lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression.
Sequence:
MPGDISYDICVIDENNIQETNVVELERLTEYESSEAQLSPSEEEATSTCSSTSKRDSLNGGYIPNNEEKQAQMAKQKLLTRKSHSTSEIETSGAHLQVKYQLETTETRCSAVYRKISPQVLIRTMLEMTEEEFAKKYSLYDCRFSYEFNGGSIKGAKNLDDPDKARETFFDEDGNRKSDTTPIFFCEYSQKRGPRMADTLRSTDRFLHPEMYPQCAYEEIYVLNGGYKNFFSCARALSVSNKLCDPDNYAAMDDPKFAEEFESQQLYKKLTKRILSKPSKSKTTSLRKTASSSSCFFKQRLV
The following text describes a protein:
Function:
Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Plays a role in replication-dependent histone mRNA degradation. Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking an RNA moiety. The presence of a N(6)-methyladenosine methylation at the second transcribed position of mRNAs (N(6),2'-O-dimethyladenosine cap; m6A(m)) provides resistance to DCP2-mediated decapping. Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degradation of their transcripts.
Subcellular Localization:
Cytoplasm, P-body. Nucleus.
Sequence:
METKRVEIPGSVLDDLCSRFILHIPSEERDNAIRVCFQIELAHWFYLDFYMQNTPGLPQCGIRDFAKAVFSHCPFLLPQGEDVEKVLDEWKEYKMGVPTYGAIILDETLENVLLVQGYLAKSGWGFPKGKVNKEEAPHDCAAREVFEETGFDIKDYICKDDYIELRINDQLARLYIIPGIPKDTKFNPKTRREIRNIEWFSIEKLPCHRNDMTPKSKLGLAPNKFFMAIPFIRPLRDWLSRRFGDSSDSDNGFSSAGSTPAKPTVEKLSRTKFRHSQQLFPEGSPGDQWVKHRQPLQQKPYNNHSETSDLLKAKNQSLRGNGRKQYQDSPNQKKRANGVHSQPAKQQNPLMKCEKKLHPRKLQDNFETDAVYDLPCSSEDQFLEHAEGQSVACNGHCKFPFSSRTFLSFKFDHNAIMKILDL
The following text describes a protein:
Function:
Plays a role in embryonic development, including proper left-right asymmetry formation. Also required for proper cilia beating. Plays a role in microtubule (MT) stabilization and this stabilization involves the maintenance of NUMA1 at the spindle poles. Colocalizes with polyglutamylated MTs to promote MT stabilization and regulate bipolar spindle formation in mitosis. Binding of CCSAP to centrosomes and the spindle around centrosomes during mitosis inhibits MT depolymerization, thereby stabilizing the mitotic spindle (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, cilium axoneme. Cell projection, axon. Cell projection, cilium. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Localizes at specific foci at the apical surface of neuroepithelial cells where cilia form along the brain ventricle lumen.
Sequence:
MVTKRIRSEYMKKFKDPKWDTYAKCYEDLLKYRLSRRLLEQAHKPWFWGEWGSETASSGKSTPLSRNKVEPLKTLDEKPERSACVTPEPAAEAETQAAEVQDREHADTNLVPCDAEVAHPEGEEVRGKERSPAVNPDSDTQIQNMSKSKRRSSHKYTRSKVKPQAPKDPDKENRHPFALYGAGEKQTDMASKKTHNVGPAASTAEIHESALRAKTRREVEKQIKRFDKQRARSADLEKSRNKIIPDFNPWMTEYMRCFSARSR
The following text describes a protein:
Function:
Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. Restricts the CLOCK and BMAL1 localization to the cytoplasm. Plays a role in both the input and output pathways of the circadian clock: in the input component, is involved in modulating the magnitude of photic entrainment and in the output component, contributes to the regulation of a variety of liver clock-controlled genes involved in lipid metabolism.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MKAFSPVRSVRKNSLSDHSLGISRSKTPVDDPMSLLYNMNDCYSKLKELVPSIPQNKKVSKMEILQHVIDYILDLQIALDSHPTIVSLHHQRPGQNQASRTPLTTLNTDISILSLQASEFPSELMSNDSKALCG
The following text describes a protein:
Function:
Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities.
