lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Global transcriptional regulator. Modifies gene expression by affecting chromatin.
Subcellular Localization:
Nucleus. Chromosome. Note=Localizes to pericentric heterochromatin associated with the X chromosome.
Sequence:
MGKKNPNARHTDAATPLTTDDSNSSSVSRRESATESKSASESESSPPRSNTKQSRTHKNVKASGKATVSSSSDSDQAVANSSANDEEKEPVCKIRIVPLEKLLASPKTKERPSRGSQQKNVTINDSSDEEPLKGSKLVLPARKSRNKNASIIELSDSEEVDEEEESLLVAIPLPKEAQQTKPEKNSSKASKESIEKRQKAQKEATTSSARAIRSVNGTRRGSLSSERSSRASSSRAESPPRPKRCVVRLKRVSLPKTKPAQKPKKMSSDSEEAATTSKKSRQRRSKSESEADSDYEAPAAEEEEEEERKSSGDEEEAANSSDSEVMPQRKRRRKKSESDKGSSDFEPEEKQKKKGRKRIKKTSSGESDGDGDDDKQKNKRKHIRKIIKTKDLDLTTKEAAKEEDDRRKRIEDRQKLYNRIFVKSESVEINELVLDFDEESKKALLQVDKGLLKKLKPHQVAGVKFMWDACFETLKESQEKPGSGCILAHCMGLGKTLQVVTLSHTLLVNTRRTGVDRVLIISPLSTVNNWAREFTSWMKFANRNDIEVYDISRYKDKPTRIFKLNEWFNEGGVCILGYDMYRILANEKAKGLRKKQREQLMQALVDPGPDLVVCDEGHLLKNEKTSISKAVTRMRTKRRIVLTGTPLQNNLREYYCMIQFVKPNLLGTYKEYMNRFVNPITNGQYTDSTERDLRLMKHRSHILHKLLEGCIQRRDYSVLAPYLPPKHEYVVYTTLSELQQKLYGYYMTTHREQSGGDVVGKGARLFQDFQDLRRIWTHPMNLRVNSDNVIAKRLLSNDDSDMEGFICDETDEDEAASNSSDSCETFKSDASMSGLAASSGKVKKRKTRNGNAGGGDSDSDLEMLGGLGGGSSVQKDDPSEWWKPFVEERELNNVHHSPKLLILLRLLQQCEAIGDKLLVFSQSLQSLDVIEHFLSLVDSNTKNYEFEGDVGDFKGCWTSGKDYFRLDGSCSVEQREAMCKQFNNITNLRARLFLISTRAGGLGINLVAANRVVIFDVSWNPSHDTQSIFRVYRFGQIKPCYIYRLIAMGTMEQKVYERQVAKQATAKRVIDEQQISRHYNQTDLMELYSYELKPSTEREMPILPKDRLFAEILTEHEKLIFKYHEHDSLLEQEEHENLTEEERKSAWAEYEAEKTRTVQASQYMSYDRNAFGNQVMGQFGNASGSVTSNKIFGFRSDILLQLLNMKISKDHQELNQNQVIQLVPTYLQQLYNEMNNGDPTMYKDLLNLHSNIVHPSGMYMNPLLYANQNPNAAGYNQGTGGVPPMAGGSVAHGPPAAPAPGFEPDKVYEID
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; The proteasome is 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:
MNGFIHSFIQDAGSLESSAKEGWGRVRAWALSLSLWLQLSDIFVIRLDGFQKAAVQLVKPAKGTTTLAFVFKHGVIVAADSSASMGNSISSQSVKKILEINPYLLGTMAGGAADCQFWQRNLGTRCRLHELANKRHISVTGASKLLANTLYSYRGMGLFMGTMIAGWDETGPGLYYVDSEGGRVKGTRFSVGSGSTYAYGVLDTVFKQDMSIDEAVELARRSIYHATLRDGASGGVVSGKQSMLVVTVRDHCEAQNFDSPFAHFSIYYFASSLETLLKCSLLCGPSGWKKMSGDDGGELHHSYYPVQETPAEAEMSEASV
The following text describes a protein:
Function:
Transcriptional repressor.
Miscellaneous:
MISCELLANEOUS: Does not bind methylated DNA.
Subcellular Localization:
Nucleus. Note=Nuclear, in large foci.
