lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MDHEFLITMRLSFSLALITTLILLPVGIFLGYFLSLKRNLLTSLTETLVYMPLVLPPSVLGFYLLLIFSPSSFLGAFLQDVLNVKLVFSFQGLILGSVIFSLPFMVSPIKSALISLPASLKEASYSLGKGEYYTLFFVLLPNIKPSLLMAIITTFTHTIGEFGVVMMLGGDILGETRVASIAIFNEAEALNYSKAHQYALTLTLISFSLLFVTLFLNKKQSSFL
The following text describes a protein:
Function:
Essential for the imd/NF-kappa-B (Imd) humoral and epithelial immune response to Gram-negative bacteria. Functions as an adapter protein that transduces immunity signals from the activation of pathogen recognition receptors (PRRs) by bacterial infection to the Imd signaling pathway. Binding of diaminopimelic acid-type (DAP-type) bacterial peptidoglycans (PGN) causes multimerization or clustering of PGRP receptors which activate the Imd cascade probably by recruiting imd, Fadd and Dredd to the receptor complex. Once in proximity, Dredd cleaves imd in a Fadd-dependent manner to enable its association and activation by the ubiquitin E3-ligase DIAP2. The activated form of imd recruits and activates the Tab2/Tak1 complex thus acting upstream of the IKK complex (ird5 and key) to activate Rel and induce the expression of antimicrobial peptides such as Def, Dpt and Cecropin. Also able to inhibit the viral replication of the Sindbis virus. Involved in promoting the polyubiquitination and stability of faf which in turn, regulates the Imd pathway by controlling imd polyubiquitination and/or stability; they may therefore form a regulatory feedback mechanism within the Imd pathway. Not required for the cuticle melanization immune response to bacterial challenge.
Sequence:
MSKLRNLLPTIFGGKEAQNPTPVEGRLEKDAAPVDDNEPDNNNSGALALPSTAGTPTASSDLTESVLRELSDPNYNSMDVVHSANIPGTLSNVQTNNTMNVHSAQQQVVMNFSNANNLHFGSVYNFNQNLSACSSRKGSTSTAEESVASPDGKPRASATRKTVSIVAMMQSQEEPDVRLLDVVSTHLGEGWKQVMRDLGMSEGQIDQAIIDHQMHGNIREVIYQLLLQWIRSSADGVATVGRLTTLLWESQHRDCVQRMKLVWKALEKRKTNS
The following text describes a protein:
Function:
Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring approximately 15 minutes before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation. CDCd11 with SHS1 11 are involved in the recruitment of BNI5 and thereby ensure efficient localization at the bud neck of MYO1, the type II myosin of the actomyosin contractile ring.
Miscellaneous:
MISCELLANEOUS: Present with 5620 molecules/cell in log phase SD medium.
Subcellular Localization:
Membrane; Peripheral membrane protein. Bud neck. Note=Present at the bud neck during cell division. Probably interacts with phosphoinosides such as phosphatidylinositol 4-phosphate or phosphatidylinositol 5-phosphate.
Domain:
The C-terminal extension (CTE) that contains a coiled coil is important for the recruitment of BNI5 and subsequent localization at the bud neck of MYO1.
