lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
A bacteriolysin able to lyse both L.monocytogenes and S.aureus.
Subcellular Localization:
Cell surface. Cell membrane. Note=Anchored by its GW repeats to the cell surface.
Domain:
The C-terminus has 8 GW repeats.
Sequence:
MKKLVKSAVVFAGLVFIGTSATMITEKASAASTDPVQKVDGQATYIPKGVRDGTATEEHDGFEDGTNSVLQQVPLLRATTGYPDVNAYIKSNKFSTAKIEKQLKSQFPKFNYRNGYGKPEGIVIHETANNSSTITGEINYMSTNYNNAFVHAFVDKSRIIQIHPTENGVWGAGQYANARFIQVELVRSKTFDEFARSINNYAYYAAYLLDQYNLPVDSAHSDGKGTVWSHDAVTRYLGGTTHTDPVAYFNQWGYNFNNFVSLINEKYKAMQVNYEKIEYDKAITAYSRVKTATGNSVWTKPNKTEGAKLVNPLSSYSGKNLRIIREAKTSGGTIWYQFSVGGKTIGWVDSKALNTFYTPSMEKTITGTRYVLPSKQTVHYYGLPVEDSAIDRGPLSKFNGQALTLQREATIEGQLWYRVKDLGWVKAVNLTTTKYDLIEYDKAITAYSRVKTAAGNYVWSKPNKTEGAKQGSALSTYSGKNMRIIREAKTSSGTIWYQFSIDGKTIGWVDTKALNTFYTPSMEKNLTATRYVAPGQETQHYYGLPVADSAIDRGPLSKFAGQTLTVQREATIEGQLWYRVKDLGWTKASTLTATQYDKLEYDKAITAYSRVKTATGNSVWTKPYRTSGYKLVNPLSSYAGKNLRIIREAKTSSGIWYQFSVGGKTIGWVDSKALNTFYTPSMEKTITGTRYVLPSKQTVHYYGLPVEDSAIDRGPLSKFNGQALTLQREATIEGQLWYRVKDLGWVKAANLTTTKYDTLSYDKAITAYSRVKTATGNSVWTKPNKIEGAQKISALSTYSGKNMRILREAKTSSGTIWYQFSVGGKTIGWVETKALNTFYTPSMEKNLTATRYVLTSKKNEHYYGLPVVDSAIDRGPLSKFSGKTLTVQREATIEGQLWYRVKDLGWTKAANLSAKKQ
The following text describes a protein:
Function:
Involved in the galactosylation of the N-linked core oligosaccharide Man(9)GlcNAc(2).
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MAVLQWKLSRVIFVLLIIGISSFLIYFQFGNSFSASPALERLQDVFSKPSVQEYDYLVPLDEDMQGLSTTYHQATINEDDPQEPKSHEIVILLASDGRSSGNMAPETFNQCIENRINYAKHHNYGFEYVNVSQMNIPPVWAKMPAIIQTMNKHPHAKWIWWLDQDALILNTELSIQEHILSPDVLVEKLMKNEPMISPFSADLERLTPSSYTVDSARSLGLLISQDLNGLNAGSFFVRRSPMMALFLDLWGDKSFRENKVADHEQALLGYFVRYHPEIAAIIGILPQTLINSYPVGQPEMGWKEGHLVIHFAGCWVENRCQVLWDEYRERVH
The following text describes a protein:
Function:
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Sequence:
MFRFTKDERLLRRADFLRLSAAARKLHTSSFIVLWTPGETGRRRIGITVSRKVGTAVVRNRIKRLVREYYRHHRDALPSIDLNVIAKKGAERLDYHGVCRELGPVVERLAGLEC
The following text describes a protein:
Function:
Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Arp2/3 complex plays a critical role in the control of cell morphogenesis via the modulation of cell polarity development.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MGEEAPAVDYSAVVEKHLGICDQVIKGGMSIEEGLKEMLDVIPLGCKDTGILEKNAEAILSVLASVKEVKESYISTLSVEEQSWLMMYVYKGLGASENKEATIVPPAQIMFKWFNAIYKVGGDGCVMRAVSRRKAL
The following text describes a protein:
Function:
Catalyzes the synthesis of S-sulfocysteine, utilizing O-phosphoserine (OPS) and thiosulfate as substrates. To a lesser extent, can also use sulfide as donor substrate, producing L-cysteine. CysK2 thus provides a third metabolic route to cysteine, either directly using sulfide as donor or indirectly via S-sulfocysteine. S-sulfocysteine might also act as a signaling molecule triggering additional responses in redox defense in the pathogen upon exposure to reactive oxygen species during intracellular survival or dormancy. Cannot utilize thiocarboxylated CysO as a sulfur donor and O-acetylserine (OAS) as acceptor substrate.
