lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Dehydrogenase involved in the conversion of monodictyphenone to the prenyl xanthones such as emericellin, shamixanthone and epishamixanthone. Monodictyphenone is first converted to variecoxanthone A via a paeciloxanthone intermediate by the consecutive actions of the FAD-dependent monooxygenase mdpD and the xanthone prenyltransferase xptB. XptB catalyzes regular O-prenylation at the hydroxy group of C-7 of the xanthone ring. Variecoxanthone A is further prenylated to emericellin by xptA before being reduced to shamixanthone and epishamixanthone by the dehydrogenase xptC.
Sequence:
MAKLSVILLFRSLLLCGALTVSRHATLVTEREVQSSKYDFIVVGGGVSGLTVADRLTEIPDVSVLVIEAGPVDRGEDFVYVPGSYERDPYIWPGLTNEPSAELNNRVFDSVVARVAGGGSIVNAMIFLRGTALDFDGWESLGNHGWGWEGMLPYFIKSENFTRPTPELAHEGNITWDDSVRGHDGPVRYSYPNYIYPGLGRLYEAALHIGIQPRLDPNGGQNTGVFNQPFAIDAATWTRSSARRNHYDPAVSRPNYHFLSDTTVARVIFDGTRAVGVEYLPSRGGGISTAFAAKEVLVAAGALHTPQVLQLSGVGPRDLLEALNIPIISDLPGVGSNLQDQTTFPFVYTWDSAVTPNVTTFLTNTTWATEQRVLYDQHLPSVWTLTRPLAPKFAFLSYEDATANTAYASILDDAQARDPADSLPGDIHPTVLAGYAVQRQIMFNEFRDAGLAVGGMSWDTDANVQVFNVKPFSRGYVYINQTDPLANPVIDFRTASDPTDFQLHIALLHKQRELFNAPSLAALGPTEVVPGPAVQTDEDIIKLMREILQPSNGHQCCSAPMMPRELGGVLSPEMKVYGTTGLRVIDISHWPKELSGPPMASIYAAGEKAADIIKGEHGWLGN
The following text describes a protein:
Function:
Catalyzes the epimerization at C4 of 3-dehydro-D-gulosides leading to 3-dehydro-D-glucosides. Probably functions in a metabolic pathway that transforms D-gulosides to D-glucosides. Can use methyl alpha-3-dehydro-D-glucoside and methyl beta-3-dehydro-D-glucoside as substrates in vitro. However, the actual specific physiological substrates for this metabolic pathway are unknown. Cannot act on D-psicose, D-fructose, D-tagatose, D-sorbose, L-xylulose, or L-ribulose.
Sequence:
MKIGTQNQAFFPENILEKFRYIKEMGFDGFEIDGKLLVNNIEEVKAAIKETGLPVTTACGGYDGWIGDFIEERRLNGLKQIERILEALAEVGGKGIVVPAAWGMFTFRLPPMTSPRSLDGDRKMVSDSLRVLEQVAARTGTVVYLEPLNRYQDHMINTLADARRYIVENDLKHVQIIGDFYHMNIEEDNLAQALHDNRDLLGHVHIADNHRYQPGSGTLDFHALFEQLRADNYQGYVVYEGRIRAEDPAQAYRDSLAWLRTC
The following text describes a protein:
Function:
Involved in pre-mRNA splicing.
Subcellular Localization:
Nucleus.
