lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in the regulation of vernalization (By similarity). Binds to DNA in vitro in a non-sequence-specific manner. XLG2 promotes the DNA binding activity of RTV1 specifically to promoter regions of FT and SOC1 in vivo and thus leads to the activation of floral integrator genes.
Subcellular Localization:
Nucleus.
Sequence:
MQMDSAQNQFNKRARLFEDPELKDAKVIYPSNPESTEPVNKGYGGSTAIQSFFKESKAEETPKVLKKRGRKKKNPNPEEVNSSTPGGDDSENRSKFYESASARKRTVTAEERERAVNAAKTFEPTNPYFRVVLRPSYLYRGCIMYLPSGFAEKYLSGISGFIKLQLGEKQWPVRCLYKAGRAKFSQGWYEFTLENNIGEGDVCVFELLRTRDFVLEVTAFRVNEYV
The following text describes a protein:
Function:
Histone methyltransferase. Methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression. The silencing mechanism via DNA CpNpG methylation requires the targeting of chromomethylase CMT3 to methylated histones, probably through an interaction with an HP1-like adapter. By its function, KYP is directly required for the maintenance of the DNA CpNpG and asymmetric methylation. Involved in the silencing of transposable elements.
Miscellaneous:
MISCELLANEOUS: Mutations in the KYP/SUVH4 gene decrease the level of histone H3-K9 dimethylated, trimethylated or dimethylated in association with H3-K14Ac by factors of 4,3 and 3, respectively. The level of monomethylated H3-K9 is unchanged. Such mutations lead to a drastic decrease of cytosine methylation at CpNpG sites, causing the reactivation of endogenous retrotransposons. The KRYPTONYTE methyltransferase name was given according to its involvement in SUPERMAN gene silencing.
Subcellular Localization:
Nucleus. Chromosome. Chromosome, centromere. Note=Associates with centromeric constitutive heterochromatin and at a lower level with regions of euchromatin.
Domain:
Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity; In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.
Sequence:
MAGKRKRANAPDQTERRSSVRVQKVRQKALDEKARLVQERVKLLSDRKSEICVDDTELHEKEEENVDGSPKRRSPPKLTAMQKGKQKLSVSLNGKDVNLEPHLKVTKCLRLFNKQYLLCVQAKLSRPDLKGVTEMIKAKAILYPRKIIGDLPGIDVGHRFFSRAEMCAVGFHNHWLNGIDYMSMEYEKEYSNYKLPLAVSIVMSGQYEDDLDNADTVTYTGQGGHNLTGNKRQIKDQLLERGNLALKHCCEYNVPVRVTRGHNCKSSYTKRVYTYDGLYKVEKFWAQKGVSGFTVYKYRLKRLEGQPELTTDQVNFVAGRIPTSTSEIEGLVCEDISGGLEFKGIPATNRVDDSPVSPTSGFTYIKSLIIEPNVIIPKSSTGCNCRGSCTDSKKCACAKLNGGNFPYVDLNDGRLIESRDVVFECGPHCGCGPKCVNRTSQKRLRFNLEVFRSAKKGWAVRSWEYIPAGSPVCEYIGVVRRTADVDTISDNEYIFEIDCQQTMQGLGGRQRRLRDVAVPMNNGVSQSSEDENAPEFCIDAGSTGNFARFINHSCEPNLFVQCVLSSHQDIRLARVVLFAADNISPMQELTYDYGYALDSVHGPDGKVKQLACYCGALNCRKRLY
The following text describes a protein:
Function:
As part of the central apparatus of the cilium axoneme plays a role in cilium movement and thereby cell motility.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium axoneme.
