lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Probable effector of the planar cell polarity signaling pathway which regulates the septin cytoskeleton in both ciliogenesis and collective cell movements including covergent extension during gastrulation. Controls cell shape but not polarization during convergent extension. Proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recruitment of peripheral IFT-A proteins to basal bodies.
Subcellular Localization:
Cell membrane. Cytoplasm, cytoskeleton, cilium axoneme. Cytoplasm, cytoskeleton, cilium basal body. Note=Also found adjacent to the cilium basal body.
Sequence:
MSFCLTELYLWSLKNNLHIGDEDVGVHQYHEKKEAALHPDYGFLEEKQQWMESRGFPWILKNKRPEKLRDNLTELEELMQSSECVLSKWKNKYVCQLLFGSGVLVSISLSGPQLEKVVIDRSLVGKLISNPISDAIFTDSFIILSFLKENKLCLIQFTKKINSPDINRQLDKLSLLDLKISYTDIPGPKGRHLVRHLAINSMQDLALCWWPVPVDDVKPWSPVSSEKDRANLVLLSNSSCKLEVLSYIRTEGDLLNACFSINQPYQICTVEHSLNSNKEPMADRFIYECVRNKIQCVSVTRVPLRSRVISCAVNTSEDKLVLGCEDSSLILYESDCKVTLLAQADLLPDLIRWHPNGTIFVVASSQGELQIFDMALSPIRAQILAEEIEPNSTIQVCKQFNVSSTLVEMHWAAPHTLLQNMDMTDIYNLLYLRFDGGPIGVLQLKLGAICRGQLGAMEIISQYIRHDEVDEAVGLLSSMNWNTMGHQCFTSMTAIVNHLLRQRLTPDREAQLEASLGTFYSPTRPLLDTIVLQYRDPISRYARRFFHHLLRYQRFEKAFLLAVDIGARDLFMDIHYLALDKGELALAKVARKKAEEIDAESINSGVEPLLPTDTLADVNEAFVDLSLIPQVEDRILGSFPSTDLGAHNSIQRNANRQLVHIENEIGIEVYAESLDKSLPWNQECFEEDFAEENPEGIGSLKVVHFGLV
The following text describes a protein:
Function:
Catalyzes the reversible hydration of carbon dioxide. Can hydrate cyanamide to urea; Reversible hydration of carbon dioxide.
Subcellular Localization:
Cytoplasm.
Sequence:
HSGPDTWWVHYPSASGSMQSPVDIITEETWQASRENSNFEPLEIDYSSMGGGSNVTGGPYRHYNFLLEQIHMHWGESDKNGSEHYVNGKGYSAELHFVHWNEDLYSSYEEAARNDDGILVLAVFVQFIQKHKNTKTHTDKHTQTHTNSQPEDTSKFWTYQGSLTTPPCYESVTWVIFENCIYTSSAVLKKYRELKYYAENETRPDDEFDGQLKTNNRPVQPIGVRKVRQINSQLID
The following text describes a protein:
Function:
Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and angiogenin (ANG). May play a role in redox homeostasis. Required to inhibit the cytotoxic tRNA ribonuclease activity of ANG in the cytoplasm in absence of stress. Relocates to the nucleus in response to stress, relieving inhibition of ANG in the cytoplasm, and inhibiting the angiogenic activity of ANG in the nucleus.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSLDIQSLDIQCEELSDARWAELLPLLQQCQVVRLDDCGLTEARCKDISSALRVNPALAELNLRSNELGDVGVHCVLQGLQTPSCKIQKLSLQNCCLTGAGCGVLSSTLRTLPTLQELHLSDNLLGDAGLQLLCEGLLDPQCRLEKLQLEYCSLSAASCEPLASVLRAKPDFKELTVSNNDINEAGVRVLCQGLKDSPC
The following text describes a protein:
Function:
Acts as a co-chaperone for HSP90.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MNYMPLHSVMDICSRHPTLKWAQRGDLLYITIDLPDAKAVNLKLEPEGKFYFSATSGADNIPYEIDINLYDNVNVDVSTLTKIQLFSVVLGHHLSLMCYTNFSSKRLECPCKKCSCIVGSWELQESKASVGSRNIVYIVKKEESKWWSRLLKQEGRTPTFIKVDWNKWVDEDEQDDKAGPDMDYDDVNFSSLNLGGGGGGEEEEEDFDDEDEDESDTATEEEKEEETINASSQVEAKAKA
The following text describes a protein:
Function:
Mitochondrial membrane protein that catalyzes the essential first step of biosynthesis of glycerolipids such as triglycerides, phosphatidic acids and lysophosphatidic acids. Esterifies acyl-group from acyl-coenzyme A (acyl-CoA) to the sn-1 position of glycerol-3-phosphate, to produce lysophosphatidic acid. Has a narrow hydrophobic binding cleft that selects for a linear acyl chain. Catalytic activity is higher for substrates with a 16-carbon acyl chain.
