lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
ADP-ribosylates double-stranded DNA by targeting the N2 amino group of dG residues; 10-fold less active on tRNA. Induces apoptosis in a range of human cell lines. May play a role in removing unnecessary or harmful cells during pupation (Probable). May play a role in defense against parasitic wasps; its habitual predator Cotesia glomerata is only susceptible after removal of its eggshell or the surface of the larval caudal vesicle, while other wasps are damaged by this protein (Probable). The wild-type catalytic domain (residues 1-233) cannot be expressed in E.coli as it is unstable probably due to its toxicity. A catalytic domain fragment (Glu-165 mutated to Gln) binds dsDNA but not ssDNA; the presence of the linker inhibits DNA-binding.
Domain:
The N-terminus (residues 1-233) has the ADP-ribosylation catalytic domain. NAD(+)-binding or the presence of the linker do not alter the structure of the catalytic domain, however in vitro the presence of the linker masks the DNA- and NAD(+)-binding regions and thus prevents dsDNA-binding by the catalytic domain.
Sequence:
MADRQPYMTNGIQAAVVEWIRALDLEIISLLLSRAWPMALLATSELRWRPTVLTDTDNVVRLDRRQRLVRWDRRPPNEIFLDGFVPIVTRENPDWEETDLYGFAKNNHPSIFVSTTKTQRNKKKYVWTPRNANRGIVYQYEIYAPGGVDVNDSFSDASPWPNQMEVAFPGGIQNIYIRSARELHNGRIQRIWINPNFLDPGDLEPIVSSSRTPQVIWRMNHPDGGHRDQRSERSASSYDDLMYGGTGNVQEDTFGDEPNNPKPIAAGEFMIESIKDKNSFLDLSKNVNGGVIHSNLYSGGDNQIWVFSYDDNKKAYRIQSYQNSYLYLSWDSNASSKEMILRGYTNSGSNNQYWQIEQTGKNYRLRNLLNLDMIITAQDKPSAFGGKEVIVNTEISNSNTKISQEWKMIPFDFRPIIDGDYNIFNVDLSNQVVDFSNQPDLLVHGHIFCDNENQTWHFTYNSTYHAYKIWSGRKSNLLLTWDSNAASKEMVVRAYTESRSKNQYWRIEQTGSKSYKVRNLENSSMILGLTRVSTPYGGLNLMVEDDSDGHSDLHSDWDIKPIFYQDIPDGDYNIFNDNFPNIAIDFTNQEGSLIHGHNFCSNNNQKWSFVFDGKRKAYRIKSGVRSNLWLSWDSNASSKEMVLRAYTESGSSNQYWRLDEANDGSYRIRNLQDYYKLIALTNKNTPYGGKELIVSDNKESGNTWYLKKLGEVPLPNRKFRIATKLNYKKVIDSSTSYNLIITHDLNFASSIWELVYDSSKKAYNIYSSDINNLGWIYQNKNFFVKLGNIDGPDHGDLRYFWTIEYSMQTGCYLIRSLHDPANAVGYTDSESVITDTSTYSDNQLFHFILM
The following text describes a protein:
Function:
Golgi membrane protein involved in vesicular trafficking.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MATPNPDGALPGAGPPAPSHNIAVFFHGFFKVVAIVWYWICTIVSNSFVVNFVVCIVLLALDFWVTKNITGRLLVGLRWWNEANDTGSAWRFETLPEGVRQVLPREKRFFWLACMGATAHWILACIIAVFGLSSYIIVAIMGLLFSGSNLWGYFKCSREAQADLKGYINSTSNTLMQGAIKQQLNSAVSRV
The following text describes a protein:
Function:
Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex assembly is part of an intermediate PSMD9:PSMC6:PSMC3 module, also known as modulator trimer complex; PSMD9 is released during the further base assembly process.
Sequence:
MAAPISADDVKKLMARKDEIEEEIKTWQDVLESQKGVGMSGPLVDTEDFPRSDIDVYQVRTARHNIICLQNDHKAIMREIEEGLHNLHAQAREKGQGEKIEIRPENTDKLEPFARVDSVAAGGPASMAGLQVGDQVLQFGSVTPANFTGLQNIGQVVQHSEGKTVPVRVLRGEETMNLGLRPQRWSGRGLLGCNIVPVT
The following text describes a protein:
Function:
Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites.
