lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the conversion of hercynylcysteine sulfoxide to ergothioneine by cleaving the cysteine residue at the sulfur atom, the last step in the biosynthesis pathway of ergothioneine.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAENNVYGHEMKKHFMLDPDYVNVNNGSCGTESLAVYNKHVQLLKEAQSKPDFMCNAYMPMYMEATRNEVAKLIGADSSNIVFCNSATDGISTVLLTFPWEQNDEILMLNVAYPTCTYAADFAKNQHNLRLDVIDVGVEIDEDLFLKEVEQRFLQSKPRAFICDILSSMPVILFPWEKVVKLCKKYNIVSIIDGAHAIGHIPMNLANVDPDFLFTNAHKWLNSPAACTVLYVSAKNHNLIEALPLSYGYGLREKESIAVDTLTNRFVNSFKQDLPKFIAVGEAIKFRKSIGGEEKIQQYCHEIALKGAEIISKELGTSFIKPPYPVAMVNVEVPLRNIPSIETQKVFWPKYNTFLRFMEFKGKFYTRLSGAVYLEESDFYYIAKVIKDFCSL
The following text describes a protein:
Function:
Orphan receptor.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTNNSTCIQPSVISTTALPVTYIFLFIIGLFGNSLAQWVFLTKIGKKTSTHIYLANLVTANLLVCTAMPFMGIYFLRGFYWKYQSVQCRLVNFLGTLSMHVSMFVSLLILSWIAISRYATLMKKESKQEATSCYERMFYGHVLKRFRQPNFARTMCIYIWGVVLVIIIPVTLYYSVVEATEEGQSQCYNRQMELGARPSQIAGLIGTTFIGFSFLVVVTSYYSLVSHLRRVRTCTSITEKDLTYRSVKRHLLIIQVLLVVCFLPYSIFKPIFYVLHQREGDCQQLNYLIEAKNILTCLASARSSTDPIIFLLLDKTFKKTLYGLLTKS
The following text describes a protein:
Function:
Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.
Sequence:
MLFLKVRVLDIDLENLVLINSEDLKSSQYFPQDRVVVEFKGKEVIGILHSSTTLINRGEIGLPQKVVKELGVKEGDIVTIKHAEKPKSLPYIRKKMDGNKLKKEEIFEIIDEMVDGKLTNIEISAFVTSLYINGMDMDEIEAMTIRMAETGEMVNWEGHIFDVHSIGGVPGNKYALLVVPIVASAGLKIPKTSSRAITSAAGTADVVEVLTRVDLTIEEIKRVVKETNGCMVWGGALDLAPADDITINVERPLGIDPEPLLLSSVMAKKLAMGVNKLLIDIPTGYGAKVKSIKEASSLARKFIELSDRLRIVTECAITYGGQPIGRAIGPALEAKEALLALEDYTQAPTSLVEKSISLAGILLEMGGVAPTGEGKELAEDLLARGKAHDKFMEIIVAQGGKEVSSDEIEVGKYKADIHSPIDGYVTRISNAGITKIAKEAGAPNDKKAGIYLNVKVGNKVEKGDVLYTIYSDSEERLKSAIKLARILYPIKVEGMLLQKISRF
The following text describes a protein:
Function:
Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress.
Subcellular Localization:
Secreted.
Sequence:
MVIMMRNAKILRRLWGQRCRELCSCNTTSQHNSYAFFSMIVSSGNENGTVEREAIPNRTLKGFDIIDMIKDEIEEECPRIVSCSDILVLATRDGIVLVQLESRIITRAQFWKYGNIHNQCIMAGGLYYPVLMGRRDSKESFFDETMAEIPRPNGNITETLRLFSLRGFDERETVALLGGHNIGKIGCEFIQLRFSNFMGTAIPSGFLEELMQKCPDDNSTITKMFNEHTARGLSESAMSYSQGLSALSSFGTSFDNHYYKTLMRGRGLLFADQQLMANEKTAAVVMDYALDEGTKFRTEFAHAMDKLSNIGVLTGFQEEVRHSCSHLNSDQ
The following text describes a protein:
Function:
Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.
Subcellular Localization:
Cytoplasm.
