lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Subcellular Localization:
Cytoplasm.
Sequence:
MFTNPFGRKKDMSDDQKKNNQPDTEADNAENIKFAADDTELRAGDETDADFEMPEGFPEMDENMFGQVQEMMAKLERVDELEKENADLKNRLGRLASDFEGYRNRTTIESAEAHDKGVSKAAEALMPVYDDIDRALSLSVDDAAKLVPGMQAVQNKVLTIFGTLGLEATGREGEQFDPQWHEAIQVVAGDEDEKIVQTYQLGFKMGDRLVRPARVVVSRKG
The following text describes a protein:
Function:
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
Sequence:
MNTPTATTAQPPRIIRQLPAHLVNQIAAGEVIERPASVVKELLENSIDAGSTRIELSLEGGGVELIRISDDGCGMTAEQLPLAVTSHATSKLPDDESLFHVGTLGFRGEALASIASVSQMTIRSRAEGQDGGCQIDIRGGVIETPGPCGCPVGTVIEVRNLFFNTPVRRKFLKTPQTERGHIVEAFTRLALANPKVHFVLRNGDKEMFDLLPTTRWADRIESFFGTEISEALIPIENQDETVQISGYACDPSVSRGNNRMQYLFLNGRHIRDRALQHALGEAYRGMLMVGRHPVCFLRMRMPADMIDVNVHPAKLEVRFTDSGRVYSRLLQTLRQRFLSTDMTHRVGSNPVPAPMSEEEQRQTVPESVMGMRPNEVDQQRQSVIEWARTGGPPSGPTATSNSQMLGGASGTPDFRPFGESNSIGHGSQASTGMTAPSAPLASPNTWSPGSASGIDSQRPSTAAEGIEMTPWDGDNAGESNANDSGTTISPHDASQSAGVPTPSVSHLGFQVHQRYLVTQDEKGMVVIDQHALHERVLYERVCQKVLHEDASLEAQQLLVPEPVSLTPAERAAALEVKDTLSRIGLEIEDFGGETILIQSYPAMLPNKPPADMLRTVLESVMGAGRDPNPKDLLNHLLSTVACKAAVKAGDPLSPEEITSLLEQKDLYQETHHCPHGRPTALFFSRDELDRMFGRLGPRGRASVSP
The following text describes a protein:
Function:
Secreted tripeptidyl-peptidase which degrades proteins at acidic pHs and is involved in virulence.
Subcellular Localization:
Secreted, extracellular space.
Sequence:
MRLSHVLLGTAAAAGVLASPTPNDYVVHERRAVLPRSWTEEKRLDKASILPMRIGLTQSNLDRGHDLLMEISDPRSSRYGQHLSVEEVHSLFAPSQETVDRVRAWLESEGIAGDRISQSSNEQFLQFDASAAEVERLLGTEYYLYTHQGSGKSHIACREYHVPHSLQRHIDYITPGIKLLEVEGVKKARSIEKRSFRSPLPPILERLTLPLSELLGNTLLCDVAITPLCISALYNITRGSKATKGNELGIFEDLGDVYSQEDLNLFFSTFAQQIPQGTHPILKAVDGAQAPTSVTNAGPESDLDFQISYPIIWPQNSILFQTDDPNYTANYNFSGFLNTFLDAIDGSYCSEISPLDPPYPNPADGGYKGQLQCGVYQPPKVLSISYGGAEADLPIAYQRRQCAEWMKLGLQGVSVVVASGDSGVEGRNGDPTPTECLGTEGKVFAPDFPATCPYLTTVGGTYLPLGADPRKDEEVAVTSFPSGGGFSNIYERADYQQQAVEDYFSRADPGYPFYESVDNSSFAENGGIYNRIGRAYPDVAAIADNVVIFNKGMPTLIGGTSAAAPVFAAILTRINEERLAVGKSTVGFVNPVLYAHPEVFNDITQGSNPGCGMQGFSAATGWDPVTGLGTPNYPALLDLFMSLP
The following text describes a protein:
Function:
Plays an important role in caveolar biogenesis and morphology. Regulates caveolae morphology by inducing membrane curvature within caveolae. Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in the lung and fat endothelia but not in the heart endothelia. Negatively regulates the size or stability of CAVIN complexes in the lung endothelial cells (By similarity). May play a role in targeting PRKCA to caveolae.
