lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Seems to link microtubules to dendritic lamellar body (DLB), a membranous organelle predominantly present in bulbous dendritic appendages of neurons linked by dendrodendritic gap junctions. May operate in the control of brain-specific organelle translocations (By similarity).
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton. Note=Localizes preferentially to the ends of tyrosinated microtubules.
Sequence:
MQKPSGLKPPGRGGKHSSPVGRPSVGSASSSVVASTSGSKEGSPLHKQASGPSSSGAATTVSEKPGPKAAEVGDDFLGDFVVGERVWVNGVKPGVVQYLGETQFAPGQWAGVVLDDPVGKNDGAVGGVRYFECPALQGIFTRPSKLTRQPTAEGSGSDTHSVESLTAQNLSLHSGTATPPLTGRVIPLRESVLNSSVKTGNESGSNLSDSGSVKRGDKDLHLGDRVLVGGTKTGVVRYVGETDFAKGEWCGVELDEPLGKNDGAVAGTRYFQCPPKFGLFAPIHKVIRIGFPSTSPAKAKKTKRMAMGVSALTHSPSSSSISSVSSVASSVGGRPSRSGLLTETSSRYARKISGTTALQEALKEKQQHIEQLLAERDLERAEVAKATSHICEVEKEIALLKAQHEQYVAEAEEKLQRARLLVENVRKEKVDLSNQLEEERRKVEDLQFRVEEESITKGDLETQTQLEHARIGELEQSLLLEKAQAERLLRELADNRLTTVAEKSRVLQLEEELSLRRGEIEELQHCLLQSGPPPADHPEAAETLRLRERLLSASKEHQRDSTLLQDKYEHMLKTYQTEVDKLRAANEKYAQEVADLKAKVQQATTENMGLMDNWKSKLDSLASDHQKSLEDLKATLNSGPGAQQKEIGELKALVEGIKMEHQLELGNLQAKHDLETAMHGKEKEGLRQKLQEVQEELAGLQQHWREQLEEQASQHRLELQEAQDQCRDAQLRAQELEGLDVEYRGQAQAIEFLKEQISLAEKKMLDYEMLQRAEAQSRQEAERLREKLLVAENRLQAAESLCSAQHSHVIESSDLSEETIRMKETVEGLQDKLNKRDKEVTALTSQMDMLRAQVSALENKCKSGEKKIDSLLKEKRRLEAELEAVSRKTHDASGQLVHISQELLRKERSLNELRVLLLEANRHSPGPERDLSREVHKAEWRIKEQKLKDDIRGLREKLTGLDKEKSLSEQRRYSLIDPASPPELLKLQHQLVSTEDALRDALNQAQQVERLVEALRGCSDRTQTISNSGSANGIHQPDKAHKQEDKH
The following text describes a protein:
Function:
Mediates the hydrolysis of some nucleoside diphosphate derivatives, possibly using both NADH and ADP-ribose as substrates.
Sequence:
MLPYLQSSAPPKEGFEYHHAEKGYVMLTYWIPEEEPCMLHANASHQVGVGRLCQYKEPLSHKIIIDNLEIKAAKWMPLVEFVDQPMIKGEKMFKPSLYYNVVHGDDPSHSNCTADFY
The following text describes a protein:
Function:
May play a role in homeostasis or cellular differentiation in cells of neural, epithelial and germline origins. May also act as a death receptor-associated anti-apoptotic protein, which inhibits the mitochondrial apoptotic pathway.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs).
Domain:
Contains 2 ubiquitin-conjugating enzyme family-like (UEV-like) regions. These regions lack the critical Cys residues required for ubiquitination but retain the ability to bind ubiquitin.