Subcellular Localization:
Cytoplasm.
Sequence:
MDNNNAFQLSFDEQHYAWLAIDVPGEKMNTLQAAFAEEMQAVFATLNEKRGQIKGLIIHSLKPDNFIAGADVRMLEACQSVHEAQALASQGQQMFQQLADLPFPVVAAIHGPCLGGGLELALACDYRVCTEDEVTRLGLPEVMLGLLPGSGGTQRLPRLIGLLPALDLILTGKQLRAKKAKKLGVVDACVPHSVLLDVAKRLLEEKGHKKRAQVTLPIKEKLLANTDLGRKLIFDQAAKKTQQKTRGNYPAAQAILEVIQYGLEKGMHAGLEYEAKRFAELVMTRESKALRSIFFATTEMKKDLGADAKPAPVAAVGVLGGGLMGAGISHVTVAKAKTSVRIKDVANDGVLNALNYNYKLFDKQRQRKILTKAQLQAQMSQLSGGTGFVGFDRCDVVIEAVFEDLKLKQQMVADIEANAKPTTIFATNTSSLPIHQIASQAQRPQNIVGLHYFSPVEKMPLVEVIPHATTSDETIATVVTLARKQGKTPIVVKDCAGFYVNRILAPYMNEAAQVLMAGEPIEKLDAALLDFGFPVGPITLLDEVGVDIGAKIMPILVKELGPRFQGPDVFDVLLKDNRKGRKSGKGFYTYKGSKKKEVDKSVYKLLKLTPESKLNDKEIAMRCLLPMLNEAVRCLDEGIIRSARDGDMGAIFGIGFPPFLGGPFRYMDTLGLTKVVEMMNQHTEKYGERFAPCDGLLTRAGLGEKFYP
The following text describes a protein:
Function:
NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L-allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate. Able to catalyze the reduction of the malonic semialdehyde to 3-hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimidine degradation since both are able to detoxify malonic semialdehyde.
Miscellaneous:
MISCELLANEOUS: L-threonine, D-allo-threonine, DL-threo-3-phenyl-serine, malonate, DL-malate, citrate, isocitrate, DL-lactate, DL-tartrate, gluconate, glycerol and glycolate are inert as substrates.
Sequence:
MIVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWCNIDILVNNAGLALGMEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLVGGTEFSNVRFKGDDGKAEKTYQNTVALTPEDVSEAVWWVSTLPAHVNINTLEMMPVTQSYAGLNVHRQ
The following text describes a protein:
Function:
Aerial growth, conidiation, and dispersal of filamentous fungi in the environment rely upon a capability of their secreting small amphipathic proteins called hydrophobins (HPBs) with low sequence identity. Class I can self-assemble into an outermost layer of rodlet bundles on aerial cell surfaces, conferring cellular hydrophobicity that supports fungal growth, development and dispersal; whereas Class II form highly ordered films at water-air interfaces through intermolecular interactions but contribute nothing to the rodlet structure (Probable). RodA is a class I hydrophobin involved in the morphogenesis of the dispersible conidia and the resistance to environmental stress. RodA alone is responsible for rodlet formation, sporulation, conidial hydrophobicity, resistance to physical insult or anionic dyes, and immunological inertia of the conidia. Acts as a virulence factor that masks host Dectin-1 and Dectin-2 recognition of conidia, resulting in impaired neutrophil recruitment to the cornea and increased fungal survival and clinical disease.
Subcellular Localization:
Secreted. Spore wall.
Sequence:
MKFSLSAAVLAFAVSVAALPQHDVNAAGNGVGNKGNANVRFPVPDDITVKQATEKCGDQAQLSCCNKATYAGDVTDIDEGILAGTLKNLIGGGSGTEGLGLFNQCSKLDLQIPVIGIPIQALVNQKCKQNIACCQNSPSDASGSLIGLGLPCIALGSIL
The following text describes a protein:
Function:
Histone reader involved in homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks (By similarity). Specifically recognizes and binds histone H3.1 lacking methylation at 'Lys-27' (H3K27me1).
Subcellular Localization:
Nucleus, nucleoplasm. Chromosome.