Sequence:
MSTASTPPINLFRRKKEHKRGITYTMLLCGPAGTGKTAFANNLLETKIFPHKYQYGKSNASISSNPEVKVIAPTKVVSFNSKNGIPSYVSEFDPMRANLEPGITITSTSLELGGNKDQGKPEMNEDDTVFFNLIMTHGIGENLDDSLCSEEVMSYLEQQFDIVLAEETRIKRNPRFEDTRVHVALYFIEPTGHGLREVDVELMKSISKYTNVLPIITRADSFTKEELTQFRKNIMFDVERYNVPIYKFEVDPEDDDLESMEENQALASLQPFAIITSDTRDSEGRYVREYPWGIISIDDDKISDLKVLKNVLFGSHLQEFKDTTQNLLYENYRSEKLSSVANAEEIGPNSTKRQSNAPSLSNFASLISTGQFNSSQTLANNLRADTPRNQVSGNFKENEYEDNGEHDSAENEQEMSPVRQLGREIKQENENLIRSIKTESSPKFLNSPDLPERTKLRNISETVPYVLRHERILARQQKLEELEAQSAKELQKRIQELERKAHELKLREKLINQNKLNGSSSSINSLQQSTRSQIKKNDTYTDLASIASGRD
The following text describes a protein:
Function:
The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein. It acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated form binds strongly to apatite and calcium (By similarity); The uncarboxylated form acts as a hormone secreted by osteoblasts, which regulates different cellular processes, such as energy metabolism, male fertility and brain development. Regulates of energy metabolism by acting as a hormone favoring pancreatic beta-cell proliferation, insulin secretion and sensitivity and energy expenditure. Uncarboxylated osteocalcin hormone also promotes testosterone production in the testes: acts as a ligand for G protein-coupled receptor GPRC6A at the surface of Leydig cells, initiating a signaling response that promotes the expression of enzymes required for testosterone synthesis in a CREB-dependent manner. Also acts as a regulator of brain development: osteocalcin hormone crosses the blood-brain barrier and acts as a ligand for GPR158 on neurons, initiating a signaling response that prevents neuronal apoptosis in the hippocampus, favors the synthesis of all monoamine neurotransmitters and inhibits that of gamma-aminobutyric acid (GABA). Osteocalcin also crosses the placenta during pregnancy and maternal osteocalcin is required for fetal brain development.
Subcellular Localization:
Secreted.
Sequence:
YLDSGLGAPVPYPDPLEPKREVCELNPNCDELADHIGFQEAYQRFYGPV
The following text describes a protein:
Function:
Kinase required for the regulation of cell division and differentiation. Is part of a signal transduction pathway, activating PleD by phosphorylation.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MILPTALKSRLALEFETLPDPFRRPAARAAGLDPAHAWRLGWLAAVCLAAAAALFTADSGGWPVWAALGAGALPALVSLIFTREDERTQSWLLVLWAVGGSLAAVLTGGVGGAMAAWCLAPVAAASTQDQPKRLAEGAALALIGACVAALTQLSGLAPAAPTGPLAFVLGFLALVTTGLGLAAGLLIGRRRQGARDDRYASEIIGLETLLDGLPHLAIAVRGQGQVTAVRGAAPPGVTRADLVNRGLTGAAAPGDRQRLTAAIAQAHREGSASLTFNPALGVERVVALDMHRVAPNQLVGVLRDITVERHREHALDQARIDAEALAAGRARFLANMSHELRTPLNAIMGFSDIMRARMFGPLSDRYAEYAELIHESGGHLLDLINDVLDMSKIEAERFELQRGVFDAREAVQAAMRLLRVQSDTAGVQLRGVLPPGELEVDADRRALKQIVLNLVSNALKFTPRGGQVTVTAHGYDGVLEIVVADTGVGISPEDLERLGRPYEQAGGAEQRARGTGLGLSLVRAFAQLHGGEMVIESRLGAGTTVSVRLPVLLAPMVAATPTPPAAPEAPSAPEPAPTVEEPPPASLGDNVIAFAPR
The following text describes a protein:
Function:
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in arbutin, cellobiose, and salicin transport.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Domain:
The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain; The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Sequence:
MAKNYAALARSVIAALGGVDNISAVTHCMTRLRFVIKDDALIDSPTLKTIPGVLGVVRSDNQCQVIIGNTVSQAFQEVVSLLPGDMQPAQPVGKPKLTLRRIGAGILDALIGTMSPLIPAIIGGSMVKLLAMILEMSGVLTKGSPTLTILNVIGDGAFFFLPLMVAASAAIKFKTNMSLAIAIAGVLVHPSFIELMAKAAQGEHVEFALIPVTAVKYTYTVIPALVMTWCLSYIERWVDSITPAVTKNFLKPMLIVLIAAPLAILLIGPIGIWIGSAISALVYTIHGYLGWLSVAIMGALWPLLVMTGMHRVFTPTIIQTIAETGKEGMVMPSEIGANLSLGGSSLAVAWKTKNPELRQTALAAAASAIMAGISEPALYGVAIRLKRPLIASLISGFICGAVAGMAGLASHSMAAPGLFTSVQFFDPANPMSIVWVFAVMALAVVLSFILTLLLGFEDIPVEEAAAQARKYQSVQPTVAKEVSLN
The following text describes a protein:
Function:
Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates histone H2B. The SAGA complex is recruited to specific gene promoters by activators, where it is required for transcription.
