lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Dicer-like endonuclease involved in cleaving double-stranded RNA in the RNA interference (RNAi) pathway. Produces 21 to 25 bp dsRNAs (siRNAs) which target the selective destruction of homologous RNAs leading to sequence-specific suppression of gene expression, called post-transcriptional gene silencing (PTGS). Part of a broad host defense response against viral infection and transposons. Controls the expression of the non-LTR retrotransposon Tad in the African strain, Adiomopoume.
Sequence:
MAVATRLPFIPPEATSQIIGGDEDLIDLSQEDVVSDNDDRGNASDVESEDGVKRWTVNPEPKPKKISAKKLADTAAFNSWIEEHQETLARDQRKAAIEAARVAGVDVLPAIGFDSERIITSPREYQVELFERAKQQNTIAVLDTGSGKTLIAAMLLRWVITGELEDREKGLPRRIAFFLVDKVALVFQQHSFLTKNLDFPMEKLCGEMVEGVESKAFWKEALEQNEVVVCTAEILSTALHHSWIRMDQINLLIFDEAHHTKKDHPYARIIKNFYIDEQLERRPRILGLTASPVDAKVDPRRAAAELEALLHSQIATAADPAALQHTICKPKTELVVEYVRGRPDSETVLNKQLRKLVGGQELFKKPLNFTTSAASKLGTWCADRYWQLFFKQEDIVKLESRTERDLMKVAALDEITEKHVKQVREAHELVNAHTFSPAALDPTMLSSKVIMLVRILRDQFERGVGAQRCIIFVRQRNTAMLLADLLQQPEIKSHIPSIAAEVLVGGGTTGSSYVNAKINFQQQNRIIRKFKLGEINCLFATSVAEEGLDIPDCNIVIRFDLYDTLIQCIQSRGRARRPDSRYIQMIEKGNYEHHSRILRAKGAEDVLRKFCEALPEDRKLTGNHMNLDYLLRKEKGKRQYTVPDTGAKLSYMQSLVCLANFTATLPHPPETSLSPEYYITTVPGGFQCEVVMPDASPIKSAVGKVHLSKGVAKCAAAFELCLALLKAGHLDNHLQSVFTKQLPEMRNARLAVSSKKKTEYAMRLKPELWSVRGVVTQLFATAFVLENPDTLGRSSRPLLLLSRSALPEVASFPLFFGTKRFSKVRCVPIPGSVQADDTLVEQLTRFTLKAFMDVFSKEYEATAVNLPYFLSPMDGGHGFDFRLAKSPAHLIDRKALAYVSENEKVPYTFLEPDDFFQDKFVVDPYDGARKFFTHHRRHDMKPTDPVPDGIVAPNHRAWRGLGTTHDILNYSNSLWSKSRGFMIFQADQPVVEAALISTRRDFLDDTLRDEDVEPQQCFLILEPMRISPIPADVVAMLLCFPSIIHRVESNLVALDACKLLGLDLRPDLALEAFTKDSDNSDEHDAEKENFQTGMGDNYERLEFLGDSFLKMATTIAIYTLIPDKGEFEYHVERMLLICNKNLFNNALEIGLEEYIRSMSFNRRQWYPEGLILKKGKSKDARQRHVLADKSIADVCEALIGAAYLTGQEKGSFDMAIKAVTAMVKDKKHRMISYGDYYAVYQKPTWQTESANSAQRDMAKKFSERMGYKFKHPRLLRAAFQHPTYPSLYERLPSYQRLEFLGDALFDMVAVDYLFRKFPAADPQWLTEHKMAMVSNQFLCCLSFHLGFNKCIATMSPSILKDIAEYVTEIEEALETAKQEAINAGKTADEYSRDYWVHITHASRLPKCLSDVVEAYIGAIFVDSEYDYSVVQNFFNMHVLPFFEDMHLYDTFANKHPVTFVANMMAHKFRCNEWRSFAKELDTDVTEGRGGRGGNGAVAGEISEINPPKVVSALLVHGKTVVHAVAASGRYAKSAMAKKAIKLLEGMSVEEFRERLGCNCKGVPMEVDGGVPEADVDGEVHGTAV
The following text describes a protein:
Function:
Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stranded 3'-5' exonuclease activity and single-stranded endonuclease activity.
Sequence:
MVQILHISDTHLGKRQYSLVEREKDIYDIFSQLVDIAIKEHVDVIIHSGDLFDVSSPTTNALVMAIKILKRLKDVNIPFLSIPGDHDTPKRKGYLIPHNILSELDLIKILNYEKPYIIKGIEVYGIPHIPTVSKSILVSALSALRPKSSRSILLLHQGVKQILPYDGSWQMELGSLPKGFGYYALGHIHTRWRLTQDDGSVIAIAGSPDIMREEEIEGYEKFGKGAYLIDFSKDLPILSTINITVRPQKVVTINTKNIKKDILTIRDDLIEHNKSENNKPILHIIVEGERMRKDLLYKELLPLNDVALYYRIYKDETTQTVDNLSYTLPRDKGLDKIIIEYLTKYEKFSEDEANLILQMIKNVESDEIVNEILKKLTGVNL
The following text describes a protein:
Function:
Involved in symbiosome development.