Domain:
The N-terminal half of the protein mediates transcription repression.
Sequence:
MGKTSQRKQCDCENPSKPCLSTSIPLRMSSYTFKRPVTKITSHLGNEVRYYQWEETLEKPEQACWQKRLQGLQAYSSAGELLSTSDLAKTLKDLTSTDTVASASDTQATSIDITSVPTLESSSHLANMIPEAGPQILCKEFLVTEQDIINQERKVKIARERLAVALIAHKLASEMETVRGSRKANL
The following text describes a protein:
Function:
7beta-hydroxysteroid dehydrogenase that catalyzes the reduction of the 7-oxo group of 7-oxo-lithocholate (7-oxo-LCA), to yield ursodeoxycholate (UDCA). As R.gnavus is a common core bacterium of the human gut microbiota, this enzyme contributes to the formation of UDCA in the human colon. UDCA is regarded as a chemopreventive beneficial secondary bile acid due to its low hydrophobicity; it protects hepatocytes and bile duct epithelial cells against necrosis and apoptosis induced by more hydrophobic secondary bile acids like deoxycholate (DCA). This enzyme is also able to catalyze the reverse reaction in vitro, i.e. the oxidation of the 7beta-hydroxy group of UDCA to 7-oxo-LCA, but much less efficiently than the reduction reaction.
Sequence:
MTLREKYGEWGIILGATEGVGKAFCERLAKEGMNVVMVGRREEKLKELGEELKNTYEIDYKVVKADFSLPDATDKIFAATENLDMGFMAYVACLHSFGKIQDTPWEKHEAMINVNVVTFMKCFYHYMKIFAAQDRGAVINVSSMTGISSSPWNGQYGAGKAFILKMTEAVACETEKTNVDVEVITLGTTLTPSLLSNLPGGPQGEAVMKTAQTPEEVVDEAFEKLGKELSVISGERNKASVHDWKANHTEDDYIRYMGSFYQE
The following text describes a protein:
Function:
Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
Sequence:
MRGSGRSDIVISAVDALDICITLARNDCDKYPGSVAAKLGVSSGLIYLVGQPTINWGDSDQPRPFRQRRYFYYLSGVEEADCYLTYDIKNDLLTLYVPDFDLHRAIWMGPTLTVKEARERYDVDQVRYHASLKGDIQRWADNYNKTSLLYILHDTQKPQVLSNELRLDDELLLPAMDAARGIKDEHEIRMIREANRVSALAHRKVLENVLRMSTEAEIEGLFLDTCISHGAKNQAYEIIAGSGENAAVLHYVKNNEPLQGRQLVCLDAGAEWNCYASDVTRTFPLAADWPTARARDIYQLVEEMQEECIKRIQKGVRFLDLQVLAHVIAIEGLMRLGILKGGSVEEIRESGASTVFFPHGLGHHVGLEVHDVSAKRLTAVEGDKEYYSSILVPSMSHCPCTLSAPLLEEGMVVTVEPGIYFSRLALANARKLAFAKYINFDEAEKYIPIGGVRIEDDILVTSSGHENLTTAPKGEEMLEIIRRGIDS
The following text describes a protein:
Function:
May be involved in environmental stress response.
