lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Negatively regulates the expression of phosphate-starvation-responsive genes under phosphate-rich conditions. The PHO80-PHO85 cyclin-CDK holoenzyme phosphorylates and inactivates the transcription factor PHO4, by preventing its association with the transcription factor PHO2 and the nuclear import receptor PSE1, and by promoting association with the nuclear export receptor MSN5, excluding PHO4 from the nucleus. PHO80-PHO85 phosphorylates and inactivates protein kinase RIM15 by retaining it in the cytoplasm, antagonizing RIM15-induced entry into stationary phase. PHO80-PHO85 also phosphorylates and inactivates the calcineurin-responsive transcription factor CRZ1, linking PHO85 to calcium signaling.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Localizes predominantly to the cytoplasm under phosphate-rich conditions and concentrates in the nucleus upon phosphate starvation.
Sequence:
MESTSGERSENIHEDQGIPKVILPADFNKCSRTDLVVLISRMLVSLIAINENSATKKSDDQITLTRYHSKIPPNISIFNYFIRLTKFSSLEHCVLMTSLYYIDLLQTVYPDFTLNSLTAHRFLLTATTVATKGLCDSFSTNAHYAKVGGVRCHELNILENDFLKRVNYRIIPRDHNITLCSIEQKQKKFVIDKNALGSLDLDSYSYVNRPKSGYNVLDKYYRRIVQLVGSFNASPDKSRKVDYVLPPNIDIVSESGSQTTQLKGSSSPNSHSSQKRYSEAKDAHIYNKRSKPD
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 (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MEEHIQDRREIAFLHSGEFLHGDSDSKDHQPNESPVERHHESSIKEVDFFAAKSQPFDLGHVRTTTIVGSSGFNDGLGLVNSCHGTSSNDGDDKTKTQISRLKLELERLHEENHKLKHLLDEVSESYNDLQRRVLLARQTQVEGLHHKQHEDVPQAGSSQALENRRPKDMNHETPATTLKRRSPDDVDGRDMHRGSPKTPRIDQNKSTNHEEQQNPHDQLPYRKARVSVRARSDATTVNDGCQWRKYGQKMAKGNPCPRAYYRCTMAVGCPVRKQVQRCAEDTTILTTTYEGNHNHPLPPSATAMAATTSAAAAMLLSGSSSSNLHQTLSSPSATSSSSFYHNFPYTSTIATLSASAPFPTITLDLTNPPRPLQPPPQFLSQYGPAAFLPNANQIRSMNNNNQQLLIPNLFGPQAPPREMVDSVRAAIAMDPNFTAALAAAISNIIGGGNNDNNNNTDINDNKVDAKSGGSSNGDSPQLPQSCTTFSTN
The following text describes a protein:
Function:
Part of the ABC transporter complex OppABCDF involved in the uptake of oligopeptides (By similarity). Probably responsible for the translocation of the substrate across the membrane (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MFKYILKRLGLAVVAMFIVMSIVFFLVNATGNVPLSATSARDIAAVQAQLQEFGFNDPIIVRYFRYWAKLFSFQADALGIYYANPNQTIGEIVFARVPNTLYVVLISFLIGSLLGIFLGMVSGLNRGKFLDAAINVLVVLFVSIPSFVVGLGLLKLAGFLNLPPRFINFDDAFFSFDRFLLASIIPILSLVFYSSAAFTYRIRNEVVEVMNQDYIKTAKSKGLGMFAVARYHIFRNSIIPSIPLFVFGISGAFSGGFIIESLFGVQGVSRILIDSVQVNETNMVMFNILFIQGIPLLASVFIEFIYVLVDPRIRIANSSNVSLLTKLKFLSSRHQWLMKWNKINSDNAQNIVFNSPLHHQLLELNAIDYKTKTVQLTTEQKTALNISATANFILLGNKCLKLKTIHG
The following text describes a protein:
Function:
Phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (eIF2alpha), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis. May phosphorylate eIF2alpha during hypoxia. Proposed to have a role in alleviating endoplasmic reticulum stress.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Domain:
The lumenal domain senses perturbations in protein folding in the ER, probably through reversible interaction with HSPA5/BIP.
