lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Serine protease required for epidermal surface formation in embryos and juvenile plants. Involved in embryonic cuticle formation downstream of BHLH95/ZOU.
Subcellular Localization:
Secreted.
Sequence:
METNPRKLRSYSYICLIVCIFVLVVCAILSRAEEKEGKGENDDHIPKIYSILVEGEPLAFRASTNINSKAMALEAKKIEEIHDEILGSTLEKGSYTKLYSFKHVINAIAVRTTASQAKKLGKTKGVKAVEEDKGVKLMTTYTPDFLELPQQVWQKISNEGDRRAGEDIVIGFVDTGINPTHPSFAALDLTNPYSSNLSRLHFSGDCEIGPFFPPGSCNGKIISARFFSAGARASGALNSSLDILSPFDASGHGSHVASIAAGNAGVPVIVDGFFYGRASGMAPRSRIAVYKAIYPSIGTLVDVIAAIDQAIMDGVDVLTLSVGPDEPPVDKPTVLGIFDLAMLLARKAGVFVVQAVGNNGPSPSSVLSYSPWVVGVAAGNTDRSYPAPLILDGGQTVQGVGLSGPTLGAPLVQHRLVLAKDAVRTNGSVLQPLTRDIEECQRPENFDPAAVFGSIVICTFSDGFYNQMSTVLAITQTARTLGFMGFILIANPRFGDYVAEPVIFSAPGILIPTVSAAQIILRYYEEKTFRDTRGVATQFGARARIGEGRNSVFAGKAPVVSRFSSRGPAFIDATRSPLDVLKPDILAPGHQIWGAWSLPSAFDPILTGRSFAILSGTSMATPHIAGIGALIKQLNPSWTPAMIASAISTTANEYDSNGEIISAEYYELSRLFPSNHFDHGAGHVNPARALDPGLVLPAGFEDYISFLCSLPNISPATIRDATGVLCTTTLSHPANLNHPSVTISALKESLVVRRSFQDVSNKTETYLGSVLPPNGTTVRLTPTWFTVPPQKTQDLDIEFNVTQVLNKFTFGEVVLTGSLNHIIRIPLSVKTI
The following text describes a protein:
Function:
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Sequence:
MNIKIKKRDGQYEPLQVEKTKKMVKLACEGIEGCDPLELELDSRIQFRDGMTTKEIQRTLIQTAIEKVIQNSKDNNGNNIKKTNANWQYVAARLLCFDLYKEAKISRHYNSFGYGDYYQLVKKLVKIKLYGEYLIQNYSDEEIKELAKYIVPERDELFNYEGLKLLNDRYLIKGNNGEILELPQERFMTIAMHLAIPEGDKKVFYAKKFYDLLSELKVTVATPTLGNAGTPFYQLSSCFISVVGDNLWSIYDVNQKFAQVSKHGGALGIYTGKIRALNSEIRGHKNASGGVVPWIRLYNDTAVAVDQLGKRKGGAAITLDIWHKDIFDFLDLKTNNGDDRRKAHDIFPSVSIPDLFMKRLEKRESWSLFDPYIVEKIMGYKLEDYFDDEDRKEFTNKYLECERNTNIPRDTVPTLDIMKKLMKSAVETGTPFIFFRDTVNKANPNKHKGMIYSSNLCHEIAQNMSESRLLEEEIIDGNGYSEIVQRVKAGDMVTCNLNSINLSKVKKEEFNECIPFQIRMLDNVISLNKLPVKEAKVTSDKYRAIGLGTSGYHHFLANNKIRWESDEHIKVADEIYEEIAYIAIKSSMELAKEKGSYPAFKDSEWETGKYFERRGYNSERWKKLQSNIKKYGMRNGYITAIAPTGSTSNIANTTAGIDPVFKKFFMEEKKGSFTPKTAPDLNEENFWYYKEAHTIDQQWSIKACAVRQKHIDQAQSFNLYITPEIKAKEILNMYIESWKQGVKTIYYVRNKSLEMDECTSCSS
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of adenine in helix 25.1 in 25S rRNA. Required both for ribosomal 40S and 60S subunits biogenesis. Required for efficient pre-rRNA cleavage at site A2.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSLFPSAFESGVSKISPTLASAGKGGKKTNKRKHSDANAGLGQAQQVKQADANFEKLMRKFEGGEAIGKEEGKESMGVVGKKRNKKNKSRQVNDEEIVHSTPRAKGDKPKPKPTPKSDQAKLNQAAKQNQTDTPPSKKSKANKITPGFKLEPVQLPIPIPPPSKGTKLKVGGEGNLTEMQKDMQAKLEGARFRWINEQLYSTPSTEALAMMRKDPKIFADYHQTHRLLTSAWPSPPLPHMINLLSSLPSGTVIADLGCGDAGLARALVPQGKIVMSFDLVGDNGVLGAETTESNAAGGWVVEADFLEKVPLPGRPGGLDYGVSATEESEGKGKRKNKKKGSRKRDVASSEIVDAVVCCLSLMGTNWVGGISEACRILKQGGTFHVAEVTSRFTSTEAFVSTVESFGFELEEESQPSTHFTLFRFTKNSEVPLGPVKGQEGWEERVRKGEEILRACVYKKR
The following text describes a protein:
Function:
Involved in both the assembly of spliceosomal snRNPs and the methylation of Sm proteins. Chaperone that regulates the assembly of spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus (By similarity).