Sequence:
MGSQQKPCANNCGFFGTSEKRNLCSKCYKDLCLEEELAAMKSVLCSPAPPSPGTAGQSKPANRCGTCNKKVGLTGFACKCGSTFCGVHRYPEKHECTYDFKGEAREAISKANPVVKGDKVDRF
The following text describes a protein:
Function:
Putative adhesin which may be involved in cell adhesion and virulence (By similarity). Involved in the regulation of filamentous growth.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MFASYLLLVLWIIRLVPTTHAHTGNDAEYLLNTVLKRDATSLSRNAYLDSEATSGATNYCSDCDNDEVIVTVDGTSTIWTILLDSTISTLVTTTSTEKTTLTSCGQSCTKSKDASSVSSSSASSSTSRSLIFRTSTKTVTDTTTLPTVTEINTFTTTDSHIVLVYTDINSESTITGDYTFIKNKNTRTVIITDYVTSTVGGETQIVTQTTTSVVYELVVTCPDHDFATTLTGSETFVPPTTAPKPVETPSPEPSTTILSIKSESSVPSATTSVLDTSITLETSSSSIEFSTSTQESSSIGPSSSSSIGSCTSSSISTEESLSTTKLSSSFTSISSWEELSSSFTQSTTSSNAEPSSSFAESFTTESLSSTIEATSSMEDISNNSVLTSSIFSETTTNESSSYTDEPSSSEEITNTYEPSSSTESSTTDQFSSLLSSSLPVTSTSSTTISSATPITTVLSTSITSQDTNCEATITNISTNTLIETITVNGNTTIYTETQLSTYLTSNTSINCPNTNSATTTTTQVIPTATTEQIHTTTLNGSIIVSTETATLKTTVIITHCPECTNESSTSEYSSSLKAESSQQSIPTIESNLSELSVSSTLSLVESTASGKCSGLTTTTFTSIVSTTTESIYTITSNESTFEMTTTVTNIGTIVITTCPTITPVSSSYSSSESLSSSVSTSLLTESNSTISQSTVSTDKSSLTNDNQISTVSTETPLTSITIIETTSKTTESLYTTTSNDSTHIFTTTIIDVQTNTIVTCPTTTSTLTSSHTSDNEKPASLSSSSLIESDHIADGTTTSTTFQSTSTTTVDHHCSSCSEILLSTSSSIIGNKSTSTSISSIETSASSSYHSSEPEVMSSSSSTSIKQSSDSIPSTSQTHVSTTSSSVSSLETTTTTTENSPTSNGFSSSSIVTSVNVPDYVSSSVSSTSSTTSSPSTESSSNGLVSTVTESSTANENTSEITTIDNTSITSEKVTGTNSNPKTSEIIKDATITTSGNVESLHSTTPISSTSIISTNAISSSDTTTLTITNTLTYSIDSITTMKTSSITTAPPPPQQKESSSVLSSSLIINSSTPTIIPTINIPITFEGNANSLGLKNGDNSWIIGIMMIGLLMI
The following text describes a protein:
Function:
Microperfuranone synthase is the only protein required for the biosynthesis of the secondary metabolite microperfuranone from phenylpyruvic acid (PPA). Several steps for the microperfuranione biosynthesis have been proposed. These steps include the activation of PPA, by the micA adenylation (A) domain to AMP-phenylpyruvic acid followed by loading of the PPA unit to the thiolation and peptide carrier (T) domain and eventually transferring to the thioesterase (TE) domain. After loading another PPA unit onto the T domain, aldol condensation establishes the carbon-carbon bond between the alpha- and beta-carbon of the two PPA units. Sulfur-assisted furan ring formation, TE domain mediated hydrolysis, decarboxylation, and keto-enol tautomerization would generate microperfuranone attached to the T domain. Finally, microperfuranone is released by the TE domain.
Sequence:
MVGSVVEAHRQSVGCLRNLSQLLAWASNTSGGLIFYSREDDVLTSTRISYAELLADAGEKARLIGQITGLSSESIILLHFDTQREVIEWFWAATLAGYLPAISTPFVDDTARRKAHLLHLHAQLNQPVVLTSKRLVPEFLGLEELRLHDVESLLSSAAKDGLIQYLGVQKLAEDVAVLMLTSGSTGSAKAVPLRHGQLLTAIQGKSTHHGTLPGDVFYNWVGLDHVASLTEIHLHALILGSDQVHTAASELLRNSLQFVRLLDTHKVAYTFAPNFFLTKVLDSLRENPTFTADLSSLKALISGGESNVVVTCDKLTRELRRRGVQAEVIRPGFGMTETCAGSIYSRACPSYDIRQSLEFASLGSCIPGMHMRIMSITEPGKLAAPGESGELQVAGPVVFDHYYNDETATRNAFTPDGWFITGDLGWIDDAGNLNLAGRTKDTIIVNGVKWSSTELEAAIEEEAVSGLVRSFTVVVPTRPPGSATEEIAVVYSPAYAPEDYHARYETAQVISKTVSLLTGTKPARLIPLPQSLLEKSSLGKISHSKVRAALESGEYASIERADQLILAQYRQFKWRPAKSDSERAVQKALVEFLQVPAEGINMDDSIYDLGVSSLNLILLRSTLQRMLDPKIDIPLSIILNNPTPGAIARSIDSSRSSLAGYNAIVPLQQHRHGGTPLFCIHPGSGEVLVFVALAAHFPTRPVYALRTRGYGSNEQLFGSIEETVETYATQIRQVQPHGPYAIAGYSLGSTLAFEVAKVLEAQGEEVKFLASIDYPPHIAHYVRDLNWTDVLLHIAFFLELIDEKTMVEVTPYLHTLDRQTALTHILNIGDAERARALAIDTKHLGLISDIAENFRVNVKTYKPQGKVQHLDVFVADPPTYAARDRKDWRENKLGRWVDFCETKVEFHDCPGIHAKMLNREHIAGFAKVFKAAMRRRGV
The following text describes a protein:
Function:
Binds to the 23S rRNA.
