lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
During primary cilia disassembly, involved in cilia disassembly. Required specifically to control cilia retraction as well as the liberation and duplication of the basal body/centrosome. May act by stimulating AURKA activity at the basal body in a cell cycle-dependent manner.
Subcellular Localization:
[Isoform 1]: Golgi apparatus, Golgi stack. Golgi apparatus, trans-Golgi network; [Isoform 2]: Nucleus; Cytoplasm. Cytoplasmic vesicle. Note=Accumulates specifically at the basal body and ciliary necklace during the early steps of cilia assembly and disassembly, when structural, functional and regulatory proteins are delivered to cilia. At S phase, accumulates in vesicles and declines during mitosis. In node pit cells, found close to the ciliary membrane along the axoneme. In spermatocytes, localizes to particles along the stabilized microtubules of tails.
Sequence:
MNTEEIPVAPPLRGVTPALQWKVNNYSFGTRQARKLFPHYHPPTWLGNLYLPLRGMPHTGPGCYAAATDWNGLAYNLSKVPTSTKGYAIGARTAVRFKPISKDVTPYPGMYQKVDTLSEKHKKSFAPFNILMPRFRSAAKGDSYPGPGTYNPEMKSVPKVTWPMKFGSPDWSQVPCLEKRTLKAELSADKDFRKHRSRVAYFSLYYQ
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Required for proper complex I assembly. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MSATAGRVVRAGSAAVRTVAPLKSNNAAEARMSVLQAYKEFQRLTPKFWWDFGLHDMPLGVFRAVIKKQFTKNGHLTDVRVVDRLVGETNMHMESIRMAYYNPDHVRNYLFAENVEAKPKDFLSKFLNGKE
The following text describes a protein:
Function:
Involved in the high-affinity L-arabinose membrane transport system. Binds with high affinity to arabinose, but can also bind D-galactose (approximately 2-fold reduction) and D-fucose (approximately 40-fold reduction).
Subcellular Localization:
Periplasm.
Sequence:
MHKFTKALAAIGLAAVMSQSAMAENLKLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDDQFVNAKGKPMDTVPLVMMAATKIGERQGQELYKEMQKRGWDVKESAVMAITANELDTARRRTTGSMDALKAAGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKHWLIVGMNDSTVLGGVRATEGQGFKAADIIGIGINGVDAVSELSKAQATGFYGSLLPSPDVHGYKSSEMLYNWVAKDVEPPKFTEVTDVVLITRDNFKEELEKKGLGGK
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.
Sequence:
MQQGDGTEAQVTWDDQQNINRFGRLNNRLHELADEIRLAKEANENLEDAGNELILSDEDVVRFQIGEVFAHMPVDDVETRLEQMKEDAAKKLEKLEEEKESILAQMAELKKILYGKFGEAINLEED
The following text describes a protein:
Function:
Phosphatase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-glucose in a two step process.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MPSGAQGNTQSAAYKRIVNVSRNFQFKAALNKDTREWTFQHRSSGTALYSAIASLGDPSSPWDAVYVASPGPVQISEGNDHTVETKIDEAAVVHRSSSIVISPEDQEIFLKKATEYYRKKNIEADIVPVWGKVQRVPQAKSSSATITPSVSNKLSTAYQSIKSEALKDGPMYADSVLWDVLHYRIPTLDGYQQHNLWKNFTRWSQYFADNIVSNYRPGDLILIHDYSLFLLPRLIRKQLSDAPIVFFLHAPFCTSEVFRCLSKRAEILKGVLASNVIAMQTDSYTRHFLSTCSNVLGLETTSTHIDTSDGFRVVVFSSHVSIDVPRVYSRCNSKPVSLKIQQLKSLYPSDKKLIVGRDQLTKACGVTHKLRAFRELLIHFPKWRGHVVLIQITSLPVGNNYSNEELKKTENLVAQINSEFGSLDYTPVIHFHQLLDPDEYYALLSVANIACVSSVRDSMNTMALEYVACQQKNKGSLILSEFSGTAELLLSAYLVNPYDYSRFAETINYCLNMTEKERERRFSSLWKQATSQSSQQWIYKLINRAAYEVKALESHMTTPLLTYNILIKPYRNAKRRLFLLDYDGTLIESARNSIDAVPTDRLLRTLKRLASDSRNIVWILSGRSQKFMEEWMGDISELGLSSEHGSAIRPPLAGSWSSCAENLDLSWKDTVRDFFQYYVERTPGSYIEEKKHSISWCYQNANTTYSKFQSLECQTNLEDMLKHYDVEISPAKSFLEVHPNYLNKGSIVRRILKRSGSVDFVFCAGDDKTDENMFEVFLPTAFSNSHLIDEIDSTEYSGSHHTDDNSDANKVENVKVATFRVHIGLTDKPTLSDYHLPAPRDLGELLHNL
The following text describes a protein:
Function:
Required for plant immunity against the bacterial pathogen Pseudomonas syringae pv. tomato DC3000 (Pst DC3000).
