lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Subcellular Localization:
Cytoplasm.
Sequence:
MPGGRATAAQPRTKRPLAWSPNRRRMHLSSARALLAEAERANERRMLVLAGDRAAGVRTADTLLDDLPIPLSETTLVATQDALACEHVPTRNADRLLGTTQRAVVIDLHEDCRPNALGRVVGAVDGGGLLVVLAPPLAEWPTRDGAFAAGLAVPPFDAADVTGRFRRRLADTMRAHPGIAIYDVDTDTLSDDGRTRPAPRLPDPDPDPQPTADVPAAAIDACVTPDQAAALASFAALRDPGHAVVADADRGRGKSSVAGLAAACLAAEGHDVLVTAPRRRNTTELFARAGALLADLGALASDGDTVETAAGGRIRFSKPPAAADLPGDPDAVFADEAAAIPVRLLESLLDCQRLAFTTTVHGYEGAGRGFDVRFRDRLADATQTVHETSLTDPIRYAGTDPIEPWAFRALLLGARPAVEPLVADATPDTAAYVALSGADLAADEHLLREAFGLLVSAHYRTEPNDLARLLDAPNLTMRALVADGHVASVALLAREGGLADDRRAAMYDGQRVKGNMIPDVLTSQLRDEAAATTVGYRVLRIATHPAVRSRGLGSRLLGELRAEFNGHADWLGVGYGATPALLSFWAANGYSTVHLSTTRNDTSGEYSAIMLDALSDAGRALHDRHAGWFADRIGGVLSDALRDLDADVARGALRACATTPSLALSERDWRTVAGAAHGPGMYSVDPRPFRRLAVHHLVAGDADLLSPDEQRLLVGALLQARPWDGLADDLGYHSASQAMRALGDALQALVAAHGTAAARAEVARFTED
The following text describes a protein:
Function:
Toxic component of a type IV toxin-antitoxin (TA) system. Acts as a toxin inhibitor that blocks cell division and cell elongation via FtsZ and possibly also MreB (although no interaction with MreB has been proven). Overexpression results in inhibition of growth in liquid cultures and a decrease in colony formation. These effects are overcome by concomitant expression of cognate antitoxin YafW, which leads to toxin loss by an unknown mechanism. Overexpression leads to formation of lemon-shaped cells and cell lysis; inactivated by overexpression of cognate antitoxin YafW but not when the 2 genes are coexpressed from the same plasmid. Also neutralized by overexpression of non-cognate antitoxins YfjZ and CbeA. Co-overexpression of toxin YkfI and antitoxin YafW leads to formation of elongated cells.
Miscellaneous:
MISCELLANEOUS: Encoded in prophage CP4-6.
Sequence:
MKTLPAITQRAVKPCLSPVAVWQMLLTRLLEQHYGLTINDTPFCNEAVIKEHIDAGITLADAVNFLVEKYELVRIDRKGFSWQEQSPYLRAADILRARQATGLLRQSRNNVVR
The following text describes a protein:
Function:
Phospholipase involved in maintaining the lipid droplet morphology. Has phospholipase activity with broad substrate specificity, acting on glycerophospholipids phosphatidylethanolamine (PE), phosphatidic acid (PA), phosphatidycholine (PC) and phosphatidylserine (PS), primarily at sn-2 position. It can later remove fatty acids from the sn-1 position of the produced lysophospholipids such as lysophosphatidylethanolamine (LPE). Also shows activity toward phosphatidylglycerol, but, in contrast to what was observed with the other phospholipids tested, prefers the sn-1 position.
Miscellaneous:
MISCELLANEOUS: Present with 1210 molecules/cell in log phase SD medium.
Subcellular Localization:
Lipid droplet. Membrane; Single-pass membrane protein.