Subcellular Localization:
Mitochondrion outer membrane; Peripheral membrane protein.
Sequence:
MDETALSLGTIDVSYLSTSAECSVSRCKHSNEEWGECNSRPTLFRSATLKWKETLSRKRPFVGRCCYVCTPQSRDNFFNASIPSLGLRNVIYINETHTRYRGWLARRLCYVLFVLERDVHKGMFAKNLTENVLNSSRVQKAIVDEASEPSVPGSFAQTDPKAINKVKKKARKILQEMVANVSPALIRLTGWVLLKLFNSFFWNIQIHRGQIEMVKAATEMNLPLIFLPVHKSHIDYLLLTFILFCHNIKAPYIAAGNNLNIPIFSTLIRKLGGFFIRRKLDQSSDGRKDFLYRALLYVHIEELLRQQQFLEIFLEGTRSRSGKTSSPRAGLLSVVVDALFSNATPDVLIIPVGISYDRIIEGHYNSEQLGKPKKNESLWSIARGVFRMLRKNYGCVRVDFAQPFSLKEYVNSQSQKTVPAPLSLEQALLPAILPSRPNDTVDEGTEASLPNSKDITSEPYRRELIANLAEHILFTANKSCAVMSTHIVACLLLYRHRQGTDLSRLVEDFFSMKEEVLARDFDLGFSGNSDDVVMHAIHLLGNCVNITNTSRNNEFFITPSTTIPAVFELNFYSNGILHVFIKEAVIACSLHAVQSKRFRNGTNGASPSLISQEHLVRKAASLCYLLSNEFTVSLPCQLIYQVCHEAVEKLIQYGILLVAEDDQEDVSPSLTEQQWNKKLPEPLTWRSDEEDEDSDFGEEQRDCYLKVSQSQEHQQYITFLQRLLGPLLEAYSSAVIFVHNFSGPVSESEYLQKLHRHLINRTEKNVAVYAESATYSHVKNAVKVFKEIGVFIQTNQKRDTILELSTTFLPQRNRQKLLEFIMSFMVL
The following text describes a protein:
Function:
Sex determination switch protein, which controls sexual development and dosage compensation in females. Sxl protein is only active in females: it is inactive in males throughout development. Acts as a mRNA-binding protein, which specifically binds to a subset of pre-mRNAs and mRNAs and regulates their processing and/or translation. Binds nanos mRNA and is involved in bam-bgcn mediated repression of nanos mRNA translation. Promotes sexual development by controlling the female-specific alternative splicing of the transformer (tra) pre-mRNA: binds tightly to a characteristic uridine-rich polypyrimidine tract at the non-sex specific 3' splice site in one of the tra introns, preventing the general splicing factor U2AF from binding to this site and forcing it to bind to the female-specific 3' splice site. Acts as an inhibitor of dosage compensation in females by preventing production of msl-2 protein, an essential component of the MSL complex, the complex that mediates X-chromosome dosage compensation. Specifically binds to uridine stretches in both the 5'- and 3'-UTR of msl-2 transcripts. Sxl first acts at the splicing level by promoting retention of an intron in the 5' UTR of msl-2 pre-mRNA. The retained intron contains Sxl-binding sites that are required for subsequent steps of repression: after msl-2 mRNA export into the cytoplasm, Sxl coordinates its translational repression by targeting early steps of translation initiation. Together with how, Sxl also prevents production of msl-2 protein by preventing nuclear export of msl-2 transcripts; [Isoform 1]: Embryo-specific product, which is expressed early only in female embryos and specifies female-adult specific splicing.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MYGNNNPGSNNNNGGYPPYGYNNKSSGGRGFGMSHSLPSGMSRYAFSPQDTEFSFPSSSSRRGYNDFPGCGGSGGNGGSANNLGGGNMCHLPPMASNNSLNNLCGLSLGSGGSDDLMNDPRASNTNLIVNYLPQDMTDRELYALFRAIGPINTCRIMRDYKTGYSFGYAFVDFTSEMDSQRAIKVLNGITVRNKRLKVSYARPGGESIKDTNLYVTNLPRTITDDQLDTIFGKYGSIVQKNILRDKLTGRPRGVAFVRYNKREEAQEAISALNNVIPEGGSQPLSVRLAEEHGKAKAAHFMSQMGVVPANVPPPPPQPPAHMAAAFNMMHRGRSIKSQQRFQNSHPYFDAKKFI
The following text describes a protein:
Function:
Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming queuine, allowing a nucleophilic attack on the C1' of the ribose to form the product.