Sequence:
MGRDEMQMSEAKRAYRSAKEEGNRQEEARWANVIGDILKNRGEYVEALKWFRIDYDVSVKYLPEKHLLPTCQSLGEVYLRLEHFKDALIYQKKHLELAKDASDLVEQQRACTQLGRTYYEMFLRSDDDHYSIRNAKKYFKSAMKLAQTLKENPATSRSSFLKEYIDAHNNIGMLQMELDNLEEAKKLLIRGLEICNEEEVSEDDDGRSRLHHNLGNVYMELRMWDKSREHIEQDIIICKKIEHRQGEAKGYINLGELHYRVQKYDEAILCYQKALNLAQSMEDEDALASQIDQNIETVKKAIEVMDELKKEEQNLKKLTRNMIIAKGTSQERKSLLQQNASLDCLIEKSSMIFAWLKHCEYAKRKKRIASELCDKGKLSDSFLVIGESYQKLRKFNKAIKWYTKSWEMYKSIGNLEGQALAKVNMGNVLDSNGDWAGALDAFQEGYRIAVEANLPSVQLSALENMHYSHMIRFDNIEEARRLQHEIDKLKESKSEDLEAYDVAKDCCSETDTEGNDHLPDVRSSACFSAEMSKSDSGRSKTLAGLEEVEDDEPLISFLRSSERLPKLKRAYVEKQNIPTEPRELTPKTLSKSTNSQQTGGGRKRIRVVLSDDEGDIDNEEGLKGRLQKCPVEGVATFDASRWFILLVWQDVPAADFKCTNSSENPINVEESTCSHKFTSSNPTNQYGNAIRCTGKVFIASDVNDDQCVTFRIDDDLIQLEVHSCICDDKLDIESLKVELACLYYLQLPKEKISKGLLPIIQHMKYGGRSLESFDAFKDQLGKDIIEVSIDGWVQKRLMKLYIECCKELSEAPNMKLLKKLYISEVEDEVVVSECELQDISVTPLLNALQTHKTVAMLDLSHNLLGNGTMEKLQQFFISSCQNYVDLTLDLHCNRFGPTTLFQICECPVLFTRLGVLNLSGNRLTDACGSYLSTILKNCKVLYSLNIENCSITSRTIQKVADALGAESTLAQLCIGYNSPVTGNAITNLLVKLDTLKSFSELNLNGLKLSKPVVDRLCQLAKTSCLTHLMLGCTNLGSDGSLQLVESLFSRAQESVKLDLSYCGLESTCIHKFTASVSLVHGILELNLGGNPIMKEGANALASLLMNPQCCLKVLVLSKCQLGLAGVLQLIKALSENDTLEELNLADNASKELTLQQNLSSVNSENLQPALKTSDGVSKEVDTDQQGLCAMNTDCNDLEVADSEDDKIRVESAASGFDNSCTSSCQKNSSFECQFIQELSSAIGMAKPLQLLDLSNNGFSTQAVKTLYSAWSSRSGAGPTWKHIKEQIIHFSVEGNKCCRVKPCCRKN
The following text describes a protein:
Function:
Non-catalytic subunit of the heterodimeric RalGAP1 and RalGAP2 complexes which act as GTPase activators for the Ras-like small GTPases RALA and RALB.