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Sequence:
MAERVYPADSPPQSGQFSGNFSSGEFPKKPAPPPSTYVIQVPKDQIYRIPPPENAHRFEQLSRKKTNRSNCRCCFCSFLAAVFILIVLAGISFAVLYLIYRPEAPKYSIEGFSVSGINLNSTSPISPSFNVTVRSRNGNGKIGVYYEKESSVDVYYNDVDISNGVMPVFYQPAKNVTVVKLVLSGSKIQLTSGMRKEMRNEVSKKTVPFKLKIKAPVKIKFGSVKTWTMIVNVDCDVTVDKLTAPSRIVSRKCSHDVDLW
The following text describes a protein:
Function:
Fasciclin-like arabinogalactan protein; part of the gene cluster that mediates the biosynthesis of elsinochrome C, a perelyenequinone phytotoxin structurally similar to cercosporin. The first step of elsinochrome C biosynthesis is performed by the polyketide synthase elcA which catalyzes the formation of nor-toralactone. The starter unit acyltransferase (SAT) domain of elcA initiates polyketide extension by the selective utilization of acetyl-CoA, which is elongated to the heptaketide in the beta-ketoacyl synthase (KS) domain by successive condensations with six malonyl units introduced by the malonyl acyltransferase (MAT) domain (By similarity). The product template (PT) domain catalyzes C4-C9 and C2-C11 aldol cyclizations and dehydrations to a trihydroxynaphthalene, which is thought to be delivered to the thioesterase (TE) domain for product release (By similarity). The bifunctional enzyme elcB then methylates nor-toralactone to toralactone before conducting an unusual oxidative aromatic ring opening. The next step in perylenequinone biosynthesis is an O-methylation at the nascent OH-6 of the elcB product performed by the O-methyltransferase elcD. The oxidative coupling of the two monomeric naphthol units in perylenequinone biosynthesis is catalyzed by the FAD-dependent monooxygenase elcE and the multicopper oxidase elcG. ElcG might catalyze the first intermolecular coupling in a regio- and stereo-selective manner via a phenol radical coupling mechanism and the elcE could forge the second C-C bond intramolecularly via a hydride transfer mechanism. The fasciclin domain-containing protein elcF might also play a role duting this step (Probable). The last piece of the puzzle in the biosynthesis of elsinochrome C is the additional annulation by enolate coupling to afford the dihydrobenzo(ghi)perylenequinone system, catalyzed by the FAD-dependent monooxygenase elcH.
Sequence:
MKLFTLLLPALTSAHSLSTLLSTHPTLSTLHSLLKQFSLLDDFNTLANITVIAPTNQAYLDLANWGFNVSQIPAPVARALFQYHVLDGEWESESIIGKGKVVHTYLKPPVLTNVTAGAAVKLSSVDGTIMTESGLGVAGGVEDVNLRFDGGVLHTLNASMVLPHNITLTAQINGLGRFLELMNRAGVVAEFEGLKDVTVFVPHDDALEKADVGKMSKEQLASLLRGHVVPNRVLYGEVFGKKGGYKSSNGWEIHVGKTADGTLTVNGIKVVKEDVILYAGVAHVIDKVLVADRVEHKGDRSYLHLDAQKPLR
The following text describes a protein:
Function:
Microtubule-associated force-producing protein that is targeted to at the leading edges of the forming cell plate during cytokinesis. Also plays a major role in plasma membrane maintenance and cell wall integrity with implications in vesicular trafficking, polar cell expansion, vascular formation, and other aspects of plant growth and development, including stigmatic papillae expansion. Collaboratively with DRP2B, participates in clathrin-coated vesicle formation during endocytosis. Necessary for BOR1 polar localization in low-boron (B) conditions as well as for BOR1 endocytosis and subsequent degradation under high-concentration of boron. Has a GTPase activity. Required for the sterols-dependent dynamic high lipid order observed at the cell plate of dividing cells. Together with SH3P2, converts the fused vesicles to tubular structures at the cell plate and phragmoplasts during cytokinesis. With DRP2B and PIP5K3, required for the precise coordination of polar ARAC3/ROP6 and ARAC4/ROP2 placement and subsequent root hair positioning during planar polarity formation in root hair-forming cells, probably by mediating the correct basal-to-planar polarity switching of D6PK into the polar, lipid-enriched domain. Involved in endocytosis required for cellulose deposition during cell wall formation and elongation. Interacts with plasma membrane-mimetic liposomes and induces their clustering.