Subcellular Localization:
Cytoplasm.
Sequence:
MALRFEILGRFNRARAAQLILPHYECQTPLFMPVGTQGTIKGLTTHQLEDIGCQIILGNTYHLALRPTSELIDELGGLHKFMNWPRALLTDSGGFQMVSLLHLADITEKGVTFQSPVDGKPMLLTPEESIQIQNRIGADIIMALDDVVKTTITGPRIEEAMYRTLRWIDRCIAAHKRPHEQNLFGIVQGGLDPVLRDICVRGLVERNLPGYAIGGLAGGEDKDSFWRVVAQCTAALPEHKPRYVMGVGYPLDILVCSALGADMYDCVYPTRTARFGTALVPEGVLKLKHKAMEDDLRPIDPTCDCMVCKTYTRAYIHCLVTKDAMGSQLLSHHNLHYMMKLSRDLHSSIVEGWFPEFVCQFLQKMFPQGDVPEWVCNAMEVAGIDISSCCAPFSSLSDKVEDTQNQEVKQ
The following text describes a protein:
Function:
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid.
Sequence:
MLDLRGDPIELTAALIDIPSESRKEARIADEVEAALRAQASGFEIIRNGNAVLARTKLNRSSRVLLAGHLDTVPVAGNLPSRRENDQLHGCGAADMKSGDAVFLHLAATLAEPTHDLTLVFYDCEEIDSAANGLGRIQRELPDWLSADVAILGEPTAGCIEAGCQGTLRVVLSVTGTRAHSARSWLGDNAIHKLGAVLDRLAVYRARSVDIDGCTYREGLSAVRVAGGVAGNVIPDAASVTINYRFAPDRSVAAALQHVHDVFDGLDVQIEQTDAAAGALPGLSEPAAKALVEAAGGQVRAKYGWTDVSRFAALGIPAVNYGPGDPNLAHCRDERVPVGNITAAVDLLRRYLGG
The following text describes a protein:
Function:
Polo kinase inhibitor required to maintain G2 arrest in the meiotic cell cycle in females. Holds heterochromatically paired homologs together from the end of pachytene until metaphase I. Haploinsufficient locus for homologous achiasmate segregation and may be required for the maintenance of heterochromatic pairings.
Subcellular Localization:
Nucleus. Chromosome.
