lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Acts as an extracellular and cell wall-bound hemophore; scavenges host heme and hemoglobin from the environment and also serves as a cell wall receptor for both (Probable). At low hemin (Hn) and hemoglobin (Hb) concentrations adsorbs Hn/Hb and presumably directs it to membrane transporters (Probable). Soluble Hbp2 can probably pass Hn/Hb to cell wall-anchored Hbp2, and both forms can accept Hn/Hb from Hbp1. May be involved in crossing the digestive barrier in infected animals. Binds host hemin (Probable). Binds host hemoglobin with affinity in the nanomolar range.
Subcellular Localization:
Cell surface. Secreted, cell wall; Peptidoglycan-anchor. Secreted. Note=Most protein is secreted. Cell wall attachment is iron-regulated, only occurring when iron levels are low or fur is deleted. Cell wall-anchored protein localizes to one cell pole or laterally. Protein does not have to be cell wall-anchored for virulence. During exponential growth detected on the cell surface as a series of dots in a helical pattern, it is excluded from the septum. The helical pattern of InlA does not overlap with that of InlH, InlJ or Hbp2. Under iron-limiting conditions accumulates at the old cell pole.
Domain:
Each NEAT domain binds hemin, whereas only NEAT1 and NEAT3 bind hemoglobin.
Sequence:
MKKLWKKGLVAFLALTLIFQLIPGFASAADSRLKDGGEYQVQVNFYKDNTGKTTKESSEADKYIDHTATIKVENGQPYMYLTITNSTWWQTMAVSKNGTRPEKPAQADVYQDRYEDVQTVSTDAAKDTRVEKFKLSSLDDVIFSYMHIKVDAISYDHWYQVDLTIDPSTFKVISEPAVTTPVTLSDGIYTIPFVAKKANDDSNSSMQNYFNNPAWLKVKNGKKMVAMTVNDNKTVTALKTTLAGTLQDVKVVSEDKDANTRIVEFEVEDLNQPLAAHVNYEAPFNGSVYKGQADFRYVFDTAKATAASSYPGSDETPPVVNPGETNPPVTKPDPGTTNPPVTTPPTTPSKPAVVDPKNLLNNHTYSIDFDVFKDGTTETSMMESYVMKPALIKVENNQPYVYLTLTNSSWIKTFQYKVNGVWKDMEVVSGDINKNTRTVKYPVKDGTANTDVKTHVLIEDMPGFSYDHEYTVQVKLNAATIKDITGKDVTLKEPVKKDILNTGNVASNNNAGPKLAKPDFDDTNSVQKTASKTEKNAKTNDSSSMVWYITLFGASFLYLAYRLKRKRLS
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:
MISFSLPPPPPISSLNHHHRRLICQTNKSKSTMPVEFDFLGLERTQRQQEQQLPSDSKKLSSIRDLQNAASRLNPNFLKSIISQPTGPQPAPVSPSPVKTAPLTIFYNGTISYFEATAEVVANLMKMAEEGKIQLKHKQEIEQPQPPNQQQHQQQHQQQHQQQHHHQQQHQHQHQHQQRGILMERFNTDSNGDMPLYRKKSLQRFFEKRKERLTSAAPYPTSSYSSVGDVDEYVNQKLANKNKMEQSKSFSSSSSTTTPAGSLRG
The following text describes a protein:
Function:
Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis (By similarity).
Subcellular Localization:
Apical cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection. Cell projection, microvillus membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cell projection, microvillus. Note=Localization to the apical membrane of parietal cells depends on the interaction with PALS1. Microvillar peripheral membrane protein (cytoplasmic side). Localizes to cell extensions and peripheral processes of astrocytes (By similarity).
