lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3 and participates in phytic acid biosynthesis in developing seeds. Phytic acid is the primary storage form of phosphorus in cereal grains and other plant seeds.
Sequence:
MATGRPVRLVLDASLLLDPSSTREAAAVALRPGVEELLRRLRYSNLSVAICYAEGMPTNESDFLEKVASSHLFGSIVLLAKSGNLSPIELMIEWSRTSFCFYATSRVDKGLISELQNQNWRVLSVANECSIEVPGVLNVQRLQELLLTLATLMKKELCGSSVLVIGYIMKKSREEDFAKRGAFPIYPSKGSLIFVPLSFEIPLSLQLQEVDMVLHKITDEIVKIDPNCSIDFPKGISFSAGMSEIIRFVEEHPDFCIMDPFKNIYPLLDRLQIQKILVRLQELGTEGKPKLRAPYSCKVDSFHNGELDKHLVEANLSFPLIVKPQVACGVADAHNMALVFQIEEFSNLSVPLPAVLQEYVDHGSKIFKFYVIGDKVFYAVRDSMPNARFLKPSSGGEALTFNSLKTLPVATNEQRPQTGAEDGKLLDADLVEEAAKFLKGLLGLTVFGFDVVVQEGTGDHVIVDLNYLPSFKEVPDSEAVPAFWDAVRQAYESTRGNANAQG
The following text describes a protein:
Function:
Component of an histone acetyltransferase complex.
Subcellular Localization:
Nucleus.
Domain:
The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence:
MLYLEDYLEMIEHLPQELRDRFTEMRELDLAVQNNMDSLDKKAHMFFKQCKRDELQHESMDTEFHSLRGEYFKVMEDADEKVAIATQIHELVERYLRRLDSELFKFKCELEADNNGITEILERRSLELDGNSTAATALLLSMNQKENRYYGASSANTMVNSSTGHATGAATGSSGIALVSGAAGTGGALSSISTAQLGSSQRHRKLEKRRETICTVPVQEKRANLNHSLPVVGSGSTTAAAASSSSATTAAAAASLASATTAQTHVSNHIGSIAATHLTLPVAMGVAGGSSSLASSSLATGTGSLVRQLPTNLTHTVLSTSGGATAAAAAGGNSTSVVAAGTAHGHAHVSGHSAAGATVTYNLQQLGGGAAASSAIAAAASQAIVATQQMQQGRRTASLKASYEAIHGTAGTTTDFWTQAGQGGLQQSTAGSVTVAAGTALATGAAGGSSTGSHHSHHSQSHHGGHGHGHGHGHGHGHGHGHHSSSGHGGGHSSHHQEKKQKKKLTTALTLPTVQPTAGSSSGNSIGSSSSISLESVNKLTTSAALAAASATTTYMSVGGQALLAMTPGGGGGGNLAESSAEGVPAGMIAMNLPTTTVTPGSSLTIGENGLVVEQTNEGEWSYDPNEPRYCTCNQVSYGDMVACDNDACPYEWFHYPCVGITQPPKGKWYCPKCTASMRRRGNRKN
The following text describes a protein:
Function:
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Is the primary scavenger for endogenously generated hydrogen peroxides.
Miscellaneous:
MISCELLANEOUS: The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by AhpF.
Subcellular Localization:
Cytoplasm.
Sequence:
MSLINTKIKPFKNQAFKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVASHPGEVCPAKWKEGEATLAPSLDLVGKI
The following text describes a protein:
Function:
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular Localization:
Cytoplasm.
