lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Nucleolar RNA helicase that plays a role in various biological processes including innate immunity, ribosome biogenesis or nucleolus organization. Plays an essential role in maintaining nucleolar integrity in planarian stem cells. Maintains embryonic stem cells proliferation by conventional regulation of ribosome assembly and interaction with OCT4 and POU5F1 complex. Regulates antiviral innate immunity by inhibiting the virus-triggered signaling nuclear translocation of IRF3. Mechanistically, acts by disrupting the interaction between IRF3 and importin IPO5. May play a role in later stages of the processing of the pre-ribosomal particles leading to mature 60S ribosomal subunits. Has intrinsic ATPase activity.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MADEVEKSLAFHEMGLDDRLLKAIASQGWRHPTLIQERAIPLALEGKDLLARARTGSGKTAAFVIPIIQRILDGKQAAKEQAVKALVLTPSKELCSQAYKNAVALSSCCSREVRCLDVSGTTDITSQRPMLMEKPDIVIGTPSRVLAHIQGGNLELQHSLEMLVIDEADLVFSFGYEKDIKTLLGHLPKIYQAFLMSATLSEDVQALKKLILHNPVTLKLEESQLPESDRLTQYHITCEEGDKFLIIYTLLKLRLVRGKTILFVNSIDRCYRLKLFLEQFSVPACVLNSELPVSSRCHIVNQFNQGLYNLVIATDESALDAEDAGGKEKTGKAKKKAKRFKKKKDKEYGVSRGIDFQFVSNVINFDFPTQVDSYIHRVGRTARGDSQGTALSLISAQELPLLQQAETALSGDTDDPVIKPYRFKMEEIEGFRYRAKDALRSVTKTNVREARLKEIRSEILNSEKLKSYFEDNPRDLQVLRHDKALAASKVKPHMKNVPEYLMPPSMKSNSSVITKRPQQFQGGRREQKRHKKRKEDPLRSFKYKQEES
The following text describes a protein:
Function:
Endoplasmic reticulum translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum. Acts as a dislocase that mediates the ATP-dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane. Specifically binds mitochondrial tail-anchored transmembrane proteins: has an atypically large substrate-binding pocket that recognizes and binds moderately hydrophobic transmembranes with short hydrophilic lumenal domains.
Miscellaneous:
MISCELLANEOUS: Present with 1870 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Localizes to endoplasmic reticulum regions devoid of phosphatidylinositol 4-phosphate (PI4P) hydrolytic machinery.
Domain:
Contains a large substrate-binding pocket that recognizes alpha-helical transmembranes, which alternately faces the endoplasmic reticulum lumen and cytosol, while remaining accessible to the lipid bilayer through a lateral opening. The translocase alternates between two conformations: inward-open (E1) and outward-open (E2) states. Undergoes a series of conformational changes with ATP-binding, phosphorylation of the Asp active site and subsequent dephosphorylation in a Post-Albers cycle (i.e., E1 -> E1-ATP -> E1P-ADP -> E1P -> E2P -> E2-Pi -> E1). A substrate transmembrane helix with a short, preferentially positively charged lumenal segment binds to the outward-open pocket and the E2P-to-E1 transition flips the transmembrane by a switch from the outward-open to inward-open conformation.