Domain:
Has three main structural domains: an N-terminal FERM domain, a central alpha-helical domain and a C-terminal actin-binding domain; The FERM domain is organized in a clover-shaped structure that comprises three subdomains identified as F1 (residues 2-82), F2 (residues 96-198), and F3 (residues 204-296). In the active form, the subdomain F3 adopts two mutually exclusive conformational isomers where a row of four phenylalanine side chains (Phe250, Phe255, Phe267 and Phe269) must point in the same direction. In the autoinhibited form, the F3 subdomain interacts with the C-terminal domain (residues 516-586) and stabilizes the structure, selecting only one possible arrangement of phenylalanine side chains. The FERM domain mediates binding to membrane lipids and signaling molecules; The central alpha-helical domain is composed of two alpha helices (residues 326-406 and 417-466) connected by a linker. It protrudes from the FERM domain forming a coiled coil structure where the linker can have either a loop or a helix conformation. The monomer is predicted to form an intra-molecular helix-loop-helix coiled coil structure. Whereas the dimer adopts an elongated dumbbell-shaped configuration where continuous alpha helices from each protomer are organized in a antiparallel coiled coil structure that connect FERM:C-terminal domain swapped complex at each end. The dimer is predicted to link actin filaments parallel to the plasma membrane; The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.
Sequence:
MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYVDNKGFPTWLKLDKKVSAQEVRKENPVQFKFRAKFYPEDVAEELIQDITQKLFFLQVKDGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEMHKSGYLSSERLIPQRVMDQHKLSRDQWEDRIQVWHAEHRGMLKDSAMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEQKTKRAEKELSEQIEKALQLEEERRRAQEEAERLEADRMAALRAKEELERQAQDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVNYHVQEGLQDEGAEPMGYSAELSSEGILDDRNEEKRITEAEKNERVQRQLLTLSNELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAM
The following text describes a protein:
Function:
Introduction of a cis double bond between carbons of the acyl chain.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MGECLFKLTHSIPQQKIEIFKSMDGWVENNILTLLKPVEKSWQPQDFLPDAASDGFDEQVKELRKRAKEIPDDYFVSLVGDMITEEALPTYQTLLNTLDGVRDETGASLTSWAIWTRAWTAEENRHGDLLNQYLYLPGRVDIRQRGQLSSPIGIQLGLPWNMGILSLAQICGTVASDEKRLEIAYNIIVEKLFEIDPDGTVVAFAEMMRKKITMPAHLMYDEHDLNLFEHFSAVAQRLGVYTSNDYADILEFLVDRWKVQELTGLSAEGRKAQEYVCLLAPRIRKVEERAQARSKRAPSIPFSWIFGREVKL
The following text describes a protein:
Function:
Acts as a GTPase-activating protein for RAB35. Together with RAB35 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes.
Subcellular Localization:
Cytoplasm. Membrane.
Sequence:
MSSIPSFNERVHYYKEALKPSSIDISIIQHLAEQGIPESHGLRACYWKILLRYLPLDRTQWEIHLKKSRNGYQDFINELMIDPYKGDSPPPKQEEFDHPLSVQTDSKWNEYWKDQNILIDIEKDVRRTFPSMHFFNYQQEDGKSIHYEALRRILFIYAKLNPGIKYVQGMNEILGHVYYIFATDPDQDCKKNAEADSFYCFTSLMSEIRDNFCKTLDRSDVGIISSIKKLNRILKDNDLELWTDLEDKKLNPQFYSFRWITLLLSQEFELPDVLRLWDALFSDPNRFDLLYFFCCSMLICVRDQILKSSFADSLKLLQAYPNTIDFHTIYSTALSLKNKTFKLNTENVLESGQSYAIRFFNPFASLSSPTSPNSSVNSNNSGRTSPNNSTVHDGGNNNNIISNDNNNNINNNNNNNNNHSVNTNNLKSENSITNSNSTSNSLLNKLKPSSGSSSPVTTTVLQSSIANNNNNNNINNNNNNNNNNNININNNNNNINSSSNNNNNTPTIPPNNSGNNNNNNNNNNNNNNNSNNNNNNNNNNNNNNNNNNNNNNNNNNNSNNNNINNNNNLNNNSNNNNNSTTPNNQSPSNQTPIIKGFFSKYFES
The following text describes a protein:
Function:
Catalyzes the cleavage of the interphenyl double bond (C alpha-C beta) of lignin-derived polyphenolic diaryl-propane type compounds (Stilbene).
