lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Required for normal Golgi function.
Subcellular Localization:
Golgi apparatus membrane; Peripheral membrane protein.
Sequence:
MNNQTNQQSQTQSQSQQRINFDITGWEKKSKLSTQQYLLINNLNKSTQEKPLPQKYLEDKINNDIKKEENQQLQQQQQQQQQQQQQQQSPIIENFMDNFNPKTDIDNLSDFYQWYSIIDKNNPHLHQYEWFLETIVNYSKGSNQLLSMVENCDKLVESIQTDYSNLTKKTNQLNEDCEKFFNEELKLRYIAQSIHDKLKFYNQLEIQTKKFNTTNFNVTDSTFLTSLENLENSINFMKSNSTFMESNKYLTQYGFIFSRALGLIKDYISSNLKILSRDIINAQKQLKTSVSTPTSPQLQSSSGGSPLINDFSNSTDFNDLFQHSNIRFRAFAPKLRPLCLELEKRAIGPYLSYLYDTQNIYFNNRRSILSLIMFEKLQSLSKMTDISSMIRSSSLFMIQFYENEYQIYSNFFSPPDLNNNNNNNNNNNNNDNINNSTNINNSNNTNNNNQDIINNCPAFSNILDEYSQQLYDTIRPIYIHIHSFETLCNLAHLIRNELIDDLVQKSMKYSNGFKMTIERMLQDIQERLIFIIQTYIRDEIRSYHPNSDDLDYPNKLKIYVTAESTAVDGDGNGSGNSSPTLSYKSIYSTWYPTLEKSLTCLSKLYLVLETRIFEGLAQEVVEACTFTLIQASRLLLIQQKNDPYIILDSQLFLIKNLLTLREQIAPFDINFVIIEKIVDFPNLKHSLSTLYNVGSFLTLSTNNPILSLLSPRVTNTSIDSKKDLEKELKQSIESFILSNANTIIDPLLSLLTKISVFLNQSNKNQTDPMLLSQQSFADPQRIKEIIEQVKEKASNYLPQVIDRMKLYLSISTQILLMKPIRTNIIDSFDQINQYTKKYYTEDQIKIIDLQSLKLILDKILTPSKQSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNKNENNENENENNSNVNSPSPQQL
The following text describes a protein:
Function:
Ufmylation 'reader' component of a translocation-associated quality control pathway, a mechanism that takes place when a ribosome has stalled during translation, and which is required to degrade clogged substrates. Specifically recognizes and binds ufmylated ribosomes when a ribosome has stalled, promoting the transport of stalled nascent chain via the TRAPP complex to lysosomes for degradation.
Subcellular Localization:
Endoplasmic reticulum membrane. Cytoplasmic vesicle membrane.
Domain:
The middle helical (MH) region recognizes and binds ufmylated ribosomes.
Sequence:
MEQRLAEFRAARKRAGLVAEPSASSQSTQTSGEKAEAATTPKAPSGWLKRFLVWKPRPPSAQAQPSLAQGAAWPRGLESQPPWSPAEEAPPPPQPPPPQPLTPRDRSLLTSVTLLKVLLWLVLLGLFVELEFGLAYFVLSLFYWMYVGMRGPEEKMQGEKSAYSVFNPGCEAIQGSLTAEQLERELHLRPLPRR
The following text describes a protein:
Function:
Required for the morphological differentiation and maintenance of the rhabdomeric photoreceptor apical domain. Acts as a downstream component of the gl and Pph13 transcriptional pathway which is required for photoreceptor cell development. Likely to function by regulating the trafficking or retention of rhabdomeric proteins including the phototransduction proteins ninaE and didum.
Subcellular Localization:
Cytoplasm, cell cortex. Cytoplasm, cytosol. Cell projection, rhabdomere. Note=Cortical membrane protein. In photoreceptors, restricted to the rhabdomeric portion of the apical surface. Localizes to the terminal web at the base of the rhabdomere and not to the microvilli. Phosphorylation appears to displace it from the cortex, increasing cytosol levels.
Domain:
The phospho-regulated basic and hydrophobic (PRBH) motif is sufficient and important for interaction with phospholipids permitting cortical localization. Phosphorylation of the PRBH motif by aPKC inhibits the association of the protein with the cortical membrane.
