lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Sequence:
MHPDTRSQPFAPLFDDVIVLTGPTASGKTELALRVAETLAARTNGRQEIEILSLDAIAVYRGMDIGSAKPTSDQLARAPHHLIDLVDPWDEFSVAEYLHSAHACVQDILERSKRPMFVGGTPMYLKGVLRGFDAGPPADEAFRNAVEEDLRQHGIGALRERLHQVDPLSAAKIDRGDSRRMIRALEFARATGTPISHRQLQFDTARSSHEGLVFALRVPRPVLHQRIEKRVEEMFAEGLVAEVQGLLALEQPLSKTSRQAVGYREIIEAIAAGDAPETAAERVVFHTRRLARRQETWLRSFSEIRGLGSFESDSAPDIDQCVESMVETILSFSD
The following text describes a protein:
Function:
Peptidoglycan polymerase that is essential for cell wall elongation. Also required for the maintenance of the rod cell shape.
Miscellaneous:
MISCELLANEOUS: Increased expression mediated by SigM is both necessary and sufficient to confer intrinsic resistance to moenomycin and viability to cells lacking aPBPs.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSRYKKQQSPFYQGDLIFIFGVFFIISVVSIYAAGQFGQYGNTDWIQQIVFYLLGAVAITVLLYFDLEQLEKLSLYIFIIGILSLIILKISPESIAPVIKGAKSWFRIGRITIQPSEFMKVGLIMMLASVIGKANPKGVRTLRDDIHLLLKIAGVAVIPVGLILMQDAGTAGICMFIVLVMVFMSGINWKLIAIIAGSGILLISLILLVMINFPDVAKSVGIQDYQIKRVTSWVSASNETQEDSNDSWQVDQAIMAIGSGGILGNGISNLKVYVPESTTDFIFSIIGESFGFIGCAIVVIMFFFLIYRLVVLIDKIHPFNRFASFFCVGYTALIVIHTFQNIGMNIGIMPVTGIPLLFVSYGGSSTLSTLIGFGIVYNASVQLTKYRSYLFNS
The following text describes a protein:
Function:
May form proteinaceous networks during the construction of the eggshell which then may control the deposition of the mineral phase.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix. Note=Eggshell matrix. Mostly in the mammillary bodies.
Sequence:
DPDGCGPGWVPTPGGCLGFFSRELSWSRAESFCRRWGPGSHLAAVRSAAELRLLAELLNASRGGDGSGEGADGRVWIGLHRPAGSRSWRWSDGTAPRFASWHRTAKARRGGRCAALRDEEAFTSWAARPCTERNAFVCKAAA
The following text describes a protein:
Function:
Promotes the exchange of Ras-bound GDP by GTP.
Sequence:
MKSMSSGGINKLFEGSLSKDGKTSRIEHQKIKQSGCPLLIKLMKDNGHITNVIIKSCRLKVLPGEISSLGGHLKKLHIEDNKIQEIPNLEQLEQLEELILPNNDIAKFQVSISKLTTLRLLDLSGNQLGTIPVRLFSLVSMRELYLDENQFSNFPSHLCELQKLTTLGFSNNLLKSIPTQIGQMIGLKKLILSGNQMESIPMEISNLKSLTHLDCSSNILSSIPNELGNKLSQLSFLFLQHNKLRSIPDEIGQCQSLVSLRLNNNSITLLPQSIGELENLQELYLQENRLNTLPSELGNCCSLKKLYLEFNKLIALPDRFKRLHCLNVLSLHDNLLDDLPNFLSLEFSQHLIRFTIHNNPFLRENGIDVIDSLQFLNSHLLSIQNFINNHDQQNDNSNNNNNNNNTTTTTTTTTTTTTTSTTNNNNTLFTDSYLSSASSSSFLNKSPSGLSLVGSFNGTIKKSISNSSNMNGSGSNGVGHGSGLTPKLNFKSLITSRDFSSDSDSDTDSTSSFSTYSSSTINTKRASISPRTSLTLSNSASNDSVSAVANGNGNNNNNNNNNNNNNNNSNNNNSGLVNSISSFSLSSGQINYYNISRARRGTHGNDQPHQTISPSTSTEKLQQTVSTPRQQSFFISVLNRRKSSLNNSQNGNNSNNNSNNNNNNSNNNISSLSSSNFANSLYNPLMSSSPTSSPSSSYSNLHSSFNGTSTPPFSSPSQSSPLSNSINGIHCNYSNNNNNNNNSNNNNNNNNNNNINNNNNNSNNNNNINTNGNNNSFNGIIMGSPIYKSFQSLYETLLDDLDYSKKRREELLNLSVEEKWIFLQRIKPDCTNSLVSNGVYQLQHQISSNDLKTLISSPPKLNSSQQLLSSSSSSSSLSSSSTSATHSLQNKSLPSISVCPKSPRTHMKVLSASSLFTLEDITKLRQQLVSKPVSWVINFAESTGIVSILSMITTYSQNLINNVNKDQPQSQPQPQPQPQPRPQPQQPQPQQPQPQQLLPLLSQLQPQQQQQQQQQTQQPQPQLQAQTKSDDHFIINECLGCIKLLVELEMQSLLLNDTAEIIFPLILSSQVSTKRMTFEVLELICKIFSLGSTIVLESIKNYSKKINEPLTKVFSHITSPLDSEYPADLKVSCMSLINHLIGSNHLSLEARIETRSKFLSNDILLIIKNLRIDGEGIETSSWKQLELEMKQFESMMVQDDNQTSNAEANELVSNELSQSIDNNNNNNNNNNNNSSTNLVNNNNNNNINSNCNSIINGGNSSDSLINNSVGTGVGSIMGVGSFMGVNEIEYDSPRKEFDELKSSNNNNSNSNSVNNFINNITEPIMPLTPTEGKLVVIVSMQQTRQQAQLQQQLQQQLEEEDDDEVPLSSSVATTASTTANTTLIEPNHLPIQTREVIVSVQRKSQAGDVIRSLLASNSNLKELGEWGLFVNDSNSNNNNNNNNNNNNKLSTNVIGRFLKDDEYIFDQMTTSSTSGSLSSDDGATPRLMTRSIPRFKEYRLKMIPWKVRVSLEKVKEMGLVLNANNTANGQFNESKFIAEAPMDPTMTCTGLVYHLIKKYLPNVNDRYCLEADDFGLYLDTNAGGLMWGGGTGGGYWLEPLEKLHDYEIFKDPKSTVALKLRPKGVKLKFADGTYEIFRLDLMSPTEKIFQEISEKVIDSNNNINLSYYGIFVDRQQGGANGNGISDSPILVSQSSSTSLIEESKKQRKPEWLEKGLPLYHYKINSRCCLRFALRPSNITLLIDISLFKSFQQQQQQQQQQQQQSTSSSSSSSSSSSVSSNNNSTNNSNNLIGSLNNSINTISELDESIDDNGLSSSSSDKEDQISTPSTSNLLSKFQQVDESISNLKFQLPQPIQSKQIIVQLPLHLPLGEALETDENWIETGIEREKCSFHFDSFDGILMNQTQPLNTQNFTEKNRICVLMADELEINSEQTNHNKTNIWDEPFDSSTIICDPDNPGQIRAATLNKLLEQATNNIEKDRELMNILLMTYMSFATSDILLDKLVERYNVPEHEKEQKSVVQLHTIVFLKNWLEQQAPQAASGGGLEEKFLVRLSEFVDKQISLDGYTKIVPQLKKWIDSALKEKRAYAMPEAARPNQLTTKLPSLTSSLLDDELFVAQQLTLREYETFKRIQAVEFLGQAWGKPKLQYKAPNLLKMIERFNKISTGVSTAILSQPKIKTRVKLICRFIKIAQHCRDLNNYHLLTAFMAGIRNSNVVRLRLSWAKVPKKHLHILEDLEKIMSMEGSFKEFRTKMAETIPPCIPYLGVYLKDLTFIEEGNPDSINSLINWGKKKLIYNIISIIQRCQQVSYDFGNQNQSQVAQKSDLVLNYFDSLPIALDELLYKISLNLEPRSNFNN
The following text describes a protein:
Function:
Responsible for the origin of replication (oriP) dependent replication and maintenance of viral episomes during latent infection. EBNA1 dimer interacts with the DS (dyad symmetry) element within the origin of replication oriP and with a host mitotic chromosome to initiate viral DNA replication during latency. EBNA1 binding to DS recruits the host origin recognition complex (ORC). Governs the faithful mitotic segregation of the viral episomes by binding both the FR (family of repeats) element within oriP and the host mitotic chromosomes. Forms a cell cycle-dependent tyrosine-dependent DNA cross-link and single-strand cleavage at oriP required for terminating replication and maintaining viral episomes. Counteracts the stabilization of host p53/TP53 by host USP7, thereby decreasing apoptosis and increasing host cell survival. Induces degradation of host PML through the ubiquitin-proteasome system, which promotes lytic reactivation and may impair the host cell DNA repair. Increases the association of CK2 with PML proteins which increases the phosphorylation of PML proteins by CK2, triggering the polyubiquitylation and degradation of PML. Displays inhibitory effects on a SUMO2-modified complex that includes STUB1, KAP1 and USP7. This inhibitory effect possibly participates to the maintenance of latency linked to PML silencing.