Sequence:
MAHFPDTSGMTGVLRPLRIEGDILDLEVEGEIPAQLDGTFHRVHPDAQFPPRFEDDQFFNGDGMVSLFRFHDGKIDFRQRYAQTDKWKVERKAGKSLFGAYRNPLTDDASVQGMIRGTANTNVMVHAGKLYAMKEDSPCLIMDPLTLETEGYTNFDGKLKNQTFSAHAKIDPVTGNFCNFGYAATGLLTTDCSYFEIDPAGNLLFETEFQVPYYCMMHDYGLTEHYAIFHIVPCSPNWDRLKAGLPHFGFDTTLPVWLGVVPRGPGVTNKDVRWFKAPKTIFASHVMNAFEEGSKIHFDTPQAENNAFPFFPDIHGAPFDPVAARPYLHRWTVDLGSNSEDFAEVRQLTSWIDEFPRVDARYVGQPYRHGWGLVMDPEMEMEFARGRASGFKMNRIGHWDHATGKEDSWWCGPQSIIQEPCFVPRMADSAEGDGYIIALVDNLITNYSDLVVLDALNLKDGPIGRAKLPIRLRSGLHGNWADASKLPIAA
The following text describes a protein:
Function:
Ammonium transporter that mediates the excretion of ammonium. Controls ammonium homeostasis during growth and development. Ammonium has been shown to function as a morphogen at multiple steps during the development.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Endosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. Cytoplasmic vesicle, phagosome membrane; Multi-pass membrane protein.
Sequence:
MVAGEIIKGVAAEITNGSSSSVVQKYLDCANQVAPDPGNTTWVLLSTILVLGMMPALAFFEAGLLRSKNTLSIITQIMSGIVVLTVMWQAFGYSLTFGPDQKGIIGNLDHAFLINVSYDDCSPNAPNIPAAAYAFFMMMFANITPLLMTGAFAERVKFKAFIALTVAWEIIVFYPVAHWIWGGGWLHKYFGVLDFAGGIVIHTSAGVSALVIALYVGRRKDFEKYGGEFPPSNLPLATIGAALLWMGWFGFNAGSALAAGNIATSAVASTQIGGSFSAIVWIILSAAKGKPNTVSVINGVIAGLAGITPASGYINSQYSIGLGICLGLASYYSVVLLKHKLHIDDALDVSSVHGLTGIIGSLAIGFCAELSVNPNGANGAFYGNPKLIGTQLLGVVSVAVWAAAWTWVLLKIIDATIGVKIDESEEELGLDLVEHGEFAYHNISLQGNENHYSSVINSHDFFK
The following text describes a protein:
Function:
Putative E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation; As part of the PRC1-like complex, repress class I KNOX gene expression. PcG PRC1 complex maintains the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility.
Subcellular Localization:
Nucleus.
Domain:
The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.
Sequence:
MPSLKSFSAAEEEDDQLGRNSEAERFNPEAVEKEEDPDKMDEKDESGDEEDDVKRDQVEAEDEEALGEEEDSKERSQSSSAGELSESEYMVVDLADICKDVQCSICLGIIRKTRTVMECLHRFCRECIDKSMRLGNNECPTCRKHCASRRSLRDDPNFDALIAALFKNIDKFEEEELNFRQDDEARNKQIQASIAQVSQRQSKALVKRKSVGKGTAILSRSRRSGGGSRRRRNCRNIEQDTSEANDDDDQNKRGKDSSSDEPCERQRKKRSATQPSSSNANNNDNCAGNGTEQTHQRDSRVISPVLVWNSELIAWGRGGTRSNTRQGNNNQGAISKRNARLKRLVEYLGSLEGNSVELDIHLKLVSLDTEGLLNLHEPYLCFRPTLLVKQLREYVARHLKLKAEEVELLVSKDGDTVIGNKTSTEKMQSLQDDETVAKLKVDCISSNGYMIVVYRRKQIA
The following text describes a protein:
Function:
Structural component of the gap junctions.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Cell junction, gap junction.
