lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Probable core component of cullin-based SCF-like E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit.
Subcellular Localization:
Nucleus.
Sequence:
MAKPNGKLQFKTLQGHGAFSDPDFPKRTWKLLKTAMRQIHQKNASNLSFEELYRNGYNMVLQKHGEILYNNLKKMVDKHLKGVAKTISDSMDDKFLQELNGSWINHKTAMLMIRDILMYMDRNYVKQNNLLSVFDLGLCLFRDNVAHCPSIKDRLLNTLLSMVQKEREGEIIDRILIKNIVEMLIDLGVNSKGVYIEDFEKPLLLKTSSHYQAQSQSLITTCSCPDYMKKVEICLKEELERVSHYLDSSSEPKLKEVCEKQLISNHMRTLIDMENSGLISMLKDDKIDDLKRMYSLFSRVADGLNLMKDVISGYVKEIGKSIVMDEEKVKLLLIIYMNTKEQGTYFQSLLDLKDKYDNLLSNALFNDKQFIHSIQQAFEYFINLNPRSPEYISLFIDEKLKKGLKGVSEEDVDIILDKILMLFRLIQEKDVFEKYYKQHLAKRLLLGRSVSDDAERNMIAKLKTECGYQFTSKLEGMFTDMRLSQDTMAGFKNFIQGFDKPLPIDLNVHVLTTGFWPTQNTSNCNLPREILHCCETFKKFYLGNHNGRLLLWQTNMGTAELKANFPSKTHELQVSSYQMVILLHFNDSPRLSFKEISDLTAIPVLDLKRNLLALTNPKNKILEKESTATTKGIDESDIFIYNSKFKSKLFRVKIMAVAQKETPVEEKETREKVDEDRKHQIEASIVRIMKARRTLEHSNLVSEVIKQLQTRFVPNPVVVKKRIESLIEREYLERSKQDRKIYNYMA
The following text describes a protein:
Function:
N-methyltransferase; part of the gene cluster that mediates the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid with a unique, fused spirobicyclic ring system. The first step of the pathway is the production of the malonamoyl-CoA starter unit for the polyketide synthase vrtA. The aldolase vrtJ may be involved in the synthesis of the malonamate substrate for malonamoyl-CoA synthetase vrtB. The polyketide synthase vrtA then may utilize the malonamoyl-CoA starter unit, followed by sequential condensation of eight malonyl-CoA units to form the polyketide backbone. The cyclization of the last ring could be mediated by the lactamase-like protein vrtG. The proposed post-PKS tailoring steps are a hydroxylation at C5 catalyzed the cytochrome P450 monooxygenase vrtE, a hydroxylation at C12a catalyzed by VrtH and/or VrtI, and an O-methylation by the O-methyltransferase vrtF. VrtC is then proposed to catalyze the transfer of a geranyl group synthesized by vrtD to the aromatic C ring of the tetracyclic polyketide intermediate of viridicatumtoxin to yield previridicatumtoxin. Finally, the cytochrome P450 monooxygenase vrtK catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to afford viridicatumtoxin.
Sequence:
MTTTTTTDDTQKLDPSASDEVIYKSWDLLIYEIWVLGIVSTWAWGCSTTEYLLPQFRANVGTNHLDVGSGTGYYLRKGGIPASTRLTLLDLERPALDLGLQRCGRSDARGLQADILQPLPVIDKFDSVSMYYLLHCIPASVEDKCAIFKHIKHNMTPDGVIHGANVLGKGVRNDGHFAAYVRRGVLKAGIFHNLDDNAYDFEHALRMNFEEVETRVVGSVFIFRASRPKLDEGDLLET
The following text describes a protein:
Function:
Extracellular matrix protein that plays a role in epidermal differentiation and is required for epidermal adhesion during embryonic development.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix, basement membrane.