Sequence:
MTKKSFVSSPIVRDSTLLVPKSLIAKPYVLPFFPLYATFAQLYFQQYDRYIKGPEWTFVYLGTLVSLNILVMLMPAWNVKIKAKFNYSTTKNVNEATHILIYTTPNNGSDGIVEIQRVTEAGSLQTFFQFQKKRFLWHENEQVFSSPKFLVDESPKIGDFQKCKGHSGDLTHLKRLYGENSFDIPIPTFMELFKEHAVAPLFVFQVFCVALWLLDEFWYYSLFNLFMIISMEAAAVFQRLTALKEFRTMGIKPYTINVFRNKKWVALQTNELLPMDLVSITRTAEESAIPCDLILLDGSAIVNEAMLSGESTPLLKESIKLRPSEDNLQLDGVDKIAVLHGGTKALQVTPPEHKSDIPPPPDGGALAIVTKTGFETSQGSLVRVMIYSAERVSVDNKEALMFILFLLIFAVIASWYVWVEGTKMGRIQSKLILDCILIITSVVPPELPMELTMAVNSSLAALAKFYVYCTEPFRIPFAGRIDVCCFDKTGTLTGEDLVFEGLAGISADSENIRHLYSAAEAPESTILVIGAAHALVKLEDGDIVGDPMEKATLKAVGWAVERKNSNYREGTGKLDIIRRFQFSSALKRSASIASHNDALFAAVKGAPETIRERLSDIPKNYDEIYKSFTRSGSRVLALASKSLPKMSQSKIDDLNRDDVESELTFNGFLIFHCPLKDDAIETIKMLNESSHRSIMITGDNPLTAVHVAKEVGIVFGETLILDRAGKSDDNQLLFRDVEETVSIPFDPSKDTFDHSKLFDRYDIAVTGYALNALEGHSQLRDLLRHTWVYARVSPSQKEFLLNTLKDMGYQTLMCGDGTNDVGALKQAHVGIALLNGTEEGLKKLGEQRRLEGMKMMYIKQTEFMARWNQPQPPVPEPIAHLFPPGPKNPHYLKALESKGTVITPEIRKAVEEANSKPVEVIKPNGLSEKKPADLASLLLNSAGDAQGDEAPALKLGDASCAAPFTSKLANVSAVTNIIRQGRCALVNTIQMYKILALNCLISAYSLSIIYMAGVKFGDGQATVSGLLLSVCFLSISRGKPLEKLSKQRPQSGIFNVYIMGSILSQFAVHIATLVYITTEIYKLEPREPQVDLEKEFAPSLLNTGIFIIQLVQQVSTFAVNYQGEPFRENIRSNKGMYYGLLGVTGLALASATEFLPELNEAMKFVPMTDDFKIKLTLTLLLDFFGSWGVEHFFKFFFMDDKPSDISVQQVKIASK
The following text describes a protein:
Function:
Component of a SNARE complex that may be the effector of SEC4 function in exocytosis.
Sequence:
MGLKKFFKIKPPEEATPEQNKDTLMELGISVKNPSKKRKEKFAAYGKFANDKAEDKVYAPPGYEQYARPQDELEDLNASPLDANANEATAGSNRGSSGTQDLGNGAESNSMQDPYAIENDDYRYDDDPYARFQANKSNGRGSVNAAPYGDYGGGYNGTSLNSYNNDGPYSNQNTSNSWVNANGRNSLNHSNSTLNVGPSRQTRQPPVSTSTNSLSLDQRSPLANPMQEKRNPYADMNSYGGAYDSNTNRSSGTRQGSSKNANPYASMANDSYSNGNLNRSANPYSSRSVRQPQSQQAPMTYTPSFIASDEAARNSEVDLNEEPRTGEFDFEEVYADKSAENRAALDEPDLNAVMTNEDSIDLNASEVDHSSRQQQQQQWFMDEQQQQQQHFNATNNQYGDQRGYKTFEEIQKEEEARQQQEEDEAVDEIKQEIKFTKQSSVASTRNTLKMAQDAERAGMNTLGMLGHQSEQLNNVEGNLDLMKVQNKVADEKVAELKKLNRSILAVHVSNPFNSKRRRREREEQLKNRKIEEKLMREQTSQQLSQSTQRIEGAMNANNNISEVRERYQRKNVLEKAKRYQFENDEEDDEMELEIDRNLDQIQQVSNRLKKMALTTGKELDSQQKRLNNIEESTDDLDINLHMNTNRLAGIR
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ105me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MGRDFRGGRGDTRGGGRGGDRGRGAPRGRGGRGGRGGRMGGAPKAFVVPHPRLAGVFVAKGQQEALVTKNMVPGESVYNEKRISVEDKQTGEKVEYRVWNPFRSKIAAGIIGGVSDIFIKPGAKVLYLGAASGTTVSHVSDVVGSEGVVYAVEFSHRSGRDLVNMAKKRTNIVPIIADARKPLEYRMLVGMVDVVFADVAQPDQARIVGLNSQYFLKKGGHFMISIKANCIDSTNRAEVVFQHEVQRLKDEGLTPQEQLTLEPYERDHAIVIGVYNA
The following text describes a protein:
Function:
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
Sequence:
MNTWGNKIRLSIFGESHGEAIGIVIDGLEAGTKLNLENINKFIERRKAGKSSFTTSRKEKDEYKILSGYKDGYTTGAPLCVIFENTNTISKDYENLKDLLRPNHADYPAGIKFKGFNDVRGGGHFSGRMTLPLTFAGAIAIDILGEKGIKIFSHIKRILDIKDKSFLDFKEKDLEKFENLKESSLPFIENDLEDKTKELLEKIKLSGNSVGGEIECSCFNLPIGLGNPFFDSLESKISHLAFSVPAIKGISFGIGFDFANILGSEANDLYYLDNNEIKTRTNNNGGILGGLSTGMPLVFSVVVKPTSSISLEQKTVNIKEMKEDILKINGRHDTCIVPRVLPVIEAIMALAILDEIL
The following text describes a protein:
Function:
Is involved in regulation of translation. Is preferentially associated with CBC-bound spliced mRNA-protein complexes during the pioneer round of mRNA translation. Contributes to enhanced translational efficiency of spliced over nonspliced mRNAs. Recruits activated ribosomal protein S6 kinase beta-1 I/RPS6KB1 to newly synthesized mRNA. Involved in nuclear mRNA export; probably mediated by association with the TREX complex.