Sequence:
MTSDKHLFVLIHGLWGNYTHMESMRTILSTTLKKEDVNDDMIYFLPKQNAMFKTFDGIEIIGYRTLIEVCEFIRDYKDGKITKLSVMGYSQGGLVARFMIGKMLTEFKELFEDIEPQLFITMATPHLGVEFYNPTGIAYKSALYSALRTLGSTILGKSGREMFIANSSNNILVKLSQGEYLEALSLFKWRIAFANVKNDRTVAFYTAFITDCDPFIDFDNKLKYTFEEKIPGSGYKGILPKIVDLNALNVNSHAPTKPTKTYKKWGRTILIILVATFLILPIALVMNGLGTAYSYIVTCKYRKMLSNGILHNEVRGKLGLTEQLKGYVTDAYGSIINSALDMDANYEASNSNLVNEEELPWKEFIQKYTTINDGVWKSKFKKLPFDENRKVILRNLNKLKWIRVPIYIKAVNAHGVIVARRGMDENTAATGIACIEFTAQLLAYLMHKSN
The following text describes a protein:
Function:
Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism. Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway. The interaction with the membrane-bound IL6R and IL6ST stimulates 'classic signaling', whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells; IL6 is a potent inducer of the acute phase response. Rapid production of IL6 contributes to host defense during infection and tissue injury, but excessive IL6 synthesis is involved in disease pathology. In the innate immune response, is synthesized by myeloid cells, such as macrophages and dendritic cells, upon recognition of pathogens through toll-like receptors (TLRs) at the site of infection or tissue injury. In the adaptive immune response, is required for the differentiation of B-cells into immunoglolin-secreting cells. Plays a major role in the differentiation of CD4(+) T cell subsets. Essential factor for the development of T follicular helper (Tfh) cells that are required for the induction of germinal-center formation. Together with IL21, controls the early generation of Tfh cells and are critical for an effective antibody response to acute viral infection. Required to drive naive CD4(+) T cells to the Th17 lineage, through 'cluster signaling' by dendritic cells. Also required for proliferation of myeloma cells and the survival of plasmablast cells; Acts as an essential factor in bone homeostasis and on vessels directly or indirectly by induction of VEGF, resulting in increased angiogenesis activity and vascular permeability. Induces, through 'trans-signaling' and synergistically with IL1B and TNF, the production of VEGF. Involved in metabolic controls, is discharged into the bloodstream after muscle contraction increasing lipolysis and improving insulin resistance. 'Trans-signaling' in central nervous system regulates energy and glucose homeostasis. Mediates, through GLP-1, crosstalk between insulin-sensitive tissues, intestinal L cells and pancreatic islets to adapt to changes in insulin demand (By similarity). Also acts as a myokine (By similarity). Plays a protective role during liver injury, being required for maintenance of tissue regeneration. Also has a pivotal role in iron metabolism by regulating HAMP/hepcidin expression upon inflammation or bacterial infection. Through activation of IL6ST-YAP-NOTCH pathway, induces inflammation-induced epithelial regeneration (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MKFLSARDFQPVAFLGLMLLTATAFPTSQVRRGDFTEDTTHNRPVYTTSQVGGLITYVLREILEMRKELCNGNSDCMNSDDALSENNLKLPEIQRNDGCFQTGYNQEICLLKICSGLLEFRFYLEFVKNNLQDNKKDKARVIQSNTETLVHIFKQEIKDSYKIVLPTPTSNALLMEKLESQKEWLRTKTIQLILKALEEFLKVTMRSTRQT
The following text describes a protein:
Function:
Involved in the formation of secondary alcohols and ketones in stem cuticular wax. Catalyzes the hydroxylation of a methylene unit in the middle of alkane molecules to form secondary alcohols and possibly also a second hydroxylation leading to the corresponding ketones.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MAMLGFYVTFIFFLVCLFTYFFLQKKPQGQPILKNWPFLRMLPGMLHQIPRIYDWTVEVLEATNLTFYFKGPWLSGTDMLFTADPRNIHHILSSNFGNYPKGPEFKKIFDVLGEGILTVDFELWEEMRKSNHALFHNQDFIELSVSSNKSKLKEGLVPFLDNAAQKNIIIELQDVFQRFMFDTSSILMTGYDPMSLSIEMLEVEFGEAADIGEEAIYYRHFKPVILWRLQNWIGIGLERKMRTALATVNRMFAKIISSRRKEEISRAKTEPYSKDALTYYMNVDTSKYKLLKPNKDKFIRDVIFSLVLAGRDTTSSVLTWFFWLLSKHPQVMAKLRHEINTKFDNEDLEKLVYLHAALSESMRLYPPLPFNHKSPAKPDVLPSGHKVDANSKIVICIYALGRMRSVWGEDALDFKPERWISDNGGLRHEPSYKFMAFNSGPRTCLGKNLALLQMKMVALEIIRNYDFKVIEGHKVEPIPSILLRMKHGLKVTVTKKI
The following text describes a protein:
Function:
The THO complex is required for cell proliferation and for proper export of heat-shock mRNAs under heat stress.