Sequence:
MYSEWRSLHLVIQNDQGHTSVLHSYPDSVGREVANAVVRPLGQALNSSSAAGNESFLKTDKEVKWTMEVICYGLTLPLDGDTVKYCVDVYTDWIMALVLPKDSIPLPIIKEPNLYVQSILKHLQNLFVPRQEQGSNQIRLCLQVLRAVQKLARESTTMARETWEVLLLFLLQINDTLLAAPTVQGGIAENLAEKLIGVLFEVWLLACTRCFPTPPYWKTAKEMVGNWRHHAAVVEQWSKVICALTSRLLRFIYGPSFPPFKVPDEDASLIPPEMDNECIAQTWFRFLHMLSNPVDLSNPAIVSSTPKFQEQFLNVSGMTQELNQYPCLKHLPQIFFRAMRGISCLVDAFLGISRPRSDSAPPTPVNRLSMPQNTAPINTTPPHNRRHRAVTVNKATMKTSTVSTAHASKVQHQTSSTSPLSSPNQTSSEPRPLPAPRRPKVNSILNLFGSWLFDAAFVHCKLHNGINRDSSMTASFIQILLSYKSSITTQTNMEFRRKGSQLSTDTMTSNPMFDASEFPDNYEAGRAEACGTLCRIFCSKKTGEEILPAYLSRFYMLLIQGLQITDYVCHPVLASIILNSPPLFCCDLKGIDVVVPYFISALETILPDRELSKFKTYINPIELRRSSINILLSLLPLPHHFGTVKSEVVLEGKFSNDDGFSNDKPVTFLSLKLRLVNILIGALQTETDPNNTQMILGAMLNIVQDSALLEAIGCQMEMNGGENNLKSHSRTNSGISSASGGSTEPTTPDSERPAQALLRDYALNTDTAAGLLIRSIHLVTQRLNSQWRQDMSISLAALELLSGLAKVKVVVDSSDRKRAISSVCSYIVYQCSRPAPLHSRDLHSMIVAAFQCLCVWLTEHPDMLDEKDCLREVLEIVELGISGSKSKSSEQEVKYKGDKEPNPASMRVKDAAEATLTCIMQLLGAFPSPSGPASPCSLVNETTLIKYSRLPSINKHSFRYFVLDNSVILAMLEQPLGNEQNDSFPSVTVLIRGMSGRLAWAQQLCLLPRGAKANQKLFLPEPRPVPKNNVGLKYSVKHRPFPEEVDKIPFVKADLSIPDLHEIVNEELEDRHEKLRNDMSQQIAYEIALDQQSEEEWRKKSFPDPITDCKPPPPAQEFQTARLFLSHFGFLSLEALKEPTNSRLPPHLIALDSTLAGFFDDIGYLDLLPCRPFDTVFIFYMKAGQKTSQEILRNAESSRNVQPHFLEFLLSLGWPVDVGKHPGWTGHVATSWSINSCGDGEGAEQDEVVSCEDSGASVFNGQKKVLYYADALTEIAFVIPSPVESLTDSLESNISDQESDLHMDLLPGILKQPSLTLELFPNHTDNLNSSQRLSPTSRARKLPQGRTVPPMGPETKVSVVWVERYDDIENFPLADLMSETSTGVETTANSSTSLRSTTLEKEVPVIFIHPLNTGLFRIKIQGATGKFNMVIPLVDGMIVSRRALGFLVRQTIINVCRRKRLESDSYNPPHVRRKQKIADIVNKYRNKQLEPEFYTSLFQEVGLKHCNP
The following text describes a protein:
Function:
Has very low cyanoalanine synthase and cysteine synthase activities.
Subcellular Localization:
Mitochondrion.
Sequence:
MATLSRFLKKRSLASNRLFSTQLPHTNIKSEVSQLIGKTPMVYLKKVTEGCGAYIAVKQEMFQPTSSIKDRPALAMINDAEKKGLISPEKTTLIEPTSGNMGISMAFMAAMKGYKMVLTMPSYTSMERRVTMRAFGADLILTDPTKGMGGTVKKAYELLESTPNAFMLQQFSNPANTQVHFDTTGPEIWEETLGNVDIFVMGIGSGGTVTGVGLYLKSKNPNVKIYGLEPTESNILNGGKPGPHHITGNGVGSKPDIVDMDLMEEVLMVSSEDAVNMARELAVKEGLMVGISSGANTVAALRLAQKPENKGKLIVTVHASFGERYLSSVLYQDLRKEAENMQPVSVD
The following text describes a protein:
Function:
Necessary for male gametophyte development, as well as ovule specification and function. Involved in cell-cell communication process required during early anther development, and regulating cell division and differentiation to organize cell layers. Required for the development of high-ordered vascular strands within the leaf and a correlated control of leaf shape, size and symmetry. May regulate the CLV1-dependent CLV3-mediated signaling in meristems maintenance.