lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Atypical bHLH transcription factor that acts as a negative regulator of a variety of shade avoidance syndrome (SAS) responses, including seedling elongation and photosynthetic pigment accumulation. Acts as a direct transcriptional repressor of two auxin-responsive genes, SAUR15 and SAUR68. May function in integrating shade and hormone transcriptional networks in response to light and auxin changes.
Miscellaneous:
MISCELLANEOUS: Plants overexpressing PAR1 are dwarf with compact rosettes and inflorescences, epinastic leaves, shorter flowering stems and siliques and a general dark-green phenotype. Plants silencing PAR1 exhibit a slight increase in the length of hypocotyls, cotyledons and primary leaves.
Subcellular Localization:
Nucleus.
Sequence:
MEETLATPDATRRSLSPSCSATVKSRAAGFERRTKRRLSETNASVREDREEAEEEEDEVKEKIEALQRIIPGGAALGVDALFEETAGYILSLQCQIKTIKVLTSFLQRIDQEDMKFGG
The following text describes a protein:
Function:
May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Sequence:
MEEATEPGLCYRDKSKVVHEGLARFFNRETFSDLTVVDPDGNRIRCHQLVLSSCSRKFADMLEQGKVEELPVRGVDAQGLYLVLRFFYTGECHVDHTSVIAVYDAANRLDVDGLATACDVYSKQLLGPGTACTLFQQAQRFALQEFAESCSRIIRVRFDEVVHSEDFLTVDRPTLMKILEDNIPHHNEGSIFRAAWRWGMSSLARMQEMPKVFKMVKVPNLSMQDLVNIAGPLPGPAPQLVRNRGASNPTATGHTAAGSQFQQASARAPDTLEVLSPAKLREAQSYLIQQMLGGMDLVRAVRSTVQMYGSGDGEPPAPPAAPAPCLQLGSHTLPPHRISGGVPGHCNGGGMPSAHYHQNQCFPAPQHQPARYHRVTNNLDSMPSHPATAPAMPGTAAAAWNHLHHNQHHQHESPEMANSCAASGGHDVEDDVQHQPRVPAGYQQASRGAHGGAGAAGRRGDGQQGTVFGGTGGERPSGTAVSGTAGSGGDQDDAVSGARHAAAGGHGRGKDRDGDQSGVQHQVMEALRKLNPDLQGQAIVVVVNPTGSPPPAAAPPAAIVRHGSGVRVMCQVDKCNQAMACQQEQYQRLRICEHHYHALEVQHEGMRQRFCQSCGRLHPVEEFESNMHACRARCGVDSRQRKRLRPDEHADTAECRPAPGMHGRVAMPQQMPRHGAHQVAHHVAHQVAHQVAHQVVQGVMLPASQPPQVPTWDWAMQSDQQRMHAGVPAVEHGQCQDLAAGTPSSTGSAGNAPQKHSGQMALPPLPQPHLPQQGQRGGMLPPQQFHQQQQQPNLASYPSVPPPRRPQMQPTDQPLHRVSSVPAQFQGGESNQHCMQPPAPQQPQNAPVRHLSLSGLPTGAPGSMPLHPNQRVRPSNPTPQLQMQQAPDLPRQYSAPPQQGQVVVQLQPATGAQGEDKLVAFGAPAAGGMAKLILSTVPLDAPAGNAGAGGAQGLMHAPSSRPAGPQQPGQLQAPLRRPSPGVVRPGGTDSHVSTSRGALPQQGGAPALRQSLASGPGRPMAPHHGMQSVNPGGRPGAPQRTTMPPPSSAPAQRQSAPRLAEGRAPSLNLRPSAEATGARVNAVPSQQLMQQLPPPPQQAPTQASAQAGAPMWPAPQQGLPQAAQQHAFIQQQQVQQAQQVQVPQAQRPLEQQQQQQQLPEQQAQPPQEGSLNQDAFCGQAALASEYPQLQSMPMHMDSTEYAYGEQACNGGAPQTADPSPPQPPQPPPPPPPGWQQLPPDQNALYGQGELQYHQPQMQPLFHDGAMQAAGSAAAGNSAVGGAAGEEPTTPRHAGIRAPQVAVMGGGGMAAALAATISGNAAVSSFDNRLGLPRDLRVSINGNYSFGDLHELVTPGSHGLLDSGLVSPNTELFNILNTGNGAEDTLGMGPMLDLLGPGESMYDDTANTSQALLPGPSGAGTAGPSVPPTLPLPPQQ
The following text describes a protein:
Function:
Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the elongation of long chain acyl-ACP substrates by the addition of two carbons from malonyl-ACP to an acyl acceptor. Involved in the initial extension of the mycolate chain and forms monounsaturated fatty acids that averaged 40 carbons in length.