Subcellular Localization:
Nucleus.
Domain:
The C-terminal SGF11-type zinc-finger domain forms part of the 'catalytic lobe' of the SAGA deubiquitination module; The long N-terminal helix forms part of the 'assembly lobe' of the SAGA deubiquitination module.
Sequence:
MSEYSFDGSEDQESEDCQLVNYAPDVLSELVDDVILGLCFDVHRSCKMGTFFVDDVDPAELKEFEIVDQVGLDIFGQPVSSKKQYECECPNCGRTISANRFAPHLEKCMGMGRNSSRIASKRLQNTGKCESEGDDDDDNDWTYGEKKKKKKSDKKANSPRQSKPSKSSKNGDIPSVGSVGSEKSSGGYVNYEAMSIEERRTVLKQICGVISEHTKRMCTRSHRCPQHSDEQRRQVRLYLLGSAASSLLDDDVHVDIDGYEDSPVVSATGHHHPTNLPKRDHLGRFMSAQQVAAMAAGLPWDTASNSSPGSSVSSMRVVQQWETMGMTTTGPASNSSASASAPPPTKKKKSKKKEGHTHKKSKSKNPVLQQYDLH
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent transferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14) to produce wybutosine-86.
Subcellular Localization:
Cytoplasm.
Sequence:
MQLFISPSKRDIKAVKTELEKRELFDKTTGVISHDGSMFVATTVTEGGRETSDGFVEITDPSINVSSECKYFVRERSPDQKHPSITDDMPKRYTIYGSMALFTAGSFAGWEKTKIQRALTEWLKDKPGVTHVAVNSPISKQQNVIRHPGITRLVGDWGPYPADHPMLYDHPTSEDFHNAYWVTTTQNDIKQCWAPMYTMFSRGNIKEKARVLNSPIFKSSSNSLVVDLYCGIGYFFLSYAQLKPRLILGWDINAWSIEGLRRGAQLAKLSLQVVKEGEKPDWSKVGPPGTTHAIVFNESNEKAVERIEELRRFNETTTMEALPLTHINMGLLPDCKQAWGTATSLAQSGVTTYHVHENVAMNEIEEFTRERGKVFGKHLHTEMVKTFAPGVGHIVWDFIST
The following text describes a protein:
Function:
May be an activating cyclin for the cyclin-associated kinase CDK10.
Sequence:
MDTCNVPGSNKDVKTHFKVSRFIIEAGVKLGMHSVPIATACTVYHKFFKETSLEKYDPYLVAMSAIYLAGKVEEQHLRTRDIINVCHRYQNPGHEPLEVDSKFWELRDSIVHCELLMLRMLNFRVSFQHPHKYLLHYLISLNNWMNRHSWERTPIATAAWALLRDSYHGDLCLRHEPQHIAVAVLYFALQCYGIEVPSNNNAETSWWQVFSEDVTELTINNIISDLINIYTMDTEIA
The following text describes a protein:
Function:
In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity.