Miscellaneous:
MISCELLANEOUS: Binds phosphatidylserine (PS) in a calcium-independent manner. PS-binding is inhibited by phosphotidic acid and phosphatidylinositol. Does not bind phosphatidylcholine (By similarity).
Subcellular Localization:
Cytoplasm, cytosol. Membrane, caveola. Note=Localizes in the caveolae in a caveolin-dependent manner.
Domain:
The leucine-zipper domain is essential for its localization in the caveolae.
Sequence:
MGEDAAQAEKFQHPNTDMLQEKPSNPSPMPSSTPSPSLNLGSTEEAIRDNSQVNAVTVHTLLDKLVNMLDAVRENQHNMEQRQINLEGSVKGIQNDLTKLSKYQASTSNTVSKLLEKSRKVSAHTRAVRERLEKQCVQVKRLENNHAQLLRRNHFKVLIFQEESEIPASVFVKEPVPSTAEGKELADENKSLEETLHNVDLSSDDELPGDEEALEDSAEEKMEESRAEKIKRSSLKKVDSLKKAFSRQNIEKKMNKLGTKIVSVERREKIKKSLTPNHQKASSGKSSPFKVSPLSFGRKKIREGESSAENETKLEEQVQDDHEEGSFTEGLSEASLPSGLLEGSAEDAEKSALRGNNSGVGSNADLTIEEDEEEESVALQQAQQVRYESGYMLNSKEMEESSEKHVQAAVLHVDQTA
The following text describes a protein:
Function:
[Spike protein S1]: Attaches the virion to the host cell membrane by interacting with sialic acids, initiating the infection; [Spike protein S2]: Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes; [Spike protein S2']: Acts as a viral fusion peptide after S2 cleavage occurring upon virus endocytosis.
Subcellular Localization:
[Spike protein S2]: Virion membrane; Single-pass type I membrane protein. Host endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Some S oligomers may be transported to the plasma membrane, where they may mediate cell-cell fusion; [Spike protein S1]: Virion membrane; Peripheral membrane protein. Host endoplasmic reticulum-Golgi intermediate compartment membrane; Peripheral membrane protein. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Some S oligomers may be transported to the plasma membrane, where they may mediate cell-cell fusion. S1 is not anchored to the viral envelope, but associates with the extravirion surface through its binding to S2.
Domain:
The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins.
Sequence:
MLVTPLLLVTLLCALCSAVLYDSSSYVYYYQSAFRPPSGWHLQGGAYAVVNISSEFNNAGSSSGCTVGIIHGGRVVNASSIAMTAPSSGMAWSSSQFCTAHCNFSDTTVFVTHCYKHGGCPLTGMLQQNLIRVSAMKNGQLFYNLTVSVAKYPTFRSFQCVNNLTSVYLNGDLVYTSNETIDVTSAGVYFKAGGPITYKVMREVKALAYFVNGTAQDVILCDGSPRGLLACQYNTGNFSDGFYPFTNSSLVKQKFIVYRENSVNTTCTLHNFIFHNETGANPNPSGVQNIQTYQTKTAQSGYYNFNFSFLSSFVYKESNFMYGSYHPSCKFRLETINNGLWFNSLSVSIAYGPLQGGCKQSVFKGRATCCYAYSYGGPSLCKGVYSGELDHNFECGLLVYVTKSGGSRIQTATEPPVITQNNYNNITLNTCVDYNIYGRTGQGFITNVTDSAVSYNYLADAGLAILDTSGSIDIFVVQGEYGLNYYKVNPCEDVNQQFVVSGGKLVGILTSRNETGSQLLENQFYIKITNGTRRFRRSITENVANCPYVSYGKFCIKPDGSIATIVPKQLEQFVAPLFNVTENVLIPNSFNLTVTDEYIQTRMDKVQINCLQYVCGSSLDCRKLFQQYGPVCDNILSVVNSVGQKEDMELLNFYSSTKPAGFNTPVLSNVSTGEFNISLLLTNPSSRRKRSLIEDLLFTSVESVGLPTNDAYKNCTAGPLGFFKDLACAREYNGLLVLPPIITAEMQALYTSSLVASMAFGGITAAGAIPFATQLQARINHLGITQSLLLKNQEKIAASFNKAIGHMQEGFRSTSLALQQIQDVVSKQSAILTETMASLNKNFGAISSVIQEIYQQFDAIQANAQVDRLITGRLSSLSVLASAKQAEYIRVSQQRELATQKINECVKSQSIRYSFCGNGRHVLTIPQNAPNGIVFIHFSYTPDSFVNVTAIVGFCVKPANASQYAIVPANGRGIFIQVNGSYYITARDMYMPRAITAGDVVTLTSCQANYVSVNKTVITTFVDNDDFDFNDELSKWWNDTKHELPDFDKFNYTVPILDIDSEIDRIQGVIQGLNDSLIDLEKLSILKTYIKWPWYVWLAIAFATIIFILILGWVFFMTGCCGCCCGCFGIMPLMSKCGKKSSYYTTFDNDVVTEQYRPKKSV
The following text describes a protein:
Function:
Subunit OSCP, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). Part of the complex F(0) domain (By similarity). Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity).
Subcellular Localization:
Mitochondrion. Mitochondrion inner membrane.
Sequence:
MLARFSRTAIKSGRYFSTSAKNTAPVSEAEEIEILKAVEAPQFKDAVKKTRQQYQDMISKLTNDESGKSITQSTGLRPTINISTPSGKIAHALFDAASSMRSVGIVAKELTQVKTIIDKTPGLKTALEGDIDNSEKTVMLELLQGSVTLSPVSGFFLYYMTYENNFKLINPALTDFKRLVGSLDTEMSIKLTVAHQYSEAEKKDLETNVKSFFPPETQFKFSYNVDPEIQKGYIIESPFINHDASYSTAVKKVKAQEQSVLAEFLNDIKNGIKNQTAVWETKEFRDKYLTLDESKN
The following text describes a protein:
Function:
Involved in the maintenance and repair of the intestinal mucosa. Promotes the mobility of epithelial cells in healing processes (motogen) (By similarity).
Subcellular Localization:
Secreted, extracellular space, extracellular matrix. Cytoplasm.
Sequence:
MEARVLWLLALVLALGSSSLADQYVGLSENLCAVPAKNRVDCGYPEISPEQCVNRGCCFDSSIPEVPWCFKPLQDTECTF
The following text describes a protein:
Function:
Together with AlgI and AlgF, forms an inner membrane complex which probably interacts with the alginate polymerization-transport complex and adds acetyl groups at the O-2 and O-3 positions of mannuronate residues. Acetylation of alginate is important for the architecture of biofilms and increases resistance to opsonic killing in the host.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein; Periplasmic side. Periplasm.
Sequence:
MTQSISRPLQYAYIAAFGGLLLGLAGWSLKSVPGFSAAADTPLLNGKLAHAFEAHYDKEFPIKRLGTNLWAALDYTLFHEGRPGVVIGKDGWLFTDEEFKPAPSGQQLEDNWALVRGVQRELNRRGVKLVLAVIPAKARLYPEHIGREQPAALHDSLYQDFLARARAAGIDSPDLLGSLRQAKDNGAVFLRTDTHWSPLGAETVAQRLGAEIRETHLLDVPAQNFVTRVGEERTHKGDLLSFLPLDPLFDELLPRPEQLQQRTTEAAPALPGGQQSGAGDDLFGDSQQPRLALVGTSYSANPRWNFEGALKQALSADLINYAKEGKGPLEPMLELLQDEGFRKDPPQLLVWEFPERYLPMASDLSQFDADWVAQLKASGGRDERLAASRND
The following text describes a protein:
Function:
Negative regulator of transcription elongation.
