lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein pabp-1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by rgb-30/xrn1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. par-2/pan3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit par-1/pan2 to mRNA via its interaction with RNA and with pabp-1.
Subcellular Localization:
Cytoplasm.
Domain:
The N-terminal zinc finger binds to poly(A) RNA; Contains a pseudokinase domain. The protein kinase domain is predicted to be catalytically inactive because some of the residues important for catalytic activity are substituted and it lacks the equivalent of the binding site for a peptide substrate. However, it has retained an ATP-binding site and ATP-binding is required for mRNA degradation, stimulating the activity of the PAN2 nuclease in vitro. The nucleotide-binding site is juxtaposed to the RNase active site of par-1/pan2 in the complex and may actually bind nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active site of the deadenylase and thus increasing the efficiency with which this distributive enzyme degrades oligo(A) RNAs (By similarity); The pseudokinase domain, the coiled-coil (CC), and C-terminal knob domain (CK) form a structural unit (PKC) that forms an extensive high-affinity interaction surface for par-1/pan2.
Sequence:
MAATRYNSGDLRRQVGSPRAKNRDTKETLCRNVVIYGHCRWEDSGCTFNHDQNKASVSQTDLNSNRRVFNVESPSFTPANQQQSAGKKSTFSSQAASAAPFTPRGVGTSTPTLQQANDSTIFNPAAIREFTPQNYDVGNTISQNGAQHVTQDGGLYSDPFSISSLGQTMPPQGQYNPYANDPNNLAGAGAGLYQPAGFGNGLVHPPNYHLYQPPSELYRPSLQPYQRTTYDFFIPKDRRENLQKKLFHMQQLLPNSGLPNLDRWHSLFPLDTKATRNSTCFGYPSWMYKAQNNKNGRHFALRRIEGYRLTNEKAILNVTKEWKKIINANIVTVHEAFTTEFFGDSSLIFVYDFHPLSETLYDHHFPPNNSHNRLRNTNKIPENLLWSYVCQIANALLAIHNAKLAARCLELSKIIWENNRIRLAACSILDVLHHDSPNRKTIEELQQEDFVKFGRIILALATNTPTLNFNNIDAALATIVPRYSTQLRGVLEWLIKPSAPGETKTVETLLGGITTHLANFANFVMQESDEKEFHLMRELENGRIARLMFKLSVVNERGDSCGVHNWSETGERLLLKLFRDYVFHQVDADGKARLDTNHYLNCLSKLDASSEEQILLTSRDNATVFVVSYRSIRQMLDRAYGELGKESKPSATGATI
The following text describes a protein:
Function:
Aspartic protease, which is part of the necrosis cell death pathway. Promotes B.thuringiensis Cry6Aa stability by preventing its proteolysis by host gut proteases. Required for Cry6Aa-induced necrotic death of intestinal cells. Cry6Aa uptake into the host intestinal cells triggers an increase in intracellular Ca(2+) levels leading to lysosome rupture and to the subsequent release of asp-1 which leads to necrosis.
Subcellular Localization:
Cytoplasm. Lysosome. Secreted.
Sequence:
MQTFVLLALVAACSAAVIQVPTHKTESLRAKLIKEGKYTAFLASQHAARAQQLNTGFQPFVDYFDDFYLGNITLGTPPQPATVVLDTGSSNLWVIDAACKTQACNGYPDSGYTKQKFDTTKSTTFVKETRKFSIQYGSGSCNGYLGKDVLNFGGLTVQSQEFGVSTHLADVFGYQPVDGILGLGWPALAVDQVVPPMQNLIAQKQLDAPLFTVWLDRNLQIAQGTPGGLITYGAIDTVNCAKQVTYVPLSAKTYWQFPLDAFAVGTYSETKKDQVISDTGTSWLGAPNTIVSAIVKQTKAVFDWSTELYTVDCSTMKTQPDLIFTIGGAQFPVKSVEYVLDLQLGGGKCALAVFSMGSGGFGPSWILGDTFIRQYCNVYDIGNGQIGFATAVHKGL
The following text describes a protein:
Function:
Involved in endoplasmic reticulum-associated protein degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP to the ER during ERAD.
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein.
