ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9SGD2 | MKRSVRPLFSALLFAFFAATLICRVAIRRSSFSFASAIAELGSSGLMTEDIVFNETLLEFAAIDPGEPNFKQEVDLISDYDHTRRSHRRHFSSMSIRPSEQQRRVSRDIASSSKFPVTLRSSQAYRYWSEFKRNLRLWARRRAYEPNIMLDLIRLVKNPIDVHNGVVSISSERYLSCAVVGNSGTLLNSQYGDLIDKHEIVIRLNNAKTERFEKKVGSKTNISFINSNILHQCGRRESCYCHPYGETVPIVMYICQPIHVLDYTLCKPSHRAPLLITDPRFDVMCARIVKYYSVKKFLEEKKAKGFVDWSKDHEGSLFHYSSGMQAVMLAVGICEKVSVFGFGKLNSTKHHYHTNQKAELKLHDYEAEYRLYRDLENSPRAIPFLPKEFKIPLVQVYH | Function: Galactosyltransferase involved in the biosynthesis of type II arabinogalactan. Possesses galactosyltransferase (GalT) activity in vitro, transferring galactose from UDP-galactose to a mixture of various oligosaccharides derived from arabinogalactan proteins. Forms a complex with GALT31A that can work cooperatively to enhance the activities of adding galactose residues at O6 positions to beta-1,6-galactan and beta-1,3-galactan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 45935
Sequence Length: 398
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q9UHL9 | MALLGKRCDVPTNGCGPDRWNSAFTRKDEIITSLVSALDSMCSALSKLNAEVACVAVHDESAFVVGTEKGRMFLNARKELQSDFLRFCRGPPWKDPEAEHPKKVQRGEGGGRSLPRSSLEHGSDVYLLRKMVEEVFDVLYSEALGRASVVPLPYERLLREPGLLAVQGLPEGLAFRRPAEYDPKALMAILEHSHRIRFKLKRPLEDGGRDSKALVELNGVSLIPKGSRDCGLHGQAPKVPPQDLPPTATSSSMASFLYSTALPNHAIRELKQEAPSCPLAPSDLGLSRPMPEPKATGAQDFSDCCGQKPTGPGGPLIQNVHASKRILFSIVHDKSEKWDAFIKETEDINTLRECVQILFNSRYAEALGLDHMVPVPYRKIACDPEAVEIVGIPDKIPFKRPCTYGVPKLKRILEERHSIHFIIKRMFDERIFTGNKFTKDTTKLEPASPPEDTSAEVSRATVLDLAGNARSDKGSMSEDCGPGTSGELGGLRPIKIEPEDLDIIQVTVPDPSPTSEEMTDSMPGHLPSEDSGYGMEMLTDKGLSEDARPEERPVEDSHGDVIRPLRKQVELLFNTRYAKAIGISEPVKVPYSKFLMHPEELFVVGLPEGISLRRPNCFGIAKLRKILEASNSIQFVIKRPELLTEGVKEPIMDSQGTASSLGFSPPALPPERDSGDPLVDESLKRQGFQENYDARLSRIDIANTLREQVQDLFNKKYGEALGIKYPVQVPYKRIKSNPGSVIIEGLPPGIPFRKPCTFGSQNLERILAVADKIKFTVTRPFQGLIPKPDEDDANRLGEKVILREQVKELFNEKYGEALGLNRPVLVPYKLIRDSPDAVEVTGLPDDIPFRNPNTYDIHRLEKILKAREHVRMVIINQLQPFAEICNDAKVPAKDSSIPKRKRKRVSEGNSVSSSSSSSSSSSSNPDSVASANQISLVQWPMYMVDYAGLNVQLPGPLNY | Function: May be a transcription regulator involved in cell-cycle progression and skeletal muscle differentiation. May repress GTF2I transcriptional functions, by preventing its nuclear residency, or by inhibiting its transcriptional activation. May contribute to slow-twitch fiber type specificity during myogenesis and in regenerating muscles. Binds troponin I slow-muscle fiber enhancer (USE B1). Binds specifically and with high affinity to the EFG sequences derived from the early enhancer of HOXC8 (By similarity).
Sequence Mass (Da): 106057
Sequence Length: 959
Domain: The N-terminal half may have an activating activity.
Subcellular Location: Nucleus
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G4MWY1 | MATPLQIMPLPVWPITFLEDAVVYLSALFTPWFTAFCVLWLHRYVRLIVHCYSHWTYKSKPIPSKPSYTSDDVTVVIPTIHDNFDELRPSLESILATKPHELIMVTTADKFEDLQRVAKTLSSPNIRIFCTQYANKRIQVCEALPKITTRITIMADDDVTWPSTMMPWILAPFEDPKIGGVGTCQRVKRVREGGLGLRIWNWLGAAYIERRNFEISATHNMDGGTSCMSGRTGAYRSEILRDYEFLEGFMKEEWWGKILKADDDNFVSRWLVSHKWKTWIQYEQECELETTLEDNIKFLYQCSRWARSNWRSNWTSLVKERHVWKQQWWCTYALHIATFTSLAFVFDFLILAALWWGTEGWEPVNRNRAIYAQLAFLAFSKVVKLVGLFRRHPADIMFLPVSIIFGYFHGLIKIYAGLTLNMTSWGSRTDGDTDDAHRLAPGPVRCSSLNTPRSEHKLPHYMQERDEIVNEKQQMREEEWEHL | Function: Glycosyltransferase that plays an important role in infection-related morphogenesis and pathogenesis . Involved in stress tolerance and hyphal hydrophobicity via its regulation of the expression of nydrophobin MPG1 . May regulate growth, pathogenicity, and cell wall integrity (CWI) through glycosylation of heat shock protein SSB1, and other (unidentified) substrates may contribute to conidiation . Candidate proteins as potential substrates of GT2 include several heat shock proteins (SSB1/MGG_02503, MGG_06759 and MGG_06958), two coiled-coil domain-containing proteins (MGG_04321 and MGG_09571), aminopeptidase 2 (MGG_16472), and a nuclease domain-containing protein (MGG_12646) .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56495
Sequence Length: 483
Domain: The conserved DxD and QxxRW domains are necessary for the full function.
Subcellular Location: Cell membrane
EC: 2.4.1.-
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F9WWD1 | MLSILGWFWAFVSAFVLRYLRTIVNCISNWTYRPIPIPDNPTYGPQDVTIILPTIAQGGEELEGTLRTCLRTEPYEIILVTIDANVKNLTLLAKKINSKKIRVLSVREANKRRQMCRAIPEVSTRITIFVDDDVIWPVKLLPWILAPFENPQMGGVGTSQRRVRPEKMNAWVFLNMGYLERRNWDCSACLHIDGGLPCLSGRTAAYRTSILQDDAFTHGFTNETWRTMQLNADDDNFITRWLYSHNWKIGMQYHKEAEVLTTLEAGPKYLSQCLRWVRSNWRSNIKSMFVERHYWYTQLWTTYSCLQTTITAWALPWDAFLFYSLHKASTDWSDDSRKMAFTLLFLWIFGFTKNVKLWGHYFRYPVDVIYIPVHIAFGYFHGLIKFWGLVTLSETTWGSRDGADSSELNRIRMMPLPPYGSTTPDGRKSETFEYMQEMPLIDQLPAYDTHDRHPPLSNMTSTITTTTPFHD | Function: Glycosyltransferase involved in the maintenance of the outermost surface of the fungal cell wall . Likely functions in the synthesis of a currently unknown, potentially minor but widespread, extracellular or outer cell wall polysaccharide which plays a key role in facilitating many interactions between plants and fungi by enabling hyphal growth on solid matrices .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54871
Sequence Length: 471
Subcellular Location: Cell membrane
EC: 2.4.1.-
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P35894 | MYLFLSNLSLADISFTSTTLPKMIVDIQTNNRAISYSGCLTQMSFFMLFGCLDSLLLTAMAYDRFVAICHPLHYQVIMNPRLCGLLVFLSILISLLVSQLHNSVVLQLTYFKSVDISHFFCDPSLLLNLACSDTFTNNIVMYFVGAISGFLPISGIFFSYYKIVSSILRMPSPGGKYKAFSTCGS | Function: Possible taste receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20605
Sequence Length: 185
Subcellular Location: Cell membrane
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P35895 | TTVPKMLINLQKQNKAISYAGCITQLSFVLLFAGMENFLLAAMAYDRYVAICKPLRYTAIMKAHLCLVMTLLSLCISIVDALLHGLMILRLSFCTFLEIPHYFCELYQVIKLSCSDTLINNILVYTMTSTLGGVPLGGIIFSYFKIISSILRMPSSGSRHRAFSTCGS | Function: Possible taste receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18666
Sequence Length: 168
Subcellular Location: Cell membrane
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P35897 | MYLFFSNLSFNDICIITTTIPKMLMNVQSHDQSITYLGCLSQVYLIVNFGSIESCLLAVMAYDRYVAICHPLKYTVIMNHYFCVMLLLFACSLALHMCLFHILMVLILTFCTKTEIPHFFCELAHIIKLTCSDNFINYLLIYTVSVLFFGVHIVGIILSYIYTVSSVLRMSLLGGMYKAFSTCGSHLSVVSLFYGTGFGVHISSPLTDSPRKTVVASVMYTVVTQMHGPFIYSL | Function: Possible taste receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26376
Sequence Length: 234
Subcellular Location: Cell membrane
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Q89ZV6 | MQEKIIILDFGSQTTQLIGRRVRELDTYCEIVPYNKFPKEDPTIKGVILSGSPFSVYDKDAFKVDLSEIRGKYPILGICYGAQFMAYTNNGKVEPAGTREYGRAHLTSFCKDNVLFKGVRENTQVWMSHGDTITAIPDNFKKIASTDKVDIAAYQVEGEKVWGVQFHPEVFHSEDGTQILRNFVVDVCGCKQDWSPASFIESTVAELKAQLGDDKVVLGLSGGVDSSVAAVLLNRAIGKNLTCIFVDHGMLRKNEFKNVMNDYECLGLNVIGVDASEKFFAELAGVTEPERKRKIIGKGFIDVFDVEAHKIKDVKWLAQGTIYPDCIESLSITGTVIKSHHNVGGLPEKMHLKLCEPLRLLFKDEVRRVGRELGMPEHLITRHPFPGPGLAVRILGDITREKVRILQDADDIYIQGLRDWGLYDQVWQAGVILLPVQSVGVMGDERTYERAVALRAVTSTDAMTADWAHLPYEFLGKISNDIINKVKGVNRVTYDISSKPPATIEWE | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 56656
Sequence Length: 507
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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Q8A525 | MKQDMIVILDLGSHENTVLARAIRALGVYSEIYPHDITVEELKALPNVKGIIINGGLNNVIDGVAIDVNPSIYTMGIPVMAAGHDKATCAVKLPAFTDDIEAIKAAIKSFVFDTCQAEANWNMANFVNDQIELIRRQVGDKKVLLALSGGVDSSVVAALLLKAIGENLVCVHVNHGLMRKGESEDVVEVFSNQLKANLVYVDVTDRFLDKLAGVEDPEQKRKIIGGEFIRVFEEEARKLDGIDFLGQGTIYPDIVESGTKTAKMVKSHHNVGGLPEDLKFQLVEPLRQLFKDEVRACGLELGLPYEMVYRQPFPGPGLGVRCLGAITRDRLEAVRESDAILREEFQIAGLDKKVWQYFTVVPDFKSVGVRDNARSFDWPVIIRAVNTVDAMTATIEPVDWPILMKITDRILKEVKNVNRVCYDMSPKPNATIEWE | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 48286
Sequence Length: 435
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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Q5V1K0 | MTRIDVIDNHGQFTHLEQRALRDMGVDVSLRDNTTPPEEIDADGIVLSGGPDMDDIGNCPEYLDLDVPVLGICLGMQLIADELGGRVGGGEYGGYADVTVDILDDDDPLLGSLYPETRVWASHADEVKEVPPGFERTATSDVCGVEAMSNTDEAIYGVQWHPEVAHTEEGEEVFENFLSVCDQQSVARQ | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 20567
Sequence Length: 189
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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A8AC69 | MVKVLVVAFGGQYNHLIKRSIERIGHEAALRPYNLPPPDEGEFDCVVFGGGPLTMPKDFDKVKGLEAYLRWKKPLLGICLGHQVLALLNGGEVGPSPKPEYGDVTIFVDDEDDILRGLAPSFRAWESHNEEVLREPPNSKVIAHSENTRVQALKYYNGPYYGVQFHPEVQHTEKGSLVFQNFVELCKR | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 21143
Sequence Length: 188
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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Q8THC7 | MRELKILVVNNYGQFCHLIHRAVRDLDMDTKIIPNVTPIEDILAEEPDGLILSGGPEMERAGLCFDYVREIDIPILGICLGHQAIALAYGGHVHSGKKGGYAEIEIEVIEEDDILRGLGPKITVWASHADEVAILPEGFIHLARSDICEIEAMRHPTKPIYGVQWHPEVSHTKKGDELLTNFFEVCDRY | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 21177
Sequence Length: 189
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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Q81IS3 | MIILKKQHDTIIVLDFGSQYNQLIARRIREFGVYSELHPHTITAEEIKAMNPKGIIFSGGPNSVYGEGALHCDEKIFELGLPIFGICYGMQLMTQQFGGKVERANHREYGKAVLKVENESKLYANLPEEQVVWMSHGDLVTGLPEGFVVDATSESCPIAGMSNEAKNLYGVQFHPEVRHSEHGNDLIKNFVFGVCGCSEGWNMENFIEVELEKIRETVGDKKVLCALSGGVDSSVVAVLIHKAIGDQLTCIFVDHGLLRKGEAEGVMKTFSEGFHMNVIKVDARDRFMDKLKGVEDPEQKRKIIGNEFIYVFDDEASKLQGMDFLAQGTLYTDIVESGTATAQTIKSHHNVGGLPEDMQFKLIEPLNTLFKDEVRVLGSELGIPDEIVWRQPFPGPGLGIRVLGEITEEKLEIVRESDAILREEIIKAGLDREIWQYFTALPGMRSVGVMGDERTYDYTVGIRAVTSIDGMTADWARIPWDVLEKISVRIVNEVKHVNRIVYDVTSKPPATIEWE | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 57634
Sequence Length: 515
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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P29727 | MTKLVNEMILVLDFGSQYNQLITRRIREFGVYSELHPHTLTAEEIKKMNPKGIILSGGPNSVYDENSFRCDEKIFELDIPVLGICYGMQLMTHYLGGKVEAASQREYGKANIRIEGTPDLFRDLPNEQVVWMSHGDLVVEVPEGFTVDATSHHCPNSAMSKADKKWYGVQFHPEVRHSEYGNDLLKNFVFGVCECEGEWSMENFIEIEMQKIRETVGDKQVLCALSGGVDSSVVAVLIHKAIGDQLTCIFVDHGLLRKGEAEGVMKTFSEGFNMNVIKVDAKDRFLNKLKGVSDPEQKRKIIGNEFIYVFDDEADKLKGIDYLAQGTLYTDIIESGTATAQTIKSHHNVGGLPEDMQFELIEPLNTLFKDEVRALGTELGIPDEIVWRQPFPGPGLGIRVLGEVTEEKLEIVRESDAILREEIANHGLERDIWQYFTVLPDIRSVGVMGDARTYDYTIGIRAVTSIDGMTSDWARIPWDVLEVISTRIVNEVKHINRVVYDITSKPPATIEWE | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 57849
Sequence Length: 513
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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A1URR0 | MDTSHSDTVLIIDFGSQVTQLIARRVRAMGVYSEIVPFQSALGGINRIKPKAVILSGSPYSTLDNGSPRAPIEVFEAGIPVLGICYGQQVMCVQLGGKVEAGHEREFGRAFLEIKEESALFDGVWEKGSSQQVWMSHGDRVTALPEGFCVIGTSKGAPYAAISDEKRNFYAVQFHPEVVHTPDGEKLLQNFVCKISGIKNNWSMAAYRDQAIAAIREKVGKNRVICGLSGGVDSSVTAVLLHEAIGDQLTCIFVDHGLIRKNEAEEVLKLFRDNYNIELIHVNAADMFINALEGETDPEKKRKTIGRLFIEVFEEETKKIGGAKFLAQGTLYPDVIESVSAIGEAITIKSHHNVGGLPERMNMKLVEPLRELFKDDVRSLGRELGLPEEFIKRHPFPGPGLAIRCPGAVTREKIEILREADAIYLDEIRKAGLYDKIWQAFAILLPVQTVGVMGDGRTYEFVCALRAVTSVDGMTADFYPHDMDFLSRTAARIINEVRGINRVVYDITSKPPGTIEWE | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 57267
