lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradation via the proteasome. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGTMIKVKTLTGKEIEIDIEPTDTIDRIKERVEEKEGIPPVQQRLIYAGKQLADDKTAKDYNIEGGSVLHLVLALRGGC
The following text describes a protein:
Function:
An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Subcellular Localization:
Cytoplasm. Cell inner membrane; Peripheral membrane protein.
Sequence:
MKTKAGFVALIGKPNAGKSTLLNTLLNAHLALVSHKANATRKLMKCIVPFKDKEWYESQIIFLDTPGLHHQEKLLNQCMLSQALKAMGDAELCVFLASVHDDLKGYEEFLSLCQKPHILALSKIDTATHKQVLQKLQEYQQYDSQFLALVPLSAKKSQNLNALLECISQHLSPSAWLFEKDLMSDEKMRDIYKEIIRESLFDFLSDEIPYESDVMIDKFIEEERIDKVYARIIVEKESQKKIVIGKNGVNIKRIGTNARLKMQEVGEKKVFLNLQVIAQKSWSKEEKSLQKLGYIHRRNRD
The following text describes a protein:
Function:
Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Sequence:
MMAVASSRTPAVTSFIAPLVAMVGGGQLARMTHQAAIALGQNLRVLVTSADDPAAQVTPNVVIGSHTDLAALRRVAAGADVLTFDHEHVPNELLEKLVADGVNVAPSPQALVHAQDKLVMRQRLAAAGVAVPRYAGIKDPDEIDVFAARVDAPIVVKAVRGGYDGRGVRMARDVADARDFARECLADGVAVLVEERVDLRRELSALVARSPFGQGAAWPVVQTVQRDGTCVLVIAPAPALPDDLATAAQRLALQLADELGVVGVLAVELFETTDGALLVNELAMRPHNSGHWTIDGARTSQFEQHLRAVLDYPLGDSDAVVPVTVMANVLGAAQPPAMSVDERLHHLFARMPDARVHLYGKAERPGRKVGHINFLGSDVAQLCERAELAAHWLSHGRWTDGWDPHRASDDAVGVPPACGGRSDEEERRL
The following text describes a protein:
Function:
Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE).
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Sequence:
MASPAAGTPPFLTKTYAMVEDPSTDETISWNDSGTAFVVWRPAEFARDLLPKHFKHSNFSSFVRQLNTYGFKKVVADRWEFANDCFRRGEKHLLGGIQRRKGSGTGGAGAAPAGGIPTAIPISSPPTSSGGEPAVSSSPPRGAAGIAAGVSGAVAELEEENARLRRENARLARELARARRVCDGVRRLVSRYDHDHGGGEEEAGEGDVKPMLFGVAIGGKRSREENGEDEEEEEEEGADEDGEDDEVEEDDEERERHAARRVPVREGKVRRTTELSDLDVLALSVRAAAAARPGGASRDRKSSVS
The following text describes a protein:
Function:
Probably involved in the biogenesis of the COX complex.