Sequence:
MSTDPPRTSSRPRQKSQRALEHEDTKRYLEQQLDSPAKIPRPRPKSKPKHRSYCVCKQDTSGPMIECDVCSDWFHFKCINLAEDDAEKIHKYVCPSCTLSNPDQYTTYSYDIASFPSPSPPPGLELGPAGAGVQEIIKPRPSDGKGKSKHEDQKKKSILAKRKSKTETSRGGEDADGTGDGEDDDDDGDKVMATSSAHDSDSASVSASSSDSNPRHPDSDSDAASNASGPSRKRPRPRPRVPSKSTNVQRGDEKPSLPSSSSTQPKPKPKPKPKPRSISQSHPQPETKHVQAKTLPPIRQYVLSKLTLLFHTLFSSPPSSHPFTEEESARYAADVERAMFQAFKDIHPSTASTTTTTFSATATTGVGAAAKESAGTRYKTQFNLLTSSLTKNKHLLRPSLLQSILSRSLPPTALALLSASDLASAAQLEEMERAKQAVLESTVKTREEREREREMMSGGGGGVRAGRDGLEQLEDTREKEMWEVRKEEERERSEQREREHEQRERRESEVERDSVHPDDGSLSKDVKSIKDTIKHEPSRSPTIPSTAIPHHRRTSTSTSTLTPTSTPFKTEPAKPAFELTSAWGASNLQGGGNDQGGGGGGGRLERKPKKLDLSDQAIAGSVGDVGGVGGGAGEGDLDLDLDLGYGSGEMDLDELDYTGEVDAAAAADGAGGHGDGVDQEAEIENREEGEGLGEEGKGENQQKKKWEELMERPIEWSGWITNPAVPSSLRPPIALRLLTPHPSSSSNFTQSHTQIHPPWTALLPNSTIEITGRVPTKASVQYLSDMRLNPGKELICVLFTFGKPYAHGEGDGQAEGEKREWERLVGYHVERDRHAIYLPYGPKGPPPPPPASLSPSTTEGVQNTFKELYLIPLRPGDALPEFCELVDGLDVLNGRSAGNEDGTGGDLARGKENGKVGSVWLGVFVGSKRRNGSVSTSASANGSASAQRQIQTQTQVQKEGRPQARSESQSQTPPHDPRGPRIPRPAFIPPAHGASPSISSSRPSVHPLSPASAQSQSSGPGQGVIQNEKLQQLMASLNPSSLGLPGLPGLSGLPGLPNLPGVHGGAQVGTPPFPPGGTTPLGTGTGVSNSPPTLPRPPQHLQTNHLNQRLPPPPPTLPPPPGGYRPPPYGYIPTPPQGPAMTHGYGSPPYRRGSGGAYAYPLGSSGPPGPRGPPGPGPLPRPPLPPGAQAAQGGRPPQEERHHPNQNRQQEQGHRQGQRQGQRWRNERGNGNNNGGWKRRGH
The following text describes a protein:
Function:
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Domain:
The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers.
Sequence:
MSETFSPNLTFTEGFVLGQASFLIILLLFIRYVVFSPSEQIDHEGWRKRRAERADLLSNHTPPPLSNLLSKTSYDMSIHPAESSDWVNVLLAQILQGYRNDLLSEGGEEGARQRIEGWLNPKGENLSWLDPIDVTSLSLGTSYPLLSNARIRPADGQGRLRAEIDVDYLDSLSMTLSTAVLVNFPKPRFAVLPVTLGVELVSIGGTMSVQLHEPIEDRQHIHVNLLPDFHLNLKVTSLLGSRAKLQDIPKLEQLIVSRLRNLVQDRFVHPNHISLALPRILSPSVSSTPILEGLGEGAVDAMKDAVSDGMKRMVEDFMGENPVEGALNGQGEEQWLDDDFPPTPLVQPPGTFPTLSVSSRQSHRQSLPPSRPQSTTQGQPQLFYRRPLIHPTQSYPHYNTYTLDPQIPHSVSYRHPPRGSHVHNPPETPVPQRPSHGQGRMSTTSSLTPSQSQSQFRFRGQFASGVTPGQVGTSR
The following text describes a protein:
Function:
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Sequence:
MSDESRPSPAETPATTFAETSAETSAAGRSPARTAAVIPAAGRGVRLGPGAPKALRALGGTPMLIHAVRAMAASRAVSLVVVVAPPDGAGEVKSLLDAHALPERTDFVVVPGGETRQESVRLGLDALPPEYGIVLVHDAARPLVPVDTVDAVIDAVREGAPAVVPAVPLADTVKQVEPAAAPGEPEPVVATPERARLRAVQTPQGFDRATLVRAHGTVTDDVTDDASMVEQLGLAVVVVPGHEEAFKVTRPLDLVLAEAVLARRRLNDGF
The following text describes a protein:
Function:
Phosphodiesterase responsible for the U6 snRNA 3' end processing. Acts as an exoribonuclease (RNase) responsible for trimming the poly(U) tract of the last nucleotides in the pre-U6 snRNA molecule, leading to the formation of mature U6 snRNA.
