lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Pectin methylesterase (PME) inhibitor that targets PME from seeds and modulates PME activity and pectin methylesterification during seed germination. Promotes mucilage release by limiting methylesterification of homogalacturonan in seed coat epidermal cells.
Subcellular Localization:
Secreted, extracellular space, apoplast.
Sequence:
MTSSSSSPITFTLLLLLSLLVALNPNPSLASTGSNINTNDIVTQYSTYVRNACNVTRYNRLCVRTLWPFAIVARNNTSKWARASVAVTITDTKRVLRLLLKTQRSAVGESERIALSDCRELFVDSLDNLYKSLAVLRTLNADEFQRQISDLATWLSAALTDDDTCLDGFEETSSRTRTVRMVRRKATKCMRLCSNALALLKKLAFDGL
The following text describes a protein:
Function:
Serine/threonine-protein kinase that may function as a signaling receptor of extracellular matrix component. Binding to pectin may have significance in the control of cell expansion, morphogenesis and development.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MSLLVLLLQLLLSWSRPIMAISSTVSVAKPGCKDKCGTISVPYPFGFGEANCYRESFDLTCNSTSFDPPKLFLGTNGTVEVIDISPLGSLRVRNFVGYDCYNRSGGHSRNRPWMDLKMKPYSFSDVHNRFTSIGCDIYTYISGSKGRNFTSGCSMVCSDQQSLVNGSCSGIGCCQTSIPKGFKEYDVEVHSFHNHTRVMDYNPCSYGFLVDAEWYKFSVGDLFGYMDFYNRNDEKVPVVLDWAIENYTCENVSRSDPSYACGKNSDCYNSPNGLGYLCNCSQGYHGNPYLEDGCQDVDECAGAHMNDCKMICTNTPGSYNCSCPPGMEGDGRKTGTGCTALPSSLMQIALGTGFGILLLLFLSSWLYWGIQKRKQNKRKEKFFEQNGGFLLRQQLSSRNGGVDAAKIFSEEDLKRATNYFDESRILGRGGYGTVYKGILPNNKTVAIKKSKIMDESQVEQFINEVIILSQINHKNVVKLLGCCLESEIPLLVYEFITNGTLFQHIHDEEHKSSISWDNRLRIATETATALAYLHSAASPPIIHRDIKSANILLDDNYMAKVSDFGASRLVPLDQTQFTTLVQGTLGYLDPEYFHTSQLTDKSDVYSFGIVLVELLTGRKALEFDRPEKERNLAIHFITSLKEDNVLELLEDRVLHEASKDQIQEVTNLVKRCLSVKGEERPTMKEVAMELEGRIRSIVQHPWVEPNHEDAEYLLAEPSNPHNCNTTEYDSLRNHVVISLDSGFPEEFLLRYLLLGVLDWAIEKYTCENVPRSDPSYACRNNSECFNSPNGLGYLCKCSPGYHGNPYLDDGCQDVNECADEAKNECKAPLAICTNMPGSYTCSCPSGWEGDGRKNGTGCTALQNKRSSVMQIALGTSFGVLLLLFIGSWLYWGIQKRKQTKLKEKFFQQNGGILLTQKLSSRDGNAEMAKIFTEEELKKATNNYDESRILGRGGYGIVYKGCLPNNRIVAIKKSKIKDESQVEQFINEVVILSQINHKNVVKLLGCCLESEVPMLVYEFITNGTLSHHIHDEVHKSSFSWEYRLRIGTETALALAYLHSAASPPIIHRDIKSANILLDDNYMAKVSDFGASRLVPLDQTQFTTLVQGTMGYLDPEYFQTSQLTEKSDVYSFGVVLVELLTGRKALEFHRPEKEKNLATYFITWMKEGNVLEILEDRLLQEASKDQLRQITNLAKRCLNMKGEERPTMKEVAMELEELRMHKEHLSSENNDEEAIHLLIGEPSNLHSCKTSEHHSIRDHVVISLNSGR
The following text describes a protein:
Function:
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein. Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
Sequence:
MQVGSFLSTSLLLQIGSFKPIEAKFVELIGAIGLIVGILFLLLGATLGVLVVVWLERKVSAGVQQRVGPEFAGPLGLLQALADGLKLVLKEAVHPSRADERLFRLGPAMVVVPVFLSYLIIPFGPGMMLEDLGVGVLFWISVSSIAPLGLLMSGYASNNKFSFLGGLRAAAQSISYEIPLALSVLAVCLLSSSLNTSDIVEAQSGFGVLSWNVWRQPIGFILFLISSLAECERLPFDLPEAEEELVAGYQTEYTGIQFGLFYVGSYVNLIASSLFVTVLYLGGWGLPLPGVVERIVPAGLQGSLLPALVGFIGLFATLLKAYCFLFFAILTRWTLPRVRIDQLLDLGWKFLLPVSLGNLLLTACCKLAFV
The following text describes a protein:
Function:
Catalyzes the hydrolysis of the amide bond in N-(4-oxoglutarate)-L-cysteinylglycine (deaminated glutathione), a metabolite repair reaction to dispose of the harmful deaminated glutathione. Possesses amidase activity toward deaminated ophthalmate in vitro. Plays a role in cell growth and apoptosis: loss of expression promotes cell growth, resistance to DNA damage stress and increased incidence to NMBA-induced tumors. Has tumor suppressor properties that enhances the apoptotic responsiveness in cancer cells; this effect is additive to the tumor suppressor activity of FHIT. It is also a negative regulator of primary T-cells.
Miscellaneous:
MISCELLANEOUS: According to Rosetta Stone theory, the existence of a fusion protein in one genome predicts that the separate polypeptides expressed in other organisms function in the same cellular or biochemical pathway. In Drosophila melanogaster and Caenorhabditis elegans, NitFhit is a fusion protein composed of a C-terminal Fhit domain and a domain related to plant and bacterial nitrilase.
Subcellular Localization:
[Isoform 1]: Mitochondrion; [Isoform 2]: Cytoplasm.
Sequence:
MLGFITRPPHQLLCTGYRLLRTPVLCTQPRPRTMSSSTSWELPLVAVCQVTSTPNKQENFKTCAELVQEAARLGACLAFLPEAFDFIARNPAETLLLSEPLNGDLLGQYSQLARECGIWLSLGGFHERGQDWEQNQKIYNCHVLLNSKGSVVASYRKTHLCDVEIPGQGPMRESNYTKPGGTLEPPVKTPAGKVGLAICYDMRFPELSLKLAQAGAEILTYPSAFGSVTGPAHWEVLLRARAIESQCYVIAAAQCGRHHETRASYGHSMVVDPWGTVVARCSEGPGLCLARIDLHFLQQMRQHLPVFQHRRPDLYGSLGHPLS
The following text describes a protein:
Function:
Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Subcellular Localization:
Cytoplasm.
Sequence:
MKITIIGAGNIGSAVAACLAKGHLYNEKDIIISTPHTDKLENLHKQFPAIRIMTENQYAISEADIIILAVKPCIVDEVLSPLRFSRTQILVSLVTGISISHLAHLSETEMPIFRVVPNIAITEHSSLTLITSRKAGKEHQQLIKQTFEEGGKCLFAEEKQLDIISALTSSGIAFALKYIHAAMQAGIELGISAEDAMRMTAYSMEGATELILNHDTHPLLEIEKAATPGGATIKGLNELEHRGFTSAVIHAIKSSATVSTDKETEE
The following text describes a protein:
Function:
Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB.
Miscellaneous:
MISCELLANEOUS: Present with 1130 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MSSTIFYRFKSQRNTSRILFDGTGLTVFDLKREIIQENKLGDGTDFQLKIYNPDTEEEYDDDAFVIPRSTSVIVKRSPAIKSFSVHSRLKGNVGAAALGNATRYVTGRPRVLQKRQHTATTTANVSGTTEEERIASMFATQENQWEQTQEEMSAATPVFFKSQTNKNSAQENEGPPPPGYMCYRCGGRDHWIKNCPTNSDPNFEGKRIRRTTGIPKKFLKSIEIDPETMTPEEMAQRKIMITDEGKFVVQVEDKQSWEDYQRKRENRQIDGDETIWRKGHFKDLPDDLKCPLTGGLLRQPVKTSKCCNIDFSKEALENALVESDFVCPNCETRDILLDSLVPDQDKEKEVETFLKKQEELHGSSKDGNQPETKKMKLMDPTGTAGLNNNTSLPTSVNNGGTPVPPVPLPFGIPPFPMFPMPFMPPTATITNPHQADASPKK
The following text describes a protein:
Function:
Promotes growth and fasciculation of neurites from cultured hippocampal neurons. May be involved in fasciculation as well as myelination of developing neural axons. May have a role in regeneration as well as neural plasticity in the adult nervous system. May mediate homophilic as well as heterophilic cell-cell interaction and contribute to signal transduction through its intracellular domain (By similarity). Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Perikaryon. Cell projection, dendrite. Note=Colocalizes with KCNB1 at high-density somatodendritic clusters on the surface of hippocampal and cortical neurons. Associated with axons of neuronal cells (By similarity).