Sequence:
MSQTITQSRLRIDANFKRFVDEEVLPGTGLDAAAFWRNFDEIVHDLAPENRQLLAERDRIQAALDEWHRSNPGPVKDKAAYKSFLRELGYLVPQPERVTVETTGIDSEITSQAGPQLVVPAMNARYALNAANARWGSLYDALYGSDIIPQEGAMVSGYDPQRGEQVIAWVRRFLDESLPLENGSYQDVVAFKVVDKQLRIQLKNGKETTLRTPAQFVGYRGDAAAPTCILLKNNGLHIELQIDANGRIGKDDPAHINDVIVEAAISTILDCEDSVAAVDAEDKILLYRNLLGLMQGTLQEKMEKNGRQIVRKLNDDRHYTAADGSEISLHGRSLLFIRNVGHLMTIPVIWDSEGNEIPEGILDGVMTGAIALYDLKVQKNSRTGSVYIVKPKMHGPQEVAFANKLFTRIETMLGMAPNTLKMGIMDEERRTSLNLRSCIAQARNRVAFINTGFLDRTGDEMHSVMEAGPMLRKNQMKSTPWIKAYERNNVLSGLFCGLRGKAQIGKGMWAMPDLMADMYSQKGDQLRAGANTAWVPSPTAATLHALHYHQTNVQSVQANIAQTEFNAEFEPLLDDLLTIPVAENANWSAQEIQQELDNNVQGILGYVVRWVEQGIGCSKVPDIHNVALMEDRATLRISSQHIANWLRHGILTKEQVQASLENMAKVVDQQNAGDPAYRPMAGNFANSCAFKAASDLIFLGVKQPNGYTEPLLHAWRLREKESH
The following text describes a protein:
Function:
Protein-lysine N-methyltransferase. Monomethylates PRMT5, modulating its transcriptional activity (By similarity). May also act as a histone methyltransferase. Plays a critical role in cardiac development. Acts as a key epigenetic regulator of gene expression during cardiac development via its dual activities as a methyltransferase and negative regulator of HDAC1.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MDLPCQDWVCHVEQKWAELRSEETERFSLLTDIDAIFNYGLSLICPEDLNILSRISEKFSVKKSPETASEFRQQGNLSFKVKDYPAAVLHYSKGVCHADKNTDELSLCYANRSAALFYQGLYQACLEDIRRSLEAGYPSHLQDKLQTRQTACQNQLRKAEKPNIPHTDHQLSPCQKTVNSTGHLSDGVSVYFSSDKGRHMLVMENKPAGEVVLEDEAYCSVLIPANIFNTGTNKAVETFGTEDRHCHHCLSQSLSFVPCPKCSYARYCGESCQKDAWDQWHQWECPVGADLLAIGVLGHLALRVVLKAGQTEVQMGIKNTKDHVTTYKNDSPVQLSLGGDCGKSLDHTDCFHGSSYMGIYSLLPHVAQHSPASRFLMAITMAVIYGKLQGGPPPNKWMSFKDEGVKASWQPEMSMLGATALRHMMQLRCNAQAITAVRVKEESGMAVQSSSEIRIATAIFPVLSLLNHSCSPNTSISFTTGFQPDPHNQLGCSEGHFDHPKGSRSGVTVTVRASKDLTAGQEILHCYGPHRSRMEVKERQRLLLEQYFFQCVCQACQRDLSEGSPNAKEHTAPGMKCVKCGKPLQSHTDGYTCSWSSCGHQISSADVQNRLQGFQLLLDEAVHLMEQDRLNEALHILQSAFSQANSILTETHPFQGELADALARLYASTGEWSLAASHLKRSLVAIQAQFGEDSIELGRQLFKLAQLHFNGRDGVASLSVIPRARRLLSLHCSPRCEELQELSEMEHCLQGLL
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase involved in the positive regulation of the gametogenesis progression. Mediates the proteasomal degradation of KRP6, a cyclin-dependent kinase inhibitor which accumulates during meiosis and blocks the progression of subsequent mitoses during gametophyte development. Functions in association with RHF2A. Possesses E3 ubiquitin-protein ligase activity when associated with the E2 enzyme UBC8 in vitro.