Miscellaneous:
MISCELLANEOUS: EBNA1 is possibly linked to multiple sclerosis in the host. Antibodies that recognize both EBNA1 and the host protein HEPACAM/GlialCAM can be produced when B cells undergo somatic hypermutations. A mimicry has also been proposed between ANO2 (Anoctamin 2) and EBNA1.
Subcellular Localization:
Host nucleus.
Domain:
The N-terminus contains the region UR1 that binds zinc and is essential for EBNA1 to activate transcription. This domain dimerizes upon coordinating. The Gly-Gly-Ala repeat region (GAr) inhibits the mRNA translation of EBNA1 in cis and thus prevents MHC-I restricted presentation of EBNA1 epitopes to the host cytotoxic T cells. The chromosome-tethering regions contain Gly-Arg (GR) repeats that function as AT hooks and are involved in EBNA1 stable replication and partition of episomes. The C-terminus DNA binding and dimerization domain (DBD/DD) is required for the viral latent DNA replication.
Sequence:
MSDEGPGTGPGNGLGQKEDSSGPEGSGGSGPQRRGGDNHGRGRGRGRGRGGGRPGAPGGSGSGPRHRDGVRRPQKRPSCIGCKGAHGGTGSGAGAGGAGAGGAGAGGGAGAGGGAGGAGGAGGAGAGGGAGAGGGAGGAGGAGAGGGAGAGGGAGGAGAGGGAGGAGGAGAGGGAGAGGGAGGAGAGGGAGGAGGAGAGGGAGAGGAGGAGGAGAGGAGAGGGAGGAGGAGAGGAGAGGAGAGGAGAGGAGGAGAGGAGGAGAGGAGGAGAGEEAGGAGAGGGAGGAGAGGAGGAGAGGAGGAGAGGAGGAGAGGGAGAGGAGAGGGGRGRGGSGGRGRGGSGGRGRGGSGGRRGRGRERARGRSRERARGRGRGRGEKRPRSPSSQSSSSGSPPRRPPPGRRPFFHPVGDADYFEYLQEGGPDGEPDVPPGAIEQGPTDDPGEGPSTGPRGQGDGGRRKKGGWFGKHRGQGGSNPKFENIAEGLRVLLARSHVERTTEEGNWVAGVFVYGGSKTSLYNLRRGIALAVPQCRITPLSRLPFGMAPGPGPQPGPLRESIVCYFMVFLQTHIFAEVLKDAIKDLVMTKPAPTCNIKVTVCSFDDGVDLPPWFPPMVEGAAAEGDDGDDGDEGGDGDEGEEGQE
The following text describes a protein:
Function:
Component of the commander complex that is essential for endosomal recycling of transmembrane cargos; the commander complex is composed of the CCC subcomplex and the retriever subcomplex. Component of the retriever complex, which is a heterotrimeric complex related to retromer cargo-selective complex (CSC) and essential for retromer-independent retrieval and recycling of numerous cargos such as integrin alpha-5/beta-1 (ITGA5:ITGB1). The recruitment of the retriever complex to the endosomal membrane involves CCC and WASH complexes. In the endosomes, drives the retriever and recycling of NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo essential for the homeostatic maintenance of numerous cell surface proteins associated with processes that include cell migration, cell adhesion, nutrient supply and cell signaling.