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Sequence:
MREKYTKEEAVKNWEKKKNKPSSPKGVGEFLKKKKGRFYIIGKCITMLLCSHK
The following text describes a protein:
Function:
Inhibitory regulator of the Ras-cyclic AMP pathway. Stimulates the GTPase activity of Ras1.
Sequence:
MTKRHSGTLSSSVLPQTNRLSLLRNRESTSVLYTIDLDMESDVEDAFFHLDRELHDLKQQISSQSKQNFVLERDVRYLDSKIALLIQNRMAQEEQHEFAKRLNDNYNAVKGSFPDDRKLQLYGALFFLLQSEPAYIASLVRRVKLFNMDALLQIVMFNIYGNQYESREEHLLLSLFQMVLTTEFEATSDVLSLLRANTPVSRMLTTYTRRGPGQAYLRSILYQCINDVAIHPDLQLDIHPLSVYRYLVNTGQLSPSEDDNLLTNEEVSEFPAVKNAIQERSAQLLLLTKRFLDAVLNSIDEIPYGIRWVCKLIRNLTNRLFPSISDSTICSLIGGFFFLRFVNPAIISPQTSMLLDSCPSDNVRKTLATIAKIIQSVANGTSSTKTHLDVSFQPMLKEYEEKVHNLLRKLGNVGDFFEALELDQYIALSKKSLALEMTVNEIYLTHEIILENLDNLYDPDSHVHLILQELGEPCKSVPQEDNCLVTLPLYNRWDSSIPDLKQNLKVTREDILYVDAKTLFIQLLRLLPSGHPATRVPLDLPLIADSVSSLKSMSLMKKGIRAIELLDELSTLRLVDKENRYEPLTSEVEKEFIDLDALYERIRAERDALQDVHRAICDHNEYLQTQLQIYGSYLNNARSQIKPSHSDSKGFSRGVGVVGIKPKNIKSSNTVKLSSQQLKKESVLLNCTIPEFNVSNTYFTFSSPSTDNFVIAVYQRGHSKVLVEVCICLDDVLQRRYASNPVVDLGFLTFEANKLYHLFEQLFLRK
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular Localization:
Mitochondrion.
Sequence:
MSLYSNIRTFSTRSIVLNRIKPLKFEDLTKIKLREPVVPRVANFEVSPDHPLWQFFPQGNKTKVAIRESEELDLDSREWSSAELRQKSFEDLHKIWYLTLKERNILSREVRLGESLGMGDFRQFNNVDRKLIKTQKRIKQVLLERQVAVERAQATMQDDIQKYLDDFKTRYVNCEADEVEDYHEKLVRLQYAIFGINPNLSLELLQDEETIDVNFVKGLSYIANLKVERHLKLNPQTEFELPLNGPVEELPFFLNDVEVAISQVKQLRDSGKSRMLHKIEVIPFLKQAIESHMQQEENIGGYEEEQNKN
The following text describes a protein:
Function:
Involved in the biosynthesis of the siderophore enterobactin (macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine). Catalyzes the reversible conversion of chorismate to isochorismate.
Sequence:
MDTSLAEEVQQTMATLAPNRFFFMSPYRSFTTSGCFARFDEPAVNGDSPDSPFQQKLAALFADAKAQGIKNPVMVGAIPFDPRQPSSLYIPESWQSFSRQEKQASARRFTRSQSLNVVERQAIPEQTTFEQMVARAAALTATPQVDKVVLSRLIDITTDAAIDSGVLLERLIAQNPVSYNFHVPLADGGVLLGASPELLLRKDGERFSSIPLAGSARRQPDEVLDREAGNRLLASEKDRHEHELVTQAMKEVLRERSSELHVPSSPQLITTPTLWHLATPFEGKANSQENALTLACLLHPTPALSGFPHQAATQVIAELEPFDRELFGGIVGWCDSEGNGEWVVTIRCAKLRENQVRLFAGAGIVPASSPLGEWRETGVKLSTMLNVFGLH
The following text describes a protein:
Function:
Catalyzes the ATP-dependent translocation of sphingoid long-chain bases (LCBs) from the cytoplasmic site toward the extracytoplasmic side of the membrane (flip-flop). Involved in the establishment of the functional lipid asymmetry of the plasma membrane. Regulates intracellular levels of LCBs, sphingolipid precursors that are growth inhibitory at increased levels.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNTMDLAVITEWTPTSTATSTTLSTIAATYAPALQSKISGAVHTLTSKGSTIANMDYISASRIIRGAQASLSIISAEHVLETATATDVQAQATQIIWQATENLLDLAWEENVYDIPRLNRTANILFLVLFAITFAIACLMWIKSRYWWFNVAWTCGTALEFLGYLGRVLSFSDMKKFDYYLLQLIALTLSPVFLMAGIYFLFGQLVVIHGRQYSWLKPLHYSYIFITCDVVSLVIQAVGGGMTAIAAQEYDDVDPGTYTMIAGIAFQVFSMSVFLLCWLVFCWNIYFRDISVNESKPSPYQKKSFMTFIKLLLNGDDANMYKLKVLDKYYNSSYKDLRRRPLYNYYAIAITLAVIAVYIRCIYRVVELAQGFSGYLITHEVYIMTLDAAMIGICCIIFILFHPQVVMGSSNVVGLRSIAKNKDQETGDKSYEEKTNNDIVSDNEESTLQGQNIVRGDPIQENKE
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular Localization:
Cytoplasm.