Subcellular Localization:
Nucleus.
Sequence:
MPKDTHRHQSPSTGSTWPLGNKKKSNSLNTDRLKPNAIQTTVSKASIVDKPNAPVPVRTVAHIEGNWATYIYIPIELQEDLQAELKDWIKQATTQFPSWHSHIQLDSNDSLGLHVSLCQTAYLKVFQIDRFMALLEQQIGLQSRFTVSFNGVSSYVNDEQTRSFVGMDIGHGHEELLELVQCVDLALTAFHQPPFYKNPRFHASIVWSPTTRASSFDNPIESIPDSLRDIPKKLHNTLFLVRSVVCKSGNKLKQFDL
The following text describes a protein:
Function:
A DNA polymerase, required for DNA repair after DNA damage induced by ionizing radiation (IR); this is not the major DNA polymerase. Following severe irradiation (7 kGy of gamma irradiation) genomic DNA is fragmented. DNA is progressively degraded for the first 1.5 hours after IR, in a step promoted by RecA and counterbalanced by DNA Pol I and Pol III, followed by massive DNA synthesis and genome reassembly in the next hour. Optimal priming of DNA synthesis requires both RecA and RadA, Pol III initiates DNA synthesis while both Pol I and Pol III are required for its continuation. May also have 5'-3' exonuclease activity (By similarity).
Sequence:
MVFCGDGGLSCESIDFALCCLRGRSGNYVQSRILPMADASPDPSKPDTLVLIDGHALAFRSYFALPPLNNSKGEMTHAIVGFMKLLLRLARQKSNQVIVVFDPPVKTFRHEQYEGYKSGRAQTPEDLPGQINRIRALVDALGFPRLEEPGYEADDVIASLTRMAEGKGYEVRIVTSDRDAYQLLDEHVKVIANDFSLIGPAQVEEKYGVTVRQWVDYRALTGDASDNIPGAKGIGPKTAAKLLQEYGTLEKVYEAAHAGTLKPDGTRKKLLDSEENVKFSHDLSCMVTDLPLDIEFGVRRLPDNPLVTEDLLTELELHSLRPMILGLNGPEQDGHAPDDLLEREHAQTPEEDEAAALPAFSAPELAEWQTPAEGAVWGYVLSREDDLTAALLAAATFEDGVARPAPVSEPDEWAQAEAPENLFGELLPSDKPLTKKEQKALEKAQKDAEKARAKLREQFPATVDEAEFVGQRTVTAAAAKALAAHLSVRGTVVEPGDDPLLYAYLLDPANTNMPVVAKRYLDREWPADAPTRAAITGHLLRELPPLLDDARRKMYDEMEKPLSGVLGRMEVRGVQVDSDFLQTLSIQAGVRLADLESQIHEYAGEEFHIRSPKQLETVLYDKLELASSKKTKLTGQRSTAVSALEPLRDAHPIIPLVLEFRELDKLRGTYLDPIPNLVNPHTGRLHTTFAQTAVATGRLSSLNPNLQNIPIRSELGREIRKGFIAEDGFTLIAADYSQIELRLLAHIADDPLMQQAFVEGADIHRRTAAQVLGLDEATVDANQRRAAKTVNFGVLYGMSAHRLSNDLGIPYAEAATFIEIYFATYPGIRRYINHTLDFGRTHGYVETLYGRRRYVPGLSSRNRVQREAEERLAYNMPIQGTAADIMKLAMVQLDPQLDAIGARMLLQVHDELLIEAPLDKAEQVAALTKKVMENVVQLKVPLAVEVGTGPNWFDTK
The following text describes a protein:
Function:
Multicopper oxidase involved in copper homeostasis and copper tolerance under aerobic conditions. Is responsible for the oxidation of Cu(+) to the less harmful Cu(2+) in the periplasm, thereby preventing Cu(+) from entering the cytoplasm.
