lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May function as an adapter protein.
Sequence:
MAKWLRDYLSFGGRRPPPQPPTPDYTESDILRAYRAQKNLDFEDPYEDAENRLEPDPAGPGDSKNPGDAKYGSPKHRLIKVEAADMARAKALLGGPGEELEADTEYSDPFDAQPHPAPPDDGYMEPYDAQWVMSELPGRGVQLYDTPYEEQDPETADGPPSGQKPRQSRMPQEDERPADEYDQPWEWKKDHISRAFAVQFDSPEWERTPGSAKELRRPPPRSPQPAERVDPALPLEKQPWFHGPLNRADAESLLSLCKEGSYLVRLSETSHQDCSLSLRSSQGFLHLKFARTRENQVVLGQHSGPFPSVPELVLHYSSRPLPVQGAEHLALLYPVVTQTP
The following text describes a protein:
Function:
Involved in the transport of maltose and maltodextrins.
Subcellular Localization:
Cell outer membrane; Multi-pass membrane protein.
Sequence:
MKTSLRTLSVALAAALVSPSVLAIEKIDFHGYMRAGVGVSSDGGLAEWQKTMVGRLGNESDTYGEIGLGAEVYKKEDVSFYLDSMVSMLSDGSNDSETTIGDDAQFGLRQLNLQIKGLIPGDKEAVIWGGKRYYQRHDLHIIDTKYWNISGSGAGIENYTVGPGAVSVAWVRGDANDVDTRITGDSDVNINYIDVRYAGFKPWAGSWTEVGIDYAMPNPTKQQKEYGGLYDADNAVMLTGEISQDMFGGYNKLVLQYANKGLAQNMISQGGGWYDMWHKTDEAKGYRVINTGLIPITDKFSFNHVLTWGSANDITEYTDKTNLISLVGRAQYQFTQYVRAIGEVGGFYQKDTYHNGSNYKQGGEKYTIALGLAEGPDFLSRPELRVFASYLNDSENGKPFEDGTSNDTWNFGVQVEAWW
The following text describes a protein:
Function:
Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins.
Subcellular Localization:
Endoplasmic reticulum.
Sequence:
IGLLFQYLWLFVLGGEQLSPFKDDILYHINWAGSNVNLQQFQTPGTEYNSEDTIIMTSANNEKYSCTLPSKVSAEKSSDGSTEISMSPVRGLSGLFKSGQCKYYYEPFWTYEICHGKHIKQYHELQSDDSKGDIIKTTEFYLGTLDGKVDEEGMLIGVEDVAPTSKEEVPTRNTAGVKTPYYAVVMDGGTACDLRPGVNRQTTVYYICGPESNNDILSVTETSSCEYEVVVLSPQMCNLPLYNVERKQVHEIQCIAVDDAPAKPVALKLQLEEEAPVNPYVNIFSPDNSRVRKIFRPLTQNDDEPKQDDLRRVEVQKISTLVDKSLLNEFLSGSYCLRGGTGWWRFEFCYGKHVHQYHDDAKLGRTTISVGTWNKQEHKEWAKLNISTHCNTQGDTRVSMVQHFYGHGDVCEETGKPRQVVVRMKCKKSPASSHAVSIYLLEPSKCVYILGVESAIVCGLLDSADAEGMLKHEP
The following text describes a protein:
Function:
Catalytic component of the GATOR2 complex, a multiprotein complex that acts as an activator of the amino acid-sensing branch of the mTORC1 signaling pathway. The GATOR2 complex indirectly activates mTORC1 through the inhibition of the GATOR1 subcomplex. GATOR2 probably acts as an E3 ubiquitin-protein ligase toward GATOR1. In the presence of abundant amino acids, the GATOR2 complex mediates ubiquitination of the NPRL2 core component of the GATOR1 complex, leading to GATOR1 inactivation. In the absence of amino acids, GATOR2 is inhibited, activating the GATOR1 complex. In addition to its role in regulation of the mTORC1 complex, promotes the acidification of lysosomes and facilitates autophagic flux. Within the GATOR2 complex, WDR24 constitutes the catalytic subunit that mediates 'Lys-6'-linked ubiquitination of NPRL2.
Subcellular Localization:
Lysosome membrane.