Sequence:
MSPEVALNRISPMLSPFISSVVRNGKVGLDATNCLRITDLKSGCTSLTPGPNCDRFKLHIPYAGETLKWDIIFNAQYPELPPDFIFGEDVEFLPDPSALQNLASWNPSNPECLLLVVKELVQQYHQFQCSRLRESSRLMFEYQTLLEEPQYGENMEIYAGKKNNWTGEFSARFLLKLPVDFSNIPTYLLKDVNEDPGEDVALLSVSFEDTEATQVYPKLYLSPRIEHALGGSSALHIPAFPGGGCLIDYVPQVCHLLTNKVQYVIQGYHKRREYIAAFLSHFGTGVVEYDAEGFTKLTLLLMWKDFCFLVHIDLPLFFPRDQPTLTFQSVYHFTNSGQLYSQAQKNYPYSPRWDGNEMAKRAKAYFKTFVPQFQEAAFANGKL
The following text describes a protein:
Function:
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. QCR10 has a role in CIII assembly and RIP1 stability.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MISFFPNKPMYHVQPHISFITPERTMKTIPAFSRWAFAAVAGVFVFAMQVPKVKTTILQPIAFIGDHFKDKTPEEDKWL
The following text describes a protein:
Function:
Multifunctional regulator of fatty acid metabolism. Represses transcription of at least eight genes required for fatty acid transport and beta-oxidation including fadA, fadB, fadD, fadL and fadE. Activates transcription of at least three genes required for unsaturated fatty acid biosynthesis: fabA, fabB and iclR, the gene encoding the transcriptional regulator of the aceBAK operon encoding the glyoxylate shunt enzymes.
Subcellular Localization:
Cytoplasm.
Domain:
The N-terminus binds DNA, the C-terminus (residues 83-239) is responsible for dimerization. The C-terminal domain binds acyl-CoA.
Sequence:
MVIKAQSPAGFAEEYIIESIWNNRFPPGTILPAERELSELIGVTRTTLREVLQRLARDGWLTIQHGKPTKVNNFWETSGLNILETLARLDHESVPQLIDNLLSVRTNISTIFIRTAFRQHPDKAQEVLATANEVADHADAFAELDYNIFRGLAFASGNPIYGLILNGMKGLYTRIGRHYFANPEARSLALGFYHKLSALCSEGAHDQVYETVRRYGHESGEIWHRMQKNLPGDLAIQGR
The following text describes a protein:
Function:
Specifically required for meiosis II (MII). Binds to slp1, an activator of the anapahase promoting complex/cyclcosome (APC/C), and counteracts its function in promoting proteolysis of cdc13. By suppressing the degradation of cdc13 at anaphase I this protein may help maintain a sufficient level of cdc2 kinase activity to complete MII.
Miscellaneous:
MISCELLANEOUS: Expression of the full-length mes1 protein requires the presence of the mei2 protein.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MVNTDNKENEPPNMEKAHMDSSNALYRVQRPLQRRPLQELSIELVKPSQTITVKKSKKSTNSSSYFAQLHAASGQNPPPSVHSSHKQPSKARSPNPLLSMR
The following text describes a protein:
Function:
Catalyzes the final step in the biosynthesis of the membrane lipid glucosylceramide (GluCer), the transfer of glucose to ceramide. Glucosylceramides play important roles in growth, differentiation and pathogenicity. Plays an important role in conidiation and virulence.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Domain:
The D1, D2, D3, (Q/R)XXRW motif is a critical part of the GCS active site, involved in catalysis and UDP-sugar binding.