Subcellular Localization:
Cytoplasm, cytosol. Nucleus. Cytoplasm, cytoskeleton.
Sequence:
MVLIMRVSPPEHGLLYTANNIKLKLGDKVVGEGTVYIAQNTLSWQPTELAEGISIEWKQVSLHGISSNPRKCIYFMLDHKVEWNGVYGDPPQQAVNGRNGGGSEAEVDEGNGSDEHDEDDNFEDAVDEQFGEVTECWLMPEDIHTVDTMYSAMTTCQALHPDSANSDSEDSDPMQDAGGLEDEAMEEDDALTLGRNGVQNLSLDDDEERFEDADE
The following text describes a protein:
Function:
Major surface antigen of procyclic forms.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MAPRSLYLLAILLFSANLFSGVGFAAAAEGPEDKGLTKGGKGGKGTKVSDDDTNGTDPDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPGAATLKSVALPFAIAAVGLVAAF
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:
MLKLIEDAIERTSAAPQASAPEVRTQSDIDEELKKLLEQIQAKIYVVGVGGAGCNTINRMMQVGIQGAKIIAMNTDAQDLLKVRAHKKILLGKELTRGLGAGNNPKIGEEAAKESEREIREALEGADMVFITCGLGGGTGTGAAPVVAEIAKKMGALTVAVVTLPFTVEGIRRIKNAEYGLERLKKNTDTVIVIPNDKLMEVAPNLPIHMAFKVADEILVQAVKGITELITKPGLVNLDFNDVRAVMKDGGVAMIGIGESDSEKRALEAAQQALNSPLLDVDISGAKGALISISGSDVKLEEAQQIIELVTSKLDPEAQVIWGIQLDEELGKMIRILLVVTGVSSPYSVAEEEEESYFGEEERRPIKLDLDEL
The following text describes a protein:
Function:
Part of the sfmACDHF fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes.
Miscellaneous:
MISCELLANEOUS: The operon is cryptic under classical laboratory conditions, but is functional when constitutively expressed.
Subcellular Localization:
Fimbrium.
Sequence:
MAMACLCLANISWATVCANSTGVAEDEHYDLSNIFNSTNNQPGQIVVLPEKSGWVGVSAICPPGTLVNYTYRSYVTNFIVQETIDNYKYMQLHDYLLGAMSLVDSVMDIQFPPQNYIRMGTDPNVSQNLPFGVMDSRLIFRLKVIRPFINMVEIPRQVMFTVYVTSTPYDPLVTPVYTISFGGRVEVPQNCELNAGQIVEFDFGDIGASLFSAAGPGNRPAGVMPQTKSIAVKCTNVAAQAYLTMRLEASAVSGQAMVSDNQDLGFIVADQNDTPITPNDLNSVIPFRLDAAAAANVTLRAWPISITGQKPTEGPFSALGYLRVDYQ
The following text describes a protein:
Function:
Plays a role in the cellular response to DNA damage and the maintenance of genome stability through its association with the MRN damage-sensing complex. Promotes chromatin loading and activity of the MRN complex to facilitate subsequent ATM-mediated DNA damage response signaling and DNA repair.