Subcellular Localization:
Cytoplasm. Nucleus speckle.
Sequence:
MADISLDELIRKRGAATKGRLNARPGVGGVRSRVGIQQGLLGQPARTATFQQRFDARQKIGLSDARLKLGVQDAREKLLQKDARFRIKGKVQDAREMLNSRKQQVTVPQKPRQVADAREKISLKRSSPATFLSPPIGTVTPALKLTKTIQVPQQKAMAPLHTHPAGMRINVVNNHPAKQNLYDLEEDDDSVAPIPSKQMKFAASSSFLHHVAGLSSSKFSMSKALPLTKVVQNDAYTAPALPSSVRTKALTSMSRTLVNKEESPKELPPAEPVLSPLEGTKMTVNNLHPRVTEEDIVELFCVCGALKRARLVHPGVAEVVFVKKDDAITAYKKYNNRCLDGQPMKCNLHMNGNVITSDQPILLRLSDSPSVKKESELPRRVNSTASSNPPAEVDPDTILKALFKSSGASVTTQPTEFKIKL
The following text describes a protein:
Function:
Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk.
Subcellular Localization:
Secreted.
Sequence:
TEIPTINTIASGEPTSTPTIEAVESTVATLEASPEVIESPPEINTVQVTSTAV
The following text describes a protein:
Function:
Binds to but does not cross-link actin. Required for the formation and maintenance of inner ear hair cell stereocilia and staircase formation. Essential for normal hearing.
Subcellular Localization:
Cell projection, stereocilium.
Sequence:
MEAQQALVASKDGDMATLERLFEAGALRPDITDDLGAGLVHHATRAGHLDCVKFLVQRAKLPGNQQAHNGATPVHDAAATGNLAELCWLVRDAGCGLQDQDASGVSPLHLAARFGHPALVEWLLREGHAATLETLEGALPLHHAAVSGDLTCLKLLTAAHSSGVNQRTCSGASPLYLACQEGHLHLAQFLVKDCGADVRLRALDGMSSLHAAAAHGHYSLVVWLVTFTDIGLTARDNEGATALHFAARGGHTPILDRLLLMGAPIMRDSWGGTPLHDAAENGHMECCQTLLSHHVDPFLRDEDGYTAIDLAEYHGHQDCAQFLREMSRPVRVLMTPPPPPFPPPPLLAAKLSLEEERRGDSGLKSPSSATLSPVWPAQPVPREPMACTAPLRVTTPDALQGPEVEARDSRAGLATLQLDGLPAGDLDMLVPTQDERGRPIPEWKRQVMVRKLQARLGADHPPEDQDQSQRQDSGPTAAEQATWRYSQTHQAILGPFGELLTEDDLVYLEKQINDLQLRRRCQEYESELGRLAAQLQALLPEPLVSITVNSHFLPRAPGLEDEEAPVLATELEASEEPGKAEPRGQPLPFWCSHIGRLVRSMSLLLKGMNGLAQGEEKPPSPVPQDLGKETIAGPSRSEAQREIQECGVSVRTLRGNFEFAPDLPCALNSGPCELGVRPGQCLRGCWSAPPQPRGDAMGGEPGPGDTEEASDSGISCEEAPSEAGAGPGLDLASLRKERIVMLFLGHWKKSAYTPALRTAACRTLEAQRARSRGPEAAGSPRPSSPQPSDGPRLGHLWQQRGIITHLLGTWKAIMAHVPARQLRRLSRRERGPLSPEQFLPHVDGAPVPYNSLSLDLFMLGYFQLLECDLPAEERKMRHLLCFEVFEHLGAHGWEAVRAFHKAVTDEVAAGRRAWTDGFEDIKARFFGSSQGPPWDVEPGRKLGLTPLGSLPHASLPGSGPEPAVPPRLGSDSQGSSFNSGDICGYIDRSFAFWKEKEAEMFNFGE
The following text describes a protein:
Function:
Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting (By similarity). Acts as a component of the DHIC (ddl-1-containing hsf-1 inhibitory complex) which modulates lifespan by sequestering the heat shock transcription factor hsf-1 to negatively regulate its binding to DNA and its transcriptional activity.
