ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q6D3A9 | MSSPVPGLMLPEKRVVEVRNLSVYFEQQGQRTDAVRNLTFSVDRGETLAIVGESGSGKSVTSLALMRLVEHAGGVIHQGDMLFRRRDGQVLDLRGARQRVMRTLRGADLAMIFQEPMTSLNPVFPVGEQIAESIRLHQRMDRRAARAETLRMLDLVRIPEARNVLDRYPHQLSGGMRQRVMIAMALSCKPSLLIADEPTTALDVTIQAQILQLIRVLQREMDMAVIFITHDMGVVAEVAERVLVMHRGESVEAASVGQIFAAPQHPYTQGLLAAVPALGSMRGQPFPAKFPLLDQNTARIVDNVPQDTVPAHAEPILQVS... | Function: Part of the ABC transporter complex GsiABCD involved in glutathione import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + glutathione(out) + H2O = ADP + glutathione(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 69390
Sequence Len... |
E3PJ86 | MFWRDITLSVWRKKTTGLKTKKRLLPLVLAAALCSSPVWAEEATFTANFKDTDLKSFIETVGANLNKTIIMGPGVQGKVSIRTMTPLNERQYYQLFLNLLEAQGYAVVPMENDVLKVVKSSAAKVEPLPLVGEGSDNYAGDEMVTKVVPVRNVSVRELAPILRQMIDSAGSGNVVNYDPSNVIMLTGRASVVERLTEVIQRVDHAGNRTEEVIPLDNASASEIARVLESLTKNSGENQPATLKSQIVADERTNSVIVSGDPATRDKMRRLIRRLDSEMERSGNSQVFYLKYSKAEDLVDVLKQVSGTLTAAKEEAEGTVG... | Function: Part of a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane (Probable). This subunit forms the outer membrane channel (Probable).
Sequence Mass (Da): 74202
Sequence Length: 686
Domain: The N0 region interacts in the periplasm w... |
P45758 | MKGLNKITCCLLAALLMPCAGHAENEQYGANFNNADIRQFVEIVGQHLGKTILIDPSVQGTISVRSNDTFSQQEYYQFFLSILDLYGYSVITLDNGFLKVVRSANVKTSPGMIADSSRPGVGDELVTRIVPLENVPARDLAPLLRQMMDAGSVGNVVHYEPSNVLILTGRASTINKLIEVIKRVDVIGTEKQQIIHLEYASAEDLAEILNQLISESHGKSQMPALLSAKIVADKRTNSLIISGPEKARQRITSLLKSLDVEESEEGNTRVYYLKYAKATNLVEVLTGVSEKLKDEKGNARKPSSSGAMDNVAITADEQTN... | Function: Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane. This subunit would form the outer membrane channel.
Sequence Mass (Da): 70698
Sequence Length: 650
Domain: The N0, N1, N2 and N3 domains are periplasmic, while th... |
P15644 | MIIANVIRSFSLTLLIFAALLFRPAAAEEFSASFKGTDIQEFINTVSKNLNKTVIIDPSVRGTITVRSYDMLNEEQYYQFFLSVLDVYGFAVINMNNGVLKVVRSKDAKTAAVPVASDAAPGIGDEVVTRVVPLTNVAARDLAPLLRQLNDNAGVGSVVHYEPSNVLLMTGRAAVIKRLLTIVERVDNAGDRSVVTVPLSWASAADVVKLVTELNKDTSKSALPGSMVANVVADERTNAVLVSGEPNSRQRIIAMIKQLDRQQATQGNTKVIYLKYAKASDLVEVLTGISSTMQSEKQAAKPVAALDKNIIIKAHGQTNA... | Function: Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins. Required for the translocation of pullulanase . This subunit forms the outer membrane channel (By similarity).