Sequence:
MLGFFGPLYEQLVGMLRKQQGQLAFDTIDRVNAWFTPFVLVAMTLAISCKQYFGQPIKCWTPREFSGSWDGYVHDFCFIENTYFVPNGTEVTDEARGGRHINYYRWVPLVLLFQAAMFVLPYHLWNLFHKRTTINLKGSLRFFEGALKKLEPAQACESFAGEIWNRLSDIRNSSNKLYGFQATINYFLLKLGFIVNCILQMVLLKHFLDVDDYFWGFFHLWNVEFKGTAEKEDSIFPRIVLCDFKVRNLGQQHQHTVSCIMILNMIIEKLYICFYFWLIFVFVVTTAGMIHFAFQILFRRHSLIPTNLNNKNKMNPTRSHEFIKDYLNFDGCLLLTYVDAQFGAFRTSQVIDGLVHRFTNELDSDSSAVTSLNEDHPERYVAFNTDTIPMDRYARKHHSLIEEVDGPSAPPANEEKKEI
The following text describes a protein:
Function:
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Subcellular Localization:
Cytoplasm. Mitochondrion intermembrane space.
Domain:
The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation; The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine. It is required for correct assembly of the 2 Fe-S clusters; The twin Cx2C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space.
Sequence:
MSISIIPPEVVSRLKDATVLILWGPGSSPEDVQKFSQELSSQQCNRVVVEHFERLVVSGHPKSTFSVVLSNLFEPHTTSHSFDLLSEVIRIMKPSGIVCGKELTDLKISANLKLAGFCNITVDSSNSIFSAQTQNFEVGSSSKLSFAKPSVWTLSDALIDDQVELINEDDLLDESDLIKPDAESLRVCGTTGKRKACKDCSCGLAEELGAGQAVKTTTTSATSSCGSCYLGDAFRCASCPYLGMPAFKPGEKIQLSERQLNPDL
The following text describes a protein:
Function:
May be involved in the reorganization of actin cytoskeleton mediated by RND1, RND2 and RND3. Promotes RHOA activation mediated by GNA12 and GNA13.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MFYAGIDKNKNEFQIKNAQQEQQGTPVQSNRKAQGSDQPKPVSAKPPKVLKDAGSKAINYPQITHDILDQQTANLILKDLPIGQPSQQFDAVEALLNQHKIQNQSPIRSSQKDSGNSKDLNSAMARRLADVEKLAQNQKLELKEKYNIIEQLREKVQELTEINRKLGSGDKQAYMNEINNLKEEKQKQQKKIEDMEKFLQKYGVKWVGDKISDEDDKKMKQMASDMKQMKPLFNYHLPKEISIDVIKRRIEELNYIMEKDGANQIVKNANGMHQFQKMEPLPIGFYRNGIAMKGHKFFSYGSNDAYQILADILEGYFPYQLKQQFPNGTPLKLIDKTEEVYEAKADDKKQCGYEDLAEKQLKPMKKEQFLEQLPECVIKNGKIIPIRSDIEKRLSGQPNLNATQQLRSAGCRQDPIDGNWIVDTEAQRRVDNGEDLEDVCTLKFRTETGKYSLIALMFGNQRICDMYQLVSGLKEYQDRNIQIILNFPRTVFQKDDQTTLEEAGLMPSAQLFFNLI
The following text describes a protein:
Function:
Mutarotase that catalyzes the interconversion of beta-D-galactose and alpha-D-galactose during galactose metabolism. Beta-D-galactose is metabolized in the liver into glucose 1-phosphate, the primary metabolic fuel, by the action of four enzymes that constitute the Leloir pathway: GALM, GALK1 (galactokinase), GALT (galactose-1-phosphate uridylyltransferase) and GALE (UDP-galactose-4'-epimerase). Involved in the maintenance of the equilibrium between the beta- and alpha-anomers of galactose, therefore ensuring a sufficient supply of the alpha-anomer for GALK1. Also active on D-glucose although shows a preference for galactose over glucose.