Sequence:
MTVKTSKCVCFFLLGLIQLIRGSLVKTNAVLKVKRGQSVFLQEDDLQFRIPRVKDSCKLEVVLNEPITQRVGSLTPQVFDCHFMADEVKYTHNGCPILKEDTVKLRLYRFTETETYSELFSLRVEILEPECNVIQFGSQQLVVPEFYGLSNVLDGNVVSFNYEHRHNIECTIRVTGLETHLPVHGQLVTGEPEKADGPRGDEPDSFVSLRRQLDNKARAHCKTDDCLKGLKLLKITKVPCNDFLMMGIRYQHTDPPSPHTDYISIRLDLTDTRSRSIIQSEQAWIPVTITGALPNQPPKPAFMSMFILEVDQFILTPLSTATVDAEDDETPKQRLVFNITKPPSEGFITHLSDHTKPVSSFSWTDLNGMLISFQPPNSSATHRRNYEVEFEVHDFYFEKSQPVTVHVSIRTADTNAPRVSWNMGLSLLEGQSRPITWDQLQIVDNDNLKAVKIITVDGLQHGRLTVRGGKGFMFTVNDIKSGVVHYHHDDSDTTKDYIVFRITDGLHQTRHKFPINILPKDDSPPFLITNMLLELSEGQTALLRGSILQACDMDSSDDYIMFNVTRAPQAGEIMKMPGPGITGYPVNRFLQKDLFHSIIYYRHSGREVFDDSFEVVLSDFHDPPNLSEPQVIVIQIQPVPDQPPQEAPGVSRHLVINETDVVYLTKQQLHFVDLESPDSELTYTVTTPPFYTTTYGGSDAGRLFLVDSIPKFSKDSSAPMLRLFTQHAVNYMKVAYMPPIPDIGPYPQHIQFVLSVTNQQGSTTTGICFNVTVLPVDNQAPEVQVKLLVVDEGGEIWVTEDHMHLSDRDSLQDSIHVELKTAPQHGSVYLDGKLMVPGQTFTVRDLKSLKVRYRHDSSETERDEIKFIATDGTNTADFILRIKVTLVNDEVPVLVAGLKPMLWCAEGQEVFITIEYICATDPDSDDRSLMYMIARQPYHGVVQRNGIIVDRFIQADLNAGFISYRHTGQEIGLRPRHDVVTFVISDGETEPISPCCSERDTLFNPQNSLPVYDLNITVYPVNNQPPSIATGEVFMVDEGGSASITVTHLTXVDQDSAPEDLQLILVSPPHFGYIENILPSPGFEKSNVGISIASFTYRDVLDGHINYVQSRHQRMEPTTDQLMLQVSDGKQQSSPVPLYIIISPTNDEIPDFQTQNITVFEGDRTELNSSVISAVDLDVPQERLMFSIVQNPQHGSIISLPHRNQVSHYKRGAEEPVQHFCMDDLKSGMTLMYVHDDSESEQDEFILQLSDGKHKLQKHVQVKILPVNDEEPQIIRNTGIEMEAGESRLISSAVLSAHDEDTPPDHILYVFESLPTHGAIQMKVGSDWLSVSAGVNCSQKVLDMNLLRYLHTAHPGEPTADFFVFHLFDGKNRSPPQHFHITVKQLEKGDIALFLKPVRVSRGDRVVFTTDVLLXVDGADQPEELLYVITAPPAHGHVELIKHSGVQIQSFSQLDIAANLVCYVHDNRATAPRESLQFMVSNGISTRNGTLEILVDLTDKVLPTLVHNSGLRVPQGSTVVLSTAVLSLSDPDSPASTLSYRLIQTPQYGQLLLKGQALVAGAHFTQQDLQDLDVTYKHSGGASQIDRFTFTASDSTDRGFLLDGRVQTEPVFFTLQIEALDSSAPQVAVLETLWKVELLKDGRYGIFISSRELKAEDTNTADADLTFHILRAPYIGYLENHTSGEFVRQRFSQMDLNRRNILYVINSALDALSDSLEFAVSDALGNTGLSHKLNFSWAGVELTRTQYTVCESQGSVSLTIQRKGNMQDSSYVTVQVKELTASAGKDFIPASSLIQFDPGVASRVWKVEIVQDSLEEADEKFEVSLASPVAAVLKDNSRATISIKDSNGQCVERQITAGSSLQGREVRPGPYPQHGSIQLETLPLSPEGVIRGDGDTTDQAPAAPKKRLRVTGNGKVVQPSETIRRGSELIYKYHGLVSMAVEEDESASRTDRQAEVQVNSRGQQQRLLTVQTKPQQTSRHTSSRLLQRTHTQTSSKRCSPDLSGLLHYNQSSGRLFRCNGDSWRPWTPTNETVKAQRCPQGWTYHSNNCYLLSSERKASWSTAARACRERFSGHLVSVQSKAHMAWLWDFSQRKPFWIGLHDGESRGRWEWMDGQSVTYTNWRRNPPKNQKKKETRRCVLVWKKSRWQIRDCQRGKGHRYVCYTQLH
