lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II). Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. Required for respiration and the maintenance of the mitochondrial compartment.
Miscellaneous:
MISCELLANEOUS: Present with 1560 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MLPTFKRYMSSSAHQIPKHFKSLIYSTHEVEDCTKVLSVKNYTPKQDLSQSIVLKTLAFPINPSDINQLQGVYPSRPEKTYDYSTDEPAAIAGNEGVFEVVSLPSGSSKGDLKLGDRVIPLQANQGTWSNYRVFSSSSDLIKVNDLDLFSAATVSVNGCTGFQLVSDYIDWNSNGNEWIIQNAGTSSVSKIVTQVAKAKGIKTLSVIRDRDNFDEVAKVLEDKYGATKVISESQNNDKTFAKEVLSKILGENARVRLALNSVGGKSSASIARKLENNALMLTYGGMSKQPVTLPTSLHIFKGLTSKGYWVTEKNKKNPQSKIDTISDFIKMYNYGHIISPRDEIETLTWNTNTTTDEQLLELVKKGITGKGKKKMVVLEW
The following text describes a protein:
Function:
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Sequence:
MAPAKKGGEKKKGRSAINEVVTREYTINIHKRIHGVGFKKRAPRALKEIRKFAMKEMGTPDVRIDTRLNKAVWAKGIRNVPYRIRVRLSRKCNEDEDSPNKLYTLVTYVPVTTFKNLQTKFSL
The following text describes a protein:
Function:
Deubiquitinating enzyme that plays a role in various cellular processes, including DNA repair, cell cycle regulation, and immune response. Plays a role in the inhibition of type I interferon signaling by mediating the 'Lys-33' to 'Lys-48' ubiquitination transition of TBK1 leading to its degradation. Cleaves the ubiquitin chain from the histone demethylase LSD1/KDM1A and prevents it from degradation by the 26S proteasome, thus maintaining LSD1 protein level in cells. Plays a role in the DNA damage response by regulating the deacetylase activity of HDAC1. Mechanistically, removes the 'Lys-63'-linked ubiquitin chain promoting the deacetylase activity of HDAC1 in response to DNA damage. Also acts as a specific deubiquitinase of histone deacetylase 3/HDAC3 and cleaves its 'Lys-63'-linked ubiquitin chains to lower its histone deacetylase activity. Regulates MYC levels and cell proliferation via antagonizing ubiquitin E3 ligase FBXW7 thereby preventing MYC 'Lys-48'-linked ubiquitination and degradation. Participates in antiviral response by removing both 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of Zika virus envelope protein E. Constitutively associated with IL-33R/IL1RL1, deconjugates its 'Lys-27'-linked polyubiquitination resulting in its autophagic degradation.
Subcellular Localization:
Cytoplasm. Nucleus. Note=In response to DNA damage, recruited to DNA damage sites in the nucleus.