Domain:
The LRR repeat region mediates homodimerization.
Sequence:
MQPQRDLRGLWLLLLSVFLLLFEVARAGRSVVSCPANCLCASNILSCSKQQLPNVPQSLPSYTALLDLSHNNLSRLRAEWTPTRLTNLHSLLLSHNHLNFISSEAFVPVPNLRYLDLSSNHLHTLDEFLFSDLQALEVLLLYNNHIVVVDRNAFEDMAQLQKLYLSQNQISRFPVELIKDGNKLPKLMLLDLSSNKLKKLPLTDLQKLPAWVKNGLYLHNNPLECDCKLYQLFSHWQYRQLSSVMDFQEDLYCMHSKKLHNIFSLDFFNCSEYKESAWEAHLGDTLTIRCDTKQQGMTKVWVSPSNEQVLSQGSNGSVSVRNGDLFFKKVQVEDGGVYTCYAMGETFNETLSVELKVYNFTLHGHHDTLNTAYTTLVGCILSVVLVLIYLYLTPCRCWCRGVEKPSSHQGDSLSSSMLSTTPNHDPMAGGDKDDGFDRRVAFLEPAGPGQGQNGKLKPGNTLPVPEATGKGQRRMSDPESVSSVFSDTPIVV
The following text describes a protein:
Function:
Pointed-end-associated component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding (By similarity). The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. May regulate the association of the dynactin complex with the plasma membrane.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MSNTIVIVYLGANRIEIGRSADACPQEIIAWKTGSINEKNREELKKIFEHYFQICNILGNREVQVLILEDIFISVVEKRIICSILFKEFDCAHVSFVPRAIVHCLSCNTRNAIVIDIGTNYTTCVPIFDLRPLQQFIKYSKRGKRQVESRIPLPGSLYMPIFFDEEYNSKNCEVDETPVINLVKNIVESLPIDLRRPLRENIIIVNIEEAYETVIRNLFKLKMDTSKIQFPKNYWQAGSACAKILLHYKGSNIVGIERDEFYNNPHIAPDWFDYYFRTGVKRLQ
The following text describes a protein:
Function:
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM34 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10.
Subcellular Localization:
Membrane. Mitochondrion outer membrane; Multi-pass membrane protein. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Domain:
Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Sequence:
MSFEFKWPKFSPSFYDHAKDLLSTALNKGDKPAIIADRIEVNQLDMGTIPPDLEILEIGDLGRDRFRGIFRMTYAGDASIRLQTKVQVNPLRQRTPTATSDVLTTPPILFASTPLIVPMTLSLSSLKLRAIVVLVISRLEGVTLVFKNDPLESVQVSSTFDSLAAIQTFLQSEIERQLRDLFRSELPSIIHQLSRRWLGRDNPDGRSQARVELPSTSAPSTPTPSLPTAQSNGDHNGLLSVPDEIEGYDPTYGLRPSHPPLVGCFTNYRSLIKQKNRKLGLGAVLSHTDDEEEHSKEDLIPSDVSSSTLYSPPHSPTPSPQQKQKKPDASRAKKPMIKPKIFHSHSAGIVNSALSSSGISSHNGHEGTRSSSKALEPKARMKLEDLQEARVEEEQLEEGEVLRSRRLERLSMQSHSVSSSGLAARMMSIREKAQRKRPEQIRMSTSPISTFRTQPLPRPTPSIFPSTQRSSMTCLPAYASNCGTPVRSHAHSPIFLGSRSTSPMRGEDEKNDQEGGEESEGEGSQCALLASLVRSNCTLSPFSRSISHFAARSTPLRHSSPSSALSSPTRVSHLNELHSFYSRDTVDLDQLHLRSSWNDLHADGFKQKRVIKINKKN
The following text describes a protein:
Function:
Required for cytochrome c complex (COX) IV assembly and function Protects COX assembly from oxidation-induced degradation, COX being the terminal component of the mitochondrial respiratory chain.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MAALRPGSRALRRLLCRSFSGGGGVRLARERPTDHRDAASSRVSRFCPPRQSCHDWIGPPDKCSNLRPVHFHIPENESPLEQRLRELRQETQEWNQQFWAKQNLSFNKEKEEFIYSRLQAKGAGLRTESGQRATLDAEEMADFYKDFLSKNFQKHMRYNRDWYKRNFAITFFMGKVVLERMWSKLRQKKTSS
The following text describes a protein:
Function:
Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing.