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MRLLFLLLLVMHFTDFSAGKQPRLPEYQALLALKTAITDDPQLTLASWNISTSHCTWNGVTCDTHRHVTSLDISGFNLTGTLPPEVGNLRFLQNLSVAVNQFTGPIPVEISFIPNLGYLNLSNNIFGMEFPPQLTRLRNLQVLDLYNNNMTGELPLEVYQMTNLRHLHLGGNFFGGRIPPEYGRFPSLEYLAVSGNALVGEIPPEIGNITTLQQLYVGYYNTFTGGIPPAIGNLSQLLRFDAANCGLSGEIPPEIGKLQNLDTLFLQVNSLSGSLTPEIGYLKSLKSLDLSNNMFSGEIPPTFAELKNITLVNLFRNKLYGSIPEFIEDLPELEVLQLWENNFTGSIPQGLGTKSKLKNVDLSSNKLTGNLPPNMCSGNNLQTIITLGNFLFGPIPESLGRCESLNRIRMGENYLNGSIPKGLLSLPRLSQVELQNNILTGTFPDISSKSNSLGQIILSNNRLTGPLPPSIGNFAVAQKLLLDGNKFSGRIPAEIGKLQQLSKIDFSHNNFSGPMAPEISQCKLLTYVDLSRNQLSGEIPSEITGMRILNYLNLSRNHLVGSIPSPISSMQSLTSVDFSYNNFSGLVPGTGQFSYFNYTSFLGNPDLCGPYLGPCKEGVVDGVSQPHQRGALSPSMKLLLVIGLLVCSIVFAVAAIIKARSLKKASEARAWKLTAFQRLDFTCDDILDSLKEDNIIGKGGAGIVYKGVMPSGEHVAVKRLPAMSRGSSHDHGFNAEIQTLGRIRHRHIVRLLGFCSNHETNLLVYEYMPNGSLGEMLHGKKGGHLHWDTRYKIAVESAKGLCYLHHDCSPLILHRDVKSNNILLDSSFEAHVADFGLAKFLQDSGTSECMSAIAGSYGYIAPEYAYTLKVDEKSDVYSFGVVLLELVSGKKPVGEFGDGVDIVQWVRKMTDGKKDGVLKILDPRLSTVPLNEVMHVFYVALLCVEEQAVERPTMREVVQILTELPKSPGAKSDDSTVTDQSPPPSDSALESPTSIPEETKDHHQPTPQSPPPDLLSI
The following text describes a protein:
Function:
Antitoxin component of a type II toxin-antitoxin (TA) system.
Sequence:
MARSINIDLQGGVVPISQAAASLAALIRRAKVSGQPVVITQKGYPSAVLLNIELFEQLRALALQAEQSHQQ
The following text describes a protein:
Function:
Dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also functions as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring of PtdIns(3,4,5)P3/phosphatidylinositol 3,4,5-trisphosphate, PtdIns(3,4)P2/phosphatidylinositol 3,4-diphosphate and PtdIns3P/phosphatidylinositol 3-phosphate with a preference for PtdIns(3,4,5)P3. Furthermore, this enzyme can also act as a cytosolic inositol 3-phosphatase acting on Ins(1,3,4,5,6)P5/inositol 1,3,4,5,6 pentakisphosphate and possibly Ins(1,3,4,5)P4/1D-myo-inositol 1,3,4,5-tetrakisphosphate (By similarity). Negative regulator of PI3K chemotaxis pathways. Overexpression leads to a suppression of a PI3K-dependent activation of pkbA, and these cells exhibit chemotaxis defects consistent with a reduction in PI3K activity.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Cytoplasm, cell cortex. Note=Found uniformly on the plasma membrane in unstimulated cells. In response to chemoattractant stimulation, there is a rapid and transient release from the plasma membrane. Constitutively localized in the cortex of polarized cells.
Sequence:
MSNLLRVAVSKQKRRYQKNGYDLDLAYITDNIVAMGFPSEKVEGVFRNPMKDVQRFLDQYHKDHFKVYNLCSERVYDHSKFYGRVGYYPFDDHNAPQFEMIDAFCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWLMYCGMWKNTEDSLRFYAALRTYNQKGVTIPSQIRYVGYFGRSIRESIKYVPRNVTLKKIVLRPLPKEINLSEVQFNISVGKNCVFNSKEHNMNVVISKKKKTVVDKNKKDPKKKLTKENSEKNIDSQQQQQSQSSLSQSQQGQSSPNMQSLSASGTISSGSNVGTVNGNTLHQLGGSQFSLSDLADGNTIGNDEYISFEIGALSLAGDIRIEFTNKQDDRMFMFWVNTSFVQQLEIIPKSGLDKAHKDKNHKAFPEDFHVELTFDQLDQQQSHTTVVASAEEQTNNQHYPQSSNNVATSSSHHDNITVVASDAPQNNNNNNNLNSSNSNNATTTTTKNNISLASSQSNPVQQESNPSTTTQVSEENSAPKVEAEKIENSNASANDSETSSNSSS
The following text describes a protein:
Function:
Lipolytic acyl hydrolase (LAH).