Sequence:
MDKILEGLVSSSHPLPLKRVIVRKVVESAEHWLDEAQCEAMFDLTTRLILEGQDPFQRQVGHQVLEAYARYHRPEFESFFNKTFVLGLLHQGYHSLDRKDVAILDYIHNGLKLIMSCPSVLDLFSLLQVEVLRMVCERPEPQLCARLSDLLTDFVQCIPKGKLSITFCQQLVRTIGHFQCVSTQERELREYVSQVTKVSNLLQNIWKAEPATLLPSLQEVFASISSTDASFEPSVALASLVQHIPLQMITVLIRSLTTDPNVKDASMTQALCRMIDWLSWPLAQHVDTWVIALLKGLAAVQKFTILIDVTLLKIELVFNRLWFPLVRPGALAVLSHMLLSFQHSPEAFHLIVPHVVNLVHSFKNDGLPSSTAFLVQLTELIHCMMYHYSGFPDLYEPILEAIKDFPKPSEEKIKLILNQSAWTSQSNSLASCLSRLSGKSETGKTGLINLGNTCYMNSVIQALFMATDFRRQVLSLNLNGCNSLMKKLQHLFAFLAHTQREAYAPRIFFEASRPPWFTPRSQQDCSEYLRFLLDRLHEEEKILKVQASHKPSEILECSETSLQEVASKAAVLTETPRTSDGEKTLIEKMFGGKLRTHIRCLNCRSTSQKVEAFTDLSLAFCPSSSLENMSVQDPASSPSIQDGGLMQASVPGPSEEPVVYNPTTAAFICDSLVNEKTIGSPPNEFYCSENTSVPNESNKILVNKDVPQKPGGETTPSVTDLLNYFLAPEILTGDNQYYCENCASLQNAEKTMQITEEPEYLILTLLRFSYDQKYHVRRKILDNVSLPLVLELPVKRITSFSSLSESWSVDVDFTDLSENLAKKLKPSGTDEASCTKLVPYLLSSVVVHSGISSESGHYYSYARNITSTDSSYQMYHQSEALALASSQSHLLGRDSPSAVFEQDLENKEMSKEWFLFNDSRVTFTSFQSVQKITSRFPKDTAYVLLYKKQHSTNGLSGNNPTSGLWINGDPPLQKELMDAITKDNKLYLQEQELNARARALQAASASCSFRPNGFDDNDPPGSCGPTGGGGGGGFNTVGRLVF
The following text describes a protein:
Function:
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB).
Subcellular Localization:
Endosome membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MTSLDVLINKATDPTLTSDNWQYILDVCDRISADPETETKRTITILKTKLTSKDANVVLRSLSLLISIAENCGSRVKQEIATKSFLQDALVKRLSDKKLHATVKYKICEVLTQLYNAFKGDPSLKPMTDAYNKARSEHPRYFSKQTQGPSKPAKKERTQQDKDREEDELQRALKLSLQEFEQQKTGKKEPDVNKPLPEIQPEPESPPVETVATVSKVRALYDLVSYEPDELSFRKGDVITVIESVYRDWWRGSLPSGKIGIFPLNYVTPIVNKSPQDIAKEIEIENKLITEEQRKIERLLAILSSQQIETINEDEVTHLYNEIIPLRIQLGNSIDKYGARQEELKVLNQSLNSEIKLYNELLDKSISSRAKHNTGGAMYQMSPYPTEQFPGQSQPQLSQQQQHQPYAQPQQTSNYAQQSQTVPPQFTQSQQTQPQYHQSHTRTGSHQEVPQYSGYNSNNIPPPATTFNQYPPSQLQQQDTSAGFGNDVYNRAAPGQPY
The following text describes a protein:
Function:
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity).
Subcellular Localization:
Cytoplasm.
Domain:
Lacks the C-terminal regulatory region which is replaced by HisZ.
Sequence:
MLTIALPKGSLLRDSIDRFQQIGLDFSAFLEPKNRQLQILDPTHRAKALLVRAWDVPVYVEYGQAQLGIVGYDILREKKPAVAQLADLNFGGCRLSVAVPQASPYRRSVDLPPHGRVASKFVHCALEHFRRLDLPVEIIPLYGSVELGPITGMSEAIVDLVSTGRTLQENGLMEIEVLFDSSARLIAHPLSYRVNGDRLLDWVEKLRSVI
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:
MSVVISTSLGSLLINLRFVDCPKASFNFLALCASSYYDGCRFHRLVPETFVLTGDPTGTGKGGESVFVHHQDIKQRYFEDEGMGNALHDRRGVVSMAHKGNKPDTNASQFFILFKPCPSLDSKHTAFGVVDFGWNDGESERTLKRVEELEADGSYNVLDVEARILSTTVLYNPFAEGHIKLNV
The following text describes a protein:
Function:
Non-catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth. The TSC-TBC complex acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1. In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) by the mTORC1 signaling. The TSC-TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1 (By similarity). Within the TSC-TBC complex, TSC1 stabilizes TSC2 and prevents TSC2 self-aggregation (By similarity). Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling. Also acts as a co-chaperone for HSP90AA1 facilitating HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and glucocorticoid receptor NR3C1 (By similarity). Increases ATP binding to HSP90AA1 and inhibits HSP90AA1 ATPase activity. Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (By similarity). Recruits TSC2 to HSP90AA1 and stabilizes TSC2 by preventing the interaction between TSC2 and ubiquitin ligase HERC1 (By similarity).