Sequence:
MDRASSASQLIASNVTNKTDPRSLNSRVFIGNLNTMLVTKADVEAIFSKYGKIVGCSVHKGYAFVQFAQERNARTAVQGEDGRMVVGQVLDVNLAGEPKPHRSKTTKRSAGDMYSSSSSFELDYDFQRDYYDRMYSYPSRVPAPPPLSRAVIPSKRPRVSTSGATSRRTKSSFATSSKSSQRTSSRTLKADDLQTIKRELSQIKHKVDFLLESLDRMEKDHGKKSEGKSVKAEVGEVSPLQHSSKKEREREEQEINDSEEERDLLGEEEEEEEEEEVCVVVAGGRHPKPCDILMLLRLTSVFVLLRLKARVERMRMRKRKEKRKRVSMKKGKMMAIALMVTTRNFKRSGYQTSTQISALSVLLKRLKQVFKRSIYDDVDVCALILADTAITSV
The following text describes a protein:
Function:
Probable RNA-binding protein, which may be required during spermatogenesis. May act by binding to the 3'-UTR of mRNAs and regulating their translation.
Subcellular Localization:
Cytoplasm.
Sequence:
GLLRPLLARLRAKISRWLAFFSLPHFGGEGLDPRVTAQVHDDPRDPEEAVAVAVSPGASACWPRRGRSAEAVTATQTSNQTQTDSLSPSPNPVSPVPLNNPTSAPRYGTVIPNRIFVGGIDFKTNENDLRKFFSQYGSVKEVKIVNDRAGVSKGYGFVTFETQEDAQKILQEAEKLNYKDKKLNIGPAIRKQQVGIPRSSIMPAAGTMYLTTSTGYPYTYHNGVAYFHTPEVTSVPPPWPSRSVSSSPVMVAQPVYQQPAYHYQAPAQCLPGQWQWGVPQSPASSAPFLYLQPSEVIYQPMEIAQDGGCVPPPLSLMEASVAEPYSDHGVQATYHQVYAPSAIAMPAPVMQPEPIKTVWSIHY
The following text describes a protein:
Function:
Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (msh2-msh6 heterodimer) and MutS beta (msh2-msh3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops. After mismatch binding, MutS alpha or beta forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MSDNEQEESSQVVLKEDKTFVTFFQSLVSSNEDTDTIRLFDRKGYYSIHGEDAVFVAMMHFKSKKSLKYWSISDPNPKKKIKIDNDGSLTTTASSSQQQQQELGLAVLTIRQGYEFENIVKELLDEKKKIEIWSMKPNSKQQWELIKKGSPGNTQMFEDVLLNGNCEGSVMMALKVTREKGSIVFGISFGDATFKTIGVSQFMDNDNLSNLSSFIMQMSVKECLLCCDQKNYDYQKVKEKLSDAGIPFTELPKSDFSSKNAEQDLTRLLGSVKNNLPDIEQEHAIQSASCLIKHLDLLSNPNYFGKFKLEKYDLDRYMKLDSSSFKGLHIIDLKDSSVSAAAGGGGAGGASSSSNKDQSLYNLLNQCNTPMGSRLLLQWVKQPLLNAEEIEARLNFVEAFYNDLELRQSLRSNDLKKIGDLDRLSKKLHGQKATLEDCVNLYGIVTRLPVVLQSLNNHSSIHQELIKVNFIESLESIISDFAKFCAMVEKTIDLDLANDKHEYVIRSSFDETLRGIQLKKDQISNKIERFRVDIADDLNLDEAKVKLHYSEKDMFLLRISRKDEVAIRDKKKYIVHATAKDGVRFATREIDTLNEAYKKWSAEYLDKQDGLAKRTLQIAASFVPLIEDLSSLIATLDVFVTLSHVSSIAPIPFIRPEIIPLGSDENGAGTVIIGGRHPCVEIQDNVNFIANDIDLTRGQSQFQIITGPNMGGKSTFIRQVGLIVLMAQIGCFVPAQKATIAVVDCILSRVGAGDSQLRGVSTFMAEMLETSYILKVATKNSLIIIDELGRGTSTYDGFGLAWGIAEYICNQIGGFCLFATHFHELTILSDLLPMVKNLHVSASTQNNTFTLLYKVEQGPCDQSFGIHVAILANFPSQVIENAKQKAKELESFESNTLKQNHNKFLEEFKEINFNSNDVEKSLSLVNSLLNKYSIDIN
