lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid. DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline. EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine. Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A. Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus. The role of the cytochrome P450 monooxygenase easK within the cluster has not been identified yet.
Sequence:
MLLLTFTLPVVTLLLAHIIRSWFRLRHIPGPFWAKITDLWREHHYIKGDYGDRPMAPYFAIPSLLGMESAMDQIQQELEDQICRRVTIDVVLWMRLFSLESLHWIAFSNKLGYLSEGKDTDGILSILQSKFIGLAGQLCGWIHRTTLRFHFPKSCTGTAVAPSQRKASHRDLLAHFMDASQKNPETLEERGVLGATISTIFAGTDTTGTSLTFFMYYLIKHPAALARLQEELDSAVRSGNLSYPPKWVEVSTLKYLQAVFKETLRLHSTARMSLYRVVGPEGLDLCGERLPSGTNLGCFGYTAHRNEPIYGRDAALFRPERWIEASNDTLLSMERASL
The following text describes a protein:
Function:
Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MIKEETVSYFQTFDGVMAESDKEEELDATKAKVEKVREENEKLKLLLSTILNNYNSLQMQVSKVLGQQQGASSMELDHIDRQDENNDYDVDISLRLGRSEQKISKKEENKVDKISTKNVEESKDKRSALGFGFQIQSYEASKLDDLCRQVKLANAENKCVSSRKDVKSVRNENHQDVLEEHEQTGLKKTRVCVKASCEDPSINDGCQWRKYGQKTAKTNPLPRAYYRCSMSSNCPVRKQVQRCGEEETSAFMTTYEGNHDHPLPMEASHMAAGTSAAASLLQSGSSSSSSSTSASLSYFFPFHHFSISTTNSHPTVTLDLTRPNYPNQLPDDYPLSSSSFSLNFSSPDPPPPSSHDHTLNFSGLRTQAPLSTDSLLARYRTRLSGQQ
The following text describes a protein:
Function:
Transporter for ammonium (both charged and uncharged NH3 and NH4) to use as a nitrogen source. The affinity of MEP2 is about twenty times higher than that of MEP1. MEP3 has the lowest affinity.
Miscellaneous:
MISCELLANEOUS: Present with 3820 molecules/cell in log phase SD medium.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MARGDGHLWTETYDSSTVAFMILGAALVFFMVPGLGFLYSGLARRKSALALIWVVIMATLVGILQWYFWGYSLAFSKTATNNKFIGNLDSFGFRNVYGKISDDSTYPELIYAIFQMMFMCVALSIIAGATAERGKLFPHMVFLFVFATLVYCPITYWIWAPGGWAYQWGVLDWAGGGNIEILSAVAGFVYSYFLGRRKENLLINFRPHNVSMVTLGTSILWFGWLLFNAASSLSPNMRSVYAFMNTCLSATTGGMTWCLLDYRSEKKWSTVGLCSGIICGLVAATPSSGCITLYGSLIQGIIAGVVCNFATKIKYYLKVDDSLDLLAEHGIAGVVGLIFNALFAADWVIGMDGTTKHKGGWLTHNWKQMYIQIAYIGASAGYCAVVTAIICFVLGKIPGVHLRVTEEAEALGLDEDQIGEFAYDYVEVRRDYYQWGVDTDALHTTCNGANSASETNPTEDSQNSSLSSATVSGQNEKSNNPKLHHAKEA
The following text describes a protein:
Function:
Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (Probable). Involved in the regulation of grain size. Acts as positive regulator of grain width and size by influencing cell proliferation. Functions partially antagonistically with GW2 in the regulation of grain width. Possesses deubiquitinating enzyme activity in vitro.