Subcellular Localization:
Cytoplasm. Nucleus. Nucleus speckle.
Sequence:
MSEQCQLRPHSDTLVRKLVEMNDEEIIKQRLLIDGDGTGEDRRIVVLLKQFLKWASDSLDSNPIMYDRLMAQFAQCKLTALKNVQTLQMIAGERDNYTQLVEHHEESIVLAKAEIESSKKELITAKQIRKNKMEYDLLASLIQDQPDRSETQRHIETIRREIDDLVQKKLKMERKFQKRRNDFTLLMYTIHELEQQLDQDSSSSASSSSSDCDARSEPDLDDNGIMEVSDEDDDLNNSTPTKFDGARGEPKYHSVSTEDSKAMSVEEDTVLELSIDKDEHDVDVAVAN
The following text describes a protein:
Function:
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Sequence:
MRILFLGSPSFAVHALEALVAAGHEIVGVVTQPDRPAGRDRRLTPPPVKIAAMAHNLPVLQPETLRDPTVVETLSALQPEVGVVAAYGEILRRAVLSIPPLGYLNIHPSLLPLYRGPTPVAGAILAGETVTGVTIMLLDPSMDSGPILAQAVVDLPPTARAGQLTDELFRIGADLLVQVLPRYARGEIEPRPQDHSRATVTKMLKKEDGRIDWSLPAIVIERMTRAYDPWPGAYTFWRGQPLRIIKAAVASADGTNVPGTVIGRSGSGHPLVQTGSDALELIEVQPASRRPMSGSAWLAGVHADNIRLGE
The following text describes a protein:
Function:
Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to the unmature virions, thereby facilitating subsequent uncoating. Without maturation, the particle lacks infectivity and is unable to uncoat. Late in adenovirus infection, in the cytoplasm, may participate in the cytoskeleton destruction. Cleaves host cell cytoskeletal keratins K7 and K18.
Miscellaneous:
MISCELLANEOUS: All late proteins expressed from the major late promoter are produced by alternative splicing and alternative polyadenylation of the same gene giving rise to non-overlapping ORFs. A leader sequence is present in the N-terminus of all these mRNAs and is recognized by the viral shutoff protein to provide expression although conventional translation via ribosome scanning from the cap has been shut off in the host cell.
Subcellular Localization:
Virion. Host nucleus. Note=Present in about 10 copies per virion.
Sequence:
MGSSEQELKAIVKDLGCGPYFLGTYDKRFPGFVSPHKLACAIVNTAGRETGGVHWMAFAWNPRSKTCYLFEPFGFSDQRLKQVYQFEYESLLRRSAIASSPDRCITLEKSTQSVQGPNSAACGLFCCMFLHAFANWPQTPMDHNPTMNLITGVPNSMLNSPQVQPTLRRNQEQLYSFLERHSPYFRSHSAQIRSATSFCHLKNM
The following text describes a protein:
Function:
Promotes CCP110 ubiquitination and proteasome-dependent degradation. By counteracting accumulation of CP110, maintains normal centriolar homeostasis and preventing formation of ectopic microtubular organizing centers.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole.
