lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Ubiquitin E3 ligase that acts as a limiting factor for crossing-over during meiosis: required during zygonema to limit the colocalization of RNF212 with MutS-gamma-associated recombination sites and thereby establish early differentiation of crossover and non-crossover sites. Later, it is directed by MutL-gamma to stably accumulate at designated crossover sites. Probably promotes the dissociation of RNF212 and MutS-gamma to allow the progression of recombination and the implementation of the final steps of crossing over (By similarity). Modulates cyclin-B levels and participates in the regulation of cell cycle progression through the G2 phase. Overexpression causes delayed entry into mitosis.
Subcellular Localization:
Nucleus. Chromosome. Note=Associates to the synaptonemal complex.
Sequence:
MSLCEDMLLCNYRKCRIKLSGYAWVTACSHIFCDQHGSGEFSRSPAICPACNSTLSGKLDIVRTELSPSEEYKAMVLAGLRPEIVLDISSRALAFWTYQVHQERLYQEYNFSKAEGHLKQMEKIYTQQIQSKDVELTSMKGEVTSMKKVLEEYKKKFSDISEKLMERNRQYQKLQGLYDSLRLRNITIANHEGTLEPSMIAQSGVLGFPLGNNSKFPLDNTPVRNRGDGDGDFQFRPFFAGSPTAPEPSNSFFSFVSPSRELEQQQVSSRAFKVKRI
The following text describes a protein:
Function:
Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation; Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.
Sequence:
MFSCHPFSEECTKALNQVVAYHLHTSHVYFAMAHSFMTGKKETFPFVQHFETLADSRREYANRFLNHLWTRNKKICPPPTYEKVDMKEITTPKSALLMAQNMEETLTKILLALKAAARRESDLLKFLTSVLCKQREFKEYLESQLSPPQKGKRKNEKEAQTEQPSTSSGVKGYLSSKRSKPGDHKATTTSNC
The following text describes a protein:
Function:
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Sequence:
MTTESLETLVEQLSGLTVLELSQLKKLLEEKWDVTAAAPVVAVAGAAAAGDAPASAEPTEFAVILEDVPSDKKIGVLKVVREVTGLALKEAKEMTEGLPKTVKEKTSKSDAEDTVKKLQEAGAKAVAKGL
The following text describes a protein:
Function:
Probably plays a role in patterning events during embryonic limb development. May also be involved in programmed cell death.
Subcellular Localization:
Nucleus.
Sequence:
MAPAADMTTAPTGVRSDEPPASAFSKPGGGLPVAAAMGGEEESDKPKVSPSPLPFSVEALMADRRKPPGGRDGPEGSGPPLGSARANLGALTTEAPTSPLPLGGHFPSVGALGKLPEDALLKAESPEKPERSPWMQSPRFSPPPPRRLSPPACTLRKHKTNRKPRTPFTTAQLLALERKFRQKQYLSIAERAEFSSSLSLTETQVKIWFQNRRAKAKRLQEAELEKLKMAAKPMLPPAAFGISFPLGGPAVAGASLYGASSPFQRAGLPVAPVGLYTAHVGYSMYHLT
The following text describes a protein:
Function:
May have a role in growth and in the early stages of development. Affects the timing of development.
Miscellaneous:
MISCELLANEOUS: The PTPase domain is interrupted by a PTPase insert which shares no homologies with other PTPase proteins.
Subcellular Localization:
Cytoplasm. Cell membrane. Note=Might be tethered to the plasma membrane.