Subcellular Localization:
Membrane. Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MRLHHSRPFLTGSLLHKPIIQPTNNNNNTLIIRFSRFSCSPSRTSRAAADGSQGSSSGFREPLDTSNWKPRVNRRWTPMTIVLVSVPILTFALGTWQVQRLGWKKELIKDLENKMALEPISLPKHINPKVIPEFEYRKVKLTGRFDHSKEIFIESRTREGELGYHLITPFHPHNGGQPILVNRGFIKRQLKDPRSRPLSHESKDVVEVIGMLRKQESKSFFQPNNSKDSNQWYFVDIQEIAEHLETAPILVDAITCTSSTFSSSSLCLSTKLFLKS
The following text describes a protein:
Function:
Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MKIMSFQASRAAVLMLAAAWLASPVSAQTQTPPAAPAQSTARPAPISPVPAAPSTPAPAVPAPAASTATAPAAATASPAAIAPATAKPDAASATAPAMKELSPWVMFMSADVIVKAVMIGLAFASLMTWTVLIAKSIELSVASGRLRSALKKISEARSLAEAQMALGTKEGILPSFLAAALREARMSAGLSSDAGIKERAASSFSEIVRAEARRIRIGMGVLATIGSTSPFVGLFGTVWGIMNSFIGISKSQTTNLAVVAPGIAEALLATAIGLVAAIPAVIIYNHFSRVTKSYLELVSRASGAAGRLLSRDLDRSHGSVHSRAAE
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 mannosyl-D-glycerate transport. Also involved in thermoinduction of ompC.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Domain:
The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain; The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-2 domain; The EIIC type-2 domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Sequence:
MVLFYRAHWRDYKNDQVRIMMNLTTLTHRDALCLNARFTSREEAIHALTQRLAALGKISSTEQFLEEVYRRESLGPTALGEGLAVPHGKTAAVKEAAFAVATLSEPLQWEGVDGPEAVDLVVLLAIPPNEAGTTHMQLLTALTTRLADDEIRARIQSATTPDELLSALDDKGGTQPSASFSNAPTIVCVTACPAGIAHTYMAAEYLEKAGRKLGVNVYVEKQGANGIEGRLTADQLNSATACIFAAEVAIKESERFNGIPALSVPVAEPIRHAEALIQQALTLKRSDETRTVQQDTQPVKSVKTELKQALLSGISFAVPLIVAGGTVLAVAVLLSQIFGLQDLFNEENSWLWMYRKLGGGLLGILMVPVLAAYTAYSLADKPALAPGFAAGLAANMIGSGFLGAVVGGLIAGYLMRWVKNHLRLSSKFNGFLTFYLYPVLGTLGAGSLMLFVVGEPVAWINNSLTAWLNGLSGSNALLLGAILGFMCSFDLGGPVNKAAYAFCLGAMANGVYGPYAIFASVKMVSAFTVTASTMLAPRLFKEFEIETGKSTWLLGLAGITEGAIPMAIEDPLRVIGSFVLGSMVTGAIVGAMNIGLSTPGAGIFSLFLLHDNGAGGVMAAIGWFGAALVGAAISTAILLMWRRHAVKHGNYLTDGVMP
The following text describes a protein:
Function:
The dimeric enzyme acts as an E1 ligase for SUMO1 and SUMO2. It mediates ATP-dependent activation of SUMO proteins and formation of a thioester with a conserved cysteine residue on SAE2.
Subcellular Localization:
Nucleus.
Sequence:
MATQQQQSAIKGAKVLMVGAGGIGCELLKTLALSGFEDIHIIDMDTIEVSNLNRQFLFRRSHVGQSKAKVARDAVLRFRPNINIRSYHANVKNPEFDVDFFKQFDVVLNGLDNLDARRHVNRLCLAADVPLVESGTTGFLGQVTVHIKGKTECYECQTKPAPKTYPVCTITSTPTKFVHCIVWAKDLLFAKLFGDKNQDNDLNVRSNNSASSSKETEDVFERSEDEDIEQYGRKIYDHVFGSNIEAALSNEETWKNRRRPRPIYSKDVLPESLTQQNGSTQNCSVTDGDLMVSAMPSLGLKNPQELWGLTQNSLVFIEALKLFFAKRKKEIGHLTFDKDDQLAVEFVTAAANIRAESFGIPLHSLFEAKGIAGNIVHAVATTNAIIAGLIVIEAIKVLKKDVDKFRMTYCLEHPSKKLLLMPIEPYEPNPACYVCSETPLVLEINTRKSKLRDLVDKIVKTKLGMNLPLIMHGNSLLYEVGDDLDDIMVANYNANLEKYLSELPSPILNGSILTVEDLQQELSCKINVKHRFFSEILNPVLNSVWFLIILPSTFPKLFHFTESRNQDGLSLDIILGFSNVTIRRVLTMFETGRRLTHPLLILFCHREEFDEEKEPEGMVLSGWTPSPATNGESASTSNNENPVDVTESSSGSEPASKKRRLSETEASNHKKETENVESEDDDIMEVENPMMVSKKKIRVE
The following text describes a protein:
Function:
Transcription factor involved in the regulation of gene expression in response to extracellular amino acid levels. Synthesized as latent cytoplasmic precursor, which, upon a signal initiated by the plasma membrane SPS amino acid sensor system (including CSY1 and CSH3), becomes proteolytically activated and relocates to the nucleus, where it induces the expression of SPS-sensor-regulated genes. Required for efficient alkalinization through the release of ammonia from the cells produced during the breakdown of amino acids, and subsequent switch to the hyphal form.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Note=Localizes to the cytoplasm in its unprocessed form and is targeted to the nucleus after proteolytic processing upon induction by amino acids.