Domain:
The nitrogen atoms of the two glycine residues in the GGXR motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence:
MRCAAGVAPESSGEVVSGQQVTYSTAPYFSAASAQSVSMDDSGRARTDYGFGFSAGGLLFPYFLGISEQLQSMNVLLPETPVAGASAGSIIAVCAKSGLSEEELLVAFLDLARDCRQGGTRTRLKSVLRRVLEKALPDDIHERCNGRAHLAVTRLWPEFTPQTISSFRSRTDVIDTLLTSSHIPYWFDGSLFTMYRSGVYFDGGITNFIPSTPTDVCYRISCFPSQQLKAFKGISLSPDTFEQWPYDMGTMLGWAFEPAPEDMLLKLVEKGKRDARSWALVNVPVEQLQLAGGGR
The following text describes a protein:
Function:
Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MGEEVKVFGFWASPYSHRVELALSLKGVPYEYIEEDILKNKSDLLLKYNPIHKKVLVFLHKEKPIVESIVILEYIEETWKANPILPQNLHDKAIDRFWIKFIDDKCLPAIRKATFSPENERQTAVEEACFSDVCYLLLPFPLPLPLPFPLPLGLQISLVKDFFRFLLHPGKSTMNASISTSRDHKFGAMAEMLSKASTMVFRIEPMLTPTTIQMMSA
The following text describes a protein:
Function:
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Sequence:
MKIVVAKNIGFCFGVERAIRTVEELLDEGKKVVTDGEIVHNKQVMEQLTKKGLKVSSEMTDGEVFVVRAHGIPKDRLEELKKIFPEVVDLTCPIVSQLFKTAQRYAKERKVIVFGKEDHPEMVALRGYAPAIVTKVPFKLEEKKVVFLSQTTSSLEEYKEFVAAMIRMNEFEEAVFLNTICPVTVNREREVEELSKICDLSIVVGGKHSSNTGKLFRIASKHSKTIWIESPDELPADVVKYGTVCVFSGTSTPNSLIENVVRKLKEMEGKRDGTI
The following text describes a protein:
Function:
Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates to a subcomplex that specifically deubiquitinates histones. The SAGA complex is recruited to specific gene promoters by activators, where it is required for transcription. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery.
Subcellular Localization:
Nucleus, nucleoplasm.
Sequence:
MSQEYDAKINLHLDINHGLDRVTELVQTRLIECGWRDQVRLACRKAITENEKHIPTVDELIATVTPKARSMVPDSVKRELLHELESILINVDKFGYSKSF
The following text describes a protein:
Function:
Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Could catalyze the production of N(omega)-hydroxy-L-arginine (NHA) from L-arginine.
Sequence:
MNCYPAGHLLGKGHVQLNESGENAELISQEQIGDDLNGWHRDAFEDIASRLTDPGFPCVFSRNAFRKKLVKFVFVEGSGKEDIRHLGAGLKDYVELSRDWDGALDTAYPLVVVFSADAVTADSVEQYHAFGWWVLQELHAIDPTPWPEGVDKGPQSEAWSMCFHGMPLFINMSSPAHQVRRSRNLGRHFALVINPRERFDVFAGDTPSGRKVRSNIRGRIARYDGTPHAQQLGSYGTGALEWMQYGLVEENRERADVCPFTFRGA
The following text describes a protein:
Function:
Converts the inactive gibberellin (GA) precursors GA9 and GA20 in the bioactives gibberellins GA4 and GA1. Has a small activity on GA29, producing GA8. Unable to convert GA20 to GA5, GA5 to GA3 or GA12 to GA14. Involved in the production of bioactive GA for vegetative growth and development, but not for the 3-beta-hydroxylation of GA in developing seeds.
