lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the third and last glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Glc(2)Man(9)GlcNAc(2)-PP-Dol to produce Glc(3)Man(9)GlcNAc(2)-PP-Dol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSAVRPVSGISLAARYAVPFVLLLIPLWMAKVNTVVPDPYLDEVFHVPQAQAYWDHRWFHWDPKITTPPGLYIWSYILCAAALVLRGSPKELNAGALRATNVAAAAVFLPWRLQTLLDALRKVRNTRPSGAWLSHTVLNICLFPPLFFFSGLYYTDIVSLLAVIEAYNWDIKRSAGSWSLLKTAVFVATGLTALVLRQTNIFWVAIFLGGLQVVRRLRQSSKASQASSLLQIIQSGFNNELYDPLVSEASFFDYVKTSISLVSVGLRNFIPIIISTVPYLVILAAFGGFVLWNDGVVLGHKEFHTAGLHLSQMLYIWPYFMFFSWPILIFPVINLVLPNSVIPAFFDYGFTKKQKGLPRIWTALVIIPIMLAVVHFNTIIHPFTLADNRHYIFYVFRILRSHPAIRYAAVPTAYFVGGWAVISAFGFSTTKPQPQFVPITKSNELAAAQKGQLKEAARKKEKSERKSKSKKASQVTASPPAQDQFSPEVLARIQEHLAQRQKQQQEVPRASFVLVWLAATALSLVTAPLVEPRYFIIPWVMWRLHLPPQPVPLVYRQQRPRDEREALHADLATNFSLFMETYWFLAINAATGYIFLYKGFEWPQEPGKVQRFMW
The following text describes a protein:
Function:
Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Sequence:
MHHNVFTNNPTVPIDVKNRSVSELMDGMLKTGFQGRKLAESVQAWNNMLKEKNTTVFMGLSGAMVPAGMRRIISHMIRERMIDCLVSTGANLFHDCHEALGRKHYVGSHLANDEKLFEQGVDRIYDIFAVEEEFRTADNLIADFAQEIGEITCSSREFMYLLGKELGRRGAAEDSIVVSAYRHNVPIFVPALSDSSIGIGLTIARRRGLKLEIDQIKDVDEITQIVEKSERTGVVYVGGGVPKNFIQQTEVIASILGMDIGGHDYAIQYTSDSPHWGGLSGCTFDEAVSWGKIAPQAKKVQVFVDATIALPIVAHALHEKTHDLKRIAPVFFWDGPEGLAIDYKE
The following text describes a protein:
Function:
Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
Sequence:
MAAKIAGNLEGCNVSIIVQQLQGAYERGQLKNALYQYWAQQVPKIFFTSAEVAISTQRTPDAVQAEEKLSRDVLFEPLEWFLCGGNPAAVFQQLQSLNNPPQLCGKVFKVGEPTYSCRDCCADPTCVFCIECFNKSTHKTHRYRMSTSGGGGYCDCGDVEAWKQDPWCDIHKQGLGQQSQNPIEKLPPDVAARAWEVLKIALQYAVDMLLWEQMGGLPQDLEPSVSQNTYVTMLFNDEIHTYEQVINALTKAINCESKEAVEFATVVDREGRSSVRYGNRKSCDEARTVIQKSTSSVRSKPLKVEVMHTSVCAHQAFAQKVLNWLGQVVNHSDGLRHILCTTALQQPPTGDPCVVERLMLADTALWKTARVQCHQIMMGSLLMDQESKKQFSVLYTRNYPQVQKDFMADDHDHGVSIISLSVQIFTVPTLARYLIMEHDLLAIVIRTFLDQCASCRHGRYLLDREKLQKNFRRLQFPLLDLKYVLSMVPDQWNDQLKRKFLNGFKIMVELLTSMQGMDSVTRQVGQHIEMEPEWESAFNLQIKLAPAVAMMAGWCATDKMVLIDAFRIVVKALLEIRCLQTQSRCARGEADPLHFDKDNIKIKKCPEYSFCDQEAIVVDYTVSREPVSIHLPICRLLAGLYLQLGKHGLTFNSPELYGPLDWTSPQARLSRASEIAHRASACPTPLVLARSQPPSAMDLLEQPLRTLVMIAQVHAEMWKRNGYSLFHQVYYYHNVRCRAEMQDKDIIMLQVACAQMDPNQFLIALLNKFELMNWIEGDFDDFIRLFFYGRRRDVTEKGSSATDVSAESTRDLLRFTNSLVEEFLTFLIIITGERYVPGIGQVSSEDMVRREVIHQLCISPMAHSELSKALPENNNYETGLEGVVHSVASFKKPGVTGMGRYELKPEFYKDYNPFFYHYTRADQSKSEEAQLKRKKQEGESTACPPPELPALSKEFSSLVNVLECDVFVHTIRMVLRRVNSSRSRSWTEAMVHRALHLVGMALNEEKRLYQTSPYIRFNFVKKATEGGSNSLYSALHDLLGKPRIQNHADLLTWVIDRFDEVKDLKDQKQGASDAQKAKKVSSKSKTDAERKKKAEAARKRREKILAQMSDMQKSFIRDNLELFEATGTELSSSPSMEVEGSPMVVPSQYPVAVGPDRSPATHVTLTTSTCILCQEDQEVAAGNKCVVLAAYVQRSTALSKSRGKVLEDPDKYDPLLVSPDLYHGVHTSTCGHVMHADCWQRFYEAIVAREQRRALRFRHILSYEVDRGEFLCPLCETLSNTVIPILPPSATIQPDSVSADISLSFSDWLDGLKKTVEASQQAMMKEEEDKMESSDDMPVLSPCPLPSITKNMAEMAAQGFQQLFEYMTETGARAPYSDSVKEMMKLFSRATYTNMLHDPPLPTKFGLGLDPNDDDDRVPITAWGTCAYTIRTLEWLLRDQGKPLFGSLSSRQADCITALVRVVTVSGSLSDPQTISKSALRLLSALLPQEPMKNIPCILDLDMFFTLVFLHVTISSLYCDENTAAGGTIRGVALNDKHLMHLVTAAHLVQILLAANFTSADTPMDTEETAEGSAWVKLFMAVRKEAGVQTPVVPSGWQLQTYVRESVLPFLRCSALFFHCHTGVQSPAQLQESGVSEFEPLCQYLALPADLSSLLLQNSGADVGHSVPHTIHSKWCRYPGIKESLASGPASLVKYPVEVNRLVPLPHDYSDVINRGSVFTCPMSDGDDSRAPTMCLVCEQMLCSQSYCCQTDLEGDLWGPAPHTSTPVAHVGVHVGWGYSSGGCTCGAGVGIFLRWVHMWGWGGYTCGAGVGIFLRVRECQILLLTGKTKGCFYPSPYLDDYGEHDQGLRRGNPLYLCQERYRKLQKLWLSHSIPEEVVHFMEANASFATIEWQHL
The following text describes a protein:
Function:
Inhibitor of fungal polygalacturonase. Regulates floral organ number.
Subcellular Localization:
Secreted, cell wall.
Sequence:
MASTASFMLAVLLAVAVAAAPARAVRCPPSDKQALMRVKQSLGNPATLSTWSLASADCCEWDHVRCDEAGRVNNVFIDGANDVRGQIPSAVAGLTALMSLSLFRLPGLSGPIPACLTALSNLQFLTISHTNVSGVIPDSLARIRSLDSVDLSHNSLTGPIPNSFSDLPNLRSLDLRSNKLTGCIPAGLVQGQFRSLILSYNQLTGPIPRDDAQDEINTVDLSHNRLTGDASFLFAAGRPIGKVDLSWNDLDFDLSKLVFPPELTYLDLSHNRIRGTVPRSLAALSTLQTLDLSYNRLCGPLPRLHGVIRHGCKPYEHNQCAGGAPLGGCHQS
The following text describes a protein:
Function:
Plays a role in determining ER morphology.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
The C4-type zinc finger motif is necessary both for its ER three-way tubular junction localization and formation.