Sequence:
MSVYYIVLAGFLLFMALVPFNAGQQYIDDDIEVVSSCQNGYVQNAGCDQNSQVNIIITATLDGVVTALDGETGEMIWRYEDAPLLRGTLSTSDPIDIGGTSLQLMPTLDGRLFSYTHNTNLIEPLPITTDSLLESTIRLGQDAVAGGKSVTTKGFDLFTGEQKYECSMESCGPGDTETPKNPIILIRRTTNSIRAMDTLRGIERWNLSTAEIGVTLAGGITSPTLVSDVKILLQPPDGVIVAVDKYNREEWKTNVDGHIVSVWQVYGNQIGEISIFDPSNIFTTQYEVMQREQHNLQTQSSLLYMGTSNGFPFIIQSPKAKNNLKQRMNALPELSTMTELTNPRFCTANEETRSLAYNVKDETLRLVLHNAFRHSQSKAIEDKSLSGSSARRKLQIIASDTEVSAQRIGTENLRSTSVSKSGDYGYLVLESEPQRVKFKVNSPITLMQTIFSYIFNPTAVVSFLAGLIGVTVAVVYNKIAKSSPRMIEHLSSTESAETESASHRTRTTSFAPTDDEIERFVEEGSDLSTTPIGAIHRKPLMPIEKSNIETHTQPQIKPVQRLVKTDIDTDEDSFSNDEKKRLLRNRTISRSSLEGFTSRFANEFEVKKVIGHGGFGVVFRAQSITDMNEYAVKRIAVADNDKARNRVLREARALAMFDHPGIIRYFYAWEERPPKGFQEKEDENLLGKIKAEKLAKLHEIKKAKKHTSEGKRVRSADTASFAESFAMPPVVGNTTDAENSWSTSAKPQEVGAKRTTSESKLGLHGGSDRTTAELKEESVAFSESDEESDTTEDSSSSDESPSSSSGSSIDDEPKKYNSSSGGIEFVDGSDDVDNEAVKETKKEIAVIEELSIHNRAMIVETENQELEVRERNDTGDCAYLYIVMQLCAEKTLEDWIRRSKTMESRPLFTMKNWIKQLASGLEYLHNKGFIHRDLKPGNVFFSLDSTHGHQILKIGDLGLATKTDGAPKITVRQDSDSSAKHTKNVGTRSYMSPEQLKHQQYTEKVDIFALGLVATELIISFSTASERIHTFADFQKGDIPAILDNVPESRDFLLQLTSLEPSERPTAHEVATHKFLQ
The following text describes a protein:
Function:
Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors. Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners.
Subcellular Localization:
Secreted.
Sequence:
MQPRVFSAAALLTLLLVNFAWAEEPSLVGRVQDYVHHMAQTAKEALTNVQESQAAQKARGWVSYGFDNFHGYLSLFKDKFSDLWDQTPVPSAPPTTAPLQDNSK
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Sequence:
MRIIFGILTLVCCLTCNRNPFTQTKYQPEVYTISSVVVPKPDTAVVPLPEKPGIYAIFLTTQGTMVLELFDKDAPKTVQNFIDLAQGEKEFLSRNGQKVKKPFYDGLTFHRVIENFMIQGGCPNGDGTGGPGYRFEDEINGKSLGLDQVKAGESPYYQYQLQKVVANELQIKNREEAETKRELIEKAFEDAKKLSVLEILFRTGYKYNEILKSHKAVKGSLAMANAGPNTNGSQFFINQVDTPHLDGLHTVFGQLVTGEDVVDKIVKTGNSKTTIKKVLIVDKRNVTTTPQ
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.
Sequence:
MAADPEFQPGAAPFGNFINYYSFNPPENRLRLLPAEFYTIITRHSADRPLLGLDIGCNTGNLTAALWEQFSSHSTGDSPPDGTDSTTGTAAVQTNHARGCKDSTTGTSAAAVQTNHTPDCDNSATVPALQTSSPPDGDTSTPASHTDFHMLGCDIDSVLIQRAVENNPHPAHLTFQTLDYMDPEQRQETLGSYLQRFGRTKFDVTFCFSVTMWIHLQNGDSGLMDFLRSVSGWTRFLLVEPQPWKCYRSAGRRLRKLGRDEFPRLRHLRIRSDVEKEMDRCLTEGCGMTRVGGFGETQWGRKLVLYRIRGDTVGTETGAV
The following text describes a protein:
Function:
B-type cytochrome involved in electron transfer from hydrogenase to oxygen.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MFPFRRIMRRISAVRIFFAAGILQESARDIVGKSELIRLFLRRIAFGQEQSMTEISEIPGTLDAIGAAGTSRQSIYVYEAPVRIWHWLNAALITMLVITGYLIASPLPSMPGEASNWYTMGYIRFIHFASGQALAVAFLYRIYWAIVGNAYARQLFALPFYNRIWRWGFLYELRWYLFLVRYPKKYVGHNPLANTAMFLFILAMVGMIMTGFALYAEGAGIDSLWYRFFGWVFKIFPNSQDVHTIHHLGMWFIVVFVILHIYAALREEIMSRQSMLSAIITGERTFRDSRPD
The following text describes a protein:
Function:
This protein is one of the chains of the nonenzymatic membrane component (F0) of mitochondrial ATPase.