Sequence:
MALTSFLPAPTQLSQDQLEAEERARSQRSRQTSLVSSRREPPPYGYRKGWIPRLLEDFGDGGAFPEIHVAQYPLDMGRKKKMSNALAIQVDPEGKIKYDAIARQGQSKDKVIYSKYTDLVPKEVMNADDPDLQRPDEEAIKEITEKTRVALEKSVSQKVAAAMPVRAADKLAPAQYIRYTPSQQGVAFNSGAKQRVIRMVEMQKDPMEPPRFKINKKIPRGPPSPPAPVMHSPSRKMTVKEQQEWKIPPCISNWKNAKGYTIPLDKRLAADGRGLQTVHINENFAKLAEALYIADRKAREAVEMRAQVERKMAQKEKEKHEEKLREMAQKARERRAGIKTHVEKEDGEARERDEIRHDRRKERQHDRNLSRAAPDKRSKLQRNENRDISEVIALGVPNPRTSNEVQYDQRLFNQSKGMDSGFAGGEDEIYNVYDQAWRGGKDMAQSIYRPSKNLDKDMYGDDLETRIKTNRFVPDKEFSGSDGRKRGREGPVQFEEDPFGLDKFLEEAKQHGGSKRPSDSSRPKEHEHEGKKRRKE
The following text describes a protein:
Function:
Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate; Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate).
Domain:
The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Sequence:
MTQLKSFELPIGTQLAYLAEGGANIIYRIVSQADHQILPAEYRGKLLRLRKDTPAGVSYQEIARNFDRVIRPLFNPEELVDQELVYLPKGLSQQCNDQLRAAELTGKRPKQRRGVYLSVTEPFGLLVTDMTSFGNPGTDLAELKPKWLVQSPSAPVSARRCRTCALRDMKNHDARRVGASEVRSFCPLDLVSDKFEHVLRATKFVKGYKDHTRLAKVIYRNPTLLKLLAHQRSMKDVGLYGPSPLSRDKSIAMTLRDCTMYIKMPRSEKGRVEIRLGDLDLKTAGGGKAQYWLELEHRLLSEGWYMGAKNHTRSCDCALQSPRTQPPPSM
The following text describes a protein:
Function:
G-protein coupled receptor for FARP(FMRFamide related peptide) neuropeptides. Activated by FARP neuropeptides flp-18 and flp-21. Plays a role in modulating social and feeding behavior. Required to modulate locomotion quiescence during the sleep-like state called lethargus, which occurs during molting between larval and adult stages, in part by regulating touch sensitivity.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MEVENFTDCQVYWKVYPDPSQSIYAIVPFLTVYLFLFFLGLFGNVTLIYVTCSHKALLSVQNIFILNLAASDCMMCILSLPITPITNVYKNWYFGNLLCHLIPCIQGISIFVCTFSLGAIALDRYILVVRPHSTPLSQRGAFLTTVLLWILSFVVTLPYAFNMQMIEYTEERICGYFCTEKWESAKSRRAYTMIVMLAQFVVPFAVMAFCYANIVSVLSKRAQTKIRKMVERTSALESSCAFPSHGLEQYENELNEFLDKQEKEKQRVVLQNRRTTSILVTMVVWFGITWLPHNVISLIIEYDDTQSFFRLYGRDDYDISYLLNLFTHSIAMSNNVLNPVLYAWLNPSFRQLVIKTYFGDRRKSDRIINQTSVYKTKIVHDTKHLNGRAKIGGGGSHEALKERELNSCSENLSYHVNGHTRTPTPEVQLNEVSSPEISKLVAEPEELIEFSVNDTLV
The following text describes a protein:
Function:
Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MYLPDKLVKPLSSKIDWCEPNYVVSTNIAEFWNTLSNIPMLVIPLILIYLYKDYSLKVLHCRFVNIVWALLVLTAIGSTYFHATLSLLGLFVDEIGILWMGFAMLGMWLPGVYLPEYFNKNRYHYHVLMIAGAITSTILGLIKPQINHIFLFFFLIPTLKVAKGQLSRHTSPEFQRLCKRGLVTLAFALVSWVCDRFICSFWLQIHFPYLHAIWHVLIAIATYQLGVCCSYSYALHSSPKTN
The following text describes a protein:
Function:
Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex. The ATP-bound conformation promotes DNA end binding and end tethering, and alters Mre11 nuclease activity. ATP hydrolysis promotes both Mre11 activity as well as HerA/NurA activity. Also has reversible adenylate kinase activity.
Domain:
Binding of ATP induces a closed, compact conformation of the Rad50/Mre11 complex. ATP hydrolysis opens the complex; The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer.