Sequence:
MSHQEQQFQHYPHHQHHHHHHHHHIHQVQSETQLEQRSSDLEPNRSRNTDRIGSSMDFRNLCQRIDVDGLKAKLPQLKLPKSLPKLRGRKIFRSSKSGSNAAGGGTAGGSAKDGAGAAQQTHLQVAGQSQQFINRTPQRISTISSLMYEGEQEEIRANLGQSQPGTYRSAGSLDDDYYAPGSGDRASRPISPIKIPVVGALDDSSPSENGNVRTTFTQRLQRGYKSLSELRIKHIFAKQTTVRRDNIEVDRYVEQYERELKSEKLARERRDREIAENYDIKIKTLAGTRQNTFDDDDVEHEQFERGKISHETDESGMEATPPLPSRRKPGIAATRFAKVRKPPLEMEEEQQQAAAEESPQANPPPPPPPRPSSYKQLLINKLPHLPSLPNLPQFSRTKEETTKTAENADENNASRKLSIRQNIKRLRKSIKRPSKIKSKAAAPVPDSDEEEATPDGQKTKDAPTRSSTANLRARLSRFASTEQLQQRWRKSFKVAKEPEELETKAEGSATGGASGVLGGLLVGSQLEKTLAKLNEKVHQLKFFQRNANNQNATTSKQPKPNTVGHEPIEIDDDELEATYHRSDSLEAENGNGNENDDSGEDISAEEAFGQIQEEDNEEDHSQDQTKRGQSSVSGIATAHAARQMAKLAEIQAASKSGAAAWSSESLEEIADEDYPRVLIHQEHSDAYESTLIIAVASKGSSMSPVVRSSGLKSSPAAGPKTSPHPEIRISASGPQKSMSYSPGNPRGEPVTKRSPSPEFKTPAGGNKIVPKSETSAWLPNEQIIAGFKEQTSWPAPALYKPKSIDIFEASAGGSAAFADFDEALRNAPVLRISAGSSIDTSGEEADDSCSRVTRIRVQSPQIGNSRESLMAQEEEDKEAERDSEEEEEERDPSERPPSESPPPPPLPQRRPPTKRPATPPIYDAVPPPLPVSKPPPPPSVETIPSVASLPSPAPVTRSMAQRSASMSRPAKPLVKTSSLRLTYNEQVRPGDVGKVNKLISRFEGGRPRLCPRRMHSEEYERCAQPEDEEPEMEQILELQIIERRAVDSVTPTNRAVVIPQITVNNNNNNERQLEQSDQSDQSAHQEITDTRKTKSMELALDRQNSNCSRSEYGSPLSFPSSRRSSTPTNLNANSNSNPNPSTNPNQNPSQILQHQRRSRRSMTRDDDNFYSFDSDEENSYYSISPSGSSRYVVEI
The following text describes a protein:
Function:
Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MSVLALFLSRSPLGALRARLGVTKTWSRRRHVFPPLSVLSCQLETRAPERQCLWTRRTLLTGSPPLPRTFTRIRLAASSSRDGHAHRPKPKGHEGDSAQSSLTHLYENPWTIPNMLSMTRIGLSPVLGYLVVGEDFNLALGLFAFAGMTDLLDGYIARNWANQKSALGSALDPLADKILISVLYVCLTYAHLIPVPLTIMIILRDVALIASVFYVRYKTLPPPKTLSRYFNPCYATAQLEPTFISKMNTAVQLILVAASLAAPVFNYVDSIYLQTLWFITAFTTAASAYSYYHYGQETVKVLRDDK
The following text describes a protein:
Function:
Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients. Enables the organism to utilize D-alanine, D-cysteine, D-histidine, D-leucine, D-methionine, D-phenylalanine, D-proline, D-serine, D-threonine, D-aspartate and D-valine as a nitrogen source and may also contribute to utlization of D-tryptophan, D-tyrosine and D-asparagine as a nitrogen source. Protects the organism from the toxicity of D-amino acids, including from D-alanine. May play a role in its interaction with the host.
Subcellular Localization:
Peroxisome matrix.