Sequence:
MSEELPQIEIVQEGDNTTFAKPGDTVTIHYDGKLTNGKEFDSSRKRGKPFTCTVGVGQVIKGWDISLTNNYGKGGANLPKISKGTKAILTIPPNLAYGPRGIPPIIGPNETLVFEVELLGVNGQ
The following text describes a protein:
Function:
Escort protein required for cholesterol as well as lipid homeostasis. Regulates export of the SCAP-SREBP complex from the endoplasmic reticulum to the Golgi upon low cholesterol, thereby regulating the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2. At high sterol concentrations, formation of a ternary complex with INSIG (INSIG1 or INSIG2) leads to mask the ER export signal in SCAP, promoting retention of the complex in the endoplasmic reticulum. Low sterol concentrations trigger release of INSIG, a conformational change in the SSD domain of SCAP, unmasking of the ER export signal, promoting recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi: in the Golgi, SREBPs are then processed, releasing the transcription factor fragment of SREBPs from the membrane, its import into the nucleus and up-regulation of LDLR, INSIG1 and the mevalonate pathway. Binds cholesterol via its SSD domain.
Subcellular Localization:
Cytoplasmic vesicle, COPII-coated vesicle membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MPFVEPQIGHHPAVKDVDPAGLANGRGLNSSTKGLSIPDRVALLYYKHGLLCSSYPWCTIIVAIIIVLTSCHPLLSLPFPGNEPEEISFPLPEKRISSDLEFGKSFQYPTRWGTQQPSFFIQQIVVRSSVNPWTSDLGMMDAFRGPLSEVFKLHSDIVGFHSPRSNLTLRDVCLYVESVAPRARSFQHLLPEFSCIILSPANLWKLDENTFRNDAQFLDTIFSFKNPVVEVRSSMADILYGVPLKNSGLKKFPVKTRSRVLTYAITILLKTHSEPFLYDLRLKLRNQFPLHSTTQESTSSRRTIVHIYYPERFNYLELIPLTFVYLILFLYIYFSVRKIEMVKSKFGMAFSAVVTVVASLGMSVGLCTWFGLRFTLQGRDIFPYLVVIVGLENILVLTRSVVSTPANLDVKIRVAQGLSREGWNITKNLLTEVTILTVGFFTFVPAIQEFCLFAVVALLSDFVLQMLFFSTVLSIDILRKELSEIQRQRRQLQPGQQYLSTNHTVHTLSSAERAFAGNAVHPHLRTRVHSAAVSAKNTPTAVVAPSSYTHNRSAAARVPRRIRIVHFWARTRLFQRTFMVGVVIWMSIFFYKYVVMENLADQSAGWSVEANDSSQVEFPAPHPNLKVSCSAGSNCIEPEEPDLLKESTILANSAPPELSVTSSSGKEVIDWQYRLQHPKNVELWRRLSYRHWPDLLDIYNISLAGKCIAMLPPIRISIPVNPERVSEVRNSRDGEYLTRSRWKSLASALDTLDVLDGDDSGNGGSDEDNKTPYVPSSPIQIILTTLLAIPSVVFIAYVTVVLYRCICSRHYAEWRSSSTFWGWAGNAGGGLTQESREYYSQIVAESMPLVLDGHRSPIECISTDGDVVSSVCLAGQLHIWDIQTGDAVAQIDRNTYFAAFQQQTPTSNNKTSYFPSPVWCMQCFDGQVALGCANGRIEIWSHNSGLRCLYDDGSGVGVAKLKVCGEYLLAARLNGALESFQFHADFDSPVEEVSHHVHSRRGADEYDEEDRSSPLAFRLVRLNWARAHQQPISVLDASASGSRVVTGSLDHCLKVWRLETLTALYCLHGHRGPITAMFIDEAYPCSASGSGSQDGMLCMWDLSSGTCVYSLQAHDGSVSVLTYTSSYVISLGADDKLCVWERFQGHLLNSLSLSRLALCGSLAMLNDRLLVTSRQGSLVVWDVRTGESIREVRLGDADSSTFVRNVMVVRDNVICDYGTQLRIVSFPMISTHKVE
The following text describes a protein:
Function:
May modulate protein synthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein. Microsome membrane; Single-pass type I membrane protein. Nucleus membrane; Single-pass type I membrane protein.