Subcellular Localization:
Cytoplasm.
Sequence:
MVKVVEDIFGIATNPFTKQAQVIRRYTMTNTNRLSVAIIQLGATIQSIQVPDAYHQLSDVVLGFDDVAGYTKYRNYHFGCTIGRVSDVVGNGEFIMDERRVVVSKNLGQKHQTNGGFVGFDQVIWDLEMKRPDGVTLRHISPDGHEGYPGTLKVLLHFTINDDNRFFIQIEATTNQTTPVNISNHIIFNLAGQSTGIKGIFDHQINIEAIETMETSNGDGLPTGRFKNVNDSVYDIRLPVFMGDRVRQFEKKPVKGYDVCFALDKEFDAIRTRYVGRFLHPDSGRFMEIFSNQPCVKFTTGNCFPQEPLGEPPILGKKCTRYWQHCGFSLQLLNYPDAVNQPDFPRIFINPGEHYFHETIYHFGVQESWKCCADPEELEALGEEPLRKPKAV
The following text describes a protein:
Function:
An odorant receptor which affects chemotaxis to the volatile odorant diacetyl. Specifies AWA neuronal cell fate via the odr-7 pathway.
Subcellular Localization:
Cell projection, cilium membrane; Multi-pass membrane protein.
Sequence:
MATLGEVQALVQKVCAPLALAINILLIYLILRHSPKSLGFYKYLMIYIALFEMIYAIVDIISAPDLYCFDSMFLVITFYENSSLPRWIYKVINVVFCTFFAVSMAIFALHFIYRYLAVSGSSYVKSYSFGKSFVWFFSPILYGIFYATAIEFTLSENEKTNMVLRKTYLSNRTLKVENLIYIGQNYWFTDEKGNVAINLMSWFGIAVPIFTVILSSSTMLIFGTLSYRAVASFAKNTSNSKQYHSMQLQLLNALVLQALIPVFLMQLPSFIAFTSPIFHKGNEMAGAVLGIAVALYPVLDPLPTLIIIKNFRNALFKPCTRKKIYAVQQETPIATTSQSVKIVKSI
The following text describes a protein:
Function:
Functions as a two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction.
Subcellular Localization:
Cytoplasm, cytosol. Nucleus.
Domain:
Histidine-containing phosphotransfer domain (HPt) contains an active histidine that mediates the phosphotransfer.
