lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
Subcellular Localization:
Cytoplasm. Note=Assembles at midcell at the inner surface of the cytoplasmic membrane.
Sequence:
MMSRSELARASELSALKMVLVGVGGCGNNTVNNVKRYGVRVPTVAVNTDAPTLQRISADIKILIGEGAHKGRGAAGSPELGRQIAEQDMDKILAPLRDKELIMITAGMGGGTGTGAGPTIAEAIKEKFPDKIVIGIVTLPFTSEGPTRIRNAQWGLSRMLDSADMTVVNANDLLKERAGNLPVSQAFREMDKLLVDIIDSIVGLQDIVPQPGLVNIDYSNMEVLVRGSGLGFIGIGRGRSSMEAFRNALAANYSQADIRNAKGAIVYVEGNQSQLVMRELDRIPQMLSSDYNIMSIFWGIKPNWKLYEPKIMLLATGVRSELVDRWLQGGI
The following text describes a protein:
Function:
Copper metallochaperone essential for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Binds two copper ions and delivers them to the metallochaperone SCO1 which transports the copper ions to the Cu(A) site on the cytochrome c oxidase subunit II (MT-CO2/COX2).
Subcellular Localization:
Cytoplasm. Mitochondrion intermembrane space.
Sequence:
MSSLATATCESGSSDKPAKKPLKPCCACPETKKVRDACIIEKGEEHCGQLIEAHKECMRALGFKI
The following text describes a protein:
Function:
Hydrolyzes fatty acids from S-acylated cysteine residues in proteins with a strong preference for palmitoylated G-alpha proteins over other acyl substrates. Mediates the deacylation of G-alpha proteins such as GPA1 in vivo, but has weak or no activity toward palmitoylated Ras proteins. Has weak lysophospholipase activity in vitro; however such activity may not exist in vivo.
Sequence:
MASKLSSVIIPSVQKHTATVIFLHGLGDSGQGWSFLAQEWSHLKHIKWIFPNAPLAPVTVNGGMCMPSWYDIYSFTALDKEDEEGMMRSRNYVQGLIEAEMKDGIPSERILLGGFSQGCMISFLAGLTFPKTLAGLACLSGFLPIPETLKRLFRDEAKKTPIFLAYQSYDPVIPSALSAAAAKTLDSSFGCNVSSKCYDGFEHGLTPLSFKDLGTFVETVIGKP
The following text describes a protein:
Function:
Plays a role in the inhibition of host innate immune response by disrupting the interaction between NMI and STAT1. In turn, NMI-mediated transcription of interferon-gamma stimulated genes is inhibited.
Subcellular Localization:
Virion tegument. Host cytoplasm.
Sequence:
MSVIKDCFLNLLDRWRPPKTSRPWKPGQRVALVWPKDRCLVIRRRWRLVRDEGRDAQRLASYLCCPEPLRFVGSICTYNFLKHKGDHNVPSELYLGASGAMYLWTDHIYSDSLTFVAESITEFLNIGLRRCNFITVPEELPHTASLRALAGCMHIHAFAQWRATYRGRLMVMGDYSVIRVSTIRLYDWSEINDWRVMVGSNHVEPLGWLVSPYDVINLFVDDCMRVFAANNQHVCIVADSLMEFVTRGMTRCHENGIYYGTRSMRKLNKPTCPYGVDHQLFDDA
The following text describes a protein:
Function:
Required for replication fork blocking activity at the replication fork barrier (RFB) site in rDNA and for recombination hot-spot (HOT1) activity, regulating the recombination rate and the number of rDNA copies. Binds directly to two separated sequences in the RFB.