Subcellular Localization:
Endosome.
Sequence:
MSVKIKLHRMDRVYRPPDVIDGVIIIDTPSSVSHQGVRLTAVGTIVFQLSARQVGVFEALYKSVKPIELMHKVVDIQAPGKFPRGKTEIPFAISLDTPKEGKLFESFHGAYVNIQYLLTAELIRGYLQKQMLEIVEFMVEERKEQMPRRLLESTPVNFYITQDTQKHVIAPALRSGGFKITGRVVTQCPLSEYVMGELTVEHSAIPISSIDLQLLRVESIVAGDRMATEASEIQRTQVVDGDVCRGLVVPIYMVLPRLLTCPTLAAGAFSLEFELSIVVTFEALSSRHTLLYDPDSTKMTTAHETLPLRLFRL
The following text describes a protein:
Function:
Component of the BBSome complex (By similarity). The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia (By similarity). The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function (By similarity). Required for proper BBSome complex assembly and its ciliary localization (By similarity). Required for cilia biogenesis and both the assembly and movement of intraflagellar transport proteins along the ciliary axoneme. Plays a role in the removal of degraded mechanosensory receptors within the cilia. Plays a role in guanylyl cyclase localization in the ring-like structures at the base of the finger compartment in AFD sensory neurons. In ciliated sensory neurons, required for the sensation of nitric oxide and avoidance of NO-producing organisms like P.aeruginosa.
Subcellular Localization:
Cell projection, cilium. Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, cilium axoneme. Note=Moves in anterograde and retrograde directions along the ciliary axonemes.
Sequence:
MQNYSRTDFAQVGTTNRGCMRVIPSDKEKEHDLIVVGGQNGSLICLSRKSNDTTIIFKTQPGYPVQSLALGGPASSKKKDKIFVASQNTVRGVNRKGKTFFSMETNMAEVANRMFVRGLDVVLTGRKSYSRYHDTVDSNSYLCTEDIHDVVSLVFEEAWGSREYTSILACGNSTLQIIEGNNFAYDVRLDSVPFTVSLFMGDGGHTKLLVLYGTKTGRLGLVSVPQGGGKILWEIDTTSGACVTTIVCFNVTGGQFPDIIVGKEDGLIEIYVIDETDHAHLFGTFSCDESITGISCGHVSSKSEIDIIICTFTGWLFSLAKTSRPMIENLPVAANFSVKMQQLRSEVEELQTKVNEERLRYEEITKRQGSGTGSTFFHSFQVHENFEYSAAHGAYNLTIELVIPIDFVVVQSQLPIRLMEVEKNASVVSEVRQDALNPWPLLASYRCQANVCRLELRVQANEGDSGVINLYVCPKVMPKCAQITTHYIKALSSHMRSHDFDLYRPMNTLQFTGNFSIAEAHAWLHNLLPNVPSKCPPADTITNNYQCSVNGGTQLQVVYSKGSAVFRSDCMTTICIIRDKVSEQTMKMQIRVEVACELNQDSVNHCLKLIDPKITSMLNIEKNKLYAAALKELESNNDDVFSFLSAANAKILKDHDAIYEKSEGVSIEDSGVLAILENLMVARGKLTGRSSKGRGDAIRDLISTDYSLENMQTLFKNAMND
The following text describes a protein:
Function:
Required for centrosome cohesion and recruitment of CEP68 to centrosomes.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Note=Colocalizes with gamma-tubulin during interphase and mitosis. Appears to associate with the mother centriole during G1 phase and with daughter centrioles towards G1/S phase. Localizes to the proximal ends of the centrioles (By similarity). Levels are high at interphase centrosomes but are reduced on mitotic spindle poles (By similarity).