Sequence:
MTEMLSCLVPYLDKHLVLGLLYFYDDQGVDVGDALRFVQATTALTPEGEVSLEQENKIRETAERARPALDMFFEQNVSDNCTYQLCLTESRIDELRGKGELSRGFLEKEGITPKVMTAVMDLAFLYYDAARYGDASELLSLLQCVTGYELGESKLLWGRLVCDTCSCRWPSAIAAAEKLWKQQGADGSENKSGKTTLRGDNGTSVTERVWLLHWALFPFFKGGNQYSTHLLNIVFDNKTDSIYQCVVETVCPHYLRYICAAAILNTHRRSALRRAAEMVGRIYEYSDPLTQLVREITNYRSFEDTLELLPKVSELAQGDYFLNLHADNLVENAKRLIFTQYVVTHSVVSIPYMAERLEMSAAGAEVWLADLISETKQRAKIDAVTGQMFVGSQVRSVHQTVLDRLEPVDHGRR
The following text describes a protein:
Function:
Involved in cell wall 1,6-beta-glucan assembly possibly by the addition of linear side chains of 1,6-linked Glc units to a highly branched 1,6- and 1,3-linked glucan backbone.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor. Secreted, cell wall.
Sequence:
MNVNSVIYYILFLFASTILAADKTSSSVSPTLVWVTGTDANGKLATTQSTYYQSFMSTYTTAETPSSGSIGLGSISGTVGEIRTYSMTTISQGNGGLSKFNQNGLEMKNLSFVKLIGVSFIAFISFILLI
The following text describes a protein:
Function:
Binds specifically to phosphatidylinositol 3,4-diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May recruit other proteins to the plasma membrane.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Cytoplasm. Nucleus.
Sequence:
MPYVDRQNRICGFLDIEENENSGKFLRRYFILDTREDSFVWYMDNPQGLEPGASHMLGKCSTVEPYPSSYSVILMSDLNLPSGSSRVGAIKLTYISKVSDATKLRPKAEFCFVMNAGMRKYFLQANDQQDLVEWVNVLNKAIKITVPKQSDSQPASDNLSRQGDCGKKQVSYRTDIVGGVPIITPTQKEEVNECGESVDRNNLKRSQSHLPYFAPKPPADSAVIKAGYCVKQGAVMKNWKRRYFQLDENTIGYFKSELEKEPLRVIPLKEVHKVQECKQSDIMMRDNLFEIVTTSRTFYVQADSPEEMHSWIKAVSGAIVAQRGPGRSSSSSMRQARRLSNPCIQRYTSRAGECSTSIPAVLQNPNTLSVLPGQQPPPPHIPQPLAATLWSQAIPWRSEDFTNLLPRSSQGTSRSRLSLQENQLPK
The following text describes a protein:
Function:
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Subcellular Localization:
Cell membrane. Mitochondrion intermembrane space.
Sequence:
LMKTANADNGPQIAKKCLMCHSLDKDGPNKLGPHLWNVAGRPKASIADYKYSPALSKLGGVWDDDSLFAFLHKPSSYAPGTKMSFAGISKPQDIADVILFLKTYVHDK
The following text describes a protein:
Function:
May only reduce GSH-thiol disulfides, but not protein disulfides.
Sequence:
MARLLSNMVLRGIASSSNNTRVAFGPSFLKRMKFLTKGTDDSVVNEDLPTNGFASSDTHPTKITSDPVTHKDFQSTNKSTGISVLDIVQQDVQNNPVMIYMTGLTDAPRCGFSALAVKVLRQYGVPIRARDILGDLKLKENVKAHTDWPTNPQIFIKGEFLGGSDIILSMHQKGELKDLLADITGDDRQGRE
The following text describes a protein:
Function:
Mediates the transport of CDP-ribitol (By similarity). Does not exhibit CMP-sialic acid, UDP-galactose and UDP-N-acetylglucosamine transport activity (By similarity).
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MIAISADESPESSSPALRLRWLFLLLLLVLIYGSHAPLLSLCKTQAQIPFSASSCVLLIETSKLFISFASLLASGSVSTLRISISMTTASPYAVPAVLYAFNNHLVVFMQAYMDPSSFQVLSNLKIASTALLYTSCLGKRLHRRQWFAMGLLVSAGVSHSCFSYDLEGKRETAVYITSWGLLLVLVYCFVSGLAAVYTERVLKSQRLPLSMQNLFLYTFGVVVNLASHLSGGEQKGFFEGYSAVVWVIVAGQVANGLLMSVVMKHGTGITRLFVISSAMLVNAVLSWGILGVQLTGYFLFPVVLIGWAVYLYYT
The following text describes a protein:
Function:
Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive secretory pathway, with unique restricted distribution in both neuroendocrine and non-neuroendocrine tissues.