Sequence:
MFVLSTARCTETRANKPTNHRRAEPDLTTSPRLLSSLLFSSLLSPLSTPRTRPSYNANAPSPSRTPMITLQSITDAVGLGSARYGGFQWSVALGWIGLVWYSTVTTVCALGYYKLWKHCLRRPQSSYCATAQNAPHVTVIRPVKGLEPHLYDCLASSFRQEYPRGKLTVCLCVSSRSDPAYATLEKLVADFPHVDARIYVEEEDPLLQPDHKPMYNLGPNPKIRNMSRAYREAKGDIVWIADCNVWVGKGVCGRMVDKLCGLGSGSSTEYKFVHHLPVAVDVTGVIGVDERRALETSGAARVKDGKSACAPGVLAMGGGRLEELFLSSSHAKMYTAINTVLIAPCIVGKSNMFRRSHLDYLTTTASCQFNPGIDYFSDNICEDHLIGDLLWKNRVREEKEDGKHLGKHALVFGDLAFQPIANMSVQSYIARRVRWLRVRKFIVMLATLVEPGTESILCSLYGAWGVTTVLAEYFQNKILSTWTTFFTFFGFSILTWCLIDWTVYIMLHSGKTVERDENTPSFARPPQGTTRRRFSHWLAAWLGREILAFPIWFWAIWGGMTVTWRDRQFRIGLDTKAHEIGGNSRAGLLEEQASGRENENEATSLITTAVKRQTRGNR
The following text describes a protein:
Function:
Carrier protein involved in proton-driven auxin influx. Mediates the formation of auxin gradient from developing leaves (site of auxin biosynthesis) to tips by contributing to the loading of auxin in vascular tissues and facilitating acropetal (base to tip) auxin transport within inner tissues of the root apex, and basipetal (tip to base) auxin transport within outer tissues of the root apex. May be involved in lateral roots and nodules formation.
Subcellular Localization:
Cell membrane. Endomembrane system; Multi-pass membrane protein.
Sequence:
MNLEQGQEKGTQNDGYGRASAHTTDRDSWHQVGLMLVTSFNCGWILSFSNLVMWPLGWTWGIICLIVVGFYTAYANWLLAAFHFIDDRRFIRYRDLMGYVYGKGMYQLTWVFQFLTLLLGNMGLILLGGKALKAINSEFSDSPLRLQYYIVITGAAYFFYSFFFPTISAMKNWLGASAVVTFTYIIFLLIVLIKDGRSNSNRDYDIGESEVMNKVFNAFGAISAIIVCNTSGLLPEIQSTLRKPAMKNMRKALYLQYTVGVLFYYGVTVMGYWAYGSMVSAYLPENLSGPKWIDVLINAIVFLQSIVTQHMFVAPIHEALDTKFLEIDKAMHSGENLKRLFLLRALFFTGNTFVAAAFPFMGDFVNFLGSFSLVPLTFMFPSMVFIKVKGRTARIEKKAWHWFNIVFSFLLTIATTISAIRLIVNNIQKYHFFADA
The following text describes a protein:
Function:
Tethering component of the holoenzyme telomerase ribonucleoprotein (RNP) complex. Telomerase is an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER. In the telomerase holoenzyme complex, acts as a hub that anchors the two heterotrimeric subcomplexes with the catalytic core.
Subcellular Localization:
Chromosome, telomere.
Sequence:
MKLLLQNQNIFQKLKNTLNGCIKKFYDTYQDLEQMQKFEMIVEDKLLFRYSCSQSEMFSAQIQAHYLEKRVLQLTDGNVKYIVNFRDKGVLDKANFFDTPNNSLVIIRQWSYEIYYTKNTFQINLVIDEMRCIDIITTIFYCKLELDFTQGIKGISKSSSFSNQIYEYSAQYYKAIQLLKKLLINDSYISELYNSTKSKQQPRLFIFQSFKPKMNLAEQNLSRQFEQCQQDDFGDGCLLQIVNYTHQSLKQIENKNNSNQIVNGQNEISKKKRVLKSNEDLYKISLQKQLKIFQEEEIELHSQSTIRNQTNQQLETFESDTSKRNSEKILHSINELNTSKQKVNQMNSSQHQIQKLENNNLNKNILNQINENDIKNELEERQQQHLTQSFNSKAQLKKIITLKKNQDILLFKPQEQEGSKKY
The following text describes a protein:
Function:
Binds with low affinity to interleukin-13 (IL13). Together with IL4RA can form a functional receptor for IL13. Also serves as an alternate accessory protein to the common cytokine receptor gamma chain for interleukin-4 (IL4) signaling, but cannot replace the function of IL2RG in allowing enhanced interleukin-2 (IL2) binding activity.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MEGPVILCLLWAAGVLGTPATSSEIPTEAHPPPVINFSVSVKNLCTIYWIWSPPEGVNAKCELWYKSHLGEEKMVSKNNFRIEEVALNERICLQVTSQCNVESTNTSDPVEMCIEPPQGDPETAVKRLQCIWHNLSKMNCIWLPGKTAPPDTKYILHYWYNTLEKSLQCTNFYVEGQFNGCSFDLLEKDVSSSDKIQIMVTDTTGAIRPSYNIINLNNVKPDHPILTNLSLQNASLYVEWESPANFRSNCLVYQVEVNNSKSMEHKVHEPKSKCHISETPPEPEGNSKNKHCFVIHDVDPDAPYTVRVRAKASRFCFEDNDLWSAWSQKKHIGQNHDSKIHTITLLFIPVAISISTLLLLLYLKRLKIIIFPPIPDPGKIFKEMFGDQNDDTLQWKKYDIYEKQIKEETDSVVLVENLKRTSQ