Miscellaneous:
MISCELLANEOUS: The Le gene controls the stem length trait studied by Gregor Mendel in 1866.
Sequence:
MPSLSEAYRAHPVHVNHKHPDFNSLQELPESYNWTHLDDHTLIDSNNIMKESTTTVPVIDLNDPNASKLIGLACKTWGVYQVMNHGIPLSLLEDIQWLGQTLFSLPSHQKHKATRSPDGVSGYGIARISSFFPKLMWYEGFTIVGSPLDHFRELWPQDYTRFCDIVVQYDETMKKLAGTLMCLMLDSLGITKEDIKWAGSKAQFEKACAALQLNSYPSCPDPDHAMGLAPHTDSTFLTILSQNDISGLQVNREGSGWITVPPLQGGLVVNVGDLFHILSNGLYPSVLHRVLVNRTRQRFSVAYLYGPPSNVEICPHAKLIGPTKPPLYRSVTWNEYLGTKAKHFNKALSSVRLCTPINGLFDVNDSNKNSVQVG
The following text describes a protein:
Function:
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MLARAFALVDKGCKACKRPLKLSVQASTLPGRRTRMPQRSCHLHRMPAQPENFPEEQHQPHNNSGGAPSSLACISEQNCAMQQSFAAMKTSGDVPVDSIRDTAEGTFDQRFATLKSIGEERVNEHELKLLLKKKSAPICYVWCDPSPWMHISQGIMKTISVNKMVKSGCKVKIVMADWFARVNREIGGNLNKMRTIGLYNIEMWKATGMALDEVELVWLSDEISQNADKYWPLVMDIARKNSVRRVRRCCQNRDPYVMGELTAAEIFLPCLQCAVILFQKVDIWLLGMEQHEANLLARQYCKHVKRRNKPVAVLHNTLPNLLQYPAMENRRHPAWAIFMEDDKEDICFKIEKAFCPPKLAEGNPCFQYIKRIILPWFGKFEVVRKRENGGTKTFLSMEELTADYESGALHPADLKLALVKSLNKTLQPVRDHFGSNAEAKDLVKAVEEYYIAD
The following text describes a protein:
Function:
The endopeptidase activity cleaves the bacterial peptidoglycan between D-alanine and L-alanine. The N-acetyl-muramidase activity cleaves between N-acetylmuramic acid and N-acetylglucosamine bonds.
Domain:
A CHAP domain is present at the N-terminus and is associated with the endopeptidase activity. The CHAP domain is responsible for nearly all the cell lysis activity. An Acm glycosidase domain is located in the central part of the protein and is associated with the muramidase activity. The Acm domain seems to require the SH3b domain for activity.
Sequence:
MATYQEYKSRSNGNAYDIDGSFGAQCWDGYADYCKYLGLPYANCTNTGYARDIWEQRHENGILNYFDEVEVMQAGDVAIFMVVDGVTPYSHVAIFDSDAGGGYGWFLGQNQGGANGAYNLVKIPYSATYPTAFRPKSFKNAVTVTDNTGLNKGDYFIDVSAYQQADLTTTCQQAGTTKTIIKVSESIAWLSDRHQQQANTSDPIGYYHFGRFGGDSALAQREADLFLSNLPSKKVSYLVIDYEDSASADKQANTNAVIAFMDKIASAGYKPIYYSYKPFTLNNIDYQKIIAKYPNSIWIAGYPDYEVRTEPLWEFFPSMDGVRWWQFTSVGVAGGLDKNIVLLADDSSKMDIPKVDKPQELTFYQKLATNTKLDNSNVPYYEATLSTDYYVESKPNASSADKEFIKAGTRVRVYEKVNGWSRINHPESAQWVEDNYLVNATDM
The following text describes a protein:
Function:
Involved in the digestion of the blood meal.
Subcellular Localization:
Secreted.