Sequence Mass (Da): 70658
Sequence Length: 660
Domain: The N0, N1, N2 and N3 domains... |
P35818 | MSQPLLRALFAPSSRSYVPAVLLSLALGIQAAHAENSGGNAFVPAGNQQEAHWTINLKDADIREFIDQISEITGETFVVDPRVKGQVSVVSKAQLSLSEVYQLFLSVMSTHGFTVVAQGDQARIVPNAEAKTEAGGGQSAPDRLETRVIQVQQSPVSELIPLIRPLVPQYGHLAAVPSANALIISDRSANIARIEDVIRQLDQKGSHDYSVINLRYGWVMDAAEVLNNAMSRGQAKGAAGAQVIADARTNRLIILGPPQARAKLVQLAQSLDTPTARSANTRVIRLRHNDAKTLAETLGQISEGMKNNGGQGGEQTGGGR... | Function: Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins (Probable). This subunit forms the outer membrane channel (By similarity). Among its substrates are PrpL, elastase LasB, chitin binding protein D (CbpD), aminopeptidase PaAP, and metalloprotease I... |
P45779 | MKYWLKKSSWLLAGSLLSTPLAMANEFSASFKGTDIQEFINIVGRNLEKTIIVDPSVRGKVDVRSFDTLNEEQYYSFFLSVLEVYGFAVVEMDNGVLKVIKSKDAKTSAIPVLSGEERANGDEVITQVVAVKNVSVRELSPLLRQLIDNAGAGNVVHYDPANIILITGRAAVVNRLAEIIRRVDQAGDKEIEVVELNNASAAEMVRIVEALNKTTDAQNTPEFLKPKFVADERTNSILISGDPKVRERLKRLIKQLDVEMAAKGNNRVVYLKYAKAEDLVEVLKGVSENLQAEKGTGQPTTSKRNEVMIAAHADTNSLVL... | Function: Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins. Required for secretion of cholera toxin through the outer membrane. This subunit forms the outer membrane channel.
Sequence Mass (Da): 73470
Sequence Length: 674
Domain: The N0, N1, N2 and N3 dom... |
P29041 | MSERMTPRLFPVSLLIGLLAGCATTPPPDVRRDARLDPQVGAAGATQTTAEQRADGNASAKPTPVIRRGSGTMINQSAAAAPSPTLGMASSGSATFNFEGESVQAVVKAILGDMLGQNYVIAPGVQGTVTLATPNPVSPAQALNLLEMVLGWNNARMVFSGGRYNIVPADQALAGTVAPSTASPSAARGFEVRVVPLKYISASEMKKVLEPYARPNAIVGTDASRNVITLGGTRAELENYLRTVQIFDVDWLSGMSVGVFPIQSGKAEKISADLEKVFGEQSKTPSAGMFRFMPLENANAVLVITPQPRYLDQIQQWLDR... | Function: Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins. This subunit forms the outer membrane channel.
Sequence Mass (Da): 79316
Sequence Length: 759
Domain: The N0, N1, N2 and N3 domains are periplasmic, while the secretin and S domains form a channe... |
Q01566 | MSDQPVNTPELRPVLPFSFARAQQILLLQDESVTVAEVVCVPDTPALALLEARRVAGVPLAVSQVSPEEFERQLVMRYQRDSEEARRLMEDIGNDIDFYTLAEELPDSDDLLDGEDDAPIIRLINAMLTEAIKHKASDIHIETFERHLLIRFRIDGVLREILRPQRQLASLLVSRIKVMAKLDIAEKRVPQDGRMALRIGGRAIDVRVSTLPSNYGERVVLRLLDKNSVRLDLEALGMAEHNRRQLDTLIHRPHGIILVTGPTGSGKSTTLYAALSRLNSAERNIMTVEDPIEYELEGIGQTQVNPKVDMTFARGLRAIL... | Function: ATPase component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Acts as a molecular motor to provide the energy that is required for assembly of the pseudopilus and the extrusion of substrates generated in t... |
Q00512 | MMTAPLPDIAAPAAPPRRLPFSFAKRQGLLFLCLEEQYWLACRPQVELAAIAEAQRFAGRRLPLKALGEDAFNQALAASYQHDSSAAMQLAEDLGGSLDLAALADQVPETEDLMEQEDDAPIIRLINAILGEAIRENASDIHLETFEKRLVVRFRVDGVLREVLEPKRELAALLVSRIKVMARLDIAEKRIPQDGRISLRVGGREVDIRVSTLPSANGERVVLRLLDKQAGRLNLQHLGMSERDRKLMDETVRKPHGILLVTGPTGSGKTTTLYASLTTLNDRTRNILTVEDPIEYHLEGIGQTQVNAKVDMTFARGLRA... | Function: ATPase component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Acts as a molecular motor to provide the energy that is required for assembly of the pseudopilus and the extrusion of substrates generated in t... |
P37093 | MTEMVISPAERQSIRRLPFSFANRFKLVLDWNEDFSQASIYYLAPLSMEALVETKRVVKHAFQLIELSQAEFESKLTQVYQRDSSEARQLMEDIGADSDDFFSLAEELPQNEDLLESEDDAPIIKLINAMLGEAIKEGASDIHIETFEKTLSIRFRVDGVLREVLAPSRKLSSLLVSRVKVMAKLDIAEKRVPQDGRISLRIGGRAVDVRVSTMPSSHGERVVMRLLDKNATRLDLHSLGMTAHNHDNFRRLIKRPHGIILVTGPTGSGKSTTLYAGLQELNSSERNILTVEDPIEFDIDGIGQTQVNPRVDMTFARGLR... | Cofactor: Removal of zinc reduces the enzymatic activity by about 2-fold.