Sequence:
MAQPETLHQVLAQPADASRVKQLQTVHEAITASLSGQQPGARVGLETLVLCAEAALKVGSLDVAHDCLERYFLEQRRYTVGMAPVELRDQYLCRAHFARGLLVSERSKGLKGKALIDGTLEGVKHVMAGLEVAAANQPRYQFLVYNASVHHWRVVAPLHRDGLRHHLLASTDRVVQALDKVPGHEEWKVRIYTALALCQSDAATVAAAQAEAAGGKAPAKGGGGAAATHDDAAKTLQRAYDTAAAAKLTELQKDVARLQVHLATLAAAAGGKGAKAGGGGAAGGAGKPGAKGAAAALDEEGALRLIQAVLTGRPDRAVAEQQLREAVAKVDPKGPDGPVKGALLRPVSRAAWAAALAGLPELAERWASRAAASSDSGPRTWSDMTRVQLALQALGPAGDTSLAPVVVAAHVKALEQLEDVLTTFTKLADVEGIHAAARLAWNAGLLLLQPGLRKHVKRAFNAAARALAVAASPLTRLRAALHLEAGKCDAAEEALIKAGQEVGKALALDYLPPPAEAAAVPWLARPLDRWAAPLARALALRTSAEPANPEEEAVSLIERSKESRNPAIKSDLLARAREKLRDLPHPPPPAPTDPPGPDRDAAHAAARRRTAVWAELMRSAASSRMDEHVLAAAPHALCVSWDPAVDREMVLLQAQLAHYEAEAAISALRRRRADISPPTRPSPPEVDGEGVRQPPATTEQLQELVVQASVRSMRGAMSVNEPWLTLNNAVQLYNAALPLMQQHRYADLYRWLRPVAEALVALPVADSDGPLAVAVAEALGRAAEHRLLLATLRAKAARDAGQELEDDDDEDSLDEDGNPPPAGDAGPHFNRRSPAYKPLPDARVAASGLDPRGFPALARLLASIGTVTAVAEAALERAGGASTQGLLEMYARLQQYRGVSSGLPAGAAAASAATSRVVSAIEALSSANRVNEEKQPAGAGAEKGGGDKGRKPHGSLAADAAAAIALLRALPGGPPLELWAKMARAVADAGVWPAALECSAAALAALPGAGRDLDVLRLEAPSDVPEMTPAGWFWASVALSVRAAALLTLVDLPSQGAATALTVRREALLHAAQAARCAAFVNKADLCESACRVAWNAALPFTTKPLLRAALIRPLGTAVEALNRVGPADKGFQVRMNCLYVESLAAAKRWGDAVAACDAASRAVKSRSLHRPLMGWKAACLAMLGKNVNAEMTKVKEHPPEAQAYAWSVLSHHSAARYDQIAAHKAAGEAVEHHGWLKAVALAGYAEWLLSSSDDKEAAEDALLAAADALLEFDTGDLDGDGTDDEDDATKAKPRSRSGGGSSSGRAGGGFRRVLSRSYSRGGGGSADGARPSEGGEGAGPAAPDPNRVPEELGSTHLERLARLYVMACQAAPNATDHTDYMLAAHHNFMRLLTQALHSAAHTAFVAARDSYNGEVAAAALEGRDPPPETPLPKPYAVVPDTLIGWGTWQITPELLETLASDAATGAVTALSRELLPQAELTLAYLELLQACLRARGYHCHCLGLAQLQRVLARMVLRDEGMYVATSLGLVAALDELGLSREAGEVEAALGDVACIGPQEEAQAAEQAALADLVLAAAGKLEAARPRSALAVGRLSFLAGGVRRANNAANAAAAAPLPPVAAASQAAAAADAAAAASFTAAGGGRGGRESPSPHDDGIHYIGGPAPGDSHGQLPEWMEDAARELGNVDLAGSAGGLLSHVSGQLLLRPFTLHDVWLKKGDYLLRRGHYAAARQLLSRARAHAADCGNREAEARCLLALSRTELAAHNPVEAVALVQAAQRFGGDIDFWAELLVQYVDCRLAGAHSTTSDAREALQGGIAMFLALARDDRAAEKPASAAGAVLRVRLARLLLTDMEMLRGQGVSTWRKSYDGAVTLVNQAIMALAAREAGLPHIEALLVQAELMLAEPTHIKDLRPRLKKVEKVLLAAEEMAVRFHAEATPRDLAPRCVTPTARLLACVRCRLAEVQLAAAEERERLAGADREKARPKFPHMRGKRDVQVVIDFIDEAGGAPPAPPGLLPEDSALALATGAAALVAAAPRDRARALLIAGRCLAFKFMMAAPEALDPLRPFVPPPKPPGAPKRPPAGAEEEEDEEGPDTAAADAAAEAAEAAATPEGAAALRLQAQAAAMLSSALASATSVQDWALGEQCALALSTLYGQLSPGLACRSLAAAQACRAAAGGQALLRAAAPAQQPEVLALAQRDKLSEVLPAPQDNVHYSALRRMLSGLKGAAARLDAAAAPPVEQQLAALPQDLRVLMLYLSPDGGRLYAAALNIPDATAEPTPPLNAEKSKKKTDASAPAAAGPRLSLLHVVEVDPAAVEALVAECRAYRRGVERTLREAIASAAAKGVGVPPEDDRPDSPSKKGKKPGSATKRPGSKQGPKSGPGAAAAAAAAAAAAGEAGKVQVFDSRLNEEWSGILEQFEEWLAPLAPWLEAAVPALPLPPPGSPDGKKEKKDKKEAAGPTKHKVALLLDPALQSLPWEAARHLATTCSEVSRSPSLQALAACHTLPRADSAAASEHAAAAAAAPAALPPLDLGRLTVIVDPRHECSTAQQARGPYTAQLIPALSAPELTQVLPAASWWGPGGPGGGLEGVPGRAPSPDTYASLLAGQATGGPCTGLLFLGVGRFAAHVPPAVLASAPLGGCEAALLFDRCNTDDAYWAQLYRDNRKSAEQRRLESPGRVATLLLAKGVRTVLVMSAAAPPAAVVKLMHGVMAGLAAGRVLGEVVYSLLTGGGGSGGAGAGVLDEFELAHLRACLQVWGAPGLLGAVLTQGNKAAKGAKK
The following text describes a protein:
Function:
RNA-binding protein involved in pre-mRNA splicing. Interacts with the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome. Involved in regulating splice site selection. Binds preferentially RNA with A/C rich sequences and poly-C stretches.