Subcellular Localization:
Lysosome membrane; Peripheral membrane protein. Cytoplasm, cytosol. Note=Recruited to lysosomal membranes in a RHEB-dependent process in absence of nutrients. In response to nutrients, the complex dissociates from lysosomal membranes and relocalizes to the cytosol.
Domain:
The C-terminal putative coiled-coil domain is necessary for interaction with TSC2.
Sequence:
MAQLANIGELLSMLDSSTLGVRDDVTAIFKESLNSERGPMLVNTLVDYYLETNSQPVLHILTTLQEPHDKHLLDKINEYVGKAATRLSILSLLGHVVRLQPSWKHKLSQAPLLPSLLKCLKMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCLKKPGHVTEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENVETFEEVVKPMMEHVRIHPELVTGSKDHELDPRRWKTLETHDVVIECAKISLDPTEASYEDGYSVSHQLSACFPYRSADVTTSPYVDTQNSYGGSTSTPSSSSRLMLFSPPGQLPQSLSSPSTRLLPEPLQASLWSPSAVCGMTTPPTSPGNVPADLSHPYSKAFGTTAGGKGTPSGTPATSPPPAPPCPQDDCVHGSAAQASATAPRKEERADSSRPYLHRQSNDRGLEDPPGSKGSVTLRNLPDFLGDLASEEDSIEKDKEEAAISKELSEITTAEADPVVPRGGFDSPFYRDSLSGSQRKTHSAASGTQGSSVNPEPLHSSLDKHGPDTPKQAFTPIDPPSGSADVSPAGDRDRQTSLETSILTPSPCKIPPQRGVSFGSGQLPPYDHLFEVALPKTACHFVSKKTEELLKKVKGNPEEDCVPSTSPMEVLDRLIEQGAGAHSKELSRLSLPSKSVDWTHFGGSPPSDELRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEKDGRLRKLEEDRAEAAEAAEERLDCCSDGCTDSLVGHNEEASGHNGETRTSRPGGTRASCGGRVTGGSSSSSSELSTPEKPPSQRFSSRWEPALGEPSSSIPTTVGSLPSSKSFLGMKARELFRNKSESQCDEDSVTMSSSSLSETLKTELGKDSGTENKTSLSLDAPHPSSPNSDNVGQLHIMDYNETHPEHS
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MRGDRPPSSMEPQMEPRLAVKVENEESECEDCLSSIKRETDPPPADGFREKEMEILQIKEEEPDSDYYQSPMERRAVPLADGVSEIKCEDEGSDAKDHITAIKCETESVPAAGAELEVLQIKIKEEEPDPEDHQTPMESSAAPLTDGESCINDGNCWDPDPPRCLIRHERRLLTETSNHFDSLDAAKEPLSGAGVLPGAALTDGTRYEDCSASADTSGFICEKCGRCFSGNSDPLAHLCADCPENFTDPHKNEEVQGVRFPCSECGKHYNNKCSLKTHQLLHTGVKPFTCKDCHKTFSLRKDLNRHQKIHTGEKPFTCTECGKGFYLRGNLNIHYKIHTGEKPYACTECGKSFSEKSKLRKHQKIHTGEKPFTCTECGKSYSEKSKLLNHHKTHTGENLFNCTECGGTFLTKNSLVQHQMIHTGEKPFTCTECGKGFSTKNSLTSHERIHTGEKPFTCSECGKCFSRKCNLNVHERIHRKEEGKERKRKSFPCTECGKTFAVKNNLKKHQQIHSLQRTIERKRNIIAQQHIGHVGHVGQEQQGLAPVTLCCSAIGASQLSESKLITVLFLPQTS
The following text describes a protein:
Function:
Lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, acts as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation. Involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking. Alternatively, regulates slow endocytic recycling of endocytosed proteins back to the plasma membrane. Also involved in cargo protein delivery to the plasma membrane. Plays a role in ciliogenesis coordination, recruits EHD1 to primary cilium where it is anchored to the centriole through interaction with tubulins (By similarity). May indirectly play a role in neurite outgrowth (By similarity).