Sequence:
MAAGSGGSGGSGGGPGPGPGGGGGPGGSGSGPGSAGELHPRTGRLVSLSACGRTARRQQPGQEFNHGLVLSREPLRDGRVFTVRIDRKVNSWSGSIEIGVTALDPSVLDFPSSATGLKGGSWVVSGCSVLRDGRSVLEEYGQDLDQLGEGDRVGVERTVAGELRLWVNGRDCGVAATGLPARVWAVVDLYGKCTQITVLPPEPGFSPPTPIPTPPLEPSAPQDSALAEQGTSGDEAFMVSPAQARPETFPNSLESHNDFANMELSEVVSNAILSAYNGGLLNVNLSSPPAGEAPGPSGAATSPILTSNDALLFHEKCGTLIKLSNNNKTAERRRPLDEFNNGVVMTNRPLRDNEMFEIRIDKLVDKWSGSIEIGVTTHNPNNLEYPATMTNLQSGTIMMSGCGILTNGKGTRREYCEFSLDELQEGDHIGLTRKSNSALHFFINGIDQGVATPLTPPVVYGVVDLYGMAVKVTIVHNNNHSDRLRRNNAILRALSPEGALRRAAPAAQAEPERLLFHPNCGQKAAITHEGRTALRPHATDDFNHGVVLSSRALRDGEVFQVRIDKMVDKWAGSIEIGVTTHNPAYLQLPSTMTNLRSGTWMMTGNGVMHNGTTILDEYGHNLDRLKAGDTVGVVRREDGTLHFFVNGMTQGPAAWNVPPGVYAVVDLYGQAAQATIVDDVEVPPVPEPLPEGNNQASPSSPSSGAGGSDLRFHQLHGSNAVITNGGRTALRHNCRSEFNDAIVISNRALRDGELFEIVIQKMVDRWSGSIEAGVTAIRPEDLEFPNTMTDIDYDTWMLSGTAIMQDGNTMRNNYGCDLDALGTGARIGMMRTAKGDLHYFINGQDQGAACSGLPPGKEVYAVVDLYGQCVQVSITNATGPMDNSLATSNSATEKSFPLHSPVAGVAHRFHSTCGKNITLEEDGTRAVRAAGYAHGLVFSTKELKTEEVFEVKVEELDEKWAGSLRLGLTTLVPGDMGPGAGGGPGLPPSLPELRTKTTWMVSSCEVRRDGQLQRMNYGRNLERLGVGSRVGLRRGADDTMHILVDGEDMGPAATGIAKNVWAVLDLYGPVRSVSIVSSTRLDEPEGTQPPSPSSDTGSEGEEEDEGEEHGPEGQEQVAVMPTALEFLENHGKNILLSNGNRTATRVASYNQGIVVVNQPLVPQLLVQVRIDFLNRQWTSSLVLGVITCPPERLNFPASACALKRAAWLLRGRGVFHNGLKICEKFGPNLDTCPEGTILGLRLDGSGGLHLHINGLDQGVAVPDVPQPCHALVDLYGQCEQVTIVSPEPGAASGKSTGTQGDMEKADMVDGIKESVCWGPPPTASPLKSCEYHALCSRFQELLLLPEDYFLPPPKRSLCYCESCRKLRGDEAHRRRGEPPREYALPFGWCRFNLRVNPRLEAGTLTKKWHMAYHGSNVAAVRRVLDRGELGAGTASILSCRPLKGEPGGGFEEPGENCAPPREEQPPPVLLSPSLQYAGAETLASKVQFRDPKSQRTHQAQVAFQVCVRPGSYTPGPPSAALREPPDPHFSPAELEWVTKEKGATLLYALLVRVE
The following text describes a protein:
Function:
Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain.
