lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in tRNAs. Probably not able to catalyze formation of N(1)-methyladenine at position 9 (m1A9) in tRNAs.
Sequence:
MAASSSIGNPYRNGFELWRKTIKACRYAVGPREHIPDLAFRLLCRHHNVQLFYTPLLKAEEILNDWDSYKYHFLNANNFQDRPLIVQLCSRDPNRMLQAAERVDSLCDAIDLTLHSETNAKTILNQAVGKDFQLLQRMISLLRDNLNMPVACKIKIAADKDSSSLIKYAKRLESAGCQLLSIGCRHKEPRFRLDDWNIVKAVKDSVVIPVFACSDISTLAEADLCLEYTGAQGIMSHDTELYYRQIKTIDDLRNLTSPLTSTMSGTKREKKRKQMKIKLTFKKQQEREKKKLKKLDQPLRETTDDYITKRQRHILRDGRLRTAMCSGQRIVIDMGLTEGMTNKEISKLCNQVGRLYGSNCIAEDPWHIYFTRFGQEDELYQRCTEFHHGFQNYKIDVTTESVLELFPPEEIVVMSPDSKNVLRKIDSSKVYVLGGIVDESIRKRISLHYGMQCEVATCRLPIPEYMMKAEKGTYNQVLSINQVFDILLHFAKTGDWVESLQVGIPQRKGWIPKATNNQS
The following text describes a protein:
Function:
Catalyzes the attachment of glycine to tRNA(Gly). Is also able produce diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice site.
Subcellular Localization:
Plastid, chloroplast. Mitochondrion.
Sequence:
MAILHFSLPLIVSFLRPHASPRFFLLPRSLSQSPFLSRRRFHRTSAVSSAAVHHQSYRNPDDDVTRAVSVPTFQQAIQRLQEYWASVGCAVMQPSNTEVGAGTMNPCTFLRVLGPEPWNVAYVEPSIRPDDSRYGENPNRLQRHTQFQVILKPDPGNSQQLFINSLSALGIDVTAHDIRFVEDNWESPVLGAWGLGWEIWMDGMEITQFTYFQQAGSLPLSPVSVEITYGLERIIMLLQEVDHFKKILYADGITYGELFLENEKEMSSYYLEHASVDRLQKHFDYFDEEARSLLALGLPIPAYDQLLKTSHAFNILDARGFIGVTERARYFGRMRSLARQCAQLWLATRESLGHPLGVASEPVPPVCHRAALEKVAEKVSEDPRSFIIEIGTEEMPPQDVINASEQLRVLVLELLENQRLRHGAVKAFGTPRRLVVLVDAMSSKQLEEEVEVRGPPASKAFDDEGNPTKAAEGFSRRYGVPLEKLYRKVSGKTEYVHARVTEPARLALEVLSEDLPGILAKISFPKSMRWNSSVMFSRPIRWVMALHGDLVVPFSFAGISSGNVSCGLRNTASASLLVQNAESYEDTMRNSGINIEIEERKKIILEKSNALAKSVSGRLVVPQNLLNEVANLVEAPVPLIGKFKESFLELPEELLTIVMQKHQKYFSIIDESGQLLPYFIAVANGAINEDVVKKGNEAVLRARYEDAKFFYEVDTRKRFSEFRDQLQGILFHEKLGTMLDKMNRLKKMVSKLCLALKIDEDLLPVVEDAASLAMSDLATAVVTEFTALSGIMARHYALRDGYSEQIAEALLEITLPRFSGDVIPKTDAGMVLAIGDRLDSLVGLFAAGCQPSSTNDPFGLRRISYGLVQILVEKDKNVNFKRVLELAASVQPTKVEANTVEDVYQFVTRRLEQLLVDNGVSPEVVRSVLAERGNNPCLAARTAYKTEKLSKGEMFPKIVEAYSRPTRIVRGKDVGVGVEVDENAFETPQERTLWSTYTSIKDRIHTGIEIEDFTEISMQLVEPLEDFFNNVFVMVEEERVRKNRLALLNNIANLPKGVIDLSFLPGF
The following text describes a protein:
Function:
One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit; Located at the polypeptide exit tunnel on the outside of the subunit.