Sequence:
MSVAITSNNNKQPQPQPQPHLKVVNNNSTFNLYTWLRSVFQYCISLIISYTSNWLLVNNDNNNNNININYKSNNNDNNNASTSLQPKISNVKAESMKIFPDLQKSNFTTYYTTEKPLHQDVLKPVICSTGITSRILPYTNEKGELEWKFTEVQGKELDEFKMHPQQQQQQQEVKQELSPAESNESNESLAKDSSTTPASISDSPSHSETESTVSSTIIANSNQIFKCPSCDAEFRVRGYLTRHMKKHSTKKAYTCPFHDKSIYVDENNITHKCHSSGGFSRRDTYKTHLKSRHFNYAKPIKSAERSKVPGQCAMCGEHFNSAEIWCEIHVEGGECKFLPMGFKGKSRIKNRLKKQIQKNKMIDPELVPFASKVLEEVEQERQKKKNYRTTGTGSESSIQSQESESSINSTPLSMQISAPVPMPVSIQQQHQHQHQHHHHVQNQHQQHVNQQQSIATPASIYSSSASSTSSYESTHSPYTPQSSRSPLSHMYNPQQPPYFNQIAQAHQQDGQKNQVKDDYDDEYCLDVDQLNTTFVNETVANYLQIHDFHSMNQYQPGQQQQQQQQQQQQQQQRQHQQQQPSMYF
The following text describes a protein:
Function:
Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-binding protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
METVRRIVKGTLLLGFCTGIGGDLWVLVAPGQERRLEMRMNYPEANPPMLAEAHKRNEMVLKVIEESAKTNENMARRSPWSS
The following text describes a protein:
Function:
Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine.
Sequence:
MSEVEAIRGTYSNLLREKRIVLLVSSGISLYKSIDTARLLIRHGAEVYAFMTPKAARLVSSDLFWWATGRRPVVRLTGKAEHIEICAKADVVLVAPATANTLVKLSLGIADNAALTCALAAANAKLVVAPAMNLAMWNTEPVRNALERLEKRGYIVPPIIEEGKAKYPPPEEIAEYVIDATAPRDYAGVRALVTAGPTHEHIDDVKYITTPSSGLTGYYFAREAAARGARVTLVTGPTNLKPPPNVEVVKVTSVLEMYKAVVERASENDLFIFSAAPLDFYVEGRIAGKLDSFLSQYQLTLRQAPKAAQEVKRLNPGAVVIGFKAEYGVSEEELIERAKRRMESGEWDFALAHDVSKMGFGTLKDQYLLIHRDGKTTRLGPAHKRELARLVLTLARGQLKSSD
The following text describes a protein:
Function:
In presence of calcium ions, it binds to surfactant phospholipids and contributes to lower the surface tension at the air-liquid interface in the alveoli of the mammalian lung and is essential for normal respiration. Enhances the expression of MYO18A/SP-R210 on alveolar macrophages.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix. Secreted, extracellular space, surface film.