Sequence:
MTERKKLVLVDGNSLAYRAFFALPLLSNDKGVHTNAVYGFAMILMKMLEDEKPTHMLVAFDAGKTTFRHGTFKEYKGGRQKTPPELSEQMPFIRELLDAYQISRYELEQYEADDIIGTLAKSAEKDGFEVKVFSGDKDLTQLATDKTTVAITRKGITDVEFYTPEHVKEKYGLTPEQIIDMKGLMGDSSDNIPGVPGVGEKTAIKLLKQFDSVEKLLESIDEVSGKKLKEKLEEFKDQALMSKELATIMTDAPIEVSVSGLEYQGFNREQVIAIFKDLGFNTLLERLGEDSAEAEQDQSLEDINVKTVTDVTSDILVSPSAFVVEQIGDNYHEEPILGFSIVNETGAYFIPKDIAVESEVFKEWVENDEQKKWVFDSKRAVVALRWQGIELKGAEFDTLLAAYIINPGNSYDDVASVAKDYGLHIVSSDESVYGKGAKRAVPSEDVLSEHLGRKALAIQSLREKLVQELENNDQLELFEELEMPLALILGEMESTGVKVDVDRLKRMGEELGAKLKEYEEKIHEIAGEPFNINSPKQLGVILFEKIGLPVVKKTKTGYSTSADVLEKLADKHDIVDYILQYRQIGKLQSTYIEGLLKVTRPDSHKVHTRFNQALTQTGRLSSTDPNLQNIPIRLEEGRKIRQAFVPSEKDWLIFAADYSQIELRVLAHISKDENLIEAFTNDMDIHTKTAMDVFHVAKDEVTSAMRRQAKAVNFGIVYGISDYGLSQNLGITRKEAGAFIDRYLESFQGVKAYMEDSVQEAKQKGYVTTLMHRRRYIPELTSRNFNIRSFAERTAMNTPIQGSAADIIKKAMIDMAAKLKEKQLKARLLLQVHDELIFEAPKEEIEILEKLVPEVMEHALALDVPLKVDFASGPSWYDAK
The following text describes a protein:
Function:
Negatively regulates Toll-like receptor-mediated NF-kappa-B signaling by disrupting IKK core complex formation through interaction with IKBKB.
Subcellular Localization:
Cytoplasm.
Sequence:
MHTLVFLSTRQVLQCQPAACQALPLLPRELFPLLFKVAFMDKKTVVLRELVHTWPFPLLSFQQLLQECAHCSRALLQERPSTESMQAVILGLTARLHTPESGASTQPLCRKHALRVLDMTGLLDDGVEQDPGTMSMWDCTAAVARTCIAQQQGGATEPGPAPIPVEVRVDLRVNRASYAFLREALRSSVGSPLRLCCRDLRAEDLPMRNTVALLQLLDAGCLRRVDLRFNNLGLRGLSVIIPHVARFQHLASLRLHYVHGDSRQPSVDGEDNFRYFLAQMGRFTCLRELSMGSSLLSGRLDQLLSTLQSPLESLELAFCALLPEDLRFLAQSPHAAHLKKLDLSGNDLSGSQLAPFQGLLQASAATLLHLELTECQLADTQLLATLPILTRCTSLRYLGLYGNPLSMAGLKELLRDSVAQAELRTVVHPFPVDCYEGLPWPPPASVLLEASINEEKFARVEAELHQLLLASGRAHVLWTTDIYGRLAADYFSL
The following text describes a protein:
Function:
Antimicrobial peptide. Synthetic peptide shows higher potency against Gram-negative bacteria than against Gram-positive bacteria. Has a very week hemolytic activity.
Subcellular Localization:
Secreted.
Sequence:
GIKDWIKGAAKKLIKTVASHIANQ
The following text describes a protein:
Function:
Plus-end directed kinesin-like motor enzyme that plays a critical role in the organization of phragmoplast microtubules during cytokinesis. Constitutes a signaling module in association with serine/threonine-protein kinase TIO that is required to support phragmoplast expansion and cell-plate growth in plant cells.
Subcellular Localization:
Cytoplasm, cytoskeleton, phragmoplast. Note=Localized to the midline of the nascent phragmoplast (late anaphase) and remains associated with the expanding phragmoplast ring.