Sequence:
MEKMSRVTTALSGSALTGRTMHCHLDAPANAISVCRDAAQVVVAGRSIFKIYAIEEEQFVEKLNLRVGRKPSLNLSCADVVWHQMDENLLATAATNGVVVTWNLGRPSRNKQDQLFTEHKRTVNKVCFHPTEAHVLLSGSQDGFMKCFDLRRKDSVSTFSGQSESVRDVQFSIRDYFTFASTFENGNVQLWDIRRPDRCERMFTAHNGPVFCCDWHPEDRGWLATGGRDKMVKVWDMTTHRAKEVHCVQTIASVARVKWRPECRHHLATCSMMVDHNIYVWDVRRPFVPAAMFEEHRDVTTGIAWRHPHDPSFLLSGSKDSTLCQHLFRDASQPVERANPEGLCYGLFGDLAFAAKESLVAVESGRKPYTGDRRHPIFFKKKVDPAAPFAGLASSALSVFEMEPGSGSMSWFVDTAERYALAGRPLAELCEHNAKVARELGRNQVAQTWTMLRIIYCSPGLVPGTNLNHSVGKGSSCGLPLMNSFNLKDMAPGLGSETRLDRSKGDTRSDTVLLDSSATLITNEDNEETEGSDVPADYLLCDVEGEDDELYLLDPEHTHSEEPEYVLPQEAFPLRHEIVDTPPGPEHLQDKADSPHVSGSEADVASLVPMDSSFSLISVSHALYDSRLPPAFFSALVCDMLHFYAEQGDVQMAVSVLVVLGERVRKDIDEQTQEHWYTSYIDLLQRFCLWNVSNQVVKLSTSRAISCLNQASTTLHVNCSHCKRPMSSRGWVCDRCHRCASMCAVCHHVVKGLFVWCQGCSHGGHLQHIMKWLEGSSHCPAGCGHLCEYS
The following text describes a protein:
Function:
Specifically methylates the N7 position of guanine in position 535 of 16S rRNA.
Subcellular Localization:
Cytoplasm.
Sequence:
MNIEEFTSGLAEKGISLSPRQLEQFELYYDMLVEWNEKINLTSITEKKEVYLKHFYDSITAAFYVDFNQVNTICDVGAGAGFPSLPIKICFPHLHVTIVDSLNKRITFLEKLSEALQLENTTFCHDRAETFGQRKDVRESYDIVTARAVARLSVLSELCLPLVKKNGLFVALKAASAEEELNAGKKAITTLGGELENIHSFKLPIEESDRNIMVIRKIKNTPKKYPRKPGTPNKSPIEG
The following text describes a protein:
Function:
The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular Localization:
Cytoplasm.
Domain:
Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Sequence:
MIGKLKGLIDSYGEDFVILDVGGVGYQVHCSTRTLQHLPSPGEAAVLSIETYVREDQIKLFGFRTDQEREWFRLLQTVQGVGAKVALAVLGTLAPSDLANAIALRDKAAVARTPGVGPKVAERIVTELKDKAPAFANVDPAVVHLAGAVDDQRAPRPVADAISALVNLGYGQPQAAAAIASASRSAGEGAETAQLIRLGLKELAK
The following text describes a protein:
Function:
Probable transcription factor that regulates neuronal differention, including synapse assembly of the cholinergic motor neuron M4. Activates expression of growth factor, neuropeptide and transcription factor genes, such as TGF-beta dbl-1, FMRFamide-like flp-5 and transcription repressor zag-1, in the M4 neuron. Required for pharynx peristalsis.
Subcellular Localization:
Nucleus.
Sequence:
MQSTQISSTTVILPSEVIQPPQQSAVPSEFKNTLPSRLNLFEGFDQSFSELTNPYQPVIPLMQRESLLGASSYYSSPSQNQRSYQNHRQHSNPDTINLRSQQQKRKPRVLFTQHQVNELEERFKKQRYVTATEREELAQCLGLTATQVKIWFQNRRYKCKRLAQDRTLQLSQIPFNPMFASAFPFGINSFGTAPSSSSSGS
The following text describes a protein:
Function:
Non-catalytic component of the proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that 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. It has an ATP-dependent proteolytic activity (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MDSSIGIKGRNFAIVAADTKISSSILVVKENHEKFQVIKDRIVMAMTGNQGDAFRTMLYVSESALYEEIQNGIELSPSVLAHMIQNKVHESLRRRQLDISSIVAGRGPEKYDLWSVDKYGAISSVPFCASGYAAYFVYGILDREYSEDITIDAALSIMQKCVNLLKERLMINLEGFMVKIVTDDGILTRTLVPEIKG
The following text describes a protein:
Function:
Probable RNA methyltransferase.