Sequence Length: 518
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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C5CBZ4 | MTQNAPHPDTPAPLSDVMPTVLVLDFGAQYAQLIARRVREANVYSEVVPASTPAAQILEREPAALILSGGPSSVYEPGAPQLDPALLEAGVPVLGLCYGFQSIAHALGGTVAQTGTREYGSTRLDSVDADSVLFADQDLEQVVWMSHGDAVTQAPEGFAVTASTAGAPVAAFEDRERRIYGVQWHPEVGHSSRGQRVLEQFLHEGAGLGADWTASGVIEEQVERIREQIGDKRAICGLSGGVDSAVAAALVQRAIGDRLTCVYVDHGLMREGESAEIEQAFGEAHGGARLVMVDAREDFLSALAGVTDPEAKRKIIGERFIRTFEKAQADIVLESEHDPDATEVRFLVQGTLYPDVVESGGGDGAANIKSHHNVGGLPDDIEFELCEPLRELFKDEVRAVGAELGLPEGIVHRQPFPGPGLGIRIIGEVTQERLDLLRRADAIVRAELTAAGLDRQIWQCPVVLLADVRSVGVQGDGRTYGHPVVLRPVTSEDAMTADWARIPDDVLSRISNRITNEVDGVNRVVLDVTSKPPGTIEWE | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 57843
Sequence Length: 539
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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P9WMS6 | MVQPADIDVPETPARPVLVVDFGAQYAQLIARRVREARVFSEVIPHTASIEEIRARQPVALVLSGGPASVYADGAPKLDPALLDLGVPVLGICYGFQAMAQALGGIVAHTGTREYGRTELKVLGGKLHSDLPEVQPVWMSHGDAVTAAPDGFDVVASSAGAPVAAFEAFDRRLAGVQYHPEVMHTPHGQQVLSRFLHDFAGLGAQWTPANIANALIEQVRTQIGDGHAICGLSGGVDSAVAAALVQRAIGDRLTCVFVDHGLLRAGERAQVQRDFVAATGANLVTVDAAETFLEALSGVSAPEGKRKIIGRQFIRAFEGAVRDVLDGKTAEFLVQGTLYPDVVESGGGSGTANIKSHHNVGGLPDDLKFTLVEPLRLLFKDEVRAVGRELGLPEEIVARQPFPGPGLGIRIVGEVTAKRVDTLRHADSIVREELTAAGLDNQIWQCPVVLLADVRSVGVQGDGRTYGHPIVLRPVSSEDAMTADWTRVPYEVLERISTRITNEVAEVNRVVLDITSKPPATIEWE | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 56046
Sequence Length: 525
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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Q5SI28 | MVLVLDFGSQYTRLIARRLRELRAFSLILPGDAPLEEVLKHRPQALILSGGPRSVFDPDAPRPDPRLFSSGLPLLGICYGMQLLAQELGGRVERAGRAEYGKALLTRHEGPLFRGLEGEVQVWMSHQDAVTAPPPGWRVVAETEENPVAAIASPDGRAYGVQFHPEVAHTPKGMQILENFLELAGVKRDWTPEHVLEELLREVRERAGKDRVLLAVSGGVDSSTLALLLAKAGVDHLAVFVDHGLLRLGEREEVEGALRALGVNLLVVDAKERFLKALKGVEDPEEKRKIIGREFVAAFSQVARERGPFRFLAQGTLYPDVIESAGGHGAAKIKSHHNVGGLPEDLEFELLEPFRLLFKDEVRELALLLGLPDTLRLRHPFPGPGLAVRVLGEVTEERLEILRRADDIFTSLLREWGLYEKVAQALAVLTPVRSVGVAGDERKYGYVLALRAVTTEDFMTADWARLPLEFLDEAARRITRRVPEIGRVVYDLTSKPPATIEWE | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 55817
Sequence Length: 503
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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Q73LZ4 | MKKKPLSAKIVFMKITEKILIVDFGGQYNQLIARRVRDLNVYSDIVPASKALDYIRENKPIGIIFTGGPNSVYEEKAPLPPKEIFNLNIPILGICYGMQAMAHCLGGKVEKSLKREFGKTLTKFDTGIPLFKNIKDKSSVWMSHVDCVSRLPEGFVSAAQTANTKNAAMANKEKKLYGIQFHAEVEHSEEGQNIIKNFLYNVCGAKGDWNMKSFLAEAIKDVQNTVKDGKVLLALSGGVDSSVLAALLNRAVGKNLTCIFVDHGLMRKNEGDEVEAAFRDTPMNFIRVNAESRFLGKLKGVSDPEKKRKIIGEEFIRVFEEEAEKIGTVDFLAQGTIYADVVESGTKGSAVIKSHHNVGGLPDHISFKSLIEPLKTLFKDEIRNLGTELGLPDYLVHRQPFPGPGLAIRIMGEITEEKLDILREADAIWRSELEHADIKKDLSQYFAVLTSTKTVGVMGDFRTYDYTLALRAVKTSDFMSADWVRIPYEVLDKVSSRIINEVKGINRIVYDITSKPPATIEWE | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 58365
Sequence Length: 523
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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Q83GZ6 | MRPVLVVDFGSQYSQLVVRAIRECGYYAEFASPSISAAECLALSPIAIFLSGGPASAYKDNAPKLDEEILNCGIPVFGICYGFQLLAQAFGGSVKKANAPEYGPADITIVNKAFFSGQPDRQTVWMSHGDSVIRAPKNFCILSTSQDAVLSFCNRDRTIAGVQWHPEVKHSRFGKHTIKAFLSSFAAPNWDPEQTICGTVDSIRKTVGCKRVLCALSGGVDSVVAATLTHRAIGDRLRCVFVDHGLLRLNEREQVEEYCSSLGLNVSTYDASDCFLSALSGIRDSEQKRKVIGREFIACFSKLQERFDIKPHFLLQGTLYPDLVESGATPGGATIKSHHNVGGLSDNLGFELLEPLKYLFKDEVRKIGLQLGIPKHIVHRQPFPGPGLAIRIIGEVTNKKLSILRAADAIVRHELRDWTDIWQCPVILLSDVQSVGVRGDSRSCGFPIVIRPVSSDDAMTADWYRLPYDVLARISGRITNEIPEIVRVVLDITPKPPATIEWE | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 55329
Sequence Length: 503
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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Q4P763 | MTEAIHSQYDSILILDFGSQYSHLITRRCRELNVYCEMLPCTQKIKDLDWKPKGIILSGSPYSVYDEVAPRVDPDVFTAGVPVLGICYGLQEIAWNHGGKVDPHDKREYGHAMVEVVKHGVPHLDALFKNWEGSVQVWMSHGDQLSKAPEDFVVIAKTPTAPFAAMAHKSKPIYGVQFHPEVTHSLRGVELFDSFVDICACRRDWTMETFIDKEIKRIREIVGPKGQVLGAISGGVDSSVAAKLMHEAIGDRFHAVMVDNGVLRTNEAAQVYEMLSKDLGVNLTVVDASEQFLSRLKDVEDPEQKRKIIGNTFIHVFEAEVAKLEKQAEDEEAAALAAGKPQEAKGKFEYLLQGTLYPDVIESISFKGPSATIKTHHNVGGLLEDMKLKLIEPLRELFKDEVRALGKLLGIPAHLVGRHPFPGPGLAIRILGPVTREQVKILQHADSIYIDEIRAAGLYDQISQAFAVLLPVRAVGVQGDKRTYDQVIALRAAATTDFMTATWYPFPAEFLSKVSNRITNEVQGVNRVVLDISSKPPATIEWL | Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 60291
Sequence Length: 543
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.5.2
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Q8D1V0 | MNNQYILIIDFGSQYTKLVARRMKDIGAKFIISSWEIKKKELLKKNIKGILLSGSPMSVLDDKSPYVSKDILNMKVPILGICYGMHTLVKQLGGKVERKSVREFGYASIKILKNHSNLFYDNFEVSEKNYTKRQKVWMSHEDSVINIPKGFSIIASTKNCKYAAIFNKKNKFYGVQFHPEVTHSEKGYLILNRFVKNICNYTNVIKYSLSIRKIILKIKNKVNDEKVILGLSGGIDSFTSAILIHKAIGNNLFCICIDNGLLRNDEILKIKNLIKKVGKINVIYINHKKRFLKSLNGITDPEKKRKTIGNLFFKIFQEQADILKAKWLAQGTIYPDIIESSQNNLLKKDNFIKSHHNVCPLPKGIKLKILEPLKHLFKDEVKKIAKKIGIPKEIIFRHPFPGPGLAVRIIGEIKEEYCNILRMADEIFISELKSENLYFNISQAFSVLLPIKSVAVMGDMRKYEWVISLRAIETLDFMSANWANIPYKILNNVSNRIINEVRGISRVVYDISNKPPSTIEWE | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 59960
Sequence Length: 522
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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Q00328 | MYRTLAFASLSLYGAARAQQVGTSTAENHPKLTWQTCTGTGGTNCSNKSGSVVLDSNWRWAHNVGGYTNCYTGNSWSTQYCPDGDSCTKNCAIDGADYSGTYGITTSNNALSLKFVTKGSFSSNIGSRTYLMETDTKYQMFNLINKEFTFDVDVSKLPCGLNGALYFVEMAADGGIGKGNNKAGAKYGTGYCDSQCPHDIKFINGKANVEGWNPSDADPNGGAGKIGACCPEMDIWEANSISTAYTPHPCRGVGLQECSDAASCGDGSNRYDGQCDKDGCDFNSYRMGVKDFYGPGATLDTTKKMTVITQFLGSGSSLSEIKRFYVQNGKVYKNSQSAVAGVTGNSITESFCTAQKKAFGDTSSFAALGGLNEMGASLARGHVLIMSLWGDHAVNMLWLDSTYPTDADPSKPGAARGTCPTTSGKPEDVEKNSPDATVVFSNIKFGPIGSTFAQPA | Function: The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
Catalytic Activity: Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
Sequence Mass (Da): 48304
Sequence Length: 456
EC: 3.2.1.91
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P15828 | MRTAKFATLAALVASAAAQQACSLTTERHPSLSWNKCTAGGQCQTVQASITLDSNWRWTHQVSGSTNCYTGNKWDTSICTDAKSCAQNCCVDGADYTSTYGITTNGDSLSLKFVTKGQHSTNVGSRTYLMDGEDKYQTFELLGNEFTFDVDVSNIGCGLNGALYFVSMDADGGLSRYPGNKAGAKYGTGYCDAQCPRDIKFINGEANIEGWTGSTNDPNAGAGRYGTCCSEMDIWEANNMATAFTPHPCTIIGQSRCEGDSCGGTYSNERYAGVCDPDGCDFNSYRQGNKTFYGKGMTVDTTKKITVVTQFLKDANGDLGEIKRFYVQDGKIIPNSESTIPGVEGNSITQDWCDRQKVAFGDIDDFNRKGGMKQMGKALAGPMVLVMSIWDDHASNMLWLDSTFPVDAAGKPGAERGACPTTSGVPAEVEAEAPNSNVVFSNIRFGPIGSTVAGLPGAGNGGNNGGNPPPPTTTTSSAPATTTTASAGPKAGRWQQCGGIGFTGPTQCEEPYICTKLNDWYSQCL | Function: The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
Catalytic Activity: Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
Sequence Mass (Da): 55694
Sequence Length: 525
EC: 3.2.1.91
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P62694 | MYRKLAVISAFLATARAQSACTLQSETHPPLTWQKCSSGGTCTQQTGSVVIDANWRWTHATNSSTNCYDGNTWSSTLCPDNETCAKNCCLDGAAYASTYGVTTSGNSLSIGFVTQSAQKNVGARLYLMASDTTYQEFTLLGNEFSFDVDVSQLPCGLNGALYFVSMDADGGVSKYPTNTAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNANTGIGGHGSCCSEMDIWEANSISEALTPHPCTTVGQEICEGDGCGGTYSDNRYGGTCDPDGCDWNPYRLGNTSFYGPGSSFTLDTTKKLTVVTQFETSGAINRYYVQNGVTFQQPNAELGSYSGNELNDDYCTAEEAEFGGSSFSDKGGLTQFKKATSGGMVLVMSLWDDYYANMLWLDSTYPTNETSSTPGAVRGSCSTSSGVPAQVESQSPNAKVTFSNIKFGPIGSTGNPSGGNPPGGNRGTTTTRRPATTTGSSPGPTQSHYGQCGGIGYSGPTVCASGTTCQVLNPYYSQCL | Function: Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose (Ref.4). The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds in cellulose to reduce the polymerization degree of the substrate and create new chain ends for exocellobiohydrolases (CBHs). The CBHs release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units (Probable).
PTM: N-glycosylated. The catalytic core domain comprises three N-linked glycans which each consist of a single N-acetylglucosamine residue.
Catalytic Activity: Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
Sequence Mass (Da): 54073
Sequence Length: 513
Domain: The enzyme consists of two functional domains, a catalytic core joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-, and proline-rich, highly glycosylated linker sequence.
Subcellular Location: Secreted
EC: 3.2.1.91
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P13860 | MFRTATLLAFTMAAMVFGQQVGTNTARSHPALTSQKCTKSGGCSNLNTKIVLDANWRWLHSTSGYTNCYTGNQWDATLCPDGKTCAANCALDGADYTGTYGITASGSSLKLQFVTGSNVGSRVYLMADDTHYQMFQLLNQEFTFDVDMSNLPCGLNGALYLSAMDADGGMAKYPTNKAGAKYGTGYCDSQCPRDIKFINGEANVEGWNATSANAGTGNYGTCCTEMDIWEANNDAAAYTPHPCTTNAQTRCSGSDCTRDTGLCDADGCDFNSFRMGDQTFLGKGLTVDTSKPFTVVTQFITNDGTSAGTLTEIRRLYVQNGKVIQNSSVKIPGIDPVNSITDNFCSQQKTAFGDTNYFAQHGGLKQVGEALRTGMVLALSIWDDYAANMLWLDSNYPTNKDPSTPGVARGTCATTSGVPAQIEAQSPNAYVVFSNIKFGDLNTTYTGTVSSSSVSSSHSSTSTSSSHSSSSTPPTQPTGVTVPQWGQCGGIGYTGSTTCASPYTCHVLNPYYSQCY | Function: The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
Catalytic Activity: Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
Sequence Mass (Da): 54858
Sequence Length: 516
Subcellular Location: Secreted
EC: 3.2.1.91
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Q9P8P3 | MYRKLAVISAFLAAARAQQVCTQQAETHPPLTWQKCTASGCTPQQGSVVLDANWRWTHDTKSTTNCYDGNTWSSTLCPDDATCAKNCCLDGANYSGTYGVTTSGDALTLQFVTASNVGSRLYLMANDSTYQEFTLSGNEFSFDVDVSQLPCGLNGALYFVSMDADGGQSKYPGNAAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNANTGVGGHGSCCSEMDIWEANSISEALTPHPCETVGQTMCSGDSCGGTYSNDRYGGTCDPDGCDWNPYRLGNTSFYGPGSSFALDTTKKLTVVTQFATDGSISRYYVQNGVKFQQPNAQVGSYSGNTINTDYCAAEQTAFGGTSFTDKGGLAQINKAFQGGMVLVMSLWDDYAVNMLWLDSTYPTNATASTPGAKRGSCSTSSGVPAQVEAQSPNSKVIYSNIRFGPIGSTGGNTGSNPPGTSTTRAPPSSTGSSPTATQTHYGQCGGTGWTGPTRCASGYTCQVLNPFYSQCL | Function: Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose . The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds in cellulose to reduce the polymerization degree of the substrate and create new chain ends for exocellobiohydrolases (CBHs). The CBHs release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units (Probable).
PTM: O-glycosylated. O-glycosylation of the cellulase linker provides protection from proteolysis. Linker glycans also contribute to binding affinity of cellobiohydrolases to cellulose.
Catalytic Activity: Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
Sequence Mass (Da): 53216
Sequence Length: 505
Domain: The enzyme consists of two functional domains, a catalytic core joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-, and proline-rich, highly glycosylated linker sequence.