Sequence:
MNLQDELDELKIYMTIDKTTIQELNRCMAEKREEQLFRHHEDAGVKKSTPEKNEKAISEQTLEKVIELENRLKSFEKNSRKLKEESKKLKKENDFLKSHLQHYQEDSESRGKELEKLLRVSSSVEQDKSELQTKVTALEREVTTLRRQVAKAKALRDENEEVVNPEEKEHCPTDKAKSEMATTDVRAQHCDCKTTTTKVKFKAAKKKCSVGRHHTVLNHSIKVMSHVENLSKDGWEDMSEGSSDSETQTFQNLGTVIVETSQNIRPIENDGNQKETDQTEDSRAQQEVQTYSCEDLKAPQNTKKMTFQNKSGSLQKNLHSALPARVNREKCKTKPAQKSSSNTILLRERIVSLQQQNSLLQNARKAAESSAKEFKEANEKLLHQQQISDHRFQTSRQTIKLTLDLAELRKEKEDLLKKVESSSDITSLAEEVSRIMAPQIQVTTLGPSRSTDLEIKQLQCKLKNATNELTKQSSSVKSLKLELLAKDDHMKAMQEKMSRMERDITMKRHLIEDLKFRQKINSESNESFNEMLGTLEKKDLKMNLLISKLNDTETAMAQIKSAASEQLQGLALQSEQVLEGTQKKLLLANEKIEEFTVFVQALVNELQSDAHRTRQQVRELRQTQKSRHACKTSTHKAQTLAASILNISRSDLEEILHTGDEMEIEKTKIDAENDKDWMLYIQKLLQGQLPFASYLLEAVLGKIKENKKLTEGYFTVMKDIK
The following text describes a protein:
Function:
Mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Also mediates heterophilic cell-cell adhesion with CADM3 and NECTIN3 in a Ca(2+)-independent manner. Interaction with CRTAM promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ T-cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM1 in vivo. In mast cells, may mediate attachment to and promote communication with nerves (By similarity). CADM1, together with MITF, is essential for development and survival of mast cells in vivo. By interacting with CRTAM and thus promoting the adhesion between CD8+ T-cells and CD8+ dendritic cells, regulates the retention of activated CD8+ T-cell within the draining lymph node. Required for the intestinal retention of intraepithelial CD4+ CD8+ T-cells and, to a lesser extent, intraepithelial and lamina propria CD8+ T-cells and CD4+ T-cells. Interaction with CRTAM promotes the adhesion to gut-associated CD103+ dendritic cells, which may facilitate the expression of gut-homing and adhesion molecules on T-cells and the conversion of CD4+ T-cells into CD4+ CD8+ T-cells. Acts as a synaptic cell adhesion molecule and plays a role in the formation of dendritic spines and in synapse assembly. May be involved in neuronal migration, axon growth, pathfinding, and fasciculation on the axons of differentiating neurons. May play diverse roles in the spermatogenesis including in the adhesion of spermatocytes and spermatids to Sertoli cells and for their normal differentiation into mature spermatozoa.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Synaptic cell membrane; Single-pass type I membrane protein. Note=Localized to the basolateral plasma membrane of epithelial cells in gall bladder.
Domain:
The cytoplasmic domain appears to play a critical role in proapoptosis and tumor suppressor activity in NSCLC.