Sequence:
MKLERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAILVGLYWPLRIKDIKKDEFTKVGARDTYIDLIFEKDGTKYRITRRFLKGYSSGEIHAMKRLVGNEWKHVTEPSSKAISAFMEKLIPYNIFLNAIYIRQGQIDAILESDEAREKVVREVLNLDKFETAYKKLSELKKTINNRIKEYRDILARTENIEELIKENEQELIQVLQEISKIEEVLPSKRSKVDMLRKEVLRLEETKVEIENSERLLEKRRGDKRTLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKKDVDAYLALKEFKNEYLDKKYKIEKELTRVEELINEIQKRIEELNEKESEKEKLENEKKEILNKLAILEKDHQLYEEIKAKKENLRQLKEKLGDKSPEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKGKCPVCGRELTDEHREELLSKYHLDLNNSKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAEQIRSIEEELNVVNLEKIEKNATEYEKLLEELRTLEGRIRGLAEDLKKLAPLEKKLAALIHKKQELEKELKELNTKLESFGFKSVEDLDSKLRELEEIYKRYLTLLNSKKELEITQREIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQKYNEEEYKKKREEKEELEKELARLEAQKKELEKRRDTIKSTLEKLKAEKENRERVKKEIKDLEKAKDFTEELIEKVKKYKALAREAALSKIGELASEIFAEFTEGKYSEVVVRAEENKVRLFVVWEGKERPLTFLSGGERIALGLAFRLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEELKDAADHVIRISLENGSSKVEVVS
The following text describes a protein:
Function:
Affects biofilm formation and mucoidy.
Subcellular Localization:
Periplasm.
Sequence:
MKKCLTLLIATVLSGISLTAYAAQPMSNLDSGQLRPAGTVSATGASNLSDLEDKLAEKAREQGAKGYVINSAGGNDQMFGTATIYK
The following text describes a protein:
Function:
Catalyzes the reduction of all-trans-retinal to all-trans-retinol in the presence of NADPH.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MITITIRCFVLTAACAALHGADSSRLPLPVAHADTLHCYLKWACTLWAVLDLNAVLNRWAENRWLWRDDTGAWDWEKEIAVVTGGAQGIGACVVKNLLSHGISCAVLDVAPLSANYTKHELNLVRYYKCDITSPHDLHSAAEAIRSDLGHTSILINNAGIGNAYTILDIPLENLKKIFDINLLSHWSTVKEFLPDMLAKKKGHIMSVASLASFVSLAAAVDYSCTKAALLAFHEGLGQELKHRYKCPQIKTTIVHPSWTKSAITAHPAIQAGLESIGVKLLEAEHVAEAMGRQIIAARSGQLILGPRISPKIRALPTWLQEVIRDSQANVVSGSGSTG
The following text describes a protein:
Function:
Thiamine-regulated, high affinity import carrier of pyridoxine, pyridoxal and pyridoxamine.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MEIPESKNSIVSQDTISSNETDIRAPKYINWIYNLDRWGVEVRGIERVSEQERIELGQKIPTWHLFIQTLGLWWSACGGLTTMSSFFLPTLLFGLNLRDAMISGLIGMIIGCLVPAYSSTMGPKSGCRQMVTARFLFGQWGVKFVALICIVGGIGWSVVNCVLGGQMLLAINHNISLAVGIVVIAIISLIVAVFGIKVLLKFQTVFSIPIFIASILFYVVVCQKANYIGESNKLINDAGYSKVTFRGNWLSYFSLCYSVTATWGSGAADYYILYPASTPSYQIFLITFLGIAVPSTFVAIAGTICGNFALSYKPWNDAYNEFGVGGLIVGTFSHWGKFGKFVAVLLYISLICNNIMNTYSVAFEFQLVDSRLTYVPRWIWATIVTIIYLVLSVCGRNHFSTILSNFLPMLGYWITMYIALLLEENFIFRSTFKVRKLHEHEFDGDYKQMYNWTNWNNPKGRTLGLAACFAFLCGCAGAIIGMNQVYYKGPIARKVGEYGADLGMWISFGFTAITYPVFRYIELRLLKK
The following text describes a protein:
Function:
Probably involved in the regulation of chromatin states (Probable). Contributes to RPP7-mediated and basal immunity, especially against Hyaloperonospora arabidopsidis isolate Hiks1.
