lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in rRNA processing.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MAPPTQRRYTNNRKRRGPREVGGAKTGDGLTRIMKRIRDLERVLKRPVPMDEQKRIELERAVAAYKVQAEDIIGDRKNKKNVEKYRMIRFFERQKASRKVKQARKLVEQADSDAKKKDAEALVVKYMADLAYTIHFPNDIKYISLYPNGAVDETAESSKQREKMRAEFAEQIKNGELDVDLERAEQVATTKKSKKKREAGADEEVKGDDEDDEFLEKAPKKAKVEEEESDDDEEDEEDDDDDDDSDDDDSDDSGEPQMEIKRTADEKQTKEEESDSEEFVDESEAESEGKPESEENSEDQDDESE
The following text describes a protein:
Function:
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Sequence:
MASQLRVYVPEHPLIKHWLGVARDENTPPVLFKTAMGELGRWLTYEAARYWLPTVDTEVKTPLAIAKASLIDPQTPFVIVPILRAGLALVEGAQGLLPLAKIYHLGLVRNETTLEPSLYLNKLPERFAPGTHLLLLDPMLATGNTIMAALDLLMARDIDANLIRLVSVVAAPTALQKLSNAHPNLTIYTAMIDEQLNDRGYIVPGLGDAGDRCFGT
The following text describes a protein:
Function:
Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Sequence:
MTEDELNKLLLAGKIAAKARDEVSLDVKASAKVLDICEEVESIIIENKAFPSFPCNISINSEAAHYSPTINDEKRIPEGAVVKLDLGAHIDGFISDTAITISLDSRYQRLLDASKTALEAAITNFKAGLSIGEIGRVIEKVIRAQGYKPIRNLGGHLIRRYELHAGVFIPNVYERGLGVIQSDSVYAIEPFATDGGGEVVEGKSITIYSLKNPNIKGLSSRENELIDFIYTRFNYLPFSERWLKEFSTNVDELRNNIKNLVKKGALRGYPILIEIKKGVVSQFEHTVIVKGDSIIVSTKSL
The following text describes a protein:
Function:
G-protein coupled receptor that plays a role in the regulation of circadian rhythms and energy metabolism. Participates in maintaining proper circadian gene expression in the suprachiasmatic nucleus (SCN), the locus of the master circadian clock in the brain. May function as a coordinator of aging-associated metabolic dysfunction, stress response, DNA integrity management, and eventual senescence. Upon binding to adropin, modulates mitochondrial energy metabolism via the p44/42-PDK4 signaling pathway, influencing pyruvate dehydrogenase activity.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MAEDNGSRAFNLTRGSIAGTAATTASVLVVTAFLGFVSLGGVFGNGLVVCVIKRLRWHGKQSSVHTFLLHLALSDLMVCCVCIPLTITANFVALDSSNTLHSIVCKTMRFFQFLAPTVSISLLTVISIDRFLVIVKPLRKTFLRRSTWLIIFAWTYSIIQFLPTFYLARIDNISIDNSTVGYCTPIPNNTSEGLGYLMFLAFCAFVLPLTTMCVMYTSICRVVWRRHEQLHDNSTAISGETLFRRSKRRILKMLLIVVAAFMFCWLPFVAYAGFVEPYLETFPNPGDLIRLASYCLGLTNSLINPVIYFFSNVVLRKSCIDLLCCRKFNFPANLQYAWSPAISRRMITSRGSSLIPDISSLRHSLHRR
The following text describes a protein:
Function:
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (alpha-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). Active on small alpha-keto acids such as 3-methyl-2-oxobutanoate, pyruvate, alpha-ketovalerate, and alpha-ketobutyrate; only uses acetyl-CoA. Complements an E.coli deletion.
Miscellaneous:
MISCELLANEOUS: In Mycobacteria this gene has a variable number tandem repeat (VNTR); in H37Rv there are 2 repeats, other strains can have up to 6 repeats; MISCELLANEOUS: Was identified as a high-confidence drug target.
Subcellular Localization:
Cytoplasm.