Sequence:
MLWFTGSIPEAIIASKQRKLPFVVYIEGSDEVSIEMGDVWSELQVSLLSQDKCIAIKLANESEQCAQFSQLYPVVCIPSLFIIGENGMPLEVLGGRLTSREIISKATAAFEVYHSQSSSGPVQVKSEDGSSEGSSQSAEHVRRHKHFSAQGNYLLQHIIILLSLQLLLSSSSLLSLLLLRLIEQKRKEKAEREKQEQIEKEAKRREEGQQLVNAKRQIEERKQQELVNQIREDRAKERAAREAVRQQIARDKAEREAQKQAELKERQQAQDTSASTTAASTYTGGGSYSNVRLQFRLPDGSGITHLFPADALLSTAHQYVVSHTGSRLPSVAMSTTYPRRQFTDDDMQRSLTDLGLAPSATIIVTEIFKHVGSSVITLSASSSEVDSAGLFGWLLAPFIAIFTFISAFLFGSPAMQRGSIIGGGGRALSLISSCFTLRTEVRRRATSPRGSNQSSDGNIHRLQNFRDDEDDQNTWNGNSTQQM
The following text describes a protein:
Function:
May be a ribosome silencing factor involved in organelle biogenesis and required for germination.
Subcellular Localization:
Mitochondrion.
Sequence:
MLTTLRSRCSSLLLNQSWKLAPNRIFASSPSFSSSAGISNVSEILTLPEVEKILADVKADNVTVIPTHNHCFWADFTVIATGRSDWHLRNIAQALVYRAKQKQKGAKHVMLPSVQGYNSKWIVIDYGKFVVHALDEKARGYFNLESLWSAESSGTDTSDQDLQNVFVKVRPKNNSKRKPAKVSS
The following text describes a protein:
Function:
DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM.
Miscellaneous:
MISCELLANEOUS: It binds to curved DNA in a sequence-nonspecific fashion.
Subcellular Localization:
Cytoplasm, nucleoid.
Sequence:
MELKDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYDQMWQHRNDPQFNRQFHHGDGQSFNAEDFDDIFSSIFGQHARQSRQRPATRGHDIEIEVAVFLEETLTEHKRTISYNLPVYNAFGMIEQEIPKTLNVKIPAGVGNGQRIRLKGQGTPGENGGPNGDLWLVIHIAPHPLFDIVGQDLEIVVPVSPWEAALGAKVTVPTLKESILLTIPPGSQAGQRLRVKGKGLVSKKQTGDLYAVLKIVMPPKPDENTAALWQQLADAQSSFDPRKDWGKA
The following text describes a protein:
Function:
Condenses choline with CDP-diglyceride to produce phosphatidylcholine and CMP.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MPVNLSMTPINKAKAWGVHAVTASGVILALLALLALVDNKPQACLLWLGLALLVDGLDGTLARKYEVKEMLPHFDGSVLDLVIDYLTYVFIPAIFIYRYIPLPEHFELLAVGVILVSSLFCFCNVNMKSTDNYFVGFPAAWNVVAVYFYVLDLHPWVNLATVLVLAALTLTRMKFLHPFRVRQFMPLNIAVTFVWLISSGLLIVQQPADLPILLGLWFAASAYFVGICLWRSAREWFG
The following text describes a protein:
Function:
Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule's plus end (By similarity). Required for cytokinesis. May be involved in a vesicle-mediated transport of myosin II, the Aurora kinase (aurK) and other proteins along mitotic extracellular microtubules toward the center of the cell and the cleavage furrow in order to ensure cell division coupled to mitosis.
Subcellular Localization:
Cytoplasm, cytoskeleton. Nucleus. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Concentrates in the nucleus in interphase cells, translocates to the cytoplasm at the onset of mitosis, appears in the centrosomes and spindle, and later is concentrated in the spindle midbody.