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target; MISCELLANEOUS: The enzyme uses a mechanism via a central aminoacrylate intermediate that is similar to that of other members of this pyridoxal phosphate-dependent enzyme family.
Sequence:
MRSRQTRDRYRLLPEGYQVTPGRNRHPGTMVGNTPVLWIPELSGTSDPDRGFWAKLEGFNPGGMKDRPALYMVECARARGDIAPGAAIVESTGGTLGLGLALAGKVYRHPVTLVTDPGLEPIIARMLTAYGAGVDMVTQPHPVGGWQQARKDRVAQLMAEYPGAWNPNQYGNPDNVGAYRSLALELVAQLGRIDVLVCSVGTGGHSAGVARVLREFNPDMRLIGVDTIGSTIFGQPASNRLMRGLGSSIYPRNVDYRAFDEVHWVAPPEAVWACRSLAATHYASGGWSVGAVALVAGWAARNLPADTTIAAVFPDGPQRYFDTIYNDAYCNEHELLGGQPPTEPDEIASPLDAVVTRWTRSTTVIDPTQVVS
The following text describes a protein:
Function:
Proposed core component of the chromatin remodeling Ino80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.
Subcellular Localization:
Nucleus.
Sequence:
MSLFDIEDIKVKPDIVCTYPDPTVPPDAAIVIDNGSYHCRAGWAGKDVPSLVFKNVLAKPRKDRSKKDTSEVVVPTVQIGNDITNIEAVRFQLRTQFDRNVVTHLHVQEQIFDYLFGRLGINADGCVPHPVLLTECVANPNYSRMLMSELMFECYGIPGIVYAVDGLLSYRMNGGQDSGLIVSCGYQATHVIPVLNGRMVEDKVRRINLGGFNMINFMFRLLQLKYPVHVNAITLSRAETMIHNYCSFAYDYTESLRNWALLEFYEQNVIKIQLPYNQNVSAPTLTAEQRLEKRKELSRRLAEINLRKREEKLAEDKVLLTRMLAAEDTLDDEDNVGFTLHEFSVKNVDEYRKMIVTLRERIAKTTQKMNSQQTNNQPEEKPLQLLQPPPNMTIEEWVIETRRKRDEILDKKQIRKQRKQDLAKRRTAAAQERMRIISHLAKKEKGVDDFGMRDEDWDVYKSISREGDSDSDAENEKLIECEEILKQHDSTFVEPVVAPGNIAEFHQLHIGVERIRVPEILFQPSMIGVQEAGLTGTIDYVLKLFPKEDQVKLVGNVMLTGGCANIRGFKERLSRELQAILPFQSVYNLMVAGSPSLDAWRGASQFANSQEFKQSLITRQLYDECGGEYFKEHTASNFYYPTPSQVSSALNDTFN
The following text describes a protein:
Function:
Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division.
Subcellular Localization:
Cytoplasm.
Sequence:
MSDNNSEQSLISVKILDRSYHIKCPPDQTQALQEAAAYVEEEMRKIRQTANINSMERIAVVTALNICHELMQLRKQKNNYIDVMNQRIQDLQRRIENFLETNAEIEV
The following text describes a protein:
Function:
Regulator of type 1 phosphatases which maintains protein phosphatase activity under strict control.
Subcellular Localization:
Nucleus.