Subcellular Localization:
Recycling endosome membrane; Peripheral membrane protein. Late endosome membrane. Cell projection, cilium membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Note=Localization to late endosomes is actin-dependent. Association to tubular recycling endosomes is regulated by RAB35 and ARF6. Interaction with tubulins achors MICALL1 to the centriole.
Domain:
Probably exists in a closed and an opened conformation due to interaction of the C-terminal RAB-binding domain (RBD), also described as bivalent Mical/EHBP Rab binding (bMERB) domain, with the N-terminal calponin-homology (CH) domain. The conformational change is regulated by RAB13 and may modulate MICALL1 interactions with functional partners.
Sequence:
MAGPRGALLAWCRRQCEGYRGVDIRDLSSSFRDGLAFCAILHRHRPDLLDFDSLSKDNVFENNRLAFEVAEKELGIPALLDPNDMVSMSVPDCLSIMTYVSQYYNHFAGSGPAGVSSPRKGLVLSSPPSEASTPADPGDRAQGEECSSGSLSKQGSHRTPSSTCAACQQHVHLVQRYLADGKLYHRHCFRCRRCSSTLLPGAYRNGPEEGTFVCAEHCARLGPSGRSGARPGTPPQPKQQQLTEEAKEVEGGSPSPKATAGAEADVPKASPEGRPQVPTKPRVPGRPQELASPPASRPTPAPRKASESTAPTPPTPRPRSSLQQENLVEQGGGSGLVNGKLQEPPIPKPRGTPKLSERTPAPRKDPPWITLVQAEPKKKPAPLPPSSSPGPPPGQEGRQVENGGVDKAAPRGPEPKPYNPFEEEEEEPPAAPSPAPGPAPTPPESTPKSLHPWYGITPTSSPKTKKRPAPRAPSTSPLTLHASRLSRSEPPSATPSPALSVESLSSESSSQAPSEELLEPPVVPKSSSEPAVHAPGTPGTSASLSANSSLSSSGELVQPSMDRTPQASPGLAPNSRGSPGPPPAKPCSGTAPTPLVLVGDKSPAPSPGTSSPQLQVKSSCKENPFNRKPSPTASPSVKKATKGSKPARPPAPGHGFPLIKRKVQSDQYIPEEDIHGEIDTIERQLDALEHRGVLLEEKLRGGVNEGREDDMLVDWFKLIHEKHLLVRRESELIYVFKQQNLEQRQADVEYELRCLLNKPEKDWTEEDRGREKVLMQELVTLIEQRNAIVNCLDEDRQREEEEDKMLEAMIKKKEFQKETEPEGKKKGKFKTMKVLKLLGNKRDTKSKCPGDRS
The following text describes a protein:
Function:
May play roles in cilia formation and/or maintenance.