Miscellaneous:
MISCELLANEOUS: Identified as a drug target. Inhibited by isoniazid (INH), thiolactomycin (TLM) and related analogs. Highly sensitive to cerulenin. Is the biological target of GSK3011724A, an indazole sulfonamide. Inhibited by the indazole JSF-3285, which is a promising preclinical candidate for tuberculosis.
Subcellular Localization:
Cytoplasm.
Domain:
Phe-404 residue probably plays a key role in the activation of the enzyme at the beginning of the catalytic cycle. A conformational change of Phe-404, possibly triggered by the substrate, is central for the activation because it switches KasA to the sufficiently reactive zwitterionic state.
Sequence:
MSQPSTANGGFPSVVVTAVTATTSISPDIESTWKGLLAGESGIHALEDEFVTKWDLAVKIGGHLKDPVDSHMGRLDMRRMSYVQRMGKLLGGQLWESAGSPEVDPDRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSACSSGSEAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTRNDEPERASRPFDKDRDGFVFGEAGALMLIETEEHAKARGAKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIRVAGCDQAAVYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPRYGDYRYAVNNSFGFGGHNVALAFGRY
The following text describes a protein:
Function:
Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. May participate to the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MAFQEFTSTAVQLFDKWMESSDPRTKGWLLMSNPIPQMLIIVFYIYFVISLGPKIMENRKPFDLKRVLIVYNIFVVSLSVYMCYEFLMAGWGTGYTFGCDLVDYSQSPKAMRMASVCWLYYFSKFIVMLDTVFFVLRKKPKQITFLHVFHHSIMPFTWWFGVRFSPGGLGTFHALLNCIVHVIMYTYYLLSALGPSFQRFLWWKKHLTSLQLIQFVLVTVHISQYFFMKDCPYPYPLFMYIIALYGIIFLLLFLNFWHHAYTKGKRLPKILQKTISPKNNNDIHHKKE
The following text describes a protein:
Function:
May be a cell surface adhesion protein.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MVRERFQNVKLWVVTVLLACGAVEMSAAAEFDISEILSDFPDFSLLNQLLTKTKVAAEINAQTGITLFAPSNHVLSAFQADVPNANDDFMGDLLRHHVAMQFFDMPGLQALQTNLSVASLLQSAPGGRAKDDVVLIANMPPSVLLDNSVETRVVINITQVVSEISIIQVDQVLRPATFPSLTPVSSTTEPPTDITATLDSFGDFSLFSSFLKQTGVDTIFEGRQSTAEGITVFAPTDDAFNLLPGQWFQNFSDDEQRLFMEYHALDRFYDLGDLWEFKHLPVNTVATTLDKPGSFLLHINSTAGVVNVAAGRSNATITATLFQATPFIMLAIDTVLLPYELFGDSMPIEMNLSVSTPGPAPSSLVIPPPPPPPPKSIARGPHSSQSTEPPPPAIPGGAPEDIRALAASLTFTLTTLVASFLLSSSLCL
The following text describes a protein:
Function:
Functions in the late secretory pathway. Required for the generation of secretory vesicles as well as for actin polarization and polarized growth (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MDENGASFQVLCLATIGFHHLRGPEIEHLFPESMDFPKEWSILPFLSLPDGAHSSEKDFVYFTLPFPNDEGTVFGLSCTRQLNASSLKNIPSDVTRSSVQKAVVVITTSPPFGHIKDNLDIVTNAYFSQGDFSNLDVLRDFFHVLTRKEQDVHIALNINLKSFLCEWRQNALVLLKVLLLGKRILVYDKSAERLGNFQYSLLSLIPCMMSHLQDVSSPSAHSLEKSLHKPASLQTSDKRSLLAYTGFPLIIFGEGSMFSPYTPLQLVHVLEAKSSTSWLAGTTNTLIMLNQNKMAEVIVRSDTHQIEFVDPTIKNLTSLTYTDKSWMEDIISRVESSLEMELPGFEGSDDWIRNQFELYIFGMLATVKYYNFLKKQDDSILSQYHYLPSTSCISDYGETFLLEWMKTNTFRIWNNIADDDLFDVILPKHPCKEEHKVPISARIATLFSAVKITPKSRDGEDEGSKEPAV
The following text describes a protein:
Function:
Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. Mutations to this protein prevent the exit from mitosis.