The following text describes a protein:
Function:
Selenoprotein with thioredoxin reductase-like oxidoreductase activity. Protects dopaminergic neurons against oxidative stress and cell death. Involved in ADCYAP1/PACAP-induced calcium mobilization and neuroendocrine secretion. Plays a role in fibroblast anchorage and redox regulation. In gastric smooth muscle, modulates the contraction processes through the regulation of calcium release and MYLK activation. In pancreatic islets, involved in the control of glucose homeostasis, contributes to prolonged ADCYAP1/PACAP-induced insulin secretion.
Subcellular Localization:
Endoplasmic reticulum membrane.
Sequence:
MRYLLVLLVAASAVIRSDASANLGGVPSKRLKMQYATGPLLKFQICVSKGYRRVFEEYMRVISQRYPDIRIEGENYLPQPIYRHIASFLSVFKLVLIGLIIVGKDPFAFFGMQAPSIWQWGQENKVYACMMVFFLSNMIENQCMSTGAFEITLNDVPVWSKLESGHLPSMQQLVQILDNEMKLNVHMDSIPHHRS
The following text describes a protein:
Function:
Responsible for the uptake of citrate in exchange with the efflux of succinate, fumarate or tartrate. Has a relatively broad specificity for C(4)-dicarboxylates and tricarboxylates.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MSLAKDNIWKLLAPLVVMGVMFLIPVPDGMPPQAWHYFAVFVAMIVGMILEPIPATAISFIAVTICVIGSNYLLFDAKELADPAFNAQKQALKWGLAGFSSTTVWLVFGAFIFALGYEVSGLGRRIALFLVKFMGKRTLTLGYAIVIIDILLAPFTPSNTARTGGTVFPVIKNLPPLFKSFPNDPSARRIGGYLMWMMVISTSLSSSMFVTGAAPNVLGLEFVSKIAGIQISWLQWFLCFLPVGVILLIIAPWLSYVLYKPEITHSEEVATWAGDELKTMGALTRREWTLIGLVLLSLGLWVFGSEVINATAVGLLAVSLMLALHVVPWKDITRYNSAWNTLVNLATLVVMANGLTRSGFIDWFAGTMSTHLEGFSPNATVIVLVLVFYFAHYLFASLSAHTATMLPVILAVGKGIPGVPMEQLCILLVLSIGIMGCLTPYATGPGVIIYGCGYVKSKDYWRLGAIFGVIYISMLLLVGWPILAMWN
The following text describes a protein:
Function:
Protein kinase which phosphorylates and activates MPK4 in vitro.