Subcellular Localization:
Mitochondrion membrane; Multi-pass membrane protein.
Sequence:
MGCYGGFQIGAGTATIALAGAAVGIGKIFSSLIHSVARSPELDTKLFGYAILGFALTEAIALFALMMAFLIFFRERKLDRVSLLCWLMPNHLQEGKEVNLITFSIISSSSGQIKTRKIQSIQFRYRNGRRLGWGRSSLIILLQTFWYVLPPNYRSDPADEKENSALLLSRRTYPPRDSWNFCGLLPPFGYAGTKSPLTTNQQTSSGWVLPFVTENKTASERTFVRFFSTKHGSLRITIGRWLPKETPIRSTPRLGGIYLIPITRRGSL
The following text describes a protein:
Function:
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair.
Subcellular Localization:
Nucleus.
Sequence:
MNIAQEVAVLQYLDIQQENPNAPNEELFNRTAESSLLLEPIEQDQLKDLVEEWMHDSNKSDSKLLSNQVSQNDNDARKNLRKRLRNDVLKDLAEEIQGCEKKLESLYEEVAKAKAKAVEDQLALEEADKEAKKAKTEAPVEAANKSLRSRKKTPEIAAPANIEPEVAPTTKTPKKRAALSNEEKQSLKKFQSAMLPMLDNISNHRFGAPFSHPVNRKEAPDYDSLVYKPQDLRTLKNMIKEGNITEVDELYREVLRIFANCKMYNGSDPANAMSIWGDECFRYTEELFDIYRQASTRSQ
The following text describes a protein:
Function:
DNA-dependent RNA polymerase which catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular Localization:
Nucleus.
Sequence:
MLHLYNSFFSSSILHKSHHTKKLVQSFHLYRDSMLCDVEACLFVWVPVKEIKESGEHPGSIVIKHFFNELTFICATEDYGYFLKVMKVKSVGNGKLSKYSTHLMFPVTFFCRTFLPKTGEVLVGIVIKVCMQGVFLKCGPMNSIYLGRRKMPNYNYVPGENPFFLSDDQSRIENEVAVRFVVFAERWSTTNVRKFDLLASIEGDSLGPVSLNGFDGLEL
The following text describes a protein:
Function:
Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. Required for functional chromatin architecture at the yeast 2-micron circle partitioning locus and promotes equal plasmid segregation.
Miscellaneous:
MISCELLANEOUS: Mutation in CSE4 causes chromosome non-disjunction and cell cycle arrest at mitosis.
Subcellular Localization:
Nucleus. Chromosome, centromere.
Sequence:
MSSKQQWVSSAIQSDSSGRSLSNVNRLAGDQQSINDRALSLLQRTRATKNLFPRREERRRYESSKSDLDIETDYEDQAGNLEIETENEEEAEMETEVPAPVRTHSYALDRYVRQKRREKQRKQSLKRVEKKYTPSELALYEIRKYQRSTDLLISKIPFARLVKEVTDEFTTKDQDLRWQSMAIMALQEASEAYLVGLLEHTNLLALHAKRITIMKKDMQLARRIRGQFI
The following text describes a protein:
Function:
Receptor for ghrelin, coupled to G-alpha-11 proteins. Stimulates growth hormone secretion. Also binds other growth hormone releasing peptides (GHRP) (e.g. Met-enkephalin and GHRP-6) as well as non-peptide, low molecular weight secretagogues (e.g. L-692,429, MK-0677, adenosine).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MWNETPSLESESNFSLDYMDESFNSLGQLPPFPGSLLTGVTVTCIALFFIGISGNLMTMLVVSRFRDMRTTTNLYLSSMALSDLLIFLCMPLDLFRLWQYRPWNFGDFLCKLFQFISESCTYSTILNITALSIERYFAICFPLRAKVVITKGKVKLVILVIWAVSFFSAGPIFVLVGVEHENGTNPMDTNECRPTEFAIQSGLLTIMVWISSIFFFLPVFCLTVLYSLIGRKLWRRKREDMGLSASLRDNNHKQTVKMLAMVVFAFILCWLPFHVGRYLFSKSFEPGSLEIAVISQYCNLFSFVLFYLSAAINPILYNIMSKKYRVAVLRLWGLRQFSQRKLSTLKDDSSRAWTELSINT
The following text describes a protein:
Function:
Acts as a negative regulator of abscisic acid (ABA) response.