The following text describes a protein:
Function:
Centrosomal protein required for establishing a robust mitotic centrosome architecture that can endure the forces that converge on the centrosomes during spindle formation. Required for stabilizing the expanded pericentriolar material around the centriole.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Sequence:
MAASAGGVWNPSAAGCGDGGYEEQLRRLQADLRDSETKRMELEREMLEYSKSDTCMTNLKYMQLKKYLKEICERQKKSLLRNQDLLREFDSIEAHIKKFASSSESLQKLKAEYEREIKSRWRLNTKHILKSEESGDAKNQKVPEARQAGINNRTAMSRGLYHTATIFMGRQMSAVSSVEDFSAPQKSSKLTKSFSISDPHSHRQPSQNSYMTDSCVVQTNNDLQRSNKSDKIDGKTYLLMGKETPVTSNVSHADGRICCSTVESKTNNCSSNSVESKMSAELNSLLHERLSPENRTTDLKSGNFHKPVEEILTHEHSGNEQGSEQPNPLAYCSEQLVSGKEHLREKFPGLRNSPQLDTNAQEEDESSNGSTDLTVSLSNSEEEDETNPQKLQQSGQDVGYNVSLKSVSPTYNKKEKYPCSQMLRRDTSSGSSSPSPATRLCLSFEGFSHLLTFIEGSVAGTTPDCLVLYQYKTVPVAELEALISLCNETGNLKQEDLELCEALVLHQLQRLLQSTANACLLPENPFNNKSEMFNGKQNRSKLTPYFAMIWKRLSEHVLFLQKHHVLLEQEAKKMFVTLLISGKHEGDSSITPELKESLPEKYENRSVAVSHQEQDSYDSQKNGLKKEEVTSWCEDESREESLVEKIPITGLNIDGSGLKEQKSDRTSSEPSFSSPERRSSLSRFENGRKIVSTIKSKAFWGESDDSNSEIEAALRPQVHCSHNDEFDDFYD
The following text describes a protein:
Function:
Component of an histone acetyltransferase complex.
Subcellular Localization:
Nucleus.
Domain:
The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence:
MDDIDFSDVSDEVIDLATNYADKYVDYVENLPFDLQRNVTRLREIDCTCREVVGEIESLYDGFANDGETKKRSGLVQIQRLLGRCQELGDEKIFIVQQINEMIENRKKSLEHSSYRFKISYRPDQKDEFRREANKVDNHRSKRTRRRQNQYQDKVKYSMMDSGFAKSGNHGNGSSANQPLEVRKEQSRTNKDETQKSEKVEKKEPISMATTIALPVAVVSTLKSTTTKPSTKVTTSSKPSTSSSNGSNKSINKGKKKKKSSRPQLERMSTRSPSPQVDVPIDPDEPTYCVCDQVSFGQMIGCDNKKCPIEWFHFSCVGLTLKPKGRWYCPDCLRDMKCKKKREK
The following text describes a protein:
Function:
Major component of the toxin co-regulated pilus (tcp) which is a type IV pilus essential for bacterial aggregation and subsequent colonization in the host small intestine.
Subcellular Localization:
Fimbrium. Membrane; Single-pass membrane protein.
Domain:
The leader sequence region and some other sequence particularities suggest that TcpA may represent a novel class of pilin, and imply the existence of a novel signal peptidase.