Subcellular Localization:
Apical cell membrane; Multi-pass membrane protein.
Sequence:
MRHAGTPVHLVVFLTCIILQHVCRTVGAGVEVPLCDGWYNNAAHPDYGSTGMPLSRDLPPAYSDDAYRPSGTDRPNPRLVSRALVKHLSNTAKDSGRTVLCVFFGQHVVDDISDVRGIACPTEYSNIALQPGDPLYNSAESDRTTKIMPFQRAVYKSGTGTSANNPRQQVNAATSWLDGSAIYGVSEAWQDRLRAFTNGSLRTSHGGKLPDMNVMGLPMQNLPSPKNQKIHKPNNLYALGNVRGNENPFLLAVSAVWTRWHNHWAHRLHTDHPEWTDDQVFQQAKRWVVATYQNIVLYEWLPAFINDTVEEYSGYNRFVDPAPSNVFTAAAMRYGHSMVPSAVFKRNSSGHAMPIRTCNTYWSAEDVIQTDEDVDGLLSGMAGQIADGGRSIVSEDLQGFLYGPLTFSRRDLVAMDIQRGRDHGLPDYNTACRQYGLAPLHNWTDIKVMNQKISDEMVSELSDLYGSVDKLDVWVGGMLAGAGAGRPGMLYKTIMKQQFLRLRDADRFWFENTQTSGFTEDELNTIRGINFKDILSRVTDVPSAQLQDDVFVWKNDGNGSPLEVDPSDLEPCTGQTTFSYFDNVDWVTFGVTVIVLCLFPLGCVFVIMVAAWRNELRTERRLQTPKKKLDLPSNAYQATEWQGRRLPTRQVVVTLQSPSLIEVRDTRDAVFRLVNIAKIARGIITVSRDRGCKFLSIHIPREYDLVLKFSSHHERETFLADLKQFLTAQQVPVELQEVELGQLQKQAVTIEDRQKTLEDFFCSVFLQALSSSRAVDDWVVQPEKWKAKSALDCELTKVEFAEAMSLRPDSQFVVQMFNLVDKDKNGYISFREFLDLVVIFSKGTMEDKLRVMFDMYDQTGNGYLSRKELTNMLGSLMELVSNNTTGRIEDLVESMFAEAGMEGEQDMSFDKFVSMMQDHKEELNQARLNIAGSDWTTLRPTRTSVPKESGRRRSSSMLPKGPWRLRRASAPVVSSGDVVSATRRKTSPKLEPIPSVPCAANTTDSDNVFTSDAVTAPNGKRRSTGRSSSDIKVQLLRETYPASAYQRKMQAFKRWVENKRLQLLYLIFYFAITFALFVERAYHYAVEAEDFGIRQLTQYGIIASRGAAASMSFSFSLLLLTMCRNSLTKLRETFLNRYIPFDYAVDFHKIVAITALVFTIIHTLGHLVNVYHFAVHPLNHLVCLFPSLRTLDNGSDQPPKWYWWAFQTMAGVTGVLLLLVVSIIYVFATGYARRRAFSAFWATHQLYIVMFILTVLHGSGRLIQNPSFHLYLIGPAIIFTLDKLVSISHRRQLVDIVKTELLPSDVTNIQFKRPDDFEYKSGQWVRIACPEQGPNEYHPMTLTSAPHENTLSVHVRAVGPWTAQLRRTYDPEDFSNGTQKLFLDGPFGEGHQDWYKYKIAVLVGGGIGITPFASILKDVAYLSSTGANMNCKKVYFLWVTRTQRHFEWFIDIIREVEEQDRRGLVAVHIFITQFFEKFDVRTTMLYIYERHFQRLSGRSLFTGLRATTHFGRPEFVSLLDSIQHQNPEVKKIGVFSCGPPGMTRNVEDACAQLNKKDLAHYVSYYENF
The following text describes a protein:
Function:
Key enzyme involved in DNA replication and DNA repair. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA.