Subcellular Localization:
Nucleus.
Sequence:
MEVDLELSVGGSFRNLETSKPKIDSKLELCSCSRSEDAKAKREIQALRRQEAKKKREKKKGMRNGGGVGDERMRLEAQRLQNRVKDRERRENNEANLTHHKSYINHRNHGIVEGPIQMMVPIKYAHPSKVQYVPLAFPCVVPCGAPATWLQPVKSLPVRQGCGGRSVLSDGWTNSSASVSHQDSGSSDIGSLSSHTRTAPPQSSEAQGQSEHSVSSYQKDSSQGTRSDKSTSFGEKVSTPVKDPTTRRNSSTGESPPSPLKKARDGNGDLGEPPKPRNQNHHPSAPSLEQMPCVSTTGNGPNGKTITGFLYRYTKAEISIVCVCHGSSFSPAGFVEHAGGIDVSHPLRHITVIPSAFA
The following text describes a protein:
Function:
Potassium channel protein that may be component of regulatory network that controls ray development and function.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MKCSFHIPEKYQWASTLFVHVALIAGVAVYTVFGALSMQWLESPDRVRALLKRELKPVESLPPPPSISGLPDRITRVYLGEELAILDPGVHECLERTILTLFHDTKCDPYSFEHLNIELIDRCYAEANVPIPEGYGGQPRKKIKNKEEEKDVIDETPAEKWSIGNSVIFAFTVITTIGYGHVAPETFEGRLFLIFYGVIGVPFTLLTIADLGMFLTRFLKNLLTMARRFAHYLVKLYQKAKKQRNKSQKTSPVMPDSERSEVWNTGKEMKEMSMRTAREPGEGDEIEVIENGNDENGKEEDEEEPENNEPRKTEESIALGITFTCYLVAGAKILSVYEPEMDFFKALYFNFVTLTTIGLGDFVPKSFDYLLITLIYIGIGLALTTMAIEIAADLLKKLHYIGRKMENVGQAVVWFGGKKMTMKSLVKHLGDQFNIPEEELANFDMSAFVDNAIKVEKGEIATLRKPPTPPVVFRERAFSFSNVRNSSESALKYVDDNRFSKTTQPTIYTVIIHETTRTIDTLHNLADAIRRDPSIPRLDLDVHYLTDMSAPTSFDENYLRTYTNARRK
The following text describes a protein:
Function:
Calcium-gated potassium channel.
Miscellaneous:
MISCELLANEOUS: It is not known whether calcium is the physiological ligand; MISCELLANEOUS: Inhibited by charybdotoxin (CTX), a protein from scorpion venom.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
The channel is composed of 4 repeated units, each containing a transmembrane pore part and a gating ring part. The gating ring is composed of eight identical RCK (Regulators of K conductance) domains, in an alternating arrangement of one domain from each of the four subunits and four from the intracellular solution. Two protein interfaces between dimers of RCK domains from the pore-forming subunit and from the intracellular solution hold the ring together. One is called the fixed interface and the other the flexible interface. The flexible interface forms a cleft where calcium binds. Upon calcium binding the gating ring undergoes a conformational change that enables it to pull open the inner helices of the pore, allowing ion conduction.