Sequence:
MSFDAVVIGSGVIGLSIARELDNRGLKVAMVARDLAEDSLSVGFASPWAGCNWYSFAEGGTPAAEWDAITFSKLAKLAEDHPDLCEKIPFCSVWDLPKSDSESEPWFKDLVFEYKKLKSTPGQHLAGGKKFGYSFKSYVLHAPNYIRHLSSEIRARGIPIHRYRLSSIDEAYNLPGIGKVSLVVNASGLGAKSLIGVEDEKVYSGRGQTVLVRAPGFKACIMHTEGFYADLDESGREITPPPPAYIIPRPGPEGHVVLGGVYQKDNWSTLPDLKEAERILKDCYNLAPELAGPNGKSWKDIEIISHNVGLRPAREGEPRLEIEEREVGTGANGGNGYEVAPKFGCEGERRKVAVVHAYGIGSAGFQASLGMAEKASDLVEKYLSGRRTSAKL
The following text describes a protein:
Function:
Necessary for protein synthesis in mitochondria. Functions as a ribosome recycling factor in mitochondria (By similarity).
Subcellular Localization:
Mitochondrion.
Sequence:
MFLRTVRSQAVRAAALHHTVAPALCMRPVLRTQTVAFSSTPVTLGKKKKGGKEPKAAAKAAAEEAVDEDLFMIEWNKFEDLSAKSVAAFAAKAKEIKAGNNSPDLINNIEVKISKDEVYQIKDIASVALKGGRTLSISVYDPSHTKQVTASILASDLNMNPQPQANSPQILNIPLPPPSAESRAEQQKELKALYNAFKADKKLTSGLAAIRDAFKKDHKKMADQKSIGKDVVKREDKKFEELQKAWTSKIEKEFKTVSDEIAKK
The following text describes a protein:
Function:
Involved in amino acid permease processing and required for the efficient translocation of structurally related amino acid permeases from the endoplasmic reticulum to the plasma membrane.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAKRSIFRFADEKGLKVAARYGVLMSTSFIFALLFHSSVADVNTLWSPGPESAFDAAETYYTLVAGSHFIVKYTVYTIMGLNMIFHLIQATGAKGDDKLFFYSSTLLYLTALILFIVNVAPSMLVVKLQNYVQFPRNMHLSVLAASHVLVEFLLAGVILIQLGYVFGYHVQSIQQREYAEDMREQELAEKAKLESESATTQSVETVSTESVSKRK
The following text describes a protein:
Function:
Catalyzes the reversible isomerization of methylmalonyl-CoA (MMCoA) (generated from branched-chain amino acid metabolism and degradation of dietary odd chain fatty acids and cholesterol) to succinyl-CoA (3-carboxypropionyl-CoA), a key intermediate of the tricarboxylic acid cycle.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MLRAKTRLFLLSPHHLKQLKKSSGSRLVWQRLLHQQQPLHPEWAALAKKQLKGKNPEELIWHTPEGISIKPLYSSRDTKDFPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLATFIVSGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFQYTAKHMPKFNSISISGYHMQEAGADAILELAYTIADGLEYCRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFRPKNSKSLLLRAHCQTSGWSLTEQDPYNNIIRTTVEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMESLTNDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEESVEVLAIDNTSVRNKQIEKLKKVKSSRDQALAERCLTALTACAASGDGNILALAVEATRARCTVGEITDAMKKVFGEHKANDRMVSGAYRQEFGESKEISFAIKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGVSTLAAGHKTLVPELIKELSTLGRPDILVICGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLNDIEKCLEKKQQSM
The following text describes a protein:
Function:
Salivary chemokine-binding protein which shows chemokine neutralizing activity and binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL5, CXCL6 and CXCL8. Binds to CXCL8 with 1:1 stoichiometry. Disrupts CXCL8 homodimer formation, disrupts the glycosaminoglycan-binding site of CXCL8 and inhibits the interaction of CXCL8 with CXCR2.
Subcellular Localization:
Secreted.