Sequence:
ARGWESGDLELFDLVEEVQLNFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYDDILINGLPDWRQPVFYYRRVRKMSNAELALLLFIILTVGHYAVVWSIYLEKQLDELLSRKKREKKKKTGSKSVDVSKLGASEKNERLLMKPQWHDLLPCKLGIWFCLTLKALPHLIQDAGQFYAKYKETRSKEKEDALTRTELETLQKQKKVKKPKPEFPVYTPLESTYIQSYDHGTSIEEIEEQMDDWLENRNRTQKKQAPEWTEEDLSQLTRSMVKFPGGTPGRWEKIAHELGRSVTDVTTKAKQLKDSVTCSPGMVRLSELKSTVQNSRPIKTATTLPDDMITQREDAEGVAAEEEQEGDSGEQETGATDARPRRRKPARLLEATAKPEPEEKSRAKRQKDFDIAEQNESSDEESLKKERARSAEEPWTQNQQKLLELALQQYPRGSSDRWDKIARCVPSKSKEDCIARYKLLVELVQKKKQAKS
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. Plays a crucial role in maintaining the genomic stability by controlling the degradation of multiple proteins involved in mitotic progression and DNA damage. Regulates epithelial homeostasis by mediating degradation of CDKN1A and isoform 2 of TP63. Plays a regulatory role in innate immunity by negatively regulating IRF3 activation and IFN-beta production. Mechanistically, inhibits TBK1 phosphorylation and 'Lys-63'-linked polyubiquitination independently of its E3 ligase activity. Alternatively, promotes 'Lys-27' and 'Lys-33'-linked ubiquitination of IFIH1/MDA5, promoting selective autophagic degradation of IFIH1/MDA5 to inhibit antiviral response.
Subcellular Localization:
Cytoplasm. Mitochondrion membrane; Single-pass membrane protein.
Sequence:
MVASKELYFPLCGDNTSLPLRGGVTGRRRVCLSAAWADPPTRRERRRAICSWSVGYGTLTEQEESPVKQDLLTKKGKVADNATLLEPRGRRLVTSIATTHASPPASRRSRSKVDLLAMPGIKTLVNRRRNSGSETQTPLVKQNGSSGNLIKPAASLASLRKYETVLALTGVLRSSSSSSSVEPLQPVNRLRVPPQESASRFCSRCSSILTLASTSRYSLNSSTGGFVPIHKETLLLCKLCLAEVPSKDACCIADCKCSFCAECMRVYVEFEIAQGAYDISCPDAQCPSKGVLNEEEIKRLAGEDLFEKHNKYRLNREIELDKNRTWCPRAGCETVCNLCPTQQCHPQSVHCPSCTTDFCSNCKLEWHEGLTCEDNSKKLAKEGKVEEPGISFNSDLIKCCPMCNVPIEKDEGCAQMMCKRCKHVFCWYCLASLDDDFLLRHYDKGPCKNKLGHSRASVIWHRTQVIGIFAGFGILLLVASPLLLLAAPCIVCCKCRVCNAGTTKLDNEEEAPVEES
The following text describes a protein:
Function:
The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C. TAF5 is involved in two modules of TFIID, in TFIID-A together with TAF3 and TBP, and in TFIID-B with TAF8. Involved in contacts between TFIID and TFIIF in the PIC.
Subcellular Localization:
Nucleus.