Miscellaneous:
MISCELLANEOUS: The dominant gain-of-function large grain1-D (lg1-D) develops significantly enlarged grains.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MLQPRESDVPVLFVVFIVLPVIAYFLLGRWHDAVSKKARVSVLAQRAAEETFKVETMATPDVILPGPSLRPMPYMRSAPSARPEYHECATCHGPAKTRCSRCKSVRYCSGKCQIIHWRQGHKQTCQQWNGFGTSSSGGLPPTENTEQMPFLSNLNSPLRGSDVHLHDMDFDTMSEPSFVTTDSYNLDTSPFLSDRSNMNKPNQFLHTSENGAAIGSYEKNDYSIDGEVPSSEILSGNKGLNNSSGSGENCGNRDVIYPLNSVVHQPNNYAPEIRKRPKASITVYESDKGVYLTSDMISSGEGPYASAAESLQRSNSSGNVTGKGNMIHKKPPYPSGKVSSSQKSQEKVLTSHQYDGHEKNPHNKNEQRSTKTAVSTNSSLQGCNGISKAGASKVEALKKPSKFLKTSLVGLINDNKRSKVLFPYEDLVKFFQYEVRGISPRGLFNCGNSCYANAVLQCLMCTKPLMIYLLLRLHSKDCCSKNWCLMCELEQYASTLRESGGPVSPSRILSNLRNIGCRLGGGSQEDAHEFLRHLVMSMQGACLDGLGGEKQVEASLQETTLIQQMFGGRLKSKVKCLRCYHESERYENIMDLTLEIHGWVESLQDALTQFTAPEDLDGENMYKCGRCSAYVKARKQLSVHEVPNILTVVLKRFQTGKYGKINKCVTFPDMLDMVPFVTGAGDNPPLYFLYAVVVHVDTENASFSGHYISYVKDMQGTWLRIDDSEVQAVSLNQVMSEGAYMLFYMRSFPRPPKIYIEKGLSSVPTCSKRHSSKSSKGSKQDLNHTESLFASSDQTYGIYDFRPDNGYIQDQHAALRTRNFYHTDDAFADSISTDFSDATSSEWSLFTSSDESSFTTESTRDSFSVVDYGDNAGLDPISSIFGPYYAQDHPPGSFASCTRLSPSNPQTRYFQENTGFVSDSSMPAHLPGNVHRGRYPDRACSSSAEPPASANPRSVYGRYGLSREGFVQTSGFCQM
The following text describes a protein:
Function:
Regulatory subunit of serine/threonine-protein phosphatase 4. May play a role in regulation of cell division in renal glomeruli. The PPP4C-PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3. Plays a role in the inhibition of TNF-induced NF-kappa-B activation by regulating the dephosphorylation of TRAF2.
Sequence:
MADLSLLQDSQEDTGGLLDFVSQDEMLTPLSRLDKYISSENVFNRQMVARSLLDTLRAVSEDEHECVSVLERIDRLADDSEPTVRAELMEQIPHIAIFCQENRPSIPSAFSRYLLPIVVRYLADQNNLVRKTSQAALLVLLEQELMERADVETLVCPVLVDLTAPDSNDDVKTEAMAIICKMAPMVGKDITERLFLPRFCEMCCDCRMFHVRKVCAANFGDICSVVGGDATEELLLPRFFQLCSDNVWGVRKACAECFMSVSSASSPEVRRSKLSAVFISLISDPSRWVRQAAFQSLGQFISTFASSSSAAGQFFRDEADWNSSTLSTHTHTPPSSETPLLCVSHNALGCEEPDVAEEGGGEQPAEEEPEVRDSTEEQEALEQDMSQQQQEVSDPEEEQEQDRTTGSSQQQEVSGPVEEQDRTPSSPAEQQEVRGPAEQEDESPSGPQQQIPEQELFNSFHYWRTPIPQIDLELELQGPQKRPSAPPLARRQLEELIENLEPHIDDPDVKAQVDVLTAALRASALDSALEDSAFLEPRAAQCEPFSTQLLSADTQRCDDGDSELSDCSAEEERRSSRQQDVVPQALLDQYLSMTDPSRAQTVDMEIAKHCAYSLPGVALTLGRHNWHCLRDTYETLASDMQWKVRRTLAFSLHELAGILGDQLTAAHLLPVFNSFLKDLDEVRIGVLKHLYDFLKLLHPDTRRKYLYQLQEFLVTDNSRNWRFRSELAEQLVLLLELYSAQDVHDYLRPLAFCLCTDRVSSVRWTSYRLVSEIIRKLSSCSSLLVCFLSELVEKFCHSQKWSSRQAFAFVCQLSIEEECLTLDQFSEHLLPPLLRLASDPVPNVRVLLAKTLRQTLLEREYLVSSSPGQQEALEHTLLSLQTDVDKDVKYFASVHPANTRLNEDAMSTTSSTY
The following text describes a protein:
Function:
The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MFARCSSSLVRPSAQGFRRFQSTLVLAEHNNETLNPITANAVTAAKKLGGDVTVLVAGTKVGPVSEAAAKLDGVKKVLVAEGDAYKGLLAESLTPLILATQEQLKFTHIVAGATAFGKAVLPRIAAKLDVSPVSDIIGVQSADTFVRTIYAGNAIQTVKSKDPVKVITVRGTNFEPTGAAGSAAAIEKAPEGDFASKTTEFVSQELTKSDRPSLTAAKIIVSGGRGMKSGDNFKMLYDLADKWGAAVGASRAAVDAGYVPNDLQIGQTGKIVAPEVYVAIGISGAIQHLAGMKDSKTIVAINKDPEAPIFQVADYGLVADLFKVVPEINEKC
The following text describes a protein:
Function:
Component of the chromatin assembly factor complex (CAF-1) involved in chromatin assembly following DNA replication and DNA repair. Required for several aspects of development, including seedling growth and leaf hair differentiation. Plays a critical role in the organization of shoot apical meristem (SAM) and root apical meristem (RAM) during postembryonic development by facilitating stable maintenance of gene expression states. Seems not required to maintain transcriptional repression of heterochromatic genes. Involved in heterologous recombination.