Sequence:
DEEEYTAPSIQGSPNTLQTSVCHPECGDKGCDGPNADQCLNCVHFSLGNSKTNRKCVSECPLGYFGDAAARRCRRCHKGCETCTGRSPAQCLSCRRGFYHHQETNTCVTLCPAGLYADESQRLCLRCHPSCQKCVDEPEKCTVCKEGFSLARGSCIPDCEPGTYFDSELVKCGECHHTCRTCVGPSREECIHCAKSFHFQDWKCVPACGEGFYPEEMPGLPHKVCRRCEENCLSCEGSSRNCSRCKAGFTQLGTSCITNHTCSNADETFCEMVKSNRLCERKLFIQFCCRTCLLAG
The following text describes a protein:
Function:
Oxygenase component of the salicylate 5-hydroxylase (S5H) multicomponent enzyme system which catalyzes the 5-hydroxylation of salicylate to gentisate. Active only on substrates with a ring-substituted carboxylate group with an adjacent hydroxyl group. Primarily active against salicylate and substituted salicylates, but not against 2-hydroxycinnamate, 3-hydroxycinnamate, 2-hydroxyphenylacetate, 3-hydroxyphenylacetate, 2-hydroxybenzophenone, 1-hydroxy-2-naphthoate, 4-methoxysalicylate or 2-hydroxyacetophenone.
Sequence:
MVDFKTYFELLNLYSDYAMVCDSANWEKWPDFFIETGTYRLQPRENFEQGLPLCLLALESKAMIRDRVYGVKETMYHDPYYQRHIVGTPRVLSVERDADGERITAEASYAVIRTKYDGDSTIFNAGYYRDVIVRTPEGLKLKSRLCVYDSEMIPNSVIYPI
The following text describes a protein:
Function:
Transmembrane adapter protein which associates with KLRK1 to form an activation receptor KLRK1-HCST in lymphoid and myeloid cells; this receptor plays a major role in triggering cytotoxicity against target cells expressing cell surface ligands such as MHC class I chain-related MICA and MICB, and UL16-binding proteins (ULBPs); these ligands are up-regulated by stress conditions and pathological state such as viral infection and tumor transformation. Functions as a docking site for PI3-kinase PIK3R1 and GRB2. Interaction of ULBPs with KLRK1-HCST triggers calcium mobilization and activation of the PIK3R1, MAP2K/ERK, and JAK2/STAT5 signaling pathways. Both PIK3R1 and GRB2 are required for full KLRK1-HCST-mediated activation and ultimate killing of target cells. In NK cells, KLRK1-HCST signaling directly induces cytotoxicity and enhances cytokine production initiated via DAP12/TYROBP-associated receptors. In T-cells, it provides primarily costimulation for TCR-induced signals. KLRK1-HCST receptor plays a role in immune surveillance against tumors and is required for cytolysis of tumors cells; indeed, melanoma cells that do not express KLRK1 ligands escape from immune surveillance mediated by NK cells (By similarity).
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MIHPGHILFLLLLPVAAAQTTPGSCSGCGSLSLPLLAGLVAADAVASLLIVGAVFLCARPRRSPAQDGKVYINMPGRG
The following text describes a protein:
Function:
Involved in the biosynthesis of terminal alkyne-containing amino acids such as L-propargylglycine (Pra) and L-beta-ethynylserine, that are produced as antibiotics by S.cattleya. Catalyzes the chlorination of L-lysine at the C4 position, leading to the production of 4-chloro-L-lysine.