Sequence:
FMAAPAEEAPEVSAQPEPAAPPAPPPPPPPPPPPPPPPAPPPPDASGDDGGAAGAASEGSPQDRQTLLAVLQFLRRSNLRESEEILRREARLPEPPEPPERPADGAAAAAAAGELDGPGPDAAAALLGRVTASAAGGPSAPGAPGAAPAPPAAPKVGIVPVEDQPDVSAVLSAYNQQGDPTMYEEYYSGLKHFIECALDCHRAELSQLFYPLFVHMYLELVYNQHESEAKSFFEKFHGDQECYYQDDLRVLSGLTKKEHMKGNETMLDFRTSKFVLRISRDSYQLLKRHLQEKQNNQIWNIVQEHLYIDIFDGMPRSKQQIDAMVGSLAGEAKREANKAKVFFGLLKEPEFEVPLDDDEEGDDNEEGKPKKKKPKKDSVGSKSKKQDPNAPPQNRIPLPELKDSDKLDKIMNMKEATKRVRLGPECLPSVCFYTFLNAYQGLTAVDVTDDSSLIAGGFADSTVRVWSVTPKKLRSVKTATDLSLIDKESDDVLERIMDEKTASELKILYGHSGPVYGASFSPDRNYLLSSSEDGTVRLWSLQTFTCLVGYKGHNYPVWDTQFSPYGYYFVSGGHDRIARLWATDHYQPLRIFAGHLADVTCTRFHPNSNYVATGSADRTVRLWDVLNGNCVRIFTGHKGPIHSLAFSPNGRFLATGATDGRVLLWDIGHGLMVGELKGHTNTVCALKFSRDGEILASGSMDNTVRMWDAVKAFEDLETDDFTTATGHINLPENSQDLLLGTYMTKSTPVAHLHFTRRNLLLAAGAYSPQ
The following text describes a protein:
Function:
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
Subcellular Localization:
Cytoplasm.
Sequence:
MAKDDVIEVDGKVVDTMPNAMFTVELENGHQVLATISGKIRKNYIRILPGDKVQVELSPYDLTRGRITYRFK
The following text describes a protein:
Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Sequence:
MTIHKTNKPRVAEDGEYATATSTLPVLQYYPARGRAEPIRLVLAFAGQAWFEPPPDSIRQIQAIQRREWDGYPFRQLPRFIDEVHGEVDLVQGGAILRHLARKYDLYGGERGDLVAAARVDMMLDGVADLRVKLRDLVVSKQLAQAAVAEYTGSVLAPERELKEHGMMGPGLACLEYVLANSRFSEAGWFVGPRPSVVDFAAFDLVDLHLAQPQLEDAVRGRFPLLVEHHDRVAGLAGVREYLASDSRHEVVWPVDWIRSTPGAGSGAAGGNA
The following text describes a protein:
Function:
Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MVDVACQLTAHGHNVQLFTSHHDKTRCFEENVSDKLMHRYYLSASFQSVFCCHFPDLLLALHTYSSKLQKLYRKPIGKLGLILSCATVFQSCDACMADLIPVNSKLNFLPINCFERKKKLVLTISAFALINSVVSMPSSGHDKHQKENVEYLEPRRLAVTEGVSDHFTFDEHFGIVPLEAMAAKKPVIACNSGGPVETIANELTGFICEPSPIELLKAISTLSTELYGAEFSTRKFGDLLNCYVLNVYNQRTE
The following text describes a protein:
Function:
3-aminobutyryl-CoA aminotransferase that acts specifically on coenzyme A (CoA) esters and catalyzes the conversion of 3-aminobutyryl-CoA into acetoacetyl-CoA in an alternative pathway of lysine fermentation.