Miscellaneous:
MISCELLANEOUS: Present with 1510 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MTKPRYNDVLFDDDDSVPSESVTRKSQRRKATSPGESRESSKDRLLILPSMGESYTEYVDSYLNLELLERGERETPIFLESLTRQLTQKIYELIKTKSLTADTLQQISDKYDGVVAENKLLFLQRQYYVDDEGNVRDGRNNDKIYCEPKHVYDMVMATHLMNKHLRGKTLHSFLFSHFANISHAIIDWVQQFCSKCNKKGKIKPLKEYKRPDMYDKLLPMERIHIEVFEPFNGEAIEGKYSYVLLCRDYRSSFMWLLPLKSTKFKHLIPVVSSLFLTFARVPIFVTSSTLDKDDLYDICEEIASKYGLRIGLGLKSSARFHTGGILCIQYALNSYKKECLADWGKCLRYGPYRFNRRRNKRTKRKPVQVLLSEVPGHNAKFETKRERVIENTYSRNMFKMAGGKGLIYLEDVNTFALANEADNSCNNNGILHNNNIGNDNFEEEVQKQFDLTEKNYIDEYDDLAHDSSEGEFEPNTLTPEEKPPHNVDEDRIESTGVAAPMQGTEEPEKGDQKESDGASQVDQSVEITRPETSYYQTLESPSTKRQKLDQQGNGDQTRDFGTSMEL
The following text describes a protein:
Function:
Responsible for synthesis of pseudouridine from uracil-54 and uracil-55 in the psi GC loop of transfer RNAs.
Sequence:
MTILEDARAVLAETPVCDACLGRCFAERSFGLSNAERGRALRTAVALADDEPYEEPEEPCWVCEGASGRFDEFADLVVDAVADASFDTYQVGTQAPPLVEENEAMLRDLAGLAEDAGEPFKSECNREVGKRVGDRTGTEVDFGRPDVLAVIDVEAETVDVTVNSAFVYGRYRKLERGIPQTKWPCSDCNGSGTLVDSPCPHCDGTGFLYPESVEQLTAPPVVDAMGGTEASFHGAGREDIDALMLGTGRPFVIEVAEPQDRHPDADALADAINDFADGKAEVEGVAVAGYEMVERVKELDARKRYRADVEFDAPVGDDDLRDAIDELDGATIEQETPNRVDHRRAHLVRERDVYDITADREDDTHATVEIEGEGGLYIKELVSSDDGRTNPSLAGLLGVGAVVTALDVVAVAGETEAFEDTEHLP
The following text describes a protein:
Function:
K(+) channel that conducts voltage-dependent outward rectifying currents upon membrane depolarization. Voltage sensing is coupled to K(+) electrochemical gradient in an 'ion flux gating' mode where outward but not inward ion flow opens the gate (By similarity). Homo- and heterodimerizes to form functional channels with distinct regulatory and gating properties (By similarity). In pancreatic islets, conducts K(+) countercurrents for Ca(2+) release from the endoplasmic reticulum (ER) and regulates the frequency and duration of cytosolic Ca(2+) oscillations coupled to secretion of pancreatic hormones. In pancreatic beta cells, drives ER Ca(2+) efflux, which in turn activates Ca(2+)-dependent plasma membrane K(+) slow currents and cytosolic Ca(2+) influx, overall contributing to synchronous cytosolic Ca(2+) oscillations. Limits glucose-induced cytosolic Ca(2+) oscillations coupled to second-phase INS secretion. Contributes to beta cell adaptation to acute inflammation by maintaining normal cytosolic Ca(2+) levels and INS secretion. May regulate beta cell mitochondrial Ca(2+) levels either indirectly via ER Ca(2+) efflux or directly by hyperpolarizing the mitochondrial membrane potential. Limits mitochondrial Ca(2+) oscillations and ATP production involved in glucose homeostasis upon metabolic stress. In pancreatic delta cells, limits Ca(2+)-induced Ca(2+)-release involved in somatostatin secretion and modulates islet paracrine signaling involved in glucagon secretion. Permeable to other monovalent cations such as Rb(+) and Cs(+) (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion inner membrane; Multi-pass membrane protein.
Domain:
The pore-forming domains 1 and 2 assemble to form a single pore in which M2 and M4 transmembrane helices line the central cavity and M1 and M3 face the lipid bilayer. The transmembrane helices are bridged by the selectivity filters 1 and 2 carrying a signature sequence TxTTxGYGD that coordinate the permeant ions. Up to four ions can simultaneously occupy the selectivity filter and at least two elementary charges must translocate across the filter to convert it into the open conformation.