Sequence:
MYHVPLIPRDAGREETIFRINQSLQKLLRVSDEIFDRVEHRITRIHGKAEAIDRRTEVLEKKLESLQESDKVITFTLPRQLPKLPEEPPTSTSLFRINIDTEHFPGSEELPAFRRADDHVLRPCEPIDFTYELNKPDKFFLTSQVLKEYEQKGWERYKKRLLGGLRELSRSPEHIAELFYAGTSIPAFEGVSGDFSKKALDADDDGGTSRSGRTTDELAQLRLHEQLLEDTALSSTLMQEDSLDDNHPLAFRINFNEKKKKTAKMVEMPDSLPNLKGHAHDFTLRDPEIDEDRLLDILPADDQIPEASEPTEAEADAPTTFILPPPPPPMKLDPSPQPAATPVEITEIPPIISPPAPPPPPPPPPPPPPPQTPSASSSVTFSPTKSVDGGRSDLMAAIRAAGGAGNAKLSRIAEKPKRKGKFDGILESSALLGASETPRNSAPAPDGGGGGGDLMSALSKALDARRKAINGKVEAQPPAKVSSTIPAPPNFDDEEWD
The following text describes a protein:
Function:
Endonuclease which cleaves flap structures at the junction between single-stranded DNA and double-stranded DNA. Specific for 5'-overhanging flap structures in which the 5'-upstream of the flap is completely double-stranded. Prefers the blocked-flap structures similar to those occurring at replication forks, in which the 5' single-strand overhang of the flap is double-stranded. Also possesses weak 5'- to 3'-exonuclease activity on nicked but not gapped double-stranded DNA. Does not cleave bubble-like or Holliday junction substrates (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MGVKELWTVLTPHAERKPINELRGKKVAIDLAGWVCESLNVVDYFVHPRHHLKNLFFRTCYLIWEQVTPVFVLEGVAPKLKGQVIAKRNELQFRGVRPKDAATGTQTAAKVDKGRTRFNHVLKQCETLLLSMGIQCVQGPGEAEAYAAFLNKHGLVDGVISQDSDCFAYGAIRVYRNFSVSTQGAQAAAGGAVDIYDMREITSRMDFGQHKIIVMALLCGCDYCPDGIGGIGKDGVLKLFNKYKESEILDRLRNWRAETDKYNALEMRVDDKSICSNCGHIGRTQSHTKSGCSVCRTKRGCDKTLWKEQRLSIKAELILRRKALLAPEFPNEEIISEFLSEPPTIPNLNLGWRQPNLVKFIKQIGHLLQWPEIYCFQKFFPILTRWQVQQAARTNAIGRVELVQPVDIIKKRTVKGVASLELRWQDPSGSFQGLIPDKQISEFELEHPKGIEELYYTVEPLDMLEAAYPDLVASFLKSKEKPPKKATRKKKTDPLSAIENIPETLDKQKANPAKPKRVVKKKKAPTEQAQPSLQQFLRREKIGGTPVKDSLPQMAQLPQQCSTPITKFLPSDLESDCDAVEFDMSDVVNGIISNPNARPTVTRHEGRQLHYEALSDDLSMRLAQLSLRKDELQEEPLPPVAEHKRDLSLVEHLPQSKRLSLDDSFDLLVKGDLKKVPHLIQPIRTPVDRFKHQHRISEHLPQPAVEPAANVSYFFNQSSDNADAFEQLMNSSLGIQEQAEEDEEEEDDLVVISD
The following text describes a protein:
Function:
Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope.
Sequence:
MADGNTPASPPPASPLQRHRYAIKSSVHNTAASRRREQAIAIGKERREALIRAKRVCRTPLSGSDDAGIEEDDMVVDKEKEGLEARTAQAVEELKSALSSQGKGAQKKKTEVLRALRRLLSQSEVPPIEAAIKAGAVPLLVQYLSFGSSDEQLLEAAWCLTNIAAGEPEETKSLLPALPLLVAHLGEKSSTLVAEQCAWAIGNVAGEGADLRSTLLAQGALWPLARLMLSSKGSAARTAAWALSNLIKGPDPKAVNELIGIEGVLNAIVQNLEKADEELATEVAWVVVYLSALSEKAISLIVRSHVPQLLIRRLLASENLQLLIPVLRGLGNVVAGDGYMVDSILIVGNNITDQALSSLIKCLRSDNRVLRKEASWVLSNIAAGSFEHKKLIFTSEATPVLIHLLNNAQYDIRKEAAYTLGNLCVVPAGSSEPPNIIVEHLVSIINSGALPGFINLLRSADIESARLGLQFLELAMRGYPDGQGPNLVEREDGIEAMERFQFHENDVMRNMANGLVDKYFGEDYGVE
The following text describes a protein:
Function:
Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. It probably carries the active site for 3'-splice site cleavage (By similarity).