Sequence:
MSSLPVFNQSHSRSESISNGQDSSSENRHTSSLSAVQYSTNTASRTQTLTATQTQESVTTQLETAGVLQLEGRGLDSSQRRVAWNDDVIDNENMNKKKSKICCIYRKPHQPDASSSSDYSSLDGSDPDEPNAYERQSKPSKRSKKKHSQSHNDCNHDHSSNKDCDTPLYS
The following text describes a protein:
Function:
Mediates the TonB-dependent high affinity transport across the outer membrane of pyrroloquinoline quinone (PQQ), a redox cofactor required for the activity of Gcd and Asd dehydrogenases. The uptake process is energised via the TonB-ExbBD complex. Not involved in the transport of an iron-containing substrate under laboratory conditions.
Miscellaneous:
MISCELLANEOUS: PQQ is a small molecule and it may also pass the outer membrane without PqqU, through porins. However, this diffusion-dependent uptake process is rather inefficient, which may be a disadvantage when only low amounts of PQQ are present.
Subcellular Localization:
Cell outer membrane; Multi-pass membrane protein.
Domain:
Possesses a conserved positively charged substrate-binding pocket.
Sequence:
MKIFSVRQTVLPALLVLSPVVFAADEQTMIVSAAPQVVSELDTPAAVSVVDGEEMRLATPRINLSESLTGVPGLQVQNRQNYAQDLQLSIRGFGSRSTYGIRGIRLYVDGIPATMPDGQGQTSNIDLSSVQNVEVLRGPFSALYGNASGGVMNVTTQTGQQPPTIEASSYYGSFGSWRYGLKATGATGDGTQPGDVDYTVSTTRFTTHGYRDHSGAQKNLANAKLGVRIDEASKLSLIFNSVDIKADDPGGLTKAEWKANPQQAPRAEQYDTRKTIKQTQAGLRYERSLSSRDDMSVMMYAGERETTQYQSIPMAPQLNPSHAGGVITLQRHYQGIDSRWTHRGELGVPVTFTTGLNYENMSENRKGYNNFRLNSGMPEYGQKGELRRDERNLMWNIDPYLQTQWQLSEKLSLDAGVRYSSVWFDSNDHYVTPGNGDDSGDASYHKWLPAGSLKYAMTDAWNIYLAAGRGFETPTINELSYRADGQSGMNLGLKPSTNDTIEIGSKTRIGDGLLSLALFQTDTDDEIVVDSSSGGRTTYKNAGKTRRQGAELAWDQRFAGDFRVNASWTWLDATYRSNVCNEQDCNGNRMPGIARNMGFASIGYVPEDGWYAGTEARYMGDIMADDENTAKAPSYTLVGLFTGYKYNYHNLTVDLFGRVDNLFDKEYVGSVIVNESNGRYYEPSPGRNYGVGMNIAWRFE
The following text describes a protein:
Function:
Nuclear genome-encoded factor involved in ribosome biogenesis in chloroplasts. Binds specific group II introns in chloroplasts and facilitates their splicing. Is required for rRNA maturation in plastids and may contribute to the assembly of the large (50S) ribosomal subunit. Required for normal development of chloroplasts. Required for the expression of transcripts encoding plastid-localized enzymes involved in abscisic acid (ABA) biosynthesis. Required for maintenance of ABA levels and response to salt stress. Possesses RNA chaperone activity for proper splicing of introns in chloroplasts. Essential for chloroplast function and abiotic stress responses.
Miscellaneous:
MISCELLANEOUS: Plants with the weak allele rh3-4 exhibits albino cotyledons, pale green leaf phenotype, slow growth, short petioles, small leaves, reduced content of chlorophyll, altered structure of chloroplast ribosomes and reduced levels of chloroplast proteins.