Subcellular Localization:
Periplasm.
Sequence:
MHRRDFLKLTAALGAATSLPLWSRAALAADFSPLPIPPLLQPDANGKINLNIQTGSVVWLPSTATQTWGYNGNLLGPAIRLQRGKAVTIDITNALPEATTVHWHGLEIPGEVDGGPQALIQPGAKRQVTFAVEQPAATCWFHPHTHSKTGHQVAMGLGGLVLIDDSDSETLPLPKQWGVDDIPVILQDKLLDKHGQVDYQLDVMTAAVGWFGDRMLTNGVPYPQQITPRGWVRLRLLNGCNARSLNLALSDGRPMYVIASDGGLLAEPVVVRELPILMGERFEVLVDTRDGQSLDLVTLPVTQMGMTLAPFDQPLPVLRIQPSLAIGSQVLPESLVVIPELADVTGVQERWFQLMMDPKLDMLGMQALVARYGMKAMAGMNMNHGDMGAMDHGNRPDMSQGKMKGMDHGTMNGAPAFNFSHANRINGKAFSMTEPAFDAKQGKYEKWTISGEGDMMLHPFHVHGTQFRILTENGKPPAEHRRGWKDIVRVEGARSEILVRFNYLAPASTPYMAHCHLLEHEDTGMMLGFTVSA
The following text describes a protein:
Function:
Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA.
Subcellular Localization:
Nucleus.
Sequence:
MVSARKKKEKKKDFQKTKLKVGKTAPKSNTHTDLSFKAKTISLPNQSIVKGITGAGGVPVGSTVSPLNNEDFKHHILLLKHHSAGTRKEALIYLTNAWNKYLASSDDLGVNIKPIVDAAAPLVLDLSEKVRAELLLLLRALCFEPGQVDPVPANQLSDISKPKFTLKPEFYTANSPLSLHIPNLALYIHSAMTHITPDIRADSTKFLLLMVTPATGESHTFSHSFDLSICSVLQRQYWAKTLNCFFALFGWSHEKTDQQLTMSSSSVTAGLAFGKQAASVKKSFLECLQLFLRSGLSEFGVKYKEIKLLDASGNDVVIEQRQPENPLFHPMSRLFTQPPNSDPFLHLNLFKSTNTSATTTSITEDVEARNQVLKTYLGSLHHGLELLAKEGGEIGRLAKKTIEVSVC
The following text describes a protein:
Function:
Probable transcriptional regulator that is required in neural development for the normal formation of sublateral cholinergic motor neuron processes. Plays a role in regulating the expression of acetylcholine transporter protein unc-17 in the sublateral processes. In particular, it is required in sublateral motor neurons for a left-right turning behavior that occurs during the lethargus phase of the normal sleep process called 'flipping'. During 'flipping' animals rotate 180 degrees about their longitudinal axis.
Subcellular Localization:
Nucleus.