Domain:
Has two major domains which are separated by two small subdomains, that are themselves joined by a flexible hinge. The N-terminal catalytic domain forms an (alpha/beta)8 TIM barrel and binds substrate (3-methyl-2-oxobutanoate) and Zn(2+). Subdomains I and II (separated by a flexible linker) make a three-helix bundle that packs against the C-terminal domain. The C-terminal regulatory domain includes two variable number tandem repeats (VNTR) in this strain. The regulatory domain binds L-Leu (the pathway end product) in the dimer interface. The individual domains of the monomers swap between monomers. The C-terminus (residues 426-644) is required for condensation of the 2 substrates.
Sequence:
MTTSESPDAYTESFGAHTIVKPAGPPRVGQPSWNPQRASSMPVNRYRPFAEEVEPIRLRNRTWPDRVIDRAPLWCAVDLRDGNQALIDPMSPARKRRMFDLLVRMGYKEIEVGFPSASQTDFDFVREIIEQGAIPDDVTIQVLTQCRPELIERTFQACSGAPRAIVHFYNSTSILQRRVVFRANRAEVQAIATDGARKCVEQAAKYPGTQWRFEYSPESYTGTELEYAKQVCDAVGEVIAPTPERPIIFNLPATVEMTTPNVYADSIEWMSRNLANRESVILSLHPHNDRGTAVAAAELGFAAGADRIEGCLFGNGERTGNVCLVTLGLNLFSRGVDPQIDFSNIDEIRRTVEYCNQLPVHERHPYGGDLVYTAFSGSHQDAINKGLDAMKLDADAADCDVDDMLWQVPYLPIDPRDVGRTYEAVIRVNSQSGKGGVAYIMKTDHGLSLPRRLQIEFSQVIQKIAEGTAGEGGEVSPKEMWDAFAEEYLAPVRPLERIRQHVDAADDDGGTTSITATVKINGVETEISGSGNGPLAAFVHALADVGFDVAVLDYYEHAMSAGDDAQAAAYVEASVTIASPAQPGEAGRHASDPVTIASPAQPGEAGRHASDPVTSKTVWGVGIAPSITTASLRAVVSAVNRAAR
The following text describes a protein:
Function:
May be involved in the polar growth of plant cells via transportation of RNAs.
Subcellular Localization:
Nucleus.
Sequence:
MREKHYSEDNSRKRKRGELEHNSDLNETVLPSDWTPDPVKNFAADDDDEETKAKDATMVLPFVKKSPVWKIYESMEVFKRVPQSPHFSPLFEAKEDFREGFALGMMVTFSGVLEKVEDLKTDVPIRQLNSLKDSFTELEKHGFTVTAPLSRIAKLLALKDRQLKILEELKVFDKEMKDESSKKHKAEQEFGEMERKILEVKNKVLELQKQEAALEKQKDATYEKICKMESRARDLGVELEDVE
The following text describes a protein:
Function:
Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
Sequence:
MTSFQSTLDDDEDGIAEELAASQREISVAEFFEKNKHMLGFDSGARGLVTAVKEAVDNALDATEEAGILPDIYVEISEGRDYYTLIVEDNGPGITNAQIPKIFGKLLYGSRFHAREQSRGQQGIGISAAVLYSQLTSGKPVRIESRTQDSETANVYELIIDTDTNEPEISAETEVSAAKSDLRGTHGTRIEMALDANMRARGQLHDYIKHTAVVNPHARIELQEPGGELKSERAEEASLPAETDEILPHPHGVELGTLIKMLAETDSHSVSGFLQSEFTRVGSKTATGIIDAFRDEHFGREMRWRPPADADLEATVADAVANKDATHTAVFARTVADAVRDADSIAPAELGALVADAAADAQDDTGTSFGETVQANVVAAVRDALTSDRVADVLGPVDEATTVQKDDATVRGLAERIAAKFESGGDTDRVTRDTLDEYVFRAAENTAEYADATIGETARENVADALWARMATVPDDPPNTSALADDRDAASDLLAAMASVNVMAPPTSCLSPIEADQLEAGLRTEFDADFYAAATRDADVHGGDPFIVEAGIAYGGDIDSEGGVQLMRFANRVPLVYQRGACATTDVLGDIGWRNYNLSQPGGSGLPQGPAVIMVHVASTNVPFTSESKDAIANVPEIEAEIELAVREAARELKSFLQKRQSMRKRQQKQDVIMDILPTMAEKVGELTGRGGVDVSDSLARIMNNVLVERARSDDGQTVTLRVENHGTGSVDVDVTDIVSAEPDGVGDDASVVAMDDEYFVKWTPAVAGDDAAELTYSVDADADCELSVSGVADARLTVSEADT
The following text describes a protein:
Function:
Parathymosin may mediate immune function by blocking the effect of prothymosin alpha which confers resistance to certain opportunistic infections.