Sequence:
MSNFTYTSAFNLSDNSPFNPAIGSSSSSSSALVVASDDDNNTDDACSICLEPFTLQDPSTVTSCKHEYHLQCIIEWSQRSKECPICWQLFVLRDPASQELLAAVEKERLLKTRNISSSSPISIHHSHDDFHSEEEESQFSSFDEQFLRHLTEAAHRRCLLRRRDGQISSSLVSSSDPTTIHPTDLVNLYRLSAISHVEHQNSNPCPSPGSMTPSPVSGHSSIPADSNNGSRISPGPSPSRSSQSPKSPEASSLPEAIKSKLAAASAKYKESISKSKQGLKEKLLARNNSVKELSKGVQREMNAGIAGVARMIERMDFSSKRFGGSAHVSTSTATASGFNFSFKGKRVEANSKSNNNGDKTEPQKLQGGETC
The following text describes a protein:
Function:
Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinase GIN4. Septins are also involved in cell morphogenesis, chlamydospores morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization, and spore wall formation. CDC11 is required for the correct localization of SEC3 at bud tips and bud necks. Plays a key role in invasive growth and virulence.
Subcellular Localization:
Bud neck. Note=Localizes to a tight ring at the bud and pseudohyphae necks and as a more diffuse array in emerging germ tubes of hyphae.
Sequence:
MNYSTENVSSAALRKRKTLKKSINFSIMIIGESGSGRSTLINTLCGGNSIVPTSSTATQDPFTKKLTLRHENVELEDNEGHKISLNIIDTPNFANSINCDDDFKIIVDFIRHQFDEVLLEESRVKRNPRFKDGRIHVLIYMINPTGHGLSDIDVKFLQHVNNLVNIIPIISKADSLTPKELKLNKELILEDLNNYGINFYKFNEYDYEQDYIDEEIIEYNKYLNSLIPFAIIGANEYRSNPNGSEDEDDILKLRILNKDFKPIDIDNAEINDFTILKNVLLVTHLNEFKDITHDSIYENYRTEALSGKQFQYVNKDSAKQEISESDYLMKEEQIKLEEERLRKFEERVHQDLINKRKELLERENELKEIEKRLLAEGLKFDENGDVVKVHEEESSENEVKVI
The following text describes a protein:
Function:
May play a role in proteolysis leading to mobilization of nitrogen during senescence and starvation.
Sequence:
MAHVRVIFISSLLFLLFSAVAAGLTFDDSNPIKLVSDSLHGFEASVVKVIGDTRHALSFARFAHRYGKSYENEKELKMRFAIFSENLDLIRSINKKGLPYTLALNDFADLTWQEFQKHRLGAAQNCSATTKGNHKLSGDVLPERKDWREEGIVSPVKDQGNCGSCWTFSTTGALEAAYHQAFGKGISLSEQQLVDCAGAFNNFGCDGGLPSQAFEYIRYNGGLETEEAYPYTAHDGTCKFSSENVGVRVLDSVNITLGAEDELKHAVAFVRPVSVAFEVASDFRFYKDGVYTSTICGKTPMDVNHAVLAVGYGVKNDVPYWLIKNSWGDDWGDNGYFRMEMGKNMCGKFQTLHLDNVKQMHIT
The following text describes a protein:
Function:
DNA polymerase delta (DNA polymerase III) participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair.
Miscellaneous:
MISCELLANEOUS: Present with 2410 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MDQKASYFINEKLFTEVKPVLFTDLIHHLKIGPSMAKKLMFDYYKQTTNAKYNCVVICCYKDQTIKIIHDLSNIPQQDSIIDCFIYAFNPMDSFIPYYDIIDQKDCLTIKNSYELKVSESSKIIERTKTLEEKSKPLVRPTARSKTTPEETTGRKSKSKDMGLRSTALLAKMKKDRDDKETSRQNELRKRKEENLQKINKQNPEREAQMKELNNLFVEDDLDTEEVNGGSKPNSPKETDSNDKDKNNDDLEDLLETTAEDSLMDVPKIQQTKPSETEHSKEPKSEEEPSSFIDEDGYIVTKRPATSTPPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK
The following text describes a protein:
Function:
Controls the onset of sexual development, by inhibiting the expression of ste11, in a pathway that is independent of the cAMP cascade.
