensor component of the NLRP9 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens, including rotavirus, initiates the formation of the inflammasome polymeric complex, made of NLRP9, PYCARD and CASP1. Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and release in the extracellular milieu. The active cytokines stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death. NLRP9 inflammasome activation may be initiated by DHX9 interaction with viral double-stranded RNA (dsRNA), preferentially to short dsRNA segments.
Subcellular Localization:
Cytoplasm. Inflammasome.
Sequence:
MAESFFSDFGLLWYLKELRKEEFWKFKELLKQPLEKFELKPIPWAELKKASKEDVAKLLDKHYPGKQAWEVTLNLFLQINRKDLWTKAQEEMRNKLNPYRKHMKETFQLIWEKETCLHVPEHFYKETMKNEYKELNDAYTAAARRHTVVLEGPDGIGKTTLLRKVMLDWAEGNLWKDRFTFVFFLNVCEMNGIAETSLLELLSRDWPESSEKIEDIFSQPERILFIMDGFEQLKFNLQLKADLSDDWRQRQPMPIILSSLLQKKMLPESSLLIALGKLAMQKHYFMLRHPKLIKLLGFSESEKKSYFSYFFGEKSKALKVFNFVRDNGPLFILCHNPFTCWLVCTCVKQRLERGEDLEINSQNTTYLYASFLTTVFKAGSQSFPPKVNRARLKSLCALAAEGIWTYTFVFSHGDLRRNGLSESEGVMWVGMRLLQRRGDCFAFMHLCIQEFCAAMFYLLKRPKDDPNPAIGSITQLVRASVVQPQTLLTQVGIFMFGISTEEIVSMLETSFGFPLSKDLKQEITQCLESLSQCEADREAIAFQELFIGLFETQEKEFVTKVMNFFEEVFIYIGNIEHLVIASFCLKHCQHLTTLRMCVENIFPDDSGCISDYNEKLVYWRELCSMFITNKNFQILDMENTSLDDPSLAILCKALAQPVCKLRKLIFTSVYFGHDSELFKAVLHNPHLKLLSLYGTSLSQSDIRHLCETLKHPMCKIEELILGKCDISSEVCEDIASVLACNSKLKHLSLVENPLRDEGMTLLCEALKHSHCALERLMLMYCCLTSVSCDSISEVLLCSKSLSLLDLGSNALEDNGVASLCAALKHPGCSIRELWLMGCFLTSDSCKDIAAVLICNGKLKTLKLGHNEIGDTGVRQLCAALQHPHCKLECLGLQTCPITRACCDDIAAALIACKTLRSLNLDWIALDADAVVVLCEALSHPDCALQMLGLHKSGFDEETQKILMSVEEKIPHLTISHGPWIDEEYKIRGVLL
The following text describes a protein:
Function:
Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and ADP-ribose to ribose 5-phosphate and AMP. The physiological substrate is probably UDP-glucose. Poor activity on other substrates such as ADP-glucose, CDP-glucose, GDP-glucose and GDP-mannose.
Subcellular Localization:
Cytoplasm.
Sequence:
NSDSNRQKRECENRFTKKTSNVVVRALDYCAYTKGYASLDAEPLHIFKMSAQPQPTIDIKGFQEKFQSIYLRSYRLNFEQDGQAREFDLTLRHSSVATLLYHKDRNQFLMVRQFRPAIFVSRILKMEENRGKTVHDVDWKKYDREIGYTRELCAGLVDKDIPLIDIAREEIDEECGYNVSNDMIRWISSFVVDSGHPQHLFYTEIDDSHKSHEGGGNNHEGEFIYQVWLSEEEARNHLISSDPRSAPGLLYALEWWFSSDYKKESPIPSPYSIPSSGALSPLQSIRFTPNPPTTKFTPVRMLFDINGMTRTWDMAPCPDSAAVLIYNRDEEKLVMNRRFRPAVFIGRSRYQPENKGVAVESIDYSKYPQEWAYSLELCSGHRQGEETAKSCAIRNATERCGYRIEDGKLRHLTKAILGISQGGDKEDIYYVECGNGDKIDGWKDPQDFTVDRADLIWDIDESNLSDSQIDEYLQSTSHLPNDTALSILRLKKHNMESAIEYSKEFGVIPDLSPIEEKVLMAVAPLPNANLDLRLKHPMTTLNKIFSALPHIPSHVIMNQLNRNGRDVESGVPTNWMPRVGHITQTAYDDMIQFKVISVDEQSKLYPNNRRATRSTTQITPDMNVIPRKIGKRDNLAIAMVGFDQNVRYDEDTSPEYRPIQWTPINRILRSMSREARPPPPSSPSPLPSPSPSVEEKSSVEDPPKRKRGRPRKNPLPVSTQSPLGLPSRPSSPSKEKRESNGKRPSNGMENESEILQSKKGKTNLDGNDQQSSSRLSGGSERKGLRELSNCYSTGRNMVTRSISISFDIHTPSPPSLTSSKSRDKLRIEMVGWHQPPPNASLIKDGFESSSNIHSPSANYQSDSSAPVSPEM
The following text describes a protein:
Function:
Potential calcium sensor.