Sequence:
MSEKSVEAAAELSAKDLKEKKEKVEEKAGRKERKKEVVEEEENGAEEEEEETAEDGEEEDDGDEEDEEEEEEEDEGPALVRAAEEEDEADPKRQKTENGASA
The following text describes a protein:
Function:
Promotes up-regulation of actin stress fiber formation.
Subcellular Localization:
Cell junction, focal adhesion. Cell junction. Cytoplasm, cytoskeleton. Note=Localized at focal adhesion sites, cell-cell junctions and cell-extracellular matrix junctions.
Sequence:
MARILGVGRSSASSLNNKEDNESDVALLSPKDPNRVHTKEQLAHPASSNLDPSMQGLPAGLSLDDFIPGHLRTHIGSSSRGTRVPVIRNGGSNTLNFQFHDPAPRTVCNGCPPPRRDGSLNPDPAWYQTWPGPGSRPSMSPKPPASQHAQNWSATWTKDSKRQDKRWVKYEGIGPVDESGMPIAPRSSVDSPRDWYRRMFQQIHRKMPDLQLDWTLEDPPKVVSARASSAEPRHLGTLQRPASRPGTTETSSGRNWNHSEETSRNTFNYNFRPSSSGLHPPNQVPRHREKVENVWTEDSWNQFLHELETGHKPKKPLVDDPVEKPAQPIEVLLERELAKLSAELDKDLRAIETRLPSPKNSQAPRRPLEQPGLEQQPSARLSSAWRPNSPHAPYFSSSRPLSPHRMADGGGSPFLGRRDFVYPSSAREPSASERGSSPSRKEEKKRKAARLKFDFQAQSPKELSLQKGDIVYIHKEVDKNWLEGEHHGRLGIFPANYVEVLPADEIPKPIKPPTYQVLEYGDAVAQYTFKGDLEVELSFRKGERICLIRKVNEHWYEGRITGTGRQGIFPASYVQINREPRLRLCDDGPQLPASPNPTTTAHLSSHSHPSSIPVDPTDWGGRTSPRRSAFPFPITLQEPRSQTQSLNTPGPTLSHPRATSRPINLGPSSPNTEIHWTPYRAMYQYRPQNEDELELREGDRVDVMQQCDDGWFVGVSRRTQKFGTFPGNYVAPV
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MDPPSLVKNEPLNHKYHLSTTESEMGSSSGPGFPEAEEEIVQVKIEKRDSDSDSGLNSLPGEVKVEKFESDVDYNPDTSEAEILQIKVDKEDFDPSAMKSEGCAVDGQEDCLNETRGWASHYCLTESRSSDSSGSLDKSMEDDGYFVGSGQHSYLCEPNTRSESDSGTQESSCFVCNKCGKYFFQHSDLLSHPCVSAHDMDISGSRPPGSYCQLHPLAHSDGKTFSCTECDKGNYTKSNLQSHQNIYRGAKPFVCTECGKGFSRKYSLNNHIRYHTGDKPFVCTECGKSFPEKGKLHSHVKIHTGEKPFMCPVCSKSFSEKCNLYNHQTIHTGEKPFMCPECGERFSRKSTLGIHKNVHTGEKPFTCPECGKNFSQKSNLRSHQRIHTGEKPFSCSICGKSFYEKKNLHRHEATHTGEKPFICSQCGKGFSDKGALHTHFRVHTKEKPFPCRECGKSFTQKSNLQIHQRIHTGQKPFICTECGDCFSVKISLQKHQKTHSIETVPRAMKPDKEVSDCNQLTMLKSETDPWTDFGVSEEEPEIIQIKIKEEEADSGDELNVMPHWDAPCTDTESPETFESDSSITTCTSSGQHHVAVPFQEKQDDELFYSKDPSKLKGEIDRYNFPEAETEILQVKIKEEEPNSDYVLSSANSTAVSLTDGESLGIVPGEIKCDQEGMNYNDVITHNEMPSDSCTHPGSHTNRYTNTRKRRKVEENLFTCSHCGKHFKRKYNLQVHQRVHTGEKPFTCTECGKSFSLKSILKSHQKVHRVEKPFQSRDSGGNSENNDTRTEEKRFKCSECRKGFSDKYSLFIHLRVHTGEKPFSCTECGERFGYKSTLRIHYKRHSGEKPFACSECGKQFFQKRNLRCHQRVHTGERPFSCIECGERFSRRSTLIAHKIVHTGNKPFTCTECGKTFSRKFDLQLHEKVHSGDKPFKCTECGKGFSQQRRLYSHLAVHTGEKPFTCTECGKGFSEKRRLYNHQAVHTGEKPFACTECGKCFALKGTLRCHQELHTGARPFTCSECGETFSKKDTLNTHLKIHTGEKPFACTECHKRFAKKSNLQRHQNVHKEKLAGASL