Sequence:
MENCRTPTNKTQITLNRTPTLKERRWNTLKVNTTNVRCSTPIFGNFRSPNLSPIESMGTKKSPVSPMRFAFKKPPAKAHPHPHQHQHHHHHHKHIHRTQLKPPPFILPKPQEEIIEPEREIKICSSPDTFSDDSNMETSLVVESRRRSIKASNHSYVVNHAANVEQILMHMGLENYVTNFEEAHIDLVKLASMERADLVKIGLNADEDCNRIMDVLQTL
The following text describes a protein:
Function:
Tumor suppressor which functions to suppress MRTFA-induced SRF transcriptional activity.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MVRGARQSQQPRSRLAPRLSGTVEKPPRKRKSRTEFTLKETMSSGGAEDDIPQGERKTVTDFCYLLDKSKQLFNGLRDLPQYGQKQWQSYFGRTFDVYTKLWKFQQQHRQVLDNRYGLKRWQIGEIASKIGQLYYHYYLRTSETSYLNEAFSFYSAIRQRSYYSQVNKEDRPELVVKKLRYYARFIVVCLLLNKMDVVKDLVKELSDEIEDYTHRFNTEDQVEWNLVLQEVAAFIEADPVMVLNDDNTIVITSNRLAETGAPLLEQGMIVGQLSLADALIIGNCNNQVKFSELTVDMFRMLQALEREPMTLASQMNKPGIQEPADKPTRRENPHKYLLYKPTFSQLYTFLAASFKELPANSVLLIYLSATGVFPTGRSDGEGPYDFGGVLTNSNRDIINGDAIHKRNQSHKEMHCLHPGDLYPFTRKPLFIIVDSSNSVAYKNFTNLFGQPLVCLLSPTAYPKALQDQSQRGSLFTLFLNNPLMAFLFVSGLSSMRRGLWEKCQEYLRKINRDIAQLLTHSRSIDQAFLQFFGDEFLRLLLTRFVFCSATMRMHKAFRETRNYPESYPQLPRDETVENPHLQKHILELASILDVRNIFFENSMDDY
The following text describes a protein:
Function:
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity). This subunit is essential for activity, but not assembly, of the enzyme complex (By similarity). This subunit is also required for silencing the ATPase activity of V-ATPase when V1 is detached from V0 (By similarity).
Subcellular Localization:
Vacuole membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MSNSDLELSNAASPPPVELDNSQVDEIINNVRCVAIPWQGYQRSGSLEENELQEIENLTGKPLSAYVKTAEEDTTAYSNLFLKLLSMKDTPDVVNFALVKLADTLLNSNKFLSAFGPAFYDFLEKDESYINYLDDDSKLLFARVFALCSSSSPCSVAKAFTLFLEYLGKLMQSLNPLTRLFAVQCLNGVLTLKAHRYALWAENTCSFRLAELLRNSIGDTQLQYYSLFCFWQLTFESHIAQDINKRFDLIKLLVQIIRSDTKTKVYRLVLAILVNLIDKAPKDTISTMLLEHVDKAVQLLQKRKWADEDITNYLDFITSTLDESSKHLSTFDMYKSELDTGILHWSPSHRSEDFWHQNAKRLNEDNYALLKKLFHIVQYNEDNTSLAVACHDLGAYIRSYPEGRSLIIKYGAKQRIMDLMSHPDPEVRFEALSTVQLLMTEVCFLSKITL
The following text describes a protein:
Function:
Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular Localization:
Nucleus.
Sequence:
MCSREQGPRGPLGVCAAGRGGPSVERAGRGEAAGPAPLAPAASARSRPAVGARKVGAGGGLPSLLFRPGAPRLCVSLSFGDTWIWSRTGCPREGPASGSAREGEREGGREGGREGGKEGGQRRLRWPRLPSPGGRPASVAVGSRGAGNGGASEAGLDRAGGTEAAGLRPAPGARSFPAGGRPYALKPDAYPGRRADCGPGDGRSYPDYMYGSPGELRDRAPQALPSPEADALAGSKHKEEKADLDPSNPVANWIHARSTRKKRCPYTKYQTLELEKEFLFNMYLTRDRRYEVARVLNLTERQVKIWFQNRRMKMKKMNKEKTDKEQS
The following text describes a protein:
Function:
Putative oxidoreductase.
Sequence:
MNANARRIWLTGASSGIGAALAEQLLEQGHRLALSARSIEPLQALAKRYPQQVLVVAGDLGDASQVRAIGEHIGQVWGALDCAILNAGTCEYVEVSAFEAAMVERVMRANVLSASYCIEAALPLLRQGNRAHLVGVGSSVTFMPLPRAEAYGASKAAMRYLMEALRIDLHAENIAVTLVSPGFVDTPLT
The following text describes a protein:
Function:
Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Subcellular Localization:
Nucleus.
Domain:
The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Sequence:
MVKIIGKGGANYVLAFGNDNDDLYRICVRGRSLRENNRSTVDNYHYALEVVKPQLGEFVCRMELVDLPVCDSLRQVLKSKIEVWDATTVTCLKMPNLVPAGSLSHTVDHFTKIHIGERAIVWEFKPKWLSGNDKYCRNCTLNLLRGQTSISYCHAQLLNPGQAGPILKSLFAGLNVPPAFIEDMEAYIAQPCSVLQRLRVAQEQVDASLGPLDQPDTAASPERCLSMTLKDVSCFVSWHKDASPVAVVVDLDMKPAAKSAHWTALQEQLDRFQPQVRH
The following text describes a protein:
Function:
Required for maintaining the appropriate mycolic acid composition and permeability of the envelope on its exposure to acidic pH. Upon expression in E.coli functions as a triacylglycerol synthase, making triacylglycerol (TG) from diolein and long-chain fatty acyl-CoA. Has very weak wax synthase activity, incorporating palmityl alcohol into wax esters in the presence of palmitoyl-CoA.