Sequence:
MADQRKKQSKWDVSSADVANPVKSAAEAAKERAAKLNAMLAAKGKLAKETGAILPLVKTQASVPLMGHKPDKDMEPITAEVEINDSPARVILCRGTTQDEISKYSGAAVSTKGCYMDAEEKAHALREDSGKRPLYLFVQGPSQAKVDLAIKRIHEIIGGADIHGKLHSNQGITPYPNMVSVTTAPSSTPSSLLIGQSSADPLPTGMHYVQDKLFVGLTYAPAEFNLKDKLLGPGVHNVIIAEINRNNFEGLELQANLKKDHIFSTLQQRLVQSHNKMEGLAAAKKLVENLIQTVHTEYQNFEMMKRSQPMGYGPHGGYPPIPPHGFQPPPHGYVPPPGGPHPPAMYPPIPPMASYYNQPLPGQPPPGHPVSHPVPPPGCPPQTQGGVTFGNDPALSGGQPAPPGGPLPPGGPLGPGGALPPVSGPPVLPSPNTTSYPYPDLPPPHAEPSSGGPYPQWTGPPGAQRPPGSEKPQLGREEGYPGFEELPDEDIHRHHEAPPPPQEFGRRRFKEKVVSGSGESRAERRSERRKPVRYPLNQQSSRHPAELPPGPHRQPTPSTRHPAPAPPPHILLSKETEKSEQAMPPPEMPASKKDVTKSRGVPFKEPMAKPISFKPAKPVAFVSKSSLSTLSSMEKDKAVTGKKHSVASPLGKILLKKKTDEPAAKKPKSSALSSLVAYDGDSSDEEEEEPSADSKHDSHSSNGASKQRLPFWAVRK
The following text describes a protein:
Function:
Plays a role in the regulation of neuronal activity.
Subcellular Localization:
Nucleus membrane; Multi-pass membrane protein. Rough endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MKRRNTEAGKPPRRPVKRAGKFAEGVCGSSFVYIKFVTIWLFILLADFILEFRFEYMWPFWLLLQSVYDTFKYQGLAYSVFFVCIAITSDTICLLFIPIQWLFFMASTYVWIHYVWHTDKGICLPTVSLWLLFMYIEATMRLRDLKSSPFHIDLCRPFAAHCIGHSCDYGIGFKSYVSYRFKLRMQREVQKENTFYYELLRQALPKEQLNHTLSVTDKDKSEVSTPSNTSNGVLPHVKKSHDRSKSSPISHDNTLQIAEVTPSPTKTTVSSSGSSSTPSLSRKSANKSVPEHIPIWTPPVQEIEVIFRKSNKSKKSSNESASSPTQQQQKSKSSNSGNNSPKSLKQNSSSRSSSVHSNDSEKQKAPILPNGHLGVKEVIPLPLTNGHVIPEKTENKIELISTPSAIERLEATIAKLQSELNQARKNDQEMKNQISLLTNLERSAKNDVNQLKKENDMLQTKVNSMVSGKQKDKQSMQSMEKKLKSEADSRVNVEKQLHEEKRRRKEEEETAKHAAAQAQNNREKEKAEALKQAKHDLENEILKLEGQLKAKQEECDVMKKEISEFQLQEKSAKESETLMSALQAMQDKNLMLENSLSAETRLKLDLFSALGDVKRQLELAHGAIYKRDAEIVDLKSRLADILSILPESRIRSSTPHYSANFLEKPPLVRLSPTQEYPNNFCTQVPAARTPVPTVVQSHPNIDPQMVGLLHPVHLDPNAAMYTPSTSGL
The following text describes a protein:
Function:
Involved in the cellular response to hydrogen peroxide (H(2)O(2)) stress. During H(2)O(2) stress, prevents oxidative damage to both DNA and proteins by diminishing the amount of unincorporated iron within the cell. Binds double-stranded, bulge-containing, bubble duplex and Holliday junction DNA with approximately equal affinity and ssDNA with lower affinity. DNA binding shows positive cooperativity. Cofitness analysis suggests it might be involved in DNA repair pathways (Probable).