Sequence:
MQTYTGIIKTPLDAIILFEACRIGLLPRVQRRLSDHERSLIRAGSVFVWDEREAGMRRWTDGKSWSASRVSGSFLTYREMEGKRKPYHHGLSTDGSLKRSPSADTTGNSSLNAYSNEDSGAASLSDEESVDDENLRGLHYKPNGLIKQSFSITTSLNHKLHLISYSSPIPDPSLVTPSSDVNLSRITIPYGLYPDAGPPLVQAPKFLAPYDILVEKVACSEDARVLDKLRQALWL
The following text describes a protein:
Function:
E3 ubiquitin ligase acting as a negative regulator of oxidative stress tolerance, probably by mediating 26S proteasome-mediated degradation of PRMT13/PRMT4B, thus preventing APX1 and GPX1 accumulation via the reduction of histone H3 methylation (H3R17me2a). Confers sensitivity to cadmium CdCl(2) and salt NaCl stresses.
Subcellular Localization:
Nucleus.
Sequence:
MAIYYKFKSARDYDTISMDGPFITVGLLKEKIYETKHLGSGKDLDIVISNAQTNEEYLDEAMLIPKNTSVLIRRVPGRPRIRIITREEPRVEDKVENVQADMNNVITADASPVEDEFDEFGNDLYSIPDAPAVHSNNLCHDSAPADDEETKLKALIDTPALDWHQQGADSFGPGRGYGRGMAGRMGGRGFGMERTTPPPGYVCHRCNVSGHFIQHCSTNGNPNFDVKRVKPPTGIPKSMLMATPNGSYSLPSGAVAVLKPNEDAFEKEMEGLTSTTRSVGEFPPELKCPLCKEVMRDAALASKCCLKSYCDKCIRDHIIAKSMCVCGATHVLADDLLPNKTLRDTINRILESGNSSAENAGSMCQVQDMESVRCPPPKALSPTTSAASGGEKKPAPSNNNETSTLKPSIEIAEITSAWASAEIVKVEKPVDASANIQGSSNGKEAAVSQLNTQPPKEEMPQQVASGEQGKRKKKKPRMSGTDLAGPDYMMPMGPGPGNQYFNGFQPGFNGVQHGFNGVQPGFNGFHHGFNGFPGPFPGAMPPFVGYGFGGVIHPDPFAAQGFGFPNIPPPYRDLAEMGNRMNLQHPIMGREEFEAKKTEMKRKRENEIRRSEGGNVVRDSEKSRIMNNSAVTSSPVKPKSRQGPPPPISSDYDRRRRSDRSSPERQSSRRFTSPPRSSSRKSERDRHHDLDSEHDRRRDRPRETDRKHRKRSEKSSSDPTVEIDDNNKSNVFTRISFPEESSGKQRKTSKSSPAPPESSVAPVSSGRRHHSRREREMVEYDSSDDEDRHFKRKPSRYKRSPSVAPSDAGDEHFRHSKRSKGERARA
The following text describes a protein:
Function:
Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second half-reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components (By similarity).
Sequence:
MEKIFLNGEFVSPSEAKVSYNDRGYVFGDGIYEYIRVYNGKLFTVTEHYERFLRSANEIGLDLNYSVEELIELSRKLVDMNQIETGVIYIQATRGVAERNHSFPTPEVEPAIVAYTKSYDRPYDHLENGVNGVTVEDIRWLRCDIKSLNLLGNVLAKEYAVKYNAVEAIQHRGETVTEGSSSNAYAIKDGVIYTHPINNYILNGITRIVIKKIAEDYNIPFKEETFTVDFLRNADEVIVSSTSAEVTPVIKLDGEPVNDGKVGPITRQLQEGFEKYIESHSI
The following text describes a protein:
Function:
Involved in nonsense-mediated mRNA decay (NMD) by acting as a bridge between the mRNA decapping complex and the NMD machinery. May act by targeting the NMD machinery to the P-body and recruiting the decapping machinery to aberrant mRNAs. Required for UPF1/RENT1 localization to the P-body. Plays a role in glucocorticoid receptor-mediated mRNA degradation by interacting with the glucocorticoid receptor NR3C1 in a ligand-dependent manner when it is bound to the 5' UTR of target mRNAs and recruiting the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay. Also acts as a nuclear receptor coactivator. May play a role in controlling the energy balance between energy storage and energy expenditure.