Sequence:
MKPTKMRNKMIYRASYQTKSKQLGSALSKDLQKKYGKRSVRVNEGDSVTILRGEFKGVDGKVAEVSTAKSSVAIEGVKKEKTKGDKFDVFIHTSNLLVTSLNTEDKWRIAKLEGKDPRKQPKEAPKAAEKPAKEEPKKETPKAEEKPAKEEPKETKVEKKSEEKEDEN
The following text describes a protein:
Function:
Vacuolar Fe(2+) uptake transporter.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Domain:
The cytoplasmic metal binding domain (MBD) is located between transmembrane 2 (TM2) and transmembrane 3 (TM3).
Sequence:
MAAQNSRATIEPEKQTLLNHHKEKHFTAGEVVRDIIIGVSDGLTVPFALAAGLSGANASSSIVITAGIAEVAAGAISMGLGGYLAAKSEADHYTRELKREEEEIINVPDVEAAEVAEILAEYGVEPHEYAPVVNALRKRPQAWLDFMMKFELGLEKPDPRRALQSAFNIAVSYILGGLVPLLPYMFIPRAQDAVIASVVITIAALLIFGYAKGYFTGNKPVKNAFQTALIGAIASAAAFGIAKVIHP
The following text describes a protein:
Function:
Has a role in the control of cell polarity and cytokinesis. Involved in bipolar growth and septum formation.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Septum.
Sequence:
MDVGTMGSRAELLAISIQFGGLWVFRDLLQMNPLFEQDHVFCTFNHPNMGLVLISFAKVDGHILAAYALSKLGPDTFSICYPFSSKLDAFAQTLDLEWQIASMHKEAAACVYEFLCVESVCLHTGENWRESVIEPEYASYIFDTINVFQSSSLTRELYSLGEPNGVREFVVDAIFDIKVDNSWWEDPSNSYWKTVIGSREMFEDSRKKTSSPSPSFASSKDAGTIPAIQKKKSLLIEMMETESTYVERLRHLVNDYALPLRDLAKSSKKLLGLYELNTLFPPCLNKLIQLNSAFLDEFEAIMSDLNFEDIDEKKFEEIDLRLACCFESHFFAFSQHYPRYLEQSNDFGNVLKMASKIPKFVEFHDQVKLNANMNVGLSQLIMEPVQRIPRYSLFLDQIILLTQEGECQHTYVRSVEIIKNIAEMPTVDAEERSRIFAGLQHIIPDLAPNMISNSRNFIDCIDVTREFLKNGQLHLIPYTLILFNDRICLVQRRSKSSIASTILDLRKQNPRNSYSKEKRAQYIGSNMNEAVELTRSMVEENTIFLISKYASSPSFFNEYPILKFRCDFENVRTMDRFYQSFQKALSMNKSQPSCLSFSKLNDFVVFFNNYSRFEYEKESKRSDIVCICTNDANVDKHKFLQDGNIVITFFQQDEDFHLSFDSWLGVSLPTEAVIAKEDLREACLNYLINIKRLLLCPFSNRNFSSLDLYSNLIQHLLSANSSPRKSRLSFGGRPGSPSKISLSLNRFYNQGGLSKSCATLPSQMYNLDHNNISQKSLKFNTHNTSKASAEKTVEHLEAFKGGFKYHTDLKNLLYPLSEKEKIEGDELYDNILKETFNEELLSHYPPNIIYATFQKYLSSFINRKFGVLLSSSFIQQLNTVENLNLSFNSTDAVYHLKKILQDLPESSLKILENIFSIASDLLLRLPLKDQCDFVTKQLAIALAPSMFGSNAVELVYYLAYHSDRIFGTVEELPTPVSPANSNNDKQLDESKFQAIAMKEMPERHPKEILPGQIEREAYEDLRRKYHLTLARLAQMTRLNEDSKKSIPLLYDRFNHDLKLIKQSVQASLIRKQCELDTAKWTLEEYESKLNAKEGCQTNIFI
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). Catalyzes the ligation of CoA on propanoate to produce propanoyl-CoA. Can also use 2-methylpropanoate (isobutyric acid), acetate, butanoate, isovalerate, pentanoate, hexanoate, 2-methylbutanoate, 2-methylpentanoate, 3-methylpentanoate and 4-methylpentanoate as substrates with a lower efficiency. Triggers the formation of very short chain acyl-CoAs from the corresponding fatty acids, including acetic acid, propanoic acid, butyric acid and its isomer.
Subcellular Localization:
Cytoplasm, cytosol.
Domain:
Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity.