Subcellular Localization:
Nucleus.
Sequence:
MKGGTIQISWHDGKPVLTVDFHPISGLLATAGADYDIKLWLINSGQAEKKVPSVSYQSSLTYHGCAVNTIRFSPSGELLASGADGGELFIWKLHPSETNQSWKVHKSLSFHRKDVLDLQWSPDDAYLISGSVDNSCIIWDVNKGSVHQILDAHCHYVQGVAWDPLAKYVASLSSDRTCRIYANKPQTKSKGVEKMNYVCQHVIMKADQQRGDETKTIKTHLFHDETLPSFFRRLSWSPDGSFLLIPAGSFKVSPTSEAVNATYVFSRKDLSRPALQLPGASKPVVVVRFCPVAFKLRGSSSEEGFFKLPYRLVFAIATLNSVYIYDTECVAPIAVLAGLHYAAITDITWSPNASYLALSSQDGYCTLVEFEDKELGEAVSISVGKKPVDGEEKKHDLEKGDELMTETTPDESKKQAELEQNEESKQPLPSKITTDGKEKEHIMQKTDDEVMTETRHEEENQPLQSKVNTPVSNKPARKRITPMAIDP
The following text describes a protein:
Function:
The spt4-spt5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MSRNLMDQDFGSEEEDDDFNPAPAEESDNEEAHHDKTRKPDRDSDARNGSDDEGADEAGEEDEEENEEGGEGEGDEEEDEEEDEDDDDVSKPRKRRKGHGGLSAFIDYEAGVDEEEDEVEDEEEEEGYGLEQHPDDVLPAGAETDDRQHRRLDRERELAATLDAEKQAQLLKERYGRNRAAATDAVIVPKRLLLPSVDDPSIWGVRCKAGKEREVVFSIQKRIEDRPPGSRNPIKIISAFERGGAMSGYIYVEARRQADVMDALQDMSNVYPRTKMILVPVKEMPDLLRVQKSEELNPGGWVRIKRGKYMNDLAQIEEVETNGLAVTVRLVPRLDYGMNEDSGAPIMDPKRKRPGANPAVARPPQRLFSEAEAKKKHSKYLTATAGLGAKSWNYLGETYIDGFLIKDMKVQHLITKNVNPRLEEVTMFARDSENGTSNLDLASLAETLKNSTAEESYLPGDPVEVFKGEQQGLVGRTSSTRGDIVTILVTEGELAGQTIEAPVKTLRKRFREGDHVKVIGGSRYQDELGMVVQVRDDTVTLLSDMSMQEITVFSKDLRLSAETGVDGKLGMFDVHDLVQLDAATVACIVKVDRESLRVLDQNGSIRTILPSQVTNKITPRRDAVATDRNGAEIRHGDTVREVYGEQRSGVILHIHRSFLFIHNKAQAENAGIVVVRTTNVVTVSAKGGRPTGPDLSKMNPALMRNGAPGGMMAPPPSKTFGRDRLLGKTVLVKKGPFKGLLGIVKDTTDVQARVELHSKNKLVTIPKELLVVKDPVTGQTIDIGRGRGGPRVPQNSAAPSSGWQGGRTPMAAADSSRTPAWGAAMSSRTPAWSGAGLGSRTPAWKADGSRTAYGGAGSRTPAWNAGARTPYGGGFGSGSGNSDFDAFAAGSRTPAWGAASGSRTPAWSASANTTSRNDNKAYDAPTPGATYSAPTPGAYGGAPTPGLSAPTPGAWADSAPTPGAYNAPTPADFGEGSRPYDAPTPAMGGAAATPGAGAYGDTDDGAPRYEEGTPSP
The following text describes a protein:
Function:
Required for the differentiation of photoreceptor cells. Plays a role in the organization of outer segment of rod and cone photoreceptors.
Subcellular Localization:
Cell projection, cilium, photoreceptor outer segment. Cytoplasm, cytoskeleton, cilium axoneme.