Sequence:
MPRAGVCGCWGGQVLPLLLAYICYLLLGATIFQLLEKQAEAQSRDQFQLEKLRFLENYTCLDQQALEQFVQVILEAWVKGVNPKGNSTNPSNWDFGSSFFFAGTVVTTIGYGNLAPSTEAGQVFCVFYALMGIPLNVVFLNHLGTGLRAHLTTLDRWEDHPRHSQLLQVLGLALFLTLGTLVILIFPPMFFSHVEGWSFREGFYFAFITLSTIGFGDYVVGTDPSKHYIAVYRSLAAIWILLGLAWLAVVLSLGSLLLHRCSRLWQLIRGLDLKDGAAPDSEPRSQKIPISA
The following text describes a protein:
Function:
Transcription factor binding to G-box elements (5'-CACGTG-3') in target genes promoters, particularly in far-red light but barely in the dark. Required during the fertilization of ovules by pollen. Repressor of phytochrome A-mediated far-red light responses including seed germination, suppression of hypocotyl elongation, and randomization of hypocotyl growth orientation. Does not inhibit phyB-induced red light responses.
Subcellular Localization:
Nucleus.
Sequence:
MSQCVPNCHIDDTPAAATTTVRSTTAADIPILDYEVAELTWENGQLGLHGLGPPRVTASSTKYSTGAGGTLESIVDQATRLPNPKPTDELVPWFHHRSSRAAMAMDALVPCSNLVHEQQSKPGGVGSTRVGSCSDGRTMGGGKRARVAPEWSGGGSQRLTMDTYDVGFTSTSMGSHDNTIDDHDSVCHSRPQMEDEEEKKAGGKSSVSTKRSRAAAIHNQSERKRRDKINQRMKTLQKLVPNSSKTDKASMLDEVIEYLKQLQAQVSMMSRMNMPSMMLPMAMQQQQQLQMSLMSNPMGLGMGMGMPGLGLLDLNSMNRAAASAPNIHANMMPNPFLPMNCPSWDASSNDSRFQSPLIPDPMSAFLACSTQPTTMEAYSRMATLYQQMQQQLPPPSNPK
The following text describes a protein:
Function:
May function as a transcriptional activator protein and may play a key role in the organogenesis of the fat body. Binds a sequence element (5'-[TA]GATAA-3') found in the larval promoters of all known alcohol dehydrogenase (ADH) genes. Acts as a homeotic gene downstream of the terminal gap gene HKB to promote morphogenesis and differentiation of anterior and posterior midgut. Together with transcriptional cofactor Bfc directly binds the promoter of phagocytic receptor crq/croquemort to upregulate its expression and stimulate efferocytosis in response to apoptotic cells, including during embryogenesis.
Subcellular Localization:
Nucleus.
Domain:
The GATA-type Zn-finger domain is required for binding DNA and interacting with Bfc. Isoform 2 differs from isoform 1 in that it has an additional zinc finger domain. It is unknown if both zinc fingers are required for DNA binding or interaction with Bfc (Probable).
Sequence:
MTKTTKPKEKAAAGGAVIGSGSGLGSVTKAGGGSLLSNAADSKIRTAKSNNNKRQAGRAATALAATTTASALAATTTAGATGSNAAANETEIAIETENGEAATPTAAATAAAANLSSLESARSQALTSVVSETARQAVTTANASATSTSTVTAATEIATATASDTAATSEAAIDDDPSAINTNNNNNNSKAQNDASESVKTKVISYHQSEDQQQQQQQQAQIYEQQQQFLSQQLISHHQQEQHQQAQQQQHQQVVQEQHQASWLAYDLTSGSAAAAAAAAAAASHPHLFGQFSYPPSHHTPTQLYEHYPSTDPIMRNNFAFYSVYTGGGGGVGVGMTSHEHLAAAAAAAAAVAQGTTPNIDEVIQDTLKDECFEDGHSTDYHVLTSVSDMHTLKDSSPYALTHEQLHQQQHHHQQQLHHHQQQQQQLYHQQQQQQQQQQHHHHHNNSTSSAGGDSPSSSHALSTLQSFTQLTSATQRDSLSPENDAYFAAAQLGSSLQNSSVYAGSLLTQTANGIQYGMQSPNQTQAHLQQQHHQQQQQQHQQHQQQQLQQQQQQHHHNQHQHHNSSSSSPGPAGLHHSSSSAATAAAVAAATAAVNGHNSSLEDGYGSPRSSHSGGGGGGTLPAFQRIAYPNSGSVERYAPITNYRGQNDTWFDPLSYATSSSGQAQLGVGVGAGVVSNVIRNGRAISAANAAAAAAADGTTGRVDPGTFLSASASLSAMAAESGGDFYKPNSFNVGGGGRSKANTSGAASSYSCPGSNATSAATSAVASGTAATAATTLDEHVSRANSRRLSASKRAGLSCSNCHTTHTSLWRRNPAGEPVCNACGLYYKLHSVPRPLTMKKDTIQKRKRKPKGTKSEKSKSKSKNALNAIMESGSLVTNCHNVGVVLDSSQMDVNDDMKPQLDLKPYNSYSSQPQQQLPQYQQQQQLLMADQHSSAASSPHSMGSTSLSPSAMSHQHQTHPHQQQQQQLCSGLDMSPNSNYQMSPLNMQQHQQQQSCSMQHSPSTPTSIFNTPSPTHQLHNNNNNNNNSSIFNNNNNNNSSSNENNNKLIQKYLQAQQLSSSSNSGSTSDHQLLAQLLPNSITAAAAAAAAAAAAAIKTEALSLTSQANCSTASAGLMVTSTPTTASSTLSSLSHSNIISLQNPYHQAGMTLCKPTRPSPPYYLTPEEDEQPALIKMEEMDQSQQQQQQQQHQQQQHGEIMLSRSASLDEHYELAAFQRHQQQQQQLQQQTAALLGQHEQHVTNYAMHKFGVDRETVVKME
The following text describes a protein:
Function:
Involved in DNA double-strand break (DSB) repair and recombination. Promotes the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase.
Sequence:
MTTSYLDTENDNDIDDNEEEEEEELANLPSTVKFFPNLSDLLDDEEYQDDDDDDGTNNNNTVINEWALRKFGTLQMKLEKMQHSRDTFQSFGSRDNLTNFSRNILYNLANEVFGFDGWSTTILDCNLTKRENKDENKYSALCVVKIRLILKDGTFREQSGQAESTNMPYKHMCYASARKKAVTDAIKNAIVGLRDLYLEYEQEQLMKQFAPEYDI
The following text describes a protein:
Function:
Orphan receptor; could be a chemoattractant receptor.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MDLINSTDYLINASTLVRNSTQFLAPASKMIIALSLYISSIIGTITNGLYLWVLRFKMKQTVNTLLFFHLILSYFISTMILPFMATSQLQDNHWNFGTALCKVFNGTLSLGMFTSVFFLSAIGLDRYLLTLHPVWSQQHRTPRWASSIVLGVWISAAALSIPYLIFRETHHDRKGKVTCQNNYAVSTNWESKEMQALRQWIHVACFISRFLLGFLLPFFIIIFCYERVASKVKERSLFKSSKPFKVMMTAIISFFVCWMPYHIHQGLLLTKNQSLLLELTLILTVLTTSFNTIFSPTLYLFVGENFKKVFKKSILALFESTFSEDSSVERTQT
The following text describes a protein:
Function:
Aquaglyceroporin that may modulate the water content and osmolytes during anhydrobiosis.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MGVFQDKVASILRIEDQQFTRELLAECIGTFFLLLIGNAANIQAAVAVGGNSTSCHIAWGIGFMFAVYLAASVSGGHLNPAISVAQSILGNLPPWKIIPYAIAQVIGAFLGAAVAYFGHHDDLWKLDGGIRQVTGGQATAGLFTTFPPDHMSVWGSLLDQIIGTAMLSGLVCLITDKRHQIPTGVVPVLAGSIMSMVAMTFGANGGFAINPARDFGPRVFCLCAGYGWEVFSAHGYYFWIPIVGALIGSIIGAWIYKIFVGLHGMNESLDIQPAKGFNEMQRNSEGILIGYDNTLSRARGGEIAAPRTYTPSYQVFESSRTQITTADRRY
The following text describes a protein:
Function:
May have an RNA/DNA binding role.
Sequence:
MSEKQSPKTSEAECSAMDLPEFEDEENWLFKVLGFQPGPSSALDDDTDDQADEPLSAAEFLHLQDILQEDRVSSTDDEDTCQAGCTEDDETSHSDRDIDNNVKVITGNIKASPSMYMEMFTDQNPQADQDLEETESDGAMNPTD
The following text describes a protein:
Function:
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP43 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation.