Sequence:
MGMVGRDIDDLPKNAANYTALTPLWFLERAATVHPTRTSVIHGSRHYTWLQTYHRCRQFASALNNHSIGLGSTVAVIAPNVPALYEAHFAVPMAGAVVNCVNIRLNASTIAFLLGHSSAAAVMVDQEFFSLAEEALKILAQESKSHYKPPLLVVIGDESCDPKTLEYALKTGAIEYEKFLEGGDPEFDWKPPEDEWQSISLGYTSGTTASPKGVVLSHRGAYLMSLSASVVWGINEGAIYLWTLPMFHCNGWCYTWGMAAFCGTNICLRQVTAKGVYSAIAKYGVTHFCAAPVVLNTIVNAPPEEAIIPLPHLVHVMTAGAAPPPSVLFAMSEKGFKVAHTYGLSETYGPSTICAWKPEWDSLPPIKQARLNARQGVRYIALEGLDVVDTKTMKPVPADGTTMGEIVMRGNAVMKGYLKNPKANEESFADGWFHSGDLAVKHPDGYIEIKDRSKDIIISGGENISSLEVENTLYLHPAVLEVSVVARPDERWGESPCAFVTLKPNIDKSNEQVLAEDIIKFCKSKMPAYWVPKSVVFGPLPKTATGKIQKHVLRAKAKEMGALKKSNL
The following text describes a protein:
Function:
Required for selective autophagy activation by ubiquitinated proteins. Implicated in sigma rhabdovirus multiplication and necessary for male fertility. Involved in activating transcription of Drs.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MPEKLLKITYQGAGPQKKINAYLRMPSQNYTILRREIELYLFQERQLPKCDVRTFWIDADKDEIEIVNQNDYEIFLAKCESNMHVQVAPLAPVEEPKATKQEGSSANAEAPSVDDPSNFTIHDAVECDGCGLAPLIGFRYKCVQCSNYDLCQKCELAHKHPEHLMLRMPTNNGPGMVDAWFTGPGLGRRSGRRSRGHCPFQETNQADPAGEPARDSRRERRQARRHAGVLTQFVEMMTNLPLNTTTATAPAEPQKPKAAEQTESPPQAEPTVTAEKAAESEAKPTEPKKVNTDQSVPRTEDPVTTPRSTQPTTPVINLDNISQIVPPEYMSAGIEILNNFSEMFSKIIDTTEGGDSGIFAPSTTPSAENKKPEEQGQSSGQSGASSANQSAVPSAAPSANQSNVPSANQSATPSISGSIPDAQLETEPLNPKPSETTTETEQERRRSDSLDPEWQLIDNAYSANNSNLINLDTTNPTAAPQEPVRDFGQLGELLRQHMNEEARVEQASANTQTAQVDTVSTSTSTTSVTTNSVGTSPAAPDDKRTVPVYHTDESINKSIHAMMAMGFSNEGAWLTQLLESVQGNISAALDVMNVSQNRN
The following text describes a protein:
Function:
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Subcellular Localization:
Cytoplasm.
Sequence:
MEVLHKPVLLRESVEFLTENGGKIYVDCTLGGGGHAKEILKKRKDIFLIGIDRDEEAIEIAKENLKEFEGRFSIYKANFKDLDLVLKEEGIDKVDGFLFDLGVSMYQLKGERGFTFQEDQPLDMRMDKEQTLTACKVVNNYPERELIRILKEYGEEKFAVRIAKAIVQRRKKKPIETTGELVDVILSVVPEYYKHGKIHPATRTFQAIRIEVNKELESLKEALEKTPYHFNSKGRLVVITFHSLEDRIVKHFIKEKEKEGIFRIITKKPVTPSEEEIRENPASRSAKLRVAEKI
The following text describes a protein:
Function:
Involved in the secondary cell wall (SCW) formation of vessel elements (e.g. protoxylem and metaxylem), thus promoting tracheary element (TE) differentiation.
Subcellular Localization:
Cell membrane; Single-pass membrane protein. Secreted, cell wall.