Subcellular Localization:
Nucleus. Mitochondrion.
Sequence:
METAELELLMEEAFTEETPSRQQFQKRAAVSYPDLVLSQGVNNRYRVVAVNVIETDSGTTEKHLTITASHSQSLENKELCILRNDWDSLSIEPGDIIHLEGECTSNTWVINGDSGYLILYPDLLLSGTSIASSIRCMRRAVLSENFKSSDSGSHQMLIGTLLHEIFQRAITDSFAQEKLQEFVVQTIQEPKHLKEMYRLNMDQDKIKEEIEDYLPSFSKWAENFMNKSFPANLPNIQLSLPSPGNKNGSDCSIEVTESLDIEENIWSPRFGLKGKIDVTVGVKIHRRCKVDYKIMPLELKTGKESNSIEHRSQVILYTLLSQERRENPEAGFLLYLRTGNMYPVLANHLDKRELLKLRNQLAFHLFHSVNKSAIGKEPTQLALLPPVISDNQTCKYCSQLHNCALYSRAVEQQVDKNFVPVTMLPKIEKEMQHLKLSHLQYFSLWYLMLTLESQAKDGRKGRRNIWLLPSSEREKTGDCIGNIIRTEHVETVCEGQHLHRFQRKNGTLPKTNLMVGDKVVVSGEEKALLALSSGFIKKIDLTTVTCILDRNLSKLPGNTLLRLDHDEGIGGIETPLGNLSKLMENSPASENLRDLIIDFREPQFIQYLSSVLPPEAKDTVATILKGLNKPQRQAMKHVLLSKDYTLIVGMPGTGKTTTICALVRILYACGFSVLLTSYTHSAVDNILLKLAKFKVGFLRLGRAQKVHPDIQKFTEEEICRSKSIKSLASLEELYNSQSVVATTCMGVSHPLFTRKQFDFCIVDEASQISQPVCLGPLFFSARFVLVGDHQQLPPLVLNSEARDLGMSESLFKRLEQNKNAVVQLTVQYRMNSKIMSLSNKLVYEGKLECGSEKVAKAIVTLPKFQDVKLNLELYADYSETLWLKGVFEPNNSVCFLNTEKVPAPEQAEKGGVSNIAEAKLIVFLTSVFLKAGCKSSDIGIIAPYRQQLKIITDLLMCSSDVMVEVNTVDKYQGRDKSIILVSFVRNNKDGTLGDLLKDWRRLNVAITRAKHKLILLGCVPSLNRYPPLEKLLSHLHSEKMIFDLPSGAHESVYHWNLE
The following text describes a protein:
Function:
Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSDEKTEKPTEKKLQDARRDGEVPISPDVTAAAVLLAALLVMKLAGSYFVEHLRALMSIGFDFTTNTRDATALHRALGRIGIQGVLLTLPFVTACLAAGLIGTFVQTGLNASLKPVTPKFDSLNPVNGVKKLFSLRSLINLLKLGIKAAVIGVVLWYGLRALMPTIIGLAYQPPADIAQIGWRALGILCALAVLVFVLVGAADWSVQHWLFIRDKRMSKDEQKREHKESEGDPEVKGKRKEFAKELVFGDPRERVAKAKVMVVNPTHYAVALAYEPDGFGLPQVVAKGVDEGALELRAYAHNQGIPIVANPPLARALHEVELGEAVPESLFETVAVVLRWVDELGRDNDEGSGPLPC
The following text describes a protein:
Function:
Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.