Sequence:
MQVILLDKIGNLGSLGDTVNVKSGYARNFLIPQGKAVMATKANVAMFESRRAELEAKVAEQLAAAQTRADQVNALEAVVIASKAGDEGKLFGSIGTRDIADAITAAGVKVSKSEVRLPEGALRNVGAYEVSVQLHSEVFATAKVQVVAE
The following text describes a protein:
Function:
Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds to sites in the 5'-flanking sequence of its coding region with various affinities. The consensus sequences of the high and low affinity binding sites are 5'-TAATGA[CG]-3' and 5'-CTAATTTT-3'.
Subcellular Localization:
Nucleus.
Domain:
The proline stretch works as a part of the transcriptional activation domain.
Sequence:
MTMSSFLINSNYIEPKFPPCEEYTQHSGSAGSSASYHPHHPHPHAPPPPPPPPPPHLHAAHPGPALPEYFPRPRREPGYQAPAAPPGPPGPPPEALYPAQAPSYPQAPYSYSSAGSAAPGPEQPPPGASPPPPPPAKGHPGPAQPLLPGHALQRRCEAAPAAGAGTGPGCALLPDKSLPGLKGKEPVVYPWMKKIHVSTVNPNYSGGEPKRSRTAYTRQQVLELEKEFHFNRYLTRRRRIEIAHTLCLSERQVKIWFQNRRMKWKKDHKLPNTKMRSSNQPSLGQQQAKAQTQGHPRPLDGAAPNAAAL
The following text describes a protein:
Function:
Functions as a receptor binding protein (RBP) and probably mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the K21-type polysaccharides of Klebsiella pneumoniae capsule.
Subcellular Localization:
Virion. Note=Tail appendage.
Domain:
Consists in a catalytic region, a carbohydrate binding region and a lectin-like region. The active site consists of catalytic dyads Asp-Glu located at the interface between 2 adjacent subunits. The lectin-like region is probably involved in trimerization.
Sequence:
MSTELTQAKGSTSRYTSRKSCAIEFNTKIDEVQYISVGLDTSTIKVFIDNNTQIPYVGNFINGNVISWVSDPVKCILTTSSGTYTLFSYGLTKNIPNLLDYDSDSATDDSTRFKKAILAGTESLYIPPREIYKDVMIGELDITSTLRLWGDSGSNINTGGSTIKKIASASYGIHFNGTGQTTRPMGGGLFNLQVRGESSTDTGPLIKVTSWSYMRINNCAIQNISDWGIIARDMMESSCEYTLFRRIGSDTTGILLMDDYIGTPNSNVNNFHFSNNTLGYSSGNWIKSSTNSNPDLIWIERNKFEWDGTPTSANITPKAVIDFGQMSRCRITNNGFTHFTTDHNNYEGILRMRSGCAYLTKLIDNDALSCSGYFGSVEGGKLQASGNFYNRGVVASGNMQFNVTSTRPQSIEPVICFTSNGNITSVGDYIDPNFISAHNMFGTSNNMFQTDTMASLYTTMNVPSLVEIRRFQLGKQYLDSNTVLTIQARVKCVDTAGTNGELKLNIDGTTDIGSSTITASTGWQLITFQLKPSQIGAGSLRFINSGTVSILFDGIYIQRSKYIDWNFAFNPGAIAAGASITSALQSYTDTIGVTGLIQSFSQPKFDGNINGLLCSVVSNNINGSFYVTLYNPTASPITPTITRCYIRLFLI
The following text describes a protein:
Function:
Activator of the canonical Wnt signaling pathway by acting as a ligand for lgr4-6 receptors, which acts as a key regulator of angiogenesis. Upon binding to lgr4-6 (lgr4, lgr5 or lgr6), lgr4-6 associate with phosphorylated lrp6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Acts both in the canonical. Wnt/beta-catenin-dependent pathway and in non-canonical Wnt signaling pathway. Acts as a key regulator of angiogenesis by controlling vascular stability and pruning: acts by activating the non-canonical Wnt signaling pathway in endothelial cells (By similarity). Can also amplify Wnt signaling pathway independently of LGR4-6 receptors, possibly by acting as a direct antagonistic ligand to RNF43 and ZNRF3 (By similarity).