Sequence:
MESSDEMHSKIITMKQSFFDEGFLIPTQFQELELLQDRDNMNFVRDVFCLFFTDMTRQFSEIEQILREEIDGQPREDMNRLLQRLKGSVLSIGALKILNGVNKMIQLFEEGNLERIMAAFEQVKMESVNLRAKVEPYFQLLESQAESFTESQAPK
The following text describes a protein:
Function:
Receptor for basic fibroblast growth factor.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MRYKNRKFCYSGSAQCDETLRSPAGEISSPGYPGDYPPRVDYTWCVNVEGATGIDVSFLGEFHIELNEDGDGTVTCKDGVEVGQGGRPVPGHHRRLLWEQHPASTEGGHRADVELDVCYSSPCTNGATCLPNLTTYTYTCHCSPGWEGTNCELVAPGALTIETSPPSPSTEEQLNLTCWATGWGFTPNISWYIVDEDSPVDAGLGEQQDTQESDSSFTSIRTLTFTPTKGDNGVTYRCVASHPALAMDVETLMTLNVRYPAEIITPPSITTRVTEGQSVTISCPADGNPGNFIYTWREGGRVIDPSTEHQYDIDNGVLNITSATSDLQGTAYSCEVSNNIGFTPAKASTVLIVDFSAESLNGGGNPTTTIIIVVVVCVVVIIAVVVAAVSILRRAMVSRERQNDAPTGVALEQIPTSSEDGYQSLRLPQGQKSAQPYQGLAVPGDSQRQSTTDVVYEDVKTSSEFPRNQLALREKLGQGEFGNVFRAEAWNISDHQGTTIVAVKTLKAATRDAAQPAFFKELEVLEVLGSHPNVVSFLGCCTDKEPFYLLLEFVPGGTLQSNLRSSRAPQTHSNLHGESKSLSSQDLTKFAWDVAKGMVFLSSKKILHRDLATRNVLVAADKTCKVSDFGISREGEEYERTAHVRLPIRWMAPESLFQRMYTSKSDVWSFGVLLWEIVTLGATPYSGMSSRQVMGHVKHGYRMEKPPHCDGKLYSIMAACWEEQPTERPSFQQLELSLEALMGGGYINLASFDETTYANLQTSGEERC
The following text describes a protein:
Function:
Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
Sequence:
MKKIYIAPIAGVTDYTFRGILEDFKPDLIFTEMVSVNALSVLNDKTISKILKLREGNAVQIFGEDIEKIKASVKYIENLGVKHINLNCGCPMKKIVNCGYGAALVKEPEKIKKILSEIKSVLNNDTKLSVKIRIGYKEPENYIQIGKIAEELGCDHITVHGRTREQLYSGKADWKYIKEVKDNISIPVIGNGDIFTGEDALEKIFYSNVDGVMLARGIFGNPWLIRDIREILEYGEIKTPTTKTDKINMAIEHLKRIRVDNDNKFVFDVRKYISWYLKGIENCAEAKRKINIISDYDEIIKILEEML
The following text describes a protein:
Function:
Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication-dependent histone mRNA degradation.
Sequence:
MASVCEICGVKLESESSKAAHYQGRKHRRLAQEIRRRQEVAKRSIFVRNFNQCTDLADEFRSFFGKYGEIVAVHSDKEKVVLLKDIRIISIVFKSLPVFAIIEFLKEESAKEVLRISQSLPEFHGRKLVIKERTADIIKGNVQKKSKEQKKVKKSLQQLSNELLERLQIDDSDTLEQQLISVMQQRELTDNDNRLRRLVCDLLQQCFVELDESVKIVPFGSAVNGFGQASGDLDIAMIMDENAITDKGFCETSTDINIEDEKVTIRRPWSTFSVVAKFIKECIPGCLDVIALSNAREPVIKFKYNECSLCCDLTINNRLGIANSQLLQEYSKLDPRVKPLVFTIRTWAYCRGITLNSGGQFTSYSLILMIIYFLQCTKPSVLPSLQTLFREQNRLILTFSYVWLISVMTGIWDCSFLSCKNATTVFKTVSIEATPSLLHKFFCFYATLFDYDQCVISVKNGLPVTFDEIVRDIAGNDVLVKAMKNFKTTPICVQDPLLLNHNTTQNVNKDGLHRFQREARVAMNNCIKILTAQSAAKDSFSRANITLKELFSPAKYKDLLAKNSFVLSVVDNFNYLSDALSDTSRLLECEDKASKQYLLTVINYFYLLKRLKVELDVDCIYNREIIKYLRHSLLTDSANGTTISVIVTEIEKLFDSKNLTCIDSCVSQPDCRDEDILVHPPAKKAKVEYEEKVIVERKFPRLFAHCKANRNTWTGRRQKRRLQERLTTSEAYFKEQPHEETVDDEKNFDIHAKEDEVDKSDGIKCLNEKEASLFSFTVMVESRQKDTMEIIAQFDLMEWESVQSFQSFYAYIKKLLQLNC
The following text describes a protein:
Function:
Reversible hydration of carbon dioxide.