Subcellular Localization:
Nucleus. Nucleus, nucleoplasm.
Sequence:
MVQEFNVLRCFSCQTFQVQQVKKAKKWTCKVCGEKQSLIKEFGRGAAADCRRHVQKLNALRGEQHQLNTQQLLAQGDEENENEDVYEVLDPKSEQEEAHVSRWSKYTDQTTEGPNEEKDDEDEDENVYTERPQFRIQGTRKRKKMSSLEPFGGNCDNYEESRAGYSQFRKQAYLPLQLEKRSSSSWNKGSVSKYSNCQRPDDVVPSARTKLPSSRQTVGHYPTACSSSTNTMENSIGNKQQIKSSYRPPTADVNKHLPIQSESPSVSSHQKFGESTIENKDSKWNKFLTIVPTQDKEEYYYESQNGKKTLIPYFTKADTVVDFEERRCPADEKDSGILNRQKVVGGNASCPTTRLPTKSVGFENAVCKPVLVKAPYSSLSLNPLFCTDEDFDDTS
The following text describes a protein:
Function:
NAD(P)H:FMN oxidoreductase component of a two-component system involved in the biosynthesis of the side chain of the aminoglycoside antibiotics in the biosynthetic pathway of butirosin. Together with BtrO, mediates hydroxylation of gamma-L-Glu-GABA-S-BtrI.
Sequence:
MDNKERNTLYQVVYAISGVTGEDGDELVETFKQGPMEVDKRDFFEIVQRVESLFDCTLDMNLEGPYLIHADEIVTKITKLNV
The following text describes a protein:
Function:
May have a role in gut contractility or in thymic development and regulation. Activates RXFP4 with high potency and appears to be the endogenous ligand for this receptor (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MKGSIFTLFLFSVLLAISEVRSKESVRLCGLEYIRTVIYICASSRWRRHLEGIPQAQQAETGNSFQLPHKREFSEENPAQNLPKVDASGEDRLWGGQMPTEELWKSKKHSVMSRQDLQTLCCTDGCSMTDLSALC
The following text describes a protein:
Function:
Preferentially oxidative, glucose-repressed isozyme that catalyzes the conversion of ethanol to acetaldehyde. Main enzyme involved in ethanol consumption. Acts on a variety of primary unbranched aliphatic alcohols (Probable). Also produces ethanol from glucose, albeit less than ADH1.
Miscellaneous:
MISCELLANEOUS: Present with 1620 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MSIPETQKAIIFYESNGKLEHKDIPVPKPKPNELLINVKYSGVCHTDLHAWHGDWPLPTKLPLVGGHEGAGVVVGMGENVKGWKIGDYAGIKWLNGSCMACEYCELGNESNCPHADLSGYTHDGSFQEYATADAVQAAHIPQGTDLAEVAPILCAGITVYKALKSANLRAGHWAAISGAAGGLGSLAVQYAKAMGYRVLGIDGGPGKEELFTSLGGEVFIDFTKEKDIVSAVVKATNGGAHGIINVSVSEAAIEASTRYCRANGTVVLVGLPAGAKCSSDVFNHVVKSISIVGSYVGNRADTREALDFFARGLVKSPIKVVGLSSLPEIYEKMEKGQIAGRYVVDTSK
The following text describes a protein:
Function:
Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MGEEHYTGYLGNKTPQLLQYNPVCKKVPVLVHNGKPIAESLIILLLQTLITVIKTDGEAQEKAIKELLEKLEVLGEGMKEFFPDGNPSIDSENVGLLDLVFFTSFGLHQVREEVLGIKIVDPEKTTLLFSWVTAINQLPLVKELTPPHDKLVAFLKFIRENALKSSSA
The following text describes a protein:
Function:
Serine protease. Has a preference for substrates with an Arg instead of a Lys residue in position P1; Serine protease. Hydrolyzes the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC and, to a lesser extent, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Val-Leu-Lys-AMC. Has a preference for substrates with an Arg instead of a Lys residue in position P1.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix. Note=Not attached to membranes.