Sequence:
MRSLGLSPDSESDGLQERYSSKEISSLFEEKEASLEEVKQAFDVFDENRDGFIDTTELQRVLTTLGFKEGSCVENCMVMIRSLDGNKDGIIDFNEFLKFMENSFC
The following text describes a protein:
Function:
Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Subcellular Localization:
Nucleus.
Sequence:
MVLSGRESLIRLIGKRRRFLPNRHSILSDPNPNPNPNPAVEQPLQRHACLSQSTPATKRKFSQRTLLQLNFTLSNSKPKFHNLTHDSNTSPVPPPQHNESEEEEQVPEAHETDLDSTISTTSSSSLPSNNGVPGITLETFIVGRKYTDNPEEICAGTAISLLRDPQNVKDLNAIKVVSVDAVCYKSLGFIPHELAQCLSPLIDNYGLGFQGHVTSVPKHSLDIVPIQITCHRTSDGESKYADETFKCLWKNAQCVVEFASRSPPSSVKYQLNFCLMLLEGPWFHVSSISYPEIVDTQKAVKGLAENEYIHSIEDANQPCESNVNDILNVLSVSELHEIWCILLKKSGGHQMKKQHLISSILFTGASVLWPQLSTMILDRTVFCIRISSKAESLMWRIERLFFLNGEQDLSSFLLVDMGKIVYPAYNCIISEPIFSNRNNLLSYEEAIEVAQIMDEALDANKTDVVLRCIKIAESCVSTDFPIQCSTSESVSSIRRVFTASWVYSKVVTVGISFLERERRYIDAINLLKWLLNVFTCDVKRGYWTLRLSVDLEYLGCTNESLQIAENGLLDPWIRAGSRMALQRRVLHLGKQPRHWNVPSFSRPLNSELGEKNRYYNEEGKQCGVEELALHYYARDGGGWLGVHAESGIWLTIFGLLMWDVIYADVPNVFYTRFQNAPLDFGTDSFYTQICDGMAEEFLIKSWETHIGTACRGVNWDCHPLDELHAIVTCVGGICLASLCKLLAQDYRSWSSGMPDLLLWRFHGEYSGEAKLVEVKGPKDRLSEQQRAWLLLLMDSGFTIEVCKVKPL
The following text describes a protein:
Function:
Controls the rotational direction of flagella during chemotaxis.
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Sequence:
MDGIIKDGFFSGKNFRKTFFALKCFLHFTGIVFEIIIVLVVAMVEFEKQMVKPFGKDRIQNIDLVKPPIPLENYNFTEEFRIDTLDKGETHFVKMKLAFGIAKEDQTLSAELAERNEQMRDLIKLIVGRKFKDELINIEDQLDFREEIKAQVNHILTEGKIQEVYFTEFIVN
The following text describes a protein:
Function:
May constitute a glutathione peroxidase-like protective system against oxidative stresses.
Subcellular Localization:
Cytoplasm.
Sequence:
MYVQKLVNDDNAFHFFISLLNQRLKIDMSTGTIYDFSVRDNSGDLVSLDKYSGLVVIIVNVASYCGLTNSNYKELKSLNDKYHLRGLRVAAFPCNQFGFQEPHCEADINKFVNEKFSFEPDLYGKVTVNGGPLIGEEEPLWTFLKKEQGGTLFDAIKWNFTKFLVNRQGKVVARFGPSTNPKSFEEEIVKLLDENKL
The following text describes a protein:
Function:
Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (GalNAc(2)GlcGalNAc(3)Bac(NAc)(2) in eubacteria, where Bac(NAc)(2) is di-N-acetyl bacillosamine) from the lipid carrier undecaprenol-pyrophosphate to an asparagine residue within an Asp/Glu-Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Domain:
Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.