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, phragmoplast. Cytoplasm, cell cortex. Cytoplasmic vesicle, clathrin-coated vesicle. Cell membrane. Note=Microtubule-associated and localized in the forming cell plate, at the vicinity of sterols, during cytokinesis, especially at the leading edges. Accumulates in a sterol-enriched, polar membrane domain during root hair initiation. Forms discreet dynamic foci in the epidermal cell cortex, which colocalize with part of the clathrin endocytic machinery. Co-localizes with BOR1 in the cell plate and the plasma membrane.
Sequence:
MENLISLVNKIQRACTALGDHGDSSALPTLWDSLPAIAVVGGQSSGKSSVLESIVGKDFLPRGSGIVTRRPLVLQLQKIDDGTREYAEFLHLPRKKFTDFAAVRKEIQDETDRETGRSKAISSVPIHLSIYSPNVVNLTLIDLPGLTKVAVDGQSDSIVKDIENMVRSYIEKPNCIILAISPANQDLATSDAIKISREVDPSGDRTFGVLTKIDLMDKGTDAVEILEGRSFKLKYPWVGVVNRSQADINKNVDMIAARKREREYFSNTTEYRHLANKMGSEHLAKMLSKHLERVIKSRIPGIQSLINKTVLELETELSRLGKPIAADAGGKLYSIMEICRLFDQIFKEHLDGVRAGGEKVYNVFDNQLPAALKRLQFDKQLAMDNIRKLVTEADGYQPHLIAPEQGYRRLIESSIVSIRGPAEASVDTVHAILKDLVHKSVNETVELKQYPALRVEVTNAAIESLDKMREGSKKATLQLVDMECSYLTVDFFRKLPQDVEKGGNPTHSIFDRYNDSYLRRIGSNVLSYVNMVCAGLRNSIPKSIVYCQVREAKRSLLDHFFAELGTMDMKRLSSLLNEDPAIMERRSAISKRLELYRAAQSEIDAVAWSK
The following text describes a protein:
Function:
Reversibly inhibits the activity of ATP2A2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in the heart muscle. The degree of ATP2A2 inhibition depends on the oligomeric state of PLN.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein. Sarcoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MEKVQYMTRSALRRASTIEVNPQTRQRLQELFINFCLILICLLLICIIVMLL
The following text describes a protein:
Function:
Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAASTRKNKAAADGSPSKHPEKPAAGVEQDSSDNESSQEDDDQTVPVQVNNACITELKNALDDTMKSYLTSKVGFTQDYFCDDVKLGLGWTSNIIAAGISLAGWHFGWEKTQGYTAYCVGAYMVLSLALTVFTSTVEKKKVFVGTKPSKASGTGPDKVTISTEVKPFDPVYQLQLEYETCKKSGPPKKYQVALKPHFKEFFDVDGILDESRWNNYLDNALKTAISKT
The following text describes a protein:
Function:
Required for (1->6)-beta-D-glucan synthesis and normal cell growth.
Miscellaneous:
MISCELLANEOUS: Present with 815 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum lumen.