Sequence:
MGIFSFLRSSTQPTPDLFEKELVELELKIQKHQDRLKAIDQRQRSTTSTITIYSSLFWAIYSSLWYLGWTPIKWTNLNSKLLSPDSKTLLLLSTNPKFNQALQVLPIILIPIGLISLRWLVQTWYQRKQESEKLRLRLLQKQLRDKVEELKKKTAYYSTKELLDRYDEKTKLNPQSSPSNPHQLGRMTMTPPNNEALRHRQRPPSSSPANLSSTLSPIQNNHPSPAYQTGPPSTGATSSAAHQQLHQKMSNSPSPSIGRGWADRFAEVLLGDDEARPESKYALICINCFAHNGLVRQEELDHIQYLCPKCGTFNPSKSKGIHQKHPSGTEAQTENSQGKRAGRKSLADSMIRRKPPIDDLFNVTDSRRVVSSVVGVPSTSTSSLSLDQASPHPAGSNGAVMDDQEGQRSDQEPDRPDSSLAQLPRDNEEDQVLELEHPITPPDIPSESSKDRKLKKKSSGQKAKQPK
The following text describes a protein:
Function:
Acts as an opponent to RZF1 during early seedling growth in term of proline accumulation in response to dehydration and abscisic acid (ABA). Confers sensitivity to abiotic stresses such as ABA, drought and osmotic stress (e.g. mannitol treatment) by preventing proline accumulation and by reducing the expression of dehydration-inducible genes. Promotes the production of lipid peroxidation by drought stress thus leading to malondialdehyde (MDA) synthesis. Prevents pollen tube elongation. Necessary for RZF1 expression in seedlings.
Subcellular Localization:
Cytoplasm.
Sequence:
MNEEERVGSSSSSSSSLPVSYGVDCEKYDFSSSVSSLSQPFSPEGSSNKSHVLENNLSFVFSLDHNSNSSLMFPRDRPCSCLHHVFEWILQRCCGCLC
The following text describes a protein:
Function:
Histone methyltransferase that monomethylates 'Lys-5', 'Lys-8' and 'Lys-12' of histone H4 (H4K5me1, H4K8me1 and H4K12me1, respectively), thereby controlling gene expression and remodeling chromatin structures.
Subcellular Localization:
Nucleus. Chromosome. Cytoplasm.
Sequence:
MVAPSETQIVQAVKAKLESGLTSTSDVVREDEVRRLLATLELEHDWQDIAVKKFISILCKHSLMPVSKPNDGCTSRSTSCPGGKKKKKSKTDTSIPKSFIDPTISFPAGIRGVYFDPVKGKGLVATRSFSKGDLLFTEDAYIPTPPPEAFDQMASGQLCAQCFLPISSAPVALAIKNCSKCKHRFCTTACYKTAMATHHTLLCTGINASAKPLIELIERQKWQSLHCVARSLARLLMTLTRQYHGQANKKADTQDSVATYGDFETVYARLSSFATVSELERRSRNPGWTTEKASFESILVEAHTALCNALDPYSSTRNANLEPFHVSADYLDSTRKPLIKDLFCLATFMKLVGRANINMEKFGGLYSLHSFLNHSCSPNLEIRHVPERAILSSMKVAAIALCDIHPDDELVISYIDPNTSLARRQLLLYRDYCFGPCTCDKCTTQLGALGLVYDPAKHAVKAFLDSVAHKTRPDPDHTLPPTSQDSTLEDQLRASLGF
The following text describes a protein:
Function:
Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation.
Sequence:
MVDTTKNTKLFTSYGVTTSKAINPDMAAKMISKAKRPLFVVGTGVLRPEILDRAVKIAKKANLPIAATGSSLNGFLDKDVDAKYINVHQLGFYLTDPAWPGLDGKGNYDTIIILEFKKYYINQVLSGTKNFSKVKSISIGKDYIQNATMSFGNISREEHFAALDELIDLL
The following text describes a protein:
Function:
Putative transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MMDHLSLVPYEGGSGAGGDAGAKYKECMRNHAAAMGGQAFDGCGEYMPASPDSLKCAACGCHRSFHRRAGSLAGGACPAPFFFSPPPPPPPHHHPPPHHPVLQGFLPSAPPRPPQLALPYHAVPAAWHHALLDPARAGSETPPRADDCSPGCGSGSFSRKRHRTKFTPEQKERMRAFAEKQGWRINRDDGGALERFCLEIGVKRNVLKVWMHNHKHQLASPTSTAAGMGMGMGMGIGINPGVLGTGTGTGAGAGAGVGVGAGTGDGDGDDDDTDDDSPPRAAVSSPSPSPISV
The following text describes a protein:
Function:
Secreted effector that translocates into the nuclei of host cells to reprogram the expression of immunity-associated genes by binding to effector binding elements (EBEs) in rice. Binds the 5'-CCACCTCC-3' EBE of promoters from targeted rice genes and probably recruits a yet to be determined host repressor. Causes ambivalent immunity with increased susceptibility to the hemibiotrophic pathogens Magnaporthe oryzae and Xanthomonas oryzae pv. oryzae, but enhances resistance to Cochliobolus miyabeanus, a necrotrophic pathogen.