Sequence:
MEDEKFPISYVHGKFLVFDVQAVEVFRKNYHILGTLVGTLPQLPQQNVFLGLPMELSKEEAFYLIEKGISYIVDDTKVHKQLLENTTKDDVKQCLKKRQSLAYDQMIAAKKKENEKKIEIMKKLGRTLPLDPLNYDEHDSFDLSWIPVDTVTTRIAEKSSMNDDFHKEEDVFENLDINRYLMFKSLVDTGFYLNPGLRFGCQFVAYPGDALRYHSHYLVNSYKWDQEIPVLFLIGGGRLGTAVKKTWLIGGSNDRNINMNGEKSKEELLLLPVRHFSIEWAGFG
The following text describes a protein:
Function:
Protein phosphatase that displays CTD phosphatase activity and regulates transcription of snRNA genes. Recognizes and binds phosphorylated 'Ser-7' of the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and mediates dephosphorylation of 'Ser-5' of the CTD, thereby promoting transcription of snRNA genes. Downstream of EIF2AK3/PERK, dephosphorylates ERN1, a sensor for the endoplasmic reticulum unfolded protein response (UPR), to abort failed ER-stress adaptation and trigger apoptosis.
Subcellular Localization:
Nucleus.
Sequence:
MSRRKEELEASIRKKVEFERKALHIVEKLLEDDITEDFLVESGRFISSSHYKDIVDERSIVKLCGYPLCRNKLGNVLKQKYRISTKTNKVYDITERKFFCSNFCYRASKYFEAQIPKSPVWLREEESPPDFHLLKEGQRGISGEEIKLQDETIKASDIENAGLSGGQCEPGSFDTLSGGSDTEQEFVSSILPGNRPRATGSAGRLPRKSIPKKKPGRKPNSKDQDRTMAVATEELNKCRLDSQEKDLISVQKKSALVASGDRLPEKRKTSESSFIDCDGSRVTMVGISKQGAERFRKKFAKSKTPFSPSVQVESLVGKENLLEVLKKTLLEWKTEETVRFLSGPKKEVTCSQSPPSATEDGRGGLGDRDPDSEPEGLRSSVAKKEGHDSLNQSLPFTGSDTAVRPVPSYESLKEETEALNLRIREFYRGEYVVTEKSSKKQVREEVDPTFPLIDSQAQNQIRKRIVLEKLRKVLPGILGPLQITLGDVYTELKSLVRTFRLTNKNIIHKPAEWTLIAIVLMSSMPQIIQSEEKNQKNAIYTQFINTLLRELHLTNEDLGSLTQIFKTVGQKDVSPCRVEPLQ
The following text describes a protein:
Function:
Sesquiterpene cyclase that converts farnesyl diphosphate to the volatile beta-selinene and the corresponding nonvolatile antibiotic derivative beta-costic acid, especially in roots upon infection by rootworm larvae (D.balteata) and fungal pathogens (e.g. Fusarium spp.).
Subcellular Localization:
Cytoplasm.
Domain:
The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Sequence:
MDGDIAAALPPVNQQSKADGTAVAAAAAAAACHGDFEPSVWGDFFVTYTSPPSLSQEPEEQMRERANFLKGEVRKKFEAAAAMSAINSAMLVDAVVHLGIDHCFREEIATALRSVHKEEGEFGSCDDLHTVAVRFLVLRQHGLWVSADVFDKFRDDTGSLSKSLLCSNPRGLLSLYNAAHMVTPEEKVLDDAIAFARSHLEAMIGELRSPMVEQVSRSLDIPLPRFSRRLESMHYIAEYGQEEGHDAQILELARLEFELVRSLHLRELREICRWWRELYNDVKLPYARDRIVEIYFWACGVIHEEEMSRARMIFAKTFAFTSLIDDTCDVHATLEEVQKFNEAMQSWEEDAVSIVPEYLRTLYSRTIKGFQEFEDMLEPNEKYSMSYVKKAYKLLLQYYLKEATWANENHTPSFKEHVQVSIISSGLPMLVPVLLMGTGLATREAFEWADSAPDMVLASGEVGRFLNDMASYKLGKNKKDVANAHECYMKEYGATGEEAFAFIANMTENAWRKINQACMEMDPAMLPAFKVAVVDLSRSMEIIYLGGKRDAYTFGSNLKDLVTSLFLKPCA
The following text describes a protein:
Function:
Acts as a negative regulator of polarized growth via an alternative mechanism to ZDS1. In heat-stressed cells appears to play a role in localizing BCY1 to the cytoplasm. Seems to interact with, and down-regulate, CDC42. Also acts as a suppressor of PKC1. May act as an integration point for distinct signaling pathways helping to maintain a balance among these different pathways.