The following text describes a protein:
Function:
Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate (TPP). TPP is an active cofactor for enzymes involved in glycolysis and energy production. Plant leaves require high levels of TPP for photosynthesis and carbohydrate metabolism.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MEVMRHVSTFLRPPPLPQAADGPAPSYALVVLNQRLPRFAPDLWSHAKLRIFADGGANRVYDGMPKFFPEQDPLEVRRRYKPDVIRGDLDSIRPEVKEFYSNLGVKVDDVSYDQDTTDLHKCIAFICDFIPEVDKSNLCILVAGALGGRFDHEAGNLNVLFKFSNIRIVLLSDDCLIQLLPKTHCHEIHIQSSAEGPHCGLIPVGAPSVSTTTTGLRWDLTNAGMSFGGLMSTSNMVREERITVRSDSDLLWTISIKKKA
The following text describes a protein:
Function:
Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays a critical role in the assembly of N-DRC and also stabilizes the assembly of multiple inner dynein arms and radial spokes. Coassembles with DRC1 to form a central scaffold needed for assembly of the N-DRC and its attachment to the outer doublet microtubules.
Subcellular Localization:
Cytoplasm, cytoskeleton, flagellum axoneme. Cytoplasm, cytoskeleton, flagellum basal body.
Sequence:
MKQAMIEEEKRSRLSKLQIHKTWRSIMREHSIQELRGDIKWMAKKHLKEVENKDRRIHTLLKALEESETQHLKATSSHFVMLDQMINVHDVRLQSMEHQFQAQLQNLNQSFYDERDQMTQDLIGTKWDMEAMVKNMKALFDEETVEKRQEFEAFLKDFEDKRKESNSVMKMIYDSKTEEMERAIERRHHDFIKQNKAKQEVFKELTFKDEKTSELCAKRMRELLTLHEKTSCMVKAMQIKGKEWDDTNKHLVDEYRTLHEHIRKINRHLSKIAQTEHDDLKRTSLFVNEATQALNKVLAFGRGLQTLARLNRKLETEHEQIFPFNPLYETPLPLAPLESFDEELVYVADEKTPIEEPSPPTLPTFHWSTHAVDDTGNEVEELDCLKKFQKRYNKAMLDKLALQLERRKLVSENQRLHLLVCKRLGTHSH
The following text describes a protein:
Function:
Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MEVKLGILGVIVHLILLYSIFDIYYTSPIIESLNAHRPNSNDPPARRLFLISADGLRYDTFQRKELAPFLHSLIDSGVASFGVSTSGVPTESRPGHVSIVAGFTEDVSAVTRGWKENPVTFDTIFNRSIESFQWGSEDITHLFSHIPHVKTKSFPAEWEDFSSLDNYKLDEWVFDKCERDLLDLPSSSLIGSSRFFFLHLVAIDTNGHGHNPDSFAYTDNLRIVDERVRRLVTKVNQVFNDSKSAYIFTSDHGMTEWGSHGGGTDLETKTPFVVWGSGVNGGAREHIQQIDLCPLMASLLAIPFPINNHGIIRTSLLNTSARFQSSVVMANFLQLREIILHQISHVGKRWWLSSEVVTTTALNSLYDQATQLAAKNRFESISSLVSSQLPLLQRSIFLYHRVDRPLLSILVAASFISFLLLLKISSVHSFYLRFIPSGKLILFLLVSSTASSIFFVSLSHIIYLILPIYLISLIPFAHVPSLILRLVSLSSLPPIMLIILLNYSFYDRRFSSLLTIYLIFLPYLLYHSRPIFSKLNVLLYGVSLSFCPFPFLPPCGVLSFPLLSSIPPIILSIILKRIRHLFPSHNQPNIDHLFSLSLITCSLIIFHSILPSYFVLRFLSWLLIPLPYIIVFRTPPRTPSRLLSLSVALFLPYSLLSSSYESLYLLLLLIFLSIFTRKSSSHSSSLFFHLPLSSTISLSCAFVPLPHVLTFLTLFSTGNLASLSSFSPSSLSRFISVFSPFTMASLLVLKLLSPILLIFIHLRSSLPSLSSSSNLISSTLIISDLLSLIFFYQLRDSGSWLEIGLSIAHFLISLSSSLAFYLLFLLSDYLLSTPLRSRSKHISNA
The following text describes a protein:
Function:
Required for ciliogenesis.
Subcellular Localization:
Cell projection, cilium. Vacuole membrane; Multi-pass membrane protein.
Sequence:
MTSKYPYVLTTQFLMLTIDIFFNALSILCYGDNMALLLIYILQDTLLIMSSLVLFVSFTATFVFQLGLIHIVLVQFLPTIIMSIFYTFVSIGYHYTSLSSTWEDQTVNIFLETHLLIFFIFHKVISCIFYSFYKRTALQISDPKYNSDSTWLRELFIKHMNDKAAKLEARNAAAAT
The following text describes a protein:
Function:
Component of the receptor for IL20, IL22 and IL24. Component of IL22 receptor formed by IL22RA1 and IL10RB enabling IL22 signaling via JAK/STAT pathways. IL22 also induces activation of MAPK1/MAPK3 and Akt kinases pathways. Component of one of the receptor for IL20 and IL24 formed by IL22RA1 and IL20RB also signaling through STATs activation. Mediates IL24 antiangiogenic activity as well as IL24 inhibitory effect on endothelial cell tube formation and differentiation.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MKTLLTILTVGSLAAHTTEDTSGLLRHVKFQSSNFENILTWDAGPASAPDTVYSVEYKKYGEKEWLAKAGCQRITQKFCNLTVETRNHTEFYYAKVTAVSSGGPPVTKMTDRFSSLQHTTIRPPDVTCIPKVRSIQMLVHPTLTPVLSEDGHQLTLEEIFHDLFYRLKLHVNHTYQMNLEGKQREYEFLGLTPDTEFLGSITILTPILSKESAPYTCRVKTLPDRTWAYSFSGAVLFSMGFLVGLLCYLGYRYITKPPVPPNSLNVQRVLSFQPLRFIQEHVLIPVLDLSGPSSLPQPIQYSQVVVSGPREPPGAGRRRHSLSDLTYVGQSDGSILQPTNGPAQQTLSPPSYAPKALPEVQPLSYAPQVASDAKALLYSPQQGIKTGPATYDPQDVLDSWPASYAVCVEDSGKDSTPGILSSPKHLKLQEDTLVRSCLPGDLSLQEVTSLGEEEAQRPKSLPPPLGFCTNGPDLHTLHSEEPETPRYLKGGLSLLSSVQIEGHPVSLPLHLHSVSCSPSDQGPSPWGLLDSLVCPKDEGPVAETEAILPSAVASELEQSTELDSLFKGLALTVQWES
The following text describes a protein:
Function:
Involved in endochondral bone formation as negative regulator of bone mineralization. Stimulates the proliferation of endothelial cells and promotes angiogenesis. Inhibits MMP9 proteolytic activity (By similarity).