Sequence:
MCAPLEKDDIRRLSQAFHRFGIVTVTELIEPHTRKLVRAEADRLLDQYAERRDLRLATTDYTRRSMSVVPSETIAANSELVTGLYAHRELLAPLEAIAGERLHPCPKADEEFLITRQEQRGDTHGWHWGDFSFALIWVLQAPPIDVGGLLQCVPHTTWDKASPQINRYLVENPIDTYHFESGDVYFLRTDTTLHRTIPLREDTTRIILNMTWAGERDLSRKLAADDRWWDNAEVSAARAIKD
The following text describes a protein:
Function:
Acts as a component of the outer kinetochore KNL1 complex that facilitates microtubule-kinetochore interactions and the spindle assembly checkpoint. Kinetochores, consisting of a centromere-associated inner segment and a microtubule-contacting outer segment, play a crucial role in chromosome segregation by mediating the physical connection between centromeric DNA and spindle microtubules. The outer kinetochore is made up of the ten-subunit KMN network, comprising the MIS12, NDC80 and KNL1 complexes, and auxiliary microtubule-associated components; together they connect the outer kinetochore with the inner kinetochore, bind microtubules, and mediate interactions with mitotic checkpoint proteins that delay anaphase until chromosomes are bioriented on the spindle.
Subcellular Localization:
Nucleus. Chromosome, centromere, kinetochore.
Sequence:
MTHYHSEYYSEVEKFEYQVTHVTEQILQEQDRLRGSTLHEYNQTILQLVSDYEMFNSNGQCDPSEINLPLEKLESWTNSLKQIHLELESIDNFLRYAIPSDQTILNLSKFNESKYETLQAEVSELRDINVVQLQKEIESLQQQITTKSDENLLISEKIKESCLEASQDIDQCWKLLEQLEAYENANPSTEVITTTDPAFSTYNQWKWNQLAESELKHINQQLITLRATKEKLDKVFSKRSELETSPKSIETFTSYQLLSQLWRSKFIRQLLPDIANLEVYPQSGKLKFEVGIMQVIMQIESGIIKSVSLFSYELSYDRIETIKEDILGRIEHQKSLFKVLVVITDYIVNSL
The following text describes a protein:
Function:
Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMOs to their mature forms and deconjugation of SUMO from targeted proteins. Cleaves precursors of SUM1 and SUM2, but not of SUM3 or SUM5. Able to release SUM1 and SUM2 from conjugates, but unable to cleave SUM3. Protease activity mainly directed at deconjugating SUM1 and SUM2 from their target proteins. Regulates salt stress responses and flowering time. Redundant with ULP1D.
Subcellular Localization:
Nucleus, nucleoplasm.
Domain:
The N-terminal regulatory domain is not required for peptidase activity in vitro.
Sequence:
MKRQRAIELDRVKKTMLNIDWDDALGDEEVPELEIIATDKIPPREPTLSGYEPAVSVRSLRDNELDDHLKRQRSLLTRLGDKLADKGEKIRNRIGELEYEKQRRMFQQRTKMQDADNGCQILEKPKSSDVFMRASTASKDTSGQGTSGSKDVSRSTFAAHFSDNLKMGPQPVKLVNDKLQDLGRGSWISKANRDSIIEKNNVWRSLPRLSKCKVSLKNFYSESKDPKGDRRPNEAYGKGKPNESSPYLLVDDDDGDDDKVIGYETPRHWSLKASPLQSSSCRKKSDDKVINLDEDEPLSPMVVEEACELPEGLPEDIYYPSSDQSDGRDLVQVSLKDLKCLSPGEYLTSPVINFYIRYVQHHVFSADKTAANCHFFNTFFYKKLTEAVSYKGNDRDAYFVKFRRWWKGFDLFCKSYIFIPIHEDLHWSLVIICIPDKEDESGLTIIHLDSLGLHPRNLIFNNVKRFLREEWNYLNQDAPLDLPISAKVWRDLPNMINEAEVQVPQQKNDFDCGLFLLFFIRRFIEEAPQRLTLQDLKMIHKKWFKPEEASALRIKIWNILVDLFRKGNQTD
The following text describes a protein:
Function:
May have the capacity to recognize and bind specific classes of odorants. May act as a carrier molecule, transporting odorants across the mucus layer to access receptor sites. May serve as a primary defense mechanism by recognizing and removing potentially harmful odorants or pathogenic microorganisms from the mucosa or clearing excess odorant from mucus to enable new odorant stimuli to be received (By similarity).