Sequence:
MRLLALVLLLLCAPLRAWTYSLRYGIPESAQVWSILVHLLGDVDNQLLTNLYPLVTGLDDEIDIQENLVALTSNVLRERYDKEDVADLLELYASLYPMGMIQHDISSNAEQDDANSSYFVLNGNRYEKPDDVFYLKSKDLTIQQKVPDVDVIQPYDVVIGTNSEAPILILYGCPTVIDSDFEEFNRNLFMEAMNGEGKFRFIWRSTCSLDGKSVEYPLTHPLEITLQNGSRMSSIPQLKKILYTVPKEILVGADNDDQLHDLEPEELRELDLRVTSLISEFYQYKKDITATLNFTKSIVNNFPLISKQLIKVSSVNKDIITSNEELNSKGFDYNMLGLYINGQNWKITSLTPYNLLTALKTEYQSLLKITNLLQELEPSKCILDSKFLLNKFSQFSLGKLQNLQPIKMDLHTIPGFSESVIYFNDIESDPQYDELVNSVQAFFDKSKFGELPEIKQNWSEIIFVIDFARLEDSEVKEALGGLVRAVNVVSQGYPQRVGLLPFSSDSDKSVVNKIYELKNSTDNLTELKSFLETMLLADGLSANAKHSKHIPVPDVFHLLDELQIDETSIIINGEIYPFRKNAWNYLIAKVIKKDTEFIRKELSNSSPKNKQISVRDLLHYKSANLRHNKYTPNYFADSVYSSVNNTALESVCSERIGYYTKNEEYNLLHTITLVDDFGSIHALKRLRNLLHTSFVGVRIRIIHVGDISDIWYQLRGSLSQKDPIGSINTFIDALKLKKVKSHTYKKSGLNQLGLHKWLPDIPLFELQKGSFIALNGRFIHLDQNEVPETEHFEAIIKREALRTIDSVFALDLLFPGFSQEIINPDLIEMISSILTRLFYQGTHIYNNGIDYTTESSLPRMDLSEFFRPNNLTMFEDGKSASIDLLLILDPLEERTQMILSLVEQFRPLKFVNIQVILMPTLELNIVPIRRIYVDDADIVKSITSEDSRSDPEVDIEMDVPNSFIVDNNYRIKKLLIELHSFSSKTVLSTGNIDGMGGVCLALVDSAGNIIDKTTTMKTFGYGQFHTDKFLKGCYIKSCDSRYTVQSFSTDGHPDFIPSDSLDILSYNPQKIAVKISEEPTHEEEYEEGRNNDTIINIFTILESGPDEEERYMQMILSILSKCPETQKVNFFILDQPFISDTLRKSCEYINSSDEMRGNVIFLNYEWPQWLRPQRFSSRRRDVSRFLFLDVLLPQNISKVLYMSPTEVPLDPFDIFQFQGLKRAPLGLFRMSGDGYWKEGYWEKMLRENNLEFYSTEPAFLVNLERFRELDAGDKYRIHYQRISTDAMSLVNIGQDLVNNLQLEVPIRFLKGSYKKKLVINDECVSEWKKKINKFASSPGDEDVPGESVSSKYQDSDNAAPLHDEL
The following text describes a protein:
Function:
ATPase required for the correct placement of the division site.
Sequence:
MAFTPPRLLPLPLPPAAAPASTRAVSARHHGGRTAPELSGPTPRVVVVTSGKGGVGKTTTTANLAASLARLGLPAVAVDADAGLRNLDLLLGLENRVHLTAADVLAGDCRLDQALVRHRALQDLHLLCLSKPRSKLPLAFGSKTLTWVADALRRSPNTPAFILIDCPAGVDAGFVTAIAPAEEAVLVTTPDITALRDADRVAGLLECDGIKDIKIIVNRVRPDLVKGEDMMSALDVQEMLGLPLLGVVPEDAEVIRSTNRGVPLVLNDPPTPAGLALDQATWRLVERDVMTAVMVEEQERPKKKGGFFSFFG
The following text describes a protein:
Function:
Transcriptional activator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters.
Subcellular Localization:
Nucleus.
Sequence:
MECAEAALKTSCRMEMAVKTPQAVLEDLWPVNGQNGVVCDDFFVDELLDLSNEEGFVNEEPAEEDEEEEDKGFVSVSPRQDRQNSTTNIVISAKDEFGSELIVPAEDLANLEWLSHFVEESFSEFCTPFPGGISTEKPMNEGPEPEPEPEQAKPCFKTPVPAKARSKRARTSGRVWCLGSPSLTESSASSTSSTSSSSPSSSWLVYPNAAQYEGPVEQFYSEEKQPEKKQKKKAIGEAASGGGAAQTPRRCSHCGVQKTPQWRTGPRGAKTLCNACGVRYKSGRLLPEYRPACSPTFSSELHSNHHRKVLEMRRKKEPSGVSESGLAPPAVSRF
The following text describes a protein:
Function:
C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.
Subcellular Localization:
Periplasm.