Subcellular Location: Secreted
EC: 3.2.1.91
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Q92400 | MFPRSILLALSLTAVALGQQVGTNMAENHPSLTWQRCTSSGCQNVNGKVTLDANWRWTHRINDFTNCYTGNEWDTSICPDGVTCAENCALDGADYAGTYGVTSSGTALTLKFVTESQQKNIGSRLYLMADDSNYEIFNLLNKEFTFDVDVSKLPCGLNGALYFSEMAADGGMSSTNTAGAKYGTGYCDSQCPRDIKFIDGEANSEGWEGSPNDVNAGTGNFGACCGEMDIWEANSISSAYTPHPCREPGLQRCEGNTCSVNDRYATECDPDGCDFNSFRMGDKSFYGPGMTVDTNQPITVVTQFITDNGSDNGNLQEIRRIYVQNGQVIQNSNVNIPGIDSGNSISAEFCDQAKEAFGDERSFQDRGGLSGMGSALDRGMVLVLSIWDDHAVNMLWLDSDYPLDASPSQPGISRGTCSRDSGKPEDVEANAGGVQVVYSNIKFGDINSTFNNNGGGGGNPSPTTTRPNSPAQTMWGQCGGQGWTGPTACQSPSTCHVINDFYSQCF | Function: The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
Catalytic Activity: Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
Sequence Mass (Da): 54320
Sequence Length: 506
EC: 3.2.1.91
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Q8GWW4 | MTIMTMIMKMAPSKSALIRFNLVLLGFSFLLYTAIFFHPSSSVYFSSGASFVGCSFRDCTPKVVRGVKMQELVEENEINKKDLLTASNQTKLEAPSFMEEILTRGLGKTKIGMVNMEECDLTNWKRYGETVHIHFERVSKLFKWQDLFPEWIDEEEETEVPTCPEIPMPDFESLEKLDLVVVKLPCNYPEEGWRREVLRLQVNLVAANLAAKKGKTDWRWKSKVLFWSKCQPMIEIFRCDDLEKREADWWLYRPEVVRLQQRLSLPVGSCNLALPLWAPQGVDKVYDLTKIEAETKRPKREAYVTVLHSSESYVCGAITLAQSLLQTNTKRDLILLHDDSISITKLRALAAAGWKLRRIIRIRNPLAEKDSYNEYNYSKFRLWQLTDYDKVIFIDADIIVLRNLDLLFHFPQMSATGNDVWIYNSGIMVIEPSNCTFTTIMSQRSEIVSYNGGDQGYLNEIFVWWHRLPRRVNFLKNFWSNTTKERNIKNNLFAAEPPQVYAVHYLGWKPWLCYRDYDCNYDVDEQLVYASDAAHVRWWKVHDSMDDALQKFCRLTKKRRTEINWERRKARLRGSTDYHWKINVTDPRRRRSYLIG | Function: Glycosyltransferase required for the addition of both glucuronic acid and 4-O-methylglucuronic acid branches to xylan in stem cell walls. In association with GUX1, is responsible for almost all of the substitutions of the xylan backbone in stem glucuronoxylan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 70059
Sequence Length: 596
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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P49075 | MFKFAALLALASLVPGFVQAQSPVWGQCGGNGWTGPTTCASGSTCVKQNDFYSQCLPNNQAPPSTTTQPGTTPPATTTSGGTGPTSGAGNPYTGKTVWLSPFYADEVAQAAADISNPSLATKAASVAKIPTFVWFDTVAKVPDLGGYLADARSKNQLVQIVVYDLPDRDCAALASNGEFSLANDGLNKYKNYVDQIAAQIKQFPDVSVVAVIEPDSLANLVTNLNVQKCANAQSAYKEGVIYAVQKLNAVGVTMYIDAGHAGWLGWPANLSPAAQLFAQIYRDAGSPRNLRGIATNVANFNALRASSPDPITQGNSNYDEIHYIEALAPMLSNAGFPAHFIVDQGRSGVQNIRDQWGDWCNVKGAGFGQRPTTNTGSSLIDAIVWVKPGGECDGTSDNSSPRFDSHCSLSDAHQPAPEAGTWFQAYFETLVANANPAL | Function: Shows enzymatic activity towards crystalline cellulose. At long reaction times. It is also able to degrade carboxymethyl cellulose and barley B-glucan.
Catalytic Activity: Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
Sequence Mass (Da): 46210
Sequence Length: 438
EC: 3.2.1.91
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Q8W4A7 | MIPSSSPMESRHRLSFSNEKTSRRRFQRIEKGVKFNTLKLVLICIMLGALFTIYRFRYPPLQIPEIPTSFGLTTDPRYVATAEINWNHMSNLVEKHVFGRSEYQGIGLINLNDNEIDRFKEVTKSDCDHVALHLDYAAKNITWESLYPEWIDEVEEFEVPTCPSLPLIQIPGKPRIDLVIAKLPCDKSGKWSRDVARLHLQLAAARVAASSKGLHNVHVILVSDCFPIPNLFTGQELVARQGNIWLYKPNLHQLRQKLQLPVGSCELSVPLQAKDNFYSAGAKKEAYATILHSAQFYVCGAIAAAQSIRMSGSTRDLVILVDETISEYHKSGLVAAGWKIQMFQRIRNPNAVPNAYNEWNYSKFRLWQLTEYSKIIFIDADMLILRNIDFLFEFPEISATGNNATLFNSGLMVVEPSNSTFQLLMDNINEVVSYNGGDQGYLNEIFTWWHRIPKHMNFLKHFWEGDEPEIKKMKTSLFGADPPILYVLHYLGYNKPWLCFRDYDCNWNVDIFQEFASDEAHKTWWRVHDAMPENLHKFCLLRSKQKAQLEWDRRQAEKGNYKDGHWKIKIKDKRLKTCFEDFCFWESMLWHWGETNSTNNSSTTTTSSPPHKTALPSL | Function: May be involved in the substitutions of the xylan backbone in stem glucuronoxylan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 71487
Sequence Length: 618
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q9FZ37 | MGTKTHNSRGKIFMIYLILVSLSLLGLILPFKPLFRITSPSSTLRIDLPSPQVNKNPKWLRLIRNYLPEKRIQVGFLNIDEKERESYEARGPLVLKNIHVPLDHIPKNVTWKSLYPEWINEEASTCPEIPLPQPEGSDANVDVIVARVPCDGWSANKGLRDVFRLQVNLAAANLAVQSGLRTVNQAVYVVFIGSCGPMHEIFPCDERVMRVEDYWVYKPYLPRLKQKLLMPVGSCQIAPSFAQFGQEAWRPKHEDNLASKAVTALPRRLRVAYVTVLHSSEAYVCGAIALAQSIRQSGSHKDMILLHDHTITNKSLIGLSAAGWNLRLIDRIRSPFSQKDSYNEWNYSKLRVWQVTDYDKLVFIDADFIILKKLDHLFYYPQLSASGNDKVLFNSGIMVLEPSACMFKDLMEKSFKIESYNGGDQGFLNEIFVWWHRLSKRVNTMKYFDEKNHRRHDLPENVEGLHYLGLKPWVCYRDYDCNWDISERRVFASDSVHEKWWKVYDKMSEQLKGYCGLNKNMEKRIEKWRRIAKNNSLPDRHWEIEVRDPRKTNLLVQ | Function: May be involved in the substitutions of the xylan backbone in stem glucuronoxylan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 64709
Sequence Length: 557
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q8GWB7 | MVRLKTSLWVLLLALVSIQLNGSFGSESSKVAYVTLLYGDEFLLGVRVLGKSIRDTGSTKDMVALVSDGVSDYSKKLLKADGWKVEKISLLANPNQVHPTRFWGVYTKLKIFNMTDYKKVVYLDADTIVVKNIEDLFKCSKFCANLKHSERLNSGVMVVEPSEALFNDMMRKVKTLSSYTGGDQGFLNSYYPDFPNARVFDPSVTPEVLKTRPVPAMERLSTLYNADVGLYMLANKWMVDDSKLHVIHYTLGPLKPWDWWTAWLVKPVDAWHSIRVKLEETLPGTGGGSNQHDELVVKFLFLLPLCALLFCIYRSIQGREGSLCWSSFSNQIRYLYYKVRSNGTLGYGGVSTMSPSYQPHSGNAQSKVPQHLGAVSVVVCFTAVLLSLGISFAIVPRQIMPWTGLVLVYEWTFTIFFLLFGVFLLFVHQHGKRIAIQSESSSLDDSAKVHQRAGGSCDVTTLYYGLGMAFLAIAAVSLPYILGITALFTRLGLMVGLAIILAAFMTYASEHLAVRWFLKGLEDRRDTTRSNSLCFLC | Function: Mediates the transfer of glucuronic acid (GlcA) from UDP-GlcA to glycosyl inositol phosphorylceramides (GIPCs) . The formation of GIPCs sphingolipids is essential for pollen function, plant growth and defense . Required for global fitness .
Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60011
Sequence Length: 537
Pathway: Sphingolipid metabolism.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.17
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D5ECW5 | MEEKKGEPLFGKVVPLPLVEEIKHSYLDYAMSVIVGRALPDARDGLKPVQRRILYAMMELGLRHNTAYKKSARVVGETMGKYHPHGDSAIYDTMVRMAQDFSMRYPLVDGQGNFGSIDGDPAAAMRYTEARLYEIGELMLADIDQDTVDWGPNFDESLQEPLCLPAMLPNLLINGSSGIAVGMATNIPPHNLVEVVDALCYLIDTEPEQVDIGEILFRMPGPDFPTGGLILGRDGIIDAYRTGRGKITMRGRTHIEEGKRGKTFIVITEIPYMVNKTNLIETIAKNVQDKTIDGVMDLRDESDREGLRIVIEVNRDTDPNLVLRQLYRRTQLQSTFGVINLALIDGYPKELSIEEMLNIFLNHRRSVVRRRTQFRLEKAEARAHIVEGLVKALDIIDEVIALIRGSATTEEAKEGLISKLDFSEAQAQAILEMRLQRLTGLEREKLEAELAQLLSDIERYQTILGNPKVLDSVIKEELLEVKRRFGNERKTEIIDAVEDVSIEDLIPESDIVVVLSRDGYLRRKDLQEYTLQGRGGKGRKGTALQEEDEVALVAVTSTHRDIYLFTSKGRVLALKGYVIPESKTGRGKLINRFVALEEGERVVTMHGRAVDGAKYAFFITLRGTAKRLDLSELENLTRAGRRVMGLDEGDEISQIVLTSGDDHLLIVTAQGQALRTHESEFRPMGRTARGVRGIRLRKNDYVIGCDVVANGRWPLLLSENGFGKRTKYDEFSLRHRGGSGVIVMNLSDRTGLIVGCWSVAEGDEIVAITSRGRMIRLAVSESPVLGRTAMGSIMMRLDEGDTVATASVVSTEDGEDD | Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 91065
Sequence Length: 817
Subcellular Location: Cytoplasm
EC: 5.6.2.2
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Q9CAF6 | MTPVLCHSTASIPNPNSLMSLSSTLRLSSSLLRRSFFRFPLTDPLCRLRRTEPSATRFFSSRTPRSGKFVVGAGKRGDEQVKEESGANNGGLVVSGDESRIVPFELHKEATESYMSYALSVLLGRALPDVRDGLKPVHRRILFAMHELGMSSKKPYKKCARVVGEVLGKFHPHGDTAVYDSLVRMAQSFSLRCPLIQGHGNFGSIDADPPAAMRYTECRLDPLAEAVLLSDLDQDTVDFVANFDNSQKEPAVLPARLPALLLNGASGIAVGMATNIPPHNLGELVDVLCALIHNPEATLQELLEYMPAPDFPTGGIIMGNLGVLDAYRTGRGRVVVRGKAEVELLDPKTKRNAVIITEIPYQTNKATLVQKIAELVENKTLEGISDIRDESDRNGMRVVIELKRGGDPALVLNNLYRHTALQSSFSCNMVGICDGEPKLMGLKELLQAFIDFRCSVVERRARFKLSHAQQRKHIIEGIVVGLDNVDEVIELITKASSHSSATAALQSEYGLSEKQAEAILEITLRRLTALERKKFTDESSSLTEQITKLEQLLSTRTNILKLIEQEAIELKDRFSSPRRSMLEDSDSGDLEDIDVIPNEEMLMAVSEKGYVKRMKADTFNLQHRGTIGKSVGKLRVDDAMSDFLVCHAHDHVLFFSDRGIVYSTRAYKIPECSRNAAGTPLVQILSMSEGERVTSIVPVSEFAEDRYLLMLTVNGCIKKVSLKLFSGIRSTGIIAIQLNSGDELKWVRCCSSDDLVAMASQNGMVALSTCDGVRTLSRNTKGVTAMRLKNEDKIASMDIIPASLRKDMEEKSEDASLVKQSTGPWLLFVCENGYGKRVPLSSFRRSRLNRVGLSGYKFAEDDRLAAVFVVGYSLAEDGESDEQVVLVSQSGTVNRIKVRDISIQSRRARGVILMRLDHAGKIQSASLISAADEEETEGTLSNEAVEAVSL | Function: A type II topoisomerase that negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 104538
Sequence Length: 950
Subcellular Location: Plastid
EC: 5.6.2.2
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O51396 | MAVGENKEQILNVRIEDEIKTSYLNYAMSVIVSRALPDVRDGLKPVHRRILYSMYEMGLRSDKAFKKAGRIVGDVLGKYHPHGDQSIYDALVRLAQDFSLRYPVIRGQGNFGSIDGDPPAAMRYTEAKMEKITEYIVKDIDKETVNFKSNYDDSLSEPEIMPSSFPFLLVNGSSGIAVGMATNMAPHNLREICDAIVYMLDNENASIFDLLKIVKGPDFPTFGEIVYNDNLIKAYKTGKGSVVIRARYHIEERAEDRNAIIVTEIPYTVNKSALLMKVALLAKEEKLEGLLDIRDESDREGIRIVLEVKRGFDPHVIMNLLYEYTEFKKHFSINNLALVNGIPKQLNLEELLFEFIEHRKNIIERRIEFDLRKAKEKAHVLEGLNIALNNIDEVIKIIKSSKLAKDARERLVSNFGLSEIQANSVLDMRLQKLTALEIFKLEEELNILLSLIKDYEDILLNPVRIINIIREETINLGLKFGDERRTKIIYDEEVLKTSMSDLMQKENIVVMLTKKGFLKRLSQNEYKLQGTGGKGLSSFDLNDGDEIVIALCVNTHDYLFMISNEGKLYLINAYEIKDSSRASKGQNISELINLGDQEEILTIKNSKDLTDDAYLLLTTASGKIARFESTDFKAVKSRGVIVIKLNDKDFVTSAEIVFKDEKVICLSKKGSAFIFNSRDVRLTNRGTQGVCGMKLKEGDLFVKVLSVKENPYLLIVSENGYGKRLNMSKISELKRGATGYTSYKKSDKKAGSVVDAIAVSEDDEILLVSKRSKALRTVAGKVSEQGKDARGIQVLFLDNDSLVSVSKFIK | Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state . Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 91379
Sequence Length: 810
Domain: The C-terminal domain (CTD, residues 499-810) contains 6 tandemly repeated subdomains known as blades, each of which is composed of a 4-stranded antiparallel beta-sheet. The blades form a flat, toroidal beta-pinwheel fold, to which DNA probably binds, inducing mild positive superhelicity (about 0.3 links/protein) .