Sequence:
MTRINPIDLSFLLLERANRPNHMAAYTIFEKPKGQKSSFGPRLFDAYRHSQAAKPFNHKLKWLGTDVAAWETVEPDMGYHIRHLALPAPGSMQQFHETVSFLNTGLLDRGHPMWECYIIDGIERGRIAILLKVHHALIDGEGGLRAMRNFLSDSPDDTTLAGPWMSAQGADRPRRTPATVSRRAQLQGQLQGMIKGLTKLPSGLFGVSADAADLGAQALSLKARKASLPFTARRTLFNNTAKSAARAYGNVELPLADVKALAKATGTSVNDVVMTVIDDALHHYLAEHQASTDRPLVAFMPMSLREKSGEGGGNRVSAELVPMGAPKASPVERLKEINAATTRAKDKGRGMQTTSRQAYALLLLGSLTVADALPLLGKLPSANVVISNMKGPTEQLYLAGAPLVAFSGLPIVPPGAGLNVTFASINTALCIAIGAAPEAVHEPSRLAELMQRAFTELQTEAGTTSPTTSKSRTP
The following text describes a protein:
Function:
Nonheme iron-dependent dioxygenase that can break carbon-arsenic bonds, playing a role in the detoxification of environmental organoarsenical compounds. Catalyzes the oxygen-dependent demethylation of highly toxic methylarsonous acid (MAs(III)) to arsenite, which can then be exported out of the cell. Can also cleave the C-As bond in several trivalent aromatic arsenicals, including roxarsone (III), nitarsone (III) and (4-aminophenyl)arsonous acid. Organoarsenical degradation by this enzyme is proposed to have a significant impact on the arsenic biogeocycle that maintains a balance between organic and inorganic species.
Miscellaneous:
MISCELLANEOUS: Organoarsenicals are used as herbicides, pesticides, antimicrobial growth promoters, and chemical warfare agents. Arsenic is the most widespread environmental toxin and is classified as a Group 1 human carcinogen.
Domain:
The thiolates of the vicinal cysteine pair (Cys95-Cys96) directly coordinate the arsenic atom of the organoarsenical substrate.
Sequence:
MKYVHVGVNVVSLEKSINFYEKVFGVKAVKVKTDYAKFLLETPGLNFTLNVADEVKGNQVNHFGFQVDSLEEVLKHKKRLEKEGFFAREEMDTTCCYAVQDKFWITDPDGNEWEFFYTKSNSEVQKQDSSSCCVTPPSDITTNSCC
The following text describes a protein:
Function:
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Subcellular Localization:
Cytoplasm.
Sequence:
MSNAKEKVSMVSLGCPKNLVDAEVMLGRLAKDRYEITTDEREADIIIVNTCSFIKEAKQESIDTILDLADRKQDGRCRLLIVTGCLPQRYQEELARELPEVDIFVGTGDYPRIAEIIEEKSSRPEQLRYIGDPNFVFDESLTRLNSSPAYTAYLKIAEGCSNCCSYCVIPSLRGAFRSRPLESVLAEARSLVAGGAREINLIAQDITTYGRDLPGAPSLETLIRELAAIDGLAWIRLLYAYPDGITDGLIQTIKNEPKVCKYLDLPIQHISDPILKRMNRRSTEPQIRELVARLREEIPDIALRTSLIVGFPGETEEDFRTLLHFVEEAQFDRLGVFCYSREEGTPAAEMPDQVSERVKRERYKKLMKAQARVSFKRNRRLIDTEEQVIVEGYSEETELLLKGRSSRQAPDIDGQVYITAGNANVGDIVRLRITDSSDYDLIGEIIS
The following text describes a protein:
Function:
May play a role in apoptosis regulation.
Subcellular Localization:
Nucleus.