Subcellular Localization:
Plastid, chloroplast. Plastid, chloroplast stroma.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MASTVGVPSLYQVPHLEISKPNSKKRSNCLSLSLDKPFFTPLSLVRRTRRIHSSSLLVPSAVATPNSVLSEEAFKSLGLSDHDEYDLDGDNNNVEADDGEELAISKLSLPQRLEESLEKRGITHLFPIQRAVLVPALQGRDIIARAKTGTGKTLAFGIPIIKRLTEEAGDYTAFRRSGRLPKFLVLAPTRELAKQVEKEIKESAPYLSTVCVYGGVSYTIQQSALTRGVDVVVGTPGRIIDLIEGRSLKLGEVEYLVLDEADQMLAVGFEEAVESILENLPTKRQSMLFSATMPTWVKKLARKYLDNPLNIDLVGDQDEKLAEGIKLYAIATTSTSKRTILSDLITVYAKGGKTIVFTQTKRDADEVSLALSNSIATEALHGDISQHQRERTLNAFRQGKFTVLVATDVASRGLDIPNVDLVIHYELPNDPETFVHRSGRTGRAGKEGSAILMHTSSQKRTVRSLERDVGCHFEFISPPTVGDLLESSADQVVATLNGVHPDSIKFFSATAQKLYEEKGTDALAAALAHLSGFSQPPSSRSLLSHEKGWVTLQLIRDPTNARGFLSARSVTGFLSDLYRTAADEVGKIFLIADDRIQGAVFDLPEEIAKELLEKDVPEGNSLSMITKLPPLQDDGPSSDNYGRFSSRDRMPRGGGGSRGSRGGRGGSSRGRDSWGGDDDRGSRRSSGGGSSWSRGGSSSRGSSDDWLIGGRSSSSSRAPSRERSFGGSCFICGKSGHRATDCPDKRGF
The following text describes a protein:
Function:
Involved in efficient integration of the N-module into mitochondrial respiratory chain complex I.
Subcellular Localization:
Mitochondrion.
Sequence:
MRIPPLQPRIRIHIQINNVTRTTTREYSSLKPRRQSKLGPTVSLEHFLQRSKALSLYRRILRDCRRIPDVKSRDETRRFVRDDFERNRNVTDLSQIKYLIGTGKTQWEGMERYITGI
The following text describes a protein:
Function:
Not known. Putative receptor.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MAFLQSAYLVMVFTVPIAGVILNTYVLRKLIRVARKSVVRFETTSGLPLAAMSVGDSITLCALLMQAIFHITPKGEVPTVVLSSICKFGIFLIHSTSAFSVWCWFFLSVLRYIAVFHPFKYRTIWRQPRNALKFLAGAVGMFQIYTLIFVTYRQEEKSCGEYDVFHESAFKHVHLLDIFLFYAIPSLLRITLDFLVLIHCYSPFSVEGLDRVTIDRRYAISGPATTKRFSHTGETDTLDNKAHVALAISITASTNTPSVKRIHHGNPKKKTAMVMRSILISVLNLLLNLPSHIFRAWASYDESSLENEIVRTLEPIAQMMYFSQFACNAFYLATSIYETNGSPRNTVISSSNRHVSRCISDDEA
The following text describes a protein:
Function:
Part of the tripartite ATP-independent periplasmic (TRAP) transport system YiaMNO involved in the uptake of 2,3-diketo-L-gulonate.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MKKILEAILAINLAVLSCIVFINIILRYGFQTSILSVDELSRYLFVWLTFIGAIVAFMDNAHVQVTFLVEKLSPAWQRRVALVTHSLILFICGALAWGATLKTIQDWSDYSPILGLPIGLMYAACLPTSLVIAFFELRHLYQLITRSNSLTSPPQGA
The following text describes a protein:
Function:
Adipokine that modulates insulin action by specifically inhibiting its target protease KLK7 in white adipose tissues.
Subcellular Localization:
Secreted.
Domain:
The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.
Sequence:
MNLVLGLGLFLAGLLTVKGLLQDRDAPDTYESPVRVQEWRGKKDARELTRHNMEFGFKLLQRLASNSRQGNIFLSPLSISTAFSMLSLGAQNSTLEEIREGFNFKEMSDRDMHMGFHYLLQKLNRETQDVKMSIGNALFMDQRLRPQQRFLKLAKNLYDADMILTNFQDLENTQKNINKYISRKTHNRIENMVKNIDPGTVMLLTNYIYFQGRWQYEFDPKQTKEEDFFIEEGKTVKVPMMFQRGMYDMAYDSQLSCTILEMPYRGNITATFVLPDSGKLRLLEQGLQADIFAKWKSLLSKRVVDVWVPRLHISATYNMKKVLSRLGISKIFEEHGDLTRISSHRSLKVGEAVHKAELRMNEKGTEGAAGSGAQTLPMETPRRMKLNAPFLMMIYENLMPSMIFLARIYNP
The following text describes a protein:
Function:
Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stranded 3'-5' exonuclease activity and single-stranded endonuclease activity.