Subcellular Localization:
Symbiosome, peribacteroid space. Symbiosome, peribacteroid membrane. Note=Also associates directly or indirectly with the cell surface of Rhizobium bacteroids within the symbiosome. Glycosylation variants NLEC-1A and NLEC-1B are abundant in the peribacterial space while NLEC-1C is probably cytoplasmic.
Sequence:
MAFYRTNLPTRELFSLVSVVIVLLATNINSVQALSFNFTKLTTANSGVTFQGDAQILPSGLIALTKSSPFPPGQYFTTVGRALSSNLVPLWDSATGKAASFVTSFSFVIDTTEGPITDGLIFFIAPPGTVIPQNSTTPFLGVVDSETSINRFVGLEFDLYRNSWDPEGRHIGIDINSIISTKTVTYNLVSGSLTKVIIIYDSPSSTLSAAIIYENGKISTISQVIDLKTVLPNTVQIGLSAATLTGESYSIHSWSFVSDLETTASYVSNI
The following text describes a protein:
Function:
Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Also plays a role in the assembly of the exocyst.
Subcellular Localization:
Bud. Bud neck.
Sequence:
MTRTSITLNVNPHTEVQAQRKRELESKLDDEVVNLELLQTSLKKTDMLTEKMQTILSSFDQRLSKLETFILPIYKSTQKLTKMHTNIDSALAQIEGFTSTLSVIKQHEAIVTKGPQGIPLAVYLESISKLKESLQNLETTKYKSSERKIQALKDTLWKGIRQLDEMFSQKLQAASDAIDPSAYQVDDDVVPSPIPDAQLSELHNLASALAESLIEIGPISAFIKQYEEIRSAHLVKSLASICQTTKDEELKSVHQRGTYQKGSSLLTQYGKNLLILLNTEHALHLKIIPKHHAVTTFAQTIVLSVDGFLDACESMLNRVRRNIQRRDINDVYMLIDVWDDLSNLFGKHVGLLAYCGKKGHDIDLVLANCSTTAISYFKEVYDEFRVDSEKKQAALSVDGTVHETTSKTINTLKRLLDFSLAMEHIIMSSQGNPGALPVTSFPEFVSKMIEALVTDLEIKSRGYKKSTLTTLFLLNNFHYILKGLKSCRLVDNLNSDTLDMVEKSIKKQLDVYRSSWMPLIEHLMDTTKISDQRIVTILSKPQREAVKERFKNFNKDFDEMFQTQKAYAIPDVELRAQVIKEVRQVLLPMYNRFYDRYVETEFSKNKEKYIKYDKDALTGALDKFFDASSESMVGRQWGRTQE
The following text describes a protein:
Function:
Catalyzes the reduction of sulfite to sulfide, a step in the biosynthesis of sulfur-containing amino acids and cofactors.
Sequence:
MPTAGSSRAPAAAREIVVVGHGMVGHRLVEAVRARDADGSLRITVLAEEGDAAYDRVGLTSYTESWDRALLALPGNDYAGDQRVRLLLNTRVTQIDRATKSVVTAAGQRHRYDTLVLATGSYAFVPPVPGHDLPACHVYRTFDDLDAIRAGAQRTLDGGHTDGGVVIGGGLLGLEAANALRQFGLQTHVVEMMPRLMAQQIDEAGGALLARMIADLGIAVHVGTGTESIESVKHSDGSVWARVRLSDGEVIDAGVVIFAAGIRPRDELARAAGLAIGDRGGVLTDLSCRTSDPDIYAVGEVAAIDGRCYGLVGPGYTSAEVVADRLLDGSAEFPEADLSTKLKLLGVDVASFGDAMGATENCLEVVINDAVKRTYAKLVLSDDATTLLGGVLVGDASSYGVLRPMVGAELPGDPLALIAPAGSGAGAGALGVGALPDSAQICSCNNVTKGELKCAIADGCGDVPALKSCTAAGTSCGSCVPLLKQLLEAEGVEQSKALCEHFSQSRAELFEIITATEVRTFSGLLDRFGRGKGCDICKPVVASILASTGSDHILDGEQASLQDSNDHFLANIQKNGSYSVVPRVPGGDIKPEHLILIGQIAQDFGLYTKITGGQRIDLFGARVDQLPLIWQRLVDGGMESGHAYGKAVRTVKSCVGSDWCRYGQQDSVQLAIDLELRYRGLRAPHKIKLGVSGCARECAEARGKDVGVIATEKGWNLYVAGNGGMTPKHAQLLASDLDKETLIRYIDRFLIYYIRTADRLQRTAPWVESLGLDHVREVVCEDSLGLAEEFEAAMQRHVANYKCEWKGVLEDPDKLSRFVSFVNAPDAVDSTVTFTERAGRKVPVSIGIPRVRS
The following text describes a protein:
Function:
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Sequence:
MKLTVKEVKEVYKPKLLPIIWKDENNTLTILDQSLLPFQKVYVDLKDVDSTALAIKNMQVRGAPAIGITAGYGMVLALTSNKNVKTLDEAIRELTRAKAILDSARPTAVNLVWATSRMLTLAKNAVENGNAKTINELIDLMKVEAKRIFDEEYDAEIQMGLYGLEKLNDSDTVLTQCNAGGLATGTGLGTALSPVKLAKALGMNVSVIAPETRPWLQGSRLTVYELMEEGIKVTLITDTAVGLVMYRGMVNSVMVGADRILRDGHVFNKIGTYKEAVIAHELGIPFYALAPTSSFDLKSNVNEIKIEERDPNEVRTIRGIPIAPENVNVYNPVFDVTPPKYIAGIITEKGIIYPPFHENIKRIVER
The following text describes a protein:
Function:
Tautomerization of L-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI). Also catalyzes the tautomerization of the methyl ester of L-dopachrome and dopamine chrome. May play a role in melanization reactions during late pupal and adult stages.