Subcellular Location: Cytoplasm
EC: 5.6.2.2
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C0R046 | MAVKKNKEDNSEERQYSTLTKDILKRVDHISIENELRESYLTYAMSVIVSRALPDVRDGLKPVHRRILYAMYDANLTHDKPYKKSAATVGEVLARYHPHGDAAVYGTMVRMAQDFSMRYLLVDGQGNFGSIDDDPPAAMRYTEARMTRFAEEMLNDIEKETVKFVPNFDDSRTEPSVLPATVPQLLVNGSMGIAIGMATNMPPHNLKEVVNAIVYYIDHQDAEIKDLMRYVQGPDFPTAGIIYGKEGIKEAYTTGKGRIKLRARLEVEETKRDREAIVVKELPYGVVKTTLHEKIADLVKQGKIEGVADIRDESSNRAGIRLIIELKKGVATQIVLNQLWKHTDLETTFGIINLALVNGEPKVLNLKELIKYFVDHRVEVITKRTEYDLNQAKAKAHILEGLLIAQANIEEVIRIIRESENTDAARTTLMNRFKLSEKQAQAILDMPLKRLTALEKLKIEQELQQLREFIAYCEDLLAHPEKILAVIKDELKKISEKYGDDRRSEIIGKTNDTEIDEEDLIHDEDVAVSITTQGFIKRVPASSYRTQGRGGVGVQGGKSQGEHYIEHLFVASTKDYLFIFTDRGKAFWMKVHEIPALSKISQGKSIKFILNLAPEEKITSYFTVSEFDPKQSIIMVTKMGTIKKMELKHLENAKKRGILALTLENNDELVAVSPVQTGDDFIMTTAAGLALRITEEKIRKMGRAAAGVKGISLDDDDICVSGNAIHKGESLIVITENGIGKRLSSKQFNVKGRGGKGQIYIKPDNKTGNVVSVKTVGDKDEIMVVTTDDMTIKIKADSIPELGRNAKGVKIVNISDGARVSDLAVVPADNEEKK | Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 93275
Sequence Length: 834
Subcellular Location: Cytoplasm
EC: 5.6.2.2
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P57277 | MKDPSREIIQVNIEEELKSSYLDYSMSVIVGRALPDVRDGLKPVHRRILFAMYILNNDWNKAYKKSARIVGDVIGKYHPHGDSAVYDAIVRMAQKFSLRYMLIDGQGNFGSVDGDSAAAMRYTEVRMSKIAHELLNDLEKNTVEFLPNYDGTEYIPEILPAKIPNLLINGSSGIAVGMATNIPPHNLNEVINGCLAYIDNNDITLEELIKHIPGPDFPTAAIINGKSGIEEAYRTGKGKIYIRAQNQIEKNKKNKKESIVFNEIPYQVNKSRLIEKIAELVKEKRIDGITALRDESDKDGMRIVIEIKREAIAEVILNQLYSLTQLQISFGINMVALCQGQPKTLSLKEILKNFLSHRQEIIIRRSLFELNKVRNRIHILEGLNMALININAIIEIIKNSVNSIDAKKIIIQKNWKSEKINYLAKKHEYYFSEKQAQAILDLRLHKITNLEQEKIIMEHNDLIKKTKELKEILENPKKMFEVIKSELLSIQNNFSDKRRTKITENHSDINMEDLINQEDVVVTLSHSGYVKYQPLSDYNAQRRGGKGKSAAKIKEEDFIESLVIANTHDTILCFSSRGILYWMKVYQLPESSRHARGRPIVNLLPLSPKERITAILPVHKYQDNLNIFMTTAHGIVKKSSLSQFKKPRFAGIIAINLHANDELIGVALTDGNNNIMLFTQNGKVVQFLENSVRTMGRTASGVKGIKIKKNDKVVSLIVPKNKGSILIATKNGYGKRTKISDFPIKSRATQGVISIKITKKNGKIIGAIQVIEKDQIMMITDAGTLVRIRVSEVGVLKRNTQGVILIRTSKNEKVVALQKIVDPMIEKIDL | Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 93879
Sequence Length: 830
Subcellular Location: Cytoplasm
EC: 5.6.2.2
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Q89AS3 | MKEVAKEIIKIDIEDELKNSYLDYAMSVIIGRALPDVRDGLKPVHRRILFAMKVLNNDWNKTYKKSARIVGDVIGKYHPHGDTAVYDAIVRMAQPFSLRYVLIDGQGNFGSIDGDSAAAMRYTEIRMSKIAYELLNDLDKNTVSFFSNYDGTEKIPEVLPAKIPNLLINGSSGIAVGMATNIPPHNIKEVINGCLAFIDDQNITLKKLMEHIPGPDFPTAGLINGKRGIEKAYKTGKGKIYIRAKSIIEIQKKTKKKSIIIYELPYQVNKARVIKGIANLVKEKKIEGITTLRDESDKEGMRIVIEIKKETKAEIILNQLYSLTQLEISFGINMVALIHGQPKVMTLKEILNAFINHRRKIIMRRSLFELNKIRKKIHILEGLIISLDNIDLIINLIKKSSTLEEAKNKLKTYHWYSKHAQYTQILKKNAHSLTPYDKKLRPIDTQKFFLTPEQIQAILELRLQKLTHLEHKKLISEYKQLFKTSNNLENILKNNNILTKIMKDELIKIRDNFGDKRRTKINVNYSDINTSDLINKENVVITLSYSGYVKYQLLSSYEAQKRGGKGKLAVKTKEEDFIENLLVANTHDIILCFSSKGILYWMKVYQLPEASRHARGRPIVNLLPLSSNERITAILPISEYKDSINIFMATSKGMVKKTSLYEFKKPRTKGIIAINLKADDELIGVSLTNGNNTIMLFTAQGKAVHFSEILVRKTGRTAIGVQGIKIKKSDKVVSLVVPKKHGNILLITEHGYGKRTEIHEFPIKSRATQGTIAMKITKKNGIVIGTMQVVNQDQIIIITNAGTLVRTRVLEIGILGRNTQGVIIIRTSKKEKVVALQKANALHLNSV | Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 95830
Sequence Length: 847
Subcellular Location: Cytoplasm
EC: 5.6.2.2
|
Q03470 | MENIFSKDSDIELVDIENSIKSSYLDYSMSVIIGRALPDARDGLKPVHRRILYAMQNDEAKSRTDFVKSARIVGAVIGRYHPHGDTAVYDALVRMAQDFSMRYPSITGQGNFGSIDGDSAAAMRYTEAKMSKLSHELLKDIDKDTVDFVPNYDGSESEPDVLPSRVPNLLLNGSSGIAVGMATNIPPHSLNELIDGLLYLLDNKDASLEEIMQFIKGPDFPTGGIIYGKKGIIEAYRTGRGRVKVRAKTHIEKKTNKDVIVIDELPYQTNKARLIEQIAELVKERQIEGISEVRDESNKEGIRVVIELKREAMSEIVLNNLFKSTTMESTFGVIMLAIHNKEPKIFSLLELLNLFLTHRKTVIIRRTIFELQKARARAHILEGLKIALDNIDEVIALIKNSSDNNTARDSLVAKFGLSELQANAILDMKLGRLTGLEREKIENELAELMKEIARLEEILKSETLLENLIRDELKEIRSKFDVPRITQIEDDYDDIDIEDLIPNENMVVTITHRGYIKRVPSKQYEKQKRGGKGKLAVTTYDDDFIESFFTANTHDTLMFVTDRGQLYWLKVYKIPEGSRTAKGKAVVNLINLQAEEKIMAIIPTTDFDESKSLCFFTKNGIVKRTNLSEYQNIRSVGVRAINLDENDELVTAIIVQRDEDEIFATGGEENLENQEIENLDDENLENEESVSTQGKMLFAVTKKGMCIKFPLAKVREIGRVSRGVTAIKFKEKNDELVGAVVIENDEQEILSISAKGIGKRTNAGEYRLQSRGGKGVICMKLTEKTKDLISVVIVDETMDLMALTSSGKMIRVDMQSIRKAGRNTSGVIVVNVENDEVVSIAKCPKEENDEDELSDENFGLDLQ | Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 96974
Sequence Length: 863
Subcellular Location: Cytoplasm
EC: 5.6.2.2
|
O84192 | MLNKEEIIVPKNLEEEMKESYLRYSMSVIISRALPDARDGLKPSQRRILYAMKQLNLTPGVKHRKCAKICGDTSGDYHPHGESVIYPTLVRMAQDWAMRYPLVDGQGNFGSIDGDPAAAMRYTEARLTHSAIFLLEDLDKDTVDMVPNYDETKYEPVVFPSKFPNLLCNGSSGIAVGMATNIPPHNLGELIEATLLVLANSQTSIEDILEVMPGPDFPTGGIICGTEGIRSTYYTGRGKLRLRARMHVEENSDKQRENIILTEMPYNVNKSRLIEQIAELINEKTLTGISDVRDESDKDGIRVVLELKKGESSEVVINRLYKFTDVQVTFGANMLALDKNLPRTMNIHRMISAWIRHRMDVIQRRTRYELNKAEARAHILEGFLKALSCMDEVVKTIRESSNKEHAKQQLVELFSFSEAQALAILELRLYQLTGLEADKVQKEYSELLEKITYYRKVLAEEELVKDIIREELQELHKVHKTPRRTRIEMDAGDVRDIEDIISDESVIITISGDDYVKRMPVKVFREQKRGGQGVTGFDMKKGSDFLKAVYSASTKDYLLIFTNFGQCYWLKVWRLPEGERRAKGKPIINFLEGIRPGEQVAAVLNVKRFEQGEYLFLATKKGVVKKVSLDAFGSPRKKGIRALEIDDGDELIAARHIANDEEKVMLFTRLGMAVRFPHDKVRPMGRAARGVRGVSLKNEQDFVVSCQVVTEDQSVLVVCDNGFGKRSLVCDFRETNRGSVGVRSIVINQRNGDVLGAISVTDCDSILLMSAQGQAIRINMQDVRVMGRATQGVRLVNLREGDTLVAMEKLSINTESVETEENLAASVQSGQDTIEE | Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 94233
Sequence Length: 836
Subcellular Location: Cytoplasm
EC: 5.6.2.2
|
P94605 | MLNEGKVLPVDISSEMKKCYIDYAMSVIVSRALPDVRDGLKPVHRRILYSMHELGLTPEKGYRKCARIVGDVLGKYHPHGDSSVYGALVRLAQDFNLRYTVVDGHGNFGSVDGDSAAAMRYTEAKMNKIALEMVRDIGKNTVDFIPNFDGEEKEPVVLPSRFPNLLVNGSAGIAVGMATNIPPHNLGEVIDGITMLIDNPEATILELMAQIKGPDFPTAGIIMGKSGIRAAYETGRGKITVRAKSEIEVEDNGKQKIIITEIPYQVNKARLVESIADLVKDKRIVGISDLRDESDRDGMRIVIEIKKDANSNIILNQLYKHTRLQDTFGINMLALVDNRPEVLNLKQILQHYIKFQEQVIRRRTEFDLEKASARAHILEGLKIALDHIDEVISLIRGSKTAQEAKLGLMDKFGLSEKQAQAILDLKLQRLTGLEREKIEDEYNELMKTIAELKSILADENKILAIIRDELNEIKAKYGDERKTAIERAENDIDIEDLIQEENVVITLTHAGYIKRINADTYTSQKRGGRGIQAMTTKEDDFVENIFITSTHNNILFFTNKGRMYKLKAYQIPEAGRAAKGTNVVNLLQLDPNEKIQAVISIKEFDEESFLVMCTKKGIIKKTVVGMYKNIRKSGLIAINLNDDDELVSVRITKGDDDIIIVTNKGLAIRFNEVDVRPLGRNALGVKGITLKEDDFVVGMEVPNQESDVLVVSENGFGKRTHVGEYKCQHRGGKGLITYKVSDKTGKLVGVRMVEDGDELMLINNLGIAIRINVSDISTTSRNAMGVTLMRNNGDEKVLALAKINKDDSEQLEDSEEVSEVHDAEENNSEE | Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 92612
Sequence Length: 830
Subcellular Location: Cytoplasm
EC: 5.6.2.2
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D8K235 | MVIGNTRPINIEDEMKNSYMDYAMSVIVSRALPDVRDGLKPVHRRILYAMSDLGMHYNTSYKKSARIVGEVLGKYHPHGDSSVYDAMVRMAQNFSLRYMLVDGQGNFGSVDGDPPAAMRYTEARLTRLAGELLVDIDKDTVEFMPNFDDSLKEPTVLPSRLPVLLMNGASGIAVGMATNIPPHNLTELCDAISYLIDNPECGLEDLMQFVKGPDFPTGGLILGRDGIKSAYATGHGKVVVRARAHVADVAETGARRQIIISELPYQVNKADLVKRIAMLSRERKINGIAEVRDESDRQGLRVVIELKRDGEPQQILNNLYKHTNLQTSFFVNMLALVNNRPVVLNLKEALNHYVAFRQEIITRRSKFELKAARARAHILEGLKIALDNLDAIINLIRHAENADTARRELMSRFELSQLQAQAILDLQLRRLANLERQKILGEYADILKQISYLEDLLANPRKVLSLVKDDLAEVKARYGDARRTEIQSQGVIEFREEDLIPHQSMVVTLTERGFIKRVPTEVYRLQHRAGRGKSIIKTREADSVRFIMVADTHDSVLLFTNRGKIFSIKCHEIPCDLLRTAKGIAIINLVPLAENERITSMIAVSRFDEETSLIMATSGGECKRTKLSDFAAVRSSGLLAMDLPKNDELIGAVIAGADENIILITHNGRSIHFPVADLRVSQRASGGVRGITLEGDDRVAGLDVARPGHFVLVVTTGGYGKLTAVEEYPLQRRAGSGVLTFKVVDKTGKVAAGKVVDREHQVMIATAEGVVIRTPVGTEDQEKGIIVMGRSTQGVIVIRPDENDRVVNFATMVE | Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 90330
Sequence Length: 814
Subcellular Location: Cytoplasm
EC: 5.6.2.2
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Q8VCB3 | MLRGRSLSVTSLGGLPVWEAERLPVEDLLLFEVSWEVTNKVGGICTVIQTKAKTTADEWGENYFLIGPYFEHNMKTQVEQCEPTNDAVRKAVDAMNKHGCQVHFGRWLIEGSPYVVLFDISSSAWNLDRWKGDFWEACGVGIPHHDREANDMLIFGSLTAWFLKEVTDHADGKHVIAQFHEWQAGTGLILSRARKLPIATVFTTHATLLGRYLCAANIDFYNQLDKFDIDKEAGERQIYHRYCMERASVHCAHVFTTVSEITAIEAEHMLKRKPDVVTPNGLNVKKFSAVHEFQNLHAMYKARIQDFVRGHFYGHLDFDLEKTLFLFIAGRYEFSNKGADIFLESLSRLNFLLRMHKSNVTVVVFFIMPAKTNNFNVETLKGQAVRKQLWDTVHCLKEKFGKKLYDGLLRGEIPDMNSILDRDDLTIMKRAIFSTQRQSLPPVTTHNMIDDSTDPILSTIRRIGLFNNRADRVKVILHPEFLSSTSPLLPMDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSVTTNLSGFGCFVQEHVADPTAYGIYIVDRRFRSPDDSCNQLTQFLYGFCKQSRRQRIIQRNRTERLSDLLDWRYLGRYYQHARHLTLSRAFPDKFHLEPTSPPTTDGFKYPRPSSVPPSPSGSQASSPQCSDAEDEEDEDERYDEEEEAERDRLNIKSPFSLNHFPKGKKKLHGEYKN | Function: Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.
PTM: Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and CSNK2A2 is required for inhibitory phosphorylation at Ser-641 (site 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an GSK3B (By similarity). Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the enzyme (By similarity). Phosphorylation at Ser-8 is not required for interaction with GYG1 . Interaction with GYG1 does not regulate the phosphorylation at Ser-8 and Ser-641 .
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + H(+) + UDP
Sequence Mass (Da): 80871
Sequence Length: 704
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.11
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P27472 | MSRDLQNHLLFETATEVANRVGGIYSVLKSKAPITVAQYKDHYHLIGPLNKATYQNEVDILDWKKPEAFSDEMRPVQHALQTMESRGVHFVYGRWLIEGAPKVILFDLDSVRGYSNEWKGDLWSLVGIPSPENDFETNDAILLGYTVAWFLGEVAHLDSQHAIVAHFHEWLAGVALPLCRKRRIDVVTIFTTHATLLGRYLCASGSFDFYNCLESVDVDHEAGRFGIYHRYCIERAAAHSADVFTTVSQITAFEAEHLLKRKPDGILPNGLNVIKFQAFHEFQNLHALKKEKINDFVRGHFHGCFDFDLDNTLYFFIAGRYEYKNKGADMFIEALARLNYRLKVSGSKKTVVAFIVMPAKNNSFTVEALKGQAEVRALENTVHEVTTSIGKRIFDHAIRYPHNGLTTELPTDLGELLKSSDKVMLKRRILALRRPEGQLPPIVTHNMVDDANDLILNKIRQVQLFNSPSDRVKMIFHPEFLNANNPILGLDYDEFVRGCHLGVFPSYYEPWGYTPAECTVMGVPSITTNVSGFGAYMEDLIETNQAKDYGIYIVDRRFKAPDESVEQLVDYMEEFVKKTRRQRINQRNRTERLSDLLDWKRMGLEYVKARQLALRRGYPDQFRELVGEELNDSNMDALAGGKKLKVARPLSVPGSPRDLRSNSTVYMTPGDLGTLQEVNNADDYFSLGVNPAADDDDDGPYADDS | Function: Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. Is believed to regulate the synthesis of glycogen.