Subcellular Localization:
Secreted.
Domain:
The FU repeats are required for activation and stabilization of beta-catenin.
Sequence:
MQLQLISIVLILHFMEYTNCQHHGSRHRGNKQVSGVSSQGCQGGCQTCSVYNGCLTCKPKLFIHLERDGMRQIGVCLASCPNGFYGTRSPDRNDCIKCGSECDSCFNRNFCLRCRAGSYLHKGKCMESCPDGLVPSDTKKECVAACPALCDLCQNSDTCTRCVPGHFLHAGQCHHVCPDEFEPNDSMECIPTVHCEVSEWSEWGTCSRSGKTCGFKWGEETRTRKVLQNPSPMGSPCPPTSEKRECFVKKKRCKPPKGQRRGEKKKRFNLQEKVTAEARRERKREREKETIDREESENRNKTEQRRRRDQSRDAGTV
The following text describes a protein:
Function:
Endonuclease that is involved in the suppression of homologous recombination and thus may have a key role in the control of bacterial genetic diversity. Has ATPase activity. Binds to DNA; Acts as a ribosome collision sensor, splitting the ribosome into its 2 subunits. Detects stalled/collided 70S ribosomes which it binds and splits by an ATP-hydrolysis driven conformational change. Acts upstream of the ribosome quality control system (RQC), a ribosome-associated complex that mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes and their subsequent degradation. Probably generates substrates for RQC.
Sequence:
MDYLESLDFPKVVEIVKKYALSDLGRKHLDTLKPTVNPWDELELVEELLNYFNRWGEPPIKGLNDISQEVEKVKSGSPLEPWELLRVSVFLEGCDILKKEFEKREYSRLKETFSRLSSFREFVEEVNRCIEQDGEISDRASPRLREIRTEKKRLSSEIKRKADDFVRTHSQILQEQMYVYRDGRYLFPVKASMKNAVRGIVHHLSSSGATVFLEPDEFVELNNRVRLLEEEERLEISRILRQLTNILLSRLNDLERNVELIARFDSLYARVKFAREFNGTVVKPSSRIRLVNARHPLIPKERVVPINLELPPNKRGFIITGPNMGGKTVTVKTVGLFTALMMSGFPLPCDEGTELKVFPKIMADIGEEQSIEQSLSTFSSHMKKIVEIVKNADSDSLVILDELGSGTDPVEGAALAIAIIEDLLEKGATIFVTTHLTPVKVFAMNHPLLLNASMEFDPETLSPTYRVLVGVPGGSHAFQIAEKLGLDKRIIENARSRLSREEMELEGLIRSLHEKISLLEEEKRKLQKEREEYMKLREKYEEDYKKLRRMKIEEFDKELRELNDYIRKVKKELDQAIHVAKTGSVDEMREAVKTIEKEKKDLEQKRIEEATEEEIKPGDHVKMEGGTSVGKVVEVKSGTALVDFGFLRLKVPVSKLRKTKKEEKKETSTFSYKPSSFRTEIDIRGMTVEEAEPVVKKFIDDLMMNGISKGYIIHGKGTGKLASGVWEILRKDKRVVSFRFGTPSEGGTGVTVVEVKV
The following text describes a protein:
Function:
The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for responses to chitin and acts redundantly with MEKK1a.
Subcellular Localization:
Cell membrane.