Sequence:
MARHLLLPLVMLVISPIPGAFQDSALSPTQEEPEDLDCGRPEPSARIVGGSNAQPGTWPWQVSLHHGGGHICGGSLIAPSWVLSAAHCFMTNGTLEPAAEWSVLLGAHSQDGPLDGAHTRAVAAIVVPANYSQVELGADLALLRLASPASLGPTVWPVCLPRASHRFVHGTACWATGWGDVQEADPLPLPWVLQEVELRLLGEATCQCLYSQPGPFNLTLQILPGMLCAGYPEGRRDTCQGDSGGPLVCEEGGRWFQAGITSFGFGCGRRNRPGVFTAVATYEAWIREQVMGSEPGPAFPTQPQKTQSDPQEPRENCTIALPECGKAPRPGAWPWEAQVMVPGSRPCHGALVSESWVLAPASCFLDPSSSDSPPRDLDAWRVLLPSRPRAERVARXXXXXXXXXXXASDLALLQLRTPVNLSAASRPVCLPHPEHYFLPGSRCRLARWGRGEPALGPGALLEAELLGGWWCHCLYGRQGAAVPLPGDPPHALCPAYQEEEEVGSCWNDSRWSLLCQEEGTWFLAGIRDFPSGCLRPRAFFPLQTHGPWISHVTRGAYLEDQLAWDWDPDGEETETQTCPPHTEHGACGLRLEAAPVGVLWPWLAEVHVAGDRVCTGILLAPGWVLAATHCVLRPGSTTVPYIEVYLGRAGASSLPQGHQVSRLVISIRLPRHLGLRPPLALLELSSRVEPSPSALPICLHPASIPPGASCWVLGWKEPQDRVPVAAAVSILTQRICNCLYQGILPPGTLCVLYAEGQENRCEMTSAPPLLCQMTEGSWILVGMAVQGSRELFAAIGPEEAWISQTVGEANFLPPSGSPHWPTGGSNLCPPELAKASGSPRAVYFLLLLTLLIQS
The following text describes a protein:
Function:
General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA domain; P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity.
Subcellular Localization:
Cytoplasm.
Sequence:
MAQKTFKVTADSGIHARPATVLVQTASKYDADVNLEYNGKTVNLKSIMGVMSLGIAKGAEITISASGADENDALNALEETMKSEGLGE
The following text describes a protein:
Function:
Adapter molecule that plays a key role in the activation of pro-inflammatory NF-kappa-B signaling following detection of bacterial pathogen-associated molecular pattern metabolites (PAMPs) (By similarity). Promotes activation of an innate immune response by inducing the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism.
Subcellular Localization:
Cytoplasm.
Sequence:
MDKELIDVDTEQTISCLTLTLYHPNHQDQKLFRGINFSRKEEIKADAVVAFGRDYNVCRYPLLSNRVSRIQFNLQLFKHFNCSTSTFEIKNLSKKNKLYVDNLELDYLNKIELPKKCMIRFGDFQILAEIDEGDSDEKFEICCEKSHVSLVQDSFIPTMQPIPECGTLNAVEIDENEC
The following text describes a protein:
Function:
Involved in the catabolism of quinolinic acid (QA).
Sequence:
MASAHGDLRHLLPATYKRLISDWLEEDCPSFDYGGFVVGESEGEAKLLGKSEGIIAGVPFFDEVFSQLGCSVEWHHHEGSSLPANQKTHVATVRGPIRKILLGERVALNILARCSGIATKTSSLLQILRSHGWKGTLAGTRKTTPGFRVVEKYGILVGGADPHRHDLSSMTMLKDNHVWACANNASSSTATTAANGEQDIAAAIPKAVQAAKAVGGFATKVEVEVRSLDEANAAIEAGADVVMLDNFTSEGVRQAAKQLKEEWTAKGKSRGSFLIEVSGGLNEVNALQYVCDDVDIFSTSSIHQGVGIVDFSLKVSLRG
The following text describes a protein:
Function:
Metalloprotease.
Subcellular Localization:
Secreted.