Sequence:
MSNFQHGNYHSYYSMRGGTSIIDPRLKCLPDSLFYEASVLDIGCNNGTVSAQIASIFGASFVLGLDIDHVLIQKARKHLEFVSSRIGPVRNPGSIVEDQFNYYPISSIKKFSRIPVQLQPPLNKQNFPHNIEFETADFLRWESKRKFKIILALSVSKWVHLNNHDEGIIKFFGKISSLLETNGVLILEPQGWDSYLKAAKKISVFNQTPENLKIQPDAFEHLLNQAGLVLEYSIEPQVNNSEYKNFAKRTMYIYKKKGIGIIKLLTST
The following text describes a protein:
Function:
Transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MKNVQEEYRKGPWTEQEDILLVNFVHAFGDRRWDFVAKVSGLNRTGKSCRLRWVNYLHPGLKRGKMTHQEERLVLELHAKWGNRWSKIAKKLPGRTDNEIKNYWRTHMRKQAQEKKRPMSPTSSSSNCCSSSMTQDTGGSNGKMNQECDDGNYSMDDIWREIDQSGANIIKPVKDIYYSEQSCYFNFPPLPLASPTWESSLESTWNMDAYESKMSSFAIDQFPLSFEHGRSSWSSLV
The following text describes a protein:
Function:
Monoglycylase which modifies both tubulin and non-tubulin proteins, adding a single glycine to the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of target proteins. Not involved in elongation step of the polyglycylation reaction. Preferentially monoglycylates alpha-tubulin over beta-tubulin. Together with TTLL3, mediates microtubule glycylation of primary and motile cilia, which is essential for their stability and maintenance. Together with TTLL3, glycylates sperm flagella which regulates axonemal dynein motor activity, thereby controlling flagellar beat, directional sperm swimming and male fertility. Monoglycylates non-tubulin proteins such as ANP32A, ANP32B, SET, NCL and NAP1.
Subcellular Localization:
Cytoplasm, cytoskeleton. Cell projection, cilium. Cytoplasm, cytoskeleton, cilium axoneme. Cytoplasm, cytoskeleton, flagellum axoneme.
Domain:
Two conserved structural elements specific among monoglycylases, IS1 and IS2, are involved in glycyl chains initiation. Two conserved structural interfaces likely constitute the binding platforms for tubulin tail and microtubule; Arg-360 is the main determinant for regioselectivity, which segregates between initiases and elongases in all tubulin--tyrosine ligase family. A glutamine residue at this position is found in elongases TTLL6, TTLL9, TTLL11, TTLL13, TTLL10 and favors glutamate-chain elongation, whereas an arginine residue is found in initiases TTLL2, TTLL4, TTLL5, TTLL3, TTLL8 and favors initiation.
Sequence:
MEPERKGLSLASSSDGDGREENKLKQGISQDLASSSRLDRYKIARQLTEKAIKEKKIFSIYGHYPVVRAALRRKGWVEKKFHFLPKVIPDVEDEGARVNDDTCAKVKENQEMALEKTDNIHDVMSRLVKNEMPYLLWTIKRDIIDYHSLTYDQMLNHYAKTASFTTKIGLCVNMRSLPWYVPANPDSFFPRCYSLCTESEQQEFLEDFRRTMASSILKWVVSHQSCSRSSRSKPRDQREEAGSSDLSSRQDAENAEAKLRGLPGQLVDIACKVCQAYLGQLEHEDIDTSADAVEDLTEAEWEDLTQQYYSLVHGDAFISNSRNYFSQCQALLNRITSVNPQTDIDGLRNIWIIKPAAKSRGRDIVCMDRVEEILELAAADHPLSRDNKWVVQKYIETPLLICDTKFDIRQWFLVTDWNPLTIWFYKESYLRFSTQRFSLDKLDSAIHLCNNAVQKYLKNDVGRSPLLPAHNMWTSTRFQEYLQRQGRGAVWGSVIYPSMKKAIAHAMKVAQDHVEPRKNSFELYGADFVLGRDFRPWLIEINSSPTMHPSTPVTAQLCAQVQEDTIKVAVDRSCDIGNFELLWRQPVVEPPPFSGSDLCVAGVSVRRARRQVLPVCNLKASASLLDAQPLKARGPSAMPDPAQGPPSPALQRDLGLKEEKGLPLALLAPLRGAAESGGAAQPTRTKAAGKVELPACPCRHVDSQAPNTGVPVAQPAKSWDPNQLNAHPLEPVLRGLKTAEGALRPPPGGKGEGTVCSRLPHHGHHVAACQTTGTTWDGGPGVCFLRQLLASELPMGPGLPRDPRAPPCLVCRGLLPPAGPCKRCRSFCAAVLQGASFVRLGGRSCSPRTP