Sequence:
MRALLARLLLCVLVVSDSKGLVSTIESRTSGDGADNFDVVSCNKNCTSGQNECPEGCFCGLLGQNKKGHCYKIIGNLSGEPPVVRR
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MTEEEDLCNQQRNLSVEQEEPEQIRVELHDPEPPQIKEEPDEPEPEEFFIIQDEGQLDLKQETDTLMEIPTYEEDKNSEADLNNQQSFNVTDGECEEGSQQEVNQDEDSTSTTDEETDTQNRDQRKRRVQSVESSHMSEEPSEMKEEPEEQEPSEMKEEPEEPFIGQYEELDLKQETDTLMEIPTYEEEEDSELTDCQDEEVNQHEESTSTTDEETDPQNRDQRKRRDRSHVQSADSSHMSESQSGKNSRITSNPSDYMGTGSDEKCYICKECGKSFCNISLFEIHIRIHAEDKRFPCTECEKSFTRKSNLKTHMRTHTGEKPFTCKECNTSFNQISGLRIHMRTHTREQPFSCEECKKSFNQISNLITHMRTHTGERPFTCKECNKSFNQISNLQKHMRTHTGEKPFSCKECKRSFNQISNLQKHMITHTGEKPFSCEKCKRSFNQISNLQKHMRTHTDEKPFSCEKCNKSFNQISNLKTHMRTHTGEKPFFCKECNKSFNQISNLQKHMILPSDWLTPPSTNPPSPLGSLLDTVSCKECVRIQSAVVAHL
The following text describes a protein:
Function:
Probably involved in copper and silver export.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MVKDTYISSASKTPPMERTVRVTGMTCAMCVKSIETAVGSLEGVEEVRVNLATETAFIRFDEKRIDFETIKRVIEDLGYGVVDEQAAVSAEVEHLSRMKRKLYVAAFAGVLLLFLAHFISLPYEDFVQLLIALPAIFYSGSSIFKAAFSALRRRTLNMDVMYSMGVGAAFLASVLSTAGVLPREYSFYETSVLLLAFLLLGRTLEARAKSRTGEAIKKLVGLQAKTAVVIRDGKEIAVPVEEVAVGDIVIVRPGEKIPVDGVVVEGESYVDESMISGEPVPVLKSKGDEVFGATINNTGVLKIRATRVGGETLLAQIVKLVEDAMGSKPPIQRLADKVVAYFIPTVLLVAISAFIYWYFIAHAPLLFAFTTLIAVLVVACPCAFGLATPTALTVGMGKGAELGILIKNADALEVAEKVTAVIFDKTGTLTKGKPEVTDLVPLNGDERELLRLAAIAERRSEHPIAEAIVKKALEHGIELGEPEKVEVIAGEGVVADGILVGNKRLMEDFGVAVSNEVELALEKLEREAKTAVIVARNGRVEGIIAVSDTLKESAKPAVQELKRMGIKVGMITGDNWRSAEAISRELNLDLVIAEVLPHQKSEEVKKLQAKEVVAFVGDGINDAPALAQADLGIAVGSGSDVAVESGDIVLIRDDLRDVVAAIQLSRKTMSKIKQNIFWALIYNVILIPAAAGLLYPIFGVVFRPEFAGLAMAMSSVSVVANSLLLRNYVPPIRRGGDSVEKIVLELSGLSCHHCVARVKKALEEAGAKVEKVDLNEAVVAGNKEDVDKYIKAVEAAGYQAKLRS
The following text describes a protein:
Function:
Required for correct functioning of the GINS complex, a complex that plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex seems to bind preferentially to single-stranded DNA.
Subcellular Localization:
Nucleus.
Sequence:
MSYNSSAGTSGVPFGAQNALLTASVRERSTDTIKPFEETLVRTLQRETRAFGDQLTQAAEHFRKQQEALDEEDIQMDPGTICALKMSASTARHNKRVLLAYAMQRRNAILDVYWACSASVPNTLVASSSNVSAEKPEGSSERVSDPISKVLTPVELEYLRAHSTLVHDLAKPYHAYTVNLLGNLARGPSRGLFIQVECMRELGEVAVGDGGGMIKFEVGSRYFVKRSEVEQLIEGGWLMEIPR
The following text describes a protein:
Function:
Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug resistance parasites.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MDITESEFTIFEVTPDPNELNNKRIKEIKGGKVNIKELFRYAGVFEIILLIIGIIGSIGVGCLNPLLMILTGDVVDTFVNGENFSKEGGSIKITTEEMNYEIMNSISDTINKLVLKMLYFAIGNMVAGFLQTICFFVLSEYQGIKIRSLYFKALLRQDPGWFDCHKTGELTSKIINDIQKIQDGMSLKFGRLFQTFSSFITGYLIGFIKCWDLTLVVLCMFPFIMVSMMGLGMSAGIFTMKSHKPFSEACSIAEQTIGNIRTVHSLTQERSFCESYNTKIMETDKYNIKKSIGIGTGLGCMMFFIMSSNALGSWYGNFVVRGKGGSDNVKAGTVLTVFMSVLLATQSLSQISTPINILNSAKVAAFNVYQTIDRIPDIDCQSIGGECPTECNGNIRFEDVQFVYPTRLSHHVLKGLDLEIKKGQTIALVGASGCGKSTTIQLIQRNYDPNGGRVTLDGKDIRELNIKWLRNQIGLVGQEPVLFAGTIRENIMLGAKEGATPSEEEMIECAKMANAHDFISKLPEGYDTIIGEKGALLSGGQKQRIAIARALIRNPSILLLDEATSALDTQSEKIVQEALEKASKGRTTIIVAHRLTTVRNADKICVFHQGEIIEQGKHQELMDLKGTYYGLVKRQSMEEEVDQETVENDLKKFREQEDKEVENISLEQTNLHNENSIVKQIKQEYKEEQKKLKHSNRFVLFRVIWNNYKHEYIFCTLGLIGGIGAGAAFPFYSLNFVDLIRVLMKLHPGINLTDEQANSILRSCMIIICIGIITMISFFCYVGLFMAAGEKMIGRIRRRFYYSIMHQNVSWFDRRENMVGAVTTKLTSDPTSLQGISAERVGDIIEIMSTVGFGFGIGLYFSWKLSLCILAVFPIISFFMFINGQLNSKNAAPAKAAYEQCGVTLVEVVEAMKTVQSLGKEDYFSQKYNNDLQIPKRGIIKWGPLLSITNAITNLLTFSINAYGYYLGICFMKKTINYQQDVPNFVDEIIDTFGDIQKALMTINSATTSFAQIGNVLPDVGKAVGAAKSIYNIIDRKPSIDCYSEEGETFNDVKGEIEFKNIHFRYPTRADNEVLKGISFKAEQGKTIALVGASGCGKSTTIQLIERFYDPTSGEVLLDGHNIKDLNIHFLRNQIGLVGQEPVLFAESVIDNIKRGVPEGVEVSNEQIYAAAKMANAHDFISAMPEGYNTMVGDRGSQLSGGQKQRIAIARALIRNPKVLLLDEATSALDSESEKIVQDALDKASKGRTTIVIAHRLSTIQNADKIYVIMRGKIVEQGKHQELIDLKGFYYTLAMQQFGTVN
The following text describes a protein:
Function:
Hydrolyzes 2-acetyl monoalkylglycerol ether (1-O-alkyl-2-acetyl-sn-glycerol), the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor (By similarity). May be responsible for the hydrolysis of cholesterol esters (such as cholesteryl (9Z-octadecenoate)) in macrophages (By similarity). Also involved in organ detoxification by hydrolyzing exogenous organophosphorus compounds (By similarity).
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein. Microsome.
Sequence:
MRSSCVLLAALLALVAYYVYIPLPSAVSDPWKLMLLDATFRGAQQVSNLIHSLGLSHHLITLNFIIISFGKKSARSSPRVKVTDTDFDGVEVRVFEGPPKPDEPLRRSVVYIHGGGWALASAKISYYDQLCTAMAEELNAVIVSIEYRLVPQVYFPEQIHDVIRATKYFLQPEVLDKYKVDPGRVGVSGDSAGGNLAAALGQQFTYVESLKNKLKLQALIYPVLQALDFNTPSYQQSMNTPILPRHVMVRYWVDYFKGNYDFVEAMIVNNHTSLDVERAAALRARLDWTSLLPSSIKKNYKPVLQTIGDARIVKEIPQLLDAAASPLIAEQEVLQALPKTYILTCEHDVLRDDGIMYAKRLESAGVNVTLDHFEDGFHGCMIFTSWPTNFSVGIRTRDSYFKWLDQNL
The following text describes a protein:
Function:
Component of the nuclear pore complex. Binds to transcriptionally active chromatin including regulatory regions.
Subcellular Localization:
Nucleus, nuclear pore complex. Chromosome. Note=Interacts with chromatin.