Sequence:
MDIKQLLLSIILTVSVVNGRGRRINIYGAENGKSDIVQLRGPAEQLVYSSPIRERRPIFRNALLSNSPLRWSKMQDLDGNYLIPYVISGNYDTVERDTIKTAMEKIANNTCIRLIPRTNQPDYAEINNKKGQGCYASIGRFPGKNVVMLESNDDQSCIQEDTVIHELFHVIGLWHEHMRADRDAFINVLYKNIEPAQYPQFEKLSSRDATTYSVPYDYNSVMHYDENAFAKPGKISMMTKDSKFQKVIGHPKDASSNDYKKVCAIYHCSKCMHQDFQQIVEQEHIELNNPIITNAPVQQGDSCTDRLGICPMLKSREMLNCKVMATFCCSSCSAPTSTTTTTSGTPSDGSLWQRIKSIFQ
The following text describes a protein:
Function:
May regulate TLP1 expression and telomerase activity, thus enabling certain prostatic cells to resist apoptosis.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein.
Sequence:
MVCKALITLCIFAAGLRVQGSPTPTLLPVSLTTKSTAPMATWTTSAQHTAMATTPVASATHNASVLRTTAASLTSQLPTHPREEAVTSPPLKREVNSTDSSPTGFSSNSSGIHLAPTPEEHSLGSPETSVPATGSQSPTLLFSQGPTSASTSPATSPSEPLSASVTSNHSSTVNNIQPTGAPMAPASPTEEHSSSHTPTSHVTEPVPKEKSPQDTEPGKVICESETTTPFLIMQEVENALSSGSIAAITVTVIAVVLLVFGAAAYLKIRHSSYGRLLDDHDYGSWGNYNNPLYDDS
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.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type III membrane protein.
Sequence:
MITDVQLAIFSNVLGVFLFLLVVAYHYINANTGKIGPKAK
The following text describes a protein:
Function:
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Sequence:
MELIFEKSKKGRKGYKLPELDVEEVNIKEYLPEEYLREELDFPEVSELDVVRHYTNLSHLNYAVDTTMVPLGSCTMKYNPRINEELVNKKEFLNVHPLTPEEYIQPLLKLVYELKELLKELGGFAEVSLQPAAGAHGELLGLLLIHAYHQDRGNKEKKVVLIPDSAHGTNPASAAICGFDIKVVKSDKKGELDFEDFIKKLDERVAALMITNPNTLGIFERKIKEIAEELHKRDALLYMDGANFNALVGRFKPGEWGVDVMHFNLHKTFSTPHGGGGPGAGPVGVSERLKPYLPVPQIEYDGKKYYLNWNIEKSVGKILAFHGHFLVWLKALAYILTYGKDIKKVSEYAVLNARYLKHLLKGVFKDPYPESPCMHEFVLSATNLTKYGVRASDVAKRILDYGFYAPTMYFPLIVREALMIEPTETENPDTLKKFALILRKIVKEAKEKPEILKKAPHRTPVRRIKEAEANRNLILKFKDIKE
The following text describes a protein:
Function:
Probable subunit of the chloroplast NAD(P)H dehydrogenase (NDH) complex of the photosynthetic electron transport chain. Required for both formation and activity of NDH. May function in assembly or stabilization of the NDH complex.
Miscellaneous:
MISCELLANEOUS: CRR3 is not conserved in cyanobacteria and seems to be a subunit of the NDH complex which is specific to the chloroplast.
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Single-pass membrane protein.
Sequence:
MAVLSTIYSITRASTPTMASLTNDSPSPLPSSSPSKLPSPTSPSKKPLKLRQVSKQMGSQNQQRRGNKPSIAQIERAFGSGSYRDSEGEMDMNTVFDELLLGHANKFESKIEKKLREIGEIFVARTEPKLRSSGKPVLMFTIQWILPIWIMSLLVACGVIKLPFSIPFLDDLIM
The following text describes a protein:
Function:
The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs (By similarity). Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core) (By similarity). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG (5Sm) are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (By similarity). To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A (By similarity). Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP (By similarity). Within the SMN complex, GEMIN2 constrains the conformation of 5Sm, thereby promoting 5Sm binding to snRNA containing the snRNP code (a nonameric Sm site and a 3'-adjacent stem-loop), thus preventing progression of assembly until a cognate substrate is bound (By similarity); May play an essential role in spliceosomal snRNP assembly in the cytoplasm and may be required for pre-mRNA splicing in the nucleus.
Subcellular Localization:
Nucleus, gem. Cytoplasm.