Sequence:
MTSGYGSDSTITGLMQAFDFYVFPVVNPDGYAYTFHAVSPCPGTSSHPCSDIYRGSAAFSETESRAIRDALVGLGSRTKAYVTVHSYSQLIMVPYGHGRGTYTKDYADQIAAARAISRAIQVKSGVYYQVGTISSLLGSAAGSSTDWVYDSANIKYSLAVELRDKGRFGFLLPNFLIISSGGNSTRPAIWIDGGTHAREWISTASTLFLIDRFLNSYNDSSQVTKLIDTFDWYMFPVINADGYKYTWTTHRLWRKNRIRNVGSLCRGVDPNRNFDVHFGLSGSSANPCAENYAGIFPFSEAESRAIRDGINNVKDRLRIYINLHSFSQLVMIPYGYSKGYTSDYKDQYEALEKLVTSIRKKNSAYYRHGTAGQALYVTSGAALDWVYDKAKVKHSFVIELRDRGLFGFILPREFINPTGEELFSGVKAVAFHVMKKDL
The following text describes a protein:
Function:
Glutamate-gated receptor that probably acts as a non-selective cation channel. May be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MVRICIQTPILLSFLLVLLFFISNCFASSQNNDDDKRIRVRVGLVLDLGSVEGKIVRSSVSMALSDFYDNHNDYKTRLSLLVRDSHGEPLLALDSVVDLLQTEGVQAIIGGNSLLEAKLLAELGEKARVPVISLNSPMSLSLSKYTHLIQATHNSASEVKGITAFLHGFDWNSVALVLEDHDDWRESMHFMVDHFHENNVHVQSKVAFSVTSSEDSLMDRLRELKDLGTTVFVVHLSEVIATRLFPCAEKLGMMGEGFAWILTSRSMSSFHDQFIDDLTKEAMEGVVGFKSYIPMSKELHNFTLRWRKTLPVEEVTGSEITRLSISGVWAHDVAWSLASAAEVTRMPTVTSTLLEAIKESRFKGLSGNFQLDDMKLLSDKFEIVNMIGSGERRVGFWNSNGSFSNRRQLSSTHDNLETIIWPGGSAQSPKGRSLRESGRKKLRVLVTSSNRFPRLMKVETDPITHEITIVEGFCIEVFQASIAPFNYEVEYIRWLNGTNYTKLAYALHSQKDKYDAAVGDITITSDRSMYVDFTLPYTEMGLGIVAAKERSMWVFFQPLTPNLWITSAAFFVLTGIIVWLIERAENKEFQGSWPQQIGVVIWFGFSTLVYAHREKLQHNLSRFVVTVWVFAVLILVTSYTATLTSMMTVQQIRFNANEDYVGHLSGSLIANAALTNSSLRAMRLLGLNTSEDYAQALMNKSVSYIVSELPYLKILLGENPGHFLMVKTQSTTNGFGFMFQKGSELAPNVSREIAKLRTSERLNEMERRWFDKQLPYTTDDTSNPITLYRFRGLFMITGVSFAFALAVLLILWLRERWEILVNSVNIYFSQRLRHFRILFTRTIHPSPLGLDNPIGENAVQMAQRNRR
The following text describes a protein:
Function:
Transcriptional repressor of nitrogen fixation and assimilation genes. Binds to two tandem operators in the glnA and nif promoters, thereby blocking transcription of the genes.
Sequence:
MDSNIDVEILSILSEASAPVGAKIIADSLKDRGYDIGERAVRYHLKVLDENSLTKKLGYSGREITEKGIEELEKANISFRIGSVFSQVIEKLYLSDFPSKVLINTAKFEGDYKTIKEMVLRSFEAGYSVGDYLNIKKKGNTVSVETLCSITFDNFLLKNGIIPTPEYGGIVKFEDYEPVNFEGVIDFKSSSIDPLVAFIMQGKTDVIGVIENGEGLVPANFRVIPKSSEKQFETILKKDMLNSVLAYGTENVLGMNLNPEQIGVVLVGGLTPLCVPHESGYTADISAATQLKDISSMEKKTKGFLEAKKKKGKFKVTPVLSKMLSKMQTINYDIEDKKGNVVVNTAKIPIEYKEEAINALKDSYENKLAISDRLKVECDDKFLNAYTICSLTVDGVFLKNKIPVIPYYGGILEVKADKKRFIEAIDYEGTSLDPHEVFFNKADGKNYILAGIRKVPMSASEKLIELNEKLGWNSIIEIGRPNNDICGVRVEKCMFGITTIGGTNPFANIRKNNIPVEMKTLHKSIDYSELTHYDDI