The following text describes a protein:
Function:
Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. Also acts as a decay-accelerating factor, preventing the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade. Seems to act as a costimulatory factor for T-cells. May play a crucial role in early embryonic development by maintaining fetomaternal tolerance.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MEASSPLDPVGRLVAFCRGGVHLAVLLLFLSPSTLGQCPAPPLFPYAKPINPTDESTFPVGTSLKYECRPGYIKRQFSITCEVNSVWTSPQDVCIRKQCETPLDPQNGIVHVNTDIRFGSSITYTCNEGYRLIGSSSAMCIISDQSVAWDAEAPICESIPCEIPPSIPNGDFFSPNREDFHYGMVVTYQCNTDARGKKLFNLVGEPSIHCTSIDGQVGVWSGPPPQCIELNKCTPPHVENAVIVSKNKSLFSLRDMVEFRCQDGFMMKGDSSVYCRSLNRWEPQLPSCFKVKSCGAFLGELPNGHVFVPQNLQLGAKVTFVCNTGYQLKGNSSSHCVLDGVESIWNSSVPVCEQVICKLPQDMSGFQKGLQMKKDYYYGDNVALECEDGYTLEGSSQSQCQSDASWDPPLPKCVSQVICKLPQDMSGFQKGLQMKKDYYYGDNVALECEDGYTLEGSSQSQCQSDASWDPPLPKCVSRSNSGLIAGIFIGIIVLILFIIFSYWMIMKFKKRNSTNEKCKEVGIYLNSKEDSCVQPQSLLTSQENNSTSSPARNSLTQEV
The following text describes a protein:
Function:
Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Acts as a positive regulator of Wnt signaling pathway by promoting beta-catenin (CTNNB1) nuclear accumulation (By similarity). Required for normal Wnt signaling and normal dorsoventral patterning during embryogenesis.
Sequence:
MSYSEKPEDITKEEWMDKLNNVHIQRADMNRLIMNYLVTEGFKEAAEKFRMESGIEPNVDLDSLDERIKIREMVLKGQIQEAIALINSLHPELLDTNRYLYFHLQQQHLIELIRLRETEAALEFAQSQLAEQGEESRECLTEMERTLALLAFDNPEESPFGDLLNMMQRQKVWSEVNQAVLDYENRESTPKLAKLLKLLLWAQNELDQKKVKYSRMTDLSKGTIEDPK
The following text describes a protein:
Function:
Phospholipid scramblase involved in lipid homeostasis and membrane dynamics processes (By similarity). Has phospholipid scramblase activity toward cholesterol and phosphatidylserine, as well as phosphatidylethanolamine and phosphatidylcholine (By similarity). Required for autophagosome formation: participates in early stages of autophagosome biogenesis at the endoplasmic reticulum (ER) membrane by reequilibrating the leaflets of the ER as lipids are extracted by ATG2 (ATG2A or ATG2B) to mediate autophagosome assembly (By similarity). Regulates ATP2A2 activity to control ER-isolation membrane contacts for autophagosome formation. In addition to autophagy, involved in other processes in which phospholipid scramblase activity is required (By similarity). Modulates ER contacts with lipid droplets, mitochondria and endosomes (By similarity). Plays an essential role in formation of cell junctions (By similarity). Upon stress such as bacterial and viral infection, promotes formation of cytoplasmic vacuoles followed by cell death. Involved in the cytoplasmic vacuolization of acinar cells during the early stage of acute pancreatitis.