Sequence:
MKHFMMPRNAILRDIGESQSPNPSLTKSKSQRKIKSSKENAPPPDLNSLIPDHRSSPAKLKSPLPPRPPSSNPLKRKLIAEATADNGVAIGVSDSGVKVIVRMKPPSKGEEEEMIVKKISNDALTINEQTFTFDSIADPESTQDEIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPANGLLEEHLSGDQRGLTPRVFELLFARLSEEQAKHAERQLKYQCRCSFLEIYNEQITDLLDPSLKNLMIREDVKSGVYVENLTEEYVKNLKDLSKLLVKGLANRRTGATSVNAESSRSHCVFTCVVESHCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAVSPSQSCRSETFSTLRFAQRAKAIQNKAIVNEVMQDDVNFLREVIRQLRDELQRVKDDKGNNPTNPNAAYTTSWNARRSLSLLRSFGLGHPKSLPNGDDDGDTEMEIDEEAVERLCAQMGLSPPAEDNNQEMSRVEKINSSLQTVVLKDESYNNSHLKSSEATDVNMEDACCQTENNGSETDNALTVAETMDDGSSVQPDSITNSLHSCISDTNQGNSPSKAENIPSCQDLVIEADVSAIVSVADTSNNTEQVSVNPVSPCLSVAPVSVSPVLIPPTESASPKIRNSRKSLRTTSMSTASQKDIERANQLTPEVVEPSPAMSTEVLNLYSALSTKKSEAFPVPTRQLAASLHRGMKLLDSYRQSTALRRSTFRLSYKALECKPSTVLSKADVGVQTYPQADEIAEDNSKEVLCSRCKCRAECDAQEISDTSNLQLVPIDNSEGSEKSNFQVPKAVEKVLAGSIRREMAMEEFCTKQASEISQLNRLVQQYKHERECNAIIGQTREDKIVRLESLMDGVLSKDDFLDEEFASLMHEHKLLKDMYENHPEVLQTRIELKRVQEELESFKNFYGDMGEREVLLEEIHDLKAQLQCYTDSSLTSARRRGSLLKLTYACDPNQAPQLNTIPESVDEGPEKTLEQERLRWTEAESNWISLAEELRTELDTNRLLMEKQKRELDTEKRCAEELTEAMQMAMQGHARMIEQYADLEEKHIQLLARHRRIREGIDDVKKAAARAGVKGAESRFINALAAEISALKVQREKEVRYFRDENKSLQSQLRDTAEAVQAAGELLVRFKEAEEGLTFAQKRAMDAEYEASEAYKKVDKLKRKYETEISTVNQQHNAEPQNPIESLQASCNDDAMAKYDEPSASDGDNQWREEFQPFYKKDEELSKLAEPSWFSGYDRCNI
The following text describes a protein:
Function:
In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity.
Sequence:
MSRLVLIDGSSYLYRAFHALPPLTNAQGEPTGALFGVVNMLRATLKERPAYVAFVVDAPGKTFRDDLYADYKANRPSMPDDLRAQVQPMCDIVHALGIDILRIDGVEADDVIGTLALQGASDGLAVTISTGDKDFAQLVRPGVELVNTMSGSRMDSDEAVIAKFGVRPNQIVDLLALMGDTVDNVPGVEKCGPKTAAKWLAEYDSLDGVIANADKIKGKIGENLRAALPRLPLNRELVTIKTDVVLASGPRALDLREPNAEALAVLYARYGFTQALRELGGAAAEAGGLTAPMAVARTEPGRARGTGFVSAPAAAPVELDPALSAPGQYETILTQAQLDSWIARLRAAGQFAFDTETDSLDALQANLIGLSVAAEPGQAAYLPFGHDFPGAPAQLDRTQALAQLAPLLTDPAVRKLGQHGKYDLHVMRRHGIALAGYADDTLLESFVLNSGSARHDMDSLAKRYLGYDTVKYEDICGKGAKQIKFAQVSLEDATRYAAEDADITLRLHQVLGKRLAAEPALESVYRDIEMPLVGVLERIEANGVCVDAAELRRQSADLSKRMLAAQQKATELAGRTFNLDSPKQLQALLFDELKLPAVVKTPKGQPSTNEEALEAIADQHELPRVILDYRSLAKLRSTYTDKLPEMIHPQSGRVHTSYHQAGAATGRLSSSDPNLQNIPIRTEDGRRIRRAFVAPAGRKLIACDYSQIELRIMAHLSGDPGLVGAFESGADVHRATAAEVFGRTIDTVSGDERRAAKAINFGLMYGMSAFGLARQLGIGRGEAQDYIALYFSRYPGVRDFMETTRQQARDKGYVETVFGRRLYLDFINAGSQGQRAGAERAAINAPMQGTAADIIKRAMVSVDGWIADHAQRALMILQVHDELVFEADADFVDTLLAEVTARMSAAASLRVPLVVDSGVGDNWDEAH
The following text describes a protein:
Function:
May be involved in sterol transfer between intracellular membranes.