Sequence:
MSALCLSLLLACQPVVFARGYAQEDAAGSWHPNEVSYDETEVKGGRSKQQSWSYTLSDALGPPNWPIVAPACGGQFQSPININTSRAIRVNRKVPLEIVGLRNRPTCITAENEGYSVKFTPKWGFRTRPMMRGGPLKTAYFFEQMHFHWGPNNSEGSEHRINGERFPLEVHLVFYNGLYQSLAEAAGEVDGLAVVGFFYDVVPGSSSFSFNSWSNFLPQVRQPGAKFEISPTRSFSLQDVVGAMGWSYYSYDGSLTTPPCLETVNWIVSNKRLSATELDMSRLRSLITKQGKQMVLNYRSPQPQNTRRVFFY
The following text describes a protein:
Function:
Non-receptor tyrosine-protein kinase which plays a role in morphogenesis by regulating the epidermal enclosure of the embryo, independently of its kinase activity. Prevents hyperactivation of the Wnt signaling pathway during endoderm development, probably by preventing hmp-2 nuclear translocation.
Subcellular Localization:
Nucleus. Cytoplasm. Cell junction. Cell membrane; Peripheral membrane protein. Note=Localizes to the nucleus during cell division in the early embryo and in seam cells and in the developing germline at the larval stage. Localizes in the cytoplasm and at the cell-cell contacts during embryo enclosure and elongation. Nuclear exclusion during elongation is regulated by integrin alpha subunit pat-3 and beta-catenin hmp-2.
Sequence:
MGTVEKSSNNDASVTDDIRSAEYYHGMVPRQDAEGFLKREGDFLVRKTEQMPGKVVLAMSVRVTDELCRHFMLNMDPTSNKFYFEHTHQESTISELINWHMTTKTPISAASGAKIRRPMERSPWLINHDSIVANKKLGEGAFGDVFIAELDQGGKQEVAVKTMRAEATREARLRFMKEARLMRKYQHKHVVKLIGVAIHEHPLMIVMEYCPNGSLLSHLKKNKVSLIEKLRFTTEAADGIAYLERSKCIHRDIAARNCLLSAKNELKISDFGMSDNKDEIKDETLEKVPIKWLAPETMQEKVYTHKTDIWTFGVLVWEIYSDGAEPYPGLTKIQTRAKIVVNDYRMKMPDGTHPTVADVVTGTCWQKNPEKRSTMDSIHKKLREFYESKK
The following text describes a protein:
Function:
Catalyzes the oxidation of D-arabinose, L-xylose, L-fucose and L-galactose in the presence of NADP(+).
Miscellaneous:
MISCELLANEOUS: Present with 30200 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MSSSVASTENIVENMLHPKTTEIYFSLNNGVRIPALGLGTANPHEKLAETKQAVKAAIKAGYRHIDTAWAYETEPFVGEAIKELLEDGSIKREDLFITTKVWPVLWDEVDRSLNESLKALGLEYVDLLLQHWPLCFEKIKDPKGISGLVKTPVDDSGKTMYAADGDYLETYKQLEKIYLDPNDHRVRAIGVSNFSIEYLERLIKECRVKPTVNQVETHPHLPQMELRKFCFMHDILLTAYSPLGSHGAPNLKIPLVKKLAEKYNVTGNDLLISYHIRQGTIVIPRSLNPVRISSSIEFASLTKDELQELNDFGEKYPVRFIDEPFAAILPEFTGNGPNLDNLKY
The following text describes a protein:
Function:
Cytokine that stimulates the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells and induces megakaryocyte maturation resulting in increased platelet production. Also promotes the proliferation of hepatocytes in response to liver damage. Binding to its receptor formed by IL6ST and IL11RA activates a signaling cascade that promotes cell proliferation. Signaling leads to the activation of intracellular protein kinases and the phosphorylation of STAT3. The interaction with the membrane-bound IL11RA and IL6ST stimulates 'classic signaling', whereas the binding of IL11 and soluble IL11RA to IL6ST stimulates 'trans-signaling'.