Sequence:
MATIFIVFVSFGCVFVLGIAAFVLCCLIKKWKCSKAIEKNEMVHVDQHLQVHENILQGPNGMKTVAITVDDDLHVHDEEECVKNEKLGTASTSKA
The following text describes a protein:
Function:
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Sequence:
MALFGAHVSSAGSILKTFKRAKDIGAEVFQFFLRSPRAWYWKGVDKETKQAFIEKLKDFKNPVMVHAPYLLNLASPNEELREKSVKVFLEELKFCDEVGIHFYNFHPGTAKGISDEEGLRNVIKSLEEVFSEYTPKFTTVLLENTAGERGDLGKNFKELKEIMNVFRGIKLGVCLDTCHAFAYGYEINTKEGFENFKREIEKMVGLESVKAVHANDSKVPLGGRKDRHEHIGKGYIGLEGFKNLLKDEYFSTLPYYIETPKENNMDPVNLSVLREIYQNNDL
The following text describes a protein:
Function:
Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP). It is essential for the degradation of carbohydrates via glycolysis.
Subcellular Localization:
Cytoplasm. Secreted. Cell surface. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface.
Sequence:
MQISDAWIRKVFTGRGDVTVEVELTVEDSVTGDVLVTRAAAPAGASRGAHEVLYFPEGGVDAALAAFEKLVAPEIVGLDVTEPYSTDGKLEEVDGTQRFEKIGGAVAIATSFAAAEAGAASLGVPLYSFIGGAYARRLPLPLGNVIGGGKHSRGLGPDIQEFLAMPLNPPDIYTAVYTNVEIHKRVLKYILKVDTSFTGGKNDEGAWTPRISSTTALKILREAAREVSGELGVEVGIGVDVAASSLWNGEKYVYKNEGVERDPREQFEFIAKLIEEYDLVYVEDPFHEEDFQSFAELRDRFKDRLIVGDDLFVTNPERIKKGGKIGAATGVIIKPDQIGTLLRAHQAVSAAREFGMRVIVSHRSGDTEYKTLAHIAVGFGAEVIKTGIMGGERTAKLNELIRIGDYLGKWATITQIRIH
The following text describes a protein:
Function:
Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MAAFDIFENSTDLDQNDTVGQNLTDDVNRSTATRLKQSVPVIALFGVSYFLIFALCVVGNTLVCFVVIKIPRMRTVTNYFILNLAVSDLLVGIFCMPATLADNVVMGKFTSPSISGFLLTLLTPLPYLHFSNKRSPLLGWPFGDVMCRLVPFMSTASVVASVFTLLAIAVDRFYAVVLPTKPKLKVTVMTKAVITIWMFAITVSLPLMIFNRDEIYEDVQQDATYLVHYCDEQWPTTGSWTKDDISKYYSFALFIICYLAPLSIILVLYMIIGYQVWYKSAPGQRASVEAQNALLKKKIKVIKMLIVVVVLFALFWLPLHTIMLLNDFTQLSASQKHVVYIYAFPIAHWLSYFNSSVNPIIYGYFNPNFRQGFKSLVISRRYANGLSEMSHTTRHEKD
The following text describes a protein:
Function:
Plays a critical role in the assembly of axonemal dynein complex, thereby playing a role in ciliary motility.
Subcellular Localization:
Cytoplasm, cytoskeleton, flagellum axoneme. Dynein axonemal particle.
Sequence:
VFDINGTDVTPRPLYHPDPLTGTAKPSKLLTSQEGSLGSEFISSYSLYQNTINPSTLGQFTRSVLGSSTVSKSSVSASESIAEDLEEPSYKRERLTSFTDLQVIRAAPEKIVTKEDLEKNIEIILTETETLRFFDLPTVMVSVESEEAEKVTQRNKNYEVLCRNRLGNDLYVERMMQTFNGAPKNKDVQCDKIIMEDKGIMSTAWDLYDSYNAMEIVSLSVKQSVVESSSKANVLPKDQDQRLPGSTTEKNIETSSLMDIENVILAKIHEDEEDHSDAILKSDKFHQDLFFMERVLMENIFQPKLAAYRQLPVLKEPEPEEPEDVLESAKHEEVEEESKKEEEEEIHAEESTIPANLERLWSFSCDLTKGLNVSSLAWNKTNPDLLAVGYGHFGFKEQKRGLACCWSIKNPMWPERIYQSPYGVTAVDFSIGAPNLLAVGYHNGTIAIYNVRSNSNVPVLDSSESPQKHLGPVWQLQWIEQDRGTTGDDKREILVSISADGRISKWVIRKGLDCYDLMRLKRTTAASNKKRGEKEKKDEALISRQAPGMCFAFHPKDTNIYLAGTEEGHIHKCSCSYNEQYLDTYRGHKGPVYKVTWNPFCHDVFLSCSADWGVIIWQQENVKPSLSFYPTTSVVYDVAWSPKSSYIFAAANENRVEIWDLHISTLDPLIVNTANPGIKFTTILFAKQTDCLLVGDTDGQVSVYELRNMPTVLETGRGDIMDTLLGSKSNQSA