The following text describes a protein:
Function:
Binds to spermatozoa upon ejaculation and may play a role in sperm capacitation. Has phosphorylcholine-binding activity (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MNPWSSYLLGWTTFLLYFYETSGKIPNLSSLGKHEFTKPWISIKEDQKDSCVFPFVYKGSSYFSCIKTNSFSPWCATRAVYNGQWKFCMADDYPRCIFPFIFRGKSHNSCITEGSFLRRLWCSVTSSFDENQQWKYCETNEYGGNSFSKPCIFPSIFRNSTIFECMEDENNKLWCPTTENMDEDGKWSLCADTRISSLVPGFPCHFPFSYKNKNYYNCIGKGTKENLTWCATSYNYDRDHTWVYC
The following text describes a protein:
Function:
Binds as a heterodimer with protein bS6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
Sequence:
MAQQTQSEIRYLTPPSVDVKKKKYCRFKKSGIRYIDYKDPEFLKKFLNEQGKILPRRITGTSLKFQRRIAQAVKRARHLALLPYVTDMMK
The following text describes a protein:
Function:
This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Tyr and Thr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Thr residue is further converted to the D-allo-isomer form. The activation sites for these amino acids consist of individual domains.
Sequence:
MAQSAQIQDIYPLSHMQEGMLFHSLMDFSSKAYIEQTSFTITGNLCVDSFQKSLNLLVSRYDIFRTIFIKEVPDLTGPQQVVLSNRELTVYREDISRLADQEQQTLIDAFMTKDREKGFDLQKDPLMRLALFDRGDSQYTCVWTHHHIIMDGWCLGIILKEFFSMYDSLKNNSPVQLGSTVPYSRYIEWLGEQDQEETAAYWSEYLKEYGNTASIPRIKRRTADGNYKADQVSFSLAPDMVEKLTEAAQNWGVTLNTLFMSIWGVLLHRYNAADDAVFGSVISGRPSAIDGIESMVGLFINTVPVRIRSAEGITFSSLVKAVQEDILSSEQHGYYPLYEIQNHSPLKQGLIDHIFVFENYPVQLHQALSVESENDEGALKLSDISMSEQTNYDFNIVIVPGESFYIKFSYNADVYEREEMLRIQGHLKQALDCILTNPDVAVSDINIVPPEEQQVIQLFNETERPYVNKTIPQLFEEQAHKTPEAAALKMGNECWTYRQLQVRANQIAHALIEKGVGSGDIVAVMMGRSMEMPAALLGIWKAGGAYMPLDPHFPAERLSFLLKDSQAAQLLIEEDLISLIPPSYEGNTITIEHTESYQTEAPNMPPGDLAYLIYTSGTTGRPKGVLVDHHGIANTLQWRREEYSMTEQDISLHLFSYVFDGCVTSLFTPLLSGACVLLTTDDEAKDVLALKRKIARYKVSHMIIVPSLYRVLLEVMTADDAKSLRIVTFAGEAVTPDLLELNQIICPSAELANEYGPTENSVATTILRHLNKKERITIGHPIRNTKVFVLHGNQMQPIGAAGELCISGAGLARGYYKQQELTQKAFSDHPFLEGERLYRTGDAGRFLPDGTIEYIGRFDDQVKIRGYRIELREIETVLRQAPGVKEAAVLARDVSAEEKELVAYIVPEKGNSLPDLYQHLAGTLPSYMIPASIINISQMPLTSSGKLDRFALPEPENNTSVTYMAPRTLIEADLAHIWEDVLNKQHIGIRDDFFQLGGQSLKAAALVSRIHKKLNVELPLSEVFSYPTVESMAVKLMSLKEHAFTQIEPADQRDVYPLSFSQKRLYALHQLADDSTGYNMPAVLELRGNLNRQRLRSVLTELVNRHEALRTVFVLDRDEPVQIIYPEMAFDLKELEMESEQMLESAIETFIKPFYLSSGPLFRACVITMGNNRGFLLLDMHHIIADGVSMSTLVQEFTDLYCGKELPALNLHYKDFAVWQQEKHPKELYKKQEAYWLGQLGGSLPTLELPLDKTRPRLPDFRGGTIEVNIDKDMADELHRLMAETGTTLYMILLAVYSILLSKLSGQEDIVVGSPAAGRPHADLERVIGMFVNTLAMRSKPEGHKTFSSYLHDIRHLALTAYEHQDYPFEELADKLDTNREVNRNPLFDAMLVLQSSEDFRFEVPGLSISSVTPKHDISKFDLTLHAEEHLSGIRCRFEYSTALFEEETITQWASYFIELVKGVTADTEMRISNMQLLPAAERRLLLEKMGQYAAYPRNENIVSLFEKQVAQYPEHIAVVCGHSQLTYRDLNEKAERAAAMLIKQGVRTGDIVGLMLDRSPDMIIGVLSILKAGGAYLPIDPEYPKERISFMLNDSGAKLLLTERGLNKPADYTGHILYIDECENNSIPADVNIEEIVTDQPAYVIYTSGTTGQPKGVIVEHRNVISLLKHQNLPFEFNHEDVWTLFHSYCFDFSVWEMFGALLNGSTLVVVSKETARDPQAFRLLLKKERVTVLNQTPTAFYGLMLEDQNHTDHLNIRYVIFGGEALQPGLLQSWNEKYPHTDLINMYGITETTVHVTFKKLSAADIAKNKSNIGRPLSTLQAHVMDAHMNLQPTGVPGELYIGGEGVARGYLNRDELTADRFVSNPYLPGDRLYRTGDLAKRLSNGELEYLGRIDEQVKVRGHRIELGEIQAALLQYPMIKEAAVITRADEQGQTAIYAYMVIKDQQAANISDIRTYLKNALPDFMLPARMIQIDSIPVTVNGKLDQKALPEPEKQAYTADDISPRNEIETVMAEIWEELLNVDELGVSANFFKLGGDSIKALQVCARLKQRGFETTVREMFEHQTLGELSARVRKDVRAIDQGPVEGEITWTPIQQWFFSQSLESHHFNQSVMIYRAERFDEAALRKVLKSLVTHHDALRIVCRHEDGRQVQINRGIDLSDEELYALELFDVKDSLTEARNTIEEAASRMQEHIRLETGPLLHAGLFRTENGDHLFLTIHHLVVDAVSWRILFEDFSTAYKQAVSGESIKLPQKTDSYLTYSQRIADYSISRQVQREAAYWDECENRHIQPIPKDNDAASNTFKDTEVIDFELSRHHTELLLTAAHKAYSTEMNDILLTALGLALQKWTGNNQFKISMEGHGRESYLEDIDISRTVGWFTSIYPVWLDMRDSDHKDKEERLGHLIKQTKDMLHRIPHKGAGYGVLKYISKRWGSQKNSPEISFNYLGQFDQDIQSNAFEVSDIKPGNEISPNWERPYALDISGAVSSGCLNMHIIYNRFQFEEKTIQTFSRHFKQTLENIIEHCTGKENQEWSASDFTDEDLTLDELSEIMGAVNKL
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MASLSRVWRIGSKVLTGSSSLVRPNLRSIPCRVYSSTTKKVEQSEFVIGKQTEIDPARVEEIIKEGTRLESDSDASDPTYVTHGFHDDPYWDTYAYRVIFFTTISIVMVFGPAFVHYLPDPTGREWARKEALVVLDERRAAGALVIDPNFIDPSKLVLPEEDPEPLRTA
The following text describes a protein:
Function:
Glycosyltransferase that specifically catalyzes mannosylation of cytoplasmic tRNA(Asp) modified with queuosine at position 34 (queuosine(34)). Mannosylates the cyclopentene moiety of queuosine(34) in tRNA(Asp) to form mannosyl-queuosine(34). Mannosylation of queuosine(34) in tRNA(Asp) is required to slow-down elongation at cognate codons, GAC and GAU, thereby regulating protein translation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSVLLLEAFYGGSHKQLLDLLKESVEDCVSFTLPAKKWHWRARTSALYFMQAVPANSSYRVLFTSSVLNLAELVALRPDLGHLKKVLYFHENQLVYPVRKSQERDFQYGYNQILSCLVADVVVFNSSFNMESFLSSISTFMKTMPDHRPKDLERLIRPKCHVLHFPIRFPDVTRFLPAHKRLRHPVRCDDIHAPAAKSHIQTSSPSSYPDVEPPEKMLNVAGTNQSHEPTSVTPHQETASPLCGHEGEKLRPLHIVWPHRWEHDKDPQLFFQTLLKLKDRQLSFEVSVLGETFTDVPDIFSEAKEQLVDHIQHWGFMPSKEDYLKVLCQADVVVSTAKHEFFGVAMLEAVHCGCYPLCPKALVYPEIFPATYLYSTPEQLCKRLQEFCKRPQLARQHVVQVSLSSFSWDSLGDNFRSLLKADSGRMFTDKHMA
The following text describes a protein:
Function:
Part of an ABC transporter complex. Responsible for energy coupling to the transport system; Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system.