Sequence:
MKSSSERIGREFFKDDVVDVSQKLIGKLLCRKFSDETIKKFRINETEAYRGPDDLACHASKGKTERTKAFFLEGGHLYVYMCYGIHWLINIVTGNADEPQATLIRGIETAPGPGRVGSRLEISKDLYGIDLCTSDIMWLEDDGVKWDYISTPRIGIDYAGEPWISKPWRYYHETEESKKVAPKVGKPKKKKISQSKKQRLADDSYSD
The following text describes a protein:
Function:
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis. Sigma-K controls genes such as mpt70 and mpt83.
Miscellaneous:
MISCELLANEOUS: Extracytoplasmic function (ECF) sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning anti-sigma factor is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, Rip1), while cytoplasmic proteases finish degrading the regulatory protein, liberating SigK (Probable).
Domain:
The sigma-70 factor domain-2 mediates sequence-specific interaction with the -10 element in promoter DNA, and plays an important role in melting the double-stranded DNA and the formation of the transcription bubble. The sigma-70 factor domain-2 mediates interaction with the RNA polymerase subunits RpoB and RpoC (By similarity); The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-H) motif that mediates interaction with the -35 element in promoter DNA. The domain also mediates interaction with the RNA polymerase subunit RpoA. Interactions between sigma-70 factor domain-4 and anti-sigma factors prevents interaction of sigma factors with the RNA polymerase catalytic core (By similarity).
Sequence:
MTGPPRLSSDLDALLRRVAGHDQAAFAEFYDHTKSRVYGLVMRVLRDTGYSEETTQEIYLEVWRNASEFDSAKGSALAWLLTMAHRRAVDRVRCEQAGNQREVRYGAANVDPASDVVADLAIAGDERRRVTECLKALTDTQRQCIELAYYGGLTYVEVSRRLAANLSTIKSRMRDALRSLRNCLDVS
The following text describes a protein:
Function:
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. Within the complex, functions as a proteasomal ubiquitin receptor (Probable).
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
The Pru (pleckstrin-like receptor for ubiquitin) domain mediates interactions with rpn2 and ubiquitin.
Sequence:
MSLITFKAGKLRRVPGTKLLRADPEKGYIVMNRDAYGLIHFQWAKRNDLENPEDDIIVFSSECTFEKVTECTTGRAYMLKYPSSAHSLFYWMQEASDDNDTSYAERINSYIKDQDLLDPARSDVATVSDMMEVDTVEQSEPIAQPTESSKESSEIGAPNSDEINSSEAVRNLLATISAQAGFGGSTVDLCEILKPSNLTDLLCQEGVIDRLMPYMPPDTPNNLEGVLAIVSSPQYAQALRSFSQALNSPGGVNIISALGLSLDESANPNEGGALQFLKAIARFVSRNNGSE
The following text describes a protein:
Function:
Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity).
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Sequence:
MSFFHVVFVAFVIAAIGAAGWFVTPKGKNQTLLRTSLLLTLTCCYLMWAITYLCQLHPLITPRRSDLRMEY
The following text describes a protein:
Function:
VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MMWYLCRVNCSDGKGRQSNSFFGLTHNHWFVFVRFLNSLKFAFVVIALPYVGFVFAFCARVWNRSASLYTYFSEKKTSDIIVNKKTYTKMLGMRSYIVFVAVVTLQHICVNSKAHENNIVNGKEFEALCGFINFALDTQTPQDLVLKVEEAEDKILSDTFAAGGDAKVSKELQELKQKVETYKEQHSDLWSSSTPTIIQKSLTEALYGNGNKQVVVKHVQGNRSDVCGRAGGQTGKKAGETLALDLLCICAASDQDEDDVVTCCNGCNTTHVGVWEPQQNSPAHWNLLHPKCSNVKREKTRPLQVLSAALRFFVSTLNTTSNSSSGPRNLLGAHDGSVEHGCSGGILDGHGRCVIYLPRHVSGSAPTIPWYLKLQEAATKMEELIQAEEYLVKIQNQVNELKREARPVPNNSSEKEKDESNNTDDGLEGKKPTTSSKRGCSGFESKVTCLQQKPRCEWNGTECVTSIRRLLTSSGVSRLPAPLKLFFLVF
The following text describes a protein:
Function:
Displays phosphatase activity for serine/threonine residues, and dephosphorylates and activates Pk92B kinase. Has apparently no phosphoglycerate mutase activity (By similarity).