Sequence:
MSRLKINLDAIERDGASATEGFCADGVRIGSLLVSSEGVRDNQGNLCVLSLSDLEVVPETEGGFLGKGSSGSVRRAVHRGSNKVVALKEIKVTGQTHINEIRRELETLHAGDFATPYLVSFYGAFAHEGSVFIAMEAMDGSLHELYKPVPPPVLACITRLMLKGLTYLHRNRHLIHRDLKPSNVLYNSRTGDIKISDFGVSSNLECTKADAHSFVGTVTYMSPERLRGEHYSYGADIWSLGLVVAELAVGVCPYAGLRGGSSEARFWALLQHLNGDGTALELPPEMDSDLADFISACVVKSPDRRPTCTELLRHPFIVRYTGAAPEAEAKPFSTTTPTVLAPGGLSSLLNRASPAAGSALPLASEGGTPKATSPSPAPVSPLTLSCPLERHDGETDADIADRTVVARWIHAVMKRAVLHKARGHGREELHQEPLAAVSASVATDSGEGGGAAGVSAASLDNGQAAQHREFRAERNLDGHSGDGGSAPVEEDCTAGVRSLTCDDLRWTSTGEPSVNLDDELNRLLF
The following text describes a protein:
Function:
DNA-binding protein exhibiting the ability to bind to both single-stranded and double-stranded DNA.
Sequence:
MKAKEIIEFIETFAPKDLAIEGDNIGLQVGDNLDKEIKKLGIALDPSLSVIKKAEKEGVDFLFTHHPLLKDPIRNFTGVIYKKLKILMENDIILYSAHTNLDICKNGLNDALAELYNLENPKPLYDNGLGRVGIFKGSFEEFLEITKKYIHKNPIVVKSKEVDDNFKLAVLSGYGLSQSSIKYVAEKADVYLSGDLTHHSKILAEELGLVVVDATHYSTEVFGLKKFKEFLSSNLDLEIISLDF
The following text describes a protein:
Function:
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of aspyridones. The polyketide-amino acid backbone preaspyridone A is first assembled by the PKS-NRPS hybrid apdA. The assembly of preaspyridone A is initiated by loading of malonyl-CoA onto apdA, followed by decarboxylation to yield the acetyl starter unit. The growing polyketide chain then elongates into a tetraketide. The adpA PKS module catalyzes three Claisen condensations, as well as beta-keto processing and methylation. Alpha-methylation step during polyketide synthesis is a prerequisite and a key checkpoint for chain transfer between PKS and NRPS modules. The downstream NRPS module contains the condensation (C), adenylation (A), and thiolation (T) domains and catalyzes the incorporation of tyrosine via the formation of the L-tyrosinyl-thioester and the amide linkage between L-tyrosinyl-thioester and the tetraketide. The bimodular assembly line is terminated with a reductase (R) domain that facilitates formation and release of the tetramic acid product. Because apdA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase apdC. ApdC appears to operate with different stereoselectivity in different PKS cycle (Ref.5). Combined with apdC, apdA is proposed to synthesize preaspyridone A via about 20 enzymatic steps. A number of oxidative steps performed successively by the cytochrome P450 monooxygenases apdE and apdB are required for the conversion of preaspyridone A to aspyridone A. The cytochrome P450 monooxygenase apdE is responsible for the oxidative dephenylation of preaspyridone A (Ref.5). Finally, the predicted FAD-dependent monooxygenase apdD and the acyl-CoA dehydrogenase apdG may be involved in the transformation of aspyridone A into aspyridone B (Probable).
Sequence:
MWSILSIKRSTSRMELMCLNAAECPINVFPEQQRNMPTESLNPGTVLIVGGGPVGLITATTLAKYGVRSVILERNLTTTKWPKMDLTNSRSMEIYQRLGIADALRNVAVPSHYPFTCLFSSGLHADKAITAWDLPSPDEYRRRIREQNDGSMPSEPWLRVSQEIFEAWLKELGMENPLIDFRAGWKVKGARELDHGVEVEAIHSDTGEVWKVSADFVIGCDGAHSAIRKSLEIPLDGGPIHGYAVLVHFKSRDLSRIQKQGQFWHLFFPNAASDGGSIKGAVIAQDEVDTWTVHRFMRPDVDHTQLSSEEIVYDLLGGMGGQPFPIRIDEVLVRSTWTPSVALARSYAGPKHRIFIAGDACHQTVPTGGYGMNTGIADGYDIGWKLAAVIQGWAGPATLLSYEKERRPVGELALQWSKVHMGNLMKMSAELGLDAHMIELNNETGAELRGAMHSYLQTHDGHNQSIGVEMGYRYVSNICVPGALDAELSPPEFHPRKYTPCTMPGYRAPHVYLTTGTPVSRLFGDGFTLVAFPEGEGLNASTEQLREAARKKALPLEVVELPGEMHAHEVWGASLVLVRPDGFVSWHGDSVRSQEEADRIIAQASGFDSEHLGNHVQAQERSAL
The following text describes a protein:
Function:
Non-catalytic subunit of the heterodimeric RalGAP1 and RalGAP2 complexes which act as GTPase activators for the Ras-like small GTPases RALA and RALB.