Sequence:
MVEERGSSRSSRGGSWGSGEDGGSSHGGKGVPKLSRTVAKKIHKYDVSADHSDYEDDGSVHSTSSSGSRRNPLSKSIIQQQSFRVGANFEEDLKTLYELIGVSKPADLAISASDWQSRGKSIAYSQPLSSPSLSQEHGEASHSNDLKPSIIDFRSEAPAASPRELPVAPVKLDAHERMTYRSDYVNSQPQNHYGRKNSPSQRSPPPESFPAFDSSPSRLGREGYGLHRMQSDPVMPTLGALSPLGTGNAHPESAGSTATRRWSFDLVPGNHEGDYANMSQVVRDNLPSAAVAMPKNGLVRRSPIIRDPNRSNSSVSNPYAQRQYPNLAEEAESSAKPESSAIPDSSAMPELPAKLESTAVPELSAKPESNAKPESEPEQDSSVEARTEHYGSVRKSKIPSALIIDKFEEPSIVSTGRSPGVVSKRPPWDTWFKGDFIGSGTFGSVYEGIDNNGMFFAVKEVSLKDQGKVGQEAIKQLEHEIALLSDIQHPNIVQYLGTERDDEKLYIFLELVSKGSLASLYKKYYFVYDQVRAYTKQILSGLKYLHDRKIIHRDIKCANILVDTNGVVKLADFGMAKQVDKLGLLKSFMGSAHWMAPEVVNPKRQYNFLADIWSLGCTVLEMATGDAPFGELECHSVLWKVGNGEGPLIPDDLEDEMKDFISKCLEVTVGNRPTCDMLLTHPFITGEPMTGPVKLVPMPELSTISEERSIDVSESPSIATSSQSGSSPSVAGDAVSPASVAVRPRSMRTLRSEFSMSSPESIAS
The following text describes a protein:
Function:
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Sequence:
MANYFNTLNLRQKLDQLGRCRFMDREEFADEANFLKGKKIVIVGCGAQGLNQGLNMRDSGLDISYALRPEAIAEKRASFQRATENGFKVGTYEELIPTADLVVNLTPDKQHSKVVADVMPLMKKDSAFGYSHGFNIVEVGEEIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHKAGVLESSFVAEVKSDLMGEQTILCGMLQAGSIVCYDKLVADGKDPAYAGKLIQYGWETITEALKQGGITLMMDRLSNSAKLRAFELAEQIKESLGFLYYKHMDDIISGHFSATMMADWANGDKDLFAWREATGKTAFENAPKYDGKISEQEYFDNGVLMIAMVKAGVELAFDAMVASGIYEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYGNYLFSNVATPILAKEIIPNLQKGDLGEPTPAVEVDNITLRDVNDAIRNHPVELIGQELRGYMTDMKRIAVAG
The following text describes a protein:
Function:
Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols; Oxidizes mannitol to mannose. Provides the initial step by which translocated mannitol is committed to central metabolism and, by regulating mannitol pool size, is important in regulating salt tolerance at the cellular level.
Sequence:
MSSEGGKEDCLGWAARDPSGFLSPYKFTRRAVGSEDVSIKITHCGVCYADVAWTRNVQGHSKYPLVPGLEIVGIVKQVGSSVQRFKVGNHVGVGTYVNSCRECEYCNDRLETQCEKAVLTFDGIDADGTVTKGGYSSHIVVHERYCFRIPENYPMDLAAPLLCAGITVYTPMIRHKEPTCTSISKKEGALSLLGADHFVISSDVEQMKAIAKSLDFIIDTAAGDHPFDPYMSVLKTGGILALVGFPSEVKFSPASLNLNMRTVSGSVTGGTKDTQEMIDLCAAQKIYPKIEVIPIDYANEALERLIKRDIKYRFVIDIENSLK
The following text describes a protein:
Function:
Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.