Subcellular Localization:
Secreted. Host nucleus. Note=Secreted via the biotrophic interfacial complex (BIC) and translocated into the nuclei of initially penetrated and surrounding cells.
Sequence:
MHLKASSILALLVIGANAYPASANSAAALVPEPQQPEAPAVAGSTVGAQVDIHHPRLEARYGRDEPQIMCGYCGKRFWNKPDLEKHIKLKPSKGGHKGQPYKEHSWNRPT
The following text describes a protein:
Function:
Endonuclease that probably plays a role in the DNA damage response and DNA repair.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MCSEARLARRAVEELLRCGADPNLVLEDGAAAVHLAAGARHPRGLRCLGALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQQGHLECARVLQDLDTRTRTRTRIGAETQEPEPAPGTPGLSGPTDETLDSIALQKQPCRGDNRDIGLEADPGPPSLPVPLETVDKHGSSASPPGHWDYSSDASFVTAVEVSGAEDPASDTPPWAGSLPPTRQGLLHVVHANQRVPRSQGTEAELNARLQALTLTPPNAAGFQSSPSSMPLLDRSPAHSPPRTPTPGASDCHCLWEHQTSIDSDMATLWLTEDEASSTGGREPVGPCRHLPVSTVSDLELLKGLRALGPEFSGHSLELAAALRTGCIPDVQADEDALAQQFEQPDPARRWREGVVKSSFTYLLLDPRETQDLPARAFSLTPAERLQTFIRAIFYVGKGTRARPYVHLWEALGHHGRSRKQPHQACPKVRQILDIWASGCGVVSLHCFQHVVAVEAYTREACIVEALGIQTLTNQKQGHCYGVVAGWPPARRRRLGVHLLHRALLVFLAEGERQLHPQDIQARG
The following text describes a protein:
Function:
Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays a critical role in the assembly of N-DRC and also stabilizes the assembly of multiple inner dynein arms and radial spokes. Coassembles with DRC1 to form a central scaffold needed for assembly of the N-DRC and its attachment to the outer doublet microtubules.
Subcellular Localization:
Cytoplasm, cytoskeleton, flagellum axoneme. Cytoplasm, cytoskeleton, flagellum basal body.
Sequence:
MAEILARLTRVSENYLQELEEEPEPQGPPKLTKAQKKAAKKEAKRLAMIEEKRLIMRDALMRELEMGKHMEEKGNEEWHEMCREIKIKELNEEMRAWGERSERNIQAKNDHIKMLLDDMAQTQDQHVRCYSKTVELIDHIRDCFHVMLGGVKSMYDQQADEMLRDYYEEVRRRTEEVEAMKTNSENIIHATNITTRDQLKEDYTIYLEQRDDRVNTEIENRFKIRDQIVRRMTHMQQQLNDFVESLRSTELDAHKYEKIHWLTERQAAFMEESRKLNAEESKYINMQAELQREMVRMDAENNSTLNDLRLEFQYFTNVRKKIELNQEMDREITHEKLRILTGECYELTKQMEKHVKSGELLLALSITCRKLQTESEKVILGGEVFDETEVDVDEYFKLQTLNLKDHVDMTEEELVELNKSLRNFWRRQAMAEAQNLLMLEEKRRLTEDNQRLIDFIKSMSVTEDPEELRTAMHVSSPTQPMPPKLFETKCQEFKSRKVVHSPTAHKEAKWEAEATLNEVILDF
The following text describes a protein:
Function:
Required for correct translation termination and probably involved in regulation of hypoxic gene expression.
Subcellular Localization:
Nucleus.