Sequence:
MEWHEVELDGSRTIAFPERIVPGFGREPSAHLDAAEYLGGIIRDGQWGWVTWRYGSDATLLVCSMSTGDYLSWHCFWSESDDLGPRKSIRCVEELFPGEHERPAMLAICLESWNSGDQRPIDCPLSTQVLIYAIRNSQVLRRFDLHGITCSALTFLDKRIYGLTRLRRFKGCLAVATEEGTVLLVDLNSDSLQASTQRRSLCSPSSKDEPSDGNLYFVSSEESKRQLSSKLTHCRSKGAHLAVRMDVASIGISCLMGISMAPGYAAGLEDGRILIYDLINFDVTTDLNSPVKRKGVNRAVKRMCLIMPPDDPKPCFYICALYQNIDVLQMMLHSVCYRGSYRDRETHTIRFKDYRSRTVRNRQILDGGICSVIGCATASTFSFAGDNGTLLIVISWHSSADKKNKLVLFDINQWYKDEMPTSVHKNEVPNYMSGYILSGLQTGLALDLRSTTILHFVSLQRYDEHFYPNSLTFDCSLLTPTGKRYYAQDGVQHRFLNALRCDRATLFLRPQIYHEDIVRLRLLPQFCELNPNATFSKIAMYELILSVALEHNCGALLNDCARSWMDGSFLCNMIDNTQLSLSTLTNWILKRAGQIKTRCSELCHGIFDYGGYPLDQRERREFQVLSGQLRELVRLQSYIVEQGRRRLTSSILDDCRANERALKTVLEYQRVLLWFIDHGLLPEGQHMDNLVPGEQAFVRLQHEYSEKRAQGKILYIDSLGKRASFPEPYPPDSLHAYIHLMLSPDIELCHKHALILYLLMDLNQQLVGRFQIAFQLDKDLATSLRCFWYLDHGDYERGVEELYKEPAPAKNLKSWQMRLLIDKLLAEGAVKAAKKVVSRPPGPLSSALHMKVLLANENITEAFQIARLDDDEDGQPLLERFFRHCIEIRRFKVLAELYLREPEERLLYSLLRQCRSRQTDCVQLIMLLQKSKFIEAVSFMDEVAAERERDESSNTILPAYSATMGPVTQNIAGTYLRIRDTLEPYQKTGPLEPFSCQLVKQNASGQLGGIFQSSAVSAHWATQCESPPKMTPVSIQSKIGYTNVPFLRHAQYGHSELPLPRRIVKPVPHQVVEKRQRELEDQRTNLQDQRQLGTERPNKRPCLMVERMVEDVKDYVRSIREKSSNQMEQEEVKQNEATNLLQPPNFLQARQSTTIRQSSSSPQPIPPILKGSGAVDAVKRAPPVATFTALAGPKRFRFVPPIPLRTDKSDKSTEMGSEGAAEGEEETDEIIVEIESRSEPRSACSYESDEEDEFLSPLVSANVSLVDPVPSRNSPHYFAPPAGPQPRNSLLHGGNGSGSKIGTATGSESSSGFGSFSTVQPAQTSSHSQFVPTVCSSKMGETQSQVFSSGSCGIKISERTTICGEMESTDLGAELTAAPSAQWSLPSARPAIQGHHQMMDTTLGMSTYDVASLEQQDTQDVENEEELKLGDTKSLEEQQNPQDEQKPEQEQDQDEDQAQEPLATGGQLAFLSNSEGTAQEPLSSPIYSLSSEDSNVSSAGIRNPMLPTLHTDDPMYSIVVESPGSITTSRSVTHTPTSFLPSDTNVSQTSSPQAPHGEDGDGTPISLYRANSLETVDDLDTTKGSLEEEEEYDDDDCVIALDGTEVRGYVARPQQSAASSSAELFAFKDECQEEAAGVPSPFLSLGATVNSDSDVADTIVLDSDEETAKEKDTQPEQRKDWPMEEETPSNESVATVEFSEQKQPRADMDIGMEVDAVPDVLEVLEVPEMEPLPVLSDVDIEMAVDEVPNVLEVLEVPELEPLPAGQATQSSGLGEIPEEDVDAEAEEQVVVKVEHVADEQPKEGDKTESKEASEEETQHNPEPLLPEEEDSRHSLKLIFSGDEDEEEQDVPTRAIHTLRPRRSFTEHQDSPRTLRPRRVSQEHRDSPTPVAGRTMSLRSTDAPTLSPASNPPVSTPKRRGLQHKYLLEVIDEHSPSDLSLPRTRSRTRLSVDSEATSSRPGTPTMTKARGKRATSQAPPTASPSVRRSLRGHSEPPAALSAQLVRKPKTARAGVRSRKTSSGVQSPVAVSPTPIDAPIDVPDSTAPEEEQPRLRRTARRRISELSDQSANGTGDLRSEASSSRTGSKSNSAASTQNRELRPRLRRTSKSEH
The following text describes a protein:
Function:
Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis. Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery. Functions by recruiting the CCR4-NOT deadenylase complex and probably other components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs, and hence promotes ARE-mediated mRNA deadenylation and decay processes. Binds to 3'-UTR ARE of numerous mRNAs.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MSASVLSSIYDFDREKVPNSNAIYLHNMLEKRNVGVPLAASNTNSNRSFGYFRSNSTNHMDFNMSNRLQIGFESSTPAFMNKENKYRDRAFSDAGERSQQLQEMLQQKPGSQINSTRYKTELCRPFEENGSCKYGEKCQFAHGYHELRNLSRHPKYKTEPCRTFHTIGFCPYGPRCHFIHNADERRAATNNTQARLSQELGILGEKESSNPFLRPRERPKLHHSLSFSGFSSSRSSDTALIDNPTSRTPPPPNCSLTPTSPCLNAFTFPDQDLKAFLAPIIPHTQSSSLYSNIQTNGCPPSPPFKMSHLPSMYPLSESPVFDSPPSPPDSLSDPEGYLSGSCCSSGTISGSESPSMDANRRLPIFSRLSISDD
The following text describes a protein:
Function:
Probable transcription factor involved in plant development.