Subcellular Localization:
Mitochondrion outer membrane; Single-pass membrane protein.
Sequence:
MRKLTSFVCGTGAGLAVYYLQRLRDPQATVNNSWTNSEKPVDPWALWDTNWDCREPRALVRPLRNSQPEEENRYNAELEKAKAKKARHIILVRHGEYLDVGDSDDTHHLTERGRKQAEFTGKRLCELGIKWDKVVASTMVRAQETSDIILKQIDFEKEKVVNCAFLREGAPIPPQPPVGHWKPEASQFLRDGSRIEAAFRRYFYRAYPDQEKESYTLIVGHGNVIRYFVCRALQFPAEGWLRISINHASITWLTISPSGNVSIKYLGDSGFMPAELLTHRIPRDAKNVV
The following text describes a protein:
Function:
Deacetylates O-acetyl-ADP ribose to yield ADP-ribose and free acetate. Down-regulates ribonuclease 3 (RNase III) activity. Acts by interacting directly with the region of the ribonuclease that is required for dimerization/activation. Overexpression inhibits biofilm formation via an RNase III-independent pathway. This inhibition is RpoS-dependent. Overexpression also results in increased susceptibility to apramycin.
Sequence:
MKTRIHVVQGDITKLAVDVIVNAANPSLMGGGGVDGAIHRAAGPALLDACLKVRQQQGDCPTGHAVITLAGDLPAKAVVHTVGPVWRGGEQNEDQLLQDAYLNSLRLVAANSYTSVAFPAISTGVYGYPRAAAAEIAVKTVSEFITRHALPEQVYFVCYDEENAHLYERLLTQQGDE
The following text describes a protein:
Function:
Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Involved in various processes, such as mitosis and cytokinesis, via its role in the regulation of actin polymerization. Together with CDC42, involved in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. In addition to its role in the cytoplasm, also plays a role in the nucleus by regulating gene transcription, probably by promoting nuclear actin polymerization (By similarity). Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. Plays a role in dendrite spine morphogenesis (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton. Nucleus. Cytoplasm. Note=Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated (By similarity). Exported from the nucleus by an nuclear export signal (NES)-dependent mechanism to the cytoplasm (By similarity).
Sequence:
MSSGQQPPRRVTNVGSLLLTPQENESLFSFLGKKCVTMSSAVVQLYAADRNCMWSKKCSGVACLVKDNPQRSYFLRIFDIKDGKLLWEQELYNNFVYNSPRGYFHTFAGDTCQVALNFANEEEAKKFRKAVTDLLGRRQRKSEKRRDAPNGPNLPMATVDIKNPEITTNRFYSSQVNNISHTKEKKKGKAKKKRLTKADIGTPSNFQHIGHVGWDPNTGFDLNNLDPELKNLFDMCGISEAQLKDRETSKVIYDFIEKTGGVEAVKNELRRQAPPPPPPSRGGPPPPPPPPHSSGPPPPPARGRGAPPPPPSRAPTAAPPPPPPSRPGVVVPPPPPNRMYPPPPPALPSSAPSGPPPPPPLSMAGSTAPPPPPPPPPPPGPPPPPGLPSDGDHQVPASSGNKAALLDQIREGAQLKKVEQNSRPVSCSGRDALLDQIRQGIQLKSVSDGQESTPPTPAPTSGIVGALMEVMQKRSKAIHSSDEDEDDDDEEDFQDDDEWED