PTM: Phosphorylated by the cyclin-CDK PCL10-PHO85. Phosphorylation causes inactivation of enzyme.
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + H(+) + UDP
Sequence Mass (Da): 80079
Sequence Length: 705
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.11
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Q9U2D9 | MPDHARMPRNLSSNKIAKTIAGEDLDEEEVLEMDAGQSAREEGRFVFECAWEVANKVGGIYTVLRSKAQISTEELGDQYCMFGPMKDGKWRLEVDPIEPENRTIRAAMKRFQADGFRCMYGRWLIEGYPKVILFDLGSGAVKMNEWKHELFEQCKIGIPHEDIESNDAVILGFMVALFLKHFRESVTSYTPLVVAHFHEWQAGVGLLMTRLWKLDIATVYTTHATLLGRHLCAGGADLYNNLDSFDLDAEAGKRKIYHQYCLERAACQTAHIFTTVSEITGLEAEHFLCRKPDVLTPNGLNVVKFAALHEFQNLHAQNKEKINQFIRGHFHGHLDFDLDKTLYFFTAGRYEFSNKGGDMFIESLARLNHYLKTTSDPRHMGVTVVAFLIYPAPANSFNVESLKGQAVTKQLKEAVDRIKEKVGQRIFDICLQGHLPEPEELMSPADNILLKRCIMSLHNSSLPPICTHNMIRADDPVLESLRRTSLFNKPEDRVKVVFHPEFLSSVSPLIGLDYEDFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSVSTNLSGFGCFMQEHVEDHEQKGIYVIDRRHKAAEESVQELAQVMYDFCGQSRRQRIILRNSNEGLSALLDWQNLGVFYRDCRRLALERLHPDVDKIMRDNEGKVPSAATSRRPSIHSSDGEDDE | Function: Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + H(+) + UDP
Sequence Mass (Da): 76459
Sequence Length: 672
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.11
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Q55GH4 | MIFGTPNSTFLENRLGSSTGMPFSSATSLNSGVDQMMNELNIQQPTSHTVLFDLSWEVAKKVGGIYTVLKTKAPVTVEEYKSRYALIGPYNASTAPTEFEPLIPGPLSSPIIENMMKKYGIHVHFGKWLVEGYPKVFLIDLHSSMHKLGEWRWDLMSGFEQAGDNETNETIVFGYQSALLLKEFAEANPNDKYIAHFHEWQASVGLILLKKWKVPVSTIFTTHATLLGRYLAAGGVDLYNQMQVLNMDFEASKRGIYHRHWIEKKSAADSHVFTTVSEITGYESEHILMRKPDVILPNGLKLDKFTALHEFQNLHAKYKGVLNEFVRGHFYGHYSDFDLDNTLYVFTAGRHEYFNKGVDMFLDSLAGLNKLLQQSGSKMTVVAFIIMPAATNNFNVESLKGHSYLKDMRRTCNTIVEAMGERLFEATSRGKMISPEELLSQEDLVMLKRRIFALKQKSSGPPVVTHNMINDNDEILQHIRRIKLFNSQEDRVKVIYHPEFLTSTNPLIPLDYTEFVRGCHLGIFPSYYEPFGMTPAECCASGCPSITSNLTGFANYMSRALQDTDSKGIFIVDRRFKSSRETVDQMTQYLWKFTQLDRRQRIELRNATEKLSELLDWRTLGKFYKTARALALERAFPPKPISRSPSPSPSSSLKLSTGLSNQIELQQQQQQQQPQPIGTTINLIPPSSNVSVTPTTTPTTTTTATTATTAPITTPKPNVIPINTGKENITLLSPNSMSSLLSDSLNEFKKQQQQQQQSKTPTTPTTTSTTTTTPSTTAAATNKSVLSNPTPTPSPNTSSFIPTNKGSTATTTTTTATPTPTPSNNTNGKPFNPIEALTKSNSSSNFATTSTASVNTNNGGTNSPVSKSIPIPSSKSLK | Function: Catalyzes the formation of apha-1,4 glycosidic bonds adding glucose residue from UDPG to the growing chain of glycogen.
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + H(+) + UDP
Sequence Mass (Da): 97515
Sequence Length: 878
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.11
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Q9VFC8 | MRRQQSYRFEDNESTSYALRMNRRFSRVESGADLKDYFDRGDIASRENRWNFEVAWEVANKVGGIYTVIRSKAYVSTEEMGEQLCMMGPYKEHCARTEMEEMEFPRGNPLLDAVNSLRSRGYKIHTGRWLVDGNPQLILFDIGSAAWKLDQFKSEMWEKCHIGIPHLDIETNDAIILGFMIAEFLEEFRNFAVTYSQNNELSAPRIVAHFHEWQAGVGLIVLRTRLVEIATVFTTHATLLGRYLCAGNTDFYNNLDKFAVDEEAGKRQIYHRYCLERGATHLAHVFTTVSEITGYEAEHLLKRKPDIITPNGLNVKKFSAIHEFQNLHAVAKEKINEFVRGHFYGHIDFDLDKTLYFFIAGRYEFGNKGADIFIEALARLNAMLKHEKPDTTVVAFLIFPTKTNNFNVDSLRGHAVIKQLRDTINNVQQAVGKRMFDTCLQGNIPNADDLLQKDDLVKIKRCMFAMQRDSMPPVTTHNVADDWNDPVLSSIRRCHLFNSRHDRVKMVFHPEFLTSTNPLFGIDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSVTTNLSGFGCFMEEHISDPKSYGIYIVDRRYIGLENSVQQLSSFMMEFSRLNRRQRIIQRNRTERLSDLLDWRTLGIYYRQARVKALQAVYPDYVDELSLYGSKNNLIFSRPHSEPPSPTSSRHTTPAPSVHGSDDEDSVDEETELKELGIK | Function: Transfers the glycosyl residue from UDPG to the non-reducing end of alpha-1,4-glucan. In larval skeletal muscle, isoform B is required for the formation of autophagosomes during starvation and during cloroquine-induced vacuolar myopathy.
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + H(+) + UDP
Sequence Mass (Da): 81754
Sequence Length: 709
Pathway: Glycan biosynthesis; glycogen biosynthesis.
Subcellular Location: Cytoplasmic vesicle
EC: 2.4.1.11
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O93869 | MAHDNREPREVKNHLLFEVATEVAHRVGGIYSVLKSKAPVTTAEYGDRYTLIGPLNHQSAAVEVEELEPSNPELKATIQAMRDRGIGILYGRWLIEGAPRVLLFDTKTAYGYMNEWKTDLWNVASIPSPDNDEETNEAIVFGYLVAWFLGEFVCHEKRKAVIAHFHEWLAGVALPLTKKRQIDVTTIFTTHATLLGRYLCAGSVDFYNNLQWFDVDAEAGKRGIYHRYCIERAAAHSCDVFTTVSHITAYESEHLLKRKPDGVLPNGLNVTKFSAMHEFQNLHQQNKEKIHDFVRGHFYGHYDFEPENTLYFFTAGRYEFRNKGVDMFIESLARLNHRLKTAGSKTTVVAFIIMPAQTTSLTVEALKGQAVIKSLRDTVDVIERGIGRRIFERSVKWHEGDPLPEEKELITSQDRVLLRRRLFAMKRHTLPPIVTHNMLNDHEDPILNQIRRVQLFNHPSDRVKIVFHPEFLSSANPVLPLDYDDFVRGTHLGVFASYYEPWGYTPAECTVMGVPSITTNLSGFGCYMEELIENSSDYGIYIVDRRSKGVDDSVNQLTQYMFEFTQKSRRQRINQRNRTERLSDLLDWKRMGMEYVKARQLALRRAYPTSFNGEEEEDFIPGVEQKISRPFSVPGSPRDRTGMMTPGDFASLQESHEGLSTEDYVAWKLPEEEDPEEYPFPLTLKQRTGPGSPLDSIQGLQLNGTR | Function: Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. Is believed to regulate the synthesis of glycogen.
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + H(+) + UDP
Sequence Mass (Da): 80907
Sequence Length: 706
Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.4.1.11
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Q9VI20 | MSKRSCQILTLLGLCLVCHEATLVGGHVLVYRKATSQLIEEFNDLPAQFGPNLPSNGLKVYVVPARRPYYGCDSLDRPPHLKYPPSAKFVALVARGECVFERKIRVAQNASYSAVIVYNNEGDDLEQMSAENITGIRIPSVFVGHTTGKALATYFTTEVVLIINDELPFNINTQLILPFSILIGMCFIIMVIYMIYKCIREQRRLRRHRLPKSMLKKLPVLRYTKNNANNKYDTCVICLEDFIEDDKLRVLPCSHPYHTHCIDPWLTENRRVCPICKRKVFTKGEARASRSRQPSLDNVTDTDDDTTPLLQQQQSNGRQVGQVSSASSAGGAAGSSSSVAAAAVAGTTRHGTFRRGHAGRNPFEESQSSDDENALLASTVRPATSSGAHERINPFDRAPNLPAHLAEQLTESRRSVWSRINFASFFRRQPAVISVAAPPYLERVESGTSAMGLPVTGTIAVASPASNNILNPNLSGSFKDEDDMPPHRSIYEPIAISTPAADSATVDDSAFLQTPTQGGIGVAALPHSASDRQFLI | Function: Endosomal E3 ubiquitin-protein ligase that regulates the recycling endosome pathway by mediating ubiquitination of Synaptobrevin (Syb) . Also acts as a regulator of transcytosis in wing imaginal disks by catalyzing ubiquitination of Syb: ubiquitination of Syb promotes transcytosis of wingless (wg) to the basolateral surface .
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 58824
Sequence Length: 536
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Endosome membrane
EC: 2.3.2.27
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P59226 | MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRFRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVAALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Can be acetylated to form H3K9ac, H3K14ac, H3K18ac and H3K23ac. H3K9ac could compete with H3K9me and prevent gene silencing. H3K9acK14ac molecules are 30-fold less abundant than H3K9ac or H3K14ac. Very low level of H3K9meK14ac. H3K14 is specifically acetylated by HAG1 and deacetylated by HDA6. H3K9ac is deacetylated by HDT1. H3K9ac is restricted to euchromatin. H3K18ac, but not H3K9ac, is cell-cycle dependent and linked to replication. Reduced H4R3me2s increases H3K14ac in the FLC chromatin and activates or maintains its transcription. Vernalization decreases H3K9/14ac in the promoter region of FLC.
Sequence Mass (Da): 15268
Sequence Length: 136
Subcellular Location: Nucleus
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Q42681 | MARTKQTARKSTGGKAPRKQLATKAARKTPATGGVKKPHRYRPGTVALREIRKYQKSTELVIRKLPFQRLVREIAQDFKTDLRFQSQAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Acetylation is generally linked to gene activation. Acetylated to form H3K9ac (11%), H3K14ac (17%), H3K18ac (11%), H3K23ac (16%) and H3K27ac (7%). H3K4, H3K35 and H3K36 are not acetylated. H3K4me prevents acetylation. 32% of the histone H3 are acetylated with, on average, 2.4 acetyl-Lys. They are all continuously deacatylated and re-acetylated with a half-life of approximately 2 min.
Sequence Mass (Da): 15296
Sequence Length: 135
Subcellular Location: Nucleus
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Q8SS77 | MARTKQSARKTTGGKAPRKQLSAKSARKGVSPASSAGAKKSRYRPGSVALKEIRRYQKSTDFLIRRLPFQRACRSVVKECSNATDIRFQGPALASIQEALEVYLVGLFEDAMLCAYHAKRVTVFPKDISLVLKLRSRHVKSISD | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Mono-, di- and trimethylated to form H3K4me1/2/3. H3K4me activates gene expression by regulating transcription elongation and plays a role in telomere length maintenance. H3K4me enrichment correlates with transcription levels, and occurs in a 5' to 3' gradient with H3K4me3 enrichment at the 5'-end of genes, shifting to H3K4me2 and then H3K4me1. H3K36me represses gene expression (By similarity).
Sequence Mass (Da): 15997
Sequence Length: 144
Subcellular Location: Nucleus
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P68431 | MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability.
Sequence Mass (Da): 15404
Sequence Length: 136
Subcellular Location: Nucleus
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A5DWE2 | MARTKQTARKSTGGKAPRKQLASKAARKSAPSTGGVKKPHRYKPGTVALREIRRFQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQEAVEAYLVGLFEDTNLCAIHAKRVTIQKKDIQLARRLRGERS | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Phosphorylated to form H3S10ph. H3S10ph promotes subsequent H3K14ac formation and is required for transcriptional activation through TBP recruitment to the promoters (By similarity).
Sequence Mass (Da): 15342
Sequence Length: 136
Subcellular Location: Nucleus
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P09988 | MARTKQTARKSTGGKAPRKQLASKAARKAAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQEAVEAYLVSLFEDTNLCAIHGKRVTIQPKDMQLARRLRGERS | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Phosphorylated by ark1 to form H3S10ph in a cell cycle-dependent manner during mitosis and meiosis. H3S10ph is also formed by ssp2, promotes subsequent H3K14ac formation by gcn5, and is required for transcriptional activation through TBP recruitment to the promoters. Dephosphorylation is performed by sds21.
Sequence Mass (Da): 15357
Sequence Length: 136
Subcellular Location: Nucleus
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P69149 | MARTKQTARKSTGAKAPRKQLASKAARKSAPATGGIKKPHRFRPGTVALREIRKYQKSTDLLIRKLPFQRLVRDIAHEFKAELRFQSSAVLALQEAAEAYLVGLFEDTNLCAIHARRVTIMTKDMQLARRIRGERF | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Phosphorylated to form H3S10ph. H3S10ph promotes subsequent H3K14ac formation by GCN5. H3S10ph is only found in the mitotically dividing MIC, but not in the amitotically dividing MAC. H3S10ph is correlated with chromosome condensation during mitotic or meiotic micronuclear divisions (By similarity).
Sequence Mass (Da): 15429
Sequence Length: 136
Subcellular Location: Nucleus
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Q4P7J7 | MARTKQTARKSTGGKAPRKQLATKAARKSAPAAGGVKKPHRYKPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQEAAEAYLVSLFEDTNLAAIHAKRVTIQPKDIALARRLRGERS | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Phosphorylated to form H3S10ph. H3S10ph promotes subsequent H3K14ac formation and is required for transcriptional activation through TBP recruitment to the promoters (By similarity).
Sequence Mass (Da): 15208
Sequence Length: 136
Subcellular Location: Nucleus
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Q6ZXX3 | MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISGLIYDETRGVLKLFLESVIRDSVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes.
Sequence Mass (Da): 11382
Sequence Length: 103
Subcellular Location: Nucleus
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P02309 | MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISGLIYEEVRAVLKSFLESVIRDSVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. Together with SPT15/TBP UAF seems to stimulate basal transcription to a fully activated level.
PTM: Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes.
Sequence Mass (Da): 11368
Sequence Length: 103
Subcellular Location: Nucleus
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B1B212 | MAKSSLSLNWSLLVLLNFLGATLSTGTDSLSCELTFNHRTLHGQCSVNGKTLLDFGDKKHEGNATEMCADLSQSLRELSEGMRNQQSGNDALNVTTQSQYNQGEFIGGFWAINTDEQHSIYFYPLNMTWRESHSDNSSAMEHWKNKNLEKDIRNVLIIYFSRCLNKLSPHFREMPKSKIKVLDTTQNTNTTQIHPTVNNSQHNSDTQGLSFTWIVIICIGGIVSFMAFMVFAWCMLKKKKGALCCSSSSTT | Function: Ligand for the KLRK1 immunosurveillance receptor. Binding to KLRK1 stimulates cell lysis in vitro.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 28224
Sequence Length: 251
Subcellular Location: Cell membrane
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B1B213 | MALLLLILESCSAGTYALNCKLTVKYRTLQGLCSVNGKTFLDFGDENHEGNATMLCPALYQSLTDISEVMWSLQSGNDALNVTTRSQYYQGEFIDGFWDINTDEQHSIYVYPLNKTWRESHSDNSSAMEQWKNKNLEKDIRNVLMVDFSCCLNKSSPHFREMPTLPTTAAHVDQPRSMACKSSPFDGLIMILLIYIL | Function: Ligand for the KLRK1 immunosurveillance receptor. Binding to KLRK1 stimulates cell lysis in vitro.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22340
Sequence Length: 197
Subcellular Location: Cell membrane
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Q56UJ5 | MNLLTGRNMVERSSKFLFIVVGSVLFMLILYQYVAPGMMNFGSPHGYMLEDDADLFPTPDPHYVKKFYFPIRDLERTVDFEIKGDDVIVFLHIQKTGGTTFGRHLVQNVRLEVPCDCRPGQKKCTCYRPNRKETWLFSRFSTGWSCGLHADWTELTNCVPGVLNKKESRMKNQRKFYYITLLRDPVSRYLSEWRHVQRGATWKTSLHMCDGRTPTPEELPPCYEGTDWSGCTLQQFMDCPYNLANNRQVRMLADLSLVGCYNMSFIPEKKRAQVLLESAKKNLRDMAFFGLTEFQRKTQYLFERTFRLKFIRPFMQYNSTRAAGVDLDNDTIQRIEELNDLDMQLYDYARDLFQQRYMYKRQLERREQRLKNQPLFPFRRTSSSDSTFRDDAPESEGSRLPTEDYMNHIINRW | Function: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate.