Sequence:
MKDYISSPLSPSNKKMPDNQKISPTNTPIRKKLFENTQSPIHFISNNNNNNITTPAKGLASVIKFNSSNYGNHHHQHHHQHHNNNNNSTVSGSAIKQHLNKSTFSTSGTTLTSSSDAILLPEDKVPMSVYLRIRPLSKKEIESKESNCFTVLNTTSVSIKSSRSDSDSNKFSFSSVLPPNTTQPQLFKTITHPLIQSFLTGHNVLLLAYGVTNAGKTYTVSGSKRNPGIIPRSLDLIFKSIPNNCLKKTENLTLSNNNNNSTNNNSKDSKDILADSSDDEYTKVDNIDSSDEDDSNAKINSNLLESFSTTNTTATTNAAAAASSTTATSNGDVIQISDQFNYSIWISYYEIYKKNIYDLLDDSPSSKKKQSLKIESDNSVVNIKGLKEILVSSVEDARDIVEQGESNRKVGGTKLNATSSRSHAVLTIKLFTSPRHIPKSDIHPSQIRCSKLCIIDLAGSERASRTETTGETFKEGSSINTSLFTLGKCIEGLKQQALQQQQQQQQHSSKRQSIHHSNPIPWRESDLTRICQEYFCGNGKASMIVNVSPSSCDSEETLNVLRFSASAKEITTLSKIKPMVFLPPPPTTPSISLKKRKSMEQPINNNNNNNNNNNNNAYYNITQLQNSVNEIKKKIHLDNLLAVGQLPISNNNNNNNGKFDYISMEKDQLLDQIQIYQKKLSNYEIKFVESEVTLREEFNNELIKNYIELENQYKERLVKESQLIHDRVQSKLSLIKNVNINQTNKLNCKIEKLELQLEQQQQKTMEANNKALVIVPQTNKRTDDEWIIEITEVQTERDNIQNKLNSILFELDEQRQHNQFSLERIQQFTLQTEQLEIERENLLTEIESMQSKGQELIKLRELEMMQLKESMNSDAQKDRENLEIQHNFETSNLNNQLQMERQEKLQIIEEMRMLKLELQQFKSNQSIEQQRNNNLIKNQYYNHNHPTAATAMTTTTPPIMSTPPIMSTPIKISSVGKFKATPSKSLIKNILGAHSNSPFKNANIESSVGGGFKVQLNIPGSPIQLAPGTPNSIQSQTPDRPILDPNQYSDSGLLMQEIDDDDYLNITGGGSANDGNWTDINVNDDSASEYDDLNSSSKSFTKKPKKTKSFGTIKRIKAVAMIPANIASSALNSSTTNIDEKEKLEKLEKLEKEKERLEKERLEKEKEKERLEKEREKEKERLEKERERLEKEKEKERERLEKEREKEKESKPKVVKKTTSSSSIISKKPSSKTTSSLTNNNNNNNNNNNNNNNNNNNNNNNNNNKSISPIKTVQSPNSPSPTKLQPHSSPNTNAKEYFNLMNPQVIIHFREPETNFVPSVTANTTTSTSTSTSKSSKKTLDSLKDTPKKIANIFSSKSSKEKEASTSSKSSSKISSSTSTTSTAPKLKRFAAITASHSIENGSESSPIEVDTPPRITKKPPVPIVSKVSSKKVSSSSSSTSSSSSSAATIKRVRKIVNEKKNYLEDDDDDVITKMATETPRKTLGLRPRNLISQPIQFR
The following text describes a protein:
Function:
Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Subcellular Localization:
Mitochondrion.
Sequence:
MARSARSSTTRLFYTLCSSTKRTPLTPQHPPPTPVAALLAGNFQLRHYAAGSATARVREEKDAVWRESLEKVRNIGISAHIDSGKTTLTERVLFYTGRIHEIHEVRGKDGVGAKMDSMDLEREKGITIQSAATYCTWKDYQVNIIDTPGHVDFTIEVERALRVLDGAILVLCSVGGVQSQSITVDRQMRRYDVPRLAFINKLDRMGADPWKVLNQARSKLRHHSAAVQVPIGLEDDFKGLIDLVQSKAYYFHGSNGEKIVTEDIPADMEAITSEKRRELIEAVSEVDDKLAESFLNDEPISSADLEAAIRRATIARKFVPFFMGSAFKNKGVQTLLDGVLSYLPCPVEVSNYALDQTKDEEKVTLTGNPSGPLVALAFKLEEGRFGQLTYLRIYEGVIRKGDFIINVNTGKKIKIPRLVRMHSNEMEDIQEAHAGQIVAVFGVDCASGDTFTDGSVKYTMTSMNVPEPVMSLAVSPVSKDSGGQFSKALNRFQKEDPTFRVGLDAESGETIISGMGELHLDIYVERIRREYKVEAQVGKPRVNFRETITKRADFDYLHKKQSGGQGQYGRVIGYVEPLEPGSGSKFEFENMLVGQTVPSNYVPAIEKGFREAANSGSLIGHPVENIRVVLTDGASHNVDSSELAFKLASIYAFRQCYTAAKPIILEPVMLVDIKVPTEFQGTVTGDINKRKGVIIGNDQEGDDSVITANVPLNMMFGYSTSLRSMTQGKGEFTMEYREHAPVSGDTQTQLVNTYKASKES
The following text describes a protein:
Function:
Component of the nuclear pore complex. Acts as a docking site for activities required for desumoylation and mRNA export. Required for the proper expression or localization of a subset of miRNAs. Plays a role in meristematic cell division by interacting with spindle assembly checkpoint proteins.