Subcellular Localization:
Secreted. Cytoplasm. Note=According to PubMed:12837268, it is cytoplasmic.
Sequence:
MLALWSLLLLWGLATPCQELLETVGTLARIDKDELGKAIQNSLVGEPILQNVLGSVTAVNRGLLGSGGLLGGGGLLGHGGVFGVVEELSGLKIEELTLPKVLLKLLPGFGVQLSLHTKVGMHCSGPLGGLLQLAAEVNVTSRVALAVSSRGTPILILKRCSTLLGHISLFSGLLPTPLFGVVEQMLFKVLPGLLCPVVDSVLGVVNELLGAVLGLVSLGALGSVEFSLATLPLISNQYIELDINPIVKSVAGDIIDFPKSRAPAKVPPKKDHTSQVMVPLYLFNTTFGLLQTNGALDMDITPELVPSDVPLTTTDLAALLPEALGKLPLHQQLLLFLRVREAPTVTLHNKKALVSLPANIHVLFYVPKGTPESLFELNSVMTVRAQLAPSATKLHISLSLERLSVKVASSFTHAFDGSRLEEWLSHVVGAVYAPKLNVALDVGIPLPKVLNINFSNSVLEIVENAVVLTVAS
The following text describes a protein:
Function:
Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS16 but not VIPAS39. The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG.
Subcellular Localization:
Cytoplasmic vesicle, autophagosome. Cytoplasmic vesicle, clathrin-coated vesicle. Early endosome. Late endosome membrane; Peripheral membrane protein; Cytoplasmic side. Lysosome membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANRTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYKREILQTYGYEHILTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF
The following text describes a protein:
Function:
Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
Domain:
The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space.
Sequence:
MDLSSLPTDDNLDDKKRAAVLLSLQEIVQKQKENVKVMDICFNKCVSKIGPKLSSSEQKCIWDCANSYFYTNVFLNQRLEQMTKILKSNSDYTNL
The following text describes a protein:
Function:
Molecular adapter which is involved in cilium biogenesis. Part of a functional complex including OFD1 a centriolar protein involved in cilium assembly. Could regulate the cAMP-dependent phosphorylation of OFD1, and its subsequent ubiquitination by PJA2 which ultimately leads to its proteasomal degradation.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite.
Sequence:
MKNKGQQQHTLAVKNGSLMNPEGQTINGLIDLIKLKSQPKIVYYFDFLVCIDQSGNPFIFYHDKNRYINIPTISPAHLISYIDNKGGQLAIALQNKTIQIVSCQNGRNLKTLKGHEHQILSMHTNHTQNLLLSVSQDQCILHSLDSFDKVHSLFSKGSIFVGASFLPSSTELATVMADKSLSIWNLSSFEIISRIQLPEQFNIKQCQLVPSIDGQRLIINCYSSKIHILDNNNNLITQDVNQGYGNGALLVKPIKKQQILILTKNFMIIQVDSSGSLIKCMEILQGKTPTHFDVYQNKIAIILNTGEIALYDLNKLNKQNQNLNSTIGVNVSTMIKENYADTLNFNNTTTNIDIKKVGNNTNTLQGSFSQSTVSKKNSKSNSMTQPINSYTLGKIYKNSEDPLKELLNYQKLQQFLKQYHVFPDDKRSLIWRSLLNLPMNQEAYNNLINQGVHPAYQKLADQYPLQSESLFSRLQRTLSCLAYYCPLFAEIDYLPQLVFPFVKLFKRGEELLIFEATLSLLIQHCQRFFENFPNAPVSLLQFHDQVFNQVEPQLYQHMKQYLGYSPIKYAWPSIRSLYTNLLTKNQWLQLIDHLILYNDLPQMIVLFMVEYFIYFKSTIMKMNDQDQLDLFFGRSNTVEIDKLIESTIYLSKSLDMDQYQINLQFLLPLQKDQYQLFSIYPKGSVQYQARVREQLQEDEQRLIQKQQQISRLQQMAQQMEQLDQLFQEKQLLTMQAEKDRQEMFDYQVEMRAQKQFQQDQQVRQQRIKQLENLEKNMNSAVQKQLDLQQQEQEFLNKQFRKTQLADNFRIVSLQEEEALQNLEYQIFSKFQHQMEQRSKQENQRKIQSQLEFRSKEKELLDQIKQEQWKMDSQQQQIKVEQLKQLRMQQIQELENEAQLEEVEYQERINQFQQDLKMIQLEREKKLRDQLFQEQISKEELQLRDKKQVEDKKRQSSVQRRQQFEQEMERIAKQHQEKLRMQEQQLMEQYKKSQSFSNQPYQPNYYQNSNYQNNFEQSSGDVREPMTSQKLSSALYDFQSSQKQQQFSPSMLVEDEREKINQLRNQLRDEMQNIREREHDEQLQSMLREREQEIFKRTQQIRDQINQEVENKNNSSTQFNSYQHITQDNSKRQQQYYSPGSSSQFSLYKPQQEVDIEPRDLSESQLTYSSGFTSPGQRY