Subcellular Localization:
Cytoplasm.
Domain:
Has a wedge shape with a highly basic apical cleft (a cantaloupe fold), where DNA might be able to bind.
Sequence:
MLILISPAKTLDYQSPLTTTRYTLPELLDNSQQLIHEARKLTPPQISTLMRISDKLAGINAARFHDWQPDFTPANARQAILAFKGDVYTGLQAETFSEDDFDFAQQHLRMLSGLYGVLRPLDLMQPYRLEMGIRLENARGKDLYQFWGDIITNKLNEALAAQGDNVVINLASDEYFKSVKPKKLNAEIIKPVFLDEKNGKFKIISFYAKKARGLMSRFIIENRLTKPEQLTGFNSEGYFFDEDSSSNGELVFKRYEQR
The following text describes a protein:
Function:
Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Note=Localizes to the Z ring in an FtsZ-dependent manner. Targeted to the membrane through a conserved C-terminal amphipathic helix.
Sequence:
MATTEFIAAIELGSSKITGVAGRKNSDGSMQILAYAQEDSSTFIRKGVIFNLDKTAQSLTSIINRLEGELKNSIAKVYVGIGGQSLRTVRNVVSRDLEEEAIISEELVNAIGDENVAIPVVDMDILDVAPQEYKVGNNLQANPVGLVGSHIEGRFLNIVARSSVRKNLEHCFQQAKIDIADQLIAPLVTANAVLTESERRSGCALIDFGADTTTISVYKNNILRFLTVLPLGGNSITRDITTLQMEEEEAERLKKTYGDALYEEDESEEPATCKLEDESRTVELGKLNNIIEARAEEIIANVWNQIQISGYEDKLLAGIILTGGAANLKNLEEMLRRRSKIEKIRMAKLPRNTVHAPSNILKKDGSQNTLFGLLFEGNQNCCLIETAPQIPVTPATPRPEPEIHKTVDMFEDDQELKEQARLARLKKEEEEKEARAAAKEAERLRKQKEKEEKERRKREAGPSWIQRKIDSLTKEIFSDDDMK
The following text describes a protein:
Function:
May be involved in calcium-dependent ubiquitination and subsequent proteasomal degradation of target proteins. Probably serves as a molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1).
Sequence:
MSELEELQKDLAEIQSVISTLKRKSNIDYLNNRIKYLENSIKILTPQKVEQPQQQQQQQQQKDQDTLIYQGITKYAWDQEGNKVKVFLNMEGIGQLPKENISSEFTSTSVDVKVKGFKGLNHRFSIKKTFDELKEKECSIKTTNNSIVINLIKKDQKNWDQLNFKEKLIDTDPSKLDKQDPQASLMNMMKEMYQNGDDDMKRTIAQAWSKSQAEKGLQ
The following text describes a protein:
Function:
Catalyzes the NAD-dependent dehydrogenation (oxidation) of a broad array of hydroxylated polyunsaturated fatty acids (mainly eicosanoids and docosanoids, including prostaglandins, lipoxins and resolvins), yielding their corresponding keto (oxo) metabolites. Decreases the levels of the pro-proliferative prostaglandins such as prostaglandin E2 (whose activity is increased in cancer because of an increase in the expression of cyclooxygenase 2) and generates oxo-fatty acid products that can profoundly influence cell function by abrogating pro-inflammatory cytokine expression. Converts resolvins E1, D1 and D2 to their oxo products, which represents a mode of resolvin inactivation. Resolvin E1 plays important roles during the resolution phase of acute inflammation, while resolvins D1 and D2 have a unique role in obesity-induced adipose inflammation.