Subcellular Localization:
Nucleus. Cytoplasm, P-body.
Domain:
The interaction between PNRC2 and nuclear receptors is dependent on the SH3 binding motif.
Sequence:
MGGGERYNIPDPQSRNASKNQQQHNRQKTKDQNSQMKIVHKKKERGHGYNPSAVQNGGKTKSLSNNSNWNASLSSPSLLFKSQASQNYAGAKFSEPPSPSVLPKPPSHWVHVSLNPSDKETMTFQLKTLLKVQV
The following text describes a protein:
Function:
Modulator of macroautophagy that causes accumulation of autophagosomes under basal conditions and enhances autophagic flux. Represses cell death and promotes long-term clonogenic survival of cells grown in the absence of glucose in a macroautophagy-independent manner. May have some role in extracellular matrix engulfment or growth factor receptor recycling, both of which can modulate cell survival.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle, autophagosome membrane; Multi-pass membrane protein. Endosome membrane; Multi-pass membrane protein.
Sequence:
MWLLALVPICLAVFGSTGIWTVFAVSVMNNSVNLTHIFPYISDCAWYPPQKCLFTQICGLIIITALWIGMIQFQQVKQLGNHGRVNNASAVMGFLSCGGLSVCSNTQVSEFHLVGALVSFVSALAYFWMQVYLTYQGQSFPERSWMGPLRALFCTIATLLGIACILSRGRIKMAGMRAATFSLTFSKAIGFYATNCDSGVAVCEFALVMVIFFLFALFAVEFRHIECRILIMKKHILKDEKSLESVKVNVSVVELFK
The following text describes a protein:
Function:
Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart. Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein. In brain, involved in cognitive function, such as learning and long-term memory.
Sequence:
WVILSLAPLRTEIKFTVKSPSAAACGARWGSGLPPAYRPRPSTWTLNGRIQKVVFSKYCNSSDIMDLFCIATGLPRNTTISLLTADDAMVSIDPTMPTFPLLHLSFFFWFIEKEELIQSVLTQVAEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSPRAGLGSPARERPGEAAGWLCRHLPDAPATDHPLLLCPQMLSCLEHMYHDLGLVRDFSINPITLRRWLLCVHDNYRNNPFHNFRHCFCVTQMMYSMIWLCRLQEKFSQMDILILMTAAICHDLDHPGYNNTYQINARTELNHHCAVAFQILAQPECNIFANVQPDGFKQIRQGMITLILATDMARHAEIMDSFKETMENFDYSNEEHVTLLKMILIKCCDISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPVVEEIMLQPLWESRDRYEELKQIDDAMKEVTRAAWETPSSRSERRKALFQIP
The following text describes a protein:
Function:
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Sequence:
MLIKWRFVLRVSVSFNMAKSNSKPYYAVRKGRKTGVFTSWDQVQPLVDRFPGAQQKRFESLAQAELWVSTAVCVSPPKSTPPSSAGSNGTQSPRLDRSPRKPTWSSSQSLGLEGVRRDLPSSPTRSKPRMDNYTTKVNNEKMEVATRATNLENPTNLTGKEETTWCPTTSEMEMGWSMFRMIQSDPWNKVEVEGRIESGRTLFEIYFNENNSQNVVRPVVVADCQTEEEQVARAVLVGVYEACKLIHARNDGLKYEIQTTSMFVIECYYRRCFKWQINGWVDTDNTPVPHREVVEPTMELLQQLKGRIRFGKLKVVEQ
The following text describes a protein:
Function:
May be involved in a process influencing telomere capping.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MGQKESQFKVLWQLQTHEEYMKQTSSFLRDFNALERYNLKENFEALSSFDNGEKIWVEDAFTTFFGIPDVIQLSPFFYRSACSFGRDLNINRQRLTFSALARFLASYTGRHKDVWSDFESNLMIIASWCDSFPKFRVEVLKNSKQISRLIHSDVQNISNFFDQNFGIRRSNIYQLCLLLLCISKLKPGESVGCHINSFLDSMFVKEQKAAFYVLQGISPDISSNIIKPSYLLHFLESNPYFLKSLGSLFELALFPHSAHNQKVQDDVSPLNDFAILSPLIHAQICFFLPKSVWQVNGLTSLFRASFHGYSMYALERKMCNYHNPSILLIKAKKINANHKSSSRPISLDATIPRKYPPHCIGTDKAVPQKFGADFHNENILLGAYISTRWRQSHMGFFGDHSTLLFQLQPIHQVYYASNLDKNYCMFDKNVGLGFGLSRHKVTNKVQYDVPGVCMYIDDGLEYGLFRHAGDGAFKPATNYENFEYEERFLIQDLEVIGVDTTKPVEPIHIGL