Subcellular Localization:
Nucleus.
Sequence:
MDCKSSDSSGTDDDLPPSHRVPRGGGGGRGGRVAGNGRPLNLPPSYPKMYDDLAADMEAQIHQIEKEAYISVLRAFKAQGDAISWEKESVITELRKELSLSNEEHRELLGRVNSDDTIRRIREWRQSGGMQPSMRNAAQVVHDTLPSPSVSASMKTHKPNQPIPSQPFASSSPSFHPQADPTHPFASSTAKRGPVPIVKGKKHKPVFPGSSSTKHAPYHPSDQPPRGQVMNRLPSVPASSSEPTNGIDPESFLGRRVRTKWPEDNTFYDAIITQYNPVEGRHALVYDIATPSETWEWVRLSEISPGDIEWIGEDPGLGNRYNGQGHGLNRTTGPNCVPQRGSGLEKNTIRKGFRTSQNGTGKKKHLDIRIRQTDVLIREVERVLRSHNPDPYEVERAKRVLEEHEHALVGAIAKLGDISDGENEGAFRR
The following text describes a protein:
Function:
Plays a role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA; Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA.
Subcellular Localization:
Nucleus.
Sequence:
VSVITQDGRVIVGTLKGFDQTVNLILNDSHERVYSSGAGVEQVALGLYVIRGDNIAVIGEIDEDVDSSIDLAEVKAEPINAVVY
The following text describes a protein:
Function:
May be involved in the control of cytoskeleton formation by regulating actin polymerization.
Sequence:
MAKFALNQNLPDLGGPRLCPVPAAGGARSPSSPYSVETPYGFHLDLDFLKYIEELERGPAARRAPGPPTSRRPRAPRPGLAGARSPGAWTSSESLASDDGGAPGILSQGAPSGLLMQPLSPRAPVRNPRVEHTLRETSRRLELAQTHERAPSPGRGVPRSPRGSGRSSPAPNLAPASPGPAQLQLVREQMAAALRRLRELEDQARTLPELQEQVRALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLATSERGGRARASPRADSPDGLAAGRSEGALQVLDGEVGSLDGTPQTREVAAEAVPETREAGAQAVPETREAGVEAAPETVEADAWVTEALLGLPAAAERELELLRASLEHQRGVSELLRGRLRELEEAREAAEEAAAGARAQLREATTQTPWSCAEKAAQTESPAEAPSLTQESSPGSMDGDRAVAPAGILKSIMKKRDGTPGAQPSSGPKSLQFVGVLNGEYESSSSEDASDSDGDSENGGAEPPGSSSGSGDDSGGGSDSGTPGPPSGGDIRDPEPEAEAEPQQVAQGRCELSPRLREACVALQRQLSRPRGVASDGGAVRLVAQEWFRVSSQRRSQAEPVARMLEGVRRLGPELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGACEVNRQNRAGYSALMLAALTSVRQEEEDMAVVQRLFCMGDVNAKASQTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQPGCDPAILDNEGTSALAIALEAEQDEVAALLHAHLSSGQPDTQSESPPGSQTATPGEGECGDNGENPQVQ
The following text describes a protein:
Function:
Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of 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.