Sequence:
MQLLKQLFKKKFVKEEHDKKTGQEGMTLLEVIIVLGIMGVVSAGVVTLAQRAIDSQNMTKAAQNLNSVQIAMTQTYRSLGNYPATANANAATQLANGLVSLGKVSADEAKNPFTGTAMGIFSFPRNSAANKAFAITVGGLTQAQCKTLVTSVGDMFPFINVKEGAFAAVADLGDFETSVADAATGAGVIKSIAPGSANLNLTNITHVEKLCTGTAPFTVAFGNS
The following text describes a protein:
Function:
Endo/exonuclease with nicking activity towards supercoiled DNA, a preference for single-stranded DNA and 5'-3' exonuclease activity.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MRCGKRHVALVKMAAKSFASRLRGSRHLLSAFVAGAVVGAAGAGFTAVQFLRSQGAEAALAVREPGGSAEKALLEQFGFPLTGTETRCYTNHALSYDQSKRVPRWVLEHISKSKIMGDADRKHCKFKPDPNIPPTFSALNEDYVGSGWSRGHMAPAGNNKFSSKAMAETFYLSNIVPQNFDNNAGYWNRIEMYCRELTERFEDVWIVSGPLTLPHTASDGKKTVSYQVIGEDNVAVPSHLYKVILARRSPVSTEPLALGAFVVPNEAIGFQPQLSEFQVSLQDLEKLSGLVFFPHLDRTSDIRNICSVDTCKLLDFQEFTLYLSTRKIEGARSVLKLEKVMENLKNAGIEPDDYFMNRYEKKLEELKAKEQSGMLERKPS
The following text describes a protein:
Function:
2-oxoglutarate-dependent dioxygenase essential for auxin catabolism and maintenance of auxin homeostasis in reproductive organs. Catalyzes the irreversible oxidation of indole-3-acetic acid (IAA) to the biologically inactive 2-oxoindole-3-acetic acid (OxIAA).
Sequence:
MVEIPVIDLRLAGARPEDSARLRDACERLGCFRVSGHGVPAALQAEMKASVRALFDLPDEAKRRNTDIIAGSGYVAPSPANPLYEAFGLLDAAVPADVDAFCARLDAPPHARETVKAYAEAMHELIVDVAGKVAASLGLEGHPFQDWPCQFRMNRYNYTQDTVGSSGVQIHTDSGFLTVLQEDDRVGGLEVLDPATDEFVRVDPVPGSFLVNIGEVGTAWSNGRLHTVKHRVQCVAAVPRISIAMFLLAPKDGRVCAPEALVDAHHPRRFKPFNYDDYRKLRLSTGERAGEALARMAA
The following text describes a protein:
Function:
Required for cell cycle progression through G2/M transition at temperatures higher than 33 degrees Celsius. Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. When associated with the RSC complex, may act coordinately with PKC1 to regulate G2/M transition. Together with LDB7, NPL6, RSC3, RSC30 components, defines a fungal-specific module within the RSC complex that plays a role in many cellular functions including the maintenance of cell wall integrity.
Miscellaneous:
MISCELLANEOUS: Present with 3550 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MSQNNTISSMNPERAYNNVTLKNLTAFQLLSQRENICELLNLVESTERHNSIINPERQRMSLEEMKKMLDALKNERKK
The following text describes a protein:
Function:
Possible role in granule neuron development.
Subcellular Localization:
Cytoplasm. Membrane; Single-pass type II membrane protein.
Sequence:
MLVTRHQPREVTYRFVKEPRGHRPRTVVQSSMSRSQVALLGLGLLLMLLLYVGLPGPSEQTSWLWGDPNITILAGLTPGDSPLFYREVLPLHQARRVDVVLLHGKAFNSHTWEQLGTLQLLAQRGYRAVALDLPGFGNSAPSKEASTEAGRAELLERVLRNLEVQNAVLVSPSLSGRYALPFLMRGHHQLHGFVPIAPASTQNYTQEQFWAVKTPTLILYGELDRILAQESLQQLRHLPNHSVVKLRDAGHACYLHKPQDFHLVLLAFLDHLP
The following text describes a protein:
Function:
Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MDLNIIRRFFQVGKFLALTPTTLRDYSATPWQKNYTVLVFFFFTVGATAALQFCWSDYMSENPIALVLWIVTDITRYVHNLYIFISVMIFKRKLWFVLIANLKKTKFRIDYSEYKFLYCAFITSHVSFSIIMSCIIFICFQLDDWYTCLRYYFVEFVQIFTQFFYLSFAPIVLKMIFLRYQHFNKTLQTQKTWHQIKTGQLRLKQTVDTFCEIFGGTILLNIIYNSSKSLIYLNKLIKQTKSWSSGSPIVILMKLTQIGIIGLFWGLIFWVIFLCDAIVSQNEEIRKNLYQMLQADPIFYENKQFEKFLKTVLSNGPEFSAVRFFSIDRSTIFQIMNSIVTFLIVVIQIKTD
The following text describes a protein:
Function:
E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity).
Subcellular Localization:
Cytoplasm.
Domain:
The N-terminal region is involved in phosphatidylethanolamine-binding and is required for ATG8-PE conjugation; The flexible region (FR) is required for ATG7-binding; The handle region (HR) contains the ATG8 interaction motif (AIM) and mediates binding to ATG8. It is crucial for the cytoplasm-to-vacuole targeting pathway (By similarity).