Sequence:
MELYEVKSATNETVQANYSKLSDHIRRLTPQGIQCSVFCGGTNCKYENPENWKADSLAIQGIYSHWITDDILAMARPSTMVIVQKNIIQQFESLGIKSIINLQSPREHASCGQPLEESGFSYDPNIFMEHNIFYYNFAWKDYGDATLVGLLNMVKVLAFAVTEGRVAIHCHAGLGRTGVLIACYLVYSLRVSANDAIRYVRLKRPGSVQTRGQILCVRHFAQFVLPRTITYCLKENINKNKYMSEFSLVRFLHRQRVILHGYEERTFKFIPKIVHCICERILKLCGCWIDEFSSNTPLTFDFLYTKLNGNIKRYESTYSLCSTNSDSLFSNELKSPEEISSPSSPNPSENGDPSDSFSELSTLDGDEIREELLIENRCFQELETQKCFNQEMSEESIVIQDINVAVDALLLDYSTLSNEIKKKVRQFQIEINSSQVGWAKLAIETDLRILAMLLFEWIESLKHPVMKREFFENIVVNYKQPEVCFQKFPAEEGYFMEYLLRFVSKINPISKENQEDLIKRIIAACSQQTLLIQGKMKPIDKGFKKLRDGTLACTIEFFQSLFELIEVHHSLKSSVYLEESKMYNENDLENDFQ
The following text describes a protein:
Function:
Involved in the biosynthesis of aklanonate which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers.
Sequence:
MAELSLAELREIMRQSLGEDEVPDLADADTVTFEDLGLDSLAVLETVNHIERTYGVKLPEEELAEVRTPHSMLIFVNERLRAAA
The following text describes a protein:
Function:
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MLKIIIPTIMLIPLTWMSKPNMIWINTTTYGLLISLISLFYLNQPNDNTLNSSLMFFSDSLSAPLLALTTWLLPLMLMASQHHLSKEPLTRKKLYISMLILLQLFLIMTFTASELIFFYILFEATLIPTLIIITRWGNQTERLNAGLYFLFYTLMGSLPLLVALLYIHNFMGSLNFLMIQYWIQPLPNSWSNIFLWLACMMAFMVKMPLYGLHLWLPKAHVEAPIAGSMVLAAVLLKLGGYGMMRITTLLNPLTNFMAYPFMMLSLWGMIMTSSICLRQTDLKSLIAYSSVSHMALVIVAVLIQTPWSYMGATALMIAHGLTSSMLFCLANSNYERIHSRTMILARGLQTLLPLMAAWWLLASLTNLALPPTINLIGELFVVMSSFSWSNITIILMGINITITALYSLYMLITTQRGKYSHHIKNIKPSFTRENALMTLHLLPLLLLSLNPKIILGPIY
The following text describes a protein:
Function:
FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of the phytotoxin stemphyloxin II. The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase sthA and the enoyl reductase sthE via condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units and 5 methylations. The C-terminal reductase (R) domain of sthA catalyzes the reductive release of the polyketide chain. Because sthA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase sthE. The short-chain dehydrogenase/reductase sthC then catalyzes reduction of dehydroprobetaenone I to probetaenone I. The cytochrome P450 monooxygenase sthF catalyzes successive epoxidation, oxidation (resulting from epoxide opening) and hydroxylation to install a tertiary alcohol in the decaline ring to yield betaenone C from dehydroprobetaenone I and betaenone B from probetaenone I. The FAD-linked oxidoreductase sthB is responsible for the conversion of betaenone C to betaenone A via an intramolecular aldol reaction between C-1 and C-17 to form the bridged tricyclic system in betaenone A. Finally, the cytochrome P450 monooxygenase sthD catalyzes the hydroxylation of C-15 to afford the final metabolite stemphyloxin II.
Sequence:
MMNPFFQNTSCSPYYRTDQPCSLGNYVSYAIPVAGVADIVAAINFTQTHNVRLVIKNTGHDYMGKSTGRGALSLWTHNLKSRQLVNYSSAHYTGPAIKVGAGVTGGEALVHASASGYRIVSGDCPTVGYSGGYSSGGGHSILNSVHGLAADNVLEWEVVTADGRHVVASPDQNSDLYWAMSGGGGGTFAVALSMTSRVHADSIIGAASLSFNATSAPSNDSFVSALNAWWAFLPSLVDVGATPSWNIFAGNFLVPNTTAPGRTAADMDTLYSPFLSELKRLGIPYAFESFSAPNYLQHYNDTDGPLPDGPLAAWA
The following text describes a protein:
Function:
Catalyzes the reduction of nitrite to ammonium in the nitrate assimilation pathway, using ferredoxin as the electron donor. Can use reduced methyl viologen but neither NADPH nor NADH as electron donors.