Sequence:
MLELKTNVIQDPELKDSLDLQENDRVEIIGDAVHYIVNDHLNRVFNYTVDQQKIHAALITTFASGKKAIVVILDDIGYVYYVGDNNNDSYIINVPFSTESAWSSPSGLYLQRHRSSDENLNTDLPHIFCLNDPLDELTLIKFDGKKILSLFDSIVYVVGEIVVTHNKKEKKLSFWRSRFIDPESDQSIKSSRNRRRESSFSREKNPDLTRSDSIHYTANTRLSEKFEEQGLAYSTIFSHIESFPITGSTSFDSILGNGVLVITTLVKELEKGYMMLFRLVRDRSPYFLDSLQLHAINLSAIKSKHLQKIVVLSSKGKVSLESPMSPSLPIEGTFRSFRVHGATLYLEDTDGVQRYISLDNRASNSLVKWCLSVIRYVLPLREYEIFYTGHLYALFAFKLSHDEAFISSILACFTFFSRDKVHVEPIEDCNEAYSLSSKFHFKKEILIASQLSSHLDYSTFKNYLMPLAITLHFISEELRLDSVVKPRKDQLVALLLQITTWLKWPRYCEYYNFDIAETFLSIPLSIQVDVEEPVGPTSILQWIIECLRSQSTVPFYGLESYGLPHSCSTMFPQTLSLMQLLDCLLNPNMTLQNLVEEMVRLGISRKRCERYPFGILCIIFTVLEIAAEEYSPNWESEELRLVNRLDVDSFLHPKTPKWVFNKQDQEVKEIKALTSTVTDSTLVDTQSFHPYKVVTDMIFREDRRLAEVNKLLNYSSQITIMTEHFDVDLSSVPMQQKVAQCICVRTLSVPIGAGMLTYGSKNPLPTEKVTPRLFNFTLHLHPGTLIIQPNKEFVTQELTEWPEFNVGVALGLSISKFSKEINTSWIMFNRPETLTAYHAGFLFGLGLNGHLKALATWHSFIYLTSKHDTTSIGLLLGLASSYLGSMDAKVTKLLSVHISALLPVGSNELNISPLTQTAGILGIGLLFHDSCHRRMSEVTMEEILASNESELKNEGYKLAAGFSLGLINLGRGSNLPGMSDLKLVSRLQVGISSQATFQSLEAGSPGAIMALTMIYMKTNDLEVAKKIDIPKSRYLLDFYRPDLILLRVAGKNLIMWDEVKADYEWVKYQIPDIMLSQFDLQEKKVLSSDDLLLYNVLAGICFSLGLRFAGTGNPKAKEILINFLDSFIRLCHLPAKTHDERVTAVTVIRCTQIVALSSSCVMAGYCDLDVLRRLRVLHGRMEPVNYGAQMATHMALGILSLGGGRYSLSRSNLAIAALLISFYPQFPRTTQDNRAHLQAARNLWALAVEERCIIPRNQDTKQPCIVPLNVVQKSGAVQKLEAPILLPPYDSISSVSTLGDKYWNLKIDLDNNSDYRELLRESQTLTLMPYDRTSSKEEPLNLFPKLKDTSSPLWNLVKTSRLFQSSNSPLNVASLQESNNKTSLGVKLLLSMDFDNLTRDRLLSLQILLQFFESCWTGVLLNKFHSRQYLFLSRDLVEDLSLRVWEYVYSHNHNEESV
The following text describes a protein:
Function:
Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MDALLAAAGPLPQKKGRPGKVHQRTPHPTSHKTVARGDGKDNIDSSTQSILSSTRLPHSFHRSNLATGSSSAPIRPDGTLGRIGDKKLRAKIASQDVGNKRAKVERDDVNEWINKAIGGERGGIEVDEDLGEKTWRVKQEEIVKEVAMNVRGKKFDLKMEDMGSYKVDYTRNGRHLAIASSRGHVATFDWQAGKLHSEIHLKETVRDIKFLHSEAYYAVAQKKYVFIYDQNGVELHKLKQHIDPTHMEFLPFHYLLSTVGNAGYLKYHDTSTGVMLTQIPTRLGSPHSMTQNPHSAIIHLGHANGTMTLWSPNMTTPHVKLLAHRGPVNGVAVDPSEHSAGRYVATSGMDGTVKLWDGRMWGKEVREWKTRNQITSLAFSGMGMLSVGGKSGVTVYQDLYKNTHRPPSPYLTLPLPSLTASATRFCPFDDLLCVGHERGISSLIVPGSGEPNFDSAEADLFETRTRRREREVRGVLEKVRPELITMDANFLGKISEGRGGETHEEREGRSFRQLGRLERLRLTGKADEPEQEGVDDEDAGLEDGEADPNGGERSIREKKERRKMKGKGGSTKRYLRKKAKKNIVDNSLLQMKAKVAAQRASEEKKRKVERGEIVQETGALARFA