Sequence:
MVLVIEIIRKHLPRVLKVPATRILLLVLAVIIYGTAGFHFIEGESWTVSLYWTFVTIATVGYGDYSPSTPLGMYFTVTLIVLGIGTFAVAVERLLEFLINREQMKLMGLIDVAKSRHVVICGWSESTLECLRELRGSEVFVLAEDENVRKKVLRSGANFVHGDPTRVSDLEKANVRGARAVIVDLESDSETIHCILGIRKIDESVRIIAEAERYENIEQLRMAGADQVISPFVISGRLMSRSIDDGYEAMFVQDVLAEESTRRMVEVPIPEGSKLEGVSVLDADIHDVTGVIIIGVGRGDELIIDPPRDYSFRAGDIILGIGKPEEIERLKNYISA
The following text describes a protein:
Function:
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with CTU1/ATPBD3 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
Subcellular Localization:
Cytoplasm.
Sequence:
MFLFFISELKDAVRVRHSCPLFVKCLQKMCQMQRGAGSSSDPCRRPLLQVRPTWEVGAPPCSFFNESRTGSGSCCLSVRSCFREYFTHKFRAMLGKTRLIFPGEKVLLAVSGGPSSSAMLSQVQQGLGQSAQKKLRFLPGLVHIDEGGALGLSLGERQRLVSELKAIFQTSGFPFHVIPLEQVLDLPTSAVNTTPPSSDRAPDCYKAAGDGGELQQGGALAEPSVHEAQTRSLQQLLGSATTLTAKEELLRTLRQHLLVHEARTRGYSKLLLGESCTRLAVRLLTCVSLGRGAHLAQDTGFSDCRFGDVTFVRPMREFSAKEIAVYNHMFRVPTVVIPSLETKTLEKASIQRLSESFVSRLQQDFPSTVSTIYRTSEKLQTAGGGCCEEDGRCLLCLCSLDTAAGKASALQARLISEQLCCQKPAGTVKVEPSPPAGPCCSSADGECGSAAGGAVCCSSEAPEKKDLQKLLCYSCQLTLRDMSSVAHLPQYILTEAQRRKRRSLMKDEISEFLLEEEEGSS
The following text describes a protein:
Function:
Binds long-chain acyl-coenzyme A molecules with a strong preference for unsaturated C18:1-CoA. Does not bind fatty acids. Plays a role in protein N-myristoylation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MASPGVLEESSSGEACSGGCPEQWDEKTEEELQGQFEQAAKHVQNVASVASTEQLLFLYARYKQVKVGRCNTPKPGFFDYEGKKKWEAWKALGDYSCQQAMNEYIETVKKLDPDWSPQALEEPHKEPKTTFGGPVVSCLYKVQETLREEDKDIFDYCRENNISRVSHALSTGAIDVNVADDEGRCLLHWACDRGHTQLVSVLLFHNAHINMQDSEGQTPLHYASACEFPDIVDLLLDHGADPSLVDNDGFQPHEVTDSKNIAAMLQQHASYGEHNKPASLLLEMPQ
The following text describes a protein:
Function:
Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB.
Sequence:
MLTALKTDTGKIRQHNEDDAGIFKGKDEFILAVVADGMGGHLAGDVASKMAVKAMGEKWNEAETIPTAPSECEKWLIEQILSVNSKIYDHAQAHEECQGMGTTIVCALFTGKTVSVAHIGDSRCYLLQDDDFVQVTEDHSLVNELVRTGEISREDAEHHPRKNVLTKALGTDQLVSIDTRSFDIEPGDKLLLCSDGLTNKVEGTELKDILQSDSAPQEKVNLLVDKANQNGGEDNITAVLLELALQVEEGEDQC
The following text describes a protein:
Function:
E3 ubiquitin ligase which catalyzes the covalent attachment of ubiquitin moieties onto substrate proteins (By similarity). Promotes the larval to adult transition by binding to the long non-coding RNA lep-5 to target the heterochronic protein lin-28 for degradation by the proteasome. This association and degradation of lin-28 also controls the timing of the sexual differentiation of individual neurons in males including the AIM, AWA, ADF, ASJ and CEM neurons. Plays a role in governing the developmental timing of male tail tip morphogenesis. Plays a role in two aspects of male mating behavior: response to hermaphrodite contact and vulva location. May play a role in the detection of preferred food sources.
Subcellular Localization:
Cytoplasm.