Sequence:
MGKWVTIIFVLFLYAIAQQENPAEEVKKQKELLLKEMGILPGDVYAEQGRDMFNKPMGNAGKSCSSCHGQDGRYLRGAYAHMPRYYKDMDAVADLDTRIKYCMEKYMGVGNVKHDLNFKSIATYVATLSNGMKMDVKLTHPKEREMYEKGRELWYARVGKMDFSCAICHDSEAGKRVFLQTVVAVKEDKVATHWPAYRFSNDQLWTMEDRIRGCFGDMRVAPPEHFHWAVVALNLYLSYKAKGGVVRVPGFIY
The following text describes a protein:
Function:
Orphan nuclear receptor.
Subcellular Localization:
Nucleus.
Sequence:
MNERGMLVDPRFDAFFKLEQIDDYKYDGADTSPSTSNGLPETSNGGRLICDVCGDVAFGKHYGINACNGCKGFFRRSVWSRRQYSCRFGGDCPVVKEHRNVCRSCRLKKCFEVGMNPDSVQNERDRNAKNGGMGGPMSSPTQSSLCKELTISNGQIKRKRLRPETVEKTTQTDGKLEINDDFDFENMQQNPTPPGLLPLKIERISTPPSDLPVPMDFSIHSAVLDIEQKVFYNCPVAVDNSINATKTPITLPFEVVFRQPHLVCNRYPMRFSNTRVLTPEDLIDGWRRHFTYYSDWCHAMDEFKALSPEDQIVLAKKKIILHGWLVHAYYSYKSGCNGICFANGAAHLPEGGHPSITEFYKECMPRYLNYVIYPMHNFQMDDAEMVLIKCIMFFSSESGLSAAGRQIVSAAREKYLSALYNYGRANKCTTSAQATLRIAKFMIMLSAITSLTHLMNEGVHVTSLFNIIEFDELIQATHKTTPPQHSPPAPMG
The following text describes a protein:
Function:
Essential for the formation of class I meiotic crossovers.
Subcellular Localization:
Nucleus.
Sequence:
MRTRFLNIDYFSTPPSHVFETLGFLNLPAPDNFPAPIVYNGEEDRLRFGSIENVSIPIGNLPIEAALSKFLSDVVPDRVSVDYRVFEIDDSSLGVYYSDEKDDGDAIADKATPKIIELETPELDFEMENKLLCTSEDHLQCFSEVLEIKNDPVKYEGSDIILQNSKDIQEQIYSVDYIPSDYFTENNTSVAENECFRKIQPWFKDARFPLLEVDEVNLSELSSLSVLDKVFTVLETIEPQDTNAGSSLIINSKELIGSKDYDLLDVLSTDCYLNKSGQSDVVPEDEFSEMDIVTILEISNAEEFQGKVAVPVTYEEFQILDVDISDVFDIFLCLQKAIEPEICYGMFSKEMNFKDFDELVVSSELAFTDDAFKSLPTPILHDYEMTRSLELIYEDVLSKIKPQSLSASNDIYLPWNLLEERNHNHCDYPFEEIVTFNIDYNWEASEGDKWVYDFIFSEDAFCEPLVEKCTEPFYGISNLDEHAPVNTSHGLLENPFQKTGARDCAVDDNAKKATLLFKSMSAFDDLTFFMDPKKAVIEDNLESRVEAAKTTNHKCMSIDSKASCRSGGMHPNPKTEEMILHSVRPSENIQALVGEFVKSYLTLVKDESENLSEDKLKLLSISKGKLIDCIRKANVHKTQLADDKTFTFALLLAIKQMTWYMCFFGIHVAYIYLNKVCRSSNPMKIGLHTLYSAVETEHKSDETDITRSHPSLAVIQGILQSEFARGNSKALLLAEKVFWSSLKRLLMSMGLSYNDLNSPSPSGNRPNVHEAIELGFLPISDCLIISYEQISPSFPVENFSVIVEYGGPNASPRYSFPSKLDSFPSFHFIKVELDMPSACGQLCAGVTVPYSLKMIKGDEVETKTGWLEEVLNFVPLEKVCYAGSSETTNESEFISMPQESERKRGIIEQGLSDQRSVIVVNTKTVDKEMIISRRSTYQKVLAMEKEGVQVVERDSDLPVDLMLSPAVCLLWYDSETVSKKSAATIGTSSSSLSWIGDIATNVLTSLSFSFSTCIMVFEGEPAFLAAVMDSSDELYAAAGSLGISLQMFCSSSANLTDEIILKCIKSSVKLSKLHVKMPESESLAESFLTKFPSVNPLTAQVILSSSGSLLEFMKLPHKSKVERTQKYHVPEESVDLFSSVCRYGAREDSRSVMTDSSSSVSSGPDSDTHHVSVHSGSKKKQYIAEKDEIDMDDLVHFSPSIEFADTQLKSSGDFQLDDSWSSKDHEIFHFDPVTEFSDAPFKPSGISHPNDSWPSKDPERFDKKSGPGSSSKDTFWEKDQPDFSVEDSLPGIPELEDWSFPVKDKFMSQNRGCKFPVMRDFNLHDNRNSENFIADYKGEVIDRADKYLEEDFPPSPGYNRFARIVSDVNEEELPRKSKSSRKLSFFGSLQPNFPKAADIDSSSERYATEKDSKYDNNTSLRGYADNYPAKRQRTLLEEVLTRRSAVPTTELPFREEISHFGGSPLSNAIRSSNQVQSSPWTVDFLNRVRERSRARKQQQSLPSYASPPSLETPGNIKKANTKRKSPSILEFFKYKGGNKLQEEKRQKRSKNSSASPKNERFYSPLKSCTPIDKRAKQSLSYTANGTGQTKLVWK
The following text describes a protein:
Function:
May act as a low affinity receptor for acetylcholine.