Sequence:
MYSGWASLQEAIESDQSNHSVLHTFPETVGRDVAVSVVKQLAASTASLAALQQRGDGSSACNPLESEKQVEWTMEVICYGLSLPLNEHEAIRDCVSVYCEWLKALTIPQPTLPTPLSKDPNPYIQKIFQHLVNLFKPRQQGMSDTNKQAVLCHRVLRSIQSVATESIVMTKHTWEVLLRFLLSINHTLLSPPLESGSLAEQLCERLLSVLFEVWLLACARCFPSPTLWRTFREMCCTWRHHPATVAQWNRINKVLTAQLIQVLYGPIFPPLKLGDDEGRIIPPELDNDGLAQAWFRFLHILGNPVDLCHPEIIGRTPKFVASINQGKKFPDQHSCLQALPDIFLKAMKGLSVLVDAYLGYPPDRLGHITDPSQGIPSRSPTIPSAAPFNAASKAKGVPSAGGRGTSSTNSGIRGGVKSNILHTGMLPGPSHSECNSILHLFGAWLFEAALMGCKFHGAATPAPFLPRRSGSLFVTPSSSSSAAAASALSNTGSFSNTSTINFTSSSTTTATTSTNASTNSRMMRRAQSIPSSSDAPHVREGHEREAISSPGAPSALLVPDRLSSPESYEEGRAEACGTLCRIFTSRKAAESILPMYLSRFYLTLTQGLSTNARQPVSGLVLSNILYNSHNLLRVDLTGVKVLIPYLLSAMDLVIPETDLRFKSLVPKNELRRASIHLLLSMLCLPHHFKDLTIQSIIQNDADDCKPEMTFMSLKPQLVDLMISGFRCESNPQNAQMLLGAMYMCILDSAMSESVEAKTSNSETPSRKESTSSVNDSEETAENAPPGSSLSGSLFALIDAAFQETSNTPITTVTDTAWAIFVRCCHLVFQQLMSTWSKDCGVAMAALELLSGVARIPMKVQDPLECKRNVKWICDHIAKQCNQPSVYHSRDLHSIIVAAFNCLTVWVVEHSYLLKDRETLQIVLEVVELGISGTKSQPKASIPAVLKQAKELKPTSTRVKNAAQGVLSCILNQLGSFPAPCGPSTVVSLLDETSLLKYVDLPNPEVKPTFKYFVMDNSILLAMLEEPLKFTKELLPTVTVIIRGPTGRHVWTFQLRHSSRKDKETAEARLIYPERPQPNDSMGTHHEITSKYFPDSINKIPITKADQSIPSLDEIETEESHEDHVTLGKLLQDQMEYEKLVSDTAHEETERVSYPNPQTESRPPKPCTEFSPARLLLSHLGYLNIESLQGPENSSLPPALVAIDDTQAGFTPDLLHLDEIPSRTFDTAFIFYVKTGQKKAEDILFNVKSKDNVQYQFLEFLQALGWPVVIGQHAGWTGHMTTSWKIPDFDANTKTQSNGNVKEELSHGGSLYSGKKQVLYFADFSSEIAFVVPTDDEPKVASNDDATQLSPVPEEPNPAQPPSSSTQQGVQPRPADLEASGSSSNSSLAGSLAGSLERPSRKFSTKGVNATPPELKVLVVWLENFEDHQTFPLADLLHKTSTGSENLTTSNNSLSKTPEPSIMIIYIHLLKSGLFRIHIQSSCTLAIPLVDGMVVSRRTLGTLVRQTVVNTCNRKRLESEKYSPPHVRRRQRIQEMVQKYQRKQSVSEFYTSLFTS
The following text describes a protein:
Function:
Binds to 23S rRNA.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MDGIKYAVFTDKSIRLLGKNQYTFNVESGSTRTEIKHWVELFFGVKVIAMNSHRLPGKVKRMGPILGHTMHYRRMIITLQPGYSIPPLRKKRT
The following text describes a protein:
Function:
Stimulates the release of gastrin and other gastrointestinal hormones.