Subcellular Localization:
Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Vacuole membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Colocalizes with MAP1LC3A and BECN1.
Domain:
The VTT domain was previously called the SNARE-assoc domain. As there is no evidence that this domain associates with SNARE proteins, it was renamed as VMP1, TMEM41, and TVP38 (VTT) domain.
Sequence:
MAENGTNCDQRRGAMSKEQHNGSFTDPSSVNEKKRRDREERQNIVLWRQPLITLQYFSLETLVVLKEWTSKLWHRQSMVVSFFLLLAALVATYYVEGAHQQYVQRIEKQFLLYAYWIGLGILSSVGLGTGLHTFLLYLGPHIASVTLAAYECNSVNFPEPPYPDQIICPDEEGTEGAISLWSIISKVRIEACMWGIGTAIGELPPYFMARAARLSGAEPDDEEYQEFEEMLEHAETAQDFASRAKLAVQKLVQKVGFFGILACASIPNPLFDLAGITCGHFLVPFWTFFGATLIGKAIIKMHIQKIFVIVTFSKHIVEQMVAFIGAVPGIGPSLQKPFQEYLEAQRQKLHHRSEAGTAQGENWLSWTFEKLVVAMVCYFILSIINSMAQSYAKRIQQRLNSEEKTK
The following text describes a protein:
Function:
Ubiquitin-conjugating enzyme E2 that is essential for peroxisome biogenesis and plays a key role in development, pathogenicity, and cell wall integrity. Required for long and very long-chain fatty acid utilization and is involved in lipid droplet accumulation and the elimination of reactive oxygen species. Controls the expression of proteins involved in protein biosynthesis, fatty acid metabolism, cell wall synthesis, oxidation-reduction reactions, as well as of the enzymes involved in the biosynthesis of the mycotoxin deoxynivalenol (DON), including TRI5, TRI6, and TRI10.
Sequence:
MPPSSSNTAAASRSASKRLIKELETWSREQKEEKGIERLGPVNEGDLMEWEAVINGRGIGQGYDEGRWLVNISIPSTYPLAPPKMTFVTPIVHPNIALQNGEICLDLLKDAWTPAYSVLECVRAVRMLLGCPETDSPLNVDVAALLRSGDVLGTRKLVELWCQDSDSRYEGP
The following text describes a protein:
Function:
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Sequence:
MATGFNPDWYYAVVVGRCTGIYTDVDDALCHTKHYSHAKFKKFPTFSEARGFLNQHALGVGNALKYADGSRIWFAYRVNGGRDDCPDPKHPDTLAAFCDGSAVRNGQPDCTAAFACIFPHNRDWDVVKPLTGRKQTNNRAEYLAALAALERANRMNYNQNKVLYIFSDSKLLIQSMTVWIYKWQSNGWQALSGTTVKNRDVLEKLLDAQGNRQVEWHHVTAHSGTVDWESHWNNVADRAARELARSTYNEN
The following text describes a protein:
Function:
Catalyzes the hydrolysis of the N-glycosidic bond of commonly occurring purine and pyrimidine nucleosides into ribose and the base, with decreasing activity, in the order: adenosine, guanosine, inosine, xanthosine, cytidine, uridine.