Miscellaneous:
MISCELLANEOUS: Enzyme stability and activity depend upon the salt concentration.
Sequence:
MASKKEQWKSDLYGDAVRDELEAFAEEGFESIPEDERDKWFTRFKFWGVFQQRTGQESYFMMRLTNANGVLEPGQLRTIAEVARDYATGPVDNPEFGNGWVDLTTRQSIQLHWLELEDIPEIWEQLESVGVTSRSAGGDTMRNITGCPVAGKDTHELVESKPLLDRFQSELREDDALSNMPRKFNISVTGCREGCAQDSINDIGLEPARKEVDGEVITGFNVRVGGGLGSRKPRVARSLDVFVADEERAYEVVRGFVELYHDHGNRDVRARARSRFFVDDWGTEKIRDRLESEYLDFELQSAGEDIRDEYTYNAGRPQSAGKSDHVGVHEQSDGRYYVGLSVAVGRLTAADALELADLADKYGSGKIRLTRRQNPIVMDVPAGALDDLLAEPLLSKHTPEPNPFQRGTVACTGTEFCSLALTETKARTARMLRWLRDNVEVPDDVHQLKIHYSGCTADCGQANTADIGLFGMRAQKDGEMVEAMDIGVGGGIGDEPSFVEWIHQRVPADEVPGAIASLVEAFAAHRTAGQTFRQWVEAEGPDAVAEYCEPIETDFEAPYMHDAKQSWYPFADEDEPPKTEQPMTSD
The following text describes a protein:
Function:
Inhibits GDP/GTP exchange reaction of RhoB. Interacts specifically with the GDP- and GTP-bound forms of post-translationally processed Rhob and Rhog proteins, both of which show a growth-regulated expression in mammalian cells. Stimulates the release of the GDP-bound but not the GTP-bound RhoB protein. Also inhibits the GDP/GTP exchange of RhoB but shows less ability to inhibit the dissociation of prebound GTP.
Subcellular Localization:
Cytoplasm.
Sequence:
MSEAEANLKPLDDDEPEETPGYVPPAQKTWEEIQNLDADDEALVKYKQTLLGVTPEELPKGPKNVVVEKVAIVPTDEKGNPVRDPIELDLIGDISKLKDSPITIKEGTYYKIKIIFKVYNDQIISGLRLHNLFYRKGIRVTKDSFMVGSYGPKFEPHEYLTPIDEAPKGMMARGKYIIRSKFIDDDKNSHLEWEWAIEIKKDWQ
The following text describes a protein:
Function:
May be involved in the regulation of meristem growth.
Sequence:
MRGMVSFAVWALFAALLSQQLFASVASVRFEDAKTYYLSPPSGSHGTPPSHTPPSSNCGSPPYDPSPSTPSHPSPPSHTPTPSTPSHTPTPHTPSHTPTPHTPPCNCGSPPSHPSTPSHPSTPSHPTPSHPPSGGYYSSPPPRTPVVVTPPSPIVDPGTPIIGGSPPTPIIDPGTPGTPFIPAPFPPITGTCDYWRNHPTLIWGLLGWWGTVGGAFGTVSIPSSIPGFDPHMNLLQALSNTRSDPIGALYREGTASWLNSMVNHKFPFTTPQVRDHFVAGLSSNKAATKQAHTFKLANEGRLKPRV
The following text describes a protein:
Function:
Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Microsome membrane.