Subcellular Localization:
Nucleus.
Sequence:
MLLEETEPPNQTLDHVLSWLEDSVSLSPLPGFDDSYLLHEFDGSQTWEWDQTQDPEHGFIQSYSQDLSAAYVGCEATNLEVVTEAPSIDLDLPPEIQQPNDQSRKRSHDGFLEAQQVKKSARSKRKAIKSSEKSSKDGNKEGRWAEKLLNPCALAITASNSSRVQHYLCVLSELASSSGDANRRLAAFGLRALQHHLSSSSVSSSFWPVFTFASAEVKMFQKTLLKFYEVSPWFALPNNMANSAILQILAQDPKDKKDLHIIDIGVSHGMQWPTLLEALSCRLEGPPPRVRITVISDLTADIPFSVGPPGYNYGSQLLGFARSLKINLQISVLDKLQLIDTSPHENLIVCAQFRLHHLKHSINDERGETLKAVRSLRPKGVVLCENNGECSSSADFAAGFSKKLEYVWKFLDSTSSGFKEENSEERKLMEGEATKVLMNAGDMNEGKEKWYERMREAGFFVEAFEEDAVDGAKSLLRKYDNNWEIRMEDGDTFAGLMWKGEAVSFCSLWK
The following text describes a protein:
Function:
Subunit b, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro. Part of the complex F(0) domain. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular Localization:
Mitochondrion. Mitochondrion inner membrane.
Sequence:
MAGKDIRNLFDNMRTDELKALDQVKSDQMEDLKQTVDEIKLEQWRSGSAEMINDALKNNLAMMLETEYLNRQAAVVEAVKRKLDYQVEVQKVDSQLAHGHMVKWIEEKVMNTITPASQKATLAACIAQLNAMPGK
The following text describes a protein:
Function:
Functions as a voltage-gated monoatomic cation channel permeable to both potassium and calcium. Plays a role in the cellular response to DNA damage (By similarity).
Subcellular Localization:
Nucleus outer membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAGSGSSAPWGKHLLHAVLMVLVALVLLHSALAQSHRDFAPPGQQRREAPVDLLTQIGRSVRETLDTWIGPETMHLISETLSQVMWAISSAISVAFFALSGIAAQLLTALGLDGDHLTQGLKLSPSQVQTFLLWGAGALVVYWLLSLLLGLVLAVLGRILGGLKLVIFLAGFVALVRSVPDPSTRALLLLALLTLYALLSRLTGSRASGAQLEAKVRGLERQVDELRWRQRRAAKGARSVEEE
The following text describes a protein:
Function:
Maleylacetoacetate isomerase; part of the L-tyrosine degradation gene cluster that mediates the biosynthesis of the brownish pigment pyomelanin as an alternative melanin. The 4-hydroxyphenylpyruvate dioxygenase hppD catalyzes the conversion of 4-hydroxyphenylpyruvate to homogentisic acid (HGA). The protein hmgX is crucial for this conversion and thus, probably functions as an accessory factor to mediate specific activity of hppD. The homogentisate 1,2-dioxygenase hmgA is then involved in the cleavage of the aromatic ring of HGA and its conversion to 4-maleylacetoacetate. When hmgA activity is lowered by the cell wall integrity (CWI) signaling pathway, HGA accumulates and leads to the production of pyomelanin through benzoquinone acetic acid after oxidation and polymerization. On the opposite, in non-stress conditions, both hppD and hmgA activities are balanced and HGA is degraded into 4-maleylacetoacetate. 4-maleylacetoacetate is further converted to 4-fumarylacetoacetate by the maleylacetoacetate isomerase maiA, which is degraded into fumarate and acetoacetate by the fumarylacetoacetase fahA (Probable).