Subcellular Localization:
Secreted.
Sequence:
MLSPQFLILSLISGLQLLSLADADPMIEVFRWKQMDFYNRGDGHLSSGGRKDRPSFSAPVVFPGKYSRRKRKIMTSRDTPVVVSSRADSDDPNASYIPYNNVPMGATHFRGRLFVTMPRRRVGIPSTLNYIDLAEDGSNRSPKLRAYPNFALNQFNASAENLVSVYRTSVDACQRLWFIDTGMLEYPNNRQQIRRPSIWVVDLATDQVLKRFDVPESIAETGRGLASITVDVKAGQCGDAYAYIPDLVYRRLYVYHLRNDRIWSFEHNYFNFDPLSGDLSIGGQTFRWDDGIFSITLGAQKLDGSRDAYFHPMASTNEFVVSNRVLQQESNAARSDHGNDFRVLGSRGPSTQSTMHAYDPGTGVIFFDEIQRNGVGCWKTSKPISAENYGSVDSNAEDMIYPSDLSIDEDGTIWVMSNSMPIFIYSTLDTSIYNFRIWKQKASLAKRGTVCE
The following text describes a protein:
Function:
A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'-UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Its main target seems to be the major flagellin gene, while its function is anatagonized by FliW.
Subcellular Localization:
Cytoplasm.
Sequence:
MLVITRKKGESLLIGDDIEITVVKLDDGSVKLAIDAPKNLTILRKELYNEVQEENKKATNFNPSILKNIKSK
The following text describes a protein:
Function:
Substrate recognition component of a SCF-like E3 ubiquitin-protein ligase complex that promotes target-directed microRNA degradation (TDMD), a process that mediates degradation of microRNAs (miRNAs). The SCF-like E3 ubiquitin-protein ligase complex acts by catalyzing ubiquitination and subsequent degradation of AGO1, thereby exposing miRNAs for degradation (By similarity).
Sequence:
MDRFSFDDSIRFEEDSLCSWSSEPESLCNNWRGWKKPAAGSGAGNGGLSGMGGMAVAGGSGAPPFGGAGASGSCTPGGNGTAMANTSTCGRHYEVSTLAELAARCVASYIPFELVEHVYPPVPEQLQLRIAFWSFPDNEEDIRLYSCLANSSADEFNRGDSLFRLRAVKDPLQIGFHLSASVVNQTPRAYFNVAVTFDRRRISSCNCTCTSSAYWCSHVVAVCLHRIHCPQEVCLRAPVSESLTRLQRDQLQKFAQYLISELPQQILPTAQRLLDELLSAQPTAINTVCGAPDPTAGASINDQTSWYLDEKTLHNNIKRILIKFCLPAPIVFSDVNYLTNSAPPAAAEWSSLLRPLRGREPEGMWNLLSIVREMYRRCDRNAVRLLEIITEECLYCDQILIWWFQTKLALMMGSHGHSGGKHSNTHSNSTALQHACSSLCDEIVALWRLAALNPGLAPDERDMLHAQFTAWHLKILDRVVKSRMMPSYTNKHQQNSRSETELFIGFKPAIEACYLDWEGYPIPGVTHTHDTNPIYYSPFTCFKHTDLKGESNNPGQLNATQALMSNNKHYNYFSSSSDHGMHAGAFKQRLDRPFRESRFYTNPADLDGGAALAGGGSGRFSTGLGSVAVGGAGAGGLGQMSGGVNNSVGGSAAAEVNPVQQQLPSGSAGVGASVTNAKVVVATDGNRSSASSEGFCENDDFGGDTSSSHNYCPPGQAVVPGQKSALTESDSQSSFDAVSHQSKDEPPVGGVGVAVGVEQALSTSDTSSASSSSSSASTASGSSNSSTSSMLMAGQEATVGVGGAVQQTTRRLSKDESFSSSSDEFNQGGVGGSAGRVAMASSGSGSGAGDTVAVGSGSTAGGDLTPVPSTSAAARAALAASSTGPVISASPHLAASAAGGLGVLGVGADQPCTSSAHAARALAAAVAASSDKPHVFSNVRPTEDAWDILLARAEGLHAHGHGAEACILAVRLAEQMLANPPNLLLELPPAPKRKGKKQNVNPISHQLTVVASATLSKCAFLCTVLSENSEHYHIGFRICLFALEMPRPPASTKPLEVKLANQEADILALLKRLPLGSAELQVIRERAEQLRSGTFKTRGEALLPINLATFIFDALVTLSPLGGSTIVPGVASTSGVSSAAGKSMVNTGTRLLLYKHNSDESLGFDAAVAALGLKANVSEAEHPLLCEGTRRQRGDLALTLLSHYKDEPRKIAKIMEKLLDRDIHTLLNAPLLPAYYSSNPPVRTRSNQPTRREDHDYGGGSGCASSNCNPVANLCELLPADYGSVGGNSRPHSSTSAELELSMCALSMASSGSQSGGVQGMVPTTNAAGTTGTPSSSSTTVSGSQNPNGNPSGSGGGGNGGGGNGGGGGGGGGGGGSTSSRSKESRYKGKRAYPSIPNQPSEASAHFMFELAKNVLTKAGGNSSTSLFTQASTSQNHHGPHRALHMCAFQLGLYALGLHNCVSPNWLSRTYSSHVSWILGQAMEIGAPAISFLIDTWEAHLTPPEAAGMADRASRGWDSNMVYPAAELALSVLPHAAALNPNEIQRAILQCKEQSDLMLERACLTVETAAKGGGVYPEVLFQVARYWYELYMRNTPNNSEFEPHDDTMDHSAVSLSALIESQQQHELQQQQQAVQQQQAVQQQQQVVQQQQQVVQQQQQLGMPNSVVPGGVGPGPGLPVAVQPPVVGSVQNPQAQFQPVGVASLAPLGLAQYPPYSFCQGLYAHHHNMSYPPGQMQMFISAGPPPPPQAYGGYQQPPPQQPPNPQQQQQVVQQQVQQQQVVQQQQQQVQMAGQAPPGHPGQQGHPGQPPSGFQPQPPPGAFQALPPQAYQAMQAGPPGPPMGPPQGYYGPPPPPPPNGPPGVGVGVGVGVGVGVMPMRQHQHQHPVYPFMQQAPPQPPQQQQPPPSQPPVRQRQPHQFTPTQLRYLLAAYNVGMLAMETLARRVHDDRPQAKYARNPPYGEDVKWLLRISKKLGTQYLHQFCICAVNSIVSPFVLHDVAIESAHYLGRNNHQMVMQHLRSALTPLVQKCQQMYIQCIHQKLYHLTQGDYEEFASIVVAARAAFQITPEGNAQFKDWLQSIKRSKSCKKELWTQINAALQSNSK
The following text describes a protein:
Function:
Glycerophosphocholine glycerophosphodiesterase responsible for the hydrolysis of intracellular glycerophosphocholine into glycerol-phosphate and choline. The choline is used for phosphatidyl-choline synthesis. Required for utilization of glycerophosphocholine as phosphate source.
Subcellular Localization:
Cytoplasm.
Sequence:
MKFGKTFPNHQVPEWAHKYVNYKGLKKQIKEITLVQDALFRQEQGAASQDGPARRRGRESKEQYLGHPEVKKLLAAFFFALDRDIEKVDGFYNMQFMEYDRRLRKLLSSAQLADITSVQRGATGYLHAPLPQYIAYGERERDGLPERYVPPHATDMSEDLAEVLTILLELRSHFRNLKWYGELNKRAFTKIMKKLDKKVGTNQQHSYFQARIKPLEFADDTPIVKALATINEILDRISPCVKDLQDKLRGEDRRLLQGSSSPIDVASQLVTKDDGAGLINELISMYRSVVLIPTRTLVTLLNKSALSRSFSCVDEILGIIPTLGDPSDINGRNFFHHHVIALGKKRTKSLEERDNINSLLSDSLDLEAAIPPEPNTRLVGAFGPDGVNSDDSPAPLSHILQQLPAHLRPSLLQRDNYKRTPLHYSAQYGLCEVTRIILQALSEWDAWNADVAIDDIDVWGDSENLTPLHLAVIGTHPLTVSTLLSFMNPEKSLNSPRLLHLATRLNSPSLLNSLLSAKGFDIDYQEPENLETALYVACKLDIYEAAEYLVKQGANMELGEKLFGWTPIFAAATEGYARIVQLLVDHGAKYDLFDESGWTPMEHAALRGHLDISQLIRITDNKAITRPKFATDWNKSTRPTETTNGLLSALTPSESGSTTTGSENKSSSLTPSTSNEMYALPARSSTSIDKISEPNKGNHRKVLKSQLSHGKVQTIKDTQLPQQPIKSFGHSFLQKDESVILLTLGTNDNRSTIPAVSLNKVPVAKASSTELDTALSLLVTCMDNLDAEPVMLDLPLHENLDSVTFKVPYKKDSSYTIFFDIVPTYGYSMANMNRENSSGMHSNVGNSTGPAYLDAQVGQCGSRLHYDQLGRDTPNTYDQRSRHQASQQKEQIATKKQSKILGRAVALLDSAPTSVGPNRRSIAEAITIPIIGSDTLEVLGIIRFDFLVVTPFVHKNLSVGPAETYWKSLVSTRVIGHRGLGKNMNTNKSLQLGENTVESFIAAASLGASYVEFDVQLTKDNIPVVYHDFLVAESGVDIPMHELTLEQFLDLNGERQRHQDAREAHRNHRSPNGRRLSMDDSSAELIKRSLMMRGDEDRTARDLNTIYGDRMRLTRTFKKNAFKANSRGHAIASSFVTLKELFKKIPQNVGFNIECKYPMVDEAEEEDIGPIAVEMNHWIDTVLEVVYDNVEGRDVIFSSFQPDVCLMLSLKQPSFPILFLTEGGTAKRCDIRAASLQNAIRFAHRWNLLGIVSAAAPIVIAPRLAQIVKSSGLVCVTYGVENNDPEIARVEMDAGVDAVIVDSVLAVRKGLTREAQDADTL
The following text describes a protein:
Function:
Mitochondrial protein that is likely to be responsible for thermogenic respiration. Likely to function in mitochondrial uncoupling i.e. creating mitochondrial proton leaks across the inner mitochondrial membrane and can therefore dissipate the mitochondrial proton gradient and convert the energy of substrate oxidation into heat instead of ATP. Involved in cold tolerance, it is required for development to the adult stage at low temperatures.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MDKAERDYWHLRSLEIEEEPRFPPTNVADPLTARNLFQLYVNTFIGANLAESCVFPLDVAKTRMQVDGEQAKKTGKAMPTFRATLTNMIRVEGFKSLYAGFSAMVTRNFIFNSLRVVLYDVFRRPFLYQNERNEEVLKIYMALGCSFTAGCIAQALANPFDIVKVRMQTEGRRRQLGYDVRVNSMVQAFVDIYRRGGLPSMWKGVGPSCMRACLMTTGDVGSYDISKRTFKRLLDLEEGLPLRFVSSMCAGLTASVLSTPADVIKSRMMNQPVDESGKNLYYKNSLDCVRKLVREEGVLTLYKGLMPTWFRLGPFSVLFWLSVEQLRQWEGQSGF
The following text describes a protein:
Function:
Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTASTALTVAIWIGVMLIGGIGSVLRFLVDRSVARRLARTFPYGTLTVNITGAALLGFLAGLALPKDAALLAGTGFVGAYTTFSTWMLETQRLGEDRQMVSALANIVVSVVLGLAAALLGQWIAQI
The following text describes a protein:
Function:
Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde. Can also convert 6-pyruvoyltetrahydropterin (PPH4) and sepiapterin to CPH4; these 2 compounds are probably intermediates in the reaction from H2NTP.
Miscellaneous:
MISCELLANEOUS: The active site is at the interface between 2 subunits. The proton acceptor Cys is on one subunit, and the charge relay system is on the other subunit (By similarity).
Sequence:
MMSTTLFKDFTFEAAHRLPHVPEGHKCGRLHGHSFMVRLEITGEVDPHTGWIIDFAELKAAFKPTYERLDHHYLNDIPGLENPTSEVLAKWIWDQVKPVVPLLSAVMVKETCTAGCIYRGE
The following text describes a protein:
Function:
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MVIYSVLVAENVSHCNETISQPDVERSASTVQPSCSTTTKTPSSPTKVSKISILHLQNHDYRKSGGGKGLALVGATVAGAGGVVGYSYVDPEFRHKVEVTVPGAEQVLEAVLGKSNLDKTKKEIKEAVVAAVPKKKEVLPPLELAPLPPVLPKEPVHVDPIDVRKDVTPIVAKPSPDVVVAKNKQLEDRLKIAIHSAEGKVRIATEAKLKTINAINEHAAVLKQTVDDAKNANWENVTAALQRAEAEARVDSGQEVDGRNYIDNLRKIVNDGKKDSTTATNPLLLNAQETANKLTHQLDEINALVNKVSSSTQNLIIQKVFQSRQESAVLNQYKDLIEKSRQQFALEMKSILPNVDVHAKVRVGEEVGKPFKKKEWFGDKKGNWKPEKRKEKRLKDKNLNEEELNALIAHAHLKVDQLRRQLSDQQVREELHISKALEEQRAADERIASEKLSIEMSRVGLQKELEIERALVESRSSWEGELEDKLKRTASAHSEHLEQVIRTQRQLFEIEQNQKVEEAVLKERGLHSKQVGAALSRLAGIEEALGSRVALDNENRRAKQFWIACHNLIDTLKHGNKAGNNIDERRLPLNESLNLLKEVSVNPEDEFVTAIIGSFPTQATTVGTYTEQDLKNRFEQLYKVGRKTATIDENGGGLGAYFWSYVKSIFLVDMPRQYSELDAIDVNNADNYEILSRAKQYVHNGDLDKAIRVVQLLKGQPAHLAHDWVLDTRAYLESRLLAQLLVAHAAVSSIRSTY
The following text describes a protein:
Function:
Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway (By similarity); The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters (By similarity).