Sequence:
MSLHGKTALVTGGAQGIGRAVVEELLQNGAKVALVDLNQSVGEECKSDLDDQFGEDNCIFIQCDVTDGEKLGDAFRNTVDRFGRLDIVINNAGINNEKNWEKTIEVNLTSVIKGTYLALEHMSKEYGKQGGAIINVSSMAAFLHSPHQPVYTATKYGVIGFSRAMADASEQGNYGVRINALCPAFVDTQLLQTVEHEETMGKFVKYKDDFKQRMDKYGVLKPSLIAEGMLRLITDESLNGAVMKITCSKGIHFHTYEPLSA
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 4447 in 28S rRNA. Required for efficient rRNA processing and 60S ribosomal subunit biogenesis. Regulates pre-rRNA processing through non-catalytic complex formation with box C/D snoRNAs and facilitates the recruitment of U3 and U8 snoRNAs to pre-90S ribosomal particles and their stable assembly into snoRNP complexes. May play a role in the regulation of the cell cycle and the increased nucleolar activity that is associated with the cell proliferation.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MGRKLDPTKEKRGPGRKARKQKGAETELVRFLPAAGDENSKRLSSRARKRAAKRRLGSAEVRETNKSPGARPLPGKLPKGAVQTPSKKGALSLFNAAQGKKRPASAYSSEEEGEEEDSEEGGVVNEGDLWGSEDSDADMVDDYGANSSSEDEEEDDSEELLPIERAARKQKAQEAVTGSQWSEEETEEEEEESPESGPREDDETEGGLQINVDEEEPFVLPLAGEMEQDAQAPDLQRVHKRIQDIVGVLRDFGTQREEGRSRAEYLQRLRKDLATYYSYGDFLLGKLMDLFPLSELVEFLEANEVPRPITLRTNTLKTRRRDLAQALINRGVNLDPLGKWSKTGLVVYDSSVPIGATPEYLAGHYMLQGASSMLPVMALAPQEHERILDMCCAPGGKTSYIAQLMKNTGVILANDANAERLKSVVGNLHRLGVTNTIISNYDGRQFPKVVGGFDRVLLDAPCSGTGIISKDPAVKTNKDEKDILRCAHLQKELLLSAIDSVSATSKTGGYLVYCTCSITVEENEWVVDYALKKRNVRLVPTGLDFGQEGFTRFRERRFHPTLRSTRRFYPHTHNMDGFFIAKFKKFSNSIPQSQTGNSATSTPTNPDLPSPKGEVTPKPERSSQPAKKARVAVQAKQRLQKRQLPKKASFQKQNGVSKGTGSELSTVSSVTKVQPSSKLQDSKQPAEKAVVVREPKVAGRLKQSPKLQSSKKVAFPKQCVPPKGMDPEIPPVPSLSKTQDAFKPEDCNQPLGNTTTGAEKVKQQLPEQSFKKTAFQKQNGTPKGPKTPTMSPRSSSRPPPAKRRKSQSRGSSQPLPSSVDG
The following text describes a protein:
Function:
Inhibits thermolysin, bacillolysin and pseudolysin, B.polymyxa metalloprotease and human MMP1 and MMP3. No activity on trypsin or cysteine protease papain.
Sequence:
MKCLLYLCLWCYCVLVSSSIVLICNGGHEYYECGGACDNVCADLHIQNKTNCPIINIRCNDKCYCEDGYARDVNGKCIPIKDCPKIRSRRSIGIPVDKKCCTGPNEHYDEEKVSCPPETCISLVAKFSCIDSPPPSPGCSCNSGYLRLNLTSPCIPICDCPQMQHSPDCQ
The following text describes a protein:
Function:
Contributes to the suppression of the host's immune response to tick salivary proteins and is important for successful feeding on hosts. Inhibitor of cysteine proteinases. Inhibits host immune responses, probably via its inhibition of host cathepsins. Inhibits host papain (in vitro). Inhibits host cathepsin L (CTSL) (in vitro). Inhibits host cathepsin L2 (CTSV) (in vitro). Attenuates IFN-beta (IFNB1)-triggered JAK/STAT signaling pathway in mouse dendritic cells. Suppresses induction of interferon-stimulated gene IRF7 and production of CXCL10 in lipopolysaccharide (LPS)-activated dendritic cells; (Microbial infection) Down-regulates TLR2-mediated host responses to infection by Borrelia burgdorferi and the production of chemokines CCL3 and CXCL10 by host dendritic cells. Enhances infection by the tick-transmitted pathogen B.burgdorferi (in vitro); (Microbial infection) Inhibits host inflammatory responses to Anaplasma phagocytophilum infection. Interacts with mouse ANXA2 and suppresses oligomerization of NLRC4, a key component of host inflammasomes that sense A.phagocytophilum infection. Indirectly targets caspase-1 (CASP1) activation and subsequent IL-1beta (IL1B) and IL18 release by inhibiting reactive oxygen species (ROS) production from NADPH oxidase complex in A.phagocytophilum-infected mouse macrophages; (Microbial infection) Promotes replication of tick-borne encephalitis virus in mouse dendritic cells and reduces anti-viral effect of host IFN-beta (IFNB1).