Subcellular Localization:
Secreted.
Sequence:
MNCVCRLVLVVLSLWPDTAVAPGPPPGSPRASPDPRAELDSTVLLTRSLLEDTRQLTIQLKDKFPADGDHNLDSLPTLAMSAGALGALQLPSVLTRLRADLLSYLRHVQWLRRAMGSSLKTLEPELGTLQTRLDRLLRRLQLLMSRLALPQLPPDPPAPPLAPPSSTWGGIRAAHAILGGLHLTLDWAVRGLLLLKTRL
The following text describes a protein:
Function:
The M protein has a crucial role in virus assembly and interacts with the RNP complex as well as with the viral membrane. Associates with phosphatidylserine (PS) and phosphatidylinositol 4,5-bisphosphate (PIP2) at the plasma membrane. Interaction with PIP2 triggers matrix protein lattice polymerization. Matrix proteins induce host membrane deformation and curvature necessary for virion assembly/budding.
Subcellular Localization:
Virion. Host cell membrane.
Sequence:
MTEIYDFDKSAWDIKGSIAPIQPTTYSDGRLVPQVRVIDPGLGDRKDECFMYMFLLGVVEDSDPLGPPIGRAFGSLPLGVGRSTAKPEKLLKEATELDIVVRRTAGLNEKLVFYNNTPLTLLTPWRKVLTTGSVFNANQVCSAVNLIPLDTPQRFRVVYMSITRLSDNGYYTVPRRMLEFRSVNAVAFNLLVTLRIDKAIGPGKIIDNTEQLPEATFMVHIGNFRRKKSEVYSADYCKMKIEKMGLVFALGGIGGTSLHIRSTGKMSKTLHAQLGFKKTLCYPLMDINEDLNRLLWRSRCKIVRIQAVLQPSVPQEFRIYDDVIINDDQGLFKVL
The following text describes a protein:
Function:
Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSRIVVNFMHGRGFIFNAEDYLKLRFEYRIVGNLIGVPVSHPRNVNQQGMPVALSAYEVKLLLDKEIITLVDKTGALQRVPSDEQSQQYGAMVEQQKQEMHMPVVEKRLEAFRKHMPRIIEGKRRKLLKSGVKEEDIHLDPEELLDQEKKRIMQEKFDQMVQIPLKYPLTLEFSECSIALSAQEDVKYRVFKSLWQQGGFITTGDAFGCDFLLYPGDPMCFHASHTVHVLAEGVSRKLDAKYLIRICRLSVVVNKLCVIAYVDESSDEVHFETLEWEGNVTNKGDTF
The following text describes a protein:
Function:
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Sequence:
MLGSWFLFIVYRTPVNEDFADGYPSDEKWHGYINNSDRVLLKVIYYSSPTSAGAECIDPDCTWVEQWVHRAGPREKIYFKPETVNAAIVTCGGLCPGLNDVIRQIVITLEIYGVKNIVGIPFGYRGFSEEIAEMPLSRKVVQNIHLSGGSLLGVSRGGPSVAEIVDSMEKRGINMLFVLGGNGTHAGANAIHNECRKRRMKVAIVGVPKTIDNDILHMDKTFGFDTAVEESQRAINSAYIEAHSAYRGIGIVKLMGRSSGFITMQASLASGQIDICXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTDCLILIPKVKIHFEILCYFDADKTNKKIILLLSMQNFLEKTNATDASGNIVFGDIGVHIQQETKKYFKATGNPADVKYIDPTYMIRACRANASDGILCTVLGQNAVHGAFAGYSGITVGICNTHYVYLPIPEVVSYPRVVDPNSRMWHRCLTSTGQPDFV