Sequence:
MTRPVLVLVHGWGCDSRTWQPVLDGLRELVPVQLVDLPGFGNTPALETFSLPAVLAAIESQLPERCVLLGWSLGAMLAVQLAARLPQQVLGVISLAANARFVASDDYPHAMAPDVNRQFNSRFAEQPQAALKMFTGLLAQGDVQERALLKQLRTQVPDAINHNWAQALQLLAELDNRAALVQLSQPLLHLLAEQDALVPIAAAESLRGLNSQHQIHVIAGSAHAVHWSQPQQLISAVQDFYETLATAVDKKRVAQSFGKAAATYDSVAGLQRAVGAQLLDYLPAQLDRTRLLDIGSGTGFFTAQLATRGAEVIALDIAQGMLDFARQQHPQAADWVCGDAENLPFAQSSVDFIFSSLVIQWCARVPQLMQELARVLKPGGRAYISTLGPGTLVELKRAWQQVDNYVHVNRFVGRTSLEQAVQQAGMQCLAFVESTRRLYFSRLRDLTHELKALGAHNINPGQAQGLTGRQRLQAFSLAYERERSPQGLPASYEVYYLVLCKP
The following text describes a protein:
Function:
Multifunctional protein that plays a central role in mitochondrial DNA base excision repair (BER) pathway induced by oxidative stress. Has apurinic/apyrimidinic (AP) endonuclease activity towards double-stranded DNA (dsDNA). Has nucleotide incision repair (NIR) activity; acts on dsDNA with oxidized bases thymine glycol and 5,6-dihydro-2'-deoxyuridine. Has 3'-5' exonuclease; can use dsDNA templates with 3'-OH termini including blunt-end, gapped and mismatched 3'-recessed. Has 3'-phosphatase activity; cleaves 3'-phosphate from blunt, recessed and gapped dsDNA templates, followed by 3'-5' exonuclease activity. Has RNase H-like activity; cleaves RNA on 3'-recessed RNA-DNA duplex. Plays a role in merosome infection of host erythrocytes (By similarity).
Subcellular Localization:
Mitochondrion.
Sequence:
MKITSLHFLIFHKNLNYVSSKVKAKKIFYQRALNNIYLCTIRTMIVDIAEIKKRDNHALDTQESQELVNKIKEIKNSDEQNNSNNNNNNSSSSNFCSNNNSPFSHKETKLMVKEEVPNSIVKNILNNNSCATSIINNKFYTQINNIIPVKPEAMKEENINVSTVNTENDISKEKKENSHYFCDEIKVMKKEYSKDDFVTDVKLEMNDKEEEEEEKQKIGQESTHINIKVEKDTFNECNNSNVNEKKRNRSVDIHNELSNKRILTEDVVVKCNIKNDVKIIVTWNMNSITVRYKNKKKWDEFMNFFNNLNADVLCFQEVRLPAMNLSEPCDNKNKNKNKNDGIRDRGKIKNSDQKSLADYEIMEQILNDDFKDYNAYFSLANIKYSGQLVLVKKNIHIESIRYNLFFENNAHIHHDEGRVILVEFSNFFLLSTYTPNNGFDHVKFERRRLFDEQLQKFVTILRNEKQKPLVWTGDLNIAPEDIDLSHPAEFRRMKKGNVPKEFIGQPGCTDFERKNFQKILTAGNLVDSYRYLQNIKLNEDKKNNIKHTPNINDNIYTWRCPFLLGKSCNKAMRIDHFIVSKEFLNRINKIHIQGFSVFHNNFYGSDHCPVILYLKNE
The following text describes a protein:
Function:
Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro).
Sequence:
MDYSHFVTTVSAARRTNPARMTNELAKKMSSTIMLSGGMPNADYFPFKSASISLNDGTTIEIGEELMKKALQYGAAEGNHELLLWLEDLQMKLHNPPTAHYTPEKGKMRICVTTGSQEGLSKVYDMLINPGDNILLDEPNFSGTMAALRPLGCNIIKVPSDEHGIIPKALKEILSRWKSDNNTHKLSNKRPKFLYTVPNGGNPSGSSLTAERKKEIYQLAQEYNFLIIEDDPYYFVQYEKTKAPSFLSMDVDGRVIRGDTFSKVISSGLRIGFLTGPDPLIDRIVRHVEASTMQTSTFTQVLIVQLLKKWGHKGFLQHVGRVSEFYKSQRDLMLAAANKWLKGLADWYTPKAGLFLWMKIKGISDTHHMIMEKAIDRGVSLLPGRDFMIDASEPSPFVRASFSYASPAQMDQGFQRLAELIREETA
The following text describes a protein:
Function:
3'-5' exonuclease.
Subcellular Localization:
Cytoplasm.