The following text describes a protein:
Function:
Relaxes negatively supercoiled (SC) DNA in an ATP-independent manner at 75 degrees Celsius. From 50-85 degrees Celsius relaxes negatively SC DNA; at up to 100 degrees Celsius it unlinks catenated DNA to form circular double-stranded (ds)DNA molecules. The promotion or prevention of DNA linking/unlinking is temperature-dependent in vitro and probably depends on other factors in vivo. One study found single-stranded binding protein (SSB) does not enhance its activity , while another study found it does. Binds single-stranded (ss)DNA and less well to Holliday junction (HJ) or forked DNA. Anneals complementary oligonucleotides to form HJ structures.
Sequence:
MNLCNVNNYYLIIAEKSKAAKKIAEALSEKPILCRKYNVSYWIIKDHNSSKYVIVPAAGHLFGLKGESGFPVYDADWKPLWEIDKNSYYTKRYYQLISSLSKYALGFINACDYDIEGSVIGYLIIKNLGDIKKAKRMKFSALTKSDILSAFRNISALDYDMINAGIARHKIDWLWGINVSRALMISLQDFAKKRVILSAGRVQSPTLVQVVNSEIERNLFIPLPKFTVSIIVKIKDYSLNIKVNKEFEKITEAKEFLNKLINKTVKVVEVENRVRLLERPSPFNLTDLQIEAGRIYGISPYNVERIAEDLYLDGLISYPRTNSQKIPSTISIYNIIKGLENSSYRKLVDLVRKITGGKYVVKQGIKDDPAHPAIHPTGEAPKNLPNSKFKIYDLIARRFLGSVSADAKLSNTIYTLKVSDFPLEFTVSYTKILERNWLDIYHFHNVKEDKPIFLSKGDEGKIVDGKVNISLSKPTSRYTKVSLLKWMESSNLGTEATRGRIIEILVKRKYLTNNGRYIIPTKLGFYIAEILNKFFPDIVDVRMTADMESKLEMIKTGKVLESKVIKENIEKLNKFIEEYKVNKDKVGESLAKALGLIKIVKCKYCDLEQYKDGLCKYHYEAKVRLLDAVEIWKERTKYDHKKILKRISSSKSTGKYVKDIVTYMLSSE
The following text describes a protein:
Function:
Involved in the catabolism of pyridoxal 5-phosphate (Vitamin B6). Catalyzes the decarboxylation of 3-hydroxy-2-methylpyridine-4,5-dicarboxylate to yield 3-hydroxy-2-methylpyridine-5-carboxylate. The decarboxylation proceeds by an aldolase-like mechanism in which the binding of the substrate frees Glu-73 residue from its interaction with manganese ion replacing it by an interaction with the hydroxyl group from the substrate. Glu-73 residue then provides the proton for the keto-enol tautomerization. The decarboxylation reaction is analogous to the retroaldol reaction except that it does not need a base as the carboxylate is likely to be deprotonated under the reaction conditions.