Sequence:
MTVDKVKLVIDSDGVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDRSNIPVYKGAAKSILSLPKDDTVSDFFGIDGIGDKPEEFPKVERSDFEGEGKHASLALIDILRENRDATLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGNYYAVGNVDGGSSAEYNFHGDPEAASIVLRRMKCPITIVPWEAFYFESKTHDASVDFSAHLKYGTPLANYLSLATSIGRVKCEANGRQYSYCDEIAVATAIDEDKIAKKSQYLYVDVELNGTKTRGQVVVDWTEQLWSNEEAPNQHTHRRVKFVTSYDVHTVDKWLHAATSGSGKFD
The following text describes a protein:
Function:
FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of viriditoxin, one of the 'classical' secondary metabolites produced by fungi and that has antibacterial activity. The first step is performed by the polyketide synthase VdtA which condenses one acetyl-CoA and 6 malonyl-CoA units to form the heptaketide monomer backbone of viriditoxin. The product of VdtA is then O-methylated on C7 by the O-methyltransferase VdtC. The O-methyl group is important for the stereoselective coupling of the monomers at the final step of viriditoxin biosynthesis. The short-chain dehydrogenase/reductase VdtF then acts as a stereospecific reductase converting the pyrone to dihydropyrone via the reduction of the C3-C4 double bond. The FAD-binding monooxygenase VdtE then converts the ketone group into a methyl-ester group to yield semi-viriditoxin. Finally, the laccase VdtB is involved in dimerization of 2 semi-viriditoxin molecules to yield the final viriditoxin. VdtB is responsible for the regioselective 6,6'-coupling of semi-viriditoxin, which yields (M)-viriditoxin and (P)-viriditoxin at a ratio of 1:2. The non-catalytic carboxylesterase-like protein VdtD affects the stereochemistical outcome of the coupling. The highly reducing polyketide synthase VdtX is not involved in viriditoxin synthesis, but might possibly play a role in the production of additional metabolites not identified yet.
Sequence:
MASMQEVDALVVGAGFGGLWMTNRLKEAGLNVLCVEKAPQAGGVWYWNCYPGARVDSRYPVYQYSDESLCKDWNWSELFPGYEEIRKYLSYAVDKWQLNSHIRYNTTVTGARFDESDHKWTVEGINGSHGTIRIRCRWYILALGFASKPYIPDFEGLNRFQGPCFHSSAWPQEGIDLKGRRVAVVGTGASAVQIIQTISKEVGHLTVYQRTPCTAMPMRQQSLTPEYQDNFKASGEMAATMRRTKYERFGGQDVQFVSRRWHEDTPEQRRAVFEQAWQKGGFHLLLSTYFEVFDDVEVNHAAWRFWAEKSRERIHNTKYKDILAPLEAVHAFGGKRTPFEQDYFEAFNRRNVDLIDMKASPILSFAEKGIITQNEGLQEFDVIILATGFDTNTGALTSIHIQDTDGILLKDRWSYDGVMTTFGMSTSKFPNMFFFYGPQAPTAFSNGPSCIELQGEFVEELILDMIGKGVTRVDTTSEAEKRWKESTLSLWNQFVFSSTKGFYTGENIPGKKAEPLNWFGGFPRYRKALTECRDGGYKEYSLRSLPKVPDPEHRGLIDKVAVVTSAQPVGA
The following text describes a protein:
Function:
Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Subcellular Localization:
Nucleus.
Domain:
The N-terminal half of the protein contains two conserved domains I and II. Domain I includes a slightly degenerated ERF-associated amphiphilic repression (EAR) motif which seems to be involved in the activity of transcriptional repression. Domain II is required for the correct degradation of the protein through the SCF-mediated ubiquitin-proteasome pathway. Interactions between Aux/IAA proteins and auxin response factors (ARFs) occur through their C-terminal dimerization domains III and IV.
Sequence:
MEGCPRNREIGPKLLDLIPQGRKWYQEDKNNTDQEKKLELRLGPPGGDEEDHSAIKKKNTEIRNIKKETEDKSFHCFNGNHFSPSNKTTSVPHISQKRTAPGPVVGWPPVRSFRKNLASTSSSKLGNESSHGGQINKSDDGEKQVETKKEGMFVKINMDGVPIGRKVDLNAYNSYEQLSFVVDKLFRGLLAAQRDISDGQGEEKPIIGLLDGKGEFTLTYEDNEGDKMLVGDVPWQMFVSSVKRLRVIKSSEISSALTFGCSKQEKMMH
The following text describes a protein:
Function:
Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1.