Sequence:
MGSVESSNQMNGSIENKTNKIDISVLRPLPTRSNSSISLSSSSHSSFSRMGSLGSLPTNSGSSSPYYNNSSFDLVDEERIKSSIYNLKNHIKCIHKIKEEFRLLEESVGPSETSEGDKKHNTSKNRYTNILPVNHTRVQLKKIQDKEGSDYINANYIDGAYPKQFICTQGPLPNTIADFWRMVWENRCRIIVMLSRESENCRIKCDRYWPEQIGGEQFSIYGNGNEVFGTYSVELVEVIQDPEREIITRNIRLTFEGETRDITQYQYEGWPDHNIPDHTQPFRQLLHSITNRQNQIIPSSDRNVPIIVHCSAGVGRTGTFCTAVIMMKKLDHYFKQLDATPIDQVVDPFTHLPITEYQSDNLDLKGLGYHFKSSIYNSNGINNNNNNNLNNNNNINNNSNGSNNTPQTEPNNEEDDDDAAESDLKYAIMDKYNSRIDFNLFSIVLKLREQRPGMVQQLEQYLFCYKTILDEIYHRLNCKLGFSLPHVNNINNYNNYSNTTTTTTSSLASTTIIHPSTNSKLN
The following text describes a protein:
Function:
Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MKNKVSLDSIISIVEMNVKFYRLLGLAPFELNTSRVRLSKPFCCAVGGFVTLYWTAMVSSIATSNHANDRISRISNYFQLITNAIMLTAILLMPAFRLRNFAEVTRALRKLEQDLQQDAIPTNCRQMARWNIGIVVGTVTVLLLATAFDCYVTVFRGFIRVDYWIITILPQFVNVIAVTQVVLLLLYINARFRKLNQLLEEEQHPVAGRKRFERASRLAGNMPANEPKKMSLHVIEVHGCGIDAANLKHLQLPKVLYRYNDLYDICKLLDRYFGLLFLLTFTSIFIVTTIQLYYSYTILYWFTGENGFTIWSLMVCLNTISINLGVLLTIVLLCEKISNKTKHANDLLADLQLRGSRYMSSEEVIKLTVPFQAPNKVFKFSAMGFFQIDCNMLCGMIGAITTYLVIYIQFYILYADEVKKSSFVSRFQI
The following text describes a protein:
Function:
Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Sequence:
MAAPAPGLISVFSSPQELGASLAQLVAQRAACCLAGSRARFALGLSGGSLVSMLARELPAAVAPAGPVSLARWTLGFCDERLVPFDHAESTYGLYRTHLLSRLPIPESQVITINPELPVEEAAEDYAKKLRQAFQGDSIPVFDLLILGVGPDGHTCSLFPDHPLLQEREKIVAPISDSPKPPPQRVTLTLPVLNAARTVIFVATGEGKAAILKRILEDQEENPVPAALVQPHTGKLCWFLDEAAARLLTVPFEKHSTL
The following text describes a protein:
Function:
May bind and stabilize microtubules during myotubes formation.
Subcellular Localization:
Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line.
Sequence:
MNFTVGFKPLLGDAHSMDNLEKQLICPICLEMFSKPVVILPCQHNLCRKCANDVFQASNPLWQSRGSTTVSSGGRFRCPSCRHEVVLDRHGVYGLQRNLLVENIIDIYKQESSRPLHSKAEQHLMCEEHEEEKINIYCLSCEVPTCSLCKVFGAHKDCEVAPLPTIYKRQKSELSDGIAMLVAGNDRVQAVITQMEEVCQTIEDNSRRQKQLLNQRFESLCAVLEERKGELLQALAREQEEKLQRVRGLIRQYGDHLEASSKLVESAIQSMEEPQMALYLQQAKELINKVGAMSKVELAGRPEPGYESMEQFTVSVEHVAEMLRTIDFQPGASGEEEEVAPDGEEGSAGPEEERPDGP
The following text describes a protein:
Function:
Involved in DNA recombination.
Sequence:
MGVFAISLLSQTVCLYFTFFSLGIALGVLFSFKIFTKKLSRQHEIIRDLEHSKAILQMSLDTRRSQEQLMEEFSHKLTSVSQAFARDMKTESQEFFSEKTQAITSVLAPVHNTLSAFKQNLENFETKQAEDRGALKEQLSQLLTAEQKLERETQALTNILKHPGSRGRWGEIQLERILEISGMLKYCDYSTQTVDSSESSSRADIVIRLPQNRSLVIDAKTPFSEEYLTDNHADPTDLVKKIKDHIKTLKTKSYWDKFEQSPEFVILFLPGESLFNDAIRCAPELMDYAGQSNVILSSPVTLMALLKTVTHVWKQENLQNQIREIGQLGKDLYQRMHKLFDHFHKVGKHLGQAVHSYNDMSSSLSARVLPILRTFDKLELSSSHNKIEALSQVSTLPHSPKVPYPENDLAECLSPEASYLKPPSSNQ
The following text describes a protein:
Function:
Substrate-recognition component of a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex, also named CRL5 complex), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as BIK, DIRAS2 and RPN1. The ECS(ASB11) complex acts as a regulator of the endoplasmic reticulum unfolded protein response by mediating ubiquitination and degradation of BIK.
Subcellular Localization:
Endoplasmic reticulum.