Catalytic Activity: 3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) + adenosine 3',5'-bisphosphate + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 48910
Sequence Length: 413
Subcellular Location: Membrane
EC: 2.8.2.-
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A0MGZ5 | MNDTERNMVERTSKFLLIVVGSVFFMLILYQYVAPGVINFGSPHGYLLGEEDMTIFPTPDPHYVKKYYFPIKDLERKIDFEIKGEDVIVFLHIQKTGGTTFGRHLVQNVRLELPCDCRPGQKKCTCYRPNRKETWLFSRFSTGWSCGLHADWTELTNCVPGVLNKRESKSKKMRKFYYITLLRDPVSRYLSEWRHVQRGATWKTSLHMCDGRTPTPEELPPCYEGTDWSGCTLQQFMDCPYNLANNRQVRMLADLSLVGCYNLSTVPEKRRSQLLLESAKKNLRDMAFYGLTEFQRKTQYLFERTFHLKFIRPFMQYNSTRAAGVDLDNDTIQRIEELNDLDMKLYDYAKDLFQQRYQYKHMLDRREQRLLRGHASFHSPFREDGAGGEGTARLPTEDYMNHIINGW | Function: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate.
Catalytic Activity: 3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) + adenosine 3',5'-bisphosphate + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 47878
Sequence Length: 407
Subcellular Location: Membrane
EC: 2.8.2.-
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A0MGZ7 | MNDKPNKWIFIPILAILFVMIGYQYVCPAGGQACHFRTGDKLVRIAPLATPDPTTDDLYREQDPEEDNPPKCASKFNFTERDLTRDVDFNIKGDDVIVFLHIQKTGGTTFGRHLVRNIRLEQPCDCKAGQKKCTCHRPGKQESWLFSRFSTGWSCGLHADWTELTNCVPVIMDKRQPPKRKRNFYYITMLRDPVSRYLSEWKHVQRGATWKTSLHMCDGRSPTQDELPTCYNGDDWSGVTLHDFMDCPSNLANNRQVRMLADLSLVGCYNLSTMNESERNPILLASAKSNLKNMAFYGLTEFQRKTQYLFERTFHLRFISAFTQINSTRAANVELRDDMRSRIEQLNMLDMQLYEFAKDLFLQRYQFVRQRERQEERLKRREERRWIRERRVNQSKEPIVENQTRVTTTEDYASQVVRW | Function: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate.
Catalytic Activity: 3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) + adenosine 3',5'-bisphosphate + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 49346
Sequence Length: 419
Subcellular Location: Membrane
EC: 2.8.2.-
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Q76KB2 | MKRAGRTMVERTSKFLLIVAASVCFMLILYQYVGPGLSLGAPSGRPYAEEPDLFPTPDPHYVKKYYFPVRELERELAFDMKGEDVIVFLHIQKTGGTTFGRHLVQNVRLEVPCDCRPGQKKCTCYRPNRRETWLFSRFSTGWSCGLHADWTELTNCVPGVLGRRESAPNRTPRKFYYITLLRDPVSRYLSEWRHVQRGATWKTSLHMCDGRTPTPEELPSCYEGTDWSGCTLQEFMDCPYNLANNRQVRMLADLSLVGCYNMSFIPENKRAQILLESAKKNLKDMAFFGLTEFQRKTQYLFERTFNLKFIRPFMQYNSTRAGGVEVDNDTIRRIEELNDLDMQLYDYAKDLFQQRYQYKRQLERMEQRIKNREERLLHRSNEALPKEETEEQGRLPTEDYMSHIIEKW | Function: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate (By similarity). May also play a role in limb development.
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: 3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) + adenosine 3',5'-bisphosphate + H(+)
Sequence Mass (Da): 48092
Sequence Length: 408
Subcellular Location: Membrane
EC: 2.8.2.-
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O52214 | MQTYLFASGLVLFLLGLVTGLLVPVSKNPRMGVAGHLQGMTNGPLLIIAGLLWPYLELPDAWQLATFWLLIYGTYANWLGVQLAALWGAGAKLAPIAAGEHRSTPLKERVVTFLLFSLIPAMFAAPIILLIGILR | Function: Catalyzes the rearrangement of hydroxylaminobenzene to 2-aminophenol. Involved in the degradation of nitrobenzene.
Catalytic Activity: N-phenylhydroxylamine = 2-aminophenol
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14610
Sequence Length: 135
Subcellular Location: Cell membrane
EC: 5.4.4.1
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O52216 | MTLHTPSTDAPLARRLLQLGIALFLLGLLTGFLLPMMANPRVGLSSHLEGVLNGMFLLALGLMWPQLSLGTGARKAAFGFAVYGTYANWLATLLAGFWGAGGRMMPIAAGGHTGTAAQEGLIAFALISLSLSMLVVCALALWGLRSAPARRNTDAPAAGPQPAA | Function: Catalyzes the rearrangement of hydroxylaminobenzene to 2-aminophenol.
Catalytic Activity: N-phenylhydroxylamine = 2-aminophenol
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16955
Sequence Length: 164
Subcellular Location: Cell membrane
EC: 5.4.4.1
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Q14520 | MFARMSDLHVLLLMALVGKTACGFSLMSLLESLDPDWTPDQYDYSYEDYNQEENTSSTLTHAENPDWYYTEDQADPCQPNPCEHGGDCLVHGSTFTCSCLAPFSGNKCQKVQNTCKDNPCGRGQCLITQSPPYYRCVCKHPYTGPSCSQVVPVCRPNPCQNGATCSRHKRRSKFTCACPDQFKGKFCEIGSDDCYVGDGYSYRGKMNRTVNQHACLYWNSHLLLQENYNMFMEDAETHGIGEHNFCRNPDADEKPWCFIKVTNDKVKWEYCDVSACSAQDVAYPEESPTEPSTKLPGFDSCGKTEIAERKIKRIYGGFKSTAGKHPWQASLQSSLPLTISMPQGHFCGGALIHPCWVLTAAHCTDIKTRHLKVVLGDQDLKKEEFHEQSFRVEKIFKYSHYNERDEIPHNDIALLKLKPVDGHCALESKYVKTVCLPDGSFPSGSECHISGWGVTETGKGSRQLLDAKVKLIANTLCNSRQLYDHMIDDSMICAGNLQKPGQDTCQGDSGGPLTCEKDGTYYVYGIVSWGLECGKRPGVYTQVTKFLNWIKATIKSESGF | Function: Cleaves the alpha-chain at multiple sites and the beta-chain between 'Lys-53' and 'Lys-54' but not the gamma-chain of fibrinogen and therefore does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly. It does not cleave (activate) prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator (pro-urokinase) to the active two chain form. Activates coagulation factor VII . May function as a tumor suppressor negatively regulating cell proliferation and cell migration .
PTM: Proteolytic cleavage at Gly-23 or Met-27 can give rise to the 50 kDa heavy chain and cleavage at Arg-313 or Lys-319 can give rise to the 27 kDa light chain. The heavy chain can undergo further proteolytic cleavage at Lys-169 or Arg-170 to give rise to 2 inactive 26 kDa fragments and the light chain can undergo further proteolytic cleavage at Arg-480 to give rise to inactive 17 kDa and 8 kDa fragments (By similarity).
Sequence Mass (Da): 62672
Sequence Length: 560
Subcellular Location: Secreted
EC: 3.4.21.-
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Q8K0D2 | MFVRMLVFRVLLLIALVGKSVIGLSLMSFIAPPDPDWTPDDYYYSYEQSSPDEDPSVTQTTPENPDWYYEDDDPCQSNPCEHGGDCIIRGDTFSCSCPAPFSGSRCQTAQNKCKDNPCVHGDCLITQKHPYYRCACKYPYTGPDCSKVLPACRPNPCQNGGVCSRHRRRSRFTCACPDQYKGKFCEIGPDDCYVGDGYSYRGKVSKTVNQNPCLYWNSHLLLQETYNMFMEDAETHGIAEHNFCRNPDGDHKPWCFVKVNSEKVKWEYCDVTVCPVPDTPNPVESLLEPVMELPGFESCGKTEVAEHAVKRIYGGFKSTAGKHPWQVSLQTSLPLTTSMPQGHFCGGALIHPCWVLTAAHCTDINTKHLKVVLGDQDLKKTESHEQTFRVEKILKYSQYNERDEIPHNDIALLKLKPVGGHCALESRYVKTVCLPSDPFPSGTECHISGWGVTETGEGSRQLLDAKVKLIANPLCNSRQLYDHTIDDSMICAGNLQKPGSDTCQGDSGGPLTCEKDGTYYVYGIVSWGQECGKKPGVYTQVTKFLNWIKTTMHREAGL | Function: Cleaves the alpha-chain at multiple sites and the beta-chain between 'Lys-53' and 'Lys-54' but not the gamma-chain of fibrinogen and therefore does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly. It does not cleave (activate) prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator (pro-urokinase) to the active two chain form. Activates coagulation factor VII (By similarity).
PTM: Proteolytic cleavage at Gly-23 or Met-27 can give rise to the 50 kDa heavy chain and cleavage at Arg-311 or Lys-317 can give rise to the 27 kDa light chain. The heavy chain can undergo further proteolytic cleavage at Arg-168 or Arg-169 to give rise to 2 inactive 26 kDa fragments and the light chain can undergo further proteolytic cleavage at Arg-478 to give rise to inactive 17 kDa and 8 kDa fragments.
Sequence Mass (Da): 62357
Sequence Length: 558
Subcellular Location: Secreted
EC: 3.4.21.-
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Q9I9R0 | MMKGAMGCPVAAVMEGSFSCTVANRFYQLLDDESDPFDNLREAERCWQQRKNLSKVVARRGDPGSRGCATRRELQKQRKQLGTPAPPPQPGQKQAPKQEECGGKDNSRAEKEHKTAWRPSFMEYLSSETESQAELTAQSLFRPTAKLNYERPRGCGRGRGGMQGRGRGGGINKSFDGFDQRGKREFGRQNDNDKIEMELTAPMEATAKTAKSPGVSEGELLNKVAEGKPREEVVQEMTLDEWKNLQQQNRPKHEFNIRRPESTVPSKAVVIHKSKYSDDIQKGELEDDYHIFRRAVNDITFQLDINFGSLPRPGCGSRGARGRGRGRQMEETGPQPEAMVQIVAPNPDDPEDFPALT | Function: Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (By similarity). Acts via its association with EEF2/eEF2 factor at the A-site of the ribosome, promoting ribosome stabilization in an inactive state compatible with storage (By similarity). Plays a key role in ribosome hibernation in the mature egg by promoting ribosome stabilization (By similarity). Ribosomes, which are produced in large quantities during oogenesis, are stored and translationally repressed in the egg and early embryo (By similarity).
Sequence Mass (Da): 39968
Sequence Length: 357
Domain: The C-terminal region is necessary for nucleus and cytoplasmic localization. The N-terminal region is necessary for nucleus and nuclear bodies localization.
Subcellular Location: Nucleus
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Q5JVS0 | MKGALGSPVAAAGAAMQESFGCVVANRFHQLLDDESDPFDILREAERRRQQQLQRKRRDEAAAAAGAGPRGGRSPAGASGHRAGAGGRRESQKERKSLPAPVAQRPDSPGGGLQAPGQKRTPRRGEQQGWNDSRGPEGMLERAERRSYREYRPYETERQADFTAEKFPDEKPGDRFDRDRPLRGRGGPRGGMRGRGRGGPGNRVFDAFDQRGKREFERYGGNDKIAVRTEDNMGGCGVRTWGSGKDTSDVEPTAPMEEPTVVEESQGTPEEESPAKVPELEVEEETQVQEMTLDEWKNLQEQTRPKPEFNIRKPESTVPSKAVVIHKSKYRDDMVKDDYEDDSHVFRKPANDITSQLEINFGNLPRPGRGARGGTRGGRGRIRRAENYGPRAEVVMQDVAPNPDDPEDFPALS | Function: Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (By similarity). Acts via its association with EEF2/eEF2 factor at the A-site of the ribosome, promoting ribosome stabilization in an inactive state compatible with storage (By similarity). Plays a key role in ribosome hibernation in the mature oocyte by promoting ribosome stabilization (By similarity). Ribosomes, which are produced in large quantities during oogenesis, are stored and translationally repressed in the oocyte and early embryo (By similarity). Also binds RNA, regulating transcription and pre-mRNA splicing . Binds (via C-terminus) to poly(U) RNA . Seems to play a role in PML-nuclear bodies formation . Negatively regulates DNA-binding activity of the transcription factor MEF2C in myocardial cells in response to mechanical stress (By similarity).
PTM: Methylated . Methylation is decreased by phorbol 12-myristate 13-acetate (PMA)-activated PKC, in vitro .
Sequence Mass (Da): 45785
Sequence Length: 413
Domain: The C-terminal region is necessary for nucleus and cytoplasmic localization . The N-terminal region is necessary for nucleus and nuclear bodies localization . Regions containing Arg-Gly-Gly repeats (RGG/RXR-box) may be preferentially methylated by PRMT1 .
Subcellular Location: Nucleus
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A1L1K8 | MKGALGSPVAAAGAAMQETFGCVVANRFHQLLDDESDPFDILREAEHRRQQQLQRKRRDEAAAASGAGHRGGRSPAVASGHRPGAAGRRESQKERKSLAVSSAQQPDSPGGPQPPGQKRTPRRGEQQGWNDNRGTDVVLDRAERRSYREYRPYDTERQAESTAEKFTDEKPVDRFDRDRPLRGRGGPRGGLRNRGRGGPGNRAFDSFDQRGKRDFERYGSSDKANRMEDSMGGCGVRTWGSGKDTSDTEPPAPMEETSMMEECQGVLDEESASKVPELEVEEENQVQEMTLDEWKNLQEQTRPKPEFNIRKPESTVPSKAVVIHKSRYRDDIVKDDYEDESHVFRKAANDITSQLEINFGNLPRPGRGARGSTRGGRGRIRRTENYGPRAEVVTQDVAPNPDDPEDFPALA | Function: Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (By similarity). Acts via its association with EEF2/eEF2 factor at the A-site of the ribosome, promoting ribosome stabilization in an inactive state compatible with storage (By similarity). Plays a key role in ribosome hibernation in the mature oocyte by promoting ribosome stabilization (By similarity). Ribosomes, which are produced in large quantities during oogenesis, are stored and translationally repressed in the oocyte and early embryo (By similarity). Also binds RNA, regulating transcription and pre-mRNA splicing. Binds (via C-terminus) to poly(U) RNA. Seems to play a role in PML-nuclear bodies formation (By similarity). Negatively regulates DNA-binding activity of the transcription factor MEF2C in myocardial cells in response to mechanical stress .
PTM: Phosphorylated by phorbol 12-myristate 13-acetate (PMA)-activated PKC isoforms at Thr-352 and Thr-373.
Sequence Mass (Da): 45826
Sequence Length: 411
Domain: The C-terminal region is necessary for nucleus and cytoplasmic localization. The N-terminal region is necessary for nucleus and nuclear bodies localization. Regions containing Arg-Gly-Gly repeats (RGG/RXR-box) may be preferentially methylated by PRMT1.