Sequence:
MSVTHGKMGLSLTQEILSHLGLANKTAAWGTLGTLRTFLSFSADKDVQRLLKAIAGQGVDRIAILDVLTNRSREQRQLISRAFHERTQQDLLKSLQAALSGNLERIVVALLQPAAHLDARELRTALKGSGSAEDVALEILATRTPPQLQECLAVYKHNFQVDAAEDIKSETRGILRDLLLALAKGGREAYTGIIDYNLAAQDVQALKQAEGPSTERTWVLVFTQRNPEHLVRVLNQYQWYTGHGLEKTVRARFHGAACVALLNLASVIRNTPLYFADKLHQALQETEPNYQALMRILISRSETDLLSIRAEFRKKFGKSLYSSLQDAVKGDCRSALLALCRAEDL
The following text describes a protein:
Function:
Orphan nuclear receptor.
Subcellular Localization:
Nucleus.
Sequence:
MQSYTNRICAVCGDTPAKIHYGVLACFGCKGFFRRAVKDGRNKYVCRFEKNCEVTKFERNACRYCRFRKCLLVGMNPDYVRPDREKSKKGKTVLSKKKSVSRSLSYRLADPSDWTSFLSPSSRKQLSEIGKLAETCSTSTNFDGIGNFSLKSLIADRSLARKTGDSEAMDCSNSPRQLNEQFLGIERIVQCVDYIDRFLVMLEEEHCRKFSVEDKSALISDTMIHLLLFESTSRFVAKGAPGLEDLKLSLAQLPICTTHLTQKIADVFETYLRKPPSIIEYSVLKAYIVLSAESTVLSNSLNESLSLARENLSELLFKVIKHSRNKTSISAANSLSTILHFVYESRNLASRIRQSQQPFFVRDSDPKIPFHKILTDIINPEVSDLLLTTANCRKLSTQMGSSLSSVPPVPPPSDTVPLFHFSPPSLSPCQISAPPPPQQQYTDYSQMPSTSSYPANSSPFQSPYRPNSLSSFPKIPLEMTKSIEEFLRPNGMTTDEMNKPLEKNWADGFRLTPVFNKDIVSQFFPELSNINQHHPF
The following text describes a protein:
Function:
Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Plays a role in the complex assembly and recruits GspM resulting in a stable complex in the inner membrane. Provides thus a link between the energy-providing GspE protein in the cytoplasm and the rest of the T2SS machinery.
Miscellaneous:
MISCELLANEOUS: Part of a cryptic operon that encodes proteins involved in type II secretion machinery in other organisms, but is not expressed in strain K12.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein.
Sequence:
MPESLMVIRSSSTLRKHWEWMTFSADSVSSVHTLTDDLPLESLADQPGAGNVHLLIPPEGLLYRSLTLPNAKYKLTAQTLQWLAEETLPDNTQDWHWTVVDKQNESVEVIGIQSEKLSRYLERLHTAGLNVTRVLPDGCYLPWEVDSWTLVNQQTSWLIRSAAHAFNELDEHWLQHLAAQFPPENMLCYGVVPHGVAAANPLIQHPEIPSLSLYSADIAFQRYDMLHGIFRKQKTVSKSGKWLARLAVSCLVLAILSFVGSRSIALWHTLKIEDQLQQQQQETWQRYFPQIKRTHNFRFYFKQQLAQQYPEAVPLLYHLQTLLLEHPELQLMEANYSQKQKSLTLKMSAKSEANIDRFCELTQSWLPMEKTEKDPVSGVWTVRNSGK
The following text describes a protein:
Function:
May function as a transcriptional repressor of cellular proliferation that regulates floral determinacy and relative size of basal pattern elements along the proximo-distal axis of the developing gynoecium.