Sequence:
MAEKLKLARSMSLFEEAKQLVPGGVAGIRRPYNFVPGEYPIFFDHGKGGRVVDVDGNEYIDFLCAYGPIIIGYREDEIDDAVINQIKNKGFCFSLTQEMQNTLVKKLRELIPCCEMAALVKTGSDATTIAIRVARGYTGKTKIARYGYHGWHDWCVEVKGGIPPKLYEDIYEFHYNDLDSLKAILEANKDDMAGIIITPIGHPNGAEVQMPKPGYLEAVRELANQYHCLLIFDEIRSGFRCSLGGAQKLFGVTPDLSTFGKAMANGYAIAALVGKEEYMQVLADKVFLSSTFFPNSDGIVAAIKTIEILERDRILDVVAAKGRKFGAEVEKVVEESGVPVNFTGAPWMPYITFKKDEAGLYKKLRTEYYTQLIRHNVFMQPYHHGYICYRHTDEDLAYTVEAIRESLAEVKKML
The following text describes a protein:
Function:
Severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MRTLGDCIEDLISARNYVQSGNYTPAQTCYDGFIASLNRYLNTLGPSAEKERWQEIKQQIKQEVASVMTLANSLSDLQRKPVKKAAPPANSIPCFDEQEDRFGPPAKPRGSVAAQQRSQLPRRQSNMGVQNTPAVRKGRNQPGSQAQVNRTPAPRGAPTYSQAQNLAPTSSAPNNASNVPVPRDITPSACQYEGISPDVAAAVHDCIVESTGVTFDQIAGLSEAKRLLEEAVVLPMLLPDFFTGVRSPWRGVLLFGPPGTGKTLLAKAIAMQAGFTFFSASASVIESKYRGEAEKMVRGLFTIARARAPSCIFIDEIDAIMSARGSGEDNECSRRIKAEILTQMQGVTTANGVGNGANGDFAEQEPKPVMTLAATNLPWDLDEALKRRLEKRIYIPLPDFESRKQLLKLNLKDITTVELDFDDLANRLEGFSGADISILVREVSMAPLRREISGKSIEEIKQMNSDPKFKEKLVVLLSDFEDAIKKTRPSVDQSAIKKYEKWFKEFGNI
The following text describes a protein:
Function:
Acts as a transcriptional repressor. May be involved in DNA damage-inducible cell cycle arrests (checkpoints).
Subcellular Localization:
Nucleus.
Sequence:
MPPNRKPEDTLLKKPLTLGLSQSYPSSALSTALKHVKIEMEDTDLPDLNSSCFGAIRMDKGPLDDDELKPLGWLHTTNVLKDINLDDDDEEDESYSKENDVGSNTYNGYGYQDDPMDPHRHINSKPPFSFSCLIFMSIEDCPLKRLPVKEIYRYIQDHFPYFRTAPTGWKNSVRHNLSLNKCFRKVDKIKGQSLGKGSLWCVDPDYRPNLLQALRKTPYHPYHHVLPYSPYGFSGGPLSNISSNQNRLSTVLSAYNGVPIPAHIALVERLLNSQLTHNQAHQNSLDLECEVDAAATMMMFRTPPDRRLAEHDRLKRESYPGARPIANQNLIIMGGLAPIQIRPEQPHCRPTLSDLAETALNELGDNRISRVAVTPENREMLKAKCTPSPSGMDHTYSLSSSIKVQADHGYSSDPGDVEMSDFSDESFEDESDMDQESRRLGDSGVHFHLEGGKRVDEKEALLPLKKRPPRMTEEDKKLADALLILSGIGAEAMPAKEAGSPGPEESTDVMMTEEVLEASR
The following text describes a protein:
Function:
Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Has a preference for 3-trans substrates.
Subcellular Localization:
Mitochondrion. Peroxisome matrix.
Sequence:
MAMAYLAWRLAQRSCPSSLQVTSFPVVQLHMNRTAMRASQKDFENSMNQVKLLKKDPGNEVKLKLYALYKQATEGPCNMPKPGVFDLINKAKWDAWNALGSLPKEAARQNYVDLVSSLSPSLESSSQVEPGTDRKSTGFETLVVTSEDGITKITFNRPKKKNAINTEMYHEIMRALKAASKDDSIITVLTGNGDYYSSGNDLTNFTDIPPGGVEEKAENSAVLLREFVGCFIDFPKPLIAVVNGPAVGISVTLLGLFDAVYASDRATFHTPFSHLGQSPEGCSSYTFPKIMSPAKATEMLIFGKKLTAGEACAQGLVTEVFPDSTFQKEVWTRLKAFAKLPPNAVRISKEVIRKREREKLHTVNAEECNVLQGRWLSDECTNAVVNFLSRKSKL
The following text describes a protein:
Function:
Repressor of jasmonate responses.
Subcellular Localization:
Nucleus.
Domain:
The jas domain is required for interaction with COI1.