Sequence:
MEDGSVSYGFKNIFITMFATFFFFKLLIKVFLALLTHFYIVKGNRKEAARIAEEIFGEISDCWADRSPLHEAAAQGRLLALKTLIAQGVNVNLVTINRVSSLHEACLGGHVACAKALLENGAHVNGVTVHGATPLFNACCSGSAACVNVLLEFGAKAQLEVHLASPIHEAVKRGNRECMEILLANNVNIDQEVPHLGTPLYAACTYQRLDCVKKLLELGANVNHGQWLDTPLHAAAKQNSVEIIHLLIDYGANLKCKNAQGQSALDLAAPKSSVEQALLLREGPPALSQLCRLCVRKCLGRNCHKTIHKLYLPDPLEKFLLYQ
The following text describes a protein:
Function:
Transcriptional regulator of the type VI secretion system.
Sequence:
MSQWLAFATQLVGVRKSHQLALQFVDLLTQGLDLSDSLLLLPSSDGRLLVPHDPQRQFAWSVTDFDVPFAHVLQSSNAMHLTAEELVFWQSNRTFSQLTSRVGMFDSVWIQPLPMDTRQVHSILLLMGESHGIVSAFENADFLKFIEVFSQQWSLLNDMEREEQRRLELKQSLTDIERDSAQRSLANALSRTLIGESAAMQKLREQIVSAANSQLSVMVQGETGTGKELVAAAVHELSSRKSAPFVAINCAAIPEHLLESELFGYCKGAFSGADSDKQGLIAQANGGTLFLDEIGDMPLTLQAKLLRVLESRTFRPLGGKQELSSDFRLVSATHVNLLDQVRKKEFRQDLYYRLFQYPITLPRLAARLEDIELLSEHFVRVFNLQHNTRIRGLNYRAIDCLKQYDFPGNVRELKHLIEFGCAQTADGTQVEASCFAHRLQTLPCLAPEATPVAVSVETENVDLEPSVALAGEPNFAVIHDLKQAVSQFEALIISERLNRFAGDRAKAAKSLGIPKRTLAYKCLKLEIKTP
The following text describes a protein:
Function:
Involved in flower development. Functions in floral reproductive organ identity by binding AGAMOUS (AG) pre-mRNA and promoting its processing. Functions in association with HUA2 and HEN4.
Subcellular Localization:
Nucleus speckle. Note=Nuclear with a speckled distribution pattern.
Sequence:
MAHRQLYSYALQPSYAAAASTVSPAPPPPQQPLPPKTGLSSLYGSSADHYFPDTTYRFLARDGSEALSNYSGTLASSSSMYHHLPNTTASHLAYPQLLQHQEVAWPPGVEVPGAASAVEPLPPGVKRTSEALYYPTLLGAHNTIGQTEAWYTTDYFTKRPKLESTSHLPIYPQRAGEKDCTHYMQTRTCKFGESCRFDHPIWVPEGGIPDWKEAPVVPNEEYPERPGEPDCPYYIKTQRCKYGSKCKFNHPREEAAVSVETQDSLPERPSEPMCTFYMKTGKCKFGLSCKFHHPKDIQLPSSSQDIGSSVGLTSEPDATNNPHVTFTPALYHNSKGLPVRSGEVDCPFYLKTGSCKYGATCRYNHPERTAFIPQAAGVNYSLVSSNTANLNLGLVTPATSFYQTLTQPTLGVISATYPQRPGQSECDYYMKTGECKFGERCKFHHPADRLSAMTKQAPQQPNVKLSLAGYPRREGALNCPYYMKTGTCKYGATCKFDHPPPGEVMAKTTSEADAAGATNTDTTQ
The following text describes a protein:
Function:
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component (By similarity). Required during sugar starvation and acts under the control of a sugar-sensing mechanism involving Ser/Thr kinases and phosphatases.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MIARRIWRSHRFLRPFSSSSVCSPPFRVPEYLSQSSSSPASRPFFVHPPTLMKWGGGSRSWFSNEAMATDSNSGLIDVPLAQTGEGIAECELLKWFVKEGDSVEEFQPLCEVQSDKATIEITSRFKGKVALISHSPGDIIKVGETLVRLAVEDSQDSLLTTDSSEIVTLGGSKQGTENLLGALSTPAVRNLAKDLGIDINVITGTGKDGRVLKEDVLRFSDQKGFVTDSVSSEHAVIGGDSVSTKASSNFEDKTVPLRGFSRAMVKTMTMATSVPHFHFVEEINCDSLVELKQFFKENNTDSTIKHTFLPTLIKSLSMALTKYPFVNSCFNAESLEIILKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAANNKLNPEDVTGGTITLSNIGAIGGKFGSPLLNLPEVAIIALGRIEKVPKFSKEGTVYPASIMMVNIAADHRVLDGATVARFCCQWKEYVEKPELLMLQMR
The following text describes a protein:
Function:
Involved in the uptake of ammonia.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MAGPEGSIFNASAMQIVQIHHYAEGSVTPEVDKLYQDDAVWIISSSFIIFTMHSGFGLLESGSVSAKDEVNIMVKNVVDVVFGGLSYWSCGFGFSYGDIPEWRNPYVGFGKFFYDPTRDYGTRETINQEGWSYASFLFQLSLATTASTIVSGAVAERAKLKSYILLGCIVILIQALPAHWVWDKEGVFYKKGVVDFAGCSAVHLVGGIIGLIATVFLKPRRNRFNEDSVHQMSSPTNALLGTFLLWWGWFGINAGSVWGITGGRWRLGARAAVATIMASIGGGATAITISFVKTKKLQVNFLINGILSSIVSITAICAVSRPWHALVIGSISSVFSIAVLPLLDRLHIDDPVGIVPIHLTSSIWGMIAVGIFCEEDKYLGSATNNRSGLLYSWSFELLWVQLQCTAAILIYSATTGFLALFLISKSPLGLRVTDYEEQIGADVIEHGLAGTNVARYVLEKPLSTRTFQTVTKAITKWKMLAKKKSRQKRMEAAKLKRQEEQETFTNGTAIANGNGNVLHHRTNATESNGTGAPKRSNGPAFNNQITPLAVSSTVSTARNGPSTGRRTESTAIEIEQPIEAVPPEVVAAAVLPPEERPGPSTNSNVSIEASVEKSPSSSTSRRSISIRSSPSIHTVSAISTAAPDSRPSTASATSIISKKSSKNSTVGKFVKAPAPRALSPPDNNPPV
The following text describes a protein:
Function:
Required for plastid vesicle formation and thylakoid membrane biogenesis, but not for functional assembly of thylakoid protein complexes.
Subcellular Localization:
Plastid, chloroplast inner membrane; Peripheral membrane protein. Plastid, chloroplast thylakoid membrane; Peripheral membrane protein.
Sequence:
MALKASPVTGLFPPLRPTASSSPSTSSNRPCSLRILPLRTSFFGNSSGALRVNVLRLACDNRLRCNGHGATMNLFERFSRVVKSYANALISSFEDPEKILEQTVIEMNSDLTKMRQATAQVLASQKQLQNKYKAAQQSSDDWYKRAQLALAKGDEDLAREALKRRKSFADNATALKTQLDQQKGVVDNLVSNTRLLESKIQEAKAKKDTLLARARTAKTATKVQEMIGTVNTSGALSAFEKMEEKVMAMESEADALTQIGTDELEGKFQMLETSSVDDDLADLKKELSGSSKKGELPPGRSTVAASTRYPFKDSEIENELNELRRKANDF
The following text describes a protein:
Function:
Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MPLVRYEVRCEHSLANPELYRSAARDDPESLLEGVAMAGLVGIVRQLGDLAEFAAEIFCGLHDELMTIGSRGHDLNMRVQQLEDELPAVERALLSEPNQLRFAYTNGSDWHASIRSDQNHCTSGDLPRFVRNYYEECRGPPQLFLLDKFDVSGVGACLKRFTDPSFFKLEWASTELLRAQREQRDKKARREKKKGRRSKTGHPTAAINQIPARVRYGSASLEDLEGLPHDLASVLKVEIPVPSHLGANREPSPLTPSGVPRDSKAILVEDPSLPTVKTVQVSASSKKSQGIKSVRISATDPESATPSGSTPKRSESDDTVRSSADRISKIIEQEDRAAAPDVGHVRVLETKEVKSSVESGDAADGVQVLSIDSRATNGLLREDSEAQTKPRSVRTPLGTPRANARGEFSMDLREGDKHSGNTLRGTDSPMPLKSSRRSAYMDAHDSVRLSGKFLWRKNLDGDDASPMGGRFSRQVSMARSGISGSEYDEFVDAPSRIGSEGESDFDSPGSVHRATHFNGDALNNVALQNHVEAQKTYIPPGMKLTEPSPTPGALVEISEVVTETKVVQMADNSSNGTVLKSLSPISMALNEDSTKSSSFLGQSDTSADYALVRDQQSVAQKPDNRSGEVMKSQGNGNLDSHIEVVSAIAIPKDMEESDLLFKGIDRTSSSLDSLPSATSPSHEGRDALQPSFTMSSRHSISSELISVSSDSEPTSPISPKSPAFHALYSPRGSPPRSSNNIVNSPPTAYLRSSPPRSHESNCSSLSVEEVPVLSESPTSFPRSPHHALVSERDSLPYEVVPLESEPVCLPSQPVAQLYPLPTLSMSPDRESPSNSGELCCPVIAGFGGPPSPRKDGESVHTAPAGEGDHPVLQLSSTLKHDTVTRLKEPSDRYQPAPPPLVSSNGGVTPRSPQCATPRYSVFSESTRSSLVLPSRAADSSGSSAPSSPYGSPKKSFQRIFLSSPSALASPSPLRNSVDDASSYPRRDENSAPSSPSGSVIIKDSPPESPRSSDNGSECESRDFDAIQGRPEMSASAGLFSQVMKETLSKREVNADDVSSIVSEKVKSPQASATKPDNNLNSLFSSISHSSSKHPEAAVEIASEFSLDSSMTDGSADHFISEKKILSSGNPFSSPQVDPLPTTLKPISTRSTTKSYRGLASSSSPDSPGKDEQFSSVQWRGKGVTPATPPRTAFKLPYQPSLRSPLRSPLRSPLHTPRSYFAETGSLKWLGRVDSGLSPKPDFSLPPNLVTHSETSSPACSPPPQLDLDSPTKSTVSSEVSEDLGSARTTVVHHYIEGEKEERYLLPDSTNVSSSTSFVNAGHVSPLRRYIQDDYDDGHVAPNERERVVPNATSNSDPSYASSSSVEDVLSTEAIDVKESNVLTRKAEIEQLALSSGTVVSNESIPITSWSAASSPDNENGDGFQHAGEVDMDDAAHSFQQSRASSSQRAEDGQELEISRNADSDVRSLYSKHGSLSLSEEFESRSQLEDVNATRLIAAAQRNQESLGVYDAVHGNENFSSSIEEAVRNQVFAPPDGVDGSSFRRQSDEQTLPSISTSEPENNNKSVNWDRTDATAEAQSMESLELQNSSNTHDALSASIAQQDRNMPKVLTFQESTLRPPPPDERTLFRDQMRTSSFNLRRADSMEKKEAVHRPVANINVAAILEKANAIRQAFAGSDDDDDGDDDWSDS
The following text describes a protein:
Function:
Antitoxin component of a type II toxin-antitoxin (TA) system. Antitoxin that counteracts the effect of the YoeB toxin. YefM binds to the promoter region of the yefM-yeoB operon to repress transcription, YeoB acts as a corepressor.
Miscellaneous:
MISCELLANEOUS: Has been described as natively unfolded and proteolytically unstable in vivo , but also as structured following overexpression in vitro. Has a half-life of approximately 1 hour in vivo.
Sequence:
MRTISYSEARQNLSATMMKAVEDHAPILITRQNGEACVLMSLEEYNSLEETAYLLRSPANARRLMDSIDSLKSGKGTEKDIIE
The following text describes a protein:
Function:
Intracellular mono-ADP-ribosyltransferase that may play a role in different processes through the mono-ADP-ribosylation of proteins involved in those processes. Required for amino acid starvation-induced mono-ADP-ribosylation and subsequent formation of Sec bodies - which are stress assemblies that promote cell survival by preserving components of the ER exit sites (ERES) during amino-acid starvation. Catalyzes the mono-ADP-ribosylation of Sec16 which is essential for Sec body formation.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Note=Membrane localization is required for mono-ADP-ribosylation and Sec body formation.
Domain:
The lumenal and transmembrane domains are necessary for mono-ADP-ribosylation and Sec body formation.
Sequence:
MTLLSGANSVGYPSQMPAKRISWRRLVALLPNSIGLSLKPVTPHLRDLHLVQRRLQDDFLGCEALWTIFMAAAWSYRYRTRLRPFPSHWNTIDLVFNTLGDAPRLEVLQQQLMHCDYQACSPNVVRLLTDILVDQADRVSLSSLRPCEFQELYAHLGMSPPKQPPTQIFEVRTGKGNEKGEAYASLRQENKESVRLGFYGCKLEKVYALLNSQNSLDNGKYLELTCDINEALARSKPQAGVGGSRCGSILRCVAVVEFVFQDNETSRDKKQVIIKDANTMQVSYLLLYGQSCNEYAMERQIKLMAEPARELLNWLERYHKKAISLGVGLLIVSSMAHFGSTFFRLLARTGFYVFKRGIL
The following text describes a protein:
Function:
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins. Within the pathway, FUM15 may be responsible for the hydroxylations at positions C-14 and/or C-15. Also plays a role in self-protection from FB1 toxicity, probably through derivatization of FB1, and may contribute to ceramide biosynthesis. The biosynthesis starts with the FUM1-catalyzed carbon chain assembly from one molecule of acetyl-CoA, eight molecules of malonyl-CoA, and two molecules of methionine (in S-adenosyl form). The C18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain. This step is catalyzed by the pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8. The resultant 3-keto intermediate is then stereospecifically reduced to a 3-hydroxyl product by reductase FUM13. Subsequent oxidations at C-10 by the cytochrome P450 monooxygenase FUM2, C-14 and C-15 by FUM6, FUM12 or FUM15, tricarballylic esterification of the hydroxyl groups on C-14 and C-15 by acyltransferase FUM14, and C-5 hydroxylation by 2-keto-glutarate-dependent dioxygenase FUM3 furnish the biosynthesis of fumonisins. The tricarballylic moieties are most likely derived from the citric acid cycle, and their addition to the carbon backbone may involve FUM7, FUM10, FUM11 and FUM14 (Probable).