Sequence:
MRRKVFEELVTATKILLNEGIMDTFGHISARDPEDPASFFLAQKLAPSLITVDDIQRFNLDGETSDNRPSYLERYIHSEIYKTRPDVQCVLHTHSPAVLPYCFVDTPLRPVTHMGAFIGESVPVYEIRDKHGDETDLFGGSPDVCADIAESLGSQTVVLMARHGVVNVGKSVREVVFRAFYLEQEAAALTAGLKIGNVKYLSPGEIKTAGKLVGAQIDRGWNHWSQRLRQAGLA
The following text describes a protein:
Function:
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MNVELEESFKKIQSHKGVVGVLIINKQGSVIKSTFDQEVSLSYSKVILDMFPKAHDLLKVNDNNDELSFFRVRSKDNDIMVTPDKDFFLMVVNKINK
The following text describes a protein:
Function:
Involved in pollen mitosis II (PMII) regulation during male gametogenesis.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein. Vacuole membrane; Multi-pass membrane protein.
Sequence:
MGSIRGDLQPLFVMPPPPLDEDCDDIFNSDESSWGLLSLSCFGIIMGLWFFASVCLIFGVYGSETVWLGPNSSILVKPSSIFVKSINAKELDFSKPGLQLYGFNGQSTPSGYFVNWTESRVLSVSQNSYKGWPYYLNRGTHMNISYNILPKGSAVRLVITEGMPFFYRSSLKDIAFRDTAWSWNLIQGSGMIQLDISKSKGYYLTVANLKRKDVEVELDIDVKVVLYDTKQSSYNCSFSNGECSFKMNERSPVENYAVVTSPALGQGVSIDDEWYIELSYQPRLIAYGSFTGVLLSFMLVAIHFCNKLKCCGGEGFLSEDDSVRTCLLADKGDNDCCNDVEASNKSLCAICFDAPRDCCFLPCGHCVSCYQCGTKIKRTKGRCPICRKKIMHVKRIYTA
The following text describes a protein:
Function:
Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.
Subcellular Localization:
Cytoplasm. Note=Localizes to the division site, in a FtsZ-dependent manner.
Sequence:
MSMKNKLKNFFSMEDEEYEYEYIETERESHEEHEQKEKPAYNGNKPAGKQNVVSLQSVQKSSKVVLSEPRVYAEAQEIADHLKNRRAVVVNLQRIQHDQAKRIVDFLSGTVYAIGGDIQRIGSDIFLCTPDNVDVSGTISELISEDEHQRW
The following text describes a protein:
Function:
Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc sequence of glycoproteins and glycolipids forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto a GalNAc residue inside the backbone core chains. ST6GalNAcIII prefers glycolipids to glycoproteins, predominantly catalyzing the biosynthesis of ganglioside GD1alpha from GM1b. GD1alpha is a critical molecule in the communication and interaction between neuronal cells and their supportive cells, particularly in brain tissues, and functions as an adhesion molecule in the process of metastasis (By similarity). Sialylation of glycoproteins or glycosphingolipids is very important in tumor development, neuronal development, nerve repair, immunological processes and regulation of hormone sensitivity (By similarity).
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MACILKRKPALAVSFIALCILLLAMRLANDVTFPLLLNCFGQPKTKWIPLSYTLRQPLQTHYGYINVRTQEPLQLNCNHCAVVSNSGQMVGQKVGEEIDRASCIWRMNNAPTKGFEEDVGYMTMVRVVSHTSVPLLLKNPDYFFKEASTTIYVIWGPFRNMRKDGNGIVYNMLKKTVDAYPDAQIYVTTEQRMTYCDGVFKDETGKDRVQSGSYLSTGWFTFILAMDACYSIHVYGMINETYCTTEGYRKVPYHYYEQGKDECNEYLLHEHAPYGGHRFITEKKVFAKWAKKHRIVFTHPNWTVS
The following text describes a protein:
Function:
Choline transporter.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MAEGIFMCFTRYEELKKFSGVNKQTLANWPFSTNLATYLDYEENWLMFLLIIGISMVAIVLKLIFWRNYIRGAIFLIDNASQAVGSLTIFPIFPWVFQVLCIRYFGSVTLYASSIVISSFKVVGPESGVTHYLVTFLQFYNVFGLVWVLSFGSVMSEMALADAFASWDWAINTPTEKPLYGLFSALRILYFNIETAALSALFALFSAHLHIFKQSLFLVSGKFLLFGKRQVPIMCAVDGTDFGQSAEKAESLSPRNVA
The following text describes a protein:
Function:
Phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA).