Sequence:
MALGWLIFPRQSQLGPSGPFTQVSNHMRKGKMVKDGSNNVPSLRPTSIWGQDRKFIYLTLNLTDAKYATVRIRPDSLFFKANGIGANGKHDYCLDFEFYKPLQPTGNTYKILGRTVEFKLLKDKVGEHWQQLCKDQPKPSWLKVDFDKFFVEDEEDEEETDNAKSEVDKVIPQLVDAEVQKLQQQDFHVGTYDITGSYMKFCQALAVLEVIHPLLGIVKSGVLTPAIQVFGRNMVLFMIISPQESIHGEKIVILLFLAWSLIEVIRYPQYALSVINYPIRIITWLRYTAWIPLYPVGFYLEGGMYMYKHMFKQRTKHLKNISGTSTSKKKS
The following text describes a protein:
Function:
Catalyzes CTP-mediated phosphorylation of dolichol, the terminal step in de novo dolichyl monophosphate (Dol-P) biosynthesis. Dol-P is a lipid carrier essential for the synthesis of N-linked and O-linked oligosaccharides and for GPI anchors.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MYIMSKKCYDTSEKIDREQECVEVNYQHRNFESILEIFSVLFIPFLCNSGKKFLQISNASFFLPACFYLLGSSSIIQLYEPLLWLSSFPFCILYVGFGENSVLYHEMYTVCLYNALLSLTQRWKWLSIVLDGLGNSSVNLKLHETVILAFLEITQNSFTFIEGILICTGLTGLCFATFSYEVSPVVSVLSGVLLISLPTLILLNLCILKLAAKLHLSALFTTCLIYFFSALLVFLVSRSWVAGQLGQAPEVWLFNQIFSHRNSLTRIKIIIWWIICLGCFIFILLRSNRNNPLGKYFTTEDEVLNFRRKTYHALVVFLFLPVCCLDPHFLHLSFSGVLFIFLFVEGIRILRLKPFGKMIHEFLWEYTDNRDHKGPLIISHIYLLIGCAIPIWLSNALKGPVASVELLVGVLCLGCGDSMASIIGKRFGKHRISKTNKSIEGVFAFSISVFLVLHLTQAFHVCPSVTFWKTLFMSLCTAILEGVSTENDNLILPMYMWVLYQALD
The following text describes a protein:
Function:
Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MGASSSTAAPDRKDSEDEMVLNDLHIETGDQNAVKNLLDDTIVEFFQGKDTFKLHYGWDNAKLLFMLLATIIAAVSHFFKHPAIPEHVLIYSCVGAFFFIHALLFGYTTFIEKDVLLRMTRTGSAGKTILVRTSFPYTESHYSLSIHHGDAKDTPKKVELYVGRYFDKDGYFSKDAFNKDIETVLSRFEKKDKKQ
The following text describes a protein:
Function:
Required for axonemal dynein assembly and ciliary motility in ciliated organs, including Kupffer's vesicle, during embryogenesis. Facilitates the onset of robust cilia motility during development.
Subcellular Localization:
Cytoplasm, cytoskeleton, flagellum axoneme. Cytoplasm, cytoskeleton, flagellum basal body.
Sequence:
MRLKRFLLRYYPPGIILEYEQSQMLKTKSIDLLDLKAESDIDPILDEIVRKEPLVTPNRTDQVRQLIERLQEKLAKPDDHKFFLFKVLRAHILPLTNVAFNKSGSNFITGSYDRACKVWDTASGEELHTLEGHRNVVYAIAFNNPYGDKIATGSFDKTCKLWSSETGKCYHTLRGHTGEIVCVAFNPQSTVIATGSMDTTAKLWDIKTGAEKNTLSGHSAEIISLSFNSMGDRVITGSFDHTVSVWDVHTGRRIHTLIGHRGEISSAQFNYDCSLIVTGSMDKTCKIWDAATGKCVGNLRGHEDEILDVVFDYTGQFIASASADSSARVYNAVTHHCICKLDGHAGEISKISFNPQGTKLLTASADKTAKIWDPKSGTCLQTLEGHTDEIFSCAFNYEGDTVITGSKDNTCRIWR
The following text describes a protein:
Function:
Mitochondrial ribosome (mitoribosome) assembly factor. Binds at the interface of the head and body domains of the mitochondrial small ribosomal subunit (mt-SSU), occluding the mRNA channel and preventing compaction of the head domain towards the body. Probable inactive methyltransferase: retains the characteristic folding and ability to bind S-adenosyl-L-methionine, but it probably lost its methyltransferase activity.