Subcellular Localization:
Nucleus envelope. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Nucleus, nuclear pore complex. Note=Located at the inner surface of the nuclear envelope during interphase and in the vicinity of the spindle during prometaphase.
Domain:
The N-terminal domain is involved in RNA and SUMO homeostasis while the C-terminal part is required for nuclear pore association.
Sequence:
MPLFMPDEELARLSSDAASVVAERADEYIRKIYAELDSVRAKADAASITAEQTCSLLEQKYLSLSQDFSSLESQNAKLQSDFDDRLAELAQSQAQKHQLHLQSIEKDGEVERMSTEMSELHKSKRQLMELLEQKDAEISEKNSTIKSYLDKIVKLTDTSSEKEARLAEATAELARSQAMCSRLSQEKELTERHAKWLDEELTAKVDSYAELRRRHSDLESEMSAKLVDVEKNYIECSSSLNWHKERLRELETKIGSLQEDLSSCKDAATTTEEQYTAELFTANKLVDLYKESSEEWSRKAGELEGVIKALEARLSQVESSYKERLDKEVSTKQLLEKENGDLKQKLEKCEAEIEKTRKTDELNLIPFSNFTRRVDNSGTSNMIEESQAVISKVPAGVSGTALAASLLRDGWSLAKIYEKYQEAVDAMRHEQLGRKEAEMILQRVLSELEEKAGFIQEERGEYERVVEAYCLVNQKLQDSVSEQSNMEKFIMELKADLRRRERENTLLQKDISDLQKQVTILLKECRDVQLRCGAARDDDEDDYPLLSDVEMEMESEADKIISEHLLKFKDINGLVEQNVKLRNLVRSLSEQIESRETELKETFEVDLKNKTDEASAKVATVLKRAEEQGQMIESLHTSVAMYKRLYEEEQKLHSSDSRSSDLSPAVVPGRKNFLHLLEDSEEATKRAQEKAFERIRILEEDFAKARSEVIAIRSERDKLAMEANFAREKLEGIMKESERKREEMNSVLARNIEFSQLIIDHQRKLRESSESLHAAEEISRKLSMEVSVLKQEKELLSNAEKRASDEVSALSQRVYRLQATLDTVQSTEEVREETRAAERRKQEEHIKQLQREWAEAKKELQEERSNARDFTSDRNQTLNNAVMQVEEMGKELANALKAVSVAESRASVAEARLSDLEKKIRSSDPKTLDMDSGGIVSLSDKEMSIELRTAKEEIEKLRGEVESSKSHMLQYKSIAQVNETALKQMESAHENFRLEAEKRQRSLEAELVSLRERVSELENDCIQKSEQLATAAAGKEDALLSASAEIASLREENLVKKSQIEAMNIQMSTLKNDLETEHEKWRVAQRNYERQVILLSETIQELTKTSQALAALQEEASELRKLADARGIENSELNAKWSEEKLMLEQQKNLAEKKYHELNEQNKLLHSRLEAKHLNSAEKNSRSGTISSGSTDSDHLEDSGLQRVVHYLRRTKEIAETEISLMRQEKLRLQSQLESALKMAESARGSLTAERASTRASLLTDDGIKSLQLQVSEMNLLRESNMQLREENKHNFEKCQEMREVAQKARMESENFENLLKTKQTELDLCMKEMEKLRMETDLHKKRVDELRETYRNIDIADYNRLKDEVRQLEEKLKAKDAHAEDCKKVLLEKQNKISLLEKELTNCKKDLSEREKRLDDAQQAQATMQSEFNKQKQELEKNKKIHYTLNMTKRKYEKEKDELSKQNQSLAKQLEEAKEEAGKRTTTDAVVEQSVKEREEKEKRIQILDKYVHQLKDEVRKKTEDLKKKDEELTKERSERKSVEKEVGDSLTKIKKEKTKVDEELAKLERYQTALTHLSEELEKLKHADGNLPEGTSAVQVLSGSILNDQAAAYVSAVEYFERVARSIASNSQVSTKPTDMVTEPSSGIPAAEPSTMTRVPSSTPLIKSPVATTQQLPKVASDNKEKRLISQKPSTEFRRPSGRRIVRPQLVKPEESPKVDVDMPEAEGTGDEGKQPAAHEPESQVTTSVRPVQTLVRKRQADSLVSEPQQDSLTQGETSSEIAPPASKKAKGSESHPDTSEGENLAKEPAIDELMDATTTTDGDNEETEAENAEEKTEEYVEAQQDNEADEPVEESPTETETIPTEEESRDQTEEENQEPLTDMESDKEEGELDLDTLEDLEEGTDVASMMRSPEKEEVQPETLATPTQSPSRMETAMEEAETTIETPVEDDKTDEGGDAAEEAADIPNNANDQQEAPETDIKPETSAATTSPVSTAPTTSSTLASAITSSGAPETEDPKRAPSPGGGSSTIVTLADRAQMKRRERIANIVVSRAPNPATRGARGRTVNLRGGGRLLPRGGRAPRGGRGQSPSPP
The following text describes a protein:
Function:
May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein.