Sequence:
MASAVLPSGSQCAAAAAVAAAAAPPGLRLRLLLLLLSAAALIPTGDGQNLFTKDVTVIEGEVATISCQVNKSDDSVIQLLNPNRQTIYFRDFRPLKDSRFQLLNFSSSELKVSLTNVSISDEGRYFCQLYTDPPQESYTTITVLVPPRNLMIDIQKDTAVEGEEIEVNCTAMASKPATTIRWFKGNKELKGKSEVEEWSDMYTVTSQLMLKVHKEDDGVPVICQVEHPAVTGNLQTQRYLEVQYKPQVHIQMTYPLQGLTREGDAFELTCEAIGKPQPVMVTWVRVDDEMPQHAVLSGPNLFINNLNKTDNGTYRCEASNIVGKAHSDYMLYVYDPPTTIPPPTTTTTTTTTTTTTILTIITDTTATTEPAVHDSRAGEEGTIGAVDHAVIGGVVAVVVFAMLCLLIILGRYFARHKGTYFTHEAKGADDAADADTAIINAEGGQNNSEEKKEYFI
The following text describes a protein:
Function:
Catalyzes the dehydration of D-mannonate.
Miscellaneous:
MISCELLANEOUS: Member of the exu locus which is required for galacturonate utilization.
Sequence:
MNMTFRWYGRGNDTVTLEYVKQIPGVKGIVWALHQKPVGDVWEKEEIRAETEYIQSYGFHAEVVESVNVHEAIKLGNEERGRYIENYKQTIRNLAGFGVKVICYNFMPVFDWTRTDMFRPLEDGSTALFFEKAKVESLDPQELIRTVEEASDMTLPGWEPEKLARIKELFAAYRTVDEEKLWDNLSFFLQEILPVAEAYGVQMAIHPDDPPWPIFGLPRIITGEASYKKLRAISDSPSNCITLCTGSMGANPANDMVEIAKTYAGIAPFSHIRNVKIYENGDFIETSHLTKDGSINIQGVMEELHKQDYEGYVRPDHGRHLWGEQCRPGYGLYDRALGIMYLNGLWDAYEAMAKKEVGI
The following text describes a protein:
Function:
Component of RNA polymerase I core factor complex that acts as a GTF2B/TFIIB-like factor and plays a key role in multiple steps during transcription initiation such as pre-initiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment (By similarity).
Subcellular Localization:
Nucleus, nucleolus.
Domain:
Although it shares weak sequence similarity with GTF2B/TFIIB, displays a similar subdomain organization as GTF2B/TFIIB, with a N-terminal zinc finger, a connecting region (composed of B-reader and B-linker regions), followed by 2 cyclin folds.
Sequence:
MDDDGGGSPGHYGGGGIHLVCEYCGHGSEYAEDDADDGFFTCRQCSAIHTSTQNTATNPFDFPMTPAHLSAHRRPTQPTPTPKPFPAPRGAATGAAAPDFDDLGEPSEPRDFATGANAWGNPEDVAARVRWRYVRGLQVILQRQLEALVERHRVGSLAASLAGTIWLRWVAASKVFDEMWVHKMLAIAASVEEGHSASKDKQSELEGDAQKSQSSYEFLFLRSLRMMLPVYSTLAVCFLACHVARETILPTDICRWAMEGKLPYVAAFTQVDKLLGSSLNDCPLSSRQLFRPTRVIGAWQLEAAAGSIAQKIGLLLPSVNFYLIAQRFLKELSLPIEKILPHACRIYEWAMPAELWLSSNPGRVPSRVCVMAILIVALRVLYGINGQGIWESIAQTENAVGSDPEASAPHSIEPDSNNSEEFDARELLCTLAASYDKINVGHDYSKEVHSYLKYCKDVVFTGMTFSLEEEHLIDIFWDMYKGKEVMLLDENAKLCQEKLRTTNGVNKRCRDGRFADTKCCSTPLGNCALQSIKSKMEENGFCYVSPRKRLVSDGYLLYTRRESSGSLIYVAHADYYILLRPFAKLAEVDVRVLHSSVLKLERRLGWIEERVGRSLNTLQNLHDEASDDERPVSD
The following text describes a protein:
Function:
ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5' splice site duplex to permit an effective competition for the 5' splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5' splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/U5 snRNP, facilitating the first covalent step of splicing (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MASNGYLNSIDAVPPPLIDSDGRPPSPPPPPPDSFVPPPPPSSLAPPPPPSSDLPPPPPSELQPPPPEPKKKKGWGAPKPGPLSIEDILKKKKEADEAAAKPKFLSKAAREKLALEKRAKEVEEQRRKRESEQDNRIPVGTVNGNGYGAANGRDGYERSHQQDNARRDSSFVPTGPRAMRNGQQNRPSSDKPNDMEPPPKSAKPATTAAGSSKASVAGEKRPANAEDLQAALIRTRYMGAETNQSTFSAKKKRRRTTEKKFNFEWNAEEDTSPDYNPIYQNRAEAGLYGRGRLAGFAEDEAATLKYAKALEERDIEAGSARAREIVEMERRRKEDAGRNSLDKHWSEKKLEHMRERDWRIFKEDFNISTKGGAIPNPMRSWSESKLPKRLLDVINQVGYDEPSAVQRAAIPIALQARDLIGVAVTGSGKTAAFLLPLLVYISELPPLNEFTKNDGPYAIILAPTRELAQQIEVEAKKFATPLGFTCVSIVGGHSLEEQSYNLRNGAEIIIATPGRLVDCIERRVLVLGQCCYIIMDEADRMIDLGFEESVNKILDALPVSNEKPDTDDAEDAQAMSRHLGGKDRYRQTMMYTATMPPAVEKIAKKYLRRPAIVTIGNIGEAVETVEQRVEFVAGEDKRKKRLNEILASGEFQPPIIVFVNIKRNCDAVARDIKHMGFTSVTLHGSKTQEQREAALASVRSGATNVLVATDLAGRGIDVPDVSLVVNFNMATNIESYTHRIGRTGRAGKSGVAITFLGNEDADTMYDLKQMLMKSSISRVPEELRKHEAAQQKSQRGQGLKKIEEGGFGGKGGAGGC
The following text describes a protein:
Function:
Indole-3-glycerol phosphate synthase required for tryptophan biosynthesis.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MEGLVPVQRLPIKVASPSLYRCNNSVSIRRSISGFAMDRKINFRAPSQFSIRAQQSDLKESLAVSSSSVEDKGNVLRIKEWEVEMYQEELAISQGIRIRRKPPSKAPLGYSGPFELRLHNNDADSPRNILEEITWYKDVEVSRMKELNPLDVLKKAVEDAPPTRDFVGALRMAHKRTGFPGLIAEVKKASPSRGILKENFDPVEIAQAYEKGGAACLSVLTDQKYFQGGFENLEAIRSAGVKCPLLCKEFVVDPWQIYYARTKGADAVLLIAAVLADLEITFLLKICKKLSLAALVEVHDEREMGRVLGIEGIELVGINNRSLETFEVDISNTKKLLEGEHGRQIRERDMIVVGESGLFTPDDIAYVQAAGVKAVLVGESIVKQNDPEKGIAGLFGRNISHT
The following text describes a protein:
Function:
NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein.
Sequence:
MASNNDSIKKTLFVVIALSLVCSIIVSAAAVGLRDKQKENAALDKQSKILQVAGIEAKGSKQIVELFNKSIEPRLVDFNTGDFVEGDAANYDQRKAAKEASESIKLTAEQDKAKIQRRANVGVVYLVKDGDKTSKVILPVHGNGLWSMMYAFVAVETDGNTVSGLTYYEQGETPGLGGEVENPAWRAQWVGKKLFDENHKPAIKIVKGGAPQGSEHGVDGLSGATLTSNGVQNTFDFWLGDMGFGPFLTKVRDGGLN
The following text describes a protein:
Function:
Involved in the regulation of lipid metabolism in adipose tissue and liver.
Subcellular Localization:
Secreted.