Sequence:
MKLQQNFTDNNSIKYTCILILIAFAFSVLCRLYWVAWASEFYEFFFNDQLMITTNDGYAFAEGARDMIAGFHQPNDLSYFGSSLSTLTYWLYSILPFSFESIILYMSAFFASLIVVPIILIAREYKLTTYGFIAALLGSIANSYYNRTMSGYYDTDMLVLVLPMLILLTFIRLTINKDIFTLLLSPVFIMIYLWWYPSSYSLNFAMIGLFGLYTLVFHRKEKIFYLTIALMIIALSMLAWQYKLALIVLLFAIFAFKEEKINFYMIWALIFISILILHLSGGLDPVLYQLKFYVFKASDVQNLKDAAFMYFNVNETIMEVNTIDPEVFMQRISSSVLVFILSFIGFILLCKDHKSMLLALPMLALGFMALRAGLRFTIYAVPVMALGFGYFLYAFFNFLEKKQIKLSLRNKNILLILIAFFSISPALMHIYYYKSSTVFTSYEASILNDLKNKAQREDYVVAWWDYGYPIRYYSDVKTLIDGGKHLGKDNFFSSFVLSKEQIPAANMARLSVEYTEKSFKENYPDVLKAMVKDYNKTSAKDFLESLNDKDFKFDTNKTRDVYIYMPYRMLRIMPVVAQFANTNPDNGEQEKSLFFSQANAIAQDKTTGSVMLDNGVEIINDFRALKVEGASIPLKAFVDIESITNGKFYYNEIDSKAQIYLLFLREYKSFVILDESLYNSSYIQMFLLNQYDQDLFEQITNDTRAKIYRLKR
The following text describes a protein:
Function:
Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.
Subcellular Localization:
Cytoplasm.
Sequence:
MRPDHRMGPPHDEEPHMPETIDAVPEIDDLRREIDELDATIIAAIQRRTEVSKTIGKARMASGGTRLVHSREMKVIERYIDALGPEGKDLAMLLLRLGRGRLGY
The following text describes a protein:
Function:
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Subcellular Localization:
Cytoplasm.
Sequence:
MNPPALTTPLIHPSAVIHPRAVLHESVQVGPFAVVGEHVRIGAGTVVGPHAVIDGWTEIGCDNVIYNGASIGTPPQDLKYRNEPSRVRIGDNNDIREFVTVNRGTDKGSETVVGDKNLLMAYVHVGHNCAIGDNVVITNAVMLAGHVHIESQARIGGLVGVHQFVHIGRLAYIGGMARVDRDVPPFTLVEGHPGRTRGLNWVGLERAGISDAAGADRESYRLLRQAYKLLYRSATPLEKALVELQALAGNPYIDHLHTFLSRSVGDPARRGPTPAARKRPGGDDA
The following text describes a protein:
Function:
Functions at a post-ubiquitation step in the ubiquitin fusion degradation (UFD) pathway.
Sequence:
MFHFSGFNMMFPEGRNFHANYKCFSVSMLPGNERTDVEKGGKIIMPPSALDTLTRLNVEYPMLFKLTNVKKSRSSHAGVLEFVADEGKCYLPHWMMENLLLGEGDILNIESVSLPVATFSKFQPHSTDFLDITNPKAVLENALRNFACLTRGDVIAIKYNKKVYELCVLETKPGNAVSIIECDMNVEFEAPVGYKDHSETQASGSGQQGAAGTVGGEIAGATNAILEEVVETFKGSGVRLDGKKKKESQLETPVVKKVLARGVPDYDFQFGLIRFDRNIRPISDRSQEDDAVAGNADASDAESFHGTGFSMKKTRK
The following text describes a protein:
Function:
Member of a high affinity multicomponent binding-protein-dependent transport system for choline.
Subcellular Localization:
Cell membrane; Lipid-anchor.
Sequence:
MKRKYLKLMIGLALAATLTLSGCSLPGLSAAADQTIKIGAQSMSESEIIASMLGQLIEHHTDLKTTTIKNLGSNAVQQQALMNGEIDIAATRYTGDALTGTLRMEPEKDPDKALALTQREFKKRYDLKWYDSYGFDNTYAFTVSKELADQYHLETVSDVKKWAPQLKLGVDNYWMKLKGNGYQDFTKTYGMTFGGTYPMQIGLVYDAVKSGKMDIVLAYSTDGRIKSYGLKMLKDDKQFFPPYDCSPVVPEKVLKEHPELEGIIKKMLGKIDTATMQELNYEVDGNLKEPSVVAKEYLEKHRYFES
The following text describes a protein:
Function:
Effector protein that binds to the host serine protease cathepsin G on the macrophage cell membrane, inhibiting its enzymatic activity and the downstream activation of caspase-1-dependent apoptosis. Thus prevents macrophage pyroptosis and helps M.tuberculosis survival within host cells.