The following text describes a protein:
Function:
Involved in membrane remodeling.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Sequence:
MEIKVDEGHQKGTKEDITRPLLEEDKDFPDIERTTWIQKAIGQTFQTTAHLANLLPTGTVLAFQLLSPIFSNGGQCDLVSKIMTSTLVAICGFSCFILSFTDSYKDKNGTICYGLATIHGFWIIDGSTTLPQELSKRYKLRFIDFVHAFMSLFVFGAVVLFDRNAVNCFFPSPSAEALEVLTALPVGVGVFSSMLFATFPTTRNGIGFPLSSK
The following text describes a protein:
Function:
Ligand for members of the frizzled family of seven transmembrane receptors.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MLPPAPSRLGLLLLLLLCPAHVGGLWWAVGSPLVMDPISICRKARRLAGRQAELCQAEPEVVAELARGARLGVRECQFQFRFRRWNCSSHSKAFGRILQQDIRETAFVFAITAAGASHAVTQACSMGELLQCGCQAPRGRAPPRPSGLPGTPGPPGPAGSPEGSSAWEWGGCGDDVDFGDEKSRLFMDARHKRGRGDIRALVQLHNNEAGRLAVRSHTRTECKCHGLSGSCALRTCWQKLPPFREVGARLLERFHGASRVMGTNDGKALLPAVRTLKPPGRADLLYAADSPDFCAPNRRTGSPGTRGRACNSSAPDLSGCDLLCCGRGHRQESVQLEENCLCRFHWCCVVQCHRCRVRKELSLCL
The following text describes a protein:
Function:
Interacts with the host phosphatase PP1 catalytic subunit (PPP1CB) and recruits it to dephosphorylate EIF2S1/eIF2alpha and therefore restores the host translation that has been shut-down by the host. Also inhibits the EIF2S1/eIF2alpha-ATF4-DDIT3/CHOP pathway.
Sequence:
MTLLTHQVPSSANMERAKASTVCAIPWTKNRPQNEVVKTAAFPCFMAKLVGTNGFKDSKNTPAPAANNRKQQLSQGRPAAPPEPAELRPSKVPAAAQPFGMCRWGRSSRADGGASDAVRPASSTASSPTITDRQPNHKKRSRRRRRPPKSSSKPTGEALESPPGHGVCIARSPTTKQEMILRVGTPPDAEIDEKALASPRPSVNSAIAFILGGNDDISDTGSDWDEVDAGEERSASDCPLDVFVMPLLNGLFSVSVRPRPTRISDEVDGVGLGAATSPHVRDANDRWNREYDADEQAQHRISKVNFGTGDAFMQVHDADDVDRRGPWEQMAIDRKRFQTRVASTEAVLAPVFSAEHRQRTFEKLHAASVD
The following text describes a protein:
Function:
Involved in transport of proteins into the mitochondrion.
Subcellular Localization:
Mitochondrion outer membrane.
Sequence:
MSSSGVITQLVTDALSMNAAQDWEDVSLFTPYLNDQALMYDFADCLAVQTFLRMTSLPFNVRQRPNVDFISPDGVVPLLKINKTLITGFNAIVDFVHKKGVTLTSHLSETQVADMRANISMIEHLLTTVEKFVLWNHDETYDKVTKLRYGSVYHWPLSSVLPFVKRRKILEELSDKDWDTKTMDEVGEQADKVFRALSAQLGSQKYLTGDLPTEADALLFGHMYTLITVR
The following text describes a protein:
Function:
Required for maturation of 30S ribosomal subunits.
Subcellular Localization:
Cytoplasm.
Sequence:
MTEPTVGSTDAELLAEPRLVVEPGVAARVSAVAGPVLQGMGYRLVRIRISGEAGCTVQIMAERPDGSMQIEDCEAISRALSPVLDVADPIDRAYRLEISSPGIDRPLVRRSDFERYAGHLVKVEMAVAHEGRKRFRGMIGAVEGDRVHLQRDDVKAGEERNVLLTMEDISEARLVLTDELIAESMRRGKAAAREMRRNLGLEPPAAPHAKISEKTTKNTKPKKKPAPTNTKKHRLAAERARRGEIEPDEGD
The following text describes a protein:
Function:
FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Oxidizes thioredoxin in vitro. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space, and can act independently of the oxidoreductase MIA40. Can oxidize the cytochrome c oxidase assembly protein COX19, a typical substrate of MIA40.