Sequence:
MPGLRRDVLRWLVALNLSFPIKNIKRDFSNGFMVAEIFSRYFPQDIHMHSYDYGSRLATKRDNWEQLNKFFRKKGFIAVKDEVDNIIQCNSEDGAGPLLERMYNFLTQKPYVPESAAEQGSLENRDPSQPDDYTSRDEGEEEEEDECSGSDSGTLSETEGETDDGGACMRLQEDNYSERAGDGLIRLSPDGSGFDFQPLVRLDVEENGNDDYFGCLDSGVRFLGEDGGQEDERVEEEQPTKKKSVNAVEKARQRENTKTRRIEKAGVKAGLKASELKQAIAGRKSSTDAGLAFRSPNRNRKENFKQYTLPDYRRQKQFGYVQLGSLGPKEDPELASKLHALQRVKEFGRHARSCNTMSHTNPALASPKAPKKPSSRKVALEFASSIPKPKRKNHSKEESKKVLPIQNPHGLTELQILEMKHQSHKEHVEAIRRDLEHFLR
The following text describes a protein:
Function:
Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins.
Subcellular Localization:
Cytoplasm.
Sequence:
MYYTVSEAEFMKAADALLKLADGILSDPNKFRKIDVNDEVVKSVLGKIPGGLDCLLEMGYSLKDNFYQMPVKISMGKIMKVKLDLKDYYDQIVLRNSLTNVSEEEATRSRKRALKQTIPRPYSKSELDLFVRLSDNFDRMFLYEEILRIKHLWTGPVEDRTKKRMEQSGLDGRYYKDIFLLELLYWFKYSFFTWVDAPECDCCGQSKLIGYVEPTLEEVVFGAYKTELYKCSECSVEIRFPRYNNPLKLLETRRGRCGEWANCFALICRSVGFETRYILANFDHVWVEVYSESQQRWLHCDPCENVCDQNLLYEKGWGREITYIFAFSLNNIQDVTWKYSSDHKALMRRRKECKESWLVKALITLRQERFKLLRLSPEAENRILNATALELVDMLNEPSEKKDEKYSGRTTGSLEWRIARGEIGSPPTFVPHTITLLPLEKEHETFEIVYNSAKDLYKRFTGSYLEVSNWSSLVYSSENIFRKVEHDWKKVYLSRTPGSQVGSLTWKIDLNLVSRIVRENVLVYVTSTTYNNATVEWTISNEKNIQLNLKPGIKYDLNVFKNSAVLRLDVKLMGGDGENAWQHAQIFRQDFNSTDDAFFVKFRTREVLGDPGQLKF
The following text describes a protein:
Function:
Essential for tachyzoite invasion of host cells by controlling rhoptry secretion. Binds to phosphatidic acid (PA) and phosphatidylinositol 4,5-bisphosphate (PIP2) lipids and thus, likely contributes to the assembly of the machinery that docks or primes the rhoptry to the parasite cell membrane prior to the fusion with the host cell membrane.
Subcellular Localization:
Cytoplasmic vesicle, secretory vesicle, rhoptry membrane; Peripheral membrane protein; Cytoplasmic side. Note=Localizes to the extremity of the neck of the rhoptry. Associates only with mature rhoptries.
Domain:
The C2 domain is a non-calcium binding domain. Cooperates with the PH domain in the binding to phosphatidic acid (PA) and phosphatidylinositol 4,5-bisphosphate (PIP2); The PH domain cooperates with the C2 domain in the binding to phosphatidic acid (PA) and phosphatidylinositol 4,5-bisphosphate (PIP2).
Sequence:
MALVLRLMGGAAGMGAKAVGGACCELGSACFRQITKGLPHPTECGCLGSLFFYLGIHDHQKFNVLVEIHELDRVPKSCSLYMTIEAGRWSATSQVVKVKGQDQRVVVEERLMVHIRQVDNEVKIFLFKKGLVKTTRLANLVLKVKEDMIDKKFPKRTWYNMKVENGKSQPRINLSLHKLDPGLPTNQSPLLQQAMLIAQQEADEKGEELKLDLAKMTAKERLTFFSQVLEGPLERLNANGGACMQFYYKAVEVKPDRWEWCYWESAAACKEGKEKEGSIPFLAISLVLPDRKNRNVFFVRYHDKDNQHDVFFRRVDRDRNLWSDGLYEFIEKLRAYRETCSTRVPSQKGADGEEKKKKKKRREDGEDSSGEKSPRKSGGKKSRRPSTSPRLDISTARRLHSPRAQVPSKSPCAHQQMYEEVMISTQSSVVGDEEPQT
The following text describes a protein:
Function:
RING-type zinc finger-containing E3 ubiquitin ligase that assembles with melanoma antigen protein (MAGE) to catalyze the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE stimulates and specifies ubiquitin ligase activity likely through recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme at the E3:substrate complex. Involved in maintenance of genome integrity, DNA damage response and DNA repair.