Miscellaneous:
MISCELLANEOUS: Present with 432 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Note=Localizes to puncta in the cell periphery representing cortical endoplasmic reticulum (cER)-plasma membrane (PM) membrane contact sites.
Domain:
The VASt domain bind sterols.
Sequence:
MSVHGRDPKKRQLRLISVAFKEASIDSPSFRASVNFFQTRVDALEDWIEKTVDFFDQKYKVSFEDFRRAKETLLSQLLPPPALLSNGFVSNQSFTPRLIDSFNKDYYDFSMKLLQIVKGDDSSHSTALLELMTTAIEPYRNVRKNFDFYQGKYDSMLASYQAIRISKTSLEPSSIKSDALQLFEVQKNYLKASLDLISAISAVKLSLDKFILESMKVLKSRSIFITKDSGRKIDLSPCINEYLDNYAIWVENSIEGSKVLDSDISNAKKQAYRYTLKRITPSSDTSDYNIRSIHSSKLLSKDTQVPPKSPEKSGWLYMKTQVGKPTREIWVRRWCFLKNAVFGMFLLSPSKTYVEETDKFGVFLTNVRYDPEEDRKFCFEVKIFGNKVTEAHDNMSKDITLVFQTSNYLDLKSWLIAFEATKKYVMSIQHDSLEYELAFKRFSPKFFEFASSTTTSIDQLITTFDKETESLYETLNCSISEYDILTLGEEKVFQFQMPTTPISTKMTQLAILSNFLTKGSWFPNAVLANIWGTTDWSEYTILPGKGKKPSSLLTIDGKRLPIRNSTIYPQYYSNELKVLDLQFKSLVFSPDQRLEKLPEELLLFKFEALWCPNKKQKFSATCFCTKDYIYCYMNSMEFICLTKISLSEIVSVEADRSSKKTLKLYDASGLQMKAIVLFSDYKLIASKLQYLLENKAIKNPNSNEEILVKFEQMEKESQEKKQEELYKIEQENSFDRKATSVSKIIKSRVTFWEMSDDASTLLNRLKKLQTEYSITYNHEYEISSKGLAHILFGDKSNAFPKCLFLARKDGEEHGKRFWYKNKDINGKSQLVRKIPFRLDMTGNFLNTGKYHRDKESKMIFATQRIVKIVDNKYYEVDLDPFFVKVPFCHLLKLSIKFVITESYDVDNHLEIKLNMTASSSSLHVLYKLEYIDSRTGKTIEKLSLAEIICQTWALKFAHSEFLLIRRVLRYYLEKIGKHGKVIKAIKLCGILGVLSNKSEEPATEKNGNSKESESMQYDIRYSCTILFLVFIKLMVYRVTNLTFVFFRILIGILLLCAEKFSRINRMMVVGLLASIMINILLSEKASVPYWSIKRAEKLFHDRLGSDKFTMQRAIYISDSDLLSSQLSVPSNNPIFEKFSEDNFNKDYQYSETRKQLAMRRNELLIELRILQDMEKQLVHDDYEKFLLEEVNKCSMVSIEMTDLWFNDTQLQNYCSICNEELEKLRPPIT
The following text describes a protein:
Function:
Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX.