Sequence:
MIQDQYLIECPINSDHDQKYLQNPPNTTVYTEVPPRQDTRDPRGINKHLKVDFSDVLAEPASFHSFDKVWTWSDILFESSKLWCYRIISLLCAVPVSLLSGILFALLGCLHIWCAMPCIQLCNICMPPVRTLWASVLDIFVAPICTSIGRCCSSIYVNVAKQRP
The following text describes a protein:
Function:
Regulatory subunit for cdc7 which activates its kinase activity thereby playing a central role in DNA replication and cell proliferation. Not required during the initiation of DNA replication in egg and during early embryonic development but is required later and throughout development. The complex cdc7-dbf4a phosphorylates mcm2 subunit.
Subcellular Localization:
Nucleus.
Sequence:
MKSTVAAVKNPTGKVQADVCKPFTGKLFYLDLTSKLISEKLEKDIKELGGAIEGFLSKEISYLITSKKEAKCVKTLKYVCSIPSPEAAPNTGESSTSPGNRRLCQEGNSSKKNEKSLVSRGKSLVKRAIKEQEILPKNSILSNALNWGVKILHVEEAKHYIEKKKTALQQVRKSQPVVKVESKPQTRRKVKPQKLKSPYIKVEDCSCQYRPLYLVLPQFRSFQNPVSNYSVEVDKKADPGQKLPETKQSVNKTGHGQDGANNPNIKLKEQKKHGYCECCLKKYDDLESHILSPQHKNFSESAYYQVVDDLISTFDFDFVDWSKYKNGRKGVGILMLAEKSKTEGQERNEANLFVSKTHNFSERVTATTPLQENTLKDQHASPCSLPCTPACNADQMFSLPSPAGSARLCNKKYKMDSNFGQLVATPLPSFNLKDSLTGSFGGREMFVAKLNETMEPATEGPKIKWDVCNIPSNISQCIPQKVDPIAQHVNQFPNGNTHCSEMTACQAALIYENVDSAADANIKLPKTVNDLHNKEGHRATDKIYPTVQSHEYLPDYSPSGNLHRKVKTSAHRNKNKDELFCRLSHKVSVPQQEDDSKFPSETLLALFESSEDKTEFFGFAGSPAYESCSMDDGDTPDQTHKKMLLSLFPHTTTSGSSFLGF
The following text describes a protein:
Function:
Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element.
Subcellular Localization:
Nucleus.
Sequence:
MCDLFWLSPGEQGDLSDVVRASLHRPHQLPTPAADEEEEEYSSLLREGGSGGDGLVVGHGHGDEQLGMVAMMMGGNTRLPSSDHHVISLHSPPATTYTRPHPEPLAGMIRRPGIGREGEMVVAPPPEIGERLQHMSIVHHPRVPAAMKPRKSQSKKVVCIPAPTAAPGASGRHSTSGEVVPSDLWAWRKYGQKPIKGSPYPRGYYRCSSSKGCPARKQVERSRTDPNMLVITYTSDHNHPWPTQRNALAGSTRPSSSSAARIAASSSSSSLAATAARNSSNTNVDVDCAGVHHQLKQESDLDLFADMDALNVFSSINKIQEDDSKQQLFDPFSSGFCDYI
The following text describes a protein:
Function:
Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity).