Sequence:
MSAAANYGEGPVVTDRGDLHGLLPELNGVELAMSLSPKHHHQGGPQVLSHLQQLHHSTPFSVTDILSPIEESYRKLELAANPPSPYRSTSSGSSINNSPGAGGTPGGGGCSMNSSYPVMGQFGGGQYCPVSENLGLTPHYSSGWYQSSAADPRFAISRLMGSSAASANMGHGLNTGMPGLGACAMPDSKPMQFPLAQRRKRRVLFTQAQVYELERRFKQQKYLSAPEREHLASLIHLTPTQVKIWFQNHRYKCKRQAKEKAMAEQNQHNQSSSSPRRVAVPVLVKDGKPCSAGSGSTQTSSSATSSDTSRTQQSPVCQPQQQAQCMGNGSLAMAYRQQNNYQQQCGTYLPLQTRAW
The following text describes a protein:
Function:
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Sequence:
MKPLTPRQQQVFDLIKSKIDDTGMPPTRAEIARELGFRSANAAEEHLKALARKQAIEIIPGASRGIRILLEDAANDEQGLPLIGQVAAGEPILAQEHVEAHYQVDPAMFKPQADFLLRVNGESMKDIGIMDGDLLAVHKTQDVRDGQVVVARVDDDVTVKRLERKGSTVLLHAENEEFAPIQVDLTSQHLTIEGLAVGIIRNTDWM
The following text describes a protein:
Function:
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MNSHNTRNQLPDTGNKINGSTNTYSSGVPGDFEEPLMAHLYELRNRLAVVLVWLFLSMLVAYPFSEKGMMLVWKEFISPELDMAVYSPLEWIFARLKLCLVFALAVSIPQFFYQLYRFAGKGLYPHEKRFFLKVVPASFLLFILGAALGYFIVLPVMFRYIFFYSGDVASAQLSVQNTLSAVTTILAGFGVVFQAPLLVVFAVKLGLVKYQTLKKQRLLVYSAIVTLSLFLSPDPTFIAQILVALLLAVLFEFSLLLVRLF
The following text describes a protein:
Function:
Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Subcellular Localization:
Nucleus.
Sequence:
MQETSKEIPAGSLPRYLDVILRHEIVEQARAGDTVIFTGTVIVLRPDISALASPEERAECRRDSSQQKSSTAGHEGVKGFKALAVRDLSYRLAFIANSVQIADGSRNTDMRNRQNDSNEDDQQQFTREELDEIQNTPDYFNKLVGSMAPTVFCHQDIKRAILLMLVGGVHKTTHEGINLRGDINVCIVGDPSCAKSQFLKYTAGIVPRSVYTSGKSSSAVGYNFNLPPAILSRFDLVYVMTDGPDEVTDYHIAHHIVRVHQKHEAALFPEFTTVQLKRYIAYAKTLKPKVKPSHVLLAVTLLKTSVISVESGDVDLSEYQDANGDNIDNTDDIENTGNRDEEQHNGAAEPASATADKGEAPPNLVISEEEYDKITHALVIRLRQHEETVSKESKQHHSLFNSPY
The following text describes a protein:
Function:
Component of the checkpoint clamp complex involved in the surveillance mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes.
Subcellular Localization:
Nucleus.
Sequence:
MLFVESDSESVNNTDICQVEDSFTASTTQIAHLSDIFQSLVSINNQAIIRIKETGIAIYSSYNHTFNVNVNIDPSLFSIYSITGEEFTLGVDLSLIGECFTSVASTLKFEKSVTCYLNYQGEGSPLVIEFEDTYILEKLEFYTYIIESGMEDDNLGIDYERVEMEAMVRSDVLTNILSDLWQIDTENLFIYAEADTLTFISNGPIGTSKLIFPNDKDVLEKLEISGDKRYVVSQFSYETFYRIFRAVRLSSKCKLIKDAHGCFSIQLLCKKLPLSGYSGTLVTINMMELNHDEFMIGWIEEQEKPVLFTSFKKVEVQSSVVDKRNVSGAVEVPLFL
The following text describes a protein:
Function:
Catalyzes three sequential steps of tetrahydrofolate biosynthesis.