Subcellular Localization:
Mitochondrion.
Sequence:
MIIFRASFAFARKVKQLRTSLINNSKKTDEENISSESIESKEKVEKVNVPENQENLEQKEKKVFEKKFIKSPEYLMACNHQPALSLPEEILKKARKVFSKYPPDELRDASYKYMRMYQLLHALEKPVSVTIKRNNLFENPENLQKLTEKKVIHLYKKGTSEQQILDKIFERRQKKDVNVDRVNSAEEKLEEFHNFASAIDYDQILTVSYFLRKVPGSFAVGQKIMTEIQKRNPNFNPKSMLDYGSGIGTWAWSFKKLYPDVKNVVCVEPNVYMRKLGKFVTQDYIKDVKFYESLSHTLELSYDYFDFISIAYVLEEINHPEARLLALQSLWAKLSDDGVMVLVCPGSPTGFRFVNDFREWILKQKGVIVAPCQHQQTCPMAKEGFQWCHFKQMFTAWPKDVFPKYIYENTAVTEKFSYLAVSKKALVQEGQDWPRITFDPLKRGKHLILDMCTDQGTLERRIVAKSHGKEGGYYEAKHLNGGDLWRFPKLPPSKVGKKRRKQPVKIL
The following text describes a protein:
Function:
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Subcellular Localization:
Cytoplasm.
Domain:
ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site; The C-terminal coiled-coil domain is crucial for aminoacylation activity.
Sequence:
MEKTYNPTSIEQDLYKTWEEQGYFKPHGDTSKDAYSIMIPPPNVTGSLHMGHAFQDTIMDTLIRCQRMKGKNTLWQVGTDHAGIATQMVVERKIAAEEGKTKHDYGRDAFIDKIWEWKAESGGTITKQLRRLGASVDWDRERFTMDDGFYKAVQEVFVRLYKDDLIYRGKRLVNWDPKLHTAISDLEVENKETKGHMWHFRYPLADGVKTADGKDYIVVATTRPETMLGDTGVAVNPEDPRYKDLIGKEIILPIVGRRIPIVGDEHADMEKGTGCVKITPAHDFNDYEVGKRHQLPMINILTFDANIRDAAEVFNSNGEASNAYGTEIPAKYQGMERFAARKAIVAEFEELGLLQEIKDHDLTVPYGDRGGVVIEPMLTDQWYVRAGILAKPAVEAVENGDIQFVPKQYENMYFSWMRDIQDWCISRQLWWGHRIPAWYDEQGNVFVGRNEEEVRAENNIAADVALRQDDDVLDTWFSSALWTFGTLGWPEKTPELKVFHPTDVLVTGFDIIFFWVARMIMMTMHFCKDEDGKAQVPFKTVYVTGLIRDENGDKMSKSKGNVLDPIDMIDGIDLESLVAKRTGNMMQPQLAAKIEKNTRKTFENGIEAYGTDSLRFTLAAMASTGRDINWDMKRLEGYRNFCNKLWNASRYVLMNTEEQDCGFAAGAELEYSLADKWIESQFELAAKEFNGHIDNFRLDMAANTLYEFIWNQFCDWYLELTKPVLWKGTEAQQRATRRTLITVLEKTLRLAHPVIPYITETIWQSVKPLVDGVEGDTIMLQALPQYDVANFNQEALDDIEWVKAFITSIRNLRAEYDINPGKPLEVMLKAANEQDAARIEANKPVLVSLAKLESIRVLADGEATPACATALVGKSELMIPMAGLIDKDAELDRLAKEIAKTQGEIARIEGKLGNEGFVAKAPEAVITKEREKLAGYQEALVKLEQQKATIAAL
The following text describes a protein:
Function:
Nuclear envelope-associated factor that is involved in the nuclear envelope ruptures during interphase (NERDI) repair, where it is locally recruited by CHMP5 and reduces cytoskeletal stress through its action on SYN2 to help reseal the ruptured membrane.