Sequence:
MNSTPRDAQAPSHRECFLPSVARTPSVTKVTPAKKITFLKRGDPRFAGVRLAVHQRAFKTFSALMDELSQRMPLSFGVRSVTTPRGLHSLSALEQLEDGGCYLCSDKKPPKTPSGPGWPQERNPTAQQLRDIEGQREAPGTSSSRKSLKTPRRILLIKNMDPRLQQTVVLSHRNTRNLAAFLSKASDLLRFPVKQLYTTSGKKVDSLQALLHSPSVLVCAGHEAFRTPAMKNARKSEAESLSGLTSRNKNGSWGPKTKPSVIHSRSPPGSRPRLPERPGPSNPSVGPAPERHPQDTPAQSGPLVAGDDMKKKVRMNEDGSLSVEMKVRFHLVGEDTLLWSRRMGRASALTAASGEDPILGEVDPVCCVWEGYPWGFSEPGVWGPRPCRVGCREAFGRGGQPGPKYEIWTNPLHASQGERVAARKRWGLAQHIRCSGLWGHGTAGRERCSQDSASPASSTGLPEGSEPESSCCPRTPEDGVDSASPSAQIGAERKAGRSLGEDPGLCTDGAGLGGPEQGGHLTPRARSEEGASSDSSASTGSHEGSSEWGGRPQGCPGKARAETSQQEASEGGDPGSPALSLSSLRSDDPQAETQGQGTEQATGAAVTREPLVLGLSGFWDSEGASSTPSTCTSSQQGRRRHRSRASAMSSPSSPGLGRVAPRGHPRHSHYCKDTHSPLDSSVTKQVPRPPERRRACQDGSVPRYSGSSSSTRTQVSGNLRPPSSGSLPSQDLLGTSSATVTPAGHSDFASGVSPHNAPSAGWAGDAGSRTCSPAPIPPHTSNSCSKSGAASLGEEARDTPPPSSPLVLQVGRPEQGAVGPHQSRCCSQPGMQPAQEAQREPSPEASWLCGRYCPTPPRGRPCPQRRSSSCGSTGSSHQSTARGPGGSPQEGTRQPGPTPPPGPNSGASRRSSASQGAGSGGLSQENTLRSGGGPQGQEEASGVSPSSLPRSSPEAVVREWLDNIPEEPILMTYEMADETTAAAGGGLRGPEVDPGDDHSLEGLGEPAEAGQQSLEGDPGQDPEPEGALLGSSDTGPQSGEGVPQGAAPEGVSEVPAEAGADREAPAGCTVSLRALPGRVSASTQIMRALMGSKQGRPSSVPEVSRPMARRLSCSAGALITCLASLQLFDEDLGSPASKVRFKDSPRYQELLSISKDLWPGCDIGEDQLDSGLWELTWSQALPDLGSHAMTENFTPTSSSGVDISSGSGGSGESSVPCAMDGTLVPQGTELPLKTSNQRPDSRTSESPGDLENQQQCCFPTFLNARACACATNEDEAERDSEEQRASSNLEQLAENTVQEEEVQLEETKGTEGEGLQEEGVQLEETKTEEGLQEEGGVQLEGTKETEGMQEEGGVQLEGTKEMEEGLQEEGVQLEEVKEGPEGGLQGEALEEGLKEEGLPEEGSIHGQELSEASSPGGKGSQEDDPVQEEEAGRASASAEPCPPEGTEEPTEPPSQLSETDPSASESQSGSQLEPGLEKLPGATMMGQEHTQAQPTQGAAERSSSVACRAALDCDPIWVSVLLKKTEKAFLAHLASAVAELRVRWGLQDNDLLDQMAAELQQDVAQCLQDSTKRELQKLQGRAGWMVLEPPREALTGELLLQTQQRRHRLRGLRNLSAFSERTLGLGPLSFTLEDEPALSTALGSQLGEEAEGEEFCPCEACVRKKVSPMSPKATMGATRGPIKEAFDLQQILQRKRGEHPDGEAAEVAPGKTHTDPTSTRTVQGAEGGLGLGLSQGPGVDEGEDGKGSQRLNRDKDPKLREAEGDAMAQKREGKTHNSETSVGSELGEAEQEGEGISERGETGGQGSGHEDNLQGEAVAGGDQDPGQSDGAEGIEAPEAEGEAQPDVEALETEGEAQPESEDVEAPEAEGEAQPESEGVEAPEAEGEAQPESEGVEAPEAEGEAQPESEGVEAPEAEGEAQPESEGVEAPEAEGEAQPESEGIEAPEAEGEAQPESEGVEAPEAEGEAQPESEGIEAPEVEGEAQPESEGVEAPEAEGEAQPESEGIEAPEAEGEAQPESEGVEAPEAEGEAQVSLGDGQSEEASESSSPVPEDRPTPPPSPGGDTPHQRPGSQTGPPSSRASSRGNCWQKDSENDHVRGDKRSPDAKSTGAPHAERKATRMYPESSTSEQEEDPLGSRTPGQGASEGYDLREDQALGSLAPTEAVGRADGFGQDDLDF
The following text describes a protein:
Function:
Necessary for the splicing of pre-mRNA. Has a role in the recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract and the 3'-splice site at the 3'-end of introns (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MTRLVWFCMQVAYCLHGWDWDIMDRGRSSNSYDSLWGGKARDNPIVSQLPLQYRIRSALTQEQQTAYQVMYRIQEITIKLRTNDLNPPTSRYRSLSPPPVYDSQGKRTNTREHRYRKKLEEERHRLVEIALKMIPHFIAPDDYRRPSKFQDKYYIPINDYPEINFVGLLLGPRGNTLKQLQQQSGCKIVIRGRGSVKEGKAATDLPKGAMNMNEPLHCVISADTEEKIPLGINAVESIIIKAITSPEGQNDLKRGQLRELAVLNGTLREDNRPCPLCGEQGHKKWECSSNPSLSMTVICQRCNQPGHAARDCTSPLNEFGKRTSDGPEFRETKKLQQDAPPPSGPVGSHPSAPGSGSANSGVAPASLHPPGTMAPPGALPPPGSLAAPGTLPPPAALPAPAAPGTLPPPVALPAPATLPQAGVPPAPDASPAVKTAVPIEGPPAPPQTAPPLRQTAATASSAGSSQSAQEEPENARNGVEKAAPGPPAAVLPPPPPPPPPPPPPPSS
The following text describes a protein:
Function:
Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
Subcellular Localization:
Nucleus. Chromosome, centromere, kinetochore. Note=Associated with kinetochores.
Sequence:
MSRQSFYADPSSAGRQMKYRKDLFPLLDTREITACLLECEFNVTQELIVKPTADFVTNLFEQFLDTFMGIPLGTIRKKARKMSRINPLESDQANGKPQQSPEEDFNDNQENDKTKDTFSALQLLILHRYLAIFFSTCGINDFVLTDIARPDGYRIRRILSAVINFIRFREDQSPKFDHLANECEATADKVSEVQAENSATMQKINAIKEKLEMDSENDESNRKNLQYINSYNRKLETKLRELKVMQERLTKEHDDYKQEKALLAKKLYDINFLYNETQEQVANLTKYAETDLSILVKITEDLSNDLSSMQTNYKNLEKSYQNMGITIDSIQVNEINLKDLLKLAEDITRNVEKRQIEGKILKDNQDNLDELTRKQMELEGQILIVQNQLNKSNKKYQDLIVQADKKESAVKLKLEETKQEFNDILSEKEKHNEEHKRIMDQIVKIQQETTAIQDAFVKESKEVELKLINLMSIIKRYMSDLRNNI
The following text describes a protein:
Function:
Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Selectively binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other phosphoinositides tested. Involved in late stages of cytokinesis. Plays a role in endosomal sorting/trafficking of EGF receptor (By similarity).
Subcellular Localization:
Cytoplasm, cytosol. Membrane; Lipid-anchor. Endosome. Late endosome membrane. Note=Localizes to the midbody of dividing cells.
Domain:
The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components.
Sequence:
MGLFGKTQEKPPKELVNEWSLKIRKEMRVVDRQIRDIQREEEKVKRSVKDAAKKGQKEVCVVLAKEMIRSRKAVSKLYASKAHMNSVLMGMKNQLAVLRVAGSLQKSTEVMKAMQSLVKIPEIQATMRELSKEMMKAGIIEEMLEDTFESMDDQEEMEEAAEMEIDRILFEITAGALGKAPSKVTDALPEPEPAGAMAASEEGEEEEDEEDLEAMQSRLATLRS
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:
MPLVRFEVRNEYRLGQPELYKEANREDPKAVLDGVAVAGLVGILRQLGDLAEFAAEVFHGLQEQVTTTASRSHKLKVRVQKIEAKLPSLEKAVLAQTSHIHLAYTAGSEWHSRIHNGQNHFISNDLPRFIMDSYEECRDPPRLHLLDKFDTGGPGSCLKRYSDPTFFRRASGNFNEPDVEKFPKEKKTRKTKKKRPSRRNADFLRSASMPNQSARMQYATTIVNGRTSSPTGTSSTNDMTLKSDLGDHSNSFDSRTGSAYVECVFHLSSSRQPEEHEPKEYSSRFMHHNDNIDSVFPDGQHSIETKNFPQSSSPEPTVPASSCDTWDEKAEIVETKGLNCDGSESPEMSTTDYDLGIHHEEIANYRDPDESGMVFDNEDAQKSSTDKNEIDEVESEPDNYEDALNTIESESENDLDCQTKRELEQLSSKVNDEGIEDEASKMAQHISVDFPAKSESYIASDISLKGMVSELPISVPSNTIVHEHASYISEEPSGSDISPKEGMVSEEPSGSDISPKEGMVSEEPSGSDISPKEGMVSEEPSGSDISPKEGIVSELPMPIPSDTVAHEHTSNTSKEPSVLDNIGSSTCADALDGSEVGSLVSDPSSSSDGISNLVEPLSEITASSACKPQESPKTQELAKSHESPESQKMAVSQESHKSQESQAELSSVLSVSFWTNGGLLGLEPSKPPDFAVSNASMQDSLARCKGEVKSSPNLGSMPSDNGERVRPGRLIKDDHFNSRCEDQDAESEKSGDFHHSNRFGSVHMGGLNGTSIAKPEKELCPDADVKSASRETSQENDENSGQMFGLGPRLLINGLRKTMSLIPDSKPEMASSQRSNALEQRNGHDSIAYHANPGKASNDKFGHKSIVDSLTSSPPLEHMKMSFHPIDGFEVSKLKLKVPDGNHSTGSFRDMFPSFQLVPEHCIPMQHAGSESDDDTFCRSSPYMSDDCLSHHSDSCSEQWEPGESPQNQDPGLYDALCRISSVESVSSSLQAGEMGKNGLHMDSGLKSEYTENGADPSLHSLLDLPSFDAVSPVLQEKENENLDPRNLIELHNPKECNPVPPPPPPVQWWVTKPASYVAEEKQNIVSDTVSEQHIVDLKLSGSIISQQHKPAPAKKHQTVEEALKFKPNNKDHWKLNAQGEVSVPPNGKGMDEKEDFLHQIKTKSFTLRRTVTAKPTFASGPAANDKVSAILEKANAIRQAVGSDDGEDDDTWSDT
The following text describes a protein:
Function:
Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2).
Sequence:
MSYNFEEERVIKEIREKNAKRVLLQFPEGLKYFSIDIVKKLREKLPNVNFIISGEPSWGACDIAEDEAQQVNADLIIHFGHTPYTWYYPKFPTIFINAESNLDISENALHSLENDISKYNGRKISLTATLQHVRLLSKIKSFLEDKGYDIVIGKPSNRFMFDGQVLGCDYKAAEVEADIYVIVSGGLFHALGLGLATNKPTIKLDPYLQKSEDITNDVRKILKVRYGKILQALDKRSWVIIQGVKVGQNRPNMIKYFYDKLTEKGYDVFTVTNKVLTLDILRNLDRNYIDVFLVTSCPRLPIDDLYNYEKPVLTPGEAKMIINNSLEPYIFPW
The following text describes a protein:
Function:
Reversible hydration of carbon dioxide.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MAATPTHFSVSHDPFSSTSLLNLQTQAIFGPNHSLKTTQLRIPASFRRKATNLQVMASGKTPGLTQEANGVAIDRQNNTDVFDDMKQRFLAFKKLKYMDDFEHYKNLADAQAPKFLVIACADSRVCPSAVLGFQPGDAFTVRNIANLVPPYESGPTETKAALEFSVNTLNVENILVIGHSRCGGIQALMKMEDEGDSRSFIHNWVVVGKKAKESTKAVASNLHFDHQCQHCEKASINHSLERLLGYPWIEEKVRQGSLSLHGGYYNFVDCTFEKWTVDYAASRGKKKEGSGIAVKDRSVWS
The following text describes a protein:
Function:
Main aspartate aminotransferase that couples nitrogen assimilation to aspartate synthesis. Has a weak, but significant, side activity toward kynurenine (Kyn). Oxaloacetate and 2-oxoglutarate, but not pyruvate, serve as amino acceptors, while Asp, Glu and Kyn serve as the best amino donors. Essential for axenic growth and survival of M.tuberculosis in macrophages and in mice.
Sequence:
MSFDSLSPQELAALHARHQQDYAALQGMKLALDLTRGKPSAEQLDLSNQLLSLPGDDYRDPEGTDTRNYGGQHGLPGLRAIFAELLGIAVPNLIAGNNSSLELMHDIVAFSMLYGGVDSPRPWIQEQDGIKFLCPVPGYDRHFAITETMGIEMIPIPMLQDGPDVDLIEELVAVDPAIKGMWTVPVFGNPSGVTYSWETVRRLVQMRTAAPDFRLFWDNAYAVHTLTLDFPRQVDVLGLAAKAGNPNRPYVFASTSKITFAGGGVSFFGGSLGNIAWYLQYAGKKSIGPDKVNQLRHLRFFGDADGVRLHMLRHQQILAPKFALVAEVLDQRLSESKIASWTEPKGGYFISLDVLPGTARRTVALAKDVGIAVTEAGASFPYRKDPDDKNIRIAPSFPSVPDLRNAVDGLATCALLAATETLLNQGLASSAPNVR
The following text describes a protein:
Function:
Role in growth on acetoin or butanediol. Involved in the breakdown of these compounds used as a carbon source.