Sequence:
MSSTKAPVPPTQAEIQQIQDQLIKARDAFQVHETELQKLSASRSKLLTQLNENEMVKKEFDLLESEAKIYKLNGPVLFKQTKEEAENTITSRLDIINNNLKTIETNFKDIEKKAMEQRNKIFEYQNKIRSLTAPPPPQAQ
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. 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. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs) (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAASVKAAHELQSRTRTDDVLISGGVEFSSLLLSKPVLEGLSASGFQRPSPIQLKAIPLGRCGLDLIVQAKSGTGKTCVFTTIALDSLILENATTQVLVLAPTREIAVQIHAVVMAIGSAMEGLECHVFIGGRPISQDKQHLKKCHIAIGSPGRIKQLIEMGALMVSSIRLFVLDEADKLLEDDSSSSFQEQINWIYSSLPANKQMLALSATYPESLAQQLSRYMREPTFVRLNPTDPGLLGLKQYYKIVPSHSLPHKVFEEKVQSLLELFSKIPFNQALVFSNLHTRAQHLADILSSKGLPAVCISGGLSQDQRLEAMWKLKQYQCRVLISTDLTSRGIDAEKVNLVINLDVPQDWETYMHRIGRAGRFGTLGVAVTYCCHGEEENKMMAIAQKCSLDLMHLPDPIPPGIMEEACDHDVIIETLSKPKIPDNFKPEKKKKAKSEQMKSKPSRESHISVVITESVTGDKSCSRAETKTKNHSPKPGRQKQMAPAANLQHDSTITQKQQNNTLPKIPPLSSFKSHTGKRMTFDDALVDYETFIREGPGRSVEIIHQYDGFYRSQDKVNGLHDAHDEDEASESYVLEESQSHQDLPPAQEVSELSSEQKTSSESSSESEMEVESESSSSVPSKSTLEALPDNKVSLVRNHSELAKSTLPSTRVPQQATRSKQKPCQPQSQDTAHHHNLPHKHRTASKSSRRPTGPKRRTRETDETEEEEAGQDYWSSYRAWAEYYNSYYHHSPYNWMTAFYMNSVYIKEMMKH
The following text describes a protein:
Function:
Involved in compound starch granule formation and starch synthesis in endosperm. May act as a regulatory scaffolding protein and affect starch synthesis and compound starch granule formation through direct interaction with isoamylase 1 (ISA1). Binds starch, amylopectin and amylose through its C-terminal carbohydrate-binding domain (CBM) in vitro.
Subcellular Localization:
Plastid, chloroplast. Note=Localizes to granule-like structures in chloroplasts.
Domain:
Contains a C-terminal (448-529) carbohydrate-binding domain (CBM).
Sequence:
MLPLLLPLPVTPPPPLPSPTLTLAPASAPRRRLVLLAAAAPHHHHHHRRRRVYRRQRAAPTQTRAPRRTLSASNAARGEEDLEEAIYEFMRRSDKPGAFPTRAELVAAGRADLAAAVDACGGWLSLGWSSGGAEAGRASSSVGVHPDYPPEAGAAAAAGGASDLAQGAVWASSREAEASPSGRQPETEEEETETKFGTGLDGMLTRLQRERERVRPPLPRSSDGAGGERDNVALMGQSGAPSHSATGGRYTPKVPDNGNIHSYHPQNGALEHNKSSKSLTNDAWRTWSLDKGGFSDFQAAEIHSTNSRKSFRHDGLDILAQDDVHGPSNGVAVHDYDINDVDSERDDIHARLQNLELDLTAALHTLRSRFDKVISDMSEGDGAKAPNGLSDDWEFEETKVMQAQEELRSIRAKIAVLEGKMALEIIEKNKIIEEKQRRLDEAEKALSELRTVYIVWSNPASEVLLTGSFDGWTSQRRMERSERGTFSLNLRLYPGRYEIKFIVDGVWRNDPLRPLVSNNGHENNLLTVT
The following text describes a protein:
Function:
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Domain:
Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
Sequence:
MEVLCMVDKQVIEEIKNNANIVEVIGDVISLQKAGRNYLGLCPFHGEKTPSFSVVEDKQFYHCFGCGRSGDVFKFIEEYQGVTFMEAVQILGQRVGIEVEKPLYSEQKPASPHQALYDMHEDAAKFYHAILMTTTMGEEARNYLYQRGLTDEVLKHFWIGLAPPERNYLYQRLSDQYREEDLLDSGLFYLSDANQFVDTFHNRIMFPLTNDQGKVIAFSGRIWQKTDSQTSKYKNSRSTVIFNKSYELYHMDRAKRSSGKASEIYLMEGFMDVIAAYRAGIENAVASMGTALSREHVEHLKRLTKKLVLVYDGDKAGQAATLKALDEIGDMPVQIVSMPDNLDPDEYLQKNGPEDLAYLLTKTRISPIEFYIHQYKPENGENLQAQIEFLEKIAPLIVQEKSIAAQNSYIHILADSLASFDYTQIEQIVNESRQVQRQNRMERISRPTPITMPVTKQLSAIMRAEAHLLYRMMESPLVLNDYRLREDFAFATPEFQVLHDLLGQYGNLPPEVLAEQTEEVERAWYQVLAQDLPAEISPQELSEVEMTRNKALLNQDNMRIKKKVQEASHVGDTDTALEELERLISQKRRME
The following text describes a protein:
Function:
Immune regulatory cytokine.