Miscellaneous:
MISCELLANEOUS: Present with 3180 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus.
Sequence:
MAESTTLETIEIHPITFPPEVLARISPELSLQRHLSLGIRPCLRKYEEFRDVAIENNTLSRYADAGNIDTKNNILGSNVLKSGKTIVITSITGGIIEETSAAIKDLDDFGEEELFEVTKEEDIIANYASVYPVVEVERGRVGACTDEEMTISQKLHDSILHSRILPKKALKVKAGVRSANEDGTFSVLYPDELEDDTLNETNLKMKRKWSYVLYAKIVVLSRTGPVFDLCWNSLMYALQSVKLPRAFIDERASDLRMTIRTRGRSATIRETYEIICDQTKSVPLMINAKNIAFASNYGIVELDPECQLQNSDNSEEEEVDIDMDKLNTVLIADLDTEAEETSIHSTISILAAPSGNYKQLTLVGGGAKITPEMIKRSLLLSRVRADDLSTRFNI
The following text describes a protein:
Function:
Translation activation factor that as part of the MRH5C complex specifically recruits cox1 mRNA to the mitochondrial ribosome for translation initiation.
Subcellular Localization:
Mitochondrion.
Sequence:
MKCCPASILDRFNAIKVINVMGLRLNGRSVPWLLQTRKFINITSPRYTAGRPVILNENQLIRYLPNYTNKGDEEVTRRKKLHEPNGPKFHELPLNQNILDGLSTNFAEYKNSTPLQQRIINALMKSGVSFIVRGWNGSGKSFGAMLSTLSMYFEALKFLKHNPVAGKPVQSGCQVLFIVPNDNLAAQYQFWIERLLHGITEKEELQHIYKILTLTPASLDSFQNRPPYIGITTFPNLQHCIKKNQPILKQFTSQLQLLIVDESDLVIPDHGRSRRLSSPEILADKIFLSSFIQLCKKNLRINMDDENVGGMGIHSQLHGKGSIPTMVFMSASNSKNGVNYLSRYITDQLGIIGIDRKHQWYWNLTSTPSVFHYLIKAQAEPKTTKVTLTNLPYEFVRFNNSMHSIGDNNFSYNNSEAVLQIFAQSVPRILNIEAKKSKLENNILKCVMIVLPKEFNPHSFCNQYKGFAVGNRFWQCRTLSTESLNFSTNLNNVVFVANPSEIRGLHLPSITHIFHLWSTFSGVAYQHIAGRLGAMGQTGKIFNFIIPDYYKSNDFKKTDFRRCILFMLQRVGIRPKSYEFDDEHF
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.
Subcellular Localization:
Cytoplasm.
Sequence:
MKQKQGFGQSLMQMMTNTAFQLDKMWSEDIKIDELMYIFGQEIQNAEAFNQKKDTLIWFCYRANIQFEGKAISDQGWGCLVRVGQMMLANALMRECKILAINKTKAMIIHLFDDNQEYSTIAPFSIQQIIKRASINLNMKIGDWYTGPKIMSVIEDLNKNNMNIKQINLVNFLEQCVLESQIDLSFKKPHLLIIHAIIGDKSLGQLEIQNLQSHMQISQFAGAIIGKNNKAFFLIGFQKNNAIFMDPHYVQESNKIEMECNLKCQPLKQLNGTIALAFYISNYMEYLEFKKQVNKLQGSIFSIIEDIGYKFT
The following text describes a protein:
Function:
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins. The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK. The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF. 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG. The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme. The cytochrome P450 monooxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone. The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone. The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin. The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin. The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MAFLSLPILTALGAVVYVLFQLVYNLYFHPLRDYPGPLLWRASSLPWKLTLLRGTMHHDLMRHHQTYGDTVRIKPDEISYANGQAWRDIHAHVPGRPEFLKDPVRLPLAPNGVMSILVSDTRNHARFRSLFGHAFSDKGLRAQEPTIARYADLLVEVLREVADTGKSVEMVRYFNMAIFDSIGALSFGESFDSLRNRELHPWVDTIHKNLKSVAISHVLRSMGVEFLAPYLMPAELRGKRQENYTYAIEKLKKRMQKTGDQGDFWDRVIVKSADGNQSGDGMSYGEMINNAAVMVVAGSETTSSALCGCTYLLCKFDKMDKAVAEVRGAFAAADQIDLVSVSRLPYLTAVIDETLRMYPSVPGQPPRVVPEGGAIVCGRFVPAETRVGVSHLGAYYAPYNFSHADKFIPERHLAGAKLEEPFRHDNYAAYQPWSVGVRNCIGRNLAYAEVRLTLAKLLWHFDISLDEERTGNFLDQKIWSIWAKRELYLEIRTREF
The following text describes a protein:
Function:
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Subcellular Localization:
Cytoplasm.