Sequence:
MAYNFVRSYIDTFRERTAAISHTSTFRETGQITPEEFVLAGDFLVFKFPSWQWGDASSAGKRVPYLPEGKQYLMTRGVPCHRRLDDNFAGEAGQDETIVGDGFAGSEGADDDGWLRTGGMAASQEAKVRDVRTVDESGNLGAAEEEDEIPDMEDMDDDEEAIIRDPQGGSSSTAPLRTYTLYICYSAHYRTPRLYLSGYGATSVPLKPQEMMEDIVGDYKDKTVTIEDFPFFEHALKTASVHPCKHASVMKVLLDRADAALKLRLAKLKAGKDIGKLDTGMEGLVDDTRLLKLSEQAKGKEGDEAKDDWEVLSEGGDDEVAIRVDQYLVVFLKFMASVTPGIEHDFTMGV
The following text describes a protein:
Function:
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATP synthases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a/ATP6 in the membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein. Note=The F-type ATP synthase complex is anchored in the mitochondrial inner membrane via the F(0) domain with the F(1) domain and the peripheral stalk extending into the mitochondrial matrix.
Sequence:
MAFGIRRAYPTPIVKPLWPYAVGGVITFFLFAKAANASMNTEEFINDPRNPRFKAGGVKEEH
The following text describes a protein:
Function:
Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4 and H2A. The NuA4 complex is also involved in DNA repair. Yaf9 may also be required for viability in conditions in which the structural integrity of the spindle is compromised (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
The coiled-coil domain is required for assembly into the NuA4 complex.
Sequence:
MPSATGTKRVRGVSIFRPFVFGSEAQPFDPATKPSNVSSDHTHQWRVYVRGVNGEDISYWIKKVQFKLHETYVQNVRTVEHPPYEVTETGWGEFEIQIKIYFVPESMEKPQTLWHSLKLHPYGPDAEGKKERREVVVSQNYEEVVFNEPVEQFYDYLTGGSGTQQMQKGKSGKNAKQAQQQRGGRTAEIPFNETPENPYSRTAENKELDRLAEANKTVEQMIKDEKERLIAREKRLAELRASEGVPAQPLKKSFSGRIPVHSQQRMAGTVGPPDS
The following text describes a protein:
Function:
Regulates the timing of initiation of DNA replication. Functions in copy number control by promoting the underreplication of DNA, which is found in many late replicating euchromatic regions of salivary gland polytene chromosomes. Promotes underreplication by localizing to active DNA replication forks in a partially SuUR-dependent manner, and inhibiting replication fork progression. Might also work as an adapter to recruit Pp1-87B to multiple sites on the chromosome and may function with Pp1-87B to mediate underreplication. Plays an essential role in embryonic development, in the transition from larvae to pupae and, probably, in proliferating tissues later on. In embryos, during mid-blastula transition, binds to and selectively delays the replication of large blocks of repetitive DNA satellite sequences during S phase in response to the activity of Cdk1; maternal Rif1 is specifically required for the normal extension of S phase 14. Unlike mammalian orthologs, does not appear to play a role in DNA damage repair.
Subcellular Localization:
Nucleus. Chromosome. Chromosome, telomere. Note=Localizes to heterochromatin in all stages of amplifying follicle cells and accumulates at active DNA replication forks in the later stages of DNA amplification. Associates with polytene chromosomes in salivary glands. Associates with heterochromatin in a dynamic manner in different mitotic stages of the cell cycle. Absent at metaphase chromosomes but re-associates with the condensed chromosomes during late anaphase. During mid-blastula transition in the S phase of embryos, dissociates from chromatin before the replication of the bound DNA satellite sequences.