Sequence:
MTKRPLGLGKKNKQKRHKPDEGADGKKESTPLDQIHVEVEGGGDPEDSVVQLKALWRNYLQSEREDERVLNGIVHECDRLLRNREQEGIELGEDFHSIYALALSELAIFRTEEKGQAGRESVGEFFDAAAERVDMGLQHFPASDVLALAKAKIIFQRIPLQYVSQLSPNNSEGADVGLQQLLEEGKSSFRVVAQDPLAVSEPLEIFSDLLEIIANFGREDEIDEGLDSDAEDEPEEVELPESHPLYELRQHLPEHAEWLQQQLLALFKVLEKPNAEEEESEATKFYRKIANKLGQSYLDAAAEPSIVFTTLTYETEDPSAEDEQKAQEAQRVAQGLTERAIEFFKEAESADDPQTWVDTAEVFISLGNLQENESETQEMLYKQAEEKMVRANKATNGKYKHILDTLLDSKT
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular Localization:
Mitochondrion.
Sequence:
MAALTPSRSVFASTCKTIAQQCSRRPVAVQQLAAVPVARQVSSSSAVQQEQDASGTSSSQQPRPRWSYTPERMKGPGFSLNLVKDPRRKQWMVNSDPAKLDAFYDAFLGQGGSRMLSEETKWLAVTHKSFDYGRRGYNTRLAFLGRQIIALETTRSILTSPVLNEPIVDKYGRTPYNHAALANIDKLIYTQPLDIMDKTKIARMGIDFGLLTVMRWKPRMPEDLESSGVVVVLNSTLFAIIGAISLEKGAAVAQRIVREKILKRLGA
The following text describes a protein:
Function:
Probable adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases.
Sequence:
MTRRENVSLYRPIEVTCYPFMYMQTPQPPQPTDKVVFPAYVLDELTKQNPDFQAPILFEVSNKSQTFKKRIVCGVESFSSPDFTYFPQWILDYLHIQPGDVATIFKVLIPKGKSVTFKPLQSTFYNIEDPKKTLESILRNYMTLTLNTTITFQMNTIIDGMNIATDVSVLISDVQPFSSIYIRETELVVEFEENLEISPKYNKPQPIEEEKSEEDEDIDFKFTPVIQQPVEQHMADSSDFKPFEGEGSRLGRSRDMEQNDYTDTELCPYCNGHIKKANFKIHELRCRKMYKVCPFCGKKLLINSEESQKHLDLHVQVKCIQCGEEIERQYLKEHMNNVCPKRLIKCEYCSLMFPANQIQQHKNYCGNTIEECDLCGAKVSLKQMQYHKENDCAFAPRNIQREQETIENFGLETSQEGCFECPMCMNHFTNQVDLDTHMLCFHPELYD
The following text describes a protein:
Function:
Cilium-specific protein required to control the microtubule-based, ciliary axoneme structure. Required for normal sensory cilium function. May act by maintaining the association between IFT subcomplexes A and B.
Subcellular Localization:
Cell projection, cilium membrane; Lipid-anchor. Note=Associates to the cilium membrane via palmitoylation. Localizes to proximal ciliary membranes, to an inversin-like subciliary membrane compartment, excluding the transition zone.
Domain:
The RVVP region and palmitoylation sites are required for compartmentalization inside cilium to prevent distal cilium and nuclear targeting.
Sequence:
MTEKSWFETIFCCCCHRTPIIRREIKLGCFGIGSAGKTTFLKVLKGEDPRDLLRTNGFSTVKMEYDETFHLTIYDVGGDKGIRGIWSNYYAEVHGIIYVIDYSTDETFTESIEALHSLTSNPHVQKKPIFLLLNNQNNREFDDVEISNETKIQAGQHKIVLFSHFNKYNGYLDNIKSATLTVMARAKKDRNEYQEQFVRFIDSISEHYVELSEGVKTAELALRIRQEEAKEQRRLMQMKVEHDALKADVAGLELRNQPPVQPPIPPDPPSDPKSASVHIEESPPMSLASSTIPSDIIQSTPETGTPRDPVNFCRISQTSTKPVSPESNSVKEEPTIILKDNYFLPPKAPGRQYSRIQRIQNVLNNRVVPK
The following text describes a protein:
Function:
Functions as a modulator of calcium-binding by calmodulin. Thereby, regulates calmodulin activity and the different processes it controls. For instance, may play a role in neuronal differentiation through activation of calmodulin-dependent kinase signaling pathways.
Domain:
Mostly intrinsically disordered, with residual structure localized to the IQ domain which mediates the interaction with calmodulin.