Sequence:
MSKAKDTGILRFDDTPLAATFPLVAIITSKVVGGVKIVGRKGLDSTEFSIVGTQDSLKGSYVIAKYLARTTPSLSLYGENALSASKIDEFIDKFAHLKSEKFNEFLKEMNEYLTLRAFLIGFNLTLADIVLFARIKMVKEIQEEINKLGKTIPHLNRWYGYLSQLESFVEADNAFNGKKETKASGKAGAEGTAATTEKVAPQKGAMGWVGNFEALNLPGLVEGKVVTRFPPEPSGYMHIGHCKAAIINNYYAEKYNGKIIIRFDDTNPSKEKEEYVENIIKDINNLGIKYEKITHTSDYFDLIHDYAIQMIKEGIAYCDDTPQVKMSEERDNAIESVHRNNSVEKNLEMFDEMKKATEQGVKCVLRAKLDMAHIDKAFRDPAIYRCNSTPHHRTGDKYKVYPLYDFACPIVDSVEGITHALRSNEYNNKRNLYNHYLEILHLENKPYISDYSRLSFFNVLLSKRKLQHFVDTGLVSGWTDPRLPTLQGITRRGLTVAALKEFILSQGASAANTTLDLGKLFVGNKAVLEPTCPRYTAIAKATAVKFTLSNGPTLPEVKDCLKYAKDPSMGTKKVTFSNNLLLEGDDCNQIKEGEEVTLMNWGNAIVETLQRNENGDVVSMTGKLHLEGDVKKTDKKLSWLSSDCADTVTVVLQDYDYIITKPKLEDGDDLDTFTNKNSKFEIEAFTDENILTLKLNDKIQFERRGFFNVDQVGDGVKPYILIYIPSGPIKPAGAALYPFKKVEKVAAPVNPKPTAKKQEKQSKK
The following text describes a protein:
Function:
Involved in yeast cell wall biogenesis.
Subcellular Localization:
Membrane; Single-pass membrane protein. Note=Localizes to the cell periphery under conditions of vegetative growth.
Sequence:
MNSAGRVHRSRAGSRGHAAISPLTMASFSVARGIRSSNVYDDTDDELSILTFFSAVRRNRLTSSLPPILSARCSSACFSVRIVLPLSLTISISALMYSTNSALGRKLTGAFSIQTNIEQSCGFFRTSIMATLPPIECPIIIGPPLVFNSCFVIKCFTSSDMTS
The following text describes a protein:
Function:
Catalytic subunit of the glycosylphosphatidylinositol-mannosyltransferase I complex which catalyzes the transfer of the first mannose, via an alpha-1,4 bond from a dolichol-phosphate-mannose (Dol-P-Man) to the glucosaminyl acyl phosphatidylinositol (GlcN-(acyl)PI) intermediate to generate alpha-D-Man-(1->4)-alpha-D-GlcN-(1->6)-(1-radyl,2-acyl-sn-glycero-3-phospho)-2-acyl-inositol and participates in the sixth step of the glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MIDTPKDIHLFWHTFNTKNVWISSFEKILFSFVDMLACVFMQKLVKSTFLLNLWIFNPLTIQVSTRGSSDTIIVLLIYVILYLLKKESYVLAALIYGFTSLQILISQKECKINDILIYLGLISGLFIALLIFFHLIYEEFLYQTYLYHFTRIDNRHNFSTYFYQIYLSFESITRTQTTLTYLPKFLIVILAGLKYYRDLPFAMLIQTLGFVVFNKVQTAQYFVCWIALIPLALQNTKMNNKEILMLSVIWLILEVQSNFGSYYLEIQGKDVFTMIFVQCVIFFLSNTYLMIKMIENRKPSEIYKIKMD
The following text describes a protein:
Function:
Toxic component of a type II toxin-antitoxin (TA) system. A probable translation-independent mRNA interferase. Overexpression causes cessation of cell growth and inhibits cell proliferation via inhibition of translation; this blockage is overcome (after 90 minutes) by subsequent expression of antitoxin HicB. Overexpression causes cleavage of a number of mRNAs and tmRNA, in a translation-independent fashion, suggesting this is an mRNA interferase.