The following text describes a protein:
Function:
Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Sequence:
MNKTIIAERFSKAISTYPREANVQRQIANKMIRLLQKHIPSPCPKVIEFGCGTGIYSRMLLRTLRPEELLLNDLCPEMRYCCEDLLREKQVSFLSGDAETISFPDKSTLITSCSALQWFDSPEEFFKRCNTLLHSQGYFAFSTFGKKNMKEIRELTGKGLPYRSREELEAALSLHFDILYSEEELIPLSFEDPMKVLYHLKQTGVNGLSAQSSLYPKHEKQTWTRRDLQHFCERYTQEFTQGTSVSLTYHPIYIIAKKKKV
The following text describes a protein:
Function:
Required for neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity. Does not act by preventing deneddylation, but rather facilitates neddylation, possibly by acting with rbx-1 to recruit the Nedd8-charged E2 enzyme to the cullin component of SCF-type complexes.
Subcellular Localization:
Nucleus.
Sequence:
MNRLKSDQKTKLRQFVQWTQVTEAVSLNFLAKANWNIEYAMTLYFDNPNLFAGSTPQPSVDRSNIERLFNQYVDPKDKVGEKRMGPHGINRLLTDLGYEATDRRVLVLAWKFTAQTQCEFSLDEWVKGMTALQADTVQNLRQRIDSINSGLESDKAKFHELYLFAFNYAKSAACRNLDLETAICCWDVLFGQRSTIMTQWIDFLWAQENAAASRLAQNVGASNAKQFKSVWISRDTWNLFWDFILLSKPDLSDYDDEGAWPVLIDQFVDYCRENLNYPKPGNASNDQQMETPSYY
The following text describes a protein:
Function:
Integral membrane subunit of the KtrCD potassium uptake transporter. The 2 major potassium transporter complexes KtrAB and KtrCD confer resistance to both suddenly imposed and prolonged osmotic stress.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MRLKFGKLIQALSPAQLIALYYFLAVTVAVILLSLPAAHKPGADWTFIDALFTAVSSVSVTGLTVVDTADTFSTIGIFILAFVLQFGGIGIMTLGTFIWLIMGKRIGLKERKLIMVDQNQSQFSGIVNLMKQVLFLILWIEFFGGLILGTYFLTYYDSYQEAYLHGFFASISATTNGGFDITGNSMIPFRHDYFVQFITMLLIIFGAIGFPVLVEVKDFLFSKHRRYPFTLFTKITTITFGSLVLFGAIGIFALEANHAFAGKSWHDILFLSLFQSTATRSGGLATIDISQLSDSTLFFICALMFIGASPSSVGGGIRTTTFALNLLALFHFARGNKAVKVFKRELHPADLMKSLVVTMMAILLVFGATLILTITEKHSLLELLFEVCSAFGTTGLSLGITADLSSVGKCVIMIVMFIGRIGILTFLYLIGRKEIEANYHYPKERVIIG
The following text describes a protein:
Function:
Required for pre-mRNA splicing.
Subcellular Localization:
Nucleus.
Sequence:
MANSKPRFDRADERALLDDRGYSGALIRGQNPALLFEKGVRERITESYYWKEQCFGLNAATLCDRAADLKFIGGTTGITGKPTPFLCLAFKMLQLVPEKAIVLEYLNFGGDEEEEDEEGGVKKEEEEDGDEKPQDPNAAGKLGQFKYLRCLAAFYIRLAWEPVEIYKTLEPLLTDYRKIKRRLKDAFTLTYVDQFIDDLLTKDRMCATSLWKLPSRANLEDLDMLEPRESPLGDEVDELDEDMKREGSEGSVRSRTRSYDSRSRSRSYDSRSRSRTRTRSRSYEDGERRRTRSPSDRGRRDSTSRSRTRSRSRRGEHSGDER
The following text describes a protein:
Function:
Tubulin-binding protein that acts as a negative regulator of Notch signaling pathway. Shuttles between the cytoplasm and the nucleus and mediates the nuclear export of rbpj/rbpsuh, thereby preventing the interaction between rbpj/rbpsuh and NICD product of Notch proteins (Notch intracellular domain), leading to down-regulate Notch-mediated transcription. May play a role in neurogenesis.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Shuttles rapidly between the cytoplasm and the nucleus.