Sequence:
MSERQSAGATNGKDKTSGDNDGQKKVQEEFDIDMDAPETERAAVAIQSQFRKFQKKKAGSQS
The following text describes a protein:
Function:
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Domain:
Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
Sequence:
MASSGSLPSLARQCRDRLNDGRGRIESRFRAGLPSVQTATALTDLYDDVIEKIWQDSLERASSSVKASQLSQLSLVAHGGYGRRDLSPYSDADLMLLTTRRSAAAAAQVASTFVRDITDAGIDCGFSVRTPRECCTLAWADAKIYTSLTESRLCFGNEQTFDRYFDRFRAGARRRRNYLNHQSLMARREERHKWGETNYLLRPNVKRSRGGLRDIQLVRWLGFATHGATSLEQLNKLNALSDEDYGTLRRAHAFMLRLRHELHFRTKRAQDVLDRPTQLDIAEDWGYQGRSGVLPVEDFMQDYFEHTRGVRYVAAYFHDDTRIRSRAAGAVESVMSRRIDENIRMGPTHIWVKSNTLEQFAQSLPDVLRLIQLANHHSRRIAHPTWQAIRKSMQDREATPPDQPAVDAFLELLKDPGRLASLLRRLHELRILDQLIPAMGRCRGLLQFNAYHKYTVDAHCIRAVEAATDFIDAENAMGRRYRRLKDKGLLHLALLIHDLGKGYEEDHSEVGRRIAGDVADLFHLSADDKDTLQWLIHKHLLVNEVAFRHDLNDPEVVHKFAAEVGSISRLELLLIHTVADLQAVGPDVLNDWKMGLIEDLYLRARRYFETGNLPGENEADLDSKIEQVKESLAEKKLDPSLIEFAKDMPLSLLRQHSTDDLIHEMHQVGEWLTHNPGCYCAGAVDPAASAVRYTIVLRQGERRVGVFARITAAFSACGLSIMRANVETVGEDLLWDQFWVNDPELKQRQPESRIEEVCRVVTKALDDPDSVMPTPRRVWQTQGAKEPSSVLLLPTKVLFDNDTFDHQTILSMFTYDRPSLLSDISGTLSQLDVVIQFAKIDTHLDQIADVFYVTNPDGSPITDSDRQETIRNALVDAVRKPLP
The following text describes a protein:
Function:
Lacks intrinsic GTPase activity. Has a low affinity for GDP, and constitutively binds GTP. Controls rearrangements of the actin cytoskeleton. Induces the Rac-dependent neuritic process formation in part by disruption of the cortical actin filaments. Causes the formation of many neuritic processes from the cell body with disruption of the cortical actin filaments.
Subcellular Localization:
Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm, cytoskeleton.
Sequence:
MKERRTPQPAVARCKLVLVGDVQGGKTAMLQVLAKDCYPETYVPTVFENYTACLESEEQRVELSLWDTSGSPYYDNVRPLCYSDSDAVLLCFDVSRPETLDSALKKWKTEILDYCPSTRVLLVGCKTDLRTDLSTLMELSHQKQAPISYEQGCAVAKQLGAEIYLECSAFTSEKSVHSVFRTASLVCLNKGSPLPPKSPTRSLSKRLLHLPSRAELISSAFKKEKAKSCSVM
The following text describes a protein:
Function:
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Subcellular Localization:
Cytoplasm.
Sequence:
MGSPFILLNYKTYNQGTGQGAVEIARACRAVSEESGIEIAVAPQLPDIYRVASEVELPIFSQHMDGVGAGSFTGHVFGKCIKEAGAVGTLINHSERRLTLAEIEASLKAAKEFGLRAVICTNNVPTTAAAAALEPDYVAIEPPELIGSGIPVSKADPEVVSGSVEAVAKINSGVKVLCGAGISKGEDLRAALDLGSQGVLLASGIVKAADPKAALEDLIRLV
The following text describes a protein:
Function:
Malonate--CoA ligase that catalyzes the formation of malonyl-CoA directly from malonate and CoA. May be required for the detoxification of malonate.