Sequence:
MLYFFAAVLCAVSTLLLLNRTLSRLRLSPARTSYDYDVIIVGGSIAGPVLAKALSDQGRKVLMVERTLFTKPDRIVGELLQPGGLNALKEVGMKECAETIGMPCHGYVVVDHKGKQVDLPYRKGASGVSFHFGDFVQSLRSHVFHNCKANVTMVEGTVNNILTEGLSFSERAYGVEYTIAEKYEVPTKPFREDPPKTNPVAATVRKVATAPLVVMCDGGMSKWKSRYQHYTPAYEYHSHFIGLVLKTVRLPKEQRGTVFFGKTGPILSYRLDDNELRLLVDYNKPTLPSLEKQSEWLIQDVAPCLPENMREQFVRVSKDTKSLRSMPMARYPPAFPSIKGYVGIGDHANQRHPLTGGGMTCCFRDAIRLANSLNGIQSLRSVNQEEMAAIEDKIQAAILNYARYRYTHSCCINLLSWALYSVFSSPALRDACFDYFLCGGNCVTGPMDLLAGLDPNVGSLFFHYCCVMLHGVANVMMRTGAYSESGKQLSNLEKLTNVASFFVDWERMKHAAYLLGKSTQIALPLAKSEFYSMWRFVDPTSPLANISKRIKTMVYTKQFNGKQRKPVGL
The following text describes a protein:
Function:
Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It also interacts with serum amyloid P component.
Subcellular Localization:
Secreted.
Sequence:
MKHQRVPVMILHSKGTMASWPFSRLWSISDPILFQVTLVATLLATVLGSCGIPPYLDFAFPINELNETRFETGTTLRYTCRPGYRISSRKNFLICDGTDNWKYKEFCVKKRCENPGELLNGQVIVKTDYSFGSEIEFSCSEGYVLIGSANSYCQLQDKGVVWSDPLPQCIIAKCEPPPTISNGRHNGGDEDFYTYGSSVTYSCDRDFSMLGKASISCRVENKTIGVWSPSPPSCKKVICVQPVVKDGKITSGFGPIYTYQQSIVYACNKGFRLEGDSLIHCEADNSWNPPPPTCELNGCLGLPHIPHALWERYDHQTQTEQQVYDIGFVLSYKCHFGYKPETDGPTTVTCQSNLEWSPYIECKEVCCPEPNLNNYGSITLHRRPSTSTHCTYISGDKISYECHSKYMFDALCTKHGTWSPRTPECRPDCKSPPVIAHGQHKVVSKFFTFDHQAVYECDKGYILVGAKELSCTSSGWSPAVPQCKALCLKPEIEYGRLSVEKVRYVEPEIITIQCESGYSVVGSENITCSEDRTWYPEVPKCEWEYPEGCEQVVTGRKLLQCLSRPEEVKLALEVYKLSLEIEILQTNKLKKEAFLLREREKNVTCDFNPE
The following text describes a protein:
Function:
Antifungal protein that acts as an inhibitor of growth of human pathogenic molds and yeasts.
Subcellular Localization:
Secreted. Host cytoplasm.
Sequence:
MHITSIAIVFFAAMGAVASPIATESDDLDARDVQLSKFGGECSLKHNTCTYLKGGKNHVVNCGSAANKKCKSDRHHCEYDEHHKRVDCQTPV
The following text describes a protein:
Function:
Binds to the 23S rRNA.
Sequence:
MKVIFTQDVKGKGKGKKGEVKEVPVGYANNFLLKKNYAVEATPGNLKQLELQKKRAKQERQQEIEDAKALKETLSNIEVEVSAKTGEGGKLFGSVSTKQIAEALKAQHDIKIDKRKMDLPNGIHSLGYTNVPVKLDKEVEGTIRVHTVEQ
The following text describes a protein:
Function:
Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Involved in the regulation of cellulose production.