Subcellular Localization:
Secreted.
Sequence:
FSRTMRISAVSLLLLSVCLLPVMAYPAKGGKLVHFGNCVLSVPIHDLEETIRGIKGHIVSASEGDPTILLLKIGTLDSVRSAESCCFLKQLLAFYLDSVLPHLRGVPTHVRRHASRLGNGLLLLARSVENCHCDCGEEVPDKTQSIRSTFDGMDKEAAVGKAVSEMDIFLNW
The following text describes a protein:
Function:
Vacuolar effluxer which mediate the efflux of amino acids resulting from autophagic degradation. The release of autophagic amino acids allows the maintenance of protein synthesis and viability during nitrogen starvation (By similarity).
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein. Note=Vacuole and punctate structures.
Sequence:
MAKISGLCVFKWYPLYAYQCPATGPSVQLKYSAMTPRHNNNVNHVYNGPDIQWEDESLRPPPAPRLFSRSSYASYASKASKRSFYSYTSSCFEADDERSDTLSFADWITTTMSGRMSPANAGDNSDSYPYGDDTDGDSSSGLPPPRYPGDDTRPTSQKELAGWYAYAFAAEVYVICGIGSFIPILLESLARENGVLLSDRSKPCGSSSDKHTTSAEGQCVVYVLGMEINTASFAMYTFSVSVLLQALLVVSISCAADHGNFRKKLLLAFAWIGSACVMAYIFISKSTYLIGALLAIISNTSFGASFVLLNSFLPLLVRHHPEIDQVGDYGSPGYATTEEGDDEDDEYQEDSTRNSTTALLGSRRYEEGEPLSRVQTTEELTSRELELSTQISAKGIGIGYIAGLFLQCVAIAILITLKNTTWSQRIVLCVIGAWWAIFTIPAAMWLRPRPGPPLPTKSNTGGIRALFHYTIYAWKSLFRTIHLARRLVDIVLFLAGWFLLSDAIATTSSTAILFAKTQLHMEPWALGMINVISTASGILGAFSWSFISRKFRLKAHQTILACIALFELIPLYGLMGYLPFVQAWGVGGLQQPWEMYPLAAIYGFVLGGLSGYCRSLYGELIPPGSEAAFYALYAITDKGSSVFGPAIVGAIIDASGEIRPAFWFLAAIVGTPALFIWFINVERGRTEGEALAEIIEGFKMNGQNGLNGNGADGLADDRRGSDASRAILGRYDDEDEE
The following text describes a protein:
Function:
Mitochondrial HMG-box protein that limits the copy number of mitochondrial DNA (mtDNA), antagonizing HMG-box containing protein ABF2, a mtDNA packaging factor.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MKATLLLKAQLSPVSYTTKKSFQRQLNRTPYTAFQYFFQLEVQKLHNVSKYEDIINHVRGNSNFKRFARNEWDSMSLTKKRLYYASFCQSMDIDILNVSKIELAKRLEIPIPAMSEYLLFRNKFKVKFDSHCSSLERKDRKSVPRPSITRKVATTEICSKSRSNTPVGKINPRKRLVALKRISRSENTAKNHSHEAQNYLYDYMKRFQQMCKECRYAWNEEVDYDQKLEIRKKLQVWRAKFEEMMDNEIQILQKNMDIMSKFGLRSESYLTAANHDTNTQPNNILPMTYLLKKK
The following text describes a protein:
Function:
Required for sperm flagellum function and male fertility.