Sequence:
MKFAHLADIHLGYEQFHKPQREEEFAEAFKNALEIAVQENVDFILIAGDLFHSSRPSPGTLKKAIALLQIPKEHSIPVFAIEGNHDRTQRGPSVLNLLEDFGLVYVIGMRKEKVENEYLTSERLGNGEYLVKGVYKDLEIHGMKYMSSAWFEANKEILKRLFRPTDNAILMLHQGVREVSEARGEDYFEIGLGDLPEGYLYYALGHIHKRYETSYSGSPVVYPGSLERWDFGDYEVRYEWDGIKFKERYGVNKGFYIVEDFKPRFVEIKVRPFIDVKIKGSEEEIRKAIKRLIPLIPKNAYVRLNIGWRKPFDLTEIKELLNVEYLKIDTWRIKERTDEESGKIGLPSDFFTEFELKIIDILGEKDFDDFDYIIKLITEGKVEEEGPLEEAVKKVSEEKGKTVRQKIESIPKKKRGTLDSWLGGAR
The following text describes a protein:
Function:
GTPase-activating protein (GAP) that most effectively accelerates the intrinsic GTPase activity of Ypt/Rab-type GTPase YPT7 involved in vacuole docking and fusion. It is also active, but to a lesser extent, on YPT31, YPT32, YPT1, YPT6 and SEC4. Provides a catalytic arginine (arginine finger) in trans to accelerate the GTP hydrolysis rate of the substrate GTPase (Probable).
Miscellaneous:
MISCELLANEOUS: Present with 2460 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MSKILFCKSKVFLHPTSDARDNIAGFLLLTLEANKLSHQAILQYIPESGLSTLEISKLLKHEAKVGTCPTSTPFVIENSINFSNLVNTSLGQAFEISLSQIYCIQFRPPSPNGWYVGSLVIYPLTEQFTGFQPPVLFFHDQLCPSTTDKLKRLRKSMNPFDDSDELYWGGVDLRNKINELMELKKSNLEPEFWLVNPSLNDLRNFVSKDLLESYNNSKKDTTELATAGVKLNEKFQEWKWNVMSKIADVTTKSTNFIDSWLTNNSPIQKSQIDNEYLQKLLNNEKVKQIEQDYDSARVYLANWSLGVKQEAERYQKQNKLFDSYRNNIFNDLNLTDELSDTEINNALQRQFPLTEAKWNSLWDENDGRLRVTVNEVKDFIFHGGLENDSLRGKVWGFLLEIYPWDSSQDERVQIDQTLAAEYDQLKLTWSKDFLQFDDEDEEEYWNDQLFRISKDVRRCDRNLEIFQYNTIDGLPPPPQQLPANENNSTSPESANDESDDADDGVRNPHLIHLQNILITYNVYNTNLGYVQGMTDLLSPIYVIMKEEWKTFWCFTHFMDIMERNFLRDQSGIHEQMLTLVELVQLMLPELSEHLNKCDSGNLFFCFRMLLVWFKREFEMEDIMHIWENFWTFYYSSQFQLFFMLAILQKNSQAILQHLNQFDQILKFFNELNGKLDWNDLMVRAELLFKKFEKMMHVMERDLQNVSSSSSSSSTGVLPCQSERLTLLLSKKPIIRHEGQRSKNSVK
The following text describes a protein:
Function:
May serve as a plug to restrain the highly pressurized packaged genome and thus would be the first virion protein to contact the host cell wall, degrading the peptidoglycan layer and thereby facilitating viral genome entry into the host bacteria. Acts probably as a multifunctional enzyme that degrades N-acetylglucosamine polymers (in vitro) and cleaves the peptide cross-links of the host cell wall. Essential for the tail assembly.
Subcellular Localization:
Virion. Note=Located at the distal tip of the tail knob.