Sequence:
MPRHETDCRYFANGYCSKGNTCTFTHDVATRNENICHFNLVGKCSYGRACRFLHTRPRNDELPSCSTPQTSQNQQNLQNSGQRVRPKQLPELKFNAQAAEFVPRWKMPQRGPVTSYAGAAASADHGESSSSFQSSHEQAQLMMCPYHQKSGDCNRQDMDCPFAHGNYCDMCQQWSLHPYNAELRKKHENECVANHTTEMERAFLLQKTEQKTCGICMENIFEKNLRFGILNGCQHCFCLDCIRQWRSKDQENVELATKTVRSCPECRQHSDYVIPSLFWVESGQEKDLLIEMYKENTKRKICKYYSNERSRGACPFGNKCFYKHQLPDGSIDPGEAPSSRRRPRLVDFLFDDNSDSDEETFRRFQEEHEEEQEELLRFVAETLPEADEESELFRQITEVLRHYQISGHRRGFQ
The following text describes a protein:
Function:
Specifically, catalyzes the dephosphorylation of inosine monophosphate (IMP) into inosine. By dephosphorylating IMP, plays a role in the purine salvage pathway. Does not have phosphotransferase activity with IMP as phosphate donor and adenosine as phosphate acceptor.
Subcellular Localization:
Cytoplasm.
Sequence:
MKNLDINTFDNIEDIPLGSSEQDPYDFFTLSDRNVMNSDMKKNIVQWNSRYSYNQLKNKDSLIMFLVEIFRSLFVSNCIDKNIDNVLLSIEEMFIDHYYNPQHSRLKYLIDDVGIFFTKLPITKAFHTYNKKYRITKRLYAPPTFNEVRHILNLAQILSLEEGLDLLTFDADETLYPDGHDFNDEVLASYISCLLKKMNIAIVTAASYNNDAEKYQKRLENLLKYFSKHNIKDGSYKNFYVMGGESNYLFKCNEEATLYSVPENEWRHYKKFVDYDTVQEILNISEKCLEKVIKDFGLCAQIQRKEKSIGLVPNKIPSLNIKNEQKNYMIKYEVLEEAVIRIKKEIIKNKITAPYCAFNGGQDLWVDVGNKAEGLLILQKLLKIQKKKCCHIGDQFLHSGNDFPTRFCSLTLWVSNPQETKACLKSIMHLNIKSFIPEVLYENQ
The following text describes a protein:
Function:
May be a receptor for oxidized free fatty acids derived from linoleic and arachidonic acids such as 9-hydroxyoctadecadienoic acid (9-HODE). Activates a G alpha protein, most likely G alpha(q). May be involved in apoptosis. Functions at the G2/M checkpoint to delay mitosis. May function as a sensor that monitors the oxidative states and mediates appropriate cellular responses such as secretion of paracrine signals and attenuation of proliferation. May mediate ths accumulation of intracellular inositol phosphates at acidic pH through proton-sensing activity (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Note=Internalized and accumulated in endosomal compartments. LPC triggers the relocalization from the endosomal compartment to the cell surface.
Sequence:
MRSEPTNAAGNTTLGVTSVLQSTSVPSSETCHVSYEESRVVLVVVYSAVCLLGLPANCLTAWLTLLQVLQRNVLAVYLFCLSLCELLYISTVPLWIIYIQNQHKWNLGPQACKVTAYIFFCNIYISILLLCCISCDRYMAVVYALESRGHRHQRTAVTISACVILLVGLVNYPVFDMKVEKSFCFEPLRMNSKIAGYHYLRFTFGFAIPLGILAFTNHQIFRSIKLSDSLSAAQKNKVKRSAIAVVTIFLVCFAPYHVVLLVKAASFSFYQGDMDAVCAFESRLYTVSMVFLCLSTVNSVADPIIYVLGTDHSRQEVSRIHTGWKKWSTKTYVTCSKDSEETHLPTELSNTYTFPNPAHPPGSQPAKLGLLCSPERLPEELC
The following text describes a protein:
Function:
Probable methyltransferase.
Sequence:
MENNNNNNKNDNEINFKKIEINETLESGKFIESKIDMKLGELIIKVQSPMCFSFHKHLVNQFCFNCFSNSHEINNAKFNKFKVDINKNYIIRCNNCKLIYFCSDECFEKVMSIESFQDSTSTNIHTPLECLILSNYHDQTISPKINTLHDQTENRMIINYLSKIAYSTNNNNKFKLLLIEMNQLIGDFNNDNNNQTLSLNEIKNIKNKSFNLRKLFNNFFFNIDKVIIEELYAKSQRNSFGLWKNSDECFGLSMYGNQTIYNNNNDKDDNISISYFNHSCFPNCVRVQENQSISIYSLIPIKKGDELSISYIDIRMSKNDRLLHLKEIYYFECKCKRCTLPPLSNLSLEIEKTIENYTCKNQSIKCTGILYLPPFNKIQRICNFCHWKEPINN
The following text describes a protein:
Function:
Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Subcellular Localization:
Nucleus.