Subcellular Localization:
Cell projection, cilium, flagellum. Note=Found along the full length of the sperm flagellum.
Sequence:
MNVIYPLAVPKGRRLCCEVCEAPAERVCAACTVTYYCGVVHQKADWDSIHEKICQLLIPLRTSMPFYNSEEERQHGLQQLQQRQKYLIEFCYTIAQKYLFEGKHEDAVPAALQSLRFRVKLYGLSSVELVPAYLLLAEASLGLGRIVQAEEYLFQAQWTVLKSTDCSNATHSLLHRNLGLLYIAKKNYEEARYHLANDIYFASCAFGTEDIRTSGGYFHLANIFYDLKKLDLADTLYTKVSEIWHAYLNNHYQVLSQAHIQQMDLLGKLFENDTGLDEAQEAEAIRILTSILNIRESTSDKAPQKTIFVLKILVMFYYLMMNSSKAQEYGMRALSLAKEQQLDVHEQSTIQELLSLISTEDHPIT
The following text describes a protein:
Function:
May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Sequence:
MASSTSDDDFITVVCSNPNRIQANTTSTDVEILISVTNIPSWDLPSILCHQTVKVQAHRNRLIQHSSYFNGLLSGSFSESGLDCIAIEWNLEAFLHILNCIYDCPLDVTSNNFLPLYEGALYFGVEMLLMRCKTWFSEVVSAEVPPQVQLDDLISIWSFGLEHARDFLPELCGSYLARNFMWAISMNCFVDIPYDLLLSCVKHMNLTVDSEMHLSNALLVWIDANTECMEGLSRNEDVCTGILKQIRLSLLPLWFAAEKRSSCHFSKFADESIDSIFRLLRIPSTGSVDALGASHLHDLRIRLTKFSKRVNLSSCSQITSVVLLLSLLPSANSIDYILRGIGQSPFNLERLDRDQCSEVLNLLPTLSFEAVQEVDISKCPRLHLQSAIECFRKSFPSLRILKAAFLLKFKISTLRKLVRKCPMVCEVDLTTDTSPIISSQVSVVSSSPAITPQISNLSLNVRDMTSFYNSGLSIAKLTLEGRNDLYDSDLQYISRFCVSLQYVNLKGCTSLTDVGIASLLRRCIKLHSVLVCDTSFGINSVLALCSSSSNHIAVEQIENELLDSLALNLQILHMGSCKCVDETSLLKLMSQMQKLKSLCLSDTRLSDGALYSFRGSSLEMLDISNTMVSNAAVAYLVGGNPGLKCLKARGCRNLSQQESDPQKREFSFSYSCRELHNEIGRACMLEEIALGWGFSYSSLEALKPAITSLRKITVGLGGLLGEDGLRKLPTICPMLELIILYFQVISDRTIMNIMANLKKLVVLAFCHCLGDISILSFKFPMPNLRKLKLQRVTPWMTNNDLFILTQSCANLVELSLLGCTLLDSESQQIISQGWPGLVSIHLEECGRVTTMGVSSLLDCKALEDLLLRHNGPGLQRSFIFDAASKLPMLRKVSLDFCDAAEGDFDIPNYGDRHFLSTLKIAKCKLQKGLKVSFVKAPRRRQVHKETLVLVWNSSTVTRTVVKERL
The following text describes a protein:
Function:
Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins; Probable hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins.
Sequence:
MTETIQSVVAHVDQQAMQKLADTLEIEANMTAILSLDERVKLKLKERARIEASARFSASYQKYKTISLTDSLALRKILFGQLMVPKEIDWCRESFIFHIHNYGLPFGLKIHKNGPCGVIAVVQAFVLRHLIFDEDDENNYKRLKAVNERERQNALALALADILWIAGEESKTAIVLLPPDDDRSKPIGASQVRLNDMTEDGILYQFNAFNDLRDFIKKKLPIFQHEFGYGVAFFLYSAILSRGIENIRNDMDDPEKILLTENERCSQELINLLLVGKAVSYVFNGILDYDYKLRKPLQQPLFGIDKRGVVGLLTLMEHVAEGNYTVGSKLKTPKYPIWVVNIELSFAVIFSCKRDLLNDWKAERQFHLWYYTGLVSQTELQRIHIDTLQTYMPKNKDNVEPLINHCIRTKWSGVKISSHSSISK