Miscellaneous:
MISCELLANEOUS: Decreases symptoms in mouse model of mannan-induced psoriasis-like inflammation by modulating immune responses. Vaccination of guinea pigs against the protein increases tick rejection during feeding, prolongs feeding times, reduces blood intake and induces visible inflammation at the bite site.
Subcellular Localization:
Secreted.
Sequence:
MTSSLALVLVFGGAAVCAELALRGGYRERSNQDDPEYLELAHYATSTWSAQQPGKTHFDTVVEVLKVETQTVAGTNYRLTLKVAESTCELTSTYNKDTCQANANAAQRTCTTVIYRNLQGEKSISSFECAAA
The following text describes a protein:
Function:
Functions as an E3 ligase that promotes polyubiquitination of SPL14/IPA1 for subsequent proteasomal degradation. Regulates plant architecture by modulating SPL14/IPA1 abundance. Promotes the degradation of SPL14/IPA1 in panicles, while it stabilizes SPL14/IPA1 in shoot apices. Ubiquitinates the SPL14/IPA1-mediated complex with 'Lys-48'-linked polyubiquitin in panicles and 'Lys-63'-linked polyubiquitin chains in the shoot apex.
Subcellular Localization:
Nucleus.
Sequence:
MGAEEEEEPASAVGREGGGGGGGARAAGAGAGGDTADDDDSGESAAAVVPCSICLDAVVAGGGDRSTARLQCGHEFHLDCIGSAFNAKGVMQCPNCRQIERGNWLYANGSRPSQDVSNDDWGHDEDFYDANQPETSRSVFLPFRFQWCPIGRLAQLPSVFDEGESAPPVTFHDFMGQNFTSEHLPVSAPGATPPGPYIAYFQPLQSSASSSSSHVTERTMDGTTYHDHWNPLPGPSDGRPLATVHPIDFHHNHWTHLPNSYSQPNSNNGVAEQMAIPVVPMRVGGLDSDSQQRGSLPSVYGNGSGSRSRIPSVPPMAPQFMRPHGNINEQYQQNSSSLYAAPQRRTAVQAVQDSMNFTLFPQAPTGPNSMETEDAGGNQFYAWERDRFAPYPLMPVDSEANWWGSTPQSHGVTDHSAAPGRRLFGQWIGAGRSPPPPPPPPADNSSYRQMHIPRM
The following text describes a protein:
Function:
Catalyzes the reduction of sulfite to sulfide, a step in the biosynthesis of sulfur-containing amino acids and cofactors.
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Sequence:
MTTARPAKARNEGQWALGHREPLNANEELKKAGNPLDVRERIENIYAKQGFDSIDKTDLRGRFRWWGLYTQREQGYDGTWTGDDNIDKLEAKYFMMRVRCDGGALSAAALRTLGQISTEFARDTADISDRQNVQYHWIEVENVPEIWRRLDDVGLQTTEACGDCPRVVLGSPLAGESLDEVLDPTWAIEEIVRRYIGKPDFADLPRKYKTAISGLQDVAHEINDVAFIGVNHPEHGPGLDLWVGGGLSTNPMLAQRVGAWVPLGEVPEVWAAVTSVFRDYGYRRLRAKARLKFLIKDWGIAKFREVLETEYLKRPLIDGPAPEPVKHPIDHVGVQRLKNGLNAVGVAPIAGRVSGTILTAVADLMARAGSDRIRFTPYQKLVILDIPDALLDDLIAGLDALGLQSRPSHWRRNLMACSGIEFCKLSFAETRVRAQHLVPELERRLEDINSQLDVPITVNINGCPNSCARIQIADIGFKGQMIDDGHGGSVEGFQVHLGGHLGLDAGFGRKLRQHKVTSDELGDYIDRVVRNFVKHRSEGERFAQWVIRAEEDDLR
The following text describes a protein:
Function:
Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Subcellular Localization:
Cytoplasm.