Subcellular Localization:
Nucleus. Chromosome, telomere.
Sequence:
MSRQMGDGHRLFLQNMMTNGIVSAAQAGMLHKKCCELHGGQEKIDDFINVVNTHLQPLFMHIRKGMSEEDGQEHFVLMDLIVESDSGSASSTAILNSADKLISKKLKKKEAELVLNKFVQDKWLKEQDGEYTLSVRCIVEMEPYMRTIYQDMIKVCYVCHNIALQCQVCENPSCEIKVHLPCVARYFRARSDPHCPACNDFWPHEIPEMQAAQSQSSQNLPSSSKENTAPTQTRRSRRV
The following text describes a protein:
Function:
First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.
Miscellaneous:
MISCELLANEOUS: Present with 3900 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MSYTDNPPQTKRALSLDDLVNHDENEKVKLQKLSEAANGSRPFAENLESDINQTETGQAAPIDNYKESTGHGSHSQKPKSRKSSNDDEETDTDDEMGASGEINFDSEMDFDYDKQHRNLLSNGSPPMNDGSDANAKLEKPSDDSIHQNSKSDEEQRIPKQGNEGNIASNYITQVPLQKQKQTEKKIAGNAVGSVVKKEEEANAAVDNIFEEKATLQSKKNNIKRDLEVLNEISASSKPSKYRNVPIWAQKWKPTIKALQSINVKDLKIDPSFLNIIPDDDLTKSVQDWVYATIYSIAPELRSFIELEMKFGVIIDAKGPDRVNPPVSSQCVFTELDAHLTPNIDASLFKELSKYIRGISEVTENTGKFSIIESQTRDSVYRVGLSTQRPRFLRMSTDIKTGRVGQFIEKRHVAQLLLYSPKDSYDVKISLNLELPVPDNDPPEKYKSQSPISERTKDRVSYIHNDSCTRIDITKVENHNQNSKSRQSETTHEVELEINTPALLNAFDNITNDSKEYASLIRTFLNNGTIIRRKLSSLSYEIFEGSKKVM
The following text describes a protein:
Function:
Reversible hydration of carbon dioxide.
Sequence:
MTMKLSVLGQLFLVICCLTVVINAMPNPQAQAPSGALVATAESGHFSYDDPNKWKEHNSLCAGEHQSPINIDTRKSRTDKFPPFRFHNYAKGLPENLENNGHTVQLTIDNLIKDLPTISGGGLEGPYEFAQMHFHWGEDEFGSEHKINNKQYAGEVHIVHWNKKYGNFVNATKHNDGLAVLGILIDLQDKENIAFSHIEQFDEIRDASKKNEKLPYSVPLKDLLPSNTASFFRYEGSLTDARCNEDVTGPFLKHQFTSPIIRQLNDDEGEPLSKNVRPTQEEHDRIVTYSGRAMQCGTCSTATADRSSEGRSDSSESGESKEITKSKTRHYGY
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
Domain:
The RING-type zinc finger domain is essential for ubiquitin ligase activity; The SBD domain (substrate-binding domain) mediates the interaction with substrate proteins. It is related to the TRAF family.