Sequence:
MFRLKTSGRGKGNLAESLLEHCSKQQSVLAGSPRNTLEQLALKKALSLLGAAWRLRDEPRDAWRRLLRLFSLGTPWDGEEAGETPQVYGLQLVSAGKMAFPEYQVWRKDILFAEREDLIRYETARVLESQLMQAALDKKWAKARELLDSVEALARTPDSVQCGKRDQALPPFLRRFTTTGVYTRCRCLGVDVLQRLKEHWRAVRLLRALLGQTHFCLSRRGHWWDRLALNLDVHLGKPGEAMDAIKEALGESGISPASRHALLTRAARLAVKLPEHPSASALRDFVPSDVTATPEVTIQGQLAERMVPGRTNMFAVRESDGALRVIPVEEVALRHYSEKGYPQGIHGEGSTFHALFGILCWDAIYADGVPDAFRSPYQAFPMDLHSDGFFASREQRFLKVFENIRTSSVEELAEQVASTYDSHSGQAGLVQWERFSSVQIQELVRCFGPEVLWRLCDLLARNFRHRRSGLPDLVVWNPVDGRLKAAEVKGPGDTLSAKQVVWLRELLALGIDCEVCHVTATSSKRLRKQENFITDKDTTTKK
The following text describes a protein:
Function:
Catalyzes the adenosylmethionine-dependent methylation of the exocyclic amino group (N(2)) of guanosine at position 10 of various tRNAs. Acts via a two-step process that leads to the formation of either N(2)-monomethyl (m(2)G) or N(2)-dimethylguanosine (m(2)(2)G).
Subcellular Localization:
Cytoplasm.
Sequence:
MPESFFVLSKEYLEIAIDEVITIAKTFDRFSKIKIISNLVIIQSKTNWYEISKKATFVKTSGQILRKMSGLFLDEGNFEILKNAKTFVCRIINLSSNQFDIPELENSMGDMISKFSNAKVKLENPDITVYLIFTNKENFFGFSKITKEKKRPKKAISQPHELDWKLTRAMINLVGLKKGETVCDPFCGTGTTLLEAESMGIHGIGLDFDEKMVEITKKNLKENGYKSRVIHSDFQEIKNMADEFDGIVTDFPYGKNTKTSEKPEEIIKKFVTIVPKRKKMAIMYKKELGDKLKLKGLKKYQIYRHKSLTRTILIK
The following text describes a protein:
Function:
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in chloroplasts and mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Subcellular Localization:
Mitochondrion. Plastid, chloroplast.
Sequence:
MMASSSSSAALLAHARLLPRRLPPLSPFVRPCSASSASSSSTRQVEPPNLAQLCDKARISLSAKEIEEFSPQISKVVDWFAQLQDVDVENIEPAIRVGALDGKSALRADTPVIFEERETMIASLPDREGPYMRVPKILKENVE
The following text describes a protein:
Function:
Catalyzes the N-acylation of UDP-3-O-(hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Prefers (3R)-3-hydroxytetradecanoyl-ACP over (3R)-3-hydroxyhexadecanoyl-ACP as the acyl donor in vitro, which is consistent with the structure of E.coli lipid A that contains over 95% (R)-3-hydroxytetradecanoate at the 2 and 2' positions.
Sequence:
MPSIRLADLAQQLDAELHGDGDIVITGVASMQSAQTGHITFMVNPKYREHLGLCQASAVVMTQDDLPFAKSAALVVKNPYLTYARMAQILDTTPQPAQNIAPSAVIDATAKLGNNVSIGANAVIESGVELGDNVIIGAGCFVGKNSKIGAGSRLWANVTIYHEIQIGQNCLIQSGTVVGADGFGYANDRGNWVKIPQIGRVIIGDRVEIGACTTIDRGALDDTIIGNGVIIDNQCQIAHNVVIGDNTAVAGGVIMAGSLKIGRYCMIGGASVINGHMEICDKVTVTGMGMVMRPITEPGVYSSGIPLQPNKVWRKTAALVMNIDDMSKRLKSLERKVNQQD