Sequence:
MPDNLYATNMSLDLSITGHSTALPQRKSRSTYRFKAANSYVDESLFGSSGVRVDQTLQWNTAPPSQTPLLWSPGEIKENKKTSSCRPKSTPAGTPRKKIQYRVKSRTPSYCDESLFGGKVEECTWDAPWVKKEDTVKIRPLLWSPSPRLVQQSSMQNAKQGPLRAVHPPETSDSPLGTHKGLGAFWKPPESDSDYSPSPFSARQRQSTPGRETVRSASCSGRVTARRGSVKMQERPPWK
The following text describes a protein:
Function:
Involved in plant defense. Confers resistance to the bacterial pathogen Xanthomonas through recognition of the microbe-associated molecular pattern (MAMP) eMax. Functionality seems to depend on the presence of the receptor kinase SOBIR1 as an adapter protein.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MRTDERRRWWVKPKKHITLVFITITMIIQFQMKGCVSCVETERMGLLQLKSYLKNLVDAEEEEEEGLSILKSWTHHEGDCCRWERVKCSDAINGHVIGLSLDRLVPVAFESQTRSLNLSLLHSFPQLQSLNLSWNWFTNLSDHFLGFKSFGTLDKLTTLDFSHNMFDNSIVPFLNAATSIRSLHLESNYMEGVFPPQELSNMTNLRVLNLKDNSFSFLSSQGLTDFRDLEVLDLSFNGVNDSEASHSLSTAKLKTLDLNFNPLSDFSQLKGLESLQELQVLKLRGNKFNHTLSTHVLKDLKMLQELDLSDNGFTNLDHGRGLEIPTSLQVLDFKRNQLSLTHEGYLGICRLMKLRELDLSSNALTSLPYCLGNLTHLRTLDLSNNQLNGNLSSFVSGLPSVLEYLSLLDNNFDGSFLFNSLVNQTRLTVFKLSSKVGVIQVQTESSWAPLFQLKMLYLSNCSLGSTMLGFLVHQRDLCFVDLSHNKLTGTFPTWLVKNNTRLQTILLSGNSLTKLQLPILVHGLQVLDISSNMIYDSIQEDIGMVFPNLRFMNFSSNHFQGTIPSSIGEMKSLQVLDMSSNGLYGQLPIMFLSGCYSLRVLKLSNNQLQGKIFSKHANLTGLVGLFLDGNNFTGSLEEGLLKSKNLTLLDISDNRFSGMLPLWIGRISRLSYLYMSGNQLKGPFPFLRQSPWVEVMDISHNSFSGSIPRNVNFPSLRELRLQNNEFTGLVPGNLFKAAGLEVLDLRNNNFSGKILNTIDQTSKLRILLLRNNSFQTYIPGKICQLSEVGLLDLSHNQFRGPIPSCFSKMSFGAEQNDRTMSLVADFDFSYITFLPHCQYGSHLNLDDGVRNGYQPKPATVVDFLTKSRYEAYQGDILRYMHGLDLSSNELSGEIPIEIGDLQNIRSLNLSSNRLTGSIPDSISKLKGLESLDLSNNKLDGSIPPALADLNSLGYLNISYNNLSGEIPFKGHLVTFDERSYIGNAHLCGLPTNKNCISQRVPEPPSVSTHAKEEENEEEGNVIDMVWFYWTCAAVYISTSLALFAFLYIDSRWSREWFYRVDLCVHHILQFKRSSVCN
The following text describes a protein:
Function:
Part of the yfcOPQRSUV 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.