Sequence:
MSTSSGFSQISSHRSISNSPDNLAFLPLHPMLLSPTDLNLGFSPNLRRTNGSVPEFFNSPEKMADRKSLDLFPQEAGFGNSNDVDSRVYKSVTAAPQTSQMTIFYAGQVFVFNNIPADRVGDVMFLASQESSRLNIPTVAARQPPILVGTPADSLSSTSPVPTRNQTSPPPPPPPSVPGALPMARKASIQRFLEKRKDRLTPRTPYQSSSPVTSKKTGENSWLGLAVQSQK
The following text describes a protein:
Function:
Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes.
Sequence:
MSKLFSEYKLKDVTLKNRIVMSPMCMYSVENKDGIATDFHFAHYVSRAAGGTGLVILEATAVQEVGRISEFDLGLWNDEQVPALKRLVDGLHYHGAKAGIQLAHAGRKAVLPGEIVAPSAIPFDEKSAKPVELTKEAIKEVVADFKRAAYRAKEAGFDVIEIHAAHGYLIHQFLSPISNRREDNYGGPAGNRYKILSDIIKAVKEVWDGPIIVRVSATDYAHGGLQLEDHIPFAKWMKADGVELIDVSTGGLVNVEPPVFPGYQVPFADEIRRGAGIATGALGLITRGEQAEEILCNERADLIIIGRELLRNPYFAKEAAETLGETIEAPKQYSRAWK
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:
MIVIALHPPWGVTHDATSRAPCSYALLSCPEPHEWTDQLRASFIAGFRSFMPILAVMQNMQSCCRQTEGHVEYEMEWEDAFTLQLKLMDVYSLFVDWCKSDKDVLEMSIVILADNLAKYRVREAHPITYENITVAGHTTYCPRWDFTVHKASVHQAMTRMYVALLLYLAKDPDVQLDSLLLKSEAESFENEGLTFEASFEPCLRTIVFVSQINAGMWKRNGIALQNMTHYYYNVKCRAFMYDKDVLFMQIAASLFSSDDMMLKLIYAFGLTNWIRREYDTETTQDETMRQIISMAESFLNWLIIIICERYNVLLSDVSQSDVRMYEIIHALCMQSMAHSELLSTINDGVIFFNDFLMKFEKEDGFEDLVKEVATFKKPTGLSGKGLYELKDEYYDRYNPYYYHYYKTNKARADENVKKFRKLKSIETDSVNPPPDCLPEFTGIFRDITNLLQCDVFVYVVKLVLLRSTSKYSKSWSESQQERALYLIELALLEETRRRKRGDTSFKFVTKALNLDAGAQASTSTTTPLPSLLVILEKFLLAWTSHHVMRDQANRIRIKLVEMSTVKDSSADMETDNPADDSTNSLQRIDAASRLSSDEKQLKIKSANEASKKSEKAQKRREKMLAHMAKMQRNFIKENQDLFESTSSEMVASNADVDMVAQESLPSQPDDTLTNHPVALGINRVPTVTTVSKHTCILCQEDQDVLPSEKALVYCCYIQNFFEGLAQRDARRNRIRSHNAYDITKKEFVCPMCENLSNAVLPIIPSLCMLSRESDENKVDVTLDEWLDGILKTVDHSIKQEQDKASKDDSFFYVPCPLSTVTKMMAEGVATRFQYLFDFIVDDNSSALSDSIVEMIKKFNDDMFEMSLDIYSYNSDYRMPLSVWNTCAYSILCIENSLRDEEKPLFGSLASKQAECLCTLVRLAAITTNLFAVSTIKRHCIRILSVMSCRYLDLNTPSITDMELFHCLVTLCYSLPSLYKEDSGGSTFVLSNGVNESNALKLVLACHILQIMIADLPARTQQDETARKQMEVDSESENDELMKICQHLRSMVGLPLCSLTPAELLQHIQLSCLPFLRCATLFFHHLTGVPAPLKLFEKNDEEFKVICEYLDLGPNLATLFNQSKHLQDVLMEWCNELSRMLDSHSSATENQTSIAAAPTASAAVAPAASSSRTQTSVHNPSLPSSSTPSYSSSSFSSSSSASTSYTVTQLSIPSTSHRPFTKIVYPRKVNRLIELPTNYSDLINQFSVFSCPKSNSNEDSRNPSMCLVCGLVVCSQSYCCQVKLDSSREDPVGAAVAHAYRCGAGTGIFLRIRDCQVMLMNGSNKGCFVSPPYLDAYGETDEFLRRGNPLALCAERYRYIEKLWINHQIASEISHKVEAYPHHGFNEWHTL
The following text describes a protein:
Function:
This protein is a component of an oligopeptide permease, a binding protein-dependent transport system. This APP system can completely substitute for the OPP system in both sporulation and genetic competence. AppA can bind and transport tetra- and pentapeptides but not tripeptides.