Sequence:
MDEFQSKAFEVGEEIEPDDNEPLTGEEYLQRVKWHSNRCPSVVVADIDYSKIKVTIPSNSYFTLPPSITKCKKELLPTPTWEKEFLNDFSEFRQKLQYIKSNRPSNNNNNNNNNNNNNNNNNNNNNLIPQLPHINDKRYWYIFCFGSNGNNNNNNNDIKMKDFNDNQEDDDDDENNEDYEYNENKEEEEEEEEEEEEEEEVEEEEEEEEEEEEVVDYSTKKPTLGNKPTMDILCRLDHVLTVALVNYHIEWLEKREFTQERSYWLYMLLSLLEKPIDPDTCSNLRSCIRRLSVFRSKITNLNDPNLPSINILFTIIAKYFDQLEPSDILYL
The following text describes a protein:
Function:
Involved in RNA splicing. Is required for the association of U4/U6 snRNP with U5 snRNP in an early step of spliceosome assembly.
Miscellaneous:
MISCELLANEOUS: Present with 1770 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MSKYIALENLPVDLQHKGATQNESTADILKQLPHERLQAVLEKIPEEDLEVRRLLSILKKPEVVENEDVQQRRIRLAEILMVDEIDLENINNMENINGEEVDEEDDEDFFTPATSELIFARRFLINYSLERSRKRLQKEMERHQKFNTRQELLSRRTELQRMANLELAGSQLVSTKPISAVSLSTDDMVVATGSWAGDLQVLNSQTLQPLTQKLDSHVGKIGAIDWHPDSNNQMISCAEDGLIKNFQYSNEEGGLRLLGDLVGHERRISDVKYHPSGKFIGSASHDMTWRLWDASTHQELLLQEGHDKGVFSLSFQCDGSLVCSGGMDSLSMLWDIRSGSKVMTLAGHSKPIYTVAWSPNGYQVATGGGDGIINVWDIRKRDEGQLNQILAHRNIVTQVRFSKEDGGKKLVSCGYDNLINVYSSDTWLKMGSLAGHTDKIISLDISNNSHFLVSGGWDRSIKLWN
The following text describes a protein:
Function:
Carrier protein involved in proton-driven auxin influx. Mediates the formation of auxin gradient from developing leaves (site of auxin biosynthesis) to tips by contributing to the loading of auxin in vascular tissues and facilitating acropetal (base to tip) auxin transport within inner tissues of the root apex, and basipetal (tip to base) auxin transport within outer tissues of the root apex. May be involved in lateral roots and nodules formation.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein.
Sequence:
MGTVAENGDMDAKAHGREDFSDQNNLDAGARFVLKSKGTWVHCGYHLTTSIVAPPLLSLPYAFTFLGWGGGISCLIIGALVTFYSYNLLSLVLEHHAQLGLRQLRFRDMANNILGPRWGRYFVGPVQFLVCYGAVVASTLLGGQCMKAIYLLSNPNGAMKLYEFVIIFGGLMLILAQVPSFHSLRHINLISLILCLAYSACATGGSIHIGSSSNEPKDYSLNGDSQDRVFGVFNAIAIVATTYGNGIIPEIQATIAAPVKGKMFKGLCVCYTVVAVTFFAVGISGYWAFGNQAEGLILSNFVSNGKPLVPKWFVLMTNIFTILQLSAVAVVYLQPTNEVLERTFADPESEEFSARNVVPRIISRSLSVVISTTIAAMLPFFGDINSLIGAFGFMPLDFILPVVFYNLTFKPSKRSLVFWLNITIATVFSALGVIAAVAAVRQISLDGNTYRLFANV
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MSSDLLTDLQRQLRDLNDNFASVVEQLVHIAPPVPVGPDDVQPLSALPGAVSRAELQIKATALSESLMQRFRNIDSLIDKLPELGEPPEQQDARIAGMLQEHRELRKELGVVMAEAEYKLDEVYGCYEALSNHVLAHEGKMGRDASEAQ
The following text describes a protein:
Function:
Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Also displays broad nucleoside diphosphate kinase activity.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Predominantly nuclear.