Miscellaneous:
MISCELLANEOUS: Plants overexpressing AAE13 show increased sensitivity to exogenous malonate.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MTATTTLKSFNYLSLINHRLNHNSYAILSSPLLPRSHPASTSFSNSGFRFFQSNHLFSSQSGSLMEVFKAAFSEASNSCDRIAIKADGKSYSYGQLTSSALRISKLFLKDDTTNGGQETKKYEGFGSLKGARIGIVAKPSAEFVAGVLGTWFSGGVAVPLALSYPEAELLHVMNDSDISLLLSTEDHSETMKTIAAKSGARFHLIPPVVNSTSETVACNQFQDDSFEAEGKFLDDPALIVYTSGTTGKPKGVVHTHNSINSQVRMLTEAWEYTSADHFLHCLPLHHVHGLFNALFAPLYARSLVEFLPKFSVSGIWRRWRESYPVNDEKTNDSITVFTGVPTMYTRLIQGYEAMDKEMQDSSAFAARKLRLMMSGSSALPRPVMHQWESITGHRLLERYGMTEFVMAMSNPLRGARNAGTVGKPLPGVEAKIKEDENDANGVGEICVKSPSLFKEYWNLPEVTKESFTEDGYFKTGDAGRVDEDGYYVILGRNSADIMKVGGYKLSALEIESTLLEHPTVAECCVLGLTDNDYGEAVTAIIIAESAAKKRREDESKPVITLEELCGWAKDKLAPYKLPTRLLIWESLPRNAMGKVNKKELKKSLENQE
The following text describes a protein:
Function:
Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2.
Miscellaneous:
MISCELLANEOUS: Present with 2010 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
The DPH-type metal-binding (MB) domain can bind either zinc or iron ions.
Sequence:
MSLVNSLTHYEILRIPSDATQDEIKKAYRNRLLNTHPDKLSKSIHDTVSNVTINKIQDAYKILSNIKTRREYDRLILENYKRQGFHNCGDGLDEFSLDDFSFDEDKLEFMMNCPRCQFVGGFHFSESLLDECIDNVDAMERSHSGYQLLTQCSACSLWLKVNFDIEEEQEGQ
The following text describes a protein:
Function:
Component of the epg-6/atg-2 complex, which is involved in the generation of autophagosomes from omegasomes and in the distribution of atg-9 and atg-13 during the autophagy-mediated degradation of protein aggregates. Binds to phosphatidylinositols on preautophagosomes, which are early autophagic structures, to promote autophagosome formation. In particular, binds with high affinity to phosphatidylinositols including phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 5-phosphate (PtdIns(5)P), but more weakly to phosphatidylinositol 4-phosphate (PtdIns(4)P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Involved in autophagy-mediated degradation of ribosomal RNA and ribosomal proteins in lysosomes, which is essential for maintaining nucleotide homeostasis.
Subcellular Localization:
Cytoplasm. Preautophagosomal structure membrane; Peripheral membrane protein. Note=Localizes to the cytoplasm of all cells during embryogenesis.
Domain:
The LRRG motif is required for recruitment to phosphatidylinositols including phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 5-phosphate (PtdIns(5)P), phosphatidylinositol 4-phosphate (PtdIns(4)P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
Sequence:
MSKKEETIFFRIEKENRPESSKKEEDENSTEEMTTLNHASVTLDHSAFAIADKDGFKMYQLNPLHFRMYKDYVIKVGPVRLVKQDGNSRRIIYVSALAGGRFAQNNLMIFDVARNEEYFEITTPSRYGPITNIHVSPNRLVALNPNRMFVWTYPDDIKQIRSEDIRSNPKGISAMSYDPTTAACYLAYPGFKTGSVQIMHLNALTARESKSPIVIEAHLTDIAQVALNCQGTLVATGSTKGTVIRVFDARTKGPLYELRRGTVQAHLQCMAFSPCSSYLAVASDKGTLHMFGIRDAEPQKKKNVLERSRGSSSIVKIQLDRPVMAIGFGKIPETPKNLQSIIAICADATYWRHEFYKDNTGNFTSHFGSYDELIEVANDSSFFRTPVE
The following text describes a protein:
Function:
Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
Subcellular Localization:
Cytoplasm.
Domain:
IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)).