Sequence:
MQQHSSKTAYVYSDKLLQYRFHDQHPFNQMRLKLTTELLLNANLLSPEQIVQPRIATDDELMLIHKYDYVEAIKHASHGIISEDEAKKYGLNDEENGQFKHMHRHSATIVGGALTLADLIMSGKVLNGCHLGGGLHHAQPGRASGFCIYNDIAITAQYLAKEYNQRVLIIDTDAHHGDGTQWSFYADNHVTTYSIHETGKFLFPGSGHYTERGEDIGYGHTVNVPLEPYTEDASFLECFKLTVEPVVKSFKPDIILSVNGVDIHYRDPLTHLNCTLHSLYEIPYFVKYLADSYTNGKVIMFGGGGYNIWRVVPRAWSHVFLSLIDQPIQSGYLPLEWINKWKHYSSELLPKRWEDRLNDYTYVPRTKEISEKNKKLALHIASWYESTRQ
The following text describes a protein:
Function:
Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.
Sequence:
MIYYAEVAFDLPIEEDTFTYEIPPNVQIGVRVLVKLRNREEEGIIVSIHQNEPNYKVFQIEKIIDKIPIVLQEQIDLAHWMKNQYIASLGECIYKMIPAGRRQVKLETFPSDAEGKPVTLNEEQQIATQNILSTFGTAAVHLLFGITGSGKTEVYIHLIQKVLETPNRSVILLVPEISLTFHIIRKLELIFPGQLAVLHSALKVSEKFKAYNELLTGKKRIAVGTRSAVFAPVSNLGLVIIDEDHDSSFKEHSSPRYHARQIALQRCRTNEAVLVMGTATPSLEIYHLAKEGKIHLHTLTKRPQGVLPPTVRIVENQKESNVLSSELSFAIKQRLEKKEQIILLLNRRGYSPLIYSPSTSSYVPCPNCTTNLCYHKKGTTICHLCGHTETLDSLQKRMGEALTLKGTGTQKLEENLLEAFPQTRVERLDQDSIQDRSLLNEVISRLLGGEIDILTGTQMIAKGLDASRVTLVGVLNAGIGLGLPDFRANERVFSLLTQVAGRAGRSKLKGEVLIETNAPNHPVIQMAMNQNYIQFYESEIPVRKELFYPPFSRLVRVVSRSKEEQISLETIELVFGVLKKFFPSKDTILLGPAPCPFYRIDSNFRNHIILKTSSLNIWREIFKKEIRPLKLSKKVYLEIDFDPLDLV
The following text describes a protein:
Function:
In the process of mRNA degradation, seems to play a role in mRNA decapping. Component of a complex containing DCP2 and DCP1A which functions in decapping of ARE-containing mRNAs. Promotes complex formation between DCP1A and DCP2. Enhances the catalytic activity of DCP2 (in vitro).
Subcellular Localization:
Cytoplasm, P-body. Nucleus.
Sequence:
MASCASIDIEDATQHLRDILKLDRPAGGPSAESPRPSSAYNGDLNGLLVPDPLCSGDSTSANKTGLRTMPPINLQEKQVICLSGDDSSTCIGILAKEVEIVASSDSSISSKARGSNKVKIQPVAKYDWEQKYYYGNLIAVSNSFLAYAIRAANNGSAMVRVISVSTSERTLLKGFTGSVADLAFAHLNSPQLACLDEAGNLFVWRLALVNGKIQEEILVHIRQPEGTPLNHFRRIIWCPFIPEESEDCCEESSPTVALLHEDRAEVWDLDMLRSSHSTWPVDVSQIKQGFIVVKGHSTCLSEGALSPDGTVLATASHDGYVKFWQIYIEGQDEPRCLHEWKPHDGRPLSCLLFCDNHKKQDPDVPFWRFLITGADQNRELKMWCTVSWTCLQTIRFSPDIFSSVSVPPSLKVCLDLSAEYLILSDVQRKVLYVMELLQNQEEGHACFSSISEFLLTHPVLSFGIQVVSRCRLRHTEVLPAEEENDSLGADGTHGAGAMESAAGVLIKLFCVHTKALQDVQIRFQPQLNPDVVAPLPTHTAHEDFTFGESRPELGSEGLGSAAHGSQPDLRRIVELPAPADFLSLSSETKPKLMTPDAFMTPSASLQQITASPSSSSSGSSSSSSSSSSSLTAVSAMSSTSAVDPSLTRPPEELTLSPKLQLDGSLTMSSSGSLQASPRGLLPGLLPAPADKLTPKGPGQVPTATSALSLELQEVEPLGLPQASPSRTRSPDVISSASTALSQDIPEIASEALSRGFGSSAPEGLEPDSMASAASALHLLSPRPRPGPELGPQLGLDGGPGDGDRHNTPSLLEAALTQEASTPDSQVWPTAPDITRETCSTLAESPRNGLQEKHKSLAFHRPPYHLLQQRDSQDASAEQSDHDDEVASLASASGGFGTKVPAPRLPAKDWKTKGSPRTSPKLKRKSKKDDGDAAMGSRLTEHQVAEPPEDWPALIWQQQRELAELRHSQEELLQRLCTQLEGLQSTVTGHVERALETRHEQEQRRLERALAEGQQRGGQLQEQLTQQLSQALSSAVAGRLERSIRDEIKKTVPPCVSRSLEPMAGQLSNSVATKLTAVEGSMKENISKLLKSKNLTDAIARAAADTLQGPMQAAYREAFQSVVLPAFEKSCQAMFQQINDSFRLGTQEYLQQLESHMKSRKAREQEAREPVLAQLRGLVSTLQSATEQMAATVAGSVRAEVQHQLHVAVGSLQESILAQVQRIVKGEVSVALKEQQAAVTSSIMQAMRSAAGTPVPSAHLDCQAQQAHILQLLQQGHLNQAFQQALTAADLNLVLYVCETVDPAQVFGQPPCPLSQPVLLSLIQQLASDLGTRTDLKLSYLEEAVMHLDHSDPITRDHMGSVMAQVRQKLFQFLQAEPHNSLGKAARRLSLMLHGLVTPSLP
The following text describes a protein:
Function:
May play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. Can cleave N-acetyl-L-Ala(4).
Sequence:
MTNPLLTSFSLPPFSAIKPEHVVPAVTKALADCRAAVEGVVAHGAPYSWENLCQPLAEADDVLGRIFSPISHLNSVKNSPELREAYEQTLPLLSEYSTWVGQHEGLYNAYRDLRDGDHYATLNTAQKKAVDNALRDFELSGIGLPKEKQQRYGEIATRLSELGNQYSNNVLDATMGWTKLITDEAELAGMPESALAAAKAQAEAKEQEGYLLTLDIPSYLPVMTYCDNQALREEMYRAYSTRASDQGPNAGKWDNSPVMEEILALRHELAQLLGFENYAHESLATKMAENPQQVLDFLTDLAKRARPQGEKELAQLRAFAKAEFGVEELQPWDIAYYSEKQKQHLYSISDEQLRPYFPENKAVNGLFEVVKRIYGITAKERTDVDVWHPEVRFFELYDENNELRGSFYLDLYAREHKRGGAWMDDCVGQMRKADGTLQKPVAYLTCNFNRPVNGKPALFTHDEVITLFHEFGHGLHHMLTRIETAGVSGISGVPWDAVELPSQFMENWCWEPEALAFISGHYETGEPLPKELLDKMLAAKNYQAALFILRQLEFGLFDFRLHAEFNPQQGAKILETLFEIKKQVAVVPSPTWGRFPHAFSHIFAGGYAAGYYSYLWADVLAADAYSRFEEEGIFNRETGQSFLDNILTRGGSEEPMELFKRFRGREPQLDAMLEHYGIKG
The following text describes a protein:
Function:
Able to cleave dimethylsulfoniopropionate (DMSP), releasing dimethyl sulfide (DMS). DMS is the principal form by which sulfur is transported from oceans to the atmosphere. The real activity of the protein is however subject to debate and it is unclear whether it constitutes a real dimethylsulfoniopropionate lyase in vivo: the low activity with DMSP as substrate suggests that DMSP is not its native substrate.
Sequence:
MNQHYSETRKIDPSRGATLGDNTPNDNNRIEIGPTQLAFGEWATAGLALPDLQRMREFRWNRLTQAVVDRDYGGVLMFDPLNIRYATDSTNMQLWNAHNPFRALLVCADGYMVIWDYKNSPFLSTFNPLVREQRFGADLFYFDRGDKVDVAADAFSNEVRTLIAEHGGGNMRLAVDKIMLHGLRALEAQGFEIMEGEELTEKTRAIKGPDEILAMRCAVHACETSVAAMEHFAREAVPQGNTSEDDVWAVLHAENIKRGGEWIETRLLASGPRTNPWFQECGPRIIQNNEIISFDTDLIGSYGICVDISRSWWVGDAAPPADMVYAMQHAHEHIMTNMEMLKPGVTIPELSERSHRLDEQFQAQKYGCLMHGVGLCDEWPLVAYPDQAVPGSYDYPLEPGMVLCVEAAVGAVGGNFTIKLEDQVLITETGYENLTSYPFDPALMGR