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Sequence:
MIELTQLWYRYPDHTPALRGINLTVAAGEKVALLGVNGAGKSTLLLHLNGTLHPERGTVVVNGTPVTKQTVRQVRAMVGLVFQNPDDQLFSATVGDDVAFGPQYMGLPPADVTQRVHQALVAVGMQGFEQRPPHRLSLGQRKRVALATVLAMQPAILALDEPSAGLDPRARRELIELLHALPQTMIIATHDLDLVADLAPRAIVMADGQIVADEATTTLLADQHRLYEFGLR
The following text describes a protein:
Function:
Tip subunit of the minor fimbriae. These filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. They play an important role in invasion of periodontal tissues and are recognized as major virulence factors (Probable).
Miscellaneous:
MISCELLANEOUS: The name (minor fimbrium subunit) does not indicate the abundance of the protein, but is derived from the greater length of the major fimbriae. In strain ATCC 33277 and strain ATCC BAA-1703 / FDC 381, major fimbriae are 300 - 1600 nM in length and about 5 nm in diameter. In contrast, minor fimbriae are only about 80 - 120 nm long. This length difference is observed only in a small number of strains, including strain ATCC 33277 and strain ATCC BAA-1703 / FDC 381, and is due to a loss of function mutation in FimB, a protein that restricts fimbrial length in other strains.
Subcellular Localization:
Fimbrium. Cell outer membrane. Note=Targeted to the outer membrane as a palmitoylated precursor. The lipid modification is no longer present after proteolytic processing to the mature form.
Sequence:
MKKYLLYASLLTSVLLFSCSKNNPSEPVEDRSIEISIRVDDFTKTGETVRYERNQGSAAERLITNLYLLLFDQSGANPAKYYIAGNTFSGGIWLPDDMKVKLDMTQSEAGERKVYVVANVDNAVKTALDAVANESDLQTVKRTTAMPWSTDIASPFLMSGNKTHDFLANRLLDNVPLVRAIAKVELNISLSEKFQIVPIIVNGSLSEFKFRYVNFDKETYVVKPTTKPDNLISSANGVWPQITDWTVWGASLNTSPAPDAGTGYTLDANGKVTALRIVTYLNERDSKGATVEVALPRVDDGTLPPPEFGPELYRLPLPDKILRNHWYKYEVEI
The following text describes a protein:
Function:
Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MNLFLSRFTGLRNTSFLGHARPFMFPRRYAHSLVAHNIGHIKLDPNEGLFFVDNLVNTPTYFYIQRYTALLFQNNLKKQLSAAFPSSDTMQLEDIIFRWQDGGAFLKVRYKEFPQDTEAVSEHVRESFRKRPVRTILHPFSTPIPHMVHGIPWLQDLYIFPSRTVDVNFEGPPLSQERLYSIFRTYGKLRSVTINSPTSATLSFSSLRSATSALNCMHGFVYGKTEFHMRYRHMNRFVAFKDWLFSHPRFTIPLVAAAITVLTASLFDPIRKFFVETNIVHGQKLRNINVVGWVKKKTRDIVLSPFHENGTNIKAPIWTTREKDCEQLKEWLDEALHSFIVVQGPRGSGKRDLVDRVVKERKNVLFFDCDRLFSTTNTEMFVSTLASQTGYFPLFSFLNNISSLIDMAAQGLIGQKTGIVSSSEGQVRQILNTTQTVLRSLALREHKEADTSVLDESEFLEVHADRLPVVILDNFQLRKLSNPMQRVVAEWAGNLVKEGIAHVLMLTPDVGGTKSLEQYVNGWENRTLLLGDADPVLAQRYVIESLPEEMQTEELRKELRVQLPKIGGRLRDLDYVARRLRVNSSSVSEAIGGIVSQNASDILQTFLRPASLTSEEKPTFTPEESWTLITYLSQHEYIPYHMLMLDPLFKGHDDAVRALEESELITITTVNARPDKVYAGKPVYVTAFRQLVNDPVLSANMQLVRCNALIGMANNAIKNDEQELQMLKDLGNLESGVKDRAHYLTTRIQKNQGVITDNEKSIERLTEALKKID
The following text describes a protein:
Function:
Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase.