Subcellular Localization:
Secreted. Host cytoplasm. Note=Is translocated into the cytoplasm of macrophages.
Sequence:
MKARLPDSPLDWLVSKFAREVPGVAHALLVSVDGLPVAASEHLPRERADQLAAVTSGLASLAGGAAQLFDGGQVLQSVVEMQNGYLLLMQVGDGSALAALAATGCDIGQIGYEMAILVERVGGVVQSCRR
The following text describes a protein:
Function:
ATP-dependent low-affinity peptide transporter which translocates a broad spectrum of peptides from the cytosol to the lysosomal lumen for degradation. Displays a broad peptide length specificity from 6-mer up to at least 59-mer peptides with an optimum of 23-mers. Binds and transports smaller and larger peptides with the same affinity. Favors positively charged, aromatic or hydrophobic residues in the N- and C-terminal positions whereas negatively charged residues as well as asparagine and methionine are not favored.
Subcellular Localization:
Lysosome membrane; Multi-pass membrane protein.
Sequence:
MRLCKAVVVTLAFMSLDIGMTTAIYILSHLDRSLLEDIRHFNIFDSVLDLWAACVYRSCLLLGATIGVAKNSTLGPRRLRASWTVIALVCLFGGIYTMVKLLLFSEVRKPVRDPWFWALFVWTYISLTASFLLWWLLSTVRPDTKALGRGAGAEGEGEGEGFPGEDRPAPEQASGATLQKLLSYTKPDIAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMEQFSAAVIVMCVLAIGSSFAAGIRGGIFTLIFARLNIRLRNRLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSDIYGKYYKRLSKEVQSALARASSTAEETISAMKTVRSFANEEEEAEVYSRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLISFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDRQPTMVHDGSLAPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGQVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFETVVEAAQKANAHGFIMELQDGYNTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTHQQLLAQGGLYARLVQRQMLGLEPTGDFTAGHREPPGNGSHKA
The following text describes a protein:
Function:
Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Gly/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of the exposed alpha-amino group of the Ala, Gly or Ser residue in the [Ala/Gly/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Some of the substrates may be primed by NTMT2-mediated monomethylation. Catalyzes the trimethylation of the N-terminal Gly in CENPA (after removal of Met-1). Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1.
Subcellular Localization:
Nucleus.
Sequence:
MTSEVIEDEKQFYSKAKTYWKQIPPTVDGMLGGYGHISSIDINSSRKFLQRFLRVGRSGVLSRRGCGSGGTAESMWGATFYTCNTAGLLAISWYLPQSLEELGWVGTVG
The following text describes a protein:
Function:
Could be involved in the maturation of NapA, the catalytic subunit of the periplasmic nitrate reductase, before its export into the periplasm.
Subcellular Localization:
Cytoplasm.
Sequence:
MSSRRELFRRLGGHPPTRRPPWTAADFAAGCTGCAACVGACPEGVLKLGAGRLVELDLSSAGCTLCGECASRCEAGLFDGARPAFPWIATIGEACLALAGIHCRSCQDACEPAAIRFRPAPGGVALAELDSQRCNGCGACLAPCPSQAIQLRALSTKESPRHA
The following text describes a protein:
Function:
Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family. Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms. Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion. Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction. Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses. Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals. Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2. May link TNFRSF1A with MAP kinase activation. May be involved in the regulation of TNFA-induced apoptosis.
Subcellular Localization:
Cell membrane. Cytoplasm.