Subcellular Localization:
Endoplasmic reticulum.
Sequence:
MRGLNNIAVALALSAIWSFGLDLGRHGTSGSSLLLALFRTLCKAYPFVVISHFVWSAIIWPTFFSPLRQLPNVPSDGWLSKETLRLVSEPRGVPQSDWINSLSNRPVDLARYRSFLGFERLLIISPKALAEVLTTKSYDFRKPGLIVSELKQATGMGVLLAEGSEHKSQRKALQTAFNYRHIKNLYPVFWDVAGEFATVLEKQIPTGTPRTSDTTAVIDIVDWASRATLDIIGRAGMGQGFDAIQNDDSRLHQAYRMIFEPSRGAIFLALLRLIFPERLVNWLPLRRNKRMRHGIQVIRSKCQELIRERKEKIKRQKAGVDNSGNDILTVALLNGVFTDEQLIDQLMTFLAAGHETTATALTWAIYILCKQPEVQNRLREEIRMHFPNPKGWPRSERPSSNTLQQAIDFKLPYLNVVCLEVMRYFAPIPLTMREATCDTTILHTFVPAGTRIILAPRVTNRDSALWGPDANNFNPDRWLSPKNGNREATEQSKFKIGNQKRDSTAAPEVTQEEVRGRTEARSNYADLTFLHGPRSCIGQSFARVEFAILLATLIANFEFQIEDESLLDERNISISRGATSRIVGGLKVRVRPIAVV
The following text describes a protein:
Function:
Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of sordarial, a salicylic aldehyde structurally related to the phytotoxin pyriculol. The most interesting aspect of this pathway is formation of an aromatic product from the highly reducing polyketide synthase srdA. SrdA synthesizes a reduced polyketide chain from one molecule of acetyl-CoA and five molecules of malonyl-CoA. The polyketide chain is then reductively released as an aldehyde. The oxidoreductases srdC, srdD and srdE then oxidize one of the hydroxy groups to facilitate the intramolecular aldol condensation, followed by dehydration to yield a salicylic aldehyde. This aldehyde can undergo facile reduction by endogenous reductases to yield the alcohol 1-hydroxy-2-hydroxymethyl-3-pent-1,3-dienylbenzene. The flavin-dependent srdI counteract against the propensity of the aldehydes to be reduced under physiological conditions and is responsible for reoxidizing 1-hydroxy-2-hydroxymethyl-3-pent-1,3-dienylbenzene back to the salicylic aldehyde. This salicylic aldehyde is then selectively epoxidized by the cupin-domain-containing oxidoreductase srdB to yield the epoxide, which can be hydrolyzed stereoselectively by the hydrolase srdG to give the final product sordarial.
Sequence:
MAVTDSTVVFISGVGKGIGAGIAKLYLSRPHHIVIGSVRDVSTPSVAELKASPTAPPGSKLLLVHIESTSSTDPAAAVEAIRAQGIDHIDIAIANAGAMPSTVPIEEVDTKDMLENYHINAIGPLLLFQALLPLLKKGTEPKWASVSTTAGSIGLVDPLAAWILPAYGGAKAALNWLTAGIASSQKEWMTTIALHPGLVQTGPGNWVAQKVGMGDKAPVTVGDSAASVVKLIDGLTKESNGKFYNAVDGTEVPW
The following text describes a protein:
Function:
Plays a role in the establishment of cell polarity and epithelial lumen formation. Also plays an essential role in ciliogenesis and subsequent Hedgehog signaling pathway that requires the presence of intact primary cilia for pathway activation. Mechanistically, interacts with and mediates RABEP2 centrosomal localization which is critical for ciliogenesis.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, cilium basal body. Cell junction. Note=Located at the distal ends of both centrioles and colocalizes to centrosomes throughout the cell cycle.