Subcellular Localization:
Cytoplasm.
Sequence:
MVRRHDDDCEDEETKISKNDEQEAWKQALLTAKDNLPEKASGPLVALLEGTSGHHHWTETNHPRPTFCNYCREKLNGVPWHGYTCDVCKVKAHRKCRDSVTEPCKWTNQSSIPQHLQFISPENTLLPHQWMEGNLPMPAKCSVCEKPCGSVRKLVDYRCIWCGCCVHDTCIAQLARSCSLGHSALSVISPLALKSVSPNGTALLREEAYGGDGLPGGSPLIVLINAKSGDSQGQRIIKKFRRILNPIQVFDIIATGPDFALTFFSQLESFRVLVCGGDGTVGWVLSAFDRLNLHSKCQLAILPLGTGNDLARVLGWGHAFYDDTLLPQVVRTMERAHTKMLDRWSVLAIEGAGDREGTVFLDAEQSQDIIHAAQQLCQTIRELVHNVSGTYSSMSNQNMLSNEEEKGQMTSQNSEESESKNLSLDDGDETIRQTTDTMTENCNTLLGKLDRLMKSLKEDSNNLEESGFEPGDDDECSTGDEMLQNRRKNEDSVVNRANSLKKALREVILMAEKGINQHYRETTTTNNTACTRRERFRKKRSKTTPSVLRIHHNKCLNTFQPPCSYQKIIISHSNLSSSSACSPPCSPAEEGPESDGKEFRSSSCKATFDISHSQSSSSAVLSALFQSQSTRNFEEILEKPSIGTVHPPTPGATREPSTACDDDDEDSQMTSSEFQKTSPEDSTSSDRPRILSDTTLNKKKNSEKIKSQSLHPICGGGPSGVDKMKQSHSDSSLYGEYEHLEGSSSGCGGGGTSGSTLLPARASDSATWQRVKERKRTVGSDLGLSSSSHLRRYSILVVFKTFKSGRSLSKKGRGLIETVYFPHFCSCRNMLSGFAGGSLIAEILLLNARVLSQMSGKVGGANSPPPTSSSSMNGPMSDCQTPFTQYKEMCVMNNYFGIGLDAKIALEFHNKREESEKTRSRSKLFMWYGILGGKELMHRTYRNLEQRIKLECDGVPIDLPSLQGIVILNIPSYSGGANFWGRNKEGPEFTVQSFDDRILEVVALFGVIHVATSRVPNAYRLQNHRIAQCRHVRIVILGDEPIPVQVDGEPWLQPPGIMQIVHKNRAQMLARNPVFDATLKKWEEQKATSSGIGTTAPSTPTALVGSSGEQIPFLTRAREFLRLIEGEIARLGVSSAFLGSLDDANAIVRGGAASGEEDPEFIDDLEEREEAVASVERVVELLEDHFGFPQRTRAPAGQPKLGPTPHFTFEIHGDEPDNWRYVINSIRQEMDREEASIRKARKQDLIAGKPKRSRFTAWFHKRFGTRSSSPFAYDNIPYWTCEEVCAWLQSIGLSEYQTTFRKNDIQGSELMHLERSDIMDIGIVKIGHVKRLQSAITELRAQNQRARRAQARKKRVAKEYKSGASGTTGGGIMGGVSGDKRKESSAERYSNCVPSTSIAGATSSGGTSSGNKRRIPPKDGESAPAVMQVDPASTDC
The following text describes a protein:
Function:
Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Endosome membrane. Lysosome membrane.