Subcellular Localization:
Secreted. Cytoplasmic vesicle, secretory vesicle lumen.
Sequence:
MEGVLLFWKYRALFFLVLCSLVLCKVHLSQASPTSQQHNDAASLSKIYPRGSHWAVGHLMGKKSIEEYPYAYDEADRSSAAVFSEGDKPSDGYQQWKESLLNLLKMIEVNEYRNSKAMREASVYNKKFSGAEDNNLKEMLDYLYQMMNMKENTSS
The following text describes a protein:
Function:
Vesicle-associated protein that binds the oxysterol-binding protein ORP3A and allows its targeting to the ER.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type IV membrane protein; Cytoplasmic side.
Sequence:
MSNELLTIDPVDLQFPFELKKQISCSLYLGNKTDNYVAFKVKTTNPKKYCVRPNTGVVHPRSSSEVLVTMQAQKEAPADLQCKDKFLLQCVVASPGATPKDVTHEMFSKEAGHRVEETKLRVVYVAPPRPPSPVREGSEEGSSPRASVSDNGNASDFTAAPRFSADRVDAQDNSSEARALVTKLTEEKNSAVQLNNRLQQELDQLRRESKRSKSGGIPFMYVLLVGLIGLILGYIMKRT
The following text describes a protein:
Function:
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MATLDENNPSKQTHRHWSIENEIKLFSLLCDYKPAGKNKQHNIKIIINNINESLDSKEEPFSEYDVWNKLRSLYDLEKIDQIEELSTENTSTEETTNQVSSGSANITKDTKNAKTTLDAKEPIQDKKEMDKEKSESSSLSTPEPPQRRTRSARDTTKSKRNLRDTPKEKSQYNDEEITSGGAEKSKVEVSSTSDHTDDQSPTPGSTKKGLDEQTNDDMSDIEDVDKDKGDETIAKIKKENTSEQEEDKNKKQTEEEAEEEEEEGDHVSGDERESKNKDTSEDEDGEDNEDQDEDDVEVIEDSHTDKENESSSEESSPEPMTKRTRQRTRSTHEKTEHTSPNIKKRTRQSVKFDDKPAEPSDTGSRKRRAPPGSVSPPHPPKTRRRTRSVTHEIEEEDASTQSADDAEPEIIKVETRHTTRRSSRISMEPSSSTPNVRVRRSSRKR
The following text describes a protein:
Function:
Binds to the 23S rRNA.
Sequence:
MKVLLLEDVKNLGKAGEVCEVKDGYGNNFLIANQKAKLATNEVINKYKAEVKKKAEKEALEKAQKLQMVETLQTITLTIHKKVGANGSLFGAITKEEITERLKEQHASLNLDKKDIELKHPIKSTGIYEIEVKLGSGVVGVFKIDVVAE
The following text describes a protein:
Function:
Catalyzes the hydrolysis of the vinyl ether bond of choline or ethanolamine lysoplasmalogens, forming fatty aldehyde and glycerophosphocholine or glycerophosphoethanolamine, respectively and is specific for the sn-2-deacylated (lyso) form of plasmalogen.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Cytoplasm.
Sequence:
MPCCDPYPWIGLNVGRLSSFPLLKYPQVRRWLAPFIVACSLYFLLWIPEDQPSWVSALVKCQPILCLVLFLWAVAPGGSYTWLLQGALTCSAVGDACLIWPEAFFYGMAVFSVAHLLYLWAFGLSPLQPGLLLCTTLASLTYYSFLLLHLEPNMVLPVAAYGLILNTMLWRGLVLGRSAGWGAVLFIFSDGVLAWDTFVYTLPFARLVTMSTYYAAQLLLTLSALRSPGLKTH