The following text describes a protein:
Function:
Processive glucosyltransferase involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. Is able to successively transfer up to three glucosyl residues to diacylglycerol (DAG), thereby catalyzing the formation of beta-monoglucosyl-DAG (3-O-(beta-D-glucopyranosyl)-1,2-diacyl-sn-glycerol), beta-diglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl)-1,2-diacyl-sn-glycerol) and beta-triglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl)-1,2-diacyl-sn-glycerol). Beta-diglucosyl-DAG is the predominant glycolipid found in Bacillales and is also used as a membrane anchor for lipoteichoic acid (LTA). Also seems to be able to form beta-tetraglucosyl-DAG, although this glycolipid has not been found in B.subtilis membrane. UgtP can only use UDP-glucose as sugar donor.
Subcellular Localization:
Cell membrane. Note=Localized in both septal membrane.
Sequence:
MNTNKRVLILTANYGNGHVQVAKTLYEQCVRLGFQHVTVSNLYQESNPIVSEVTQYLYLKSFSIGKQFYRLFYYGVDKIYNKRKFNIYFKMGNKRLGELVDEHQPDIIINTFPMIVVPEYRRRTGRVIPTFNVMTDFCLHKIWVHENVDKYYVATDYVKEKLLEIGTHPSNVKITGIPIRPQFEESMPVGPIYKKYNLSPNKKVLLIMAGAHGVLKNVKELCENLVKDDQVQVVVVCGKNTALKESLSALEAENGDKLKVLGYVERIDELFRITDCMITKPGGITLTEATAIGVPVILYKPVPGQEKENANFFEDRGAAIVVNRHEEILESVTSLLADEDTLHRMKKNIKDLHLANSSEVILEDILKESEMMTAKQKAKVLS
The following text describes a protein:
Function:
GTPase-activating protein for the ADP ribosylation factor family.
Subcellular Localization:
Cytoplasm.
Sequence:
MELLSQISFPYYQEDDTCVTLNKLSFTDELDSKRSVIALNEKKQVDTFNTIYTNTQQIVLQLASYIENPDDDEKSQFPLLIKISPEFNKLKLHVSIKPVVGFESRSLIIVKSRGVTDVDVLKNQLYDDNTQDKPMTELSKLEYRKLPIEENNHSFQKIIINDFFDPKIVNNTKLNISLWEHDSTSNEFRHFLNFSVWIDKLAPVETPINRSSFSLATKGQPLEEKSPESKLFSLGDFRKEFKIDIEDGPEFRKTLTRLENNIPWAKKIYSNLVDEFRVLESNVRRVTTSKIKVMDTIDQIVDLESTSLLKEFGFKSDFHIVFKAMFEPFEKNLNFFFENVCDHKLLNKIYANIGFTQIDSSAVYLELQKKFEADSKEYYSWLNKYLSNEKERPESKLLAKRKVFELSKFDYLNSLTKVTNNQYVNEVLENFFKFLNLKYDPRYPRLLDYHSFKDKKSNQNLLGDNYQIYMNVLLRFNSERYQFRQMIEACQTNEELTNLIRCNRLNHKSVSTSSSSPSTSTASPHNLVTSSIDEFIITKENWDLIFNDSKPPDNEIGPDDSEKSGILFTLGGQKKQGWHKEWVVLKKGQLIEYADWRKGRTPINKPIEIALANVKAITHDKRQFCFEVLTSTGSKHVFQAFDNDDRNKWVKALHNAGQLINTKRLEQAHAKSLSQEGRKKTIGKLITEFKDKPIIPGQDRSISPISLTSKAPPIEKDYLQMVRSAPDSDNSICIDCGSAESVEWISINTLTCFCINCASCHRNIGSHITRIRSLKMDKFENETELLLKYINNRVVNSYLEENLPSKEKITCDVDNETRLNFIRNKYQLKKYKSIIPDIDNLLIKAIQKINVPDALKYILCGADINLNIQINIPNRNEYLVITLFEYSLRKYIEIKEEHDRELGYKPKKLFIISELLILNGCKVSQHIKDLQKEDLGLTDAAVEYWKIRSLKLSGGKAS
The following text describes a protein:
Function:
ATP-driven pump involved in endocytosis-dependent polyamine transport. Uses ATP as an energy source to transfer polyamine precursor putrescine from the endosomal compartment to the cytosol.