Subcellular Localization:
Nucleus membrane; Lipid-anchor. Note=During nuclear envelope repair, localizes at rupture sites where it is recruited by the CHMP7/ESCRT-III axis.
Sequence:
MTHWFHRNPLKATAPVSFNYYGVVTGPSASKICNDLRSSRARLLELFTDLSCNPEMMKNAADSYFSLLQGFINSLDESTQESKLRYIQNFKWTDTLQGQVPSAQQDAVFELISMGFNVALWYTKYASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHLPKLITPAEKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKADHTLSSLEPAYSAKWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKEYGETKGPGPTVKPSGHLFFRKLGNLVKNTLEKCQRENGFIYFQKIPTEAPQLELKANYGLVEPIPFEFPPTSVQWTPETLAAFDLTKRPKDDSTKPKPEEEVKPVKEPDIKPQKDTGCYIS
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion.
Sequence:
MASAVDTTGNPIPTSAVLTASSKHITARCFQENVDFLKCKKKDPNPEKCLDKGQQVTRCVLGLLKDLHHRCTKEMDAYVGCMYYHTNEFDLCRKEQQAFEKACPLE
The following text describes a protein:
Function:
ADP-ribose glycohydrolase that hydrolyzes ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on glutamate and O-acetyl-ADP-D-ribose. Specifically acts as a glutamate mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to glutamate residues on proteins. Does not act on poly-ADP-ribosylated proteins: the poly-ADP-ribose chain of poly-ADP-ribosylated glutamate residues must by hydrolyzed into mono-ADP-ribosylated glutamate by PARG to become a substrate for OARD1. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Catalyzes the deacylation of O-acetyl-ADP-ribose, O-propionyl-ADP-ribose and O-butyryl-ADP-ribose, yielding ADP-ribose plus acetate, propionate and butyrate, respectively.
Subcellular Localization:
Chromosome. Nucleus, nucleolus. Nucleus, nucleoplasm.
Sequence:
MRTRRCGSTLILSRVLQVPPLSVSRTRFRGATEAFTIAHVTMATHVQEQGEQIKCVKGDLFSCPPTDALAHCISEDCRMGAGIAVLFKKKFGGVQELLDQQKKTGEVAVLQRDDRYIYYLITKKKVSHKPTYEDMRKSLEAMKTHCLNNGVTDISMPKIGCGLDRLDWDKVSAILGEVFEGTDIKITVYTL
The following text describes a protein:
Function:
A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus. Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation-independent manner. Also plays a role in the biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Also binds to telomerase RNA (By similarity).
Subcellular Localization:
Nucleus. Nucleus, nucleoplasm. Nucleus, Cajal body. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm. Shuttles between the nucleoplasm and Cajal bodies.
Sequence:
MALEAGDMEEGQLSDSDSDMTVVPSDRPLQMAKVLGGGSAACAPVSHYRTVKHVDSSEESLDSDDDCSLWKRKRQKCHNTPPKPEPFPFGPSGQKTALNGGKKVNNIWGAVLQEQNQDAVATELGILGMEGSIDRSRQSETYNYLLAKKLAKKESQEYTKELDKDLDEYMHGDKKPGSKEDENGQGHLKRKRPVRDRLGNRVEMNYKGRYEITEEDAPEKVADEIAFRLQEPKKDLIARVVRILGNKKAIELLMETAEVEQNGGLFIMNGSRRRTPGGVFLNLLKNTPSISEEQIKDIFYVENQKEYENKKAARKRRTQLLGKKMKQAIKSLNFQEDDDTSRETFASDTNEALASLDEAQEGPGETKLDAEEAIEVDHPQDLDIF
The following text describes a protein:
Function:
May play a role in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Subcellular Localization:
Plastid, apicoplast.