Subcellular Location: Nucleus
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A9A1Y1 | MTDSPILSPKSIAVIGASDKRGSVGATITSNIMNGFKGTVYPISPTRDTVFYKKAYKSVLDVPKSIDLAVIVIKNTLVTPVLEECGKKKIKGVIIITAGFKEVDEEGAKREQQVIDIAKKYNMQVVGPNCLGVMNLDSKTMMNSTFLKVTPKSGKIALVSQSGAICAALVEDASAQGIGFSAVVSLGNKAVMSEVDVLKILANHKQTEVIVMYLEDMGDGQEFLKVCKNITKKLKKPVLVLKSGRSPEGAKAAMSHTGALMGSDEIYDALLKQSGAIRVDTMEELFDYATAFSKQPLPSNGDLVIVSNAGGPAIISTDACSKAKIKMADITSIRKKIDEVIPPWGSSRNPVDIVGDADFNRFHNVLDRVLKHPKVGSVISMCTPSGTLNYDKLAEVIVEMSKKYKKTMLASLMGLDEGVTNREILADGNVPYYTYAEGAIRTLAAMIRFSDWVKSSPGKITKFKVNKAKAKKIFDQVKKEKRPNLLEEEGQEVLKAYGLPLPKSTLAKNEAEAVKAAKKIGYPVVMKIASPQIIHKSDAGGVKVNLTNDAEVKDAFKTIVKNAKKYNKKAEIKGVLIVEMVKGGKELIIGSKLEPGFGPVIMLGMGGIYVEVLKDVTFKLAPVTDKEADDMIASIKTQKLLQGVRGEKPSDIVKLSECIQRLSQLVSDFKEIKELDMNPVLVMEKGKGCRILDVRIGL | Cofactor: No activity with Ni(2+), Co(2+) and Ca(2+).
Function: Involved in thaumarchaeal hydroxypropionate/hydroxybutyrate (HP/HB) cycle, a modified version of the autotrophic HP/HB cycle of Crenarchaeota. Catalyzes the formation of 4-hydroxybutyryl-CoA, ADP and phosphate from 4-hydroxybutyrate, coenzyme A (CoA) and ATP. Can also use acetate, propionate and butyrate, with poor catalytic efficiency.
Catalytic Activity: 4-hydroxybutanoate + ATP + CoA = 4-hydroxybutanoyl-CoA + ADP + phosphate
Sequence Mass (Da): 75619
Sequence Length: 698
EC: 6.2.1.56
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A4YDT1 | MVTVQDFFRKFIEFQNSPNEKSLQEIVKLVGQLDLRRFNWVRDVFEDIHVKERGSKTALIWRDINTGEEAKLSYHELSLMSNRVLSTLRKHGLKKGDVVYLMTKVHPMHWAVFLAVIKGGFVMVPSATNLTVAEMKYRFSDLKPSAIISDSLRASVMEEALGSLKVEKFLIDGKRETWNSLEDESSNAEPEDTRGEDVIINYFTSGTTGMPKRVIHTAVSYPVGSITTASIVGVRESDLHLNLSATGWAKFAWSSFFSPLLVGATVVGINYEGKLDTRRYLGEVENLGVTSFCAPPTAWRQFITLDLDQFRFERLRSVVSAGEPLNPEVIKIWKDKFNLTIRDFYGQTETTAMVGNFPFLKVKPGSMGKPHPLYDIRLLDDEGKEITKPYEVGHITVKLNPRPIGLFLGYSDEKKNMESFREGYYYTGDKAYFDEEGYFYFVGRGDDVIKTSDYRVGPFEVESALLEHPAVAEAAVVGVPDTVRWQLVKAYIVLKKGYMPSKELAEEIREKMKTLLSPYKVPRIIEFVDELPKTISGKIRRVELRKREEEKRKKGEVGQNEYVF | Function: Involved in the 3-hydroxypropionate/4-hydroxybutyrate cycle which incorporates carbon dioxide into cellular carbon. Catalyzes the ligation of coenzyme A (CoA) to 4-hydroxybutyrate (4HB). It can also use butyrate, valerate, propionate, acetate and 3-hydroxybutyrate (3HB) as substrates.
Catalytic Activity: 4-hydroxybutanoate + ATP + CoA = 4-hydroxybutanoyl-CoA + AMP + diphosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 64307
Sequence Length: 564
Subcellular Location: Membrane
EC: 6.2.1.40
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A4YDR9 | MGGFKIPNYEGVDPTGSWYSVLTPLLFLERAGKYFKDKTAVVYRDSRYTYSTFYDNVMVQASALMRRGFSREDKLSFISRNRPEFLESFFGVPYAGGVLVPINFRLSPKEMAYIINHSDSKFVVVDEPYLNSLLEVKDQIKAEIILLEDPDNPSASETARKEVRMTYRELVKGGSRDPLPIPAKEEYSMITLYYTSGTTGLPKGVMHHHRGAFLNAMAEVLEHQMDLNSVYLWTLPMFHAASWGFSWATVAVGATNVCLDKVDYPLIYRLVEKERVTHMCAAPTVYVNLADYMKRNNLKFSNRVHMLVAGAAPAPATLKAMQEIGGYMCHVYGLTETYGPHSICEWRREWDSLPLEEQAKLKARQGIPYVSFEMDVFDANGKPVPWDGKTIGEVVMRGHNVALGYYKNPEKTAESFRDGWFHSGDAAVVHPDGYIEIVDRFKDLINTGGEKVSSILVEKTLMEIPGVKAVAVYGTPDEKWGEVVTARIELQEGVKLTEEEVIKFCKERLAHFECPKIVEFGPIPMTATGKMQKYVLRNEAKAKANKEKS | Function: Catalyzes the ligation of coenzyme A (CoA) to 4-hydroxybutyrate (4HB). It can also use butyrate, valerate, propionate, acetate and 3-hydroxybutyrate (3HB) as substrates.
Catalytic Activity: 4-hydroxybutanoate + ATP + CoA = 4-hydroxybutanoyl-CoA + AMP + diphosphate
Sequence Mass (Da): 62011
Sequence Length: 549
EC: 6.2.1.40
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P45856 | MEIKQIMVAGAGQMGSGIAQTAADAGFYVRMYDVNPEAAEAGLKRLKKQLARDAEKGKRTETEVKSVINRISISQTLEEAEHADIVIEAIAENMAAKTEMFKTLDRICPPHTILASNTSSLPITEIAAVTNRPQRVIGMHFMNPVPVMKLVEVIRGLATSEETALDVMALAEKMGKTAVEVNDFPGFVSNRVLLPMINEAIYCVYEGVAKPEAIDEVMKLGMNHPMGPLALADFIGLDTCLSIMEVLHSGLGDSKYRPCPLLRKYVKAGWLGKKSGRGFYDYEEKTS | Catalytic Activity: (3S)-3-hydroxybutanoyl-CoA + NADP(+) = acetoacetyl-CoA + H(+) + NADPH
Sequence Mass (Da): 31394
Sequence Length: 287
Pathway: Lipid metabolism; butanoate metabolism.
EC: 1.1.1.157
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Q45223 | MAAVIKKVGVIGAGQMGNGIAHVAALAGFDVVLNDVSADRLKSGMATINGNLARQVSKKVVTEEAKTKALSRIVAAEKLDDLADCDLVIETAVEKEEVKRKIFHELCAVLKPEAIVASDTSSISITRLAAATDRPERFIGIHFMNPVPLMELVELIRGIATDDATFEASKEFVAKLGKQVAVSEDFPAFIVNRILLPMINEAIYTLYEGVGNVEAIDAAMKLGAHHPMGPLELADFIGLDTCLSIMQVLHEGLADSKYRPCPLLVKYVEAGWLGRKTQRGFYDYRGAKPVPTR | Catalytic Activity: (3S)-3-hydroxybutanoyl-CoA + NADP(+) = acetoacetyl-CoA + H(+) + NADPH
Sequence Mass (Da): 31716
Sequence Length: 293
Pathway: Lipid metabolism; butanoate metabolism.
EC: 1.1.1.157
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P52041 | MKKVCVIGAGTMGSGIAQAFAAKGFEVVLRDIKDEFVDRGLDFINKNLSKLVKKGKIEEATKVEILTRISGTVDLNMAADCDLVIEAAVERMDIKKQIFADLDNICKPETILASNTSSLSITEVASATKRPDKVIGMHFFNPAPVMKLVEVIRGIATSQETFDAVKETSIAIGKDPVEVAEAPGFVVNRILIPMINEAVGILAEGIASVEDIDKAMKLGANHPMGPLELGDFIGLDICLAIMDVLYSETGDSKYRPHTLLKKYVRAGWLGRKSGKGFYDYSK | Catalytic Activity: (3S)-3-hydroxybutanoyl-CoA + NADP(+) = acetoacetyl-CoA + H(+) + NADPH
Sequence Mass (Da): 30583
Sequence Length: 282
Pathway: Lipid metabolism; butanoate metabolism.
EC: 1.1.1.157
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P45364 | MKLAVIGSGTMGSGIVQTFASCGHDVCLKSRTQGAIDKCLALLDKNLTKLVTKGKWMKATKAEILSHVSSTTNYEDLKDMDLIIEASVEDMNIKKDVFKLLDELCKEDTILATNTSSLSITEIASSTKRPDKVIGMHFFNPVPMMKLVEVISGQLTSKVTFDTVFELSKSINKVPVDVSESPGFVVNRILIPMINEAVGIYADGVASKEEIDEAMKLGANHPMGPLALGDLIGLDVVLAIMNVLYTEFGDTKYTAHPLLAKMVRANQLGRKTKIGFYDYNK | Catalytic Activity: (3S)-3-hydroxybutanoyl-CoA + NADP(+) = acetoacetyl-CoA + H(+) + NADPH
Sequence Mass (Da): 30668
Sequence Length: 281
Pathway: Lipid metabolism; butanoate metabolism.
EC: 1.1.1.157
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P81343 | MKKVHVLGAGTMGAGI | Catalytic Activity: (3S)-3-hydroxybutanoyl-CoA + NADP(+) = acetoacetyl-CoA + H(+) + NADPH
Sequence Mass (Da): 1570
Sequence Length: 16
Pathway: Lipid metabolism; butanoate metabolism.
EC: 1.1.1.157
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P0C2T3 | MAENSNIDDIKAPLLAALGAADLALATVNELITNLRERAEETRTDTRSRVEESRARLTKLQEDLPEQLTELREKFTAEELRKAAEGYLEAATSRYNELVERGEAALERLRSQQSFEEVSARAEGYVDQAVELTQEALGTVASQTRAVGERAAKLVGIELPKKAAPAKKAAPAKKAAPAKKAAAKKAPAKKAAAKKVTQK | Function: Required for extrapulmonary dissemination. Mediates adherence to epithelial cells by binding to sulfated glycoconjugates present at the surface of these cells; binds heparin, dextran sulfate, fucoidan and chondroitin sulfate. Promotes hemagglutination of erythrocytes of certain host species. Induces mycobacterial aggregation.
PTM: Glycosylated. Glycosylation may protect the protein from proteolytic degradation and be important for hemagglutination. It suggests that the carbohydrate moiety may be located within the C-terminal domain of HbhA (By similarity).
Sequence Mass (Da): 21534
Sequence Length: 199
Subcellular Location: Cell surface
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Q7N4V8 | MSQLFVCTVEELPDGGARKVEYTPDIALFHYDGEFFAVDDRCSHGNASISEGYLEDNATVECPLHTASFCLRTGKALCLPATDPLKTYPVVVKDGNIYITVSEEQ | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Part of the multicomponent 3-phenylpropionate dioxygenase, that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively. This protein seems to be a 2Fe-2S ferredoxin.
Sequence Mass (Da): 11536
Sequence Length: 105
Pathway: Aromatic compound metabolism; 3-phenylpropanoate degradation.
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Q8XA71 | MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDEQHLPYERPPLSKSMLLEDSPQLQSVLPAHWWQENNVHLHSGVTIKTLGRDTRELVLANGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGISANDQLAREANLDTTNGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNHAQIAAAAMLGLPLPLLPPPWFWSDQYSDNLQFIGDMRGDDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRSIRKWIQSGKTFDAKQLTDENIALKSL | Function: Part of the multicomponent 3-phenylpropionate dioxygenase, that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively.
Catalytic Activity: H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 43906
Sequence Length: 400
Pathway: Aromatic compound metabolism; 3-phenylpropanoate degradation.
EC: 1.18.1.3
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Q9I4K0 | MSNERDTSRTPTPDPAEHNAFFPSPYSLSQYTSAKTDFDGADYPTPYKGGKKVLMIGTDERYILMQNASMFSTGNHPVEMLLPMYHLDKAGFEFDVATLSGNPVKLEMWAMPGEDEAVKSIYAKYLPKLKAPRKLADLLEQAVADDSPYAAVFVPGGHGVLAGIPHSREVKRLLNAFLAKDRYIITLCHGPACLLAPAVEEKPEDYPFKGYEICVFPDALDTGANLEIGYMPGPLPWLVGENLQKLGVKILNKGITGQVHRDRKLLTGDSPLASNNLGKLAAKTLLEAFAR | Function: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress.
Catalytic Activity: H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate
Sequence Mass (Da): 31899
Sequence Length: 291
Subcellular Location: Cytoplasm
EC: 3.1.2.-
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A6QEK3 | MSQDVNELSKQPTPDKAEDNAFFPSPYSLSQYTAPKTDFDGVEHKGAYKDGKWKVLMIAAEERYVLLENGKMFSTGNHPVEMLLPLHHLMEAGFDVDVATLSGYPVKLELWAMPTEDEAVISTYNKLKEKLKQPKKLADVIKNELGPDSDYLSVFIPGGHAAVVGISESEDVQQTLDWALDNDRFIVTLCHGPAALLSAGINREKSPLEGYSVCVFPDSLDEGANIEIGYLPGRLKWLVADLLTKQGLKVVNDDMTGRTLKDRKLLTGDSPLASNELGKLAVNEMLNAIQNK | Function: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress.