Sequence:
MEKSPQKFYEIIINANSTVDQIYTAIFELRTINNQEAVELLKQGFHHLNKVENKSCLLLHEIAYALGQADLGLEPLITQFLIQIISDDQQFDVVRHEGAEALANINQKEALEIFEKYSKKNVNDDLNILQDTCTIGLEKAKSINELGHLYGKRYLGTREPAAPFEHLDKNPVEYILDDQTTLFNKYRALYYLRNNAETYFDKIDQLLTSNKLGALFKHEICFVIGQVGEAPKQIHEALINMIKDENQPAIARHEAIAAFQTVSSNKEITLEILNAYAKSPDQIVRETAIVSLKMMEFYG
The following text describes a protein:
Function:
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Sequence:
MIERIYLAKPRGFCAGVVMAIQAVEKAAVREDKPVTVYHSIVHNHTVVERLSEGGRVHFVEDLDAVDALPDSGDTVIFSAHGISPAVRERARSLGLSTIDATCPLVTKVHTEAKKYAREGYTILLIGDSAGHQEVIGTRGEAPENTILVGVLGKTGPGLNDPHAVQVPDPERLVVLTQTTLSVDDTRKTVDILKARFPALVVPPSEDLCYATKNRQDAVKNIAPNVDAFLVLTSTHSSNGMRLLELAEAECGRAYRLETAADLTRLEQNGDLGGVRSVGITSAASTPDDLVQDVVAHFRALNPALEVIEEGEWENIEFREPKKIAPTQELPRTMQ
The following text describes a protein:
Function:
Inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Subcellular Localization:
Cytoplasm. Note=Localizes to the inner membrane through interaction with PilN.
Sequence:
MLGLIKKKANTLLGIDISSTSVKLLELSRSGGRYKVEAYAVEPLPPNAVVEKNIVELEGVGQALSRVLVKAKTNLKSAVVAVAGSAVITKTIEMEAGLSEDELENQLKIEADQYIPYPLEEVAIDFEVQGLSARNPERVDVLLAACRKENVEVREAALALAGLTAKVVDVEAYALERSYALLSSQLGADTDQLTVAVVDIGATMTTLSVLHNGRTIYTREQLFGGRQLTEEIQRRYGLSVEEAGLAKKQGGLPDDYDSEVLRPFKDAVVQQVSRSLQFFFAAGQFNDVDYIVLAGGTASIQDLDRLIQQKIGTPTLVANPFADMALNGKVNAGALASDAPALMIACGLALRSFD
The following text describes a protein:
Function:
Promotes Holliday junction (HJ) branch migration and unwinds Y-shaped DNA (but not replication forks or dsDNA) in an ATP hydrolysis-dependent manner. Stimulates cleavage by HJ resolvase Hjc. Unwinds Y-shaped and 3'-flap DNA substrates. In the absence of other proteins stabilizes replication forks (prevents spontaneous unwinding); Hjc, Hjm (Hel308) and PINA coordinate HJ migration and cleavage of replication forks in a coordinated way. Inhibits the 5'-3' (but not 3'-5') helicase activity of helicase Hjm (Hel308) on overhang DNA. Probably acts as an ATP-dependent pump that pulls DNA through the hexamer (By similarity).
Miscellaneous:
MISCELLANEOUS: A triple mutation (Arg-147-Lys/Ile-199-Ser/Arg-206-Ala) forms monomers rather than hexamers where the PIN and helicase domains are in very different positions than in wild-type protein, see PDB:5YWW.
Domain:
The C-terminus (residues 434-505) forms a novel KH fold; this domain binds ssDNA but is not sufficient on its own to interact with Hjm. It is probably destabilized in the homohexamer (Probable).
Sequence:
MNDLMLDKSALLFGVSKYLEKGIITGNVLIHKSLLAELERESNDGLVSAEIALDEVKKLKDITERILVNFEIVGDDSKKGEANELSREYCLEKGCIIVTADETQKKICDAMGIQYNFLQPLKQGLSFESFFDDETMSLHIKEDTVPRAKKGKPGNWKFVNLSDKPMLSTDVRMIANEIINAVRLIKGSFVEIERRGSLIIQLGNYRVVITRPPLSDGWEITITRPVVRKRLEDYNLDERLIKRLEERAEGIIIAGAPGMGKTTFAQALAEYYMRLGKIVKTIESPRDMHLPPEITQYSKNYAEIGELHDILLLSRPDYTVYDEMRNDEDFKLYVDLRLAGVGMVGVVHATSPIDAIHRFVNRVDIGTIPNILDTIIFINSGNVSKVYTLEMTVKVPAGLKEADLARPVVEIKDLATGNTEYEIYVFGEQTMIVPVNRGITMSNMEFKISKIVNNIIPNATVKYEDGEYVIVIPKEEIGKYNRKLVQRLKRLEKKNNIKIKIKLSD
The following text describes a protein:
Function:
May form part of a complex of membrane proteins attached to acetylcholinesterase (AChE).