Sequence:
MVYVSNKYLTMSEMKVNAQYILNYLSSNGWTKQAICGMLGNMQSESTINPGLWQNLDEGNTSLGFGLVQWTPASNYINWANSQGLPYKDMDSELKRIIWEVNNNAQWINLRDMTFKEYIKSTKTPRELAMIFLASYERPANPNQPERGDQAEYWYKNLSGGGGGGLQLAQFPMDIINISQGENGSFSHKGTLCIDFVGKTEKYPYYAPCDCTCVWRGDASAYLAWTSDKEVMCADGSVRYITWVNVHESPLPFDVGKKLKKGDLMGHTGIGGNVTGDHWHFNVIDGKEYQGWTKKPDSCLAGTELHIYDVFAVNNVEIINGNGYDWKTSDWQDGDGGDGDDDNDNNKTKDLITLLLSDALHGWKA
The following text describes a protein:
Function:
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Subcellular Localization:
Cytoplasm.
Sequence:
MNFEQYESAYPPRALPPGAWVTRIGPSPTGKAHIGTALQAVINRSLADGSGGAFLLRIEDTDRERFVEGAIEDLLAALDWLGIRPDESVAHGGAYGPYVQSERLPIYQAAARQLVEVGHAYYCFCTPERLESVRMAQQAAGKPTMYDRHCRNLGREEVEKRLATGEKAVVRLKVPDGTEIAFDDLARGRIAFESQTIDDSVLLKSDGFPTYHLAVVVDDHLMRVNQIIRGEEWIPSTPKHVLLYQYFGWPMPRIAHTPILRDMSRRKLSKRSGDTSITGYRVQGYLPEGLRNFLTRIIWPHPEGKDVYDHEEFVRLFKAEDLPNTGPIVDPQLLDFINGQYLRRLSSAELYTATVEYLKFLLGLHQDIIFETYHPSAPIKQTLTRAELGSFYSAFTANPTYTERVLTLEPERYKRLSDIVVSTGFFFPALFTPADPKLLAKPLGSPEKAGALLGEYLRLYRPDAAQAEWEQSVRELAHEAGVKDGKLFMTLRVAVTGREQTPPLFEVLTILGGDEVQRRLELAAAMPVSL
The following text describes a protein:
Function:
Anti-inflammatory antagonist of interleukin-1 family of proinflammatory cytokines such as interleukin-1beta/IL1B and interleukin-1alpha/IL1A. Protects from immune dysregulation and uncontrolled systemic inflammation triggered by IL1 for a range of innate stimulatory agents such as pathogens.
Subcellular Localization:
Secreted.
Sequence:
MPWRNQLDIPGFQDYSKDQSPTITGMCSLPMTRYYIIKDADQKALYFRGDQLLVGDPNVDNCCAEKICILPNRGLDRTKVPIFLGIQGGSRCLACVETGEGPTLQLEDVNIEDLYKGGEQATRFTFFQRSSGSAFKLEAAAWPGWFLCGPAEPQQPVQLVKESEPLARTEFYFEQSR
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Sequence:
MSVTLHTDLGDIKMELNCEQTPKAAENFLALCASGYYDDNIFHRNIKGFMVQTGDPSGTGKKGTSIWKQHFDDEIVDSLRHNARGVVSMANSGPNTNGSQFFITYGKQPHIDMKYTIFGRVIDGNEVLDDLEKVPVNEKTYRPLRDVKIQRVTIHANPIAD
The following text describes a protein:
Function:
Zinc-sensing receptor that can sense changes in extracellular Zn(2+), mediate Zn(2+) signal transmission, and participates in the regulation of numerous physiological processes including glucose homeostasis regulation, gastrointestinal mobility, hormone secretion and cell death. Activation by Zn(2+) in keratinocytes increases the intracellular concentration of Ca(2+) and activates the ERK/MAPK and PI3K/AKT signaling pathways leading to epithelial repair. Plays an essential role in normal wound healing by inducing the production of cytokines including the major inflammatory cytokine IL6 via the PKC/MAPK/CEBPB pathway (By similarity). Regulates adipose tissue metabolism, especially lipolysis, and regulates the function of lipases, such as hormone-sensitive lipase and adipose triglyceride lipase (By similarity). Plays a role in the inhibition of cell death and protects against oxidative, endoplasmic reticulum and mitochondrial stress by inducing secretion of the cytoprotective pigment epithelium-derived growth factor (PEDF) and probably other protective transcripts in a GNA13/RHOA/SRE-dependent manner. Forms dynamic heteroreceptor complexes with HTR1A and GALR1 depending on cell type or specific physiological states, resulting in signaling diversity: HTR1A-GPR39 shows additive increase in signaling along the serum response element (SRE) and NF-kappa-B pathways while GALR1 acts as an antagonist blocking SRE.