Catalytic Activity: H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate
Sequence Mass (Da): 32177
Sequence Length: 292
Subcellular Location: Cytoplasm
EC: 3.1.2.-
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A0LNW5 | MFCYQCEQTAKGEGCTKIGVCGKQPEVADLQDLLLYALKGLALHAVEGAKVGVNDHETNVFTCEALFSTLTNVNFDPARFQVLIPRVVEYREKLKAKVKAAGGKVDFADPAATFTPAKTLEGLVAQGANVGLKSEPELPPDIVSLKHTLLFGLKGISAYADHANILGQHDDAVYAFIYEALAATLRKDIELGDWLKLVLKCGEMNLRTMELLDAANTGVYGHPVPTSVPLGPKQGKAILVSGHDLKDLEELLKQTEGKGINIYTHGEMLPTHGYPGLKKYAHFYGHYGTAWQNQQKEFSKFPGAILMTTNCIQKPQQAYTGNIFTTGLVGWPDVPHVTNRDFSPVIERALALPGFPETVNGKSVMVGFGRNTILGVADKVIEAVKNKNIRHFFLVAGCDGAKPGRNYYTEFVEKVPKDCVVLTLACGKFRFFDKDLGTIGGLPRLMDVGQCNDAYSAIQVAVALAKAFNCGVNDLPLSLVLSWYEQKAVAILLTLLYLGIRNIRLGPSLPAFVSGNVLDVLVKNFDIKPITTPDEDLKAILG | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
Catalytic Activity: A + H2O + NH4(+) = AH2 + H(+) + hydroxylamine
Sequence Mass (Da): 58923
Sequence Length: 542
Subcellular Location: Cytoplasm
EC: 1.7.99.1
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A6LL16 | MFCYQCSEASKGVGCTTIGVCGKTPDVANLQDLLIWLTRGISYWALKAKEYGVKDDEVNLFVAEALFSTITNVNFSAKRMVEFIERAFELRERIKHRFLEAYAEKEGKTFDEKVPEAAEWHKKGGVDLYELKGMEVGVLFDKDEDIRSLKQLLIYGLKGIAAYTDHAYILKHTNDDILYFIQKGLVETLREDITVDELVSLVLEAGKVAVDAMALLDKANTTEFGNPEITEVYTGTYNTPAILVSGHDLLDLEELLKQTEGTGIMVYTHGEMLPAHAYPKLKKYKHLAGNFGSAWWKQSEEFEEFGGAILMTTNCLVPPKESYKDRVFTTGLVGFDKLTHIPNRTDGKPKDFSPVIKKALELGPIPERKGKKIVIGFAHDQVSRLLDKVIDAVKSGAIKKFVVMGGCDGRHKEREYYTEFAKKLPKDTVILTAGCAKYRYNHLDLGDIGGIPRVLDAGQCNDSYSLVVTALKLKEALGLDDINDLPIVYNIAWYEQKAIAVLLALLYLGVKGIRLGPVLPAFISPNVLKVLVDKFNIAPITTVEEDLKVLLS | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
Catalytic Activity: A + H2O + NH4(+) = AH2 + H(+) + hydroxylamine
Sequence Mass (Da): 61544
Sequence Length: 552
Subcellular Location: Cytoplasm
EC: 1.7.99.1
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Q9X0Q4 | MQMFCYQCSQTANGTGCTEYGVCGKSPTVARLQDNLVFAIKGISAYYYHARELGYDDPEIAGFLDEALYSTLTNVNFDAQSFVEYALEAGRMNLKAMQLLKKAHIETYGEPTPVEVETGTKKGKGIIVTGHNLKALEELLKQVEGTNVYVYTHSEMLPAHGYPGLRKYKNLIGNLGKAWYDQRKLFAEYPVAILGTSNCVLIPSESYRDRMFTTSIARLPGVKHIDGYDYTEVIEKAKSLPDLEEKPGSYKLRTGFSTSVVVSLADKIKELVEAGKIKHFLVVGGCDVPFKRNEYYREFVQKLPKETVVITLACGKFRINDLDLGDIDGIPRLIDVGQCNDTIVAIEIAQALAKVFGVEVTELPLTLVLTWMEQKAVAILWTLLALGLKNIYVGPVLPAWVNEDILKVLTAEFGLKTISEPEKDIKEILKV | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
Catalytic Activity: A + H2O + NH4(+) = AH2 + H(+) + hydroxylamine
Sequence Mass (Da): 47958
Sequence Length: 431
Subcellular Location: Cytoplasm
EC: 1.7.99.1
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B5YHX5 | MFCRQCEQTANPCTKLGVCGKQPDTAYLQDLLTYALQGLATYAKEALKESSQTQNVMKRINKFTVEALFATLTNVNFDSEAIKNFIYEAVKLRDELKQMGFKVQETESCKFQPADNLQELVKQGEEANQKIFHSSSNEDVQSLKEITLYSLRGIAAYTDHAQILGQEDEKVYAFIYEALDAMQRNGDLDFWLNMVLRAGEINLRAMELLDAANTGRYGHPVPTPVPLGHKKGKAIVVSGHDLRDLELLLQQTEGKGIYVYTHGEMLPCHGYPELKKYKHFYGHYGTAWQNQQREFAQFPGAILMTTNCIIKPQESYKDRIFTTGVVGWPGVKHIKDKDFTPVIEKALELPGFTEDKEDKTVMVGFARNSVLSVADKVIELVKAGKIRHFFLVGGCDGAKPGRSYYTEFVEKTPKDTIVLTLACGKFRFFDKELGSINGIPRLLDVGQCNDAYSAIQIALALSKAFNVSINELPLSLILSWFEQKAVAILTTLLYLGIKNIRLGPTLPAFVSPNVLKVLVDNFGIKPIKTAEEDLKDILR | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
Catalytic Activity: A + H2O + NH4(+) = AH2 + H(+) + hydroxylamine
Sequence Mass (Da): 60434
Sequence Length: 539
Subcellular Location: Cytoplasm
EC: 1.7.99.1
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Q96DB2 | MLHTTQLYQHVPETRWPIVYSPRYNITFMGLEKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKWSFAVATITEIPPVIFLPNFLVQRKVLRPLRTQTGGTIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHIYPGDRFAKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNLFGLGLIGPESPSVSAQNSDTPLLPPAVP | Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
Sequence Mass (Da): 39183
Sequence Length: 347
Subcellular Location: Nucleus
EC: 3.5.1.98
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Q91WA3 | MPHATQLYQHVPEKRWPIVYSPRYNITFMGLEKLHPFDAGKWGKVINFLKEEKLLSDGMLVEAREASEEDLLVVHTRRYLNELKWSFVVATITEIPPVIFLPNFLVQRKVLRPLRTQTGGTIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERVEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYNRHIYPGDRFAKEAIRRKVELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKRDEVVFRVVRAHDIPILMVTSGGYQKRTARIIADSILNLHDLGLIGPEFPCVSAQNSGIPLLSCAVP | Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity).
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
Sequence Mass (Da): 39157
Sequence Length: 347
Subcellular Location: Nucleus
EC: 3.5.1.98
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Q55BW2 | MEYNTILNNTSKTRVCYFFDQDVGNYFYGPYHPMKPHRLCLTNNLVLNYGLHKKMHLYKARPADAEDMLKFHSEDYVDFLERVTPENINEWKDVKRFHIGEDCPVFPGLYDYCSIYSGGSIEGALKLNHRMYDIAINWSGGLHHARKDEASGFCYVNDIVLAILELLKFHARVLYIDIDVHHGDGVQEAFYLTDRVMTVSFHKFGGDFFPGTGDIDEIGAKTGKLYSVNVPLADGIDDKNYLNIFKPVIQGVMDYYRPSVIVLQCGADSLRFDRLGCFNLTIKGHAECVRFVKSFNIPTLVLGGGGYTVRNVARCWTYETSVCVDTEVNNELPYNDYIQFYSPDFQLIPDYTGLPFKYENANTKSYLESLRIKILENLRILQWAPSVQIQDVPPDIMPIDFDRDEDSKENMDKRKKKHNDFS | Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). May play a role in the regulation of the timing of gene expression during the development and in the definition aspects of the phenotype that mediate social behavior in genetically heterogeneous groups.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
Sequence Mass (Da): 48641
Sequence Length: 422
Subcellular Location: Nucleus
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Q941D6 | MSMALIVRPFFVPGSAGISGSRNICKKNQWRKYLLKPSGSSINCSFSTEKNPLLPSIQQLADARLIYSVSAALGHNKESHPECSARVPAIVNALEMNELTPKFRGSQILELANFKTATVEDIANVHDKAYVFGLEKAMDEASDSGLIFIEGSGPTYATSTTFQDSLIAAGAGMALVDSVIAASRNSVDPPIGFALIRPPGHHAVPKGPMGFCVFGNVAIAARHAQRTHGLKRIFIIDFDVHHGNGTNDAFTEDPDIFFLSTHQDGSYPGTGKISDIGKGKGEGTTLNLPLPGGSGDIAMRTVFEEIIVPCAQRFKPDIILVSAGYDAHVLDPLANLQFTTATYYSLAKDIKRLAKEVCGGRCVFFLEGGYNLESLSSSVADSFRALLGEDSLASEFDNPAYLYDEPMRKVRDAIQRAKSIHCL | Cofactor: Binds 1 zinc ion per subunit.
Function: Regulates lysine acetylation levels of plastid proteins related to photosynthesis . Involved in the regulation of the activation state of RuBisCO, which is controlled by lysine acetylation of RuBisCO activase under low-light conditions . Associates with alpha- and beta-tubulins and deacetylate alpha-tubulin . Does not seem to be required for the cellular patterning in the root epidermis . Involved in the regulation of melatonin biosynthesis by catalyzing the deacetylation of N-acetylserotonin to produce serotonin . N-acetylserotonin is methylated by acetylserotonin O-methyltransferase (ASMT) to produce melatonin (N-acetyl-5-methoxytryptamine) (Probable). Deacetylates melatonin to produce 5-methoxytryptamine . In vitro, deacetylates N-acetyltyramine and N-acetyltryptamine to produce tyramine and tryptamine, respectively .
Catalytic Activity: H2O + N-acetylserotonin = acetate + serotonin
Sequence Mass (Da): 45577
Sequence Length: 423
Subcellular Location: Nucleus
EC: 3.5.1.-
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Q8GXJ1 | MVVETIERSCEGSKRRHVNGGDIAVPCSGEECSNGDINVAPGVSAKRARVSREMTFEDIYGADALLNDDDDEDDDCDWEPVQAPMEFVKWCCVNCTMSNPGDMVHCCICGEHKESGILRHGYLASPFFKDTGLIEVEEKYGGSSSATSSTAVGFDERMLLHSEFEVKAQPHPERPDRLRAIAASLATAGVFPGRCLPINAREITKQELQMVHTSEHVDAVDTTSQLLYSYFTSDTYANEYSARAARLAAGLCADLATDIFTGRVKNGFALVRPPGHHAGVRHAMGFCLHNNAAVAALVAQAAGAKKVLIVDWDVHHGNGTQEIFEQNKSVLYISLHRHEGGNFYPGTGAADEVGSNGGEGYCVNVPWSCGGVGDKDYIFAFQHVVLPIASAFSPDFVIISAGFDAARGDPLGCCDVTPAGYSRMTQMLGDLCGGKMLVILEGGYNLRSISASATAVIKVLLGENPENELPIATTPSVAGLQTVLDVLNIQLEFWPSLAISYSKLLSELEARLIENKKNQMKRKVVRVPTWWKWGRKKLLYNFLSARMISRSK | Cofactor: Binds 1 zinc ion per subunit.
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) . Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events . Histone deacetylases act via the formation of large multiprotein complexes (Probable). Represses chlorophyll biosynthesis and photosynthesis in the dark . Is recruited by PIF3 to the promoters of chlorophyll biosynthetic and photosynthetic genes, and represses their transcription by histone deacetylation . Involved in the repression of hypocotyl cell elongation to promote photomorphogenesis . Is recruited by HY5 to the promoters of a subset of cell wall organization and auxin signaling-related genes, and represses gene expression by decreasing the levels of histone H4 acetylation in a light-dependent manner . Promotes abscisic acid (ABA) signaling . Is recruited by MYB96 to the promoters of a subset of Rho GTPase (ROP) genes, which repress ABA signaling at the early stages of signal transduction . Represses ROP expression by removing acetyl groups of histone H3 and H4 from the cognate regions, particularly in the presence of ABA . Represses the plant response to elevated ambient temperature by directly repressing warm temperature-responsive genes .
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
Sequence Mass (Da): 60020
Sequence Length: 552
Subcellular Location: Nucleus
EC: 3.5.1.98
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Q9LXN8 | MAFSMLFTGHAECVKFVKKFNLPLLVTGGGGYTKENVARCWTVETGILLDTELPNEISENDYIKYFAPDFSLKIPGGHIENLNTKSYISSIKVQILENLRYIQHAPSVQMQEVPPDFYIPDFDEDEQNPDVRVDQRSRDKQIQRDDEYFDGDNDNDAS | Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
Sequence Mass (Da): 18116
Sequence Length: 158
Subcellular Location: Nucleus
EC: 3.5.1.98
|
Q8LRK8 | MLLKFEASSELRLVDPSVSLTVLRKIRLSHLPDMTMTSESSGKKCGEGDGKVAGKSQRKVGLVYDETMCKHDTPNGKVDVECPDRIRVIWEKLQLAGVTQRCVVLGGSKAEDKHLKLVHTKKHVNLVKSISTKKKDSRRNKIASQLDSIYLNGGSSEAAYLAAGSVVKVAEKVAEGELDCGFAIVRPPGHHAESDEAMGFCLFNNVAVAASFLLNERPDLDVKKILIVDWDIHHGNGTQKMFWKDSRVLIFSVHRHDHGSFYPFGDDGDFNMVGEGPGEGFNINVPWEQGGCGDADYLAVWNHILIPVTKEFKPDIILLSAGFDAAIGDPLGGCCVTPYGYSVMLKKLMEFAHGKIVLALEGGYNLESLGKSSLACVQVLLEDKQIHGSSETYPLESTRRVIQAVRERLCTYWPSLDASMASNENLKNPSAERNSADALLREVEELKSLMAARDGELEARRKELKAKNKELEANEKELEAGLMLIRAREDVICGLHAKIESLQQERDEAVAKAERIDKELQEDRARSQEFKEDTEFCLSTLRREKELAIMAKNKDLEAKEKELEARLMLVHAREDKIHAKIERLQQERDEAVAKAERIDKELQEDRSRSRVGNGSFAFSQEFYEDMDLDELEPLSPEFNEDMDSEELEPFQVIKKNMERSHKKFIKDMECIKFIASERARVL | Cofactor: Binds 1 zinc ion per subunit.
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) . Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (Probable). Histone deacetylases act via the formation of large multiprotein complexes (Probable). Required for appropriate cellular patterning in the root epidermis . Involved in the differentiation of hair and non-hair cells in the root epidermis . Is not directly involved in the regulation of the expression of pattern genes . Regulates the transcription of certain kinase genes, which are components of a positional information relay system, by changing their histone acetylation status .
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
Sequence Mass (Da): 76634
Sequence Length: 682
Subcellular Location: Nucleus
EC: 3.5.1.98
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O22446 | MDTGGNSLASGPDGVKRKVCYFYDPEVGNYYYGQGHPMKPHRIRMTHALLAHYGLLQHMQVLKPFPARDRDLCRFHADDYVSFLRSITPETQQDQIRQLKRFNVGEDCPVFDGLYSFCQTYAGGSVGGSVKLNHGLCDIAINWAGGLHHAKKCEASGFCYVNDIVLAILELLKQHERVLYVDIDIHHGDGVEEAFYATDRVMTVSFHKFGDYFPGTGHIQDIGYGSGKYYSLNVPLDDGIDDESYHLLFKPIMGKVMEIFRPGAVVLQCGADSLSGDRLGCFNLSIKGHAECVKFMRSFNVPLLLLGGGGYTIRNVARCWCYETGVALGVEVEDKMPEHEYYEYFGPDYTLHVAPSNMENKNSRQMLEEIRNDLLHNLSKLQHAPSVPFQERPPDTETPEVDEDQEDGDKRWDPDSDMDVDDDRKPIPSRVKREAVEPDTKDKDGLKGIMERGKGCEVEVDESGSTKVTGVNPVGVEEASVKMEEEGTNKGGAEQAFPPKT | Cofactor: Binds 1 zinc ion per subunit.
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. HDA19 is involved in jasmonic acid and ethylene signaling of pathogen response. Part of a repressor complex including APETALA2 (AP2) and TOPLESS (TPL) that control the expression domains of numerous floral organ identity genes . Involved in negative regulation of salinity stress response . Represses the expression of stress tolerance-related genes, genes coding for late embryogenesis abundant (LEA) proteins that prevent protein aggregation, and positive regulators of abscisic acid (ABA) signaling, such as ABI5 and NAC019 .
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
Sequence Mass (Da): 56023
Sequence Length: 501
Subcellular Location: Nucleus
EC: 3.5.1.98
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P56521 | MDPSSAGSGGNSLPSVGPDGQKRRVCYFYDPDVGNYYYGQGHPMKPHRIRMTHSLLARYGLLNQMQVYRPNPARERELCRFHAEEYINFLRSVTPETQQDQIRLLKRFNVGEECPVLDGLYSFCQTYAGASVGGAVKFNHGHDIAINWSGGLHHAKKCEASGFCYVNDIVLAILELLKHHERVLYVDIDIHHGDGVEEAFYTTDRVMTVSFHKFGDYFPGTGDIRDIGHSKGKYYSLNVPLDDGIDDESYQSLFKPIMGKVMEVFRPGAVVLQCGADSLSGDRLGCFNLSIKGHAECVRYMRSFNVPLLLLGGGGYTIRNVARCWCYETGVALGQEPEDKMPVNEYYEYFGPDYTLHVAPSNMENKNTRQQLDDIRSKLSKLRHAPSVHFQERVPDTEIPEQDEDQDDPDERHDPDSDMEVDDHKAVEESSRRSILGIKIKREFGENATRVQDGGRVASEHRGLEPMAEDIGSSKQAPQADASAMAIDEPSNVKNEPESSTKLQGQAAAYHKP | Cofactor: Binds 1 zinc ion per subunit.
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
Sequence Mass (Da): 57546
Sequence Length: 513
Subcellular Location: Nucleus
EC: 3.5.1.98
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O42227 | MALSQGTKKKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKASAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDISVNWSGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVVYIDIDIHHGDGVEEAFYTTDRVMSVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMTKVMEMFQPSAVVLQCGADSLSGDRLGCFNLTIKGHAKCVEFIKTFNLPMLMLGGGGYTIRNVARCWTYETAVALDSEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDSVHDDSGEEDEEDPDKRISIRSSDKRIACDEEFSDSEDEGEGGRKNVANFKKVKRVKTEEEKEGEDKKDVKEEEKAKDEKTDSKRVKEETKSV | Function: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) . Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events . Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Also functions as deacetylase for non-histone proteins. In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones (By similarity).
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
Sequence Mass (Da): 54893
Sequence Length: 480
Subcellular Location: Nucleus
EC: 3.5.1.98
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