Subcellular Localization:
Cell membrane; Lipid-anchor.
Sequence:
MKRRKTALMMLSVLMVLAIFLSACSGSKSSNSSAKKSAGKPQQGGDLVVGSIGEPTLFNSLYSTDDASTDIENMLYSFLTKTDEKLNVKLSLAESIKELDGGLAYDVKIKKGVKFHDGKELTADDVVFTYSVPLSKDYKGERGSTYEMLKSVEKKGDYEVLFKLKYKDGNFYNNALDSTAILPKHILGNVPIADLEENEFNRKKPIGSGPFKFKEWKQGQYIKLEANDDYFEGRPYLDTVTYKVIPDANAAVAQLQAGDINFFNVPATDYKTAEKFNNLKIVTDLALSYVYIGWNEKNELFKDKKVRQALTTALDRESIVSQVLDGDGEVAYIPESPLSWNYPKDIDVPKFEYNEKKAKQMLAEAGWKDTNGDGILDKDGKKFSFTLKTNQGNKVREDIAVVVQEQLKKIGIEVKTQIVEWSALVEQMNPPNWDFDAMVMGWSLSTFPDQYDIFHSSQIKKGLNYVWYKNAEADKLMKDAKSISDRKQYSKEYEQIYQKIAEDQPYTFLYYPNNHMAMPENLEGYKYHPKRDLYNIEKWWLAK
The following text describes a protein:
Function:
Involved in the modulation of stomatal movement. Promotes stomatal opening. May play a role in the regulation of chitin signaling. May be involved in biotic and abiotic stress responses.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MGLEVGSLCFKLKDGGLTSRTNSFKRDDTNRHQNSPKSTMERSLSFNSWEVPKETKTDSDFEVLETKKSTPNTLNGRNCERIQIKKPTVTPPEPFVFFSPRPVTELDAAATTLQKVYKSYRTRRNLADCAVVVEELWWRTLEGAALDLSSVSFFGEEKHETAVSKWARARKRAAKVGKGLSKDEKAQKLALQHWLEAIDPRHRYGHNLHFYYDVWSASKSTQPFFYWLDIGDGKDVNLEKHPRSVLQKQCIRYLGPMEREAYEVIVEDGRLMYKQGMTLINSTEEAKSIFVLSTTRNLYVGIKKKGLFQHSSFLSGGATTAAGRLVARDGILEAIWPYSGHYLPTEDNFKEFISFLEEHNVDLTNVKRCSVNEEYSSFKSTADEEEERKEVSEEVEIPSEKEERARPVFDPVKRLSCKWTSGYGPRIGCVRDYPMELQAQALEQVSLSPRVSPANSYGPIPSPRPSPKVRVSPRLAYMGIPSPRAVKC
The following text describes a protein:
Function:
Terpene synthase that converts its substrate geranylgeranyl diphosphate (GGPP) into the diterpene beta-pinacene. Is also able to convert farnesyl diphosphate (FPP) into the sesquiterpene (E)-beta-farnesene as well as (E,E)-alpha-farnesene and beta-elemene as minor products.
Domain:
Contains several highly conserved motifs that are important for catalytic activity including the aspartate-rich 'DDxx(x)D/E' motif and the 'NDxxSxxxD/E' motif, both of which are involved in complexing metal ions to coordinate the binding of the isoprenyl diphosphate substrate in the active site.
Sequence:
MLCFNDFNFPKEWEVVPNSFKYIDIVIKEIIGFGLIKENDQELKMIVNQAISIAAYFWPYANEEQMVMGGSVLCWCVLFDDPLDTNKLDEKKGLEIVSRTEKLLLTRTLPNNPTNLEKYGFTIFEKCLKYCGTNTHMYDMLIKLTVQWIYSIIPFNKLNESPVHPETLKYIRKINIGIEFTQSIFYIINSNNKVDLIVLANPLYQKLVDLSSLNISFVNDAASFCKEIKDGGSDNNLFIILMKRLGGIEFIKEAYKQLTDLSNGYIDEFCYYEKLLLSSLSKQQQNEIQIFIDHLKYLMKGNQIWSTKTIRYATEDHPIIQLRNSTNKLIENNINMDKVSLTNKNYI