Sequence:
MQRYFIDQNADVSQRFFITKKEDIHHITNVMRYDVGSKIILTFNDQTVYLCEIADITSDKIEVDLKEKQNINTELPVDVTICSGLIKADKYEWLLQKATELGASSFIAVSMERSIVKLNEAKVAKKIERWQKIIKEAAEQSYRLVIPSIQFESNLKLICDTIDNYDYILIAYEEEAKDGELSNFKQTLQQFNAQDKVLMIFGPEGGLSENEISLFSNTSTVVGLGPRILRAETAPLYALSAISYEKELMG
The following text describes a protein:
Function:
Mitochondrial transporter that mediates uptake of thiamine pyrophosphate (ThPP) into mitochondria.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MASETLSTTDINDNSANNDVEQDITSTTTTTTNNNSVNIPAKPNDYEALFKKLDIEKTGEITFLDFKRALKKFNHPINESPELLLKVFNSFDSNHDKKIDFKDFKEYLKTTDDQILKGFNQLDQDNDGRLNKSDFIRYLKESLHVKPSVANIDLLFKQLDSNEDGYINYDEFREFLLLVPRLQGSRIKTAFTFLFEEYDINSDGDVTLINQFLDGFKFFLAGGLAGVVSRTCTAPFDRIKVFLIARTDLSSTILHSKQEIARQIASGAETHVIEALRKKLAHAEMEQAAELLAEEAKTTKSAAAARTAASGVTTASAQNAKTIRSPIVQAVRTLWRQGGIKAFYVGNGLNVMKVFPESAMKFGSFEAAKRFFARIEGVNDTTKISKISTYLAGGFGGVVAQLTVYPIDTLKFRLQCSNLDHPLNAISTAKEMLKDGGVKIFYRGIGVGLAGMFPYAALDLGTFSTIKKLLVKKYGNKDDQSLPTYLTLSLGAFSGSFAATIVYPVNLLRTRLQSQGTYAHPFRYEGFYDVFSKTVAREGYSGLWKGLVPNLAKVAPAVSISYFVYESLIRRF
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. Required for the assembly of both SST3A- and SS3B-containing OST complexes.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MAASGLLRWKVAALLAALSTGLAAGGGTRTLVLLENLNLRDTHSLFLRSLADRGFDLSFRTADDPGLSLIKYGEFLYDNLIIFAPSVEDFGGNINVETIAAFIDGGGNVLVAAGSDIGDPLRELGSECGIEFDEEKTAVIDHHHYDVSDLGQHTLIVADSENLLKAPTIVGKKPLNPVLFRGVGMVADPDNPLVLDILIGSSTSYSFFPDKPITQYPHAVGKNTLLVAGLQARNNARVIFSGSLDFFSDAFFNSAVQKATPGSQRFPQTGNFELAVALSRWVFKEEGVLRVGEVSHHRVGETQPPSAYTVTDLVEYSIVIEKLSEGKWVPFDGDDIQLEFVRIDPFVRTFLKRNGVCASLAAHAVRALHPLGLPLLRRRLLHDGRPLPLQHRLPPHEGEGEGGLSGGHSAPSWAYGAPRQRAGKGREAFGGEATDPGMNLGWQHCGKTSAGTVFDPVLFFIPSQNKEAVPTGLSSFVVPRLATAPWGPCLWLVSEKGGRDVPVEHRPDGHLFGRARM
The following text describes a protein:
Function:
Required for vacuolar assembly. Acts as a component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion.
Miscellaneous:
MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
Subcellular Localization:
Vacuole membrane; Peripheral membrane protein.