Sequence:
MFPKIMNDENFYRKAVEQAVAPPDPPDDRQRSGLRFARRIRLPRAVGLGGMFLPVAAVLVTQPVFGGWWLLLVGWSFVWPHLAWQWAAKALDPLRQEIYNLKVDAILSGMWIALMGVNMLPAAALFMMMSMNLMGAGGRRLFTVGMGLLLASCLVTLQLAGLPVAMRSSSLEVTLSLPVIMLYPLLFAWVSYQTAIKLAEHKRRLQAMSSRDGMTGVYNRRHWEILLRNEFDHSRRHHREATLLIIDIDHFKSINDTWGHDVGDEAIIALTRQLQITLRGSDIIGRFGGDEFAVIMCGTPADSAITAMSRVHERLNTLRLPGAPQVMLRISVGVAPLTPQIGHYREWLKSADMALYKAKNAGRNRTEVAA
The following text describes a protein:
Function:
Iron-storage protein.
Subcellular Localization:
Cytoplasm.
Sequence:
MLSKKLHDALNEQMNFEFYSAHAYMAMAAYCTAESYDGFANFFLVQAEEERFHAMKLYNYINDRGERAIITGFDNPNNEYESVLNAFEVALEHEREVTKRIYNLSDIAWDEREHATITFLKWFVDEQVEEEASFDSIIQKLKRITSDSNALFMLDAELEKRTFTPPAE
The following text describes a protein:
Function:
Membrane-bound E3 ubiquitin ligase expressed during late stages of lytic replication to mediate polyubiquitination of various host membrane proteins related to the immune response. Promotes ubiquitination and subsequent degradation of host MHC-I and CD1D molecules, DC-SIGN and DC-SIGNR, presumably to prevent lysis of infected cells by cytotoxic T-lymphocytes. Binds target molecules through transmembrane interaction. E3 ubiquitin-protein ligases accept ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfer it to target protein. The result of this ubiquitination is the enhancement of the endocytosis of the target chain and the delivery to the lysosome, where it is proteolytically destroyed. Induces ubiquitination not only on lysines, but also on cysteine residues.
Miscellaneous:
MISCELLANEOUS: Specific for HLA-A, HLA-B, HLA-C and HLA-E alleles.
Subcellular Localization:
Host cell membrane; Multi-pass membrane protein. Host endoplasmic reticulum. Note=Probably exerts its effects at the plasma membrane during viral infection.
Sequence:
MEDEDVPVCWICNEELGNERFRACGCTGELENVHRSCLSTWLTISRNTACQICGVVYNTRVVWRPLREMTLLPRLTYQEGLELIVFIFIMTLGAAGLAAATWVWLYIVGGHDPEIDHVAAAAYYVFFVFYQLFVVFGLGAFFHMMRHVGRAYAAVNTRVEVFPYRPRPTSPECAVEEIELQEILPRGDNQDEEGPAGAAPGDQNGPAGAAPGDQDGPADGAPVHRDSEESVDEAAGYKEAGEPTHNDGRDDNVEPTAVGCDCNNLGAERYRATYCGGYVGAQSGDGAYSVSCHNKAGPSSLVDILPQGLPGGGYGSMGVIRKRSAVSSALMFH
The following text describes a protein:
Function:
Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.
Sequence:
MLTPTRAFYQLLDLYPTAILLEFSPRNEKPYAFIGFNPLAQIIARGDEITVFLKNTVTKMKGDPFHHLRRLRQQINCIDNHPLTKLTGAAIGYLSYDAIRYVESIPDRHTASEKIADIDFKFYRDGITFDLESNNAIVSHIVEVKDELKHCYEYGLEKLADITNNLFTPARPKLSTNRKTHYSKSTSLDFKPDSNDTDFKKIVNKAKQYIAAGDIFQVVSSRTFKKPYQGKPFDIYRALKKVSPSPYHFYLQNDSLAIAGASPEKMVSVKNGIIDSVPLAGTRPRGNGKSDQTLAQELINDPKETAEHLMLVDLARNDIGIVSQAGSVEVAELMQPVNFSHVMHLASRVQVSLAKNYDAIDVLKATFPAGTLSGAPKIRAMEIIDELEHSRRGLYGGAIVALDRDDNLDTCIIIRTTIVENGIASIRAGAGIVHDSDPIAEANETRHKAKSVMAAIQLTEGGL