Miscellaneous:
MISCELLANEOUS: 'ZDS' means 'zillion different screens' as both ZDS1 and ZDS2 have been found by a wide variety of genetic screens; MISCELLANEOUS: Present with 105 molecules/cell in log phase SD medium.
Sequence:
MVLMEDMQNKDGHNTVENSSGGTDSNNNIQMRRMRKTQLSKKELFEKRKSDVLIAAKSLDTEIQNVKNLKRLSIGSMDLVIDPELEFKVNSRNSYSSDSSKESLQESLHEENIIRSEQKEEQGSEDNDAYEEGDATNVDDSIDITQTEYLHDEETLEKEKIIRNASSSTSSSARVTSRNRRLSGVKTLAHDVVLDVENDHDSKMVDLTQNLLWVPADQHPNVKPENYLELIQDTLQNIQISTNQDIDENKLELGNNHVISNRKRTGSVVRRPSRLKTSYTKFDDEPPLADKPQEGEIQVDKRISSSDIKTIRSVSLKEITEELTKISNNAGLTDSDAVTLARSLSMSGSFTNESLHLNGNHTENDNEFASNMFNETGLTIPERSSLRRSKFNTYKIRLEGSSLPQAVKLNSLMNIQTNDNRRSASSPASYTQVPQEQASLNDFHEIFDHYRRTSTDWSTENEKYVDSTNYYSDEEDLTHASISQESSLLSTDSSNNSVLIKPHNTGSMISEKLDQHVSSSEKSNTNNSEANHGWSWLNSSNGSLNANEQTYQQLTDDEDDEECVDNEKADFVNLSVSRRAKSTKRASERINHSKNRHSPIFQIHSEEAKSVVITPSVVSSSESQPSKPTAPAVVEKKVELPTDTQASTHKKNSLEKRLAKLFKRKQHNGTCKSDVKVIKKSVKKELKKKASHSSLSKFRKSPKKKPQEAEVERPSSPTKTITTEDIDTASVIEPEVRSSNASTLLPDSHTSHSSEFVVETISELDGDDSFDISGGDVNYDVEVHSSISRDTTAGLEEDIGAEREDNTSPTAPQISTLPPRKLTFEDVVKPDYSNAPIKFTDSAFGFPLPMITNSTVIMFDHRLGINVERAIYRLSHLKLSDPGRELRQQVLLSNFMYSYLNLVNHTLYMEQVGTGDIAFNGDSALGMMDKNDSDGTILIPDI
The following text describes a protein:
Function:
Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
Subcellular Localization:
Cytoplasm.
Sequence:
MAQEFVNCKIQPGKLIVFIKSTCPYCRRAQEILSQLPTKQRLLEFVDITASNHTNKIQDYLQQLTGARMVPRVFIGKDCIGGCSDLVSMQQSGELLTRLKQIGALQ
The following text describes a protein:
Function:
Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA (OSB-CoA).
Sequence:
MLIPDWLARRAALHPHRPALIYAGTTYTFAELDRWAGAVASHLRQLVTPGARVALLSRNRPGFVAIVHAAPRTAITLVPLNTRLTAAELAFQIQDSDPALLIIEHDLLPVAREAAGNRPLIVLEELTAATTAPTAPAPPIDLDAMHTIIYTSGTTGRPKGAILTAGNHWWNAIGSMLNLGLHEDDRWLAVLPLFHVGGLSILLRGAIYGIPVILHERFDPALVRHDLDAQRITIVSLVAVMLQRLLAIDPSPFPPHLRCVLLGGGPAPQTLLEQCATRGIPVTQTYGMSEAASQAATLSPAESLIRLGSAGKPLLPVELSIVTPSGQPAAPGEVGEICLRGPNISPGYLGLPPRSPTDWFHTGDLGYLDQEGYLYVVDRRSDLIIAGGENIYPAEIEAILLSHPAIAEAGVVGLPDPEWGQRPVAAIVAQQPTTAEELIAYCRSRLAGYKVPRTIVFLHELPRTAAGKLRRHELRAILLAQMSGNDH
The following text describes a protein:
Function:
Histone methyltransferase (By similarity). Might play a role in transcriptional regulation. Together with set-26, negatively regulates lifespan in a germline-independent, partially daf-16-dependent fashion. Together with set-26, plays a role in germline development and maintenance and might play a role in the restriction of the trimethylation mark on histone H3 'Lys-4'(H3K4me3) to target genes specifically in the germline.