Sequence:
MEDSTSPKVTLYTYFRSSCSARLRIALNLKSIPYTPIAVNLLKGEQSSPENIALNPSGTVPTLIVEHDSKEPVTITQSLAALEYLEEITPASSHALLPPASNPEARAVVRTLVDIMSCDVQPVTNLRILKRVAPFGVDRAAWSKDLIEDGFRAYEAIAAKSAGLFSVGDSITMADVCLLPAVWGAERAGVKVEKFPTIYRVAQRLEEEDAVKRAHWRTQPDTPEEFRVSSS
The following text describes a protein:
Function:
Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds.
Sequence:
MQYPINEMFQTLQGEGYFTGVPAIFIRLQGCPVGCAWCDTKHTWDKLSDREVSLFSILAKTKESDKWGAASSEDLLAVINRQGYTARHVVITGGEPCIHDLMPLTDLLEKSGFSCQIETSGTHEVRCTPNTWVTVSPKVNMRGGYDVLSQALERANEIKHPVGRVRDIEALDELLATLSDDKPRVIALQPISQKEDATRLCIETCIARNWRLSMQTHKYLNIA
The following text describes a protein:
Function:
Functions as a component of both the DNA-binding general transcription initiation factor complex TFIID and the transcription coactivator SAGA complex. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA acts as a general cofactor required for essentially all RNA polymerase II transcription. At the promoters, SAGA is required for transcription pre-initiation complex (PIC) recruitment. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (via core/TAF module) and promoter selectivity, interaction with transcription activators (via Tra1/SPT module), and chromatin modification through histone acetylation (via HAT module) and deubiquitination (via DUB module). SAGA preferentially acetylates histones H3 (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac) and H2B and deubiquitinates histone H2B. SAGA interacts with DNA via upstream activating sequences (UASs).
Subcellular Localization:
Nucleus.
Sequence:
MDETNSSQTPQYMKVESDDEIQPMSLDRGDGRSPSETNQTNTAGGHSQTPEKEKSENDVASSTSPNSASNSRKRSASPTLEPNIDPDDMFKDKTLEDFLNSMDDYAPIIPDVIIDYYLSLSGFSSVDPRMKRLLGLTAQKFMSDVAQDAYQYSKIRTGTSSSASGSAAAPGAGPAGANSFASASRRADRGKTVLTVEDLGAALNEYGINLRRPDFFR
The following text describes a protein:
Function:
Acts as an osmosensitive calcium-permeable cation channel.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MLLSALLTSVGINLGLCFLFFTLYSILRKQPSNVTVYGPRLVKKDGKSQQSNEFNLERLLPTAGWVKRALEPTNDEILSNLGLDALVFIRVFVFSIRVFSFASVVGIFILLPVNYMGTEFEEFFDLPKKSMDNFSISNVNDGSNKLWIHFCAIYIFTAVVCSLLYYEHKYILTKRIAHLYSSKPQPQEFTVLVSGVPLVSGNSISETVENFFREYHSSSYLSHIVVHRTDKLKVLMNDAEKLYKKLTRVKSGSISRQKSRWGGFLGMFGNNVDVVDHYQKKLDKLEDDMRLKQSLLAGEEVPAAFVSFRTRHGAAIATNIQQGIDPTQWLTEAAPEPEDVHWPFFTASFVRRWISNVVVLVAFVALLILYIVPVVLVQGLANLHQLETWFPFLKGILNMKIVSQVITGYLPSLIFQLFLLIVPPIMLLLSSMQGFISHSQIEKSACIKLLIFTVWNSFFANVLSGSALYRVNVFLEPKTIPRVLAAAVPAQASFFVSYVVTSGWTGLSSEILRLVPLLWSFITKLFGKEDDKEFEVPSTPFCQEIPRILFFGLLGITYFFLSPLILPFLLVYYCLGYIIYRNQLLNVYAAKYETGGKFWPIVHSYTIFSLVLMHIIAVGLFGLKELPVASSLTIPLPVLTVLFSIYCQRRFLPNFKSYPTQCLVNKDKADEREQNMSEFYSELVVAYRDPALSASQDSRDISP