Sequence:
MKIRFVFILSVLISGVCCISKNVSRRVANRMTAHSRFLFVHDKYKRNKNFKLKNNKEENNFINLYTVKNPLKCKIVDKINLVRPNSPNEVYHLEINHNGLFKYLEGHTCGIIPYYNELDNNPNNQINKDHNIINTTNHTNHNNIALSHIKKQRCARLYSISSSNNMENLSVAIKIHKYEQTENAPNITNYGYCSGFIKNLKINDDIYLTGAHGYFNLPNDAIQKNTNFIFIATGTGISPYISFLKKLFAYDKNNLYNRNSNYTGYITIYYGVYNEDSILYLNELEYFQKMYPNNINIHYVFSYKQNSDATSFYVQDEIYKRKTEFLNLFNNYKCELYICGHKSIRYKVMDILKSHDQFDEKKKKRVHVEVY
The following text describes a protein:
Function:
Transcription factor required for normal cell differentiation. Positively regulates LATERAL ORGAN BOUNDARIES (LOB) within the shoot apex, and the class III HD-ZIP genes REV, PHB, and PHV. Interacts directly with ASYMMETRIC LEAVES 2 (LBD6/AS2) to repress the knox homeobox genes BP/KNAT1, KNAT2, and KNAT6 and the abaxial determinants ARF3/ETT, KAN2 and YAB5. May act in parallel with the RDR6-SGS3-AGO7 pathway, an endogenous RNA silencing pathway, to regulate the leaf morphogenesis. Binds directly to KNAT1, KNAT2, and KNATM chromatin, regulating leaf development. LBD6 is required for this binding. Positive regulator of flowering that binds to the promoter of FT. Regulates FT expression by forming a functional complex with CO. Involved in leaf polarity establishment by functioning cooperatively with NUCL1 to repress abaxial genes ARF3, ARF4, KAN1, KAN2, YAB1 and YAB5, and the knox homeobox genes KNAT1, KNAT2, KNAT6, and STM to promote adaxial development in leaf primordia at shoot apical meristems at high temperatures.
Subcellular Localization:
Nucleus.
Domain:
A C-terminal domain (252-356) is required for dimerization.
Sequence:
MKERQRWSGEEDALLRAYVRQFGPREWHLVSERMNKPLNRDAKSCLERWKNYLKPGIKKGSLTEEEQRLVIRLQEKHGNKWKKIAAEVPGRTAKRLGKWWEVFKEKQQREEKESNKRVEPIDESKYDRILESFAEKLVKERSNVVPAAAAAATVVMANSNGGFLHSEQQVQPPNPVIPPWLATSNNGNNVVARPPSVTLTLSPSTVAAAAPQPPIPWLQQQQPERAENGPGGLVLGSMMPSCSGSSESVFLSELVECCRELEEGHRAWADHKKEAAWRLRRLELQLESEKTCRQREKMEEIEAKMKALREEQKNAMEKIEGEYREQLVGLRRDAEAKDQKLADQWTSRHIRLTKFLEQQMGCRLDRP
The following text describes a protein:
Function:
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MQSNQQQLKTSNQLKTNKPPIDIRSSRNNYEQSADKSPINKSFNDKKKSIPKAHAILQELFYKRQNSQEQLFKRTSSPKSQLDNTSINKSQRSISPQILYQMPFEIKKIYQQINQRLDQQKQQQNCKNKDTQKYKTEESKSHKNESTSSTINDSDEQIQNLINLEEIVFTIMAVISRKKKVINQCKNYLNRISHFILEEKDKITQQILSKQIHLERIGILVILYKALSDTFEEDQQNLKNLLFYIHNSMILHLQLINQSNTLSQSQRALIQARLNKVRPQKNYQFLDINLIRKNCNVVYSLLVLFVENSTDDKLSSLEKTLANLDRITLHQGTEFIKQEYQKILSHIEQLRLTMDSQDFQFDYEEVIDCYQIPYLSKTNRYTLVIDLDETLVHYQELVDEGQFLVRPFAQQFLKDMSKFYEIVIFTAAQQDYADFILDLIDEDKSITHRLYRQHTTLVKNTYVKDIQKIGRDIKKTIIIDNLAENFQLQPDNGIQIQSWYGDLDDQALLLLSPLLIQIVQKKIPDVREALRKFRDQMQRNIEAGISDPHLHLSLE