Subcellular Localization:
Nucleus.
Domain:
The PHD-type domain binds histone H3 when trimethylated at 'Lys-4' (H3K4me3) in combination with a nearby acetylation (K9ac, K14ac and/or K18ac), but not H3K4me3 alone.
Sequence:
MADGEHTLPADEELFEQPPPQQQQPEIAEPIVMAQEPIQGVSEDPQASEATHEAPDNYPVDHQMENQEFYHEPQIPEPQQIPQIPVFQPAAYNPPNYVAPQQRANNFGEPAAADARPLTEQEQLAAERPTEDTVWIDSDDDTDVEEAILRANFWLPYSDHNYDPPDPADRIILPTEGPFPCIAGLDEDCNIVKQWMPEDAVGPGSPGTQYRRNQQAGGGLPSTSVASQQQQLPVRHNIQNRPMVAAQPFSIGGNQVEYGGMDSRMQQRGVVRDGPQYRVMNDFGNGLPMRGLLPPRNSPAANAINRAREQQQQMYHQAGARGSLQQRAAPAPADPTPGSYQHIVNAVPGGGANPMRRVPPQARPGMIGGAANNNRARPTHVTRPMDTQEFEHPVAPAAAPPHRVVDVAPHRMTPEQRQELQQMNRQRAAPQFPAAAAQRSAEVIVIQQRPGASSRAPRPSMAQEDLLRSPTRRLSERVPQEHQTPVLEPRRFQVKVTDTYSTPIPKASDQLPAQLTEEDPPEESAAAAAPEDVPDAAPEDPPKVILKPTPPHRMTQEEKNAHFARLTTDKEKPTSSTSILPQDAAPPHVPPPPPPLVLRPHHQDETLAMVQSVFESKPRQPDTPKDKETISKIADLLRFSADEFTGQSGSSAAARQRTVSGSAARAQTYQMHHQQQQHHHQMPMDQRKRPSSGRYDALMGAMPLQQQPPPPPSQFQHTDSIAHRPRGRPKGTRHPSVAVQPQRSGGARTLPPRAQTVAMSARNGANAKNSDSESEGIDEAAEESWTMRCHCGMDHGDGDTIECEGCKTWQHMACMGLTLKSNTSKYKCEMCLPRRLPVSKAEAAREQERILNRLRAAARKQKRKSEPVEQKQKSSQPSTSRKSAPMALQQPAEPRVAQLNDYSKQASALLFGMEQTAGADTLLAESRLHKKARRMFVEEAVEALVTTDLVQIRQVILEVNGHVSMSSEVKRQPGGGNCIFMYDGLMKGTAGEDMGDGQELVCIDTKRKGNDTKFTRRSCVPNCVLKHVLGSNATLGIMIVATKDITRNTEVTLPFDADWRESEVELECAEHMKELQACPFESERRRFAAERHRAMDHKKQEAEEARRADEERRRLEEEVRRERAAKTKQMDEAEKARLEAEKAAEKEKKAKERKKMEASAAAAPESTNSITAREERRIQQAEEMFRRQEEEGKRKEARRRSKSVTPGVLEAAGTAAREDAPEASIPVPAPSPPASRRSVSRTTQPSTSSFATPTEPPAKNKRMRSVVPPKSEPASSAKRVRATTVATPKATTANDSRKRTASATGKTPVAKRSKNVAPTSFALALIEKELREQARNSTVLEMILPDYIMNEERSGLLAGQSPDFSEVRAQIEEENRMKERSRKREAKKKAVEKEKKEHRKEPKKTNEPGPAPKSEKAVEKAVEKVEKKPKSPQKPPAKPTAQNPPLKKTEEVDGIEREASESSSKESSVAPEEKKNPKKITFAEYNSRRSQKREAGECSTPPAVTRRGFIPSTEGEDLVNVELSAIPLDDHPSSSNTAPTTTIAPSVGGAPKPTSVVVKSPSTRSRTRGAASESADDAPAEHSMSLQDRVFSMFGSTVDAPAPPPPPASAETNSRRSRSTRWN
The following text describes a protein:
Function:
Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. May degrade cutin, a macromolecule that forms the structure of the plant cuticle. May also degrade suberin, a specialized macromolecule found in the cell wall of various plant tissues. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of fungal infection (By similarity). Involved in pathogenesis.