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MASPSLPGSDCSQIIDHSHVPEFEVATWIKITLILVYLIIFVMGLLGNSATIRVTQVLQKKGYLQKEVTDHMVSLACSDILVFLIGMPMEFYSIIWNPLTTSSYTLSCKLHTFLFEACSYATLLHVLTLSFERYIAICHPFRYKAVSGPCQVKLLIGFVWVTSALVALPLLFAMGTEYPLVNVPSHRGLTCNRSSTRHHEQPETSNMSICTNLSSRWTVFQSSIFGAFVVYLVVLLSVAFMCWNMMQVLMKSQKGSLAGGTRPPQLRKSESEESRTARRQTIIFLRLIVVTLAVCWMPNQIRRIMAAAKPKHDWTRSYFRAYMILLPFSETFFYLSSVINPLLYTVSSQQFRRVFVQVLCCRLSLQHANHEKRLRVHAHSTTDSARFVQRPLLFASRRQSSARRTEKIFLSTFQSEAEPQSKSQSLSLESLEPNSGAKPANSAAENGFQEHEV
The following text describes a protein:
Function:
Functions as an E3 ubiquitin ligase.
Sequence:
MENRTGLTYMNRKLSGLTVTDDSSSAFSDCNSDRSGEFPPSSSENRRLFLSRAAENPDDLIRYLVSHLDSSSSSVDEQKQAAMEIRLLTKDKPENRIKLARAGAIKPLISLVSSSDAQLQEHGVTAVLNLSLCDENKELIASSGAIKPLVRALKSGTPTAKENAACALLRLSQIEDNKIAIGRSGAIPHLVSLLETGGFRGKKDAATALYSLCSAKENKTRAVEAGVVKPLVELMADFDSNMVDKAAYVMNLLMSAAEAKPAVVEEGGVPVLVEIVEVGTQRQKEMGVSILLQLCEESVVYRTMVAREGAIAPVVALSQSSKSRAKLKAEALIEILRRPRQQQQQQQLDCNRI
The following text describes a protein:
Function:
This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Sequence:
MNNNINGTVDGQTVVEYSTVDSSVKELIEAAIQVRNNAYCPYSNFPVGAALRTTTGEIVTGCNVENGTFGPSVCAERTAVCKAISEGHREFTAVAVAAYQENEFTAPCGTCRQTLAEFSAKDIPIYLVKPAPVRVMITSLFKLLPHAFSPTFLNNK
The following text describes a protein:
Function:
Dipeptidase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide. The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP. GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp. The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain. The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin. This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties. Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure. GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides. Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA. Gliotoxin contributes to pathogenesis during invasive aspergillosis. In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species.
Sequence:
MSPSPIEEQATRLLKEVPLIDGHNDFPYMIRGWFRNDINGQDAHLYDMPIGQTDLQRLQKGLLGGQFWSAFVPCPKNPDKEVGSLEALRQTLQQLDVIHRLIERHPTILQFADSAASIWSSFRAGRVASLIGIEGLHQIADSVSALRMLHRLGVRYVTLTHNCHNAFADAATVSPELHGGLSRKGERLIRELNRMGMMIDLSHTSHEAQTQALRLSRAPVIYSHSSIYSLRAHARNVTDENLHLLHRNRGVVMICFLRELLASEADQATLAHVIDHIIYAGTRIGYEHVGIGSDFDGMLRGPDGLHDVSCYPALVAGLLERGVSEEDVKRVMGLNVIRVLEEVERVAAELQGAGEECLCDELDEVWNEDIKEQLTRERERVRKLGPQK
The following text describes a protein:
Function:
Negative regulator of the Wnt signaling pathway. Inhibits Wnt signaling in a cell-autonomous manner and functions upstream of beta-catenin (By similarity).