Sequence:
MSEGTKEPDGGEEKVVLKTHDGQEFTVDMATANRSGTLKNLLSEVGGSSDNPQVIPLPSSITSPVLGKVVEYCQRHAGGGGGTGGVQALEQFDEELVELDKDMLLDVTYAAAFLDVPRLLDLTSQAVADAIKKMSVEEVRHYFGVVSDFTEEEEKVIRSECPWAFE
The following text describes a protein:
Function:
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
Subcellular Localization:
Cytoplasm.
Sequence:
MILKRISILNYKNLEQVEIGFSAKLNCFFGQNGMGKTNLLDAVYFLSFCKSSGNPIDSQNIRHEQDFFVIQGFYEAEDGTPEEIYCGMKRRSKKQFKRNKKEYSRFSDHIGFLPLVMVSPADSELIAGGSDERRRFMDVVISQYDKEYLEALIRYNKALAQRNTLLKSEFPVEEELFLVWEEMMAQAGEIVFRKREAFIEEFIPIFQSFYSFISQDKEQVGLSYDSHARDASLLEVLKQSRERDKIMGFSLRGIHKDELNMLLGDFPIKKEGSQGQNKTYLVALKLAQFDFLKRTGQTVPLLLLDDIFDKLDASRVEQIVKLVAGDNFGQIFITDTNREHLDRILQKVGSDYKVFRVDQGVINEMGAEQ
The following text describes a protein:
Function:
Catalyzes the deacetylation of acetylated polyamines such as N-acetylputrescine and N-acetylcadaverine. Plays an important role in the metabolism of acetylated polyamines in P.aeruginosa. Is involved in the degradation pathways of N-acetylputrescine and N-acetylcadaverine, that allow P.aeruginosa to utilize these acetylpolyamines as a carbon source under glucose starvation. Shows nearly no activity against N(1)-acetylspermine and N(1)-acetylspermidine. Can also hydrolyze artificial trifluoroacetylated lysine-derivative, and to a lesser extent, acetylated lysine-derivative.
Sequence:
MLTIYSDDHRLHHGRHELIGGQFTPCFEKPSRADMVLDRVKAVGLGEVRAPRDFGLEPIRRVHSEGFVRFLQNAWQDWLATGRSHDMLPIAWPTRRLRQTEPDNIDGRLGYYSFDAGAPITAGTWQAITSSANVALSGQSELANGARSVFSLCRPPGHHAAADYMGGYCFFNNAAIAAQAFLDRGAGRVAILDVDYHHGNGTQDIFYDRADVLFTSIHGDPRFEYPYFLGYADEKGNGVGTGYNFNYPLAAGSDWATWSQALQAAIRQIQAYAADALIVSLGVDTFKEDPISQFRLDSPDYLRMGEAIGKLGLATLFVMEGGYAVEEIGINAVNVLQGFEGVHR
The following text describes a protein:
Function:
Protein with different functions depending on its subcellular location: involved in miRNA processing in the nucleus and acts as a tRNA pseudouridylate synthase in the cytoplasm. In the cytoplasm, acts as a pseudouridylate synthase by catalyzing synthesis of pseudouridine(54) and pseudouridine(55) from uracil-54 and uracil-55, respectively, in the psi GC loop of a subset of tRNAs. tRNA pseudouridylate synthase activity is enhanced by the presence of 1-methyladenosine at position 53-61 of tRNAs. Does not show tRNA pseudouridylate synthase activity in the nucleus. In the nucleus, promotes primary microRNAs (pri-miRNAs) processing independently of its RNA pseudouridylate synthase activity. Binds pri-miRNAs. Modulator of TRAIL/TNFSF10-induced cell death via activation of procaspase-8 and BID cleavage. Required for the progression of the apoptotic signal through intrinsic mitochondrial cell death.