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MGTIRSSALILACLALASAASEGAFKVSDQREMKPEHLFQHLHEVGYAAPPSPPQTRRLQVHHSETSPHDPPLFEEQKEVQPPSSPEDIPVYEEEWLTFLNPNVGKVDPALPQEAIPLQKEQPPPRIPIEQKEIDPPVQHQEEIVQSRQKEEKPPTLTGQHPPEPRTWNPARHCQQGRRGIWGHRLDGFPPGRPSPDNLKQICLPERQHVVYGPWNLPQTGYSHLSRQGEALNLLETGYSRCCRCRSDTNRLDCVKLVWEDAMTQFCEAEFSVKTRPHLCCKQRGEERFSCFQKEAPRPDYLLRPCPIHQTGISSGTQLPFPPGLPTPDNVKNICLLRRFRSVPRNLPATDAIQRQLQALTRLETEFQRCCRQGHNHTCTWKAWEDTLDGYCDRELAIKTHPHSCCHYPPSPARDECFAHLAPYPNYDRDLLTVDLSRVTPNLMDHLCGNGRVLSKHKQIPGLIQNMTVRCCELPYPEQACCGEEEKLAFIEDLCGPRRNSWKDPALCCTLSPGDKQANCFNTNYLRNVALVAGDTGNATGLGQQGPTGGTNVGPAPGSKEE
The following text describes a protein:
Function:
Probably involved in the assembly of some coat protein components implicated in both lysozyme resistance and germination. Could be required for the assembly of CotG. Associates with SpoIVD during the early stage of coat assembly.
Miscellaneous:
MISCELLANEOUS: Several coat proteins are extracted in reduced amounts from SafA mutant spores, one of which is CotG. SafA mutant spores have abnormal coat layers and have lost their resistance to lysozyme. Their response to L-alanine suggest that they have a defect at a late stage of spore germination. Their response to AGFK also suggests that they have an additional defect at a early stage of spore germination. The mutation of SafA has no effect on vegetative growth and spore resistance to heat and chloroform; MISCELLANEOUS: In wild-type cells, during the early stages of sporulation, a product of 43 kDa (the predicted size of SafA) was detected. However, in later stages, a 30-kDa species was the major form of SafA detected. The N-terminus sequence of the 30-kDa product starts at Met-164. It is not known if the smaller form results from proteolysis or from translation initiated at Met-164.
Subcellular Localization:
Spore cortex. Note=At the coat-cortex interface.
Sequence:
MKIHIVQKGDSLWKIAEKYGVDVEEVKKLNTQLSNPDLIMPGMKIKVPSEGVPVRKEPKAGKSPAAGSVKQEHPYAKEKPKSVVDVEDTKPKEKKSMPYVPPMPNLQENVYPEADVNDYYDMKQLFQPWSPPKPEEPKKHHDGNMDHMYHMQDQFPQQEAMSNMENANYPNMPNMPKAPEVGGIEEENVHHTVPNMPMPAVQPYYHYPAHFVPCPVPVSPILPGSGLCYPYYPAQAYPMHPMHGYQPGFVSPQYDPGYENQHHENSHHGHYGSYGAPQYASPAYGSPYGHMPYGPYYGTPQVMGAYQPAAAHGYMPYKDHDDCGCDGDHQPYFSAPGHSGMGAYGSPNMPYGTANPNPNPYSAGVSMPMTNQPSVNQMFGRPEEENE
The following text describes a protein:
Function:
Involved in oxidative burst-mediated signaling. Required for basal resistance to P.parasitica infection and root hair growth. Partly required for the activation of MPK3 and MPK6 by hydrogen peroxide and cellulase elicitor.
Domain:
The activation loop within the kinase domain is the target of phosphorylation.