Domain:
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Sequence:
MSPQRGGEDSGAANERAAEAPPLPSAGRTPRQLRRRGRGRSRLGPPPSPRPAPRQRRPGCCQLSQRPTQPRCMLNRCGRRLLHVLGLSFPLLTGRPLFLFPHRFMKPQVVFVLGGPGAGKGTQCARIVEKYGYTHLSAGELLRDERKNPDSQYGELIEKYIKDGKIVPVEITISLLRREMDQTMAANAQKNKFLIDGFPRNQDNLQGWNKTMDGKADVSFVLFFDCNNEICIERCLERGKSSGRSDDNRESLEKRIQTYLQSTKPIIDLYEEMGKVRKIDASKSVDEVFDEVVKIFDKEG
The following text describes a protein:
Function:
Internal capsid protein that is probably ejected along with the viral DNA and prevents degradation of viral DNA by the host type I restriction-modification antiviral defense system. Plays a role in directing proper capsid assembly.
Miscellaneous:
MISCELLANEOUS: Phage P1 Dar antirestriction system is composed of Hdf, DarA, DdrA, DdrB, DarB and Ulx. Hdf and DarA are incorporated first in the procapsid in a co-dependent manner, followed by DarB, DdrB and Ulx.
Subcellular Localization:
Virion. Note=Internal capsid protein. A proteolytically cleaved 60 kDa form is incorporated into the virion.
Sequence:
MEQFNINKGMTIKPGLDVLPPPVTDDEYRALMAGEDRYLMTESNTLEEIEATFFYDTPIHWCATDLLEAISSTRLQLHRTMQAFVRALNQKLNGTGISAGSDKTGDVAQSGARAIGGAEIGRARNVNGLPVLPAIIPLSDGQTISILFHSPTAENRITNSDTLVAFQFLLNKKDVTHTVAPMSGRDMTLAQVTMKLANLAEKNSAKFQRAQKKKKALVDEITQLQADSDQKEDAMSDLADQVAAVEGQKADLEQKINAVASEADSLYEENERLQGEIDRLNRTGGRDTIAPAGMTGGHSRALTDRLASIKNRMHMDGEATLSNGASMKQFIGDGEGYIQLTDPDGSVYMIKAKSIQGVDMADAIGKLFKAYKAGNVSEYLVQPEEHKPENVEPESAEDTGSSSPEPEVSVGAYRYALQMRPAAPGAIPEGNKAILPRPDEGDPYYEYARYGIATYDTPLSDQQMSEYDLKLLPREDSFDFLAKTLTNGPFGKYAQKALELATNSPDEFRVMLKTQFQKTFPNIAFPGGAGTEKMVQSMINALQAEVGEITQPEPAPAQPDETVSEADAEANKAIEYLNNVMDMQSTDMAEIRNARGNVREAIAALQTAGRFEENEELVNGAARHLADLLVAIQKAGVAA
The following text describes a protein:
Function:
Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with terf2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'-TTAGGG-3' sites via its association with terf2 or other factors, and regulates gene expression.
Subcellular Localization:
Nucleus. Chromosome, telomere.
Sequence:
MGDNLNRNLFQDADGKPMKFYIKPCPTKGKVRPLIESCGGQVIVHPTDGVIRLAEPDTLTPLGYVSASFIFDSVANNALQDIESYMCPDSRSGAVETCTKKSSTGRLFYTTAEDAAILEYIENYGSPALPAGGNEIWKKMEKKKITCHSWQSMKDHYKKKLMRKHYRRAVKSQKELQVEVMKHQSESKISISNGSNKRLKREPSITLWTDTSFEVASICSSRKPEQNSHPPVIDLVSENENDKECQEEEIILNEPEPTLYDRVVGHEYDSQVILPQVNSQNGMLAPAKGEDECPVVGGGEAYNSDLDYENIQINSDDGKNSAYLNNIDKDGRESLDDLLTLSSKHKQQQIIDFTIQDQVRLNNGDDNHDKFCKGTILDNEASAAVDEKNHRKQIVFIDEENLNQQNDDPDIPKISTGDQNVNLEFSNQINEEILSKYFYCDFGYELRDAKSSDRYSAHSVADQVQEMRKHHECMWEKDMRKDTNAEIKALAASMQMAEAGVACVYRALSGKCDDTRYYLKHNKTKDDFIGWNHDLDDALLCGNTAKLMEAGISEKRILQRLHYLSISDVKELIQSILYNKNA