Sequence:
MSGSLAGGDHAHFCPRLLDYIVIVGARNPNGNSAAQTPELLRRYPVEDHEDFPLPPDVVFFCQPEGCISAGVKRVSLREDNSFVFSLTEKDSNRVRFGMCVNFYRPFEKRNSTDHGGRGSAGEQPQTLQKPRTESIDGDDEGLEPQTHRRRRKQGRVRNNTLTSLCIVSHHPFFSTFRECLFILKRLIDACNQRTGGKKVGAAKGTFRNSVWGVLTGNRTDDKASLVTHDVRELETWICRLLSAPVCIPGKTRVEVSILPTEMQAPMTFALPDAHRFCLADFPMHLPLELLGVETCLKVLTCILLEHKIVLQSRDYNALSMSVMAFVAMIYPMEYMFPVIPLLPTCMSCAEQVQNLLLVPSPYIIGVPASFFLYKADFKLPDDVWLIDLDSNKITVPRCADELPPLPEPEGTQLKNHLKQALSSMSMAPQPILNLDKVQEENLAVPVRNASPSTPEMGFNPLIYGNDVDSVDIATRVAMVKFFTSKNVLGDHWVHTRTLRLYPRPVVAFQLATFLKSRGKQTDFIKRLASTQAVEYFGEWCLAPTNTTFQRIQNTVHDPVLIGDKPKWYAHQLAAVQFNVYDDNSTLASALELALTDQVDDQSEPPTDESGSDTGSEVSEDDAGGSTTSSSYSSLSDFVTDMINSGISGTTPSVPEIEVDREALAHCSPPSTLQVPPMLQESPSPVTMSPHSTATTPSPDSEKQAINPMFHEEGDRGNDTDADIDSLNYDSDSSHPSKTDALEYIAKQAKGRPELETDNNNIPKSRPYGPSMSMYELPVHGDGTGRGAGLPSLVEKGDPQSTWSLASIASKISNLKIDQSDAESVSSATSSDRNGYTRMKSSMSSFFSFATDSLQRSSSGVSTLSTRSRGSDGGKSFGPFPRAPSSRKALADKSLIRHSSSQSSLRRPPPPSKGSPQSPPDSSRINSSENQQFLKDVVSSVLEGQGVGWLQLKKLKRLMEQESLRMFVINRLLENAVRDEENSKEGRYSDHIEDVKVSRAVYKGMLAVLKACVVGLESSHDNHVPGGVASAFGVLEIAHTHYYTKEVPQLPKRKEDFDKDEDKGSRRRKNYDTRSLDEENMVAALGKRMFLKKAWQLWTGNYCLESPTFIPLPSISLPTLDHWLPESVLRGSMWIPKTAASAVSSIMKGVPKGRTESDRETTIYWGASSRAQRNPIWTATYRYKPGSDGFEVVEKPDGSTSGEDKESDRESIIEGAEGIDEDIKSAEDLLYIKQRRKMNKNNSVDSDTVSESSTLVSNSSETLANDSDYSTASNENLWPQRINHHSIRAAVSDSEIERTGGQMSPSRRAPTTTWHSKSTLSKGFRYRNGHLISTAGSTQDGIERHYIFEGLIGLERTSIWDQIPFWDEDSEISTPTILTPDVPFVKSVGMTGITAVSDIQQTVTQTVWGNGKERSALWENMQFWEDGFLDLVAQERELVGMDQAPADMIDRYKAMSAEDRKRLEEDEDKLLSTQLFNLVAYMVSMQVSKNECRRKIRRLLGKSHIGLLYSQDVMDVLDQINNLHGNDIDLKPYSSRYMRKQTFVVHAGTDTRGDLLFMEVCDDAIVLRTGNGQIQERWWYEKLINMTYCPKTKVLCLWRKKDNQTQLNKFYTKKCKELYFCVKDSMEKAAAKQNGKKPGYSLLARLIGELPMEDVHTRRKAGPELGGEFPIQDMQTGEGGLLQVTLEGINLKFIHTQELEAFIELKDIRKCNTEKGVFVLEQFDSQTRQVTVRKYKSSMANEICYAVLCVFSYVAAAKSQEKRELEAKSPVK
The following text describes a protein:
Function:
Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (SSC1) via its interaction with PAM18/TIM14. May act by positioning PAM18/TIM14 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein.
Domain:
The J-like region, although related to the J domain does not stimulate ATPase activity of mtHSP70. It nevertheless mediates the heterodimerization with the J domain of PAM18 and is therefore essential for PAM complex function (By similarity).
Sequence:
MAHRLIYQVVVTGTQVFAKAFTQAYKQAATAQAASKTSKSAASKFGGLQLDEACKILDVDETALDKVVAELNKKHKLEDIAESESVLAQIDKKFTHLYTVNSEHKSGSFYLQSKVYRAMERIRGELELDPLPKPEIEEPKKKEEEKK
The following text describes a protein:
Function:
Probable cyclin-dependent protein kinase (CDK) inhibitor that functions as a repressor of mitosis in the endoreduplication cell cycle.
Subcellular Localization:
Nucleus.
Sequence:
MMSASPEFYKPAPVFSPCSSPLRLLQQQHGEDHQEEYGYGSSGGCCRTPTGGESNLKAPGTCPPAPRKPRAPAAPCRKRLFEVEVLSLRLEELERLFWRPPPPPPTTQPQPQPQQPPQKRRRVAKLGS