Sequence:
MNKQRFVVIDVETTGNSPKKGDKIIQIAAVVIENGQITERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQLLDGAYFVAHNIHFDLGFVKYELHKAGFQLPDCEVLDTVELSRIVFPGFEGYKLTELSEELQLRHDQPHRADSDAEVTGLIFLEILEKLRQLPYPTLKQLRRLSQHFISDLTHLLDMFINENRHTEIPGYTRFSSFSVREPEAIDVRINEDENFSFEIESWEAGNEKALSELMPGYEKRDGQMMMMREVADAFANREHALIEAPPGIGKTIGYLIPAALFAKKSKKPVIISTYSTLLQQQILTKDLPIVQDLFPFPVTAAILKGQSHYLCLYKFEQVLHEEDDNYDAVLTKAQLLVWLTETNTGDVAELNLPSGGKLLWDRLAYDDDSYKRSRSEHVIGFYERAKQIAMRSDLVITNHSLLLTDEGSHKKRLPESGTFIIDEAHHFERAASEHLGKRATYIELHTKLSRIGTLKEQGLLKKMRQLFQRNSLPVDSFFELEEWLQHVQAESDAFFSSVHSFVKRRKPKEDLNRLVFKVNKESQDKSWSILTDGAERLCSMLTHLQQLFEAQSSLMEKHLKGMKSKTVFLADEYQRSMKGLQHYCQTLQKLFFGSDDDEAVWIEIDAKGAKNAVAIYAQPLEPGELLADQFFARKNSVVLTSATLTVEGSFQFMIERLGLSDFFPRTMRIESPFSYDERMQVMIPKEMKSIQDTGQPEFIQDTARYIELMAKEKQPKILVLFTSHDMLKKVHQELKHNMSASGIQLLAQGITGGSPGKLMKTFKTSNQAILLGTNHFWEGVDFPGDELTTVMIVRLPFRSPDHPLHAAKCELARKKGKNPFQTVSLPEAVLTFRQGIGRLLRSAGDKGTIIILDRRIKTAGYGRLFLDALPTTSVSEMTDSELEAYVAGEKE
The following text describes a protein:
Function:
Part of the multicomponent carbazole 1,9a-dioxygenase (CARDO), that converts carbazole (CAR) into 2-aminobiphenyl-2,3-diol.
Sequence:
MTDTHYDVVIVGAGHGGAQTAIALRQNGFAGTIAIIGAEPDLPYERPPLSKEYLAAEKGFERILIRPASFWNDRHIAMHLGCAVERVDPTQRLVFLADGRSMGYGDLVWCAGGSARRLDCTGHDLGGVHYVRTRADTDALAAELPGVSKVVIIGGGYIGLEAAAVMAKFGKNVTLIEALDRVLARVAGEPLSRFFEEKHRSRGVDVRLRTKVGCLLGQDGRVTHVELNDADPIPADLVIVGIGIIPAISPLVVAGAKASNGLLVDASGRTSIPHVYALGDCAAHVNSFAPNDIPIRLESVQNANDQAVVVARTICGTAAQYHAVPWFWSSQYDIRLQTVGLTAGYDQTFVRGDPATGSFTVVYGRDGRVIALDCVNATKDYVQGKRLVEAKALIEPGMTDPQYPLKNFMTPSPA
The following text describes a protein:
Function:
Catalyzes the hydrolysis of the cyclic ribose-phosphate to form alpha-D-ribose 1,5-bisphosphate.
Miscellaneous:
MISCELLANEOUS: The sequence shown is that of strains K12 and B.
Sequence:
MSLTLTLTGTGGAQGVPAWGCECAACARARRSPQYRRQPCSGVVKFNDAITLIDAGLHDLADRWSPGSFQQFLLTHYHMDHVQGLFPLRWGVGDPIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDTAGLPEKTLKFLRNNQPQVMVMDCSHPPRADAPRNHCDLNTVLALNQVIRSPRVILTHISHQFDAWLMENALPSGFEVGFDGMEIGVA
The following text describes a protein:
Function:
Could act as an H1-type linker histone. Has been shown to bind DNA.
Miscellaneous:
MISCELLANEOUS: Present with 6560 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus. Chromosome.
Sequence:
MAPKKSTTKTTSKGKKPATSKGKEKSTSKAAIKKTTAKKEEASSKSYRELIIEGLTALKERKGSSRPALKKFIKENYPIVGSASNFDLYFNNAIKKGVEAGDFEQPKGPAGAVKLAKKKSPEVKKEKEVSPKPKQAATSVSATASKAKAASTKLAPKKVVKKKSPTVTAKKASSPSSLTYKEMILKSMPQLNDGKGSSRIVLKKYVKDTFSSKLKTSSNFDYLFNSAIKKCVENGELVQPKGPSGIIKLNKKKVKLST
The following text describes a protein:
Function:
Innate immune adapter that mediates the recruitment and activation of IRF5 downstream of endolysosomal toll-like receptors TLR7, TLR8 and TLR9. Following recruitment to endolysosome by SLC15A4 downstream of TLR7, TLR8 and TLR9, specifically recruits IRF5 transcription factor via its pLxIS motif, leading to IRF5 activation and subsequent expression of type I interferons. Plays a role in the regulation of endolysosomal pH in immune cells such as B-cells, dendritic cells and monocytes.
Subcellular Localization:
Lysosome membrane. Endosome membrane. Nucleus. Cytoplasm. Note=Recruited to endolysosome following interaction with SLC15A4. May colocalize with TLR7 in the endosomal pathway.
Domain:
The pLxIS motif constitutes an IRF5-binding motif: following phosphorylation, the phosphorylated pLxIS motif of TASL recruits IRF5.