Sequence:
MSDYKFTLNLPETEFPMRGNLANREPEMLERWTKDGLYQQIRDSRIGRTPFILHDGPPYANGSIHIGHSVNKILKDIIVKSKTMSGFDAPYVPGWDCHGLPIELKVEQKVGKPGQKISAAEFREECRKYAAEQVDGQREDFIRLGVLGDWQNPYLTMDFATEANIVRSLSKVIENGHLHKGVKPVHWCTDCGSALAEAEVEYEDKTSPAIDVAFTAVDSKAVAVKFGVSDYSHSVSMVIWTTTPWTLPANRALSISPELDYSLVEFVKDGVTHAVILADVLVEACMTRYGAESHSVLAKIKGAALELVRFKHPFLAFDVPAILGDHVTTDAGTGVVHTAPGHGQDDFVVGQKYGLEVANPVGDNGVYKPDTEFFAGQHVFKANDNVVALLKEKGALLHHVAYRHSYPHCWRHKTPIIFRATPQWFISMDNHNLRKQALSEIEQIQWIPDWGQSRIEKMVENRPDWCISRQRTWGVPITLFVHRETEELHPDSVSLMARVANRIEQEGIQAWWDLDAAELLGEEAEQYRKVTDTLDVWYDSGSTFASVVAARPEFHGHGVDLYLEGSDQHRGWFMSSLMISTAMTGKAPYKQVLTHGFTVDGKGRKMSKSIGNVIAPQQVTNKLGADILRLWVAATDYSGEMTVSDEILNRSADAYRRIRNTARFLLANLNGFDPKNDLVAVEDMVALDRWAVRRAAALQQEIIEAYEQYNFHIVTQKLMQFCSIELGSFYLDIIKDRQYTAKQEGHARRSCQSALFHIAEAMVRWIAPVLSFTADEVWQLLPGQRDAYVFTQEWYQGLQSITLDTDLSDAYWENLLTVRNEVNKVIEQARRDKRVGGSLEAEVTLFADATLTEQLTHIGDELRFVLLTSEAKVLPLVDATSDAVETELASLKLVVNATTAEKCERCWHHREEVGTIEAHPTLCHRCVTNIEGDGEVRLFA
The following text describes a protein:
Function:
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Sequence:
MLRSGIFSQAVKEELEAIDDSWKQPRFDSLTHVVEVLTSHNPEDATQTLREQRDAIEALVDDVVRGYHKGFNKAIHNYSQILRLFSESATGLSGLKLQLADCKKLLGARHKQLQQQWYRSVILRNVISLLDQIDNVSKATKIEQYISEKRYYSAVQLHIQSISMLEREGIQGVGALQDVRAEFSNMKGVLFFKVVEDLHSHLYCKGEYSTSVIRDKNADDDLLNIDTMVLPAGSSHPFSRRTRTFKKSENGGDGSANGHVEDRRNSSDKSSISADSKDEELSQDESVGKESMKPKRATLVWLGDATPNEFVEAITKSDATLNVKYLQTMVECLNLLGKTAAAGALISQRLRQTVHDLIIEEIKAHAVAVDASRPRVEVSKISVSHKNGVLTLGLKKVQDSKHAKKVRASSEALTSIGPTGPGQTAARNLVEPVLAMLARVLANHVIVGKAMESHTGDDDTHSVSGYNIGFAVTVIQSECQQFICDILRANADATQTDSSGQAARQSKVTAADKSNAGPDEGLSFTFRFTDAMSLPAVPRPVRRRGSANAQEGFGVSTVLSDRGMYLIASLYRPVLEFTDGFTSLLPEKYASLGKEGLHNFLETFIKDQFLPRIYVDYRTRAADALASSAAFRLKTRSSVTKMSSIALLGPSVADQLASEVVAWAHAMPKYAPEFLELVQTILERTLERCRAAYTEAVLGSLSSSIIGRTDVEQLMQQDPASVLLEADCPDHYPNGEDVELEMEMNNLLLSLRPIKHDQLIHGDQKFVLLAALSESLSSLATSIQNLGSQQKKNDMASKRPSNILPSGLHSLIAKYQDLSSECLRTLRIEMQLQAIHYLQSMTGRVYVSDHDAEEPEDFIVSFTSQITRWDEEMTFYISSAKRNYAFGGICGVAATAFVKALNDMSLVNVFGVRQICRNCIAFQQALAALSSTDADMVQQRLDRVRTYYELLTMPFEALIAFVNEHDSEFSFTEVSNLLKVNVPGREIPPDAVQRIGKVLAP