Subcellular Localization:
Secreted.
Sequence:
MQTSALLLAAQALVASAGLIERQSCPSIHVFGARETTVGPGYGSAGTVVNLILNAYPGSTAEAIVYPACGGQSSCGGISYGNSAMQGTNAVASAVNSFNQRCPNTQIVLVGYSQGGQIMDNALCGGGDPGSGITNTAVPLTASAVTAVKAAILMGSPRYRAGFPYNVGTCTAQGFAARPAGFVCPSGSKIQNYCDSPDPYCCTGNNQAVHQGYGGVYGQAALTFVRSKLNSGGSPPTTPPTTPPTTPPTTPPTTPPPSGSCAALYGQCGGQGWNGATCCSQGTCRASNQWYSQCL
The following text describes a protein:
Function:
This enzyme is closely associated with an endotoxin-sensitive hemolymph coagulation system which may play important roles in both hemostasis and host defense mechanisms. Its active form catalyzes the activation of clotting factor B.
Subcellular Localization:
Secreted. Note=Secreted in hemolymph. Localizes in large granules of hemocytes.
Sequence:
MVLASFLVSGLVLGILAQQMRPVQSRGVDLGLCDETRFECKCGDPGYVFNVPMKQCTYFYRWRPYCKPCDDLEAKDICPKYKRCQECKAGLDSCVTCPPNKYGTWCSGECQCKNGGICDQRTGACTCRDRYEGAHCEILKGCPLLPSDSQVQEVRNPPDNPQTIDYSCSPGFKLKGVARISCLPNGQWSSFPPKCIRECAKVSSPEHGKVNAPSGNMIEGATLRFSCDSPYYLIGQETLTCQGNGQWSGQIPQCKKLVFCPDLDPVNHAEHQVKIGVEQKYGQFPQGTEVTYTCSGNYFLMGFNTLKCNPDGSWSGSQPSCVKVADREVDCDSKAVDFLDDVGEPVRIHCPAGCSLTAGTVWGTAIYHELSSVCRAAIHAGKLPNSGGAVHVVNNGPYSDFLGSDLNGIKSEELKSLARSFRFDYVSSSTAGRSGCPDGWFEVEENCVYVTSKQRAWERAQGVCTNMAARLAVLDKDLIPSSLTETLRGKGLTTTWIGLHRLDAEKPFVWELMDRSNVVLNDNLTFWASGEPGNETNCVYLDIRDQLQPVWKTKSCFQPSSFACMMDLSDRNKAKCDDPGPLENGHATLHGQSIDGFYAGSSIRYSCEVLHYLSGTETVTCTTNGTWSAPKPRCIKVITCQNPPVPSYGSVEIKPPSRTNSISRVGSPFLRLPRLPLPLARAAKPPPKPRSSQPSTVDLASKVKLPEGHYRVGSRAIYTCESRYYELLGSQGRRCDSNGNWSGRPASCIPVCGRSDSPRSPFIWNGNSTEIGQWPWQAGISRWLADHNMWFLQCGGSLLNEKWIVTAAHCVTYSATAEIIDPSQFKIYLGKYYRDDSRDDDYVQVREALEIHVNPNYDPGNLNFDIALIQLKTPVTLTTRVQPICLPTDITTREHLKEGTLAVVTGWGLNENNTYSEMIQQAVLPVVAASTCEEGYKEADLPLTVTENMFCAGYKKGRYDACSGDSGGPLVFADDSRTERRWVLEGIVSWGSPSGCGKANQYGGFTKVNVFLSWIRQFI
The following text describes a protein:
Function:
mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MSLNYEQNAADEQFARAHKAVSLSDDEESEGQAETTSAPNQEPHVSKSPREYYDEPGGKGNGSGADDQDEPETEAASGAANTHVVAHHYNELKEAGRKDRQKSKIFFMRNFNNWIKSQLINEYMSQIKQNKRMGDALRVLDMCCGKGGDLLKWEKAAISHLICTDIAEVSVEQCQRRYQDILQRSEKSKFANKFTAEFFACDSTLVRLRERYKDPSLQLNLVSCQFAFHYCFESMAQADCMMRNAAECLKPGGFFIATMPDAYEIIRRLRAAGPDARRFGNDVYSIEFDCETDPLPLFGAKYQFHLEGVVDCPEFLVHFPTLVKLGRKYGLQLLKRSTFADYYKENLHHGRHLLQRMSGLESVQPQRCENDEEFAHVSNFQGAQRSRSVGTLSKSEWEAATLYLVCAFKKCKNTWDTNGKPLFEFDD