Sequence:
MLSEGYLSGLAYRNDIQWSYPSSNEQVAEEKEEEMEATAAASLSYSSVDETQVQNLYVSCKSSGKVISSVYSRESQHSRNPRITVLQTNPNPVYESPNLAAVELYRDTSRETYLVPPSCKSICKNYNDLQIAGGQVMAINSATTDFPSEGSFQYGPLLKSSEIPLSMEDSMFTQPSDLPPTPIQRYSSYWRITSIKEKNSLQMQKPISNAVLNEYLEQKLVELYKQYFMDTGFHDSSPTQILASELIMTNVDQISIQVSIEKNLEISKARDIVINRLLQYGSTEISTQSLHISQYSNVNP
The following text describes a protein:
Function:
Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
Sequence:
METDSPLFGSFLPSSHDSLLERLAFVGVPKERCSKQALVEFVRANPSKISEIVSALLPTDEEVKSELKETRERSRKKRFSETMNWLQWLMFEEDPGVSLSNLAELNVDQRGVCGSVWGHNDIAYKCRTCENDPTCAICVPCFENGDHKLHDYSVIYTGGGCCDCGDETAWKREGFCSKHKGSEQIQPLPENLANSVGPVLDALFACWSGKLSSAESIVQKDALVVLLQKMSNELTFAVVEMLLEFSQSTESLLSFVARRIISSGGLLNYLVKAERFLDQDVIRKLHDLFLKLIADPVFKSEFAKAFASYYPVVISEAVKLGSDNAFKKFPLLSAFSVQILTVPTLTPFLVKEMNFLAMLLGCLNDIFVSCSGEDGVLQATKWERMSEISDRVMADLKFVTSHVVVSKYATHEHRELSRSWLLLMTFAQGMNRIKRETGIHIEDDNEYMHLFFVLGHSIAVIHSLLVTGTYSAANDKEIENEGTTKAGLDKCDGDGERYAKVGRLSHEDSVCTAMVSSSSSDSSIVPENKIDPFRARLPSSAIWLIRECLKVLETCLEDDEGISKFLCRNVSGSTMSWPKRKFSKVEIGRSVSSSLASSSRDPSTGLSPLCGDIQTNLSLDNVDGSNGEVQTDVKAYSRGVSCNSSDPNASGVHILGLCDWPDILYDVSSQPISVHLPLHRLLSLLLQKALERCYGESALHHGVNVSHEIPQADFFSYVIGDFHPYGFSALVMEHVLRIRVFCAQVIAGMWKKNADSALVTCELYRSVCWSEQGLELDLFLLQCCGALAPADSYVNKLLDRFGLSSYLSLNPNMTNEYEAVLVQEMLALLIQILQERRFCGLSTVESLRREIIFKLATGDFTHSQLVKSLPRDLSKSDELQEGKYSLRSSCWKELDLYHPRWHSRELQSAEERFSRYCGVSAVTTQLPRWRMIYPPLKGLSRIGTCKATFQIICSTLYYALQSGSSVKSRAQDGVLISALHLLSLSLDICTQQRGSNIQACCVEDSIPILELAGLEIIGLNQGTGKESLLSLLVSLMRTREGDGLHQFPEAGSCNISSWIGNLLKKFSEIDSVCMNLLQSLAPEVVGHSVFDKATSGSASDDTRKAKARERQAAILAKMKAEQSKFLSTMSSSMDDDDLRSETETSDSVVEHDSEIAIREVCSFCHDPDSKDSVSFLIFLQKSKLLSFVNRGPPSWDQCPQSEKKIPMDEAPDLQRINVSSDSLRMISHVLQLSDDATSESATDYVLEALTARLLGNGQKEKRSSDARGKDESNLESLETAMYQTVRKKTENMLNQSLTHVNHRQPDSESSSERSSVGGLSTLHRFQDIRSKQTSRYLDVSADGFHPADCDGIYLSSCGHAVHQSCLERYLNSLKERSDRRNVFEGAHIVDLVQGEFLCPACRRLANSVLPACPVDLCSVSKLQESSHAKLGRLDEQIPSLWLSEALCLLQSAANVIEDGDTLKTVSLQGDEPRRKDLQSVSNKLWNFYFSKRQEKPPGSSWLPQSIIMWDTLKYSLISMEIVTRCGKNTMLPVYGIDSLYEEFKTSKGIALSLLLRVVQSTRTKNALHVRQRFMGMKYLAESICSGMSSTSSSSIFESEGAAGSWKNINLLWSRASDPVLAHDPFSSLMWALFCLPSPFITCEESLLSIVHIFYSVSVIQTVITYCAGRLCYTSELDFKENLLSDISIALRESGGWEYFRSNNMDLSCDIKETIRKYSLPFLRRCALLWRLLKTAPGKFHEEVHMFDVPSDSNSHYMDFMYSPQSELKHVDELEKMFKIPPIDTVINDELLWSSSQTWLRHFQMEYRVNRVKGPLCITPLVPFQLMKLPNLYQDLLQRYIKKPCSNCTKVIEEPALCLLCGRLCSPIWRPCCRESGCQTHAVTCGAGTGVYLLIRRTTILLQRFARQSPWPSPYLDTFGEEDIEMARGKPLYLNEERYAALTYMVGSHGLDHSSKVLNQTTIGAFLT