Sequence:
MAKSPGNSTLEDSLGQYQRSLRERANRSIHQLKCALREVDVTVEEDALDPSTSINVENEDTGVAWHELQHSHAVNQLKALLRQQTNKENETSPPRRRKLSPSRPSECDDGSMPTMHNLVPIINDQSQYIHHLEAEVKFCKDELSGMKNRVQVVVLENERLQQELKSQRPEETLREQTFLDASGNMQNSWIMTREDSRVDEAAKRPFSHGDAETGKTASTGDANKWKLELERLKLTYEAKTDLLESQLMLLRKDLAEYQKTCEDLKERLKHKESLLAASASSRVGGLCLKCAQHEAVLSQTHSNVHIQTIERLTKERDDLMSVLVSVRSSLAEAQKRETSAYEQVKHAVQMTEEANFEKTKALIQCEQLKSELERQTERLEKELASQQEKRAVEKEMIKKEVAREREDAESKMLILSQNIAKLEAQVEKVTREKTAAVSHLEEIQNHVASQEMDVTKVCGEMRFQLNKTKMEKDEVEKEHREYKAKSHKDLEMKVQEIEKLRLELSESEQHVEQEQQKAARARQECLRVTELLGEAERQLHLTRLEKDSIQQSFSNEAKAQALQAQQREQELTQKIQQMETQHDKTESEQYLLLTSQNTFLTKLKEECCLLAKKLEKVSLKSRSQIVRLSQEKRYLCDKLEKLQKRNDELEEQCIQHGRVHETMKERLRQLDKHGQATAQQLVQLLNKQNQLLLERQNLSEEVARLRAQLPSMPQSDC
The following text describes a protein:
Function:
Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Involved in anthocyanin biosynthesis (By similarity). Polyketide binding proteins (PBP) which promotes the catalytic activities of CHS_H1 and PT1L and triggers demethylxanthohumol (DMX) production.
Subcellular Localization:
Cytoplasm.
Sequence:
MENNMVMVHEIPFPPEIKTTKPLSLLGYGITDMEIHFLQVKFTAIGVYLDSDVVKHLQQWKGKKGNELAEDDDFFDALISAPVEKYLRIVVIKEIKGSQYGVQLESSVRDRLAAEDMYEEEEEAALEKIVEFLQSKYFKKDTLITFHFPATSPTAEIVVTLEGKEESKLKVENKNVVDMIKKWYLGGTSGVSPSTISSLADNLSAELSK
The following text describes a protein:
Function:
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP); Catalyzes the formation of 41 N(4)-acetylcytidine (ac(4)C) sites in RNA, almost always on the middle C of a CCG motif. Modifications are found mostly in tRNA, with small amounts found in rRNA and mRNA.
Subcellular Localization:
Cytoplasm.
Sequence:
MIPGSNPGGRIHNVIEMFENYFMDAVKGYYRHLAIIESQDPLEKINSLIDDYLKVNKKPRVIYGFHPWLDNSKDRMKELKKRFENFLDIDYSNSEKYLGQSADLVILDAMDDFRPNYIARFVDMTKGGGIAIIYSDNILEGKLYKKSLTRYGVVKDLFEARFIELAKRYRGIIFFQGNDRITFTPYSSNETHKPYKKIPKSPKVSMELHELCLSSDQNKVLEESLFIMNLGKRVLVITAARGRGKSASIGLFLSYLMSEGNFGSIIVTSPTYYSSQEIFKFIIRGLEALNVKYKVITSRDGKIMKISTRDSRVKWVSPDLAKNEEGDLIVIDEAAAMGIEFLDYIVRSWDKVILVTTIHGYEGSGKAFLKYVDKLKGKVLLKNIKMDYPIRYAKGDPIEKFLFDVFLLDAEPHEVEYNGKLKIVEVPQEELFRDDDLLKSVYGILVTAHYRNSPDDLMLLGDMAFQKVIVGYSSENPVAVCQVVYEGGLTDKQIWDISNGLKNEGHLIPHRLIKYMRALDFGKLKGWRIMRIAVSPENQGKGIGSRVIEEVIKMAKGVDWIGSSFVADYSVLRFWIKNGFLPVYLSSIKNEELNGYSVIVIKALSERTKEFVVKLSSLLKDKLLRTSHQVYYNLNPQLIVLLLRNTYSERIEGEVPDLYVDKIKAYTEGKVPYNVIAEAAHFLVTKHFLELKADLSIEAEASLVARVLQGKSWYHAGLMLGLSSREVEDNVKQSLGVLLETYT
The following text describes a protein:
Function:
Its major function may be to aid in digestion.