Sequence:
MKQSEFRRWLESQGVDVANGSNHLKLRFHGRRSVMPRHPCDEIKEPLRKAILKQLGLS
The following text describes a protein:
Function:
Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development (By similarity). Binds iron through association with 2,3-dihydroxybenzoic acid (2,3-DHBA), a siderophore that shares structural similarities with bacterial enterobactin, and delivers or removes iron from the cell, depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor, leading to release of iron and subsequent increase of intracellular iron concentration. In contrast, association of the iron-free form (apo-24p3) with the SLC22A17 (24p3R) receptor is followed by association with an intracellular siderophore, iron chelation and iron transfer to the extracellular medium, thereby reducing intracellular iron concentration. Involved in apoptosis due to interleukin-3 (IL3) deprivation: iron-loaded form increases intracellular iron concentration without promoting apoptosis, while iron-free form decreases intracellular iron levels, inducing expression of the proapoptotic protein BCL2L11/BIM, resulting in apoptosis (By similarity). Involved in innate immunity; limits bacterial proliferation by sequestering iron bound to microbial siderophores, such as enterobactin. Can also bind siderophores from M.tuberculosis (By similarity).
Subcellular Localization:
Secreted. Cytoplasmic granule lumen. Cytoplasmic vesicle lumen. Note=Upon binding to the SLC22A17 (24p3R) receptor, it is internalized (By similarity). Releases the bound iron in the acidic lumen of cytoplasmic vesicles (By similarity).
Sequence:
MGLGVLCLALVLLGVLQSQAQDSTQNLIPAPPLISVPLQPGFWTERFQGRWFVVGLAGNAVQKERQSRFTMYSTIYELQEDNSYNVTSILVRGQGCRYWIRTFVPSSRPGQFTLGNIHSYPQIQSYDVQVADTDYDQFAMVFFQKTSENKQYFKVTLYGRTKGLSDELKERFVSFAKSLGLKDNNIVFSVPTDQCIDN
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:
MAGSSTDPTQQLNDYIRTMHDQGILDDNFDQLLALRREQNPRFITELISMFTNDAEAYIAEITNALSLTEVDFSTIISKLHQLKGSTFGIGGHRMYQACCELRVAAADGDKDRCDELFLRVKEEFNTLKQCFDSISEMRRNIISNGTRRRRRRPL
The following text describes a protein:
Function:
Regulates ion channel activity and transmembrane ion transport. Regulates ASIC2 and ASIC3 channel activity.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell membrane; Lipid-anchor; Cytoplasmic side. Membrane raft. Melanosome. Cytoplasmic vesicle. Note=Localizes to juxtanuclear structure probably derived from the Golgi apparatus. Colocalizes with cortical actin microfilaments at small plasma membrane protrusions. Associates with alpha-granular lipid rafts. Translocates from the alpha-granular lipid rafts to the cell membrane on thrombin activation and selectively enriched in released microvesicles. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Sequence:
MSDKRQSSHVQSQRIPESFRENSKTELGACGWILVAASFFFVIITFPISIWICIKIVKEYERVIIFRLGRILQGGAKGPGLFFILPCTDSLIKVDMRTISFDIPPQEVLTKDSVTISVDGVVYYRVQNATLAVANITNADSATRLLAQTTLRNALGTKNLSQILSDREEIAHHMQSTLDDATDDWGIKVERVEIKDVKLPVQLQRAMAAEAEAAREARAKVIAAEGEMNASRALKEASMVITESPAALQLRYLQTLTTIAAEKNSTIVFPLPVDMLQGIMGSNH