Subcellular Localization:
Nucleus.
Sequence:
MGRSDKAAEANGTKQPKKRAHIEPEEEEEELEEGYELEEEAELDSEDEGMELGDEDGEEEEALLEMFTQAEIIEDMRKAGEVKSGKAIAEKDRELETAADFMQWLIAPMTLEKFYSEYWEKKPFVIQRKNCRGYYNGWFGKDDVIALLRTGKMLYGKNVDVTNYVDNERVTLNKDGAADADEVLRNFEGGCSVRVLHPQRWSDPLWLMLSTLERHWESVVGCNTYLTPPGSQGFSPHFDDIEAFVLQTEGRKHWRCYAPREGGELLPRVSSPNFLQEDIGEPVLEFDLEAGDLLYMPRGTIHQANCLPDSHSMHITVSTGQQNTWADFLAITLPRALELAAEEHVELRRSVPRDVLNYMGVVHSDSSDTRREEFVGKMAQLFSLMLESAPWDPATDQLGAMFQRARLPPVPLGGAPRPSTAAKVGPDTKVRLAHPGCARLVVEGDSAVVYHMMRNPRDLHCERPAGAGHGEGEHEHDAAGGCCDGDEKPPGAAELGAGKDGEEEDDEDTTLEFPVEWAPGLELLLLSYPTTVPVSSVPLDSVDESVEMVKEMVEAGILVVQ
The following text describes a protein:
Function:
Transcriptional regulator. Critical factor essential for ovary differentiation and maintenance, and repression of the genetic program for somatic testis determination (By similarity). Prevents trans-differentiation of ovary to testis through transcriptional repression of the Sertoli cell-promoting gene SOX9 (By similarity). Has apoptotic activity in ovarian cells (By similarity). Suppresses ESR1-mediated transcription of PTGS2/COX2 stimulated by tamoxifen (By similarity). Activates SIRT1 transcription under cellular stress conditions (By similarity). Activates transcription of OSR2 (By similarity). Is a regulator of CYP19 expression (By similarity). Is a transcriptional repressor of STAR (By similarity). Participates in SMAD3-dependent transcription of FST via the intronic SMAD-binding element (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MMASYPEPENASGALLAPETGRAAKEPEAPPPPSPGKGGGGGTGTAPEKPDPAQKPPYSYVALIAMAIRESAEKRLTLSGIYQYIIAKFPFYEKNKKGWQNSIRHNLSLNECFIKVPREGGGERKGNYWTLDPACEDMFEKGNYRRRRRMKRPFRPPPAHFQPGKGLFGAGGAAGGCGVAGAGADGYGYLAPPKYLQSGFLNNSWPLPQPPSPMPYASCQMAAAAAAAAAAAAAAGPGSPGAAAVVKGLAGPAASYGPYSRVQSMALPPGVVNSYNGLGGPPAAPPPPPHPHSHPHAHHLHAAAAPPPAPPHHGAAAPPPGQLSPASPATAAPPAPAPTNAPGLQFACARQPELAMMHCSYWDHDSKTGALHSRLDL
The following text describes a protein:
Function:
Acts as a negative regulator of osmotic stress-induced gene expression. Involved in the regulation of thermotolerance responses under heat stress. Functions as an upstream regulator of heat stress transcription factor (HSF) genes. Negatively regulates HSFA1A, HSFA1B and HSFA1D, but positively controls the expression of HSFA1E, HSFA3, HSFA9, HSFB3, and DREB2C. Forms a complex with CPL1 that modulates co-transcriptional processes such as mRNA capping and polyadenylation, and functions to repress stress-inducible gene expression. Regulates pre-mRNA processing under salt stress. Involved in primary miRNA processing and pri-miRNA biogenesis. Binds both intronless and intron-containing pri-miRNAs. Acts as a regulator of biotic stress response gene expression and basal JA-mediated responses involved in defense. Acts as a negative regulator of resistance to the fungal pathogen Fusarium oxysporum.