Sequence:
MPPDTITISSLTLHLPHGLGPSAFHLTPSPPCPALLSLTIHLVPNSVSATAAGDSMAGLGVNYSSVSKAVYALANDAEKVWSGPWELMRAVSAIPLGFDDVQSVDIRLGLPKALLHALEAVYKASYAKNGEETGRSCTIRDLKVVCIVGLHEHERKEKQRLELDVKVRGGDWNVWGHKGFADEIYDFVSNSAYGTIESLNHELGQHLLKSRYLGDPTQSHLEITIRKPSAIPFATPSITIHRSQADYAPSLPSGTACNAPREALERVFVAVGSNIGDRVANITRAVSLLEEAGCKLLGTSRLYESEPMYVEDQDRFINGVIELATPLEPLEVLRLLKHIEKAVGRTKTFTNGPRVIDLDLVFYGHRVVKIGNETDEEDEHGIKWLECPHKRLREREFVLRPLADIDPEFTHPALRRSVGQLLASLPTTFPPSLSPIIPLHSHSSPLRLSIPASPYIMAIFNTTPDSFSDGDPARTNVEYALAACEKLLKGPEPPAILDIGGMSTRPGSEPCSEEDELSRVIPLVKAIRSSSNPIVASIPISVDTYRPSVAKAAVEAGASIINDVRGGQEPGMLRVMAEADVPVVLMHSRGDSKTMIAADVQDYDSHGGVIKGVIQEMRVLVEQALKSGVKRWNIILDPGLGFAKSSSQSLTLLKHLPDLVLPGTGLERLPMLVGASRKGFVGQTIKRAVPKERSFGDAAVSGWCASSGVVDILRVHEPREMAEVVKMACAIRDAE
The following text describes a protein:
Function:
Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
Sequence:
MTKQGMVVPVPEAAVAVPPNSAPLFQYPPPRAAPGVAVRKKCLQMGAGAGRIGGWVESMRASSPTHAKAAAALAAGVEEERYAAWMVKHPSALAMFDQLVAASKGKQIVVFLDYDGTLSPIVDDPDAAYMSDTMRRAVRSVAKHFPTAIVSGRCRDKVFEFVKLAELYYAGSHGMDIKGPAKGSRHTKVPIHSNLCPCILSGHPKILISLCLSYVCGSQAKGGGVLFQPASQFLPMIEQVHDSLVEKTKCIPGAKVENNKFCVSVHFRCVDEKSWITLADMVKSVLKDYPKLKLTQGRMVFEVRPTIKWDKGKALEFLLESLGYADCTDVLPVYIGDDRTDEDAFKVLRKRGQGVGILVSKHPKDTCASYSLQEPAEVMEFLLRLVEWERLSKARPKW
The following text describes a protein:
Function:
Rho GTPase-activating protein involved in the signal transduction pathway.
Subcellular Localization:
Cytoplasm.
Sequence:
MSSNPSSSYTPWVSKSISSNSLAGLSSSPSTSNRSTTRGADKEAKLLGYLQKQSKSQLPNSNVKLYKKKWFWFEPDTGTLYYSTTSSGALSQPLTPTSLSERIKSIPIVKTTHIEQSISFRLEFIITNEKKTYSLRGIDETSILNWVNTLNQWKKANFEKSSLSVTGSIENPNFINQLGEIELILSAISLSNNNLNNNNNSNNGNDSPIRPLLEKFQPDQEQIKLISEKITQKINYLKSCQNELFLFQQQQQQQNSNSNINNISNLNNSNNIFSNSLLKRLNSSQDLTNSSNSITMDDSLVDDDEDDDVLLSNGIVNNEISDIFSLLPVHLSLYVFSYLEPNDLLICAQVSTQWQKLANDNLLWIRFVFHLITPASVFDKSHNWKSVYLANTPSSKKKEGANGKEKYMNRTISMYGVTPLTSTKSLKEGWLYKRGDDILRIWKKRASVSTRKNCFKIIQSKYMTGAIQKKRMPYYLASDREDDCIEWFSILSNAIKLNTQHQGQYGVVNIGQSNTLPNGISPIATPSKYNQYHTVSNINSLFSNNNNNNNSHSSGKPRKSHKKSFSSSSTSSNNNTLFDSNPQHLSSTPVNLTPIYPMFGLPITKIIENQSAIASQQYLKVPYLLHVCLSHILEKGIREEGIFRVSGSLREIQELQEDFEQGRDIDLNQHDIHAISGLVKTFFRKLPHSLVPSDLDEYSTSVQLATSQTEDEKIQEFKFIFESITPNSFHIFKILLLLLKQIVLYESQNKMTIENLLIVIMPTLKCSPVLITNGIKYYEQIFNQ