Sequence:
MLEGDEKQSRALDFNRLEVLSLLGRGAKGVVFLVRDDDAKLLALKVILKEAIEKKKKGRESEDDEYKRVSFEQGVLSRFDHPLFPSLHGVLATDKVIGYAIDYCPGQNLNSLRKMQSESMFSDEIIRFYAAELVLALDYLHNQGIVYRDLKPDNVMIQENGHLMLIDFDLSTNLAPRTPQPSPSLSKPSPTMKRKKRLFRFTSFCNSGISPQESISVHSSSTLAVSDSSGEKSNSFVGTEEYVAPEVISGDGHDFAVDWWSLGVVLYEMLYGATPFRGSNRKETFYRILSKPPNLTGETTSLRDLIRRLLEKDPSRRINVEEIKGHDFFRGVDWEKVILVSRPPYIPAPDDGGDKGTDVNTKMDVENIVQEIFAARQEREKQSGDNNKNANMKIKDNTSGEWVKGLNNNHDLESDNNFLVF
The following text describes a protein:
Function:
An ATPase (By similarity). Part of the ESX-3 specialized secretion system, which is important for iron and zinc uptake or homeostasis.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein.
Sequence:
MTNQQHDHDFDHDRRSFASRTPVNNNPDKVVYRRGFVTRHQVTGWRFVMRRIAAGIALHDTRMLVDPLRTQSRAVLMGVLIVITGLIGSFVFSLIRPNGQAGSNAVLADRSTAALYVRVGEQLHPVLNLTSARLIVGRPVSPTTVKSTELDQFPRGNLIGIPGAPERMVQNTSTDANWTVCDGLNAPSRGGADGVGVTVIAGPLEDTGARAAALGPGQAVLVDSGAGTWLLWDGKRSPIDLADHAVTSGLGLGADVPAPRIIASGLFNAIPEAPPLTAPIIPDAGNPASFGVPAPIGAVVSSYALKDSGKTISDTVQYYAVLPDGLQQISPVLAAILRNNNSYGLQQPPRLGADEVAKLPVSRVLDTRRYPSEPVSLVDVTRDPVTCAYWSKPVGAATSSLTLLAGSALPVPDAVHTVELVGAGNGGVATRVALAAGTGYFTQTVGGGPDAPGAGSLFWVSDTGVRYGIDNEPQGVAGGGKAVEALGLNPPPVPIPWSVLSLFVPGPTLSRADALLAHDTLVPDSRPARPVSAEGGYR
The following text describes a protein:
Function:
Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity).
Miscellaneous:
MISCELLANEOUS: Most taste cells may be activated by a limited number of bitter compounds; individual taste cells can discriminate among bitter stimuli.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MLTLTRIRTVSYEVRSTFLFISVLEFAVGFLTNAFVFLVNFWDVVKRQPLSNSDCVLLCLSISRLFLHGLLFLSAIQLTHFQKLSEPLNHSYQAIIMLWMIANQANLWLAACLSLLYCSKLIRFSHTFLICLASWVSRKISQMLLGIILCSCICTVLCVWCFFSRPHFTVTTVLFMNNNTRLNWQIKDLNLFYSFLFCYLWSVPPFLLFLVSSGMLTVSLGRHMRTMKVYIRDSRDPSLEAHIKALKSLVSFFCFFVISSCAAFISVPLLILWRDKIGVMVCVGIMAACPSGHAAVLISGNAKLRRAVTTILLWAQSSLKVRADHKADSRTPC
The following text describes a protein:
Function:
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Subcellular Localization:
Cytoplasm. Mitochondrion intermembrane space.
Sequence:
MSSPAPSTSHNAANSTQAFSLKTRRPIDEDDLLTAEDREAKSTVEKLDCATRRRACKNCTCGRAELERQLEAGGSQVMGAMPPGGCGNCAKGDAFRCAGCPYLGMPAFDNAVDGKVKLDLTDDI
The following text describes a protein:
Function:
Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
Subcellular Localization:
Nucleus.