Subcellular Localization:
Early endosome membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Recycling endosome membrane; Multi-pass membrane protein.
Sequence:
MDKEERKIINQGQEDEMEIYGYNLSRWKLAIVSLGVICSGGFLLLLLYWMPEWRVKATCVRAAIKDCEVVLLRTTDEFKMWFCAKIRILSLETYPVSSPKSMSNKLSNGHAVCLLENPTEENRHRISKYSQTESQQIRYFTHHSVKYFWNDTIHNFDFLKGLDEGVSCTSIYEKHSAGLTKGMHAYRKLLYGVNEIAVKVPSVFKLLIKEVLNPFYIFQLFSVILWSTDEYYYYALAIVVMSIVSIVSSLYSIRKQYVMLHDMVATHSTVRVSVCRVNEEIEEIFSTDLVPGDVMVIPLNGTIMPCDAVLINGTCIVNESMLTGESVPVTKTNLPNPSVDVKGIGDELYNPETHKRHTLFCGTTVIQTRFYTGELVKAIVVRTGFSTSKGQLVRSILYPKPTDFKLYRDAYLFLLCLVAVAGIGFIYTIINSILNEVQVGVIIIESLDIITITVPPALPAAMTAGIVYAQRRLKKIGIFCISPQRINICGQLNLVCFDKTGTLTEDGLDLWGIQRVENARFLSPEENVCNEMLVKSQFVACMATCHSLTKIEGVLSGDPLDLKMFEAIGWILEEATEEETALHNRIMPTVVRPPKQLLPESTPAGNQEMELFELPAIYEIGIVRQFPFSSALQRMSVVARVLGDRKMDAYMKGAPEAIAGLCKPETVPVDFQNVLEDFTKQGFRVIALAHRKLESKLTWHKVQNISRDAIENNMDFMGLIIMQNKLKQETPAVLEDLHKANIRTVMVTGDSMLTAVSVARDCGMILPQDKVIIAEALPPKDGKVAKINWHYADSLTQCSHPSAIDPEAIPVKLVHDSLEDLQMTRYHFAMNGKSFSVILEHFQDLVPKLMLHGTVFARMAPDQKTQLIEALQNVDYFVGMCGDGANDCGALKRAHGGISLSELEASVASPFTSKTPSISCVPNLIREGRAALITSFCVFKFMALYSIIQYFSVTLLYSILSNLGDFQFLFIDLAIILVVVFTMSLNPAWKELVAQRPPSGLISGALLFSVLSQIIICIGFQSLGFFWVKQQPWYEVWHPKSDACNTTGSGFWNSSHVDNETELDEHNIQNYENTTVFFISSFQYLIVAIAFSKGKPFRQPCYKNYFFVFSVIFLYIFILFIMLYPVASVDQVLQIVCVPYQWRVTMLIIVLVNAFVSITVEESVDRWGKCCLPWALGCRKKTPKAKYMYLAQELLVDPEWPPKPQTTTEAKALVKGNGSCQIITIT
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MPVARSLGLARAVPFGASSPSNPTVTSGQNLVAFGFYPEARNAKQEVVKAIAICHRQVKILESQLMKISEEPADSEIKDMEKIQLNEQILFLTLKIVSLLTGEDYIVVRQSADDAKHRCKVCMVNGFCKHHTPPLDHSTGKERDKEILEIISNIIFLLTEEVTVRCEDVSVYFSKEEWEYLSCNKTLYKEVMQPNSPPLCLLDWENNLDSQDNLKAEYGWDDVPCQGEDMAEEDYKVETLLNSAFPPVELNLANSASHSAYKKSVSYEEGTQRSPNIVVLAFTENMQITNAAIDKACSLNTPLSEIKGKENGKMVTNKSISASPLKKHTKATYICGLCQKLFPCNRDLIRHQKYHTGEKPFSCSVCGKCYGDNTLLVRHQRIHTADRLFPCPECGKFFVDRSQLLIHQTSHTGEKRYSCAECGKWFYYASALTKHQRIHTGEKPYSCSFCGKRFNDNSILTRHERIHTGEKPFACTVCGKRYTRRSHLSEHQRSHTGETPFICSECGICFGRQSHLKAHFRIHTSQAPLS
The following text describes a protein:
Function:
Probable component of a transcriptional corepressor complex involved in salt tolerance through modulation of reactive oxygen species levels, abscisic acid-dependent stomatal closure, photosynthesis and K(+) /Na(+) homeostasis. Has an in vitro ATPase activity.
Subcellular Localization:
Nucleus.
Sequence:
MRTGAYTVHQTLTPEAASVLKQSLTLARRRGHSQVTPLHVASTLLTSSRSNLFRRACLKSNPFTALGRQMAHPSLHCRALELCFNVSLNRLPTNPNPLFQTQPSLSNALVAALKRAQAHQRRGCVEQQQSQQNQPFLAVKVELEQLVVSILDDPSVSRVMREAGLSSVSVKSNIEDDSSVVSPVFYGSSSSVGVFSSPCSPSSSENNQGGGTLSPNPSKIWHAHLTNHHSFEQNPFFHFPKGKTFTPDQAFPVREDANPVIEVLLGKKNNKKRNTVIVGDSVSLTEGVVAKLMGRIERGEVPDDLKQTHFIKFQFSQVGLNFMKKEDIEGQVRELKRKIDSFTSWGGKGVIVCLGDLDWAVWGGGNSASSSNYSAADHLVEEIGRLVYDYSNTGAKVWLLGTASYQTYMRCQMKQPPLDVHWALQAVSIPSGGLSLTLHASSSEMASQVMEMKPFRVKEEEEGAREEEEEDKLNFCGECAFNYEKEAKAFISAQHKILPPWLQPHGDNNNINQKDELSGLRKKWNRFCQALHHKKPSMTAWRAEQSSSVLPGSLMDSSLKQNSRASSSVAKFRRQNSCTIEFSFGSNRQEGLKKTDELSLDGFKSNNDEGVKTKITLALGHSPFPSDSENSEEEEPEKAIKMSKLLEKLHENIPWQKDVLPSIVEAMEESVKRSKRKDAWMLVSGNDVTAKRRLAITLTTSLFGSHENMLKINLRTSKASEACEELKNALKKKEEVVILIERVDLADAQFMNILVDRFEAGDLDGFQGKKSQIIFLLTREDDECVENEHFVIPMVLNCNKSGSGLVNNKRKPEYDAAPTMIKKKNPRIEEDDDESNVACDISNIKKEFSRQLKFESNALDLNLRVDADEDEEEEAKPATEISSGFEERFLDSIQNRFDFTVLSDEDITKFFVTKIKDSCEEILGQREERFGFTVDAELIEKFYKGCGFFANGLFEEWVKEVFQRGLVTVKNGGKEGISVINLCLGGIDMIDQGEVYEEEEGFMGTCLPNRIHVSFVD