Sequence:
MRGLTLLSLAFLGVCSALTVPHSLVHPRDLEIRHGGIEGRITNGNLASEGQVPYIVGVSLNSNGNWWWCGGSIIGHTWVLTAAHCTAGADEASLYYGAVNYNEPAFRHTVSSENFIRYPHYVGLDHDLALIKTPHVDFYSLVNKIELPSLDDRYNSYENNWVQAAGWGAIYDGSNVVEDLRVVDLKVISVAECQAYYGTDTASENTICVETPDGKATCQGDSGGPLVTKEGDKLIGITSFVSAYGCQVGGPAGFTRVTKYLEWIKEETGIYY
The following text describes a protein:
Function:
Catalyzes the reduction of dihydromonapterin to tetrahydromonapterin. Also has lower activity with dihydrofolate.
Sequence:
MTAPIIITGVGKRIGYALAKHLLAQGHKVIGTYRSHYPSIDELQSLGATLIQCDFYDNAQVQNLIEQLSQYPKFRAIIHNASDWLADNSPEFAAHEVMQRMIQVHVNVPYQMNLALASKLQAGAEGEIGASDIIHITDYVAEKGSAKHIAYAASKAALDNLTLSFAAKLAPEVKVNAIAPAMILFNPSDDEAYRQKTLAKAILPKEAGNHEIIELMEYLLNSRYVTGRSHHVDGGRHLR
The following text describes a protein:
Function:
Mechanosensitive channel that opens in response to membrane tension and specific ionic conditions. Requires high concentrations of external K(+), NH(4)(+), Rb(+) or Cs(+) to gate. May participate in the regulation of osmotic pressure changes within the cell, although it does not appear to have a major role in osmolarity regulation. Forms an ion channel of 1.0 nanosiemens conductance. The channel can remain active for between 30 seconds and over 3 minutes; it does not desensitize upon extended pressure. Its activity is masked in wild-type cells by the MscS channel.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MTMFQYYKRSRHFVFSAFIAFVFVLLCQNTAFARASSNGDLPTKADLQAQLDSLNKQKDLSAQDKLVQQDLTDTLATLDKIDRIKEETVQLRQKVAEAPEKMRQATAALTALSDVDNDEETRKILSTLSLRQLETRVAQALDDLQNAQNDLASYNSQLVSLQTQPERVQNAMYNASQQLQQIRSRLDGTDVGETALRPSQKVLMQAQQALLNAEIDQQRKSLEGNTVLQDTLQKQRDYVTANSARLEHQLQLLQEAVNSKRLTLTEKTAQEAVSPDEAARIQANPLVKQELEINQQLSQRLITATENGNQLMQQNIKVKNWLERALQSERNIKEQIAVLKGSLLLSRILYQQQQTLPSADELENMTNRIADLRLEQFEVNQQRDALFQSDAFVNKLEEGHTNEVNSEVHDALLQVVDMRRELLDQLNKQLGNQLMMAINLQINQQQLMSVSKNLKSILTQQIFWVNSNRPMDWDWIKAFPQSLKDEFKSMKITVNWQKAWPAVFIAFLAGLPLLLIAGLIHWRLGWLKAYQQKLASAVGSLRNDSQLNTPKAILIDLIRALPVCLIILAVGLILLTMQLNISELLWSFSKKLAIFWLVFGLCWKVLEKNGVAVRHFGMPEQQTSHWRRQIVRISLALLPIHFWSVVAELSPLHLMDDVLGQAMIFFNLLLIAFLVWPMCRESWRDKESHTMRLVTITVLSIIPIALMVLTATGYFYTTLRLAGRWIETVYLVIIWNLLYQTVLRGLSVAARRIAWRRALARRQNLVKEGAEGAEPPEEPTIALEQVNQQTLRITMLLMFALFGVMFWAIWSDLITVFSYLDSITLWHYNGTEAGAAVVKNVTMGSLLFAIIASMVAWALIRNLPGLLEVLVLSRLNMRQGASYAITTILNYIIIAVGAMTVFGSLGVSWDKLQWLAAALSVGLGFGLQEIFGNFVSGLIILFERPVRIGDTVTIGSFSGTVSKIRIRATTITDFDRKEVIIPNKAFVTERLINWSLTDTTTRLVIRLGVAYGSDLEKVRKVLLKAATEHPRVMHEPMPEVFFTAFGASTLDHELRLYVRELRDRSRTVDELNRTIDQLCRENDINIAFNQLEVHLHNEKGDEVTEVKRDYKGDDPTPAVG