Sequence:
MLRAQKLHSLKSSDITAILPTEQSQKLVLAKKNGDVEVYSRDGNTLKLFQVYPDLLQNAKNDPLPPVIENFYFANELSTIFAQCKETLILLSTTNLHEYDRIIDRRGINHCWLFERSHKNKEEKNTYLIYSTINTAKMRVLIWEGRTYKNMMEASLSYRKETIRSIYPGETGITLATDLGIYHWPYNKPSLIRIEKTVKNKFPKDMISALTELKEQAEKVIEKKPKKNSHFDAQSFSSMDRMSRKSSMSSLWYRTIRNERGNKIRYTFELDGNDATPMIIDGATKKIFKVELMHNNEEPFLIATDHATFSESNSEFDHMQYLSSNLLMLYNSSTIKFVDYENGFTFLQQKIPEGIKWVKNLSGTYFLVWTSNDEVQLFSYHVDDGSEDDDQESICGDINDPDFYQLWRKVLFYKFFIDSPHSKELCVSDNPEESLDICAMKLRDLTVMWCLRIFDKFQNYMVQLERSRNSRMIRSKCEEMIIKSIFDLFIKFWAPPQLVILKVFPSAISSLVLEITGQEHHCLLKEAEEVKETYDIPPHLLNRWCLPYLTDTRRHLQNLLSKENDDESRITWCYRDREIKQSFDFFLISNHDDVDLNTMLTLIDTVLFKCYLYYNPPMVGPFIRVENHCDSHVIVTELKIRHMFKDLIDFYYKRGNHEEALKFLTDLVDELENDNTDQKQRQKIDHGVKILVIYYLKKLSNPQLDVIFTYTDWLLNRHNDSIKEILSSIFFYDSQACSSRDHLKVYGYIKKFDKLLAIQYLEFAISTFRLEGNKLHTVLIKLYLENLDIPSTRIKLKSLLETTSVYEPRTILKLLNDAIESGSDQLPTNQLNFVKYLKIFPLSKLENHKEAVHILLDEIDDYKAATSYCNDVYQSDSTKGEELLLYLYSKLVSIYDSNRNSKLILNFLQDHGSKLNSAEIYKNLPQDISLYDIGRVVSQLLKKHTSKMDETRLEKALLQVELVATTYKLNERMSSYGVLSDSHKCPICKKVISNFGTDSISWFTREGRNIITHYNCGKVLQERFNAKNEKSSRIKQKTLGEVINELNNK
The following text describes a protein:
Function:
In complex with CCZ1, is required for multiple vacuole delivery pathways including the cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and endocytosis. The MON1-CCZ1 complex acts at the fusion of vesicles with the vacuole, through its regulation of the SNARE complex during the coordinated priming and docking stages of fusion, and particularly at the stage of tethering/docking. The MON1-CCZ1 complex is recruited to membranes enriched in charged lipids, particularly phosphatidylinositol 3-phosphate (PtdIns[3]P), by GTP-associated small GTPase RAB5 homologs (YPT10, YPT52, YPT53 and VPS21). The MON1-CCZ1 complex recruits GDP-associated small GTPase YPT7 to membranes and acts as a guanine nucleotide-exchange factor (GEF), promoting nucleotide-exchange on YPT7 and triggering endosomal maturation by recruiting downstream effectors such as components of the HOPS tethering complex.
Subcellular Localization:
Endosome, multivesicular body membrane; Peripheral membrane protein. Prevacuolar compartment membrane; Peripheral membrane protein. Vacuole membrane; Peripheral membrane protein. Note=The association of the MON1-CCZ1 complex with the vacuole is regulated by the C-Vps/HOPS complex.
Domain:
The disordered N-terminal is involved in autoinhibition of the MON1-CCZ1 complex guanyl-nucleotide exchange factor activity.
Sequence:
MNLNESYLDAEIPKGQLKHSKSGNFEGIPIVATTSEPTTSVNLDETFFKKAPIAMPICDDHSVSKSTSVNSLNTTSLASRRSPLQTKKLQAKNNLLSADLAKSNDDTTRALNSPKKDFGPYLDSENDIRSRLAESIYSMETSIRGSELQRRPYVSNEIPNVFKFSKFNSNCKLNESQTLCDKNFFIFTSAGKPIYCMHGKDEQIMSYTGLVNTVISYFQVNGPSELKTISTLTSGKRLTFLDKSPILLMAQSERGESSNELLNQLDFLYSYILSSLSERQLLRLFSKRENFDLRNYLESTDFENLDEICSLICNRMFPDLLLNSLQCLPFNHSSRLKLQNVVLQQLEKRQDIPRGTLLYGLIIAPQNKLCCVLRPRGHTLHTTDLHLLFCLISHQFQNLDETQELWVPICFPKFNSSGFLYCYIKFLPNDTHSNEKSALVLISAQKDAFFSLKSFSDELIIKLEEEKLLKKINTSKGFKLSDIPAPMVHHFIYKSKQNVQYVMPHFEVNSNIALDSSQGLEYELKLKTYYQQLHGTVVRDNGNLLSRSMLNFVRWSSKDNEDLAMDETQMDFSELDEYIIGNSSFKQESVNMVGMAWVTPTFELYLIGNNGIVDKRVLFKSARKVANWCQKHESRLFISDGAVF
The following text describes a protein:
Function:
A hormone that controls sex pheromone production in females and pheromone responsiveness in male. Also mediates visceral muscle contractile activity (myotropic activity) (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MFRLYFFFNVICIFLAIRSAIGGEVPDATEQKINNFLASGKDSEDLSKRAAAMWFGPRLGKRTIASELHDEMMDEIDDNPLYYSGESPQRVASEIAQGTPYVVLLLTGRVLRQPQPVFYHSTTPRLGRRDASSSNENNSRPPFAPRLGRNLPFSPRLGRSFGAPVVDNFAY