Sequence:
MTIFKKVTTMISWVLLACALPCAADPMLGAFARRDFQKGGPQLVCSLPGPQGPPGPPGAPGSSGVVGRMGFPGKDGQDGQDGDRGDSGEEGPPGRTGNRGKQGPKGKAGAIGRAGPRGPKGVSGTPGKHGTPGKKGPKGKKGEPGLPGPCSCGSSRAKSAFSVAVTKSYPRERLPIKFDKILMNEGGHYNASSGKFVCSVPGIYYFTYDITLANKHLAIGLVHNGQYRIRTFDANTGNHDVASGSTILALKEGDEVWLQIFYSEQNGLFYDPYWTDSLFTGFLIYADQGDPNEV
The following text describes a protein:
Function:
Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.
Subcellular Localization:
Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus.
Sequence:
FSVSVLFFFFLLFPDPLISRNYKGDVSMSEIDYFMPLLMQKEEESALTPLLSRGKIHFLWIKHSNLYLVALTMKNANASLVYSFLYKVVEVFSEYFKELEEESIRDNFVIVYELLDELMDFGFPQTTDSKILQEYITQQGNKLDTGKSRVPATVTNAVSWRSEGIKYKKNEVFIDVIESVNLLVNANGSVLLSEIVGSIKLKVFLSGMPELRLGLNDRVLFELTGRKNKSVRTPMLSAIEKKTLGTSMLLNESTLTALDQCHGVMGAVVWNHGLGLVCQRMVFENFHHIWIRFSLEPESYFELYDADSPKFKTSIGSAKYLPEKDVVIWSIKSFPGGKEYLMRAHFGLPSVENEELEGRPPISVRFEIPYFTVSGIQVRYMKIIEKSGYQALPWVRYITQSGDYQLRTH
The following text describes a protein:
Function:
Mediates the regulatory switch from transcription to RNA replication (By similarity). Acts late in infection by inhibiting viral transcription and up-regulating RNA replication (By similarity). Plays a major role in antagonizing the type I IFN-mediated antiviral response. Interacts with host MAVS and prevents the interaction with its upstream partner RIGI in the signaling pathway leading to interferon production. Inhibits host RIGI signaling by preventing TRIM25-mediated RIGI ubiquitination. Also inhibits viral-induced cytokine production in dendritic cells by targeting MYD88 thereby inhibiting MYD88-dependent gene transcription. Also inhibits the phosphorylation of host IRF7 to prevent type I interferon production in dendritic cells.
Subcellular Localization:
Host cytoplasm.
Sequence:
MTLHMPCKTVKALIKCSEHGPVFITIEVDEMIWTQKELKEALSDGIVKSHTNIYNCYLENIEIIYVKAYLS
The following text describes a protein:
Function:
Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. In addition to the protease activity, also mediates delipidation of PE-conjugated ATG8 proteins.
Subcellular Localization:
Cytoplasm.
Sequence:
MVNDAQSQSWGGAATSSEVYNSRIYSFSLIFIVVIAQFWLHKSVFLQVFLEDFSSRIWITYRKGFDAISDFKLTSDVNWGCMVRSSQMLVAQALIFHHLGRSWRKPPEKPYNPDYIGTLIRTNREQADAVDGKENFPMELYVVSGDEDGERGGAPVVYIDVAAQLCSDFNKGPSTWSPILLLVPLVLGLDKINPRYIPLLKETFMFPQSLGILGVKPGTSTYIAGVQDDRALYLDPHEVQMQFLFHRPLESGYFCWSEVHFWFLELHFVLANIKWPETLETDFIYIHIIPRDAPLLESIGPQKCLAFSTDGAKFAIGGEDGHLRIFHWPSIKVLLDEPKAHKSFRDMDTGLDSEFLVSTSIDGYARIWKIDEGAPLVNLTQSSDEKIECCRFSRDGMKPFLFCTVAKGYKVVTVVWNISDWERIGYKRLLGKPISTLSVSLDGKYMALGSHDGDFCAVSEEATTLRNLTFFLTSNLKLRVNS