Subcellular Localization:
Nucleus.
Domain:
Contains a slightly degenerated ERF-associated amphiphilic repression (EAR) motif, which may be involved in the activity of transcriptional repression.
Sequence:
MAEPPPSYLHFVGPAKTRSSSKRHSFSSSAHPASHRLFPCQYCPRKFYTSQALGGHQNAHKRERAAARRNLGVLANSPPILDDNNTFLRPYPCFYQNPFQGSTSGNEPLQEQPTMMTMDGYDPFHPYPYVYPFALSGNNNDGGNGVMEEDEPLDLDLSLRL
The following text describes a protein:
Function:
A 3'-5' helicase probably involved in DNA repair. Translocates in an ATP-dependent manner 3'-to-5' on single-stranded (ss)DNA, unwinding any encountered duplex nucleic acid. An RNA:DNA hybrid with a 3'-ssDNA loading strand is a 4.5-fold better helicase substrate than 3'-tailed double-stranded (ds)DNA; substrates where the helicase loads on a 3'-ssRNA tail (DNA:RNA and RNA:RNA) are not unwound. Unlike its M.smegmatis counterpart, the ATPase is not ssDNA-dependent. Forms a clamp around the ssDNA loading strand (By similarity); Excises uracil residues from DNA; forked DNA with a dU residue is the best substrate followed by ssDNA. Inactive on dsDNA with a dU residue or DNA with an 8-oxoguanine residue. Uracil residues in DNA can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Domain:
The Lhr-Core is composed of 2 helicase domains, a winged-helix (WH) domain, and Lhr-specific domain 4. It is followed by the C-terminal domain (CTD). The Lhr-Core has ATPase activity but does not oligomerize. The C-terminal domain (CTD) has uracil-DNA glycosylase activity but requires the Lhr-Core for maximal activity. The purified Lhr-Core binds DNA, while Lhr-CTD does not.
Sequence:
MADNPDPSSLLPDVFSPATRDWFLRAFKQPTAVQPQTWHVAARSEHALVIAPTGSGKTLAAFLYALDRLFREGGEDTREAHKRKTSRILYISPIKALGTDVQRNLQIPLKGIADERRRRGETEVNLRVGIRTGDTPAQERSKLTRNPPDILITTPESLYLMLTSRARETLRGVETVIIDEVHAVAGSKRGAHLALSLERLDALLHTSAQRIGLSATVRSASDVAAFLGGDRPVTVVNPPAMRHPQIRIVVPVANMDDVSSVASGTGEDSHAGREGSIWPYIETGILDEVLRHRSTIVFTNSRGLAEKLTARLNELYAARLQRSPSIAVDAAHFESTSGATSNRVQSSDVFIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQVGGVSKGLFFPRTRRDLVDSAVIVECMFAGRLENLTPPHNPLDVLAQQTVAAAAMDALQVDEWYSRVRRAAPWKDLPRRVFDATLDMLSGRYPSGDFSAFRPKLVWNRETGILTARPGAQLLAVTSGGTIPDRGMYSVLLPEGEEKAGSRRVGELDEEMVYESRVNDIITLGATSWRIQQITRDQVIVTPAPGRSARLPFWRGEGNGRPAELGEMIGDFLHLLADGAFFSGTIPPWLAEENTIANIQGLIEEQRNATGIVPGSRHLVLERCRDEIGDWRIILHSPYGRRVHEPWAVAIAGRIHALWGADASVVASDDGIVARIPDTDGKLPDAAIFLFEPEKLLQIVREAVGSSALFAARFRECAARALLMPGRTPGHRTPLWQQRLRASQLLEIAQGYPDFPVILETLRECLQDVYDLPALERLMRRLNGGEIQISDVTTTTPSPFATSLLFGYVAEFMYQSDAPLAERRASVLSLDSELLRNLLGQVDPGELLDPQVIRQVEEELQRLAPGRRAKGEEGLFDLLRELGPMTVEDLAQRHTGSSEEVASYLENLLAVKRIFPAMISGQERLACMDDAARLRDALGVRLPESLPEIYLHRVSYPLRDLFLRYLRAHALVTAEQLAHEFSLGIAIVEEQLQQLREQGLVMNLQQDIWVSDEVFRRLRLRSLQAAREATRPVAATTYARLLLERQGVLPATDGSPALFASTSPGVYEGVDGVMRVIEQLAGVGLPASLWESQILPARVRDYSSEMLDELLATGAVIWSGQKKLGEDDGLVALHLQEYAAESFTPAEADQANRSALQQAIVAVLADGGAWFAQQISQRIRDKIGESVDLSALQEALWALVWQGVITSDIWAPLRALTRSSSNARTSTRRSHRARRGRPVYAQPVSPRVSYNTPNLAGRWSLLQVEPLNDTERMLALAENMLDRYGIISRQAVIAENIPGGFPSMQTLCRSMEDSGRIMRGRFVEGLGGAQFAERLTIDRLRDLATQATQTRHYTPVALSANDPANVWGNLLPWPAHPATLVPTRRAGALVVVSGGKLLLYLAQGGKKMLVWQEKEELLAPEVFHALTTALRREPRLRFTLTEVNDLPVRQTPMFTLLREAGFSSSPQGLDWG
The following text describes a protein:
Function:
Component of the SCF(sconB) E3 ubiquitin ligase complex involved in the regulation of sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor.
Sequence:
MPPRDTVATSPHRRRPSINAKSRSRPRTATVSTLPSSSTSDLDHDVWTGLPLVDSGDDMGGSALETMTPVCGQPGRRRSAKSFSGLRHSVDGLRALGRRLSVTIRSKSSRTSNSPFQHEHELGPQNSQDDEEDGFDHPEYVPASQGVSIPLPIPGKGLEPPIVPNHLCSGAAARAAAAAQNEMARKSEQAKLTRDSESGIGIVLQDRSDSDDETDVVRSDPAVAFPTEIMAQVLSYLDPESLMNSGLVSRAWSEQVSSQHVWRNVFRSYYGKRCHPGSGKQPAAGLGKNTFQQDWKRLYLIRRTLESRWKEGKAAAIYLQGHTDSVYCAQFDEDKIITGSRDRTIRVWDARYPWACRKIIGPAPGGVLNNGPFHDPEQQALGSSPLLTIRPPPASPAEIVSLHEKPSNYHSASILCLQFDDEIMVTGSSDHTCIIWDIKNDYKPIRRLEGHTAGVLDVCFDHRYIVSCSKDNTICVWDRRSGALVKKLYGHRGPVNAVQLRGDLIVSASGDGVAKLWNITSGLCVKEFSSRDRGLACVEFSNDARTVLTGGNDRAIYQFDANTGQLVKEIEGHTGLVRSLHLDDVNQRIVSGSYDTSVKVFDAQAGELSIDFPGWTTSWMLSVKSDYRRIVATSQDSRAVIMDFGYGLDGIDLLEG
The following text describes a protein:
Function:
ADIPOR-like receptor involved in zinc metabolism either by altering membrane sterol content or by directly altering cellular zinc levels.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MMDSSSKSLTQYIPSPMGSLSRLKQKGVDNFQKVKKSGKSIYNYNYSKFVPHPFSTIDESVKHSESGRYDDLEIIRPTKEKEVTSSVYKRNSGKSLNTESQFSLGDSDAATLVNSVATFKLNNASTSTSLVSSSSTVCSQAKSSLRSPTSRLNDTKIKEENNYISSVKDYCGPMRKSMVKTEILIEEPLNPTTDIKSFINSYNHGKAYSLGETQHLHYYQLPFPWRENRYIIHGYRFYNTHSKSLLSIFNWYGWHNETSNIWSHLLGAIYIIYLAIYDFPQSEVWRNSQVPPQARWIVFMFLAAALKCMLSSVFWHTFNGTSFLKLRSKFACVDYSGITILITASILTTEFVTMYSCYWAMYTYMSISLALGVFGVFMNWSPRFDRPEARPLRIRFFILLATMGVLSFLHLIFLTDLHYAATLFSPVTYKSVVWYLVGVVFYGSFIPERFRSDVQVDKTIPTNYELSTDLEIITKQREIHFREVPTAHSKCSSCPSHAKSFKSLWWVDYFGCSHTFWHFFVVLGVIGHYRAILDMFAKRWILS