Sequence:
MKDRETLVYWMTYSMRSNNYYWASSALYLLGTLDQLNKDDAIDFLMKCKCANGAFGGNIGSEPNIHNTLSVIQTLILYDRFDLIDQEPIVKWIQSLQKSDGSFTNGQWNEVDTKFTFCALAILKLFNKLDAINLDSAVNWLISCQNSDGGFGCFPHCESHCGQVFTSLAALSIANALEKVDCTALRLFLTERQTKDGGFNGRPEKESDVCYSWWAGAPLSILGEKDSINAEFLKDFILSAQDPDTGGIADRPGNHADPYHTFFGCAGLSLFGFFDLPKIDPVLALPVEVLKRHFRSLGAEYNK
The following text describes a protein:
Function:
An ATPase. Part of the ESX-1 specialized secretion system, which delivers several virulence factors to host cells during infection, including the key virulence factors EsxA (ESAT-6) and EsxB (CFP-10).
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein. Note=Resides at or near the cell wall, the protein is susceptible to extracellular proteases.
Domain:
Has a discontinuous central core of beta sheets stabilized by a disulfide bond that is flanked by 2 structural domain repeats on each side; the protein forms an elongated 'S'-shaped structure. Repeat A2 (approximately residues 265-323) is farthest from the cell inner membrane and is quite mobile, swinging on 2 inter-repeat loops (A, residues 234-264 and B, 324-341).
Sequence:
MGLRLTTKVQVSGWRFLLRRLEHAIVRRDTRMFDDPLQFYSRSIALGIVVAVLILAGAALLAYFKPQGKLGGTSLFTDRATNQLYVLLSGQLHPVYNLTSARLVLGNPANPATVKSSELSKLPMGQTVGIPGAPYATPVSAGSTSIWTLCDTVARADSTSPVVQTAVIAMPLEIDASIDPLQSHEAVLVSYQGETWIVTTKGRHAIDLTDRALTSSMGIPVTARPTPISEGMFNALPDMGPWQLPPIPAAGAPNSLGLPDDLVIGSVFQIHTDKGPQYYVVLPDGIAQVNATTAAALRATQAHGLVAPPAMVPSLVVRIAERVYPSPLPDEPLKIVSRPQDPALCWSWQRSAGDQSPQSTVLSGRHLPISPSAMNMGIKQIHGTATVYLDGGKFVALQSPDPRYTESMYYIDPQGVRYGVPNAETAKSLGLSSPQNAPWEIVRLLVDGPVLSKDAALLEHDTLPADPSPRKVPAGASGAP
The following text describes a protein:
Function:
Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MAKAGGITNAVNVGIAVQADWENREFISHISLNVRRLFEFLVQFESTTKSKLASLNEKLDLLERRLEMLEVQVSTATANPSLFAT
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Regulates ubiquitination of cdc25.
Miscellaneous:
MISCELLANEOUS: A cysteine residue is required for ubiquitin-thioester formation.
Subcellular Localization:
Membrane; Peripheral membrane protein. Cytoplasm.
Sequence:
MSNSAQSRRIRVTIVAADGLYKRDVFRFPDPFAVLTVDGEQTHTTTAIKKTLNPYWNETFEVNVTDNSTIAIQVFDQKKFKKKGQGFLGVINLRVGDVLDLAIGGDEMLTRDLKKSNENTVVHGKIIINLSTTAQSTLQVPSSAASGARTQRTSITNDPQSSQSSSVSRNPASSRAGSPTRDNAPAASPASSEPRTFSSFEDQYGRLPPGWERRTDNLGRTYYVDHNTRSTTWIRPNLSSVAGAAAAELHSSASSANVTEGVQPSSSNAARRTEASVLTSNATTAGSGELPPGWEQRYTPEGRPYFVDHNTRTTTWVDPRRQQYIRSYGGPNNATIQQQPVSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQNVPQYKRDFRRKLIYFLSQPALHPLPGQCHIKVRRNHIFEDSYAEIMRQSATDLKKRLMIKFDGEDGLDYGGLSREYFFLLSHEMFNPFYCLFEYSSVDNYTLQINPHSGINPEHLNYFKFIGRVIGLAIFHRRFVDAFFVVSFYKMILQKKVTLQDMESMDAEYYRSLVWILDNDITGVLDLTFSVEDNCFGEVVTIDLKPNGRNIEVTEENKREYVDLVTVWRIQKRIEEQFNAFHEGFSELIPQELINVFDERELELLIGGISEIDMEDWKKHTDYRSYSENDQIIKWFWELMDEWSNEKKSRLLQFTTGTSRIPVNGFKDLQGSDGPRKFTIEKAGEPNKLPKAHTCFNRLDLPPYTSKKDLDHKLSIAVEETIGFGQE
The following text describes a protein:
Function:
Acts as a molecular chaperone for G protein-coupled receptors, regulating their biogenesis and exit from the ER.