Sequence:
MANLMKQVIFTITVVLVLLCQAQSQESAVCSVIQGPPGRDGKDGERGMKGDPGLAGQNGSQGLKGPAGPHGKAGPPGQKGNQGERGTNGEPGQQGPKGEKGSLGTPGAPGNPGPKGSTGPRGIPGAMGTTSAQGIKGDQGLQGPKGETGLRGPAGVSGPPGKDGFAGIPGASGIPGPSGIKGSKGDKGDPDTSLTKRIELLEEKLQTILLNLEVMEKRYGFEPWFPLRNIFAKMKSLQQPFLLLAAICVGTSMAQLSGNCLSGLPGMAKGIPETIDRALQVPLLTINQRIAKLEAALNFEGKFHQVGGKIFATNGEQADFEASKLTCKKAGGRIATPMNEAENSALLSILKEQNKYAYLGVTEGVIPSIYLYLDGTPLSYSNWRKNEPNGKGKEKCVEMFTDGQWNDKACNQNRLTVCEF
The following text describes a protein:
Function:
Facilitative organic cation transporter that mediates the transport of carnitine as well as the polyamine spermidine. Mediates the partially Na(+)-dependent bidirectional transport of carnitine. May mediate L-carnitine secretion from testis epididymal epithelium into the lumen which is involved in the maturation of spermatozoa.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MGARHLEPMLERVGQLGRFQAFVYFTSVFQAISCGIHYLASVFMAVTPKFFCGIMGNVSQIVFHNSSSLKMEDSWALLTSGKDYIVVQMQNGDVWELAQCSRSRREDTSNLEYEYDGNKSDFPCLDGYIFDQTKWQSTVVTEWDLVCHREWLAKLIQPTFMFGVLLGAVIFGDLADRVGRRLIMWSTSTGQFLFGIAVAFTFDYYSFMAARFLLAMVSSGYLVVVFVYVTEFIGIKARTWASMHVHAFFAVGIMVVALMGYLVRTWWLYQIFLSITTLPFLLCCWILPETPFWLLSVGKYEEAQKVIDMMARWNNRRSCKISELCSFEQDGITNNDFSATKKHSVIDLFFNWNIARRTLTVWLIWFTGSLGYYVFSLTSVNLGGNEYLNLFLIGAVELPAYIIACIGMDKLGRRNTLIPFLILSALICFLIMLIPQDYSILSILANMAGKFAIGVAFGLIYLYTAELYPTIIRSLAVGSGSMMCRLGSVVAPFCVYLTSIWIFMPQLLVGIMAFLTGMLTLMLPETLGKPLANTWEETMELRTMKDNYSIKSPPTKSDVSSEKIEMINLKALDIDE
The following text describes a protein:
Function:
Putative membrane receptor.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MEGQDEVSAREQHFHSQVRESTICFLLFAILYIVSYFIIIRYKRKSDEQEDEDAVVNRISLFLSTFTLAVSAGAVLLLPFSIISNEILLAFPHNYYIQWLNGSLIHGLWNLASLFSNLCLFVLMPFAFFFLESEGFAGLKKGIRARILETLVMLLLLALLILGMVWVASALIDSDAASMESLYDLWEFYLPYLYSCISLMGCLLLLLCTPVGLSRMFTVMGQLLVKPAILEDLDEQIYMITLEEEALQRRLHGLSSSVEYNVMELEQELENVKILKTKLERRKKASAWERNLVYPAVMVLLLIETSISVLLVACNILCLLVDETAMPKGTRGPGIGSASLSTFGFVGAALEIILIFYLMVSSVVGFYSLRFFGNFTPKKDDTTMTKIIGNCVSILVLSSALPVMSRTLGITRFDLLGDFGRFNWLGNFYIVLSYNLLFAIMTTLCLIRKFTSAVREELFKALGLHKLHLSDTSRDSETTKPSANGHQKAL
The following text describes a protein:
Function:
Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.