Sequence:
MSKFVKTAIAAAMVMGAFTSTATIAAGNNGTARFYGTIEDSVCSIVPDDHKLEVDMGDIGAEKLKNNGTTTPKNFQIRLQDCVFDTQETMTTTFTGTVSSANSGNYYTIFNTDTGAAFNNVSLAIGDSLGTSYKSGMGIDQKIVKDTATNKGKAKQTLNFKAWLVGAADAPDLGNFEANTTFQITYL
The following text describes a protein:
Function:
O-methyltransferase that specifically monomethylates 5'-monophosphate of cytoplasmic histidyl tRNA (tRNA(His)), acting as a capping enzyme by protecting tRNA(His) from cleavage by DICER1. Also able, with less efficiently, to methylate the 5' monophosphate of a subset of pre-miRNAs, acting as a negative regulator of miRNA processing. The 5' monophosphate of pre-miRNAs is recognized by DICER1 and is required for pre-miRNAs processing: methylation at this position reduces the processing of pre-miRNAs by DICER1. Was also reported to mediate dimethylation of pre-miR-145; however dimethylation cannot be reproduced by another group which observes a monomethylation of pre-miR-145.
Subcellular Localization:
Cytoplasm.
Sequence:
MFDPGAARNGNFINYYSFNPPSERLKFIPKDLLIQVCWENCEARQEYKYEDSGRKVFLLLDVGCNSGELTRNLFNQFSEDPNAKPNSHSLFTMKILGIDIDPVLIERSEECNQNSEKLSFKMADIMSEKDRSTVLESFLKENYSLQFDISFLFSITMWIHLNNGDDGLKNFLLYICQISKCILLEPQTWKNYKSAVRRMKRSKSEPFKHFPSLKWRENVVNEICEFLTESCSMNLIKKFGETGWDRSLLLFKRSK
The following text describes a protein:
Function:
Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MVKLDRYIGVTVFVAILAVLGVILGLALLFAFIDELNDISASYGIGDALRFIFLTAPRRAYDMLPMAALIGCLVGLGTLASNSELTIMRAAGVSLSRIVWAVMKPMLVLMLAGILVGEYVAPWTENIAQSGRALAQGGGDSQSSKRGLWHRQGREYIHINAVQPNGVLYGVTRYRFDEQRGLESASFAKRARFETDHWQLEEVTTTLLHPREKRSEVVKLPTERWDAQLSPQLLNTVVMEPEALSISGLWQYIHYLADQGLNNNRYWLAFWTKVLQPLVTAALVLMAISFIFGPLRSVTLGQRIFTGVLVGFVFRIAQDLLGPSSLVFDFPPLLAVVIPASICALAGVWLLRRAG
The following text describes a protein:
Function:
Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular Localization:
Cytoplasm.
Sequence:
MATELAYAPPMKSGKLGFEGTQEVQHRIRITLSSKSVKNLEKGLCPIRSLLFLPVRSRFVRLRSDACCLAVCSDLVKGAKEKQLKVKGPVRMPTKVLNITTRKSPCGEGTNTWDRFEMRVHKRVIDLVSSPDVVKQITSITIEPGVEVEVTISDQ
The following text describes a protein:
Function:
Demethylates proteins that have been reversibly carboxymethylated. Demethylates the phosphatase PP2A catalytic subunits PPH21 and PPH22. Forms inactive complexes (PP2Ai) with phosphatase PP2A-like catalytic subunits. Involved in the regulation of cell cycle progression at START.
Sequence:
MSDDLRRKIALSQFERAKNVLDATFQEAYEDDENDGDALGSLPSFNGQSNRNRKYTGKTGSTTDRISSKEKSSLPTWSDFFDNKELVSLPDRDLDVNTYYTLPTSLLSNTTSIPIFIFHHGAGSSGLSFANLAKELNTKLEGRCGCFAFDARGHAETKFKKADAPICFDRDSFIKDFVSLLNYWFKSKISQEPLQKVSVILIGHSLGGSICTFAYPKLSTELQKKILGITMLDIVEEAAIMALNKVEHFLQNTPNVFESINDAVDWHVQHALSRLRSSAEIAIPALFAPLKSGKVVRITNLKTFSPFWDTWFTDLSHSFVGLPVSKLLILAGNENLDKELIVGQMQGKYQLVVFQDSGHFIQEDSPIKTAITLIDFWKRNDSRNVVIKTNWGQHKTVQNT