Sequence:
RVFLPLLLLGVILPGGDNEDGPTSFHLIQISTFVNNTWAQNQGSGWLDDLQIHGWESDSGTAIFLKPWSKGNFSDDEVTELVDLFRAYFIGFTREVQDRVNEFQLEYPFVIQVTAGCELHSGEAIESSLRGALGGLDFVSIQNHSCVPAPDGSSRGQKFCALTTQYQGISDIIERLLSETCPRYLLGVLDAGKAELQRQVKPEAWLSSGPTPGPGRLLLVCHVSGFYPKPVRVMWMRGEQEQPGTQQGDLMPIGEAAGLNCRVKHSSLGDQDIILYWGHPTSIGLILVAIIVPSLILLICLAFGVLRFMGSHRIGHD
The following text describes a protein:
Function:
Subunit F6, 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. In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro. Part of the complex F(0) domain. 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.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MASSSGVKLFSGVLKSFSSRQIYSRNFGASSIALGKLDPVQQIFVDQIKKYKDLSAKQGGGPVEVGPDYKQSKDDAIDRLSKMYNVGDPLKFPEFNFAEPDLEQQNISSLGDN
The following text describes a protein:
Function:
Phosphorylates the second messenger diacylglycerol (DAG) to generate phosphatidic acid (PA), another important signaling molecule. PA is required for plant development and responses to abiotic stress and pathogen attack. May be involved in the accumulation of PA during cold stress.
Sequence:
MEPAAMDSVSESNLNEFRIPSFIFQPELHVSDDGSSSPLPECPVLVFINSKSGGQLGGDLLLTYRSLLNEKQVFDLGEEAPDKVLRRIYLNLEVLKSRSKLAVEIERRLRIIVAGGDGTAGWLLGVVCDLKLSHPPPIATVPLGTGNNLPFAFGWGKKNPGTDRNSVMSFLDQVKKAKEMKIDNWHILMRMRAPRKGPCDPIAPLELPHSLHAFKRVSPTDELNMEGYHTFRGGFWNYFSMGMDAQVSYAFHSERKLHPEKFKNQLVNQSTYAKLGCTQGWFFASLFHPTSKNIAQLAKVKVMKRHGQWQDLHIPRSIRSIVCLNLPSFSGGLSPWGTPNSKKQRDRDLTPPYVDDGLLEVVGFRDAWHGLVLLAPNGHGTRLAQAHKIRFEFHKGYADHTFMRIDGEPWKQPLPEEDDTVVVEISHLGQVNMLATHDCRSRSVNDPSSPCNHDDGDDDSNEDESEHGEERKKFGAADTFKIPDGIDIAHLS
The following text describes a protein:
Function:
Serine/threonine-protein kinase involved in transcription regulation. Phosphorylates the UBC2/RAD6 ubiquitin-conjugating enzyme (E2), leading to monoubiquitination of histone H2B and the silencing of telomeric-associated genes. Also required for histone H3 methylation. Necessary for the recovery from pheromone-induced growth arrest in the cell cycle G1 phase (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MAIASLERDDHGNPRFRGCTSIRDFEFLGKLGEGTFGEVYKARSKKDGSIVALKKILMHNEKDGFPITALREIKLLKMLSHRNILQLKEMAVERSKGDGRKKPSMYMVTPYMEHDLSGLLENPAVNFTEPQIKCYMLQLLEGLKYLHGNRILHRDMKAANLLISNNGVLQIADFGLARPYDEPPPEPGKGGGEAKRDYTTLVVTRWYRPPELLLQLRRYTTAIDMWGVGCVFGEMFKGKPILAGSSDLNQTQLIFNLVGTPTEENMPGWSSLPGCEGVKSFGYKPGSLREVFKDQNPMAISLLEELLKLDWRKRINAIDAINHPYFSSPPFPARPGELPSFEDSHEFDRRRFRGQRGAIPPAPAGGSVDQQQTTEIAVFPVLHALAGSLHTGFKTILQSALLKTGMLYHMDLQTRGSRFQASLVQKIAACLLNLLCLLIHHGAWVIQIGRHVREVNAIISEDGPMGNWIHTSRLTVTLVDILEKGKAIVRVPLLIGVIWNSNTLMKGINRVILGTDVLQEREAGVLTFERLEQRIEHCTDDDKLVLVSTDAERLRQMNPVTLLVLNDSKFITHLLLSMTY
The following text describes a protein:
Function:
Probable acetyltransferase.
Subcellular Localization:
Membrane.
Sequence:
MVRLELDQIVMRRMKEDDIEIVKALIKEGCEGTENRLILHILTRPLCLFVLAVLSSVLRCLVHSFILALTIPVFLLIVFLKITMPRSTGVLGSSRPYWDYVGSSYRGMQDETLSNPYSRISGKTPVTKKPRRRIGCKDKEMSSEKITPEREQTAGQVWVAQCEGEIVGCIFRESETRPGIARICRLVTGCWYRREGLGRLLVQSLENREREAGAHRVYAHIPYPSKVGEAFFRKVGYVQLGEVENGEEEEEIEKETPEKGFMGYPLTKVYYKDL
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Miscellaneous:
MISCELLANEOUS: During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA.