Sequence:
MTTEKGEQLRQQLIAAVVKKRAAIARAHEIVVRLLEPGIPEPEFLSLLCEIGPPNYSDIVDEREINKLCGYPLCSTVLENVPKQKYSISASKNKVYDITERKKFCSGYCFKASEYIKSQVPTSPLWLRDRETRPSFQLLPRNT
The following text describes a protein:
Function:
Plays an important role in the degradation of some oligopeptides.
Subcellular Localization:
Lysosome. Cytoplasmic vesicle. Secreted.
Sequence:
MNFHPCYPVDHGVPSWILVLLLSLGLCNLQARADRVLDPDFHENYFEQYMDHFNFESFGNKTFGQRFLVSDKFWKMGEGPIFFYTGNEGDIWSFANNSGFMVELAAQQEALLVFAEHRYYGKSLPFGVQSTQRGYTQLLTVEQALADFAVLLQALRQDLGVHDAPTIAFGGSYGGMLSAYMRMKYPHLVAGALAASAPVVAVAGLGDSYQFFRDVTADFYGQSPKCAQAVRDAFQQIKDLFLQGAYDTISQNFGTCQSLSSPKDLTQLFGFARNAFTVLAMMDYPYPTDFLGPLPANPVKVGCQRLLNEGQRIMGLRALAGLVYNSSGTEPCYDIYRLYQSCADPTGCGTGSDARAWDYQACTEINLTFDSNNVTDMFPEIPFSEELRQQYCLDTWGVWPRQDWLQTSFWGGDLKAASNIIFSNGDLDPWAGGGIQSNLSTSVIAVTIQGGAHHLDLRASNSEDPPSVVEVRKLESTLIREWVAAARLKQPAMPRWPGPKKQHPSR
The following text describes a protein:
Function:
V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular Localization:
Secreted. Cell membrane.
Sequence:
MDWTWRILFLVAAATGAHSQVQLVQSGAEVKKPGASVKVSCKASGYTFTSYAMHWVRQAPGQRLEWMGWINAGNGNTKYSQKFQGRVTITRDTSASTAYMELSSLRSEDTAVYYCAR
The following text describes a protein:
Function:
A secreted protein. Acts as a strong host T-cell antigen. Involved in translocation of bacteria from the host (human) phagolysosome to the host cytoplasm. Might serve as a chaperone to prevent uncontrolled membrane lysis by its partner EsxA.
Subcellular Localization:
Secreted. Note=Probably secreted via the ESX-1 / type VII secretion system (T7SS).
Sequence:
MAEMKTDAATLAQEAGNFERISGDLKTQIDQVESTAGSLQGQWRGAAGTAAQAAVVRFQEAANKQKQELDEISTNIRQAGVQYSRADEEQQQALSSQMGF
The following text describes a protein:
Function:
Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration; Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration; Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Sequence:
MRRNSFIRTISTYTRYPDEQQKLLYLAWSAAWLRKAEVEAARVQGITLYDLMQRAAAAFFKVVCTEVPNAKKWLVLCGSGNNGGDGFEVARRASSRGGGTCVTVITVAGSKPLPPEAAAAYAALQEERQKPGVEIVMKDARTWLEEGASLSGVDVVVDGLLGTGMGGAPRGDYAAIIDRVNESGKPCFAIDIPSGLDAETGDVKGSCIRAVHTVTFIAVKPGLLTGSARNHVGKLHYDSLDLADWLLLPDQQRDVFCRRLESSHLFPLLSRSEPRRCINKAMNGKLLVVGGDSGFGGAIAMAAEAALRSGCGLVRVLTRAEHAAPIMCRCPEVMTQTLTEESLRMGLQWASCVAIGPGLGQGAWGIEALRVVEIHLRENINVPSVWDADALNILAAFSRKRNDGEQQPPSVRLNNRVITPHSAEASRLLGCTVSEVEQNRYRAAEELVARYGGVVLLKGPGTVLRIAEDARVPVPTGTAAELLFPACAVADVGNSGMASGGMGDVLTGIIAGLLAQQFPLWQATCAGCLVHGTAADLAASSQGGERGLTATTLFKYLPVCLNPTPEGFQASQCYL