Sequence:
MEDNLYDELLVELECPICTNYMSPPIRQCATGHSVCDACRNKLPKCALCQGAFTECRNHSLEALAVKMRYPCINKVSGCNAKLSYTERETHELRCPLKGFKCAMEKCTWVGRLEELAAHWASKKMSSKPYHKSNVCHTKMKSESYYVNMVNAYDRLFWFKCKLTKNKLYWAVQYIGNAAEAEGFYYEIEIFKPGRTKKRVLLSDYCQSIELENSQLFGDDSCICINTDAVNGFVSSDQLLIYYLRVNAIKDEKSEQAHGQVTDVAYKTDHGARQRDRSKGPPNLAKKDYKKKYNQHHNSKQNKQKEGFVLL
The following text describes a protein:
Function:
Has a role in transport between endoplasmic reticulum and Golgi.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MGSKHRTRAAPNPPPLFDDTSGGYSSQLGGYPAPGADVAFNVNNLLGDPVANMAMAYGSSIASQGKDIVHKELHRFVSINKLKYFFAVDTAYVAKKLGLLVFPYTHQNWKVQYSHDVPLPPRKDLNAPDLYIPTMAFITYVLLAGMALGIQQRFSPEVLGLCASTALVWVLMEVLALLLGLYLATVRSELGTFHLLAYSGYKYVGMILSVLTGLLFGSDGYYVALAWTSSALMYFTVRSLRTAASGPDSMGGPTPRQHLQLYLTLGAAAFQPLIIYWLTFHLVR
The following text describes a protein:
Function:
Regulatory photoreceptor which exists in two forms that are reversibly interconvertible by light: the Pr form that absorbs maximally in the red region of the spectrum and the Pfr form that absorbs maximally in the far-red region. Photoconversion of Pr to Pfr induces an array of morphogenic responses, whereas reconversion of Pfr to Pr cancels the induction of those responses. Pfr controls the expression of a number of nuclear genes including those encoding the small subunit of ribulose-bisphosphate carboxylase, chlorophyll A/B binding protein, protochlorophyllide reductase, rRNA, etc. It also controls the expression of its own gene(s) in a negative feedback fashion.
Sequence:
MQPKLQTNTSNPPQVYLFINMASGSKASSGFHPQQVQPQNPSTSSTPRVDSMSKAIAQYAVDARLHAVYEESGESGKSFDYSHSIKTATDSIAEQQMTAYLSKIQRGGHIQPFGCMIAIDNSSFRVIAFSENARERLGLAPQSVPSLEKTEILTIGTDVKTLFTPSSAILLERAFRAREITLLNPVWVHSKNSGKPFYAILHRIDVGIVIDLEPARTEDPALSIAGAVQSQKLAVRAISNLQALPGGDIKLLCDTVVQNVRELTGYDRVMVYKFHEDEHGEVVAECKRPDLDPYLGLHYPATDIPQASRFLFRQNRVRMIVDCHANPVPVIQDDCLMQPLCLVGSTLRAPHGCHAQYMANMGSIASLALAVIINGNEDSGGGRGTMGLWGLVVCHHTSARCIPFPLRYACEFLMQAFGLQLNLELQLASQMLEKRILRTQTLLCDMLLRDSPTGIVTQSPSIMDLVKCDGAALFYQGKYYAAGITPTESQIKDIVEWLLACHTDSTGLSTDSLADAGYPQAASLGDVVCGMAVAYITSKDFLFWFRSHTAKEMKWGGAKHHPEDKDDGQRMHPRSSFNAFLEVVKSRSLPWENAEMDAIHSLQLILRDSFKEERDSNSKAVVKIQSEEMGLQGMDELSSVAKEMVRLIETATAPIFAVDVEGRINGWNAKIAELTGLSVSEAMGKSLVQDLIFKESQEIVIRLLHHALQGEEDKNVEIKLRTFNLSEEENAIFVVVNACCSKDYTDNIVGVCFVGQDVTRQKVVMDKFVQIQGDYRAIVHSPNPLIPPIFASDENTCCSEWNTAMEKLTGWGRDDVIGKMLVGEIFGSCCRLKGPDSLTKFMIILHNAISGQDSDKYPFSFFDRRGKFVQALLSANKRVNLSGGDATGAFCFLQIASPELQQALKIQRQQENKCFARMKELAYICHEIKSPLSGIRFANLLLEATDLSEDQKQLLETSAACEKQMLKIIKDVDMENIQEGHLEVEKREFVVGSVIDAVVSQVMLILRDRGVQLIRDIPEEVKTLTVCGDQTRVQQVLTNFLLNMVQHSPSPNGWVEIQVRPSLKQVFDGITNAHIEFRMVCPGNGLPAELVQDMFQSSQWSTEEGLGLSMCRKILKLMNGEVQYIRESERCYFHIVIELPLPRGT