Subcellular Localization:
Endoplasmic reticulum membrane.
Sequence:
MAQNTTLDYPVHYHVFNGNANEMVKSLQKGHDINRKDKHGNTPLHLAVMLGHKDCIKLLLQRKPSLKAKNNYGWTPLDEAISYGDRLTVTQLLLTMKTISKQDLKAKRPRVIAALKSLGDFYMELKWEFTSWIPFLSRLLPSDICKIRKRDACIRVDSTLADFSEMKWQRGDVSLIFNGNNDAHPLPIVLDNDKKTFQKMRFKDDDAEVDEEVDLLMSNNIVSGQTTSEQVTFTKVQSGWIFRENKIETIGNFKADVFSVNGLQLIQRKRREHLSEEDKKKNKVRMRLLHLHNFILHRMSLEPPAKCKMTWQEYLESRDMPQLARLVDVKETRKAFKPQVAMSQEFPLDVNVLVDILTILSPMKQFTKLKEFIQMKLPPGFPVKLELSILPTITAKVSFQEYSSSDDIPVSIFFIPRDYKVILDILHMACVAIL
The following text describes a protein:
Function:
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (Probable). Required for the accumulation of both the NDH subcomplex A and NDHS.
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Single-pass membrane protein.
Sequence:
MAYATSTYARTSCIILPKIQNGAHFTDDTKAFRRITARRVTRIYASQGPTKPSKPSPGVDTRIHWESPDEGWIGGRSDPAKSVDEDKTNLLSDEKFAELIKDSFDSHYQFLGVSTDADLEEIKSAYRRLSKEYHPDTTSLPLKTASEKFMKLREVYNVLSDEETRRFYDWTLAQEVASRQAEKMRMKLEDPKEQDFRGYESIPDMVDRLGGRNMELSDQAMTALTFDILIVLFAVCCIAFVIVFKDPSY
The following text describes a protein:
Function:
Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MKKIIKKNNNYDNNKVKKTQTTKTGELSYEEIQKINSELSDRNKNDKLIASKEKCDVIGKSFGFIEPSIRKDIVDENIDKPFVLLSYGGTSKEIKRERKERLRLEKLKTKKLGSKKKRELSFFSISSENCIYDQYLPLHQLWTQYIQDVMQQQKGPALVNKILKADLHGAIVIVTKSKCPTFVGQKGIIVQETENTFKIITKENKLNIIPKEQCQFYLECCNQVVTIFGKHFCFRACDRANKKFKPRKNIEL
The following text describes a protein:
Function:
Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (By similarity). Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen (By similarity). This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis (By similarity). May directly bind to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis (By similarity). May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation (By similarity). May play a role in the regulation of cell morphology and cytoskeletal organization (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Enriched at sites of lipid droplet (LD) biogenesis.
Sequence:
MTEKTASHYWNEETSILKLRRKDILLFEIYATTLLLGSIYSIYVDKWSITSYFGNSKNLINLIFVKRGWFWTSLVYFYHAWDQKRNKIDFKFISRYIVATLWWMFVTQWFIGPGLIDRTFALSGGSCKNFDGDSSVFIPLTASTCKGLNGSWSGGHDLSGHVFLLTHSSLFMLSENFSFILNNGIKATSTKVLFGLLGLWWWMLFVTASFYHTTFEKCTGFFSGILEWSIVYVFSSRMPAVADLLGSSDY