Sequence:
MNWGGALGVLLGGGATLLLSFLCMPALLPVASRLLLLPRALLSMASGSPPSQPSPASGSGYVPGSVSAAFVTCPNEKVAKEIARAVVEKRLAACVNLIPQITSIYEWKGKIEEDSEVLMMIKTQSSLVPALTEFVRSVHPYEVAEVIALPVEQGNPPYLHWVHQVTESVSGSGKALP
The following text describes a protein:
Function:
Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly.
Subcellular Localization:
Nucleus.
Sequence:
MASRVNIVQVQILDNPAMFVDKFKLEITFEVFEHLPHDLEWELVYVGSGTSRDFDQVLDSALVGPIPEGRHKFVFDADHPDISKIPVDDIVGVSVLLLRCKYNDQEFINMGWFVANEYTEEELKENPPSQPLIEKLSRKVETEDLRITTFPIRWTDEDPVAEPVEDEANRVFAEDDLMPLNDDGQEDDDEEEEDDDEMEANAEEVDLNESFNERLANALDGAEQKGADEKMEDDGANEDVDMADDEPGVQINTDTKVPESMAEPLSDKTNNEMVQ
The following text describes a protein:
Function:
Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-CGAGGCG-3' motif in vitro. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE-dependent splicing. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway.
Subcellular Localization:
Nucleus.
Sequence:
MSGGGVIRGPAGNNDCRIYVGNLPPDIRTKDIEDVFYKYGAIRDIDLKNRRGGPPFAFVEFEDPRDAEDAVYGRDGYDYDGYRLRVEFPRSGRGTGRGRYGPPSRRSENRVVVSGLPPSGSWQDLKDHMREAGDVCYADVYRDGTGVVEFVRKEDMTYAVRKLDNTKFRSHEGETAYIRVKVDGPRSPSYGRSRSRSRSRSRSRSRSNSRSRSYSPRRSRGSPRYSPRHSRSRSRT
The following text describes a protein:
Function:
Involved in leaf vasculature patterning.
Subcellular Localization:
Secreted.
Sequence:
MANHKNLFFLCFLIGLGLCSARRALLSSSESEAEVAAYGVNSGLSAGLGVGIGGGPGGGSGYGGGSGEGGGAGGHGEGHIGGGGGGGHGGGAGGGGGGGPGGGYGGGSGEGGGAGYGGGEAGGHGGGGGGGAGGGGGGGGGAHGGGYGGGQGAGAGGGYGGGGAGGHGGGGGGGNGGGGGGGSGEGGAHGGGYGAGGGAGEGYGGGAGAGGHGGGGGGGGGSGGGGGGGGGYAAASGYGHGGGAGGGEGSGGYVP
The following text describes a protein:
Function:
Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine (By similarity).
Sequence:
MRLAVIGAMEEEVTILRNKLENAKTETIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGFHHTLNVGDVVISTDVRHHDVDVTAFDYEYGQVPGLPAAYAADEKLISITEEAVSELDGIQVAKGTIATGDSFMNDPKRVEEVRARFSDLYAVEMEAAAVAQVCHQFKTPFVVIRALSDIAGKESHVSFDQFLEQAAVHSTELVLKVIKRIH
The following text describes a protein:
Function:
May play a role in mitochondrial aerobic respiration. May also regulate mitochondrial organization and fission; Plays a role in mitochondrial aerobic respiration. Regulates mitochondrial organization and fission.
Subcellular Localization:
Mitochondrion.
Sequence:
PHPPPPPPPLPPPALGLHQSTSAVDLIKERREKRANAGKTLVKNNPKKPEMPNMLEILKEMNSVKLRSVKRSEQDVKPKPVDATDPAALIAEALKKKFAYRYRSDSQDEVEKGIPKSESEATSERVLSLPAGFIQPHVSKHCLG
The following text describes a protein:
Function:
Involved in pre-mRNA splicing as a component of the spliceosome.
Subcellular Localization:
Nucleus.
Sequence:
MASGSGSKNDFRRKWDKDEYEQLAQKRITEEREKKDGKPVPPIKRELLRHRDYKVDLESKLGKTIVITKTTPQAEMGGYYCNVCDCVVKDSINFLDHINGKKHQRNLGMSMRVERSSLDQVKKRFEVNKKKLEEKQKEYDFEERMKELREEEEKAKAYRKEKQKEKKRKAEEDLNFEDDDEMAAVMGFSGFGSSKKGH