Sequence:
PVTREDLGRATWTFLHSLAAQYPDKPTRQQQKDVRELMAIISRMYPCKECADHFKEVLKSNPVRANSGVDLSQWMCRVHNIVNRSLGKPQFSCERVDARWGALHCDGACDVHGRLHSMKS
The following text describes a protein:
Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Sequence:
MKTNGFYWRNEGLSMFYDHELGISSVLERLDGKIPNSQGIRKKNIRILMNTIIGNLQSADFFLGQLNNNIMADQLLFGYWGIRGLGQSLRYYLEYLGLPYQDKRYVKPEEWFGEVAQAPLNNEVLVNLPYIKDGDKWIFESGALYVYLAHKANRADLLGSTPEEQVTLAQTKGVLQDLLKSFFTLITFSEEQYAAKKEEFFKTDILWLIEKLNAFLGGRQWAAGNNLTYVDFQLFEVEETLKAFNIDTFNAQANLKKHHDEFSNIAQIKAYLGSDKFIAGPFYPPGAFRWG
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. Mdm12 is required for the interaction of the ER-resident membrane protein mmm1 and the outer mitochondrial membrane-resident beta-barrel protein mdm10. The mdm12-mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The mdm10-mdm12-mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the mdm12-mmm1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Subcellular Localization:
Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. 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:
The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers.
Sequence:
MSIDFDWSKLDSELEAKVLHLLEGQVSNLSLPSYIKHLKVVDFHFGKVSPQITIQEIGDPDPQFYENEAFELANQELEGDQCSRNNVSPVLTDLPPYAAEHPFSRLAYFNPAFNSPGILSASGLTSPIPESRPSTPMDNHQERDRSNDFQVTAHVSYDGDANLSLEAVLSMNYPNSEFAVLPFKLSFIRISIDAIAVLAKMGKRTHLCFVDTLLHGTGEHASSVIRDLTVESIIGESNKQLLKNVAKVEKFVSEKVKRIIEDELVWPSYITIE
The following text describes a protein:
Function:
Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity; Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells.
Subcellular Localization:
Nucleus.
Sequence:
MESYFVDRKAVQVEDVFLDFLKSFTVDPNSRGPPYYSAEIDAMKASESSTIFIDFSHVMLFSDLLQSAISDEFLRFEPYLRNACKRFVMEQKPTFIADDNPHKDINIAFFNLPFAKRLRELTTAEIGKLVSVTGVVTRTSEVRPELLQGTFKCLDCGGVIRNVEQQFKYTEPSICVDPTCQNRMKWALLRQESKFADWQRVRMQETSKEIPAGSLPRSMDVILRHDIVEQARAGDTVIFTGTVVVIPDILALASPGERAECRKEASQRNPSSVGKEGVRGLRALGVRDLSYRLAFIANSVQIMDGRRDIDIRNRKKGADEDDNQQFMAEEIDEIQRMRNTPDFFNKLVNSIAPTVFGHQDIKRAILLMLVGGVHKVTHEGINLRGDVNVCIVGDPSCAKSQFLKYTSGIVPRSVYTSGKSSSAAGLTATVAKEPETGEFCIEAGALMLADNGICCIDEFDKMDIRDQVAIHEAMEQQTISITKAGIQATLNARTSILAAANPTGGRYDKSKPLKYNVALPPAILSRFDLVYVMIDDPDDEIDYHIAHHIVRVHQKREDAIVPAFNTAQLKRYIAYAKTLKPKLSSEARKVLVESYVALRRGDTTPGSRVAYRMTVRQLEALIRLSEAIARSYLETQVQPRHVDVARKLLKTSIISVESTEIDLSEFQDGNRDLGDSSGGNGPDPPAQDDAQPTDAALDTQFSNAKTGASSGDKQREKLVVSDEYFQRVTQALIMRLRQHEEAVTREGDGLVGMRQRDLIMWYVHQQFDENNDISEKEAASEIKKVKTIIESLIRREGYLIVLDDGVQAAAEGEGARQAVNRNDRILAVAPNYDHAAL
The following text describes a protein:
Function:
NADPH-dependent alpha,beta-unsaturated oxoene reductase reducing the double bond of medium-chain (C9) to long-chain (C18) reactive electrophile species deriving from poly-unsaturated fatty acid peroxides. The best substrates are 13-lipoxygenase-derived gamma-ketols, but is unable to reduce the double bond of short-chain alkenals and alkenones such as acrolein, crotonaldehyde, 3-buten-2-one, 4-hexen-3-one and trans-2-hexenal, or quinones such as duroquinone, decylubiquinone, coenzyme Q0, menadione, menaquinone and phylloquinone. Can use trans-2-nonenal, trans-3-decen-2-one, 4-hydroxynonenal, 12-oxo-10(E) dodecanoate (traumatin), 4-oxononenal, trans-1,3 diphenyl-2-propenone, trans-1,4-diphenyl-2-butene-1,4-dione, 9-oxo-12,13-epoxy-(10E)-octadecenoic acid (trans-EKODE-1b), 9-hydroxy-12-oxo-10(E)-octadecenoic acid, 9-Hydroxy-12-oxo-10(E),15(Z)-octadecadienoic acid and 9,13-dihydroxy-10-oxo-11-octadecenoic acid as substrates, but has no activity with 13(R,S)-hydroperoxy-9(Z),11(E)-octadecadienoic acid (13-HPOD), 9(S),12(S),13(S)-trihydroxy-10(E)-octadecenoic acid, 13-hydroxy-12-oxo-9(Z)-octadecenoic acid, 9-oxo-10(E),12(Z)-octadecadienoic acid (9-KODE), 13-oxo-9(Z),11(E)-octadecadienoic acid (13-KODE) and 12-oxo-10,15(Z)-phytodienoic acid (12-OPDA).
Miscellaneous:
MISCELLANEOUS: The trimeric TOC159/75/34 complex is not involved in chloroplast import of CEQORH.
Subcellular Localization:
Plastid, chloroplast inner membrane. Note=Faces the stroma side of the membrane. Targeting to the chloroplast inner membrane is mediated by HP30-1, HP30-2 and HP20.
Domain:
A nonterminal hydrophilic domain (59-100) is essential for targeting to the chloroplast. The C-terminal part (101-329) is necessary and sufficient to select for the import site.
Sequence:
MAGKLMHALQYNSYGGGAAGLEHVQVPVPTPKSNEVCLKLEATSLNPVDWKIQKGMIRPFLPRKFPCIPATDVAGEVVEVGSGVKNFKAGDKVVAVLSHLGGGGLAEFAVATEKLTVKRPQEVGAAEAAALPVAGLTALQALTNPAGLKLDGTGKKANILVTAASGGVGHYAVQLAKLANAHVTATCGARNIEFVKSLGADEVLDYKTPEGAALKSPSGKKYDAVVHCANGIPFSVFEPNLSENGKVIDITPGPNAMWTYAVKKITMSKKQLVPLLLIPKAENLEFMVNLVKEGKVKTVIDSKHPLSKAEDAWAKSIDGHATGKIIVEP
The following text describes a protein:
Function:
mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MAVTPHHRLYEFAKTALIKIFAFPYATVCDLYCDGGVDTDKWGDAQIGHYIGIDASASGVNDARELWESRKKLFTSEFIELDPSADDFEAQMQEKGIQADIVCCMQHLQLCFESEEHAQKLLNNVSSLLKPGGYFVGIIPDSSTIWTKYQKNVEASHNKGLKTVPNSIRSENYVITFEVEEEKFPFFGKKYQLKFANESMFENHCLVHFPSFMRLAREAGLEYVEIQNLTEFYDDNRTQFAPLLGGYGSSLVDPRGKLVARSFDILGLYSTFVFQKPDPDAMPPIVTPELHDPENDQEEEWLWTQQASMDDGRVSRTDILPPADNEKGILGPGPADMRL
The following text describes a protein:
Function:
Transcription factor. Involved in apical dominance. Represses the growth of axillary organs (e.g. lateral branches), but enables the formation of female inflorescences. Regulates the number and length of axillary branches.
Miscellaneous:
MISCELLANEOUS: TB1 is a major QTL of the evolution from the teosinte to the maize morphology.
Subcellular Localization:
Nucleus.