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MSLPCCGRVRYLLLALLLHGLGEGSALLHPDSRSHPRSLEKSAWRAFKESQCHHMLKHLHNGARITVQMPPSIEGHWVSTGCEVRSGPEFITRSYRFYHNNTFKAYQFYYGGNRCTNPTYTLVIRGKIRLRQASWIIRGGTEADYQLHNVQIISHSEAVAEKLSQLVNRTCPGFVPGNSPWEQDVSYNLWREENGCECTRALNFAMHELQLIRVEKQYLHHNLDHLVEELFLGDIHTDATQRMYYRPSSYQPPLQNAKNHDHSCIACRIIYRSDEHHPPILPPKADLTIGLHGEWVSQRCEVRPEVLFLTRHFIFHDNNNTWEGHYYHYSDPICKHPTFTIYAKGRYSRGVHSSKVMGGTEFVFKVNHMKVTPMDIATASLLNVFNGNECGAEGSWQVGVQQDVTHTNGCVALGIRLPHTEYEIFKMEQNARGSYLLYNGQRPSDGSSPDRPEKRATSYQMPLVQCASSAPRPEESAEENKIGRYSSRAPKKDSSVFMLTLMLFICTGSHWNIHS
The following text describes a protein:
Function:
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus.
Sequence:
MENPLLTVLSHRTAGIEYRGVVTKRLATLKRRLGVQTKNTKEYSPKQVSTEDVVQDARFAQLLLLQAERAWAVSQETASILETNGSAGKRKRVASKLTKAVQYAMALEQSVSDTQSDEVRLQIATYRLLLEGALYAHKKQWQKLVQPYSAARVGLSALITLAKDAEEAELLADVISTQIDPALGVALLKVSPDRKLDLENASKGYVDAGSDFGKLVEKINPHALEVDEAHGLDEIEWRGHQAKITDPDVARTVSNALTQTKAEEKTISDYDTLLSLWQSANDLVKEELERFELAGIAAHDDTTQNAHIVLTFINFHMLQQRIERDLLLLSEVSQLKTVDRKDHAKTNKEKLPSALKISTHTRLLQLKDSVRLLGNIVQSVDEILNLAGVSNDSSLVSALTATKAAYRAQKLAAIGASYDLVGDYKNALALNSKALQLQQTVGDADHAAVTGIQVPKNAQLVANTARLQALETIAQRLTEKPLNHPVSDNMDSYPMATASDTAHNIVEFDQRLKPVLVKPVFFDIAYNYVDYPAEVQAVETAKGGEEQKTKKSGFLGGLFRK
The following text describes a protein:
Function:
Acts as a component of a SCF E3 ubiquitin ligase complexes.
Subcellular Localization:
Nucleus.
Sequence:
METLPLEICMKIFCFLDHTHLAVSQQVCRKWKLMASDNALWSNLFKERWGGDHAAFYAPLGSKSWKEVYEAQDRCDRVGLGLKIVREGSDYYLVHQGEVQRYLGSRKYRRQLSGHTSSSETDFTGESSVAEERSCRGILDKILFFIGDLEAASVDAKRSRVI
The following text describes a protein:
Function:
Ras-like protein involved in the activation of Ras protein signal transduction (By similarity). Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (By similarity). Plays a role in hyphal morphology and conidiophore development. Required for full virulence.
Domain:
The conserved rasB internal amino acid insertion (residues 109 to 131) is required for the function.
Sequence:
MTLYKLVVLGDGGVGKTALTIQLCLNHFVETYDPTIEDSYRKQVVIDQQSCMLEVLDTAGQEEYTALRDQWIRDGEGFVLVYSITSRASFTRIQKFYNQIKMVKESAHSGSPSGASYLGSPMNAPSGPPLPVPVMLVGNKSDKAVERAVSAQEGQALAKDLGCEFVEASAKNCINVEKAFYDVVRMLRQQRQQQQGGRAQDRRPTGLGPMRDRDAGPEYPKTFRPDRARHRGGIKCVIL