Subcellular Localization:
Nucleus. Cytoplasm. Mitochondrion. Note=Localizes mainly in the nucleus. tRNA pseudouridylate synthase activity is restricted to the cytoplasm. Translocates from nucleus to mitochondria during TRAIL-induced apoptosis.
Sequence:
MLPLTEENKHVAQLLFSSGTCPRCILRFCGVDLPAPYKHPSKELLNELQKFLEPEKPELILEAPNPPLKKIRLHEDGIDNLSEDGKEGVSVTEDESMAEKPSKLRVCNVCLGILQEFCEKGFITKVCQKVEASGFEFTSVVLSVSFPPQLSVREHAAWLLVKQEMGKQSLSLGRNDVVQLKEAYKWITHPLFSEELGVPTDGKSLFEVSVVFAHPETAEDCHFLGEVCRDCFKPAKNKQSVFTRMAVLKALSKIKEEDFLGQFPCPPNSPKTVCTVLEVECTHGAVFVAGRYNKYSRNLPQTPWIIDGERKMESSVEELISDHLLAVFRAESFNFSSSGREDVDVRTLGNGRPFAVELLNPHRVHFTSQEMKELQQTINKSSDKIQVRDLQLVTREAIGHMKEGEEEKTKTYSALIWTNRAIQKKDIGFLDDLKDLKIDQKTPLRVLHRRPLAVRTRAIHSMKTHYLDEHHFRLHLKTQAGTYIKEFVHGDFGRTKPNLGSLMNVTADILELDVESVDVDWPPALDD
The following text describes a protein:
Function:
Catalytic component of the DSC E3 ubiquitin ligase complex which is required for the srbA transcriptional activator proteolytic cleavage to release the soluble transcription factor from the membrane in low oxygen or sterol conditions. Required for growth during hypoxia and triazole drug susceptibility, as well as for virulence in a murine model of invasive pulmonary aspergillosis (IPA).
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein.
Sequence:
MPSQNSDVRALLIVLILLWIFFSPDSSDPASLTPPEIAHAREARFQGALDVLNTTRWGDFAPDAPSSTSPRPPSETDGPAGEIGKGNGDKHEQGPQFLNITGFSQLDGKGYAWEDLGRFRNRCREWSRNAFPSAATVGPLDDDSWEPSMVSGTWKNATGTLHGTWVRRPGTVVRQAAEYNLSAIAPGATWPSSLGEWGRNITGDHGKIELRIDEDEGDGVYEEKVEGKTSRGANLAREIQAVATIQDDASEASSWSLLLHGVHWPRQGAILLTTSSEKFDGIFGLPHLAPGPNFFHTGQHLLNETLGKIIQARKKSKYGFPGNPWGSRMEDDDSFPAQCEYVMYLQLQPLELSRQYESPQLLESYIEELERELRHPTGAPIGRIPDLRASMVAWSPDCSFFLESKGPPEFPSVDGEHLVGMKEAMFTYTAKEWLIAFAAVMLGQIWLFKEQMKLSNTPSTTGRVSFWTIGAMLFADGMIFVTACAWSLNATITLLPCLLVTFAAFISMFIEGAFLSEVWKIQEPERRIREREREQAAAAAAAAAAANRNASSSSAASTTPPPTTQPEPPTTQPAPPPPPSQPRQPIIVPSDGDIDEAEQLNNLLSGASALPLPATARQPGLPAPTNEPRPPTPFSTITGRFVLAGLFLLFISAVATSWPSHIRSFYVNTLSFLYLSLWTPQIIRNAQRNSRQAFSWRFMIGQSLLRLLPFAYFFLREDNVLLADPDPFAFLVLVAWVWIQLWVICAQSILGPRFGVPKGWVREAWDYHPVLRDDDLEGVSLPIGLARTGTGLSSSSSSSSPTEERVRGRAWSVVSLGGPAAAAETGEGSAAAAAAAAATDSAGGTRNREREKEKEREKQKGVTMRSVDCAICRELLEVPVFNNNKGSGGSSDSAASGITGVFARKAYMVTPCRHIFHTNCLEGWMKYRLQCPICREELPPL