Sequence:
MFPFCDSSSPMDLPLYQQLQLSPSSPKTDQSSSFYCYPCSPPFAAADASFPLSYQIGSAAAADATPPQAVINSPDLPVQALMDHAPAPATELGACASGAEGSGASLDRAAAAARKDRHSKICTAGGMRDRRMRLSLDVARKFFALQDMLGFDKASKTVQWLLNTSKSAIQEIMADDASSECVEDGSSSLSVDGKHNPAEQLGGGGDQKPKGNCRGEGKKPAKASKAAATPKPPRKSANNAHQVPDKETRAKARERARERTKEKHRMRWVKLASAIDVEAAAASGPSDRPSSNNLSHHSSLSMNMPCAAAELEERERCSSALSNRSAGRMQEITGASDVVLGFGNGGGGYGDGGGNYYCQEQWELGGVVFQQNSRFY
The following text describes a protein:
Function:
An alpha subtype methylase that recognizes the double-stranded sequence 5'-GATC-3' and methylates A-2 on both strands (Probable). Although it shares sequence specificity with a number of type II restriction endonucleases and methylases, it is thought to act in methyl-directed mismatch repair, initiation of chromosome replication and gene expression. Genetic interactions among priB, dam, lexA, nagC, polA, rdgB, rdgB, rep and uup link the PriA-PriB replication restart pathway to DNA double-strand break repair.
Sequence:
MKKNRAFLKWAGGKYPLLDDIKRHLPKGECLVEPFVGAGSVFLNTDFSRYILADINSDLISLYNIVKMRTDEYVQAARELFVPETNCAEVYYQFREEFNKSQDPFRRAVLFLYLNRYGYNGLCRYNLRGEFNVPFGRYKKPYFPEAELYHFAEKAQNAFFYCESYADSMARADDASVVYCDPPYAPLSATANFTAYHTNSFTLEQQAHLAEIAEGLVERHIPVLISNHDTMLTREWYQRAKLHVVKVRRSISSNGGTRKKVDELLALYKPGVVSPAKK
The following text describes a protein:
Function:
Subunit of novel type of clathrin- or non-clathrin-associated protein coat involved in targeting proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system.
Subcellular Localization:
Endomembrane system.
Sequence:
MGSQGGFYQSKEFLDLVKSIGEARSKAEEDRIVLNEIETLKRRISEPDIPKRKMKEYIIRLVYVEMLGHDASFGYIHAVKMTHDDSLLVKRTGYLAVTLFLNEDHDLIILIVNTIQKDLKSDNYLVVCAALNAVCKLINEETIPAVLPQVVELLGHPKEAVRKKAIMALHRFYQKSPSSVSHLVSNFRKRLCDNDPGVMGATLCPLFDLITIDVNSYKDLVVSFVSILKQVAERRLPKAYDYHQMPAPFIQIKLLKILALLGSGDKQASENMYTVVGDLFRKCDSSSNIGNAVLYECICCVSSIYPNAKLLESAADVISRFLKSDSHNLKYMGIDALGRLIKISPDIAEQHQLAVIDCLEDPDDTLKRKTFELLYKMTKSTNVEVIVDRMIDYMISINDNHYKTEIASRCVELAEQFAPSNQWFIQTMNKVFEHAGDLVNIKVAHNLMRLIAEGFGEDDDSADSQLRSSAVESYLRILGEPKLPSVFLQVICWVLGEYGTADGKFSASYITGKLCDVAEAYSNDETVKAYAVTALMKIYAFEIAARRKVDLLPECQSLMEELLASHSTDLQQRAYELQAVIGLDAHAVECIMPSDASCEDIEVDKGLSFLNGYVEESIEKGAQPYIPESERSGMLNISNFRNQDHHEASSHGLRFEAYELPKPTVQSRIPPASLASTELVPVPEPTYLRESYQTPSVTSVSSDAGSSELKLRLDGVQKKWGKPTYAPATSTSNSTAQKTVNGVTQVEGASSTNSRTRETYDSRKPQVEISPEKQKLAASLFGGSSKTEKRPATGHKTSKASTHMVEKSHVPKSSMEVASEKTAPVQPPPDLLDLGEPTVTSIAPFVDPFKQLEGLLDPTQVGSAAATKSPDIMALYVDTPAGIHNKDDGDLLSGLSNPSVTNMPGGTTTTQQEQRSKGPNPKDSLEKDALVRQMGVNPSSQNPNLFRDLLG