Sequence:
MPWIVGVSGASGTPYAAAVLRALLAAGESVDLVVSRASRLTLLDETGISFRDAHWRHDLREWLARGADGKPDTFDADVSGVRHWSAGDLAAGPSSGSYPTKGMLIVPASTACVAGVALGLSKDLLQRAASVTLKERRRLVVAVRETPLDGRTLRHLVTLDDAGASVVPASPAFYAGATHIQDLVDFVAGRVLDAAGVGHGLYRRWRGDLGGARPTG
The following text describes a protein:
Function:
Required for meiotic recombination and cell cycle progression. Binds to single and double-stranded DNA, in the presence of magnesium, and exhibits DNA-dependent ATPase activity. Promotes DNA strand annealing and strand exchange via DNA recombinase activity and forms helical and stacked ring nucleoprotein filaments.
Subcellular Localization:
Nucleus.
Sequence:
MEEFAEGNDDEQMIFSDIEDLTAHGIGMTDIIKLKQAGVCTVQGVHMSTKRFLLKIKGFSEAKVDKLKEAASKMCPANFSTAMEISQNRKKVWSISTGSEALNGILGGGIQSMSITEVFGEFRCGKTQMSHTLCVTAQLPRDMGGAEGKVAFIDTEGTFRPDRIKAIAERFGVDADQAMENIIVSRAYNSEQQMEYITKLGTIFAEDGQYRLLIVDSIMALFRVDYSGRGELSERQQKLNIMLARLNHISEEFNVAVFVTNQVQADPGAAMMFASNDRKPVGGHVMAHASATRLLLRKGRGEERVAKLNDSPDMPEAECSYVITPGGIADVS
The following text describes a protein:
Function:
GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity.
Subcellular Localization:
Cytoplasm. Endomembrane system.
Sequence:
MPGGLVVFFFFKYKMETESESSTSGDDSVFWLESEVTVQVTDCEEEEREEKFRKMKSSVHSEEDDFVPELHRNVHPRERPDWEETLSAMARGADVPEIPGDLTLKTCGSTASMKVKHVKKSTTPGLMGCDNIHRLPFTKGHFPKMAECAHFHYENVEFGSIQLSLSEEQNEVMKNGCESKELVYLVQIACQGKSWIVKRSYEDFRVLDKHLHLCIYDRRFSQLSELPRSDTLKDSPESVTQMLMAYLSRLSAIAGNKINCGPALTWMEIDNKGNHLLVHEESSINTPAVGAAHVIKRYTARAPDELTLEVGDIVSVIDMPPKVLSTWWRGKHGFQVGLFPGHCVELINQKVPQSVTNSVPKPVSKKHGKLITFLRTFMKSRPTKQKLKQRGILKERVFGCDLGEHLLNSGFEVPQVLQSCTAFIERYGIVDGIYRLSGVASNIQRLRHEFDSEHVPDLTKEPYVQDIHSVGSLCKLYFRELPNPLLTYQLYEKFSDAVSAATDEERLIKIHDVIQQLPPPHYRTLEFLMRHLSLLADYCSITNMHAKNLAIVWAPNLLRSKQIESACFSGTAAFMEVRIQSVVVEFILNHVDVLFSGKISMVMQEGAASLSRPKSLLVSSPSTKLLTLEEAQARTQAQVNSPIVTENKYIEVGEGPAALQGKFHTIIEFPLERKRPQNKMKKSPVGSWRSFFNLGKSSSVSKRKLQRNESEPSEMKAMALKGGRAEGTLRSAKSEESLTSLHAVDGDSKLFRPRRPRSSSDALSASFNGEMLGNRCNSYDNLPHDNESEEEGGLLHIPALMSPHSAEDVDLSPPDIGVASLDFDPMSFQCSPPKAESECLESGASFLDSPGYSKDKTSANKKDAETSGSQCQTPGSTASSEPVSPLQEKLSPFFTLDLSPTEEKSSKPSSFTEKVVYAFSPKIGRKLSKSPSMNISEPISVTLPPRVSEVIGTVSNTTAQNASSSAWDTCIEERDATNRSPTQIVKMKTNETDAQEGCESEVQPLDQVAAEEVELPGKEDQSVSSSQSKAVASGQTQTGAVTHDPPQDSVPVSSVSLIPPPPPPKNVARMLALALAESAQQASTQSLKRPGTSQAGYTNYGDIAVATTEDNLPSSYSAVALDKAYFQTDRPAEQFHLQNNAPGNCDHPLPETTAVGDPTHSNTTESGEQYHQVDLTGNQPHQTYLSGDPEKARITSVPLDSEKSDDLISFPEDQSGKNSMPAVSFLDQDQSPPRFYSGDHPPSYLGASVDKPHHPLEFADKSPTPPNLPRDKIFLPSGSLADKSPTPPNLPRDKIYPSGSPEENTSTATMTYMTTTPATAQMSTKEVSWDVAEQPTTADFAAATLQRTHRTNRPLPPPPSQRSAEQPPVVGQVQAATNIGLNNSHKVQGAVPVPERPPEPRAVDDPASAFISDSGAAAAQCPMATAVQPGLPEKVRDGARAPLLHLRAESVPAHPCGFPTPLPPTRTMESKMAAAIHSSSADATSSSNYHSFVTASSASVDDALPLPLPVPQPKHASQKTVYSSFARPDVTTEPFGPENCLHFSMTPNCQYRPQSVPPHHSKLEQHQVYGARSEPPASMGLRYNTYVAPGRNASGHHSKPCSRIEYVSSLSSSVRNTCYPEDIPPYPTIRRVQSLHAPPSSMIRSVPISRTEVPPDDEPAYCPRPLYQYKPYQSSQARSDYHVTQLQPYFENGRVHYRYSPYSSSSSSYYSPDGALCDVDAYGTVQLRPLHRLPNRDFAFYNPRLQGKNLYSYAGLPPRPRANVTGYFSPNDHNVVNMPPAADVKHTYTSWDLEDMEKYRMQSIRRESRARQKVKGPVMSQYDNMTPAVQDDLGGIYVIHLRSKSDPGKTGLLSVAEGKEGRHAAKAISPEGEDRFYRRHPEAEMDRAHHHGGHGSTQPEKPSLPQKQSSLRSRKLPDMGCSLPEHRAHQEASHRQFCESKNGPPYPQGAGQLDYGSKGIPDTSEPVSYHNSGVKYAASGQESLRLNHKEVRLSKEMERPWARQPSAPEKHSRDCYKEEEHLTQSMVPPPKPERSHSLKLHHTQNVERDPSVLYQYQPHGKRQSSVAVVSQYDNLEDYHPLPQHQRGGFAGGGMGTYVPPGFPHPQSRTYATALGQGAFLPTEWSLQHPETQIHAE
The following text describes a protein:
Function:
Magnesium transporter that may mediate the influx of magnesium.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MLLPAGHDIALMLAREPSWSAYWHLSQRVLSRLLRARLLREAPPTQGPNQNLCIPPLFSLAPQVGSRASSVVGFYGRCATTSDHEIPSTHFPHDYWLHARHFSSGASSGGGGAVERSAAMEEARGRGMGGQDGSSRVMSFTAVQAHDPTKLHLAAYPRVVLCRLAGLPLRDLRSIDPAFKSQYPAILVRPACILVSLFDQRAIITAREVLVFDPESRDAWGGGRPRIPPLARLLAQRLQTNRDEPADTASPLKEEQDTMQELDSCRKCGQTRAELNGGVEAVREGSSELYAPLQALRMAQLMDRERLYRVKRDERWLRGVTESLQQAAKEAGVPLSSSVQELEARAASLAVQRREIKHRLAARQADIFRAREKVLSSRIGRTLQDGRERHAEAVTSAALVGMFSEANSVRDKLGLAPYALLPEGMAGGERKLAVGPPEECRHHWTEWECAGPRSPVTATSPAALIQRGLPEAALPFELRVLEVILDDTCRTLADKYDGLRPDVEGVLDKLEANVKHRRALQQEEQTKLMGLKTRLLRLQGEVGAIKAALESILDNDEDMSDLYLTAKAAGRPPHKDQHEEAEELLENAARRVDDVESTLSQLMEKMSFREEHMRTMLDSQRNELLRLDVRLNLGTFSIASGGTVAALFGMNLFSGLEESPYAFLAVAGSVVGLSALFYSSILRHSVKKRIL
The following text describes a protein:
Function:
Involved in the export of mRNA from the nucleus to the cytoplasm.