Domain:
Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Sequence:
MSQNIINARVTFRNSPIHILERFTIKDIEEAYDQFKKHSGLDECVIIQTCNRIELFGKSKSQEVDKIKKTWASLAGLEEQVFDENMEVEENQNALHHLLKLTSGLDSMVLGEEQILGQIKNSITSARERKASGQHLNTLFDKAIRIGTRIRNNSGIGKGGISVGSMAVKLAEENIDELKTKKTLLIGTGEVSTLVAKSLQRRGYAFDVTSRTLSRSETFCETMGGTPVKFEEILSGFDNYDVIFVATTAPYFLVTYERITEAMKDKNKGMMILDLSNPRTVDEKVATIGGIKLMNLDQIAEMVEKNMNARLNKVKTVESIINEEVSVLEASMKRLEAEPLVKDVFKNIESLREKELQKALQMLDEKDEKRIKIIDELTKAVVESIVSTPMNNIRKASEQGNPEVVDLASKLFDYKKQEQAD
The following text describes a protein:
Function:
Transcription factor, possibly involved in transcription regulation during lens development, including that of crystallin genes. Specifically binds to the alphaCE2 enhancer element of crystallin gene.
Subcellular Localization:
Nucleus.
Sequence:
MATDLAMSAELPNSPLAIEYVNDFDLMKFEIKKEPPEADRYCHRLPPGSLSSTPISTPCSSVPSSPSFCAPSPGSQPGQNLVNGVNNNNNNSGNGNNNTQGSSGKPQMEDLYWIPNYQHHISPEALNLTPEDAVEALIGNAHHHHHHHHHQPYEGFRGQQYVGEDLSAATNGHHHPVHHHHHHHGHHAHARLEDRFSDEQLVSMTVRELNRQLRGFSKEEVIRLKQKRRTLKNRGYAQSCRYKRVQQRHMLESEKCTLQSQVEQLKQDVARLIKERDLYKEKYEKLASRAFNGGGNTRDPSSGNHVKTTSTDFFM
The following text describes a protein:
Function:
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Sequence:
PKTKTASLSKASVAVEQQTKVALIRIGTRGRRQNPHTTTDVPTYLPDKTILPCNLPREDVRDAFISLTAASLADLPPASVIGTASLRRKSQILHRYPSLNVQENFRGNVQTRLRKLNEGVVQATLLALAGLKRLSMTENVTSILSIDDMLPAVAQGAIGIACRSDDDKMAEYIATLNHEETRLAVVCERAFLQTLDGSCRTPIAGYACRNEDGNCLFRGLVASPDGTRVLETSRVGPYAVEDMIEMGVQ
The following text describes a protein:
Function:
Contributes to the last few anthocyanin biosynthetic steps. Converts cyanidin 3-O-glucoside to cyanidin 3-O-xylosyl(1->2)glucoside. Can use 3-O-glucosylated anthocyanidins/flavonols and uridine diphosphate (UDP)-xylose as substrates.
Sequence:
MGVFGSNESSSMSIVMYPWLAFGHMTPFLHLSNKLAEKGHKIVFLLPKKALNQLEPLNLYPNLITFHTISIPQVKGLPPGAETNSDVPFFLTHLLAVAMDQTRPEVETIFRTIKPDLVFYDSAHWIPEIAKPIGAKTVCFNIVSAASIALSLVPSAEREVIDGKEMSGEELAKTPLGYPSSKVVLRPHEAKSLSFVWRKHEAIGSFFDGKVTAMRNCDAIAIRTCRETEGKFCDYISRQYSKPVYLTGPVLPGSQPNQPSLDPQWAEWLAKFNHGSVVFCAFGSQPVVNKIDQFQELCLGLESTGFPFLVAIKPPSGVSTVEEALPEGFKERVQGRGVVFGGWIQQPLVLNHPSVGCFVSHCGFGSMWESLMSDCQIVLVPQHGEQILNARLMTEEMEVAVEVEREKKGWFSRQSLENAVKSVMEEGSEIGEKVRKNHDKWRCVLTDSGFSDGYIDKFEQNLIELVKS