Subcellular Localization:
Nucleus. Nucleus speckle. Note=Localizes predominantly in nuclear speckles.
Sequence:
MERSRSKRNYHYDQDYDGDSMPRSKPRYNNNYHFGGGGGGNNRYRGGGGGGGGNGRPSKSHPETMATTTYRILCHDAKAGGVIGKSGTIIKSIRQHTGAWINVHELVPGDAERIIEISDNRRRDPDGRMPSFSPAQEALFSVHDRILESEAQFGYGGPPPEEEEDYGGVRPGGGRVVTRLVVSRMHVGCLLGKGGKIIEQMRIETKTHIRILPRESNLPRCVSLSEEIVQIVGELNAVKNALAIVSSRLRESQHRDRSNFQGRSHSPERSFAAAGDDYMPQLRRQSSDRFPRGNFRNNNFSSRQSNYAEEAPAVPVGENVYSEELVFQILCPADKIVRVVGESQGIIDLLQNEIGVDVRVSDPVAGSDEQIITISSEEAPDDPFFPAQEALLHIQTQIIDLIPDKDNLITTRLLVPSRDSICLEGKAGSVSEISRLTGTSVQILAREEIPRCASINDVVIQITGEIRAAREALVELTLLLRSHMFKELSQKETPPASTSTTGPLEGVAGVMEVASSNNTIQSREGPTSSNLNLQQVSTILPQFKEGFGSVAKAGESEHREEVPVTTSRMAVPLVTRSTLEVVLPEAVVPKLVTKSRNKLAQISEWSGASVTIVEDRPEETQNIIRISGTPEQAERAQSLLQGFILSIQEDGP
The following text describes a protein:
Function:
Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Subcellular Localization:
Nucleus.
Sequence:
MEPDRIPTHPPILGPSAQNHMSASMMSHIDPVRPTNRNLRELQEGFTGDLSALQRAMHSFLSSDELIASIKDRIERGKSCVDIDLLTLHNSPDDSHRMLYTTLLTTPDVFQVFDLVLHQVALSIVVQMRDEHLKRLWDENPNISRDVFLSSTQYKNAISYYSRVANNLHLRCYPVNFPEDDSQSLRTLGPMHADSLISVSGMVSNISSRVPEMVEACFQCTVCKDVKKASVKRGKIISPIQCTNCDSLQSIEIVHNMCTFIDKRVIKIQEAPDQLTSGTPPISCSFVAYDLDLSGIRPGDRVVVVGIYRLRQTRPKQSQAVCNAALRPVIELLSIFISDSAATDSYLSAKKDSDVTDYERLKSLDPNTSYAEYYNHVTRLFPDMIPETDSGSDKRFLKLINSIAPSIFGPAYSDIKTGLLLQCFGGVQKDSYRGQIHVLLVGDPGLAKSKLLQYVAKISPRSVYTSGKGSSQAGLTATVSRHPETHEFYLDPGALLLSDGGICCLDEFDKSSEDVRSSLHEVMEHGQLSIAKAGILATLSAKTSILAAANPIDSCYNPKRTVVQNLNLPPSLLSRFDLIYLLLDNRHDTEADRALASWLVSMYISSGQAEHSGHLSSKNTAAATPDAWDPQVLRQYIYFAQKLSPVLSKSAQDALLLSYNQLRSGSYSASGRITATPRQLMSLIRLAEARARIRFSNFVTANDILEVSRLMTRAMHLAMTDQSGFINMDIFAETGGTSEAASLDMLCRAIIRYKSQRIAELQSVENEEQLTVTVLELLANMNRGLSTDQISTGESVSSELLNTALDTLVSQGLIVRNGDDVIFI
The following text describes a protein:
Function:
Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome.
Sequence:
MAAIIICSDFGAPKNKKEEQVISLGPQVAEGENIFGLCHVFASFNDTFVHVTNLSGKETICHVTGGIKVKVDRDEYSPYRCKELGITALHIKLQATGGNRTKTPGPGTQSALTALAHSGMKIGCIEDVTLIPSNSTHRKGSCCGHSL