Subcellular Localization:
Nucleus.
Sequence:
MPRGGARGGHAIAGAALRSAGLVGDGDVGMRDAAGPSRSRAGGPGGRKAQRNGGAYSPNSNGAGSSLQGRIARQRANPLGNRPPSKGKKGAINVNDGLRAGNAADTASVLKSISSQRSRAQGGGRIPGGGGIIFAGTDMPKTQNVVSLIKRFLQSRWNPQAKFLNLENMSADPILQAEGIKPPGVAGAPKELGNVIWKLCSEIYPDVVTISLANNGFRSLGPVSSLPAYFPNLQNLSLEGNELKWTKDLDTFASRKSKLTNLKELLLTGNPVHTSAIAAGNEEGYRREVLSKFRQLTLLDQKPVTPTESGFVNLQSSTKSKKVDADAAQVPLRNFPVPNKPGFVDAEAGAIMPNFLSKFFTLYDSDRNQLSEAYAPLAQFSYCLNVVPPPRARAAGFLHTMPHQKELNFDRYQDKGNRNLMRVHTPKGRHLSLHHGVGSILAILRKLPKTSHPLNDASKFVVDAWVLANNVIGARLKGEGRPEALLYINVHGEYAEAPSQGIRSFDRTFAVAPVPPDSTAAAAGWPCVILSDQLVVRHYSSPCAWSPDSLPTGEVTAEQTQAMQAAQQGAQAAAMSQPVAAPVPAAVVAGGAALPPHLQNQAPAAGINEQQHAMSLQLAAQTGLIYPFAVQCLQENGWDYNLALANFQTLKASNAIPPQAFAQP
The following text describes a protein:
Function:
O-acyltransferase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA. 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN. Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A. Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE. Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4. The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide. Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol. Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation. Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional.
Miscellaneous:
MISCELLANEOUS: In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives.
Sequence:
MPPSPDFEAFSLTPIDQANGQVFFFYNISYRVRNEASALQTIHNAIDVLLEKVPFLNGEIAFPAPVPDANNVLIVRPPRAKSEDQVPLVQVKRHSNCALPVKKLEQSPFNVPSSLPLNGLFNPLAAYPTPNRPTPVIRFQINLVNDGLILTLAFNHAVFDALGAAVIVKLLAESCRNQDKIGMDGRLGIPSTQARVRSPLLALSSRLKKNNRARVDAPSPSEFSENISHRPVAAPPPLKDECFVFCAEKLQQLRIACTSILEKLHENQKSVTGQGDVRFLSINDVLTALICESIAQARHAAKHPYRDEKLHAKPSVSECLMAVDLRKFVEPPLPHDYMGNAAIPLRFEVSSQRHASPDFHRAVREVPTGLNTSFFLAIAKTAYTIRAKLARFGESYIDSLSSFLNAHEEQKAVNILPACAIVSSLRHIKTYELQFGAELGEIQAFETGIPWVNGSCIILPLCANSSDVAGSAPWNVRITLDESTMYCFKNEPALRWALLEQGKSKVLGPCDCKADV
The following text describes a protein:
Function:
Essential for the assembly of the mitochondrial F1-F0 complex.