Sequence:
MDVDFGAQAGQSYRTVQLSAKEVLAAGRRQHYCNMIDLLASSCKSSGLIATSFTDDELVEFWLGDILPLMFDADRKIQDCAVAALAEALVALDVSVIHSAKCWPQIRSEFVDKYTIIIGEMRDAKNSNWHKIWTLLVQIMDEDLLRGCVYINKFLALVELGFRNPDNGVRSEAFLCWRVLIKIFAAYDELTSAKRLRLLLIPLRTSQSRSSHVSGIKLRVWWYLLSCLDHELPKSFDSAVEHFLAFMLGGGPRNLATGLAHNYQTARELALPCLVALWGVESSEPLQRLMRELRLETLVQPSPLMSVEVFQQHWKPLLAAAVSGLKLLTENDATEAEQLLLQLLVRNLCLAMFRLAVAPFNVACCSEIEKILQAEDNSGGRVVRALFNTIAADNLVMERVSGSDHLDVLEAYLKLVLKSKTEVPAAILQRSIACIFAVDRIEANNQNEFRMLGSFAELLMQANDEEDFEGFAFKLQVWRQVSQALSNYLRNNALEYRVAHNASLLDTWLLWPLQTLAAFAGRRASNSFDASFCDQWRQLVNAGQNAPGRKKFLTDLKATLTDLLKSKDEPLFAELFDAYVTSLIKFGLCKEAPLYKDVFGLLQTIFEQPSSQKTLEACLNTLRNLVVELRQNELMVVFDSLKPTLSSGIQCWNKMKCEGGFLEEWKRGIQEKFRKLPMKTMANQLKELFKADDLFVIIPSVWSLNPEKLTDRQKERFAEKSDIPALYNDMSQSQDSASIKPWTPKKVVIAKSKQGELALTGKDDNGEVIDITASEESEKEPVRVDVVTPIRKKPGRKSQAQKELEAAARAASLAEEPPKRQTRTRAAQKETEQVAQPQPAFEPQLRSPKKLPPSPVVQSTAAAVKQAKVAKPTPVVVIAQSEDLFPEVAAEPEPQPEPVKKPDPVPETTQLTPPDVPLEAVPSTQLPGSSGDPAASAGAVAAGEMSPKKSGTRIYNLSSPPDRKQTNNSSSPTLRPKPTGHLTGRGAQLINMIRNKKLDAASGSPYACMSTSRLVHQVTPARAQDRAEQVSTPTSELNELTGTDHTSTPIQAPPSKDLLVFSKRLPSPSASPSVSILKRKLRCESLDDVTLDSPALKRKRVSFHDPPVSVTKEYLRDAEETRSSLKPKRCLLMDKVAQTTEMRQALRRRGRLDSIIEIERFASEQTARTATTDKSLDKSTGEAPEEDAFTSLKWNDTGNAHNISISEEPVKAMEVESELETAGQDLAIMDPEAALDLAVAQLPLESVLQRYFDKSPLKSAGMLAKFLSAQMTANEKLKTNVLETLSENHSKDFLDHAVRENLSSVVCDRLNPTSVLEYVCAKSKISASCRNGLLAQVPEILKSGPRSDSERLAFVQQLMVQCSPGDDLLLDLIDLLMRTRRERNNSTSTHISKGVVSAVGSPDNVAETAADSSSNL
The following text describes a protein:
Function:
Part of a signaling cascade that regulates curli biosynthesis. The cascade is composed of two cyclic-di-GMP (c-di-GMP) control modules, in which c-di-GMP controlled by the DgcE/PdeH pair (module I) regulates the activity of the DgcM/PdeR pair (module II), which in turn regulates activity of the transcription factor MlrA and expression of the master biofilm regulator csgD. DgcM stimulates activity of MlrA by direct interaction, leading to the transcription of csgD. It also catalyzes the synthesis of c-di-GMP via the condensation of 2 GTP molecules, which contributes to the c-di-GMP pool generated by module I in a positive feedback loop. Production of c-di-GMP contributes to but is not essential for MlrA activation.
Sequence:
MITHNFNTLDLLTSPVWIVSPFEEQLIYANSAAKLLMQDLTFSQLRTGPYSVSSQKELPKYLSDLQNQHDIIEILTVQRKEEETALSCRLVLRKLTETEPVIIFEGIEAPATLGLKASRSANYQRKKQGFYARFFLTNSAPMLLIDPSRDGQIVDANLAALNFYGYNHETMCQKHTWEINMLGRRVMPIMHEISHLPGGHKPLNFVHKLADGSTRHVQTYAGPIEIYGDKLMLCIVHDITEQKRLEEQLEHAAHHDAMTGLLNRRQFYHITEPGQMQHLAIAQDYSLLLIDTDRFKHINDLYGHSKGDEVLCALARTLESCARKGDLVFRWGGEEFVLLLPRTPLDTALSLAETIRVSVAKVSISGLPRFTVSIGVAHHEGNESIDELFKRVDDALYRAKNDGRNRVLAA
The following text describes a protein:
Function:
Binds to extracellular matrix proteins. Binds to pathogen-associated molecular patterns (PAMPs) present on the cell walls of Gram-positive and Gram-negative bacteria and fungi, behaving as a pattern recognition receptor (PRR). Induces bacterial and fungal aggregation and subsequent inhibition of PAMP-induced cytokine release. Does not possess intrinsic bactericidal activity. May play a role in the innate defense and homeostasis of certain epithelial surfaces.
Sequence:
MASSTLSFGWRCPGRRLRDFMMVLLFLTCFWGIAWSTETPEADQPDIRLVNGSSRCSGRVEVLHNGVWGTVCDDSWGMEEARVVCRQLGCATAVTAPRNGYFGKGDGRIWLDELRCTGTESALSQCPSRPWGENDCHHGEDAGVVCSEVRLMGGSTPCTGRIEILHNQRWGTVCDNGWDLNDAHVVCREVGCGAALAATTAAKFGQGSGPVWMDQVNCTGEEDTLRKCPPKILAEHRCDHNKDAGVECTEPPEIRLTNGPSKCSGRVEILHEKLWGTICDDDWDLEDAQVVCQYLGCGTALSAPRGSRFGQGTGPIWLDGVNCTGTEKAISKCPAKEWGQHDCTHSEDAGVTCAELRLVGGLNRCSGRVEVYHNQQWGTICDSNWDLNDAQVVCRELDCGSATKATGGSRFGQGSDIIWLDQVNCTGKEAFLSECQKRPWGQHSCSHRGEASVECSDPNEVRLVNGTSRCTGRVEVLHNQQWGTVCDDGWDLTSAQVVCRELGCGVALSAPRGASFGRGADPIWLDDVKCKGTEAALRDCRLKAWGEHNCNHGEDAGAVCSELRLANGTSRCSGRVEIFYNQQWGTVCDDRWGSKQAEVVCRELGCGVPLKAHTKAFYGQGTGPIWLDDVNCQGTETSLKDCSASSWGHNNCNHGEDAGVECADPVELRLVNGSHRCAGRVEVFHLHQYGTVCDDSWDINEAVVVCRYLGCGTAISAPRGARFGRGADPIWMDDVECTGTETSLSSCTAKPWGSNDCNHGEDAGVICSENVRLVNGSNRCSGRVEIRSPHNDQWGTIYDRTWDLTAASILCGQLGCGVASSAPGGAHFGPGSGSVCFDDISCKGTEDTLHECNINFQGTNNCNHRHDAGVICSASPTLNVGNIRLQDGPHSCAGRLEVFHQQQWGTVCDDGWGLPDATVVCRQLGCGIALEAPHGAHFGRGLGSIVLDDVNCTGSEKALKECGGRTVGEHDCDHAEDASVVCSGQLEIRLASGPNSCSGRVEFNHNGSWVSIGDSGWKLPQATVVCRQLGCGAALSAPVGNKYGMGVGPAFLDEVECSGSELSLIECKAVPTGPHKCICGSYAGAECAGSSGSGRIAAVILGVLAIIVIIVGVLFYMRKKRGKSFAVNPFAHRREGFMENITVGSDMVNGIREMYMRGKEQIVPEADREDDTICLVKTTPEPSAENTE
The following text describes a protein:
Function:
Has an oostatic activity. Inhibits trypsin biosynthesis in the midgut epithelial cells which indirectly reduces the vitellogenin concentration in the hemolymph resulting in inhibition of oocyte development.
Miscellaneous:
MISCELLANEOUS: Can potentially be used as a larvicide. The stable three-dimensional conformation of the decapeptide means it is not degraded by gut proteolytic enzymes and can traverse the gut epithelial cells into the hemolymph of adults and larvae. Hormone fed to different species of mosquito larvae stops food digestion and causes larval mortality. The tetrapeptide (DYPA) is as effective as the decapeptide.
Subcellular Localization:
Secreted. Note=Secreted from the ovary, starting 18 hours after a blood meal, circulates in the hemolymph.
Sequence:
MNKIIAALVLFTAVIGALADYPAPPPPPPKPYHAPPPPPYHAPPHHAPAPLHPVVHTYPVKAPAAKCGANLLVGCAPSVAHVPCVPVHPHPPPPAHY