Miscellaneous:
MISCELLANEOUS: Present with 6370 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion. Mitochondrion intermembrane space. Note=Mitochondrial, either as a constituent of the matrix, or in tenous association with the internal side of the inner membrane.
Sequence:
MLPSLRKGCFIVNSIRLKLPRFYSLNAQPLGTDNTIENNTPTETNRLSKTSQKFWEKVSLNRDVEKGKIALQLDGRTIKTPLGNGIIVDNAKSLLAYLLKLEWSSLSSLSIKTHSLPLTSLVARCIDLQMTNEPGCDPQLVAKIGGNSDVIKNQLLRYLDTDTLLVFSPMNEFEGRLRNAQNELYIPIIKGMEEFLRNFSSESNIRLQILDADIHGLRGNQQSDIVKNAAKKYMSSLSPWDLAILEKTVLTTKSFICGVLLLENKKDTANLIPALKTDMDNIVRAATLETIFQVEKWGEVEDTHDVDKRDIRRKIHTAAIAAFKQ
The following text describes a protein:
Function:
Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Sequence:
MSSVDPRDTIASIDTQILDLLRERCRAMTENTASNSNPDWASTLTSIDAVVDRFKQSGSGNDGTNNEMPESEIQRNILQHVASACWRATRPGTYAFLGPPDSYSHLAALAYFGEAANLLPVSSIGAVFDAVGRSDCAGGIVPIENSTDGRVVDTFGRLSKGEVSITGEVQLAIHHQLLAMCDRDSITEVHSKPQAISQCRVWLANHLPKAKLIECSSTAAAAKLAATQAGVAAIASEAAGRRHGLRVIGANIEDNRDNVTRFAVLGHEQPAPTGQDKTTLLFQVAHQPGALADVMGIFKRHELNLTWIESFPQPGTKNEYFFVVEFPGHCQDIAIAKAIEDLKTATHHTHVLGSYGRAARAES
The following text describes a protein:
Function:
RNA-binding component of the PET complex, a multiprotein complex required for the processing of piRNAs during spermatogenesis. The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposable elements, preventing their mobilization, which is essential for the germline integrity. The PET complex is required during the secondary piRNAs metabolic process for the PIWIL2 slicing-triggered loading of PIWIL4 piRNAs. In the PET complex, EXD1 probably acts as an RNA adapter. EXD1 is an inactive exonuclease.
Subcellular Localization:
Cytoplasm. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis.
Domain:
The 3'-5' exonuclease domain lacks the conserved Asp-Glu-Asp-Asp (DEDD) residues that coordinates divalent ions essential for exonuclease activity.
Sequence:
MDNLYTKGELLQVHTKNYDVFEGRFYSMAQDKTKISLYDVKEIPHGDANDGVLHYYDSEIREVVKLQESTEKKVLKISQTKYEEILKISKKYIFINQVDKSFHEAVDDLNQQDFIAVSGDGANMGRKCKMPFLVLSTDHQIYIFDIQVMQYHAFESGLKKILEGDSPKKIAHDCRKLSDCLYHKHNVKLKSVFDTQVGDLIITKNKKVTLPNKVKSLGECLTNYLGLQQNTIDEKLDIVQSTERPLSVKIKDSLARNIAFLHHLSEVINEEMQLPFYRGVECYIENIRSSDDFKAWELCGKLNQIPKEFRNAIDY
The following text describes a protein:
Function:
The active factor is excreted into the culture medium by haploid cells of the A mating type and acts on cells of the opposite mating type (type alpha). It mediates the conjugation process between the two types by inhibiting the initiation of DNA synthesis in type alpha cells and synchronizing them with type A.
Subcellular Localization:
Cell membrane; Lipid-anchor; Cytoplasmic side.
Sequence:
MQPITTASTQATQKDKSSEKKDNYIIKGLFWDPACVIA