Function: ATPase component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Acts as a molecular motor to provide the energy that is required for ... |
P31742 | MEQRSAETRIVEALLERRRLKDTDLVRARQLQAESGMGLLALLGRLGLVSERDHAETCAEVLGLPLVDARQLGDTPPEMLPEVQGLSLRFLKQFHLCPVGERDGRLDLWIADPYDDYAIDAVRLATGLPLLLQVGLRSEIDDLIERWYGQGRSAMGTIVETADGDASSTDDIEALRDLASEAPVIRLVNLVIQHAVELRASDIHIEPFESRLKVRYRVDGVLVEGESPPAKLTAAVISRIKIMAKLNIAERRLPQDGRIMLRVQGKELDLRVSTVPTAHGESVVMRLLDRETVVFDFYKLGFTEDFLPQFRKVLEQPHGI... | Function: ATPase component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Acts as a molecular motor to provide the energy that is required for assembly of the pseudopilus and the extrusion of substrates generated in t... |
P31743 | MTEGDSARQVRQQLREQGLTPLEVNETTEKAKREANRFVLFRRGASTSELALITRQLATLVGAGLTIEEALRAVAEQCEKAHLRSLVATVRSKVVEGYSLADSLGAFPHVFDQLFRSMVAAGEKSGHLEKVLNRLADYTEQRQHMRTKLLQAMIYPIVLTLVAVGVISILLTAVVPKVVAQFEHMGQQLPATTRFLIGTSELMQHYGLWFLLLLFIGGFVWRWWLTDEKRRRHWHQVVLRLPVIGRVSRGLNTARFARTLSILNASAVPLLEGMKIAGEVLSNDFARTRIGEATERVREGTSLRKALDETKIFPPMMLHM... | Function: Component of the type II secretion system inner membrane complex required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43464
Sequence Length: 388
Subcellular Location: Cell inner ... |
P42769 | MVTVKLYGMAYSTCTKRVYTTAKEIGVDVKIVPVDLMKGEHKEPAYLDNYHPFGVIPVLEDEDGTKIYESRAISRYLVAKYGKGSSLLPSPSDPKAYGLFEQAASVEYSSFDPPASSLAYERVFAGMRGLKTNEELAKKYVDTLNAKMDGYERILSKQKYLAGNDFTLADLFHLPYGAMVAQLEPTVLDSKPHVKAWWAASLRVIPGRLLRNSSKEFM | Function: Specifically catalyzes the conjugation of synthetic 1-chloro-2,4-ditrobenzene to GSH. Also functions as a glutathione peroxidase, converting linoleate oxidation products into their corresponding hydroxyacids. This enzyme may thus serve to protect the cell from oxygen toxicity as well as from exogenous toxins ... |
P12653 | MAPMKLYGAVMSWNLTRCATALEEAGSDYEIVPINFATAEHKSPEHLVRNPFGQVPALQDGDLYLFESRAICKYAARKNKPELLREGNLEEAAMVDVWIEVEANQYTAALNPILFQVLISPMLGGTTDQKVVDENLEKLKKVLEVYEARLTKCKYLAGDFLSLADLNHVSVTLCLFATPYASVLDAYPHVKAWWSGLMERPSVQKVAALMKPSA | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the detoxification of certain herbicides.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 23822
Sequence Length: 214
EC: 2.5.1.... |
O65857 | MTPVKVFGPAQSTNVARVLLCLEEVGAEYEVVNVDFTVMEHKSPEHLKRNPFGQIPAFQDGDLYLFESRAIGKYILRKYKTREADLLREGNLREAAMVDVWTEVETHQYNSAISPIVYECIINPAMRGIPTNQKVVDESAEKLKKVLEVYEARLSQSTYLAGDFVSFADLNHFPYTFYFMGTPYASLFDSYPHVKAWWERLMARPSVKKLAAVMAPQGA | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 24924
Sequence Length: 219
EC: 2.5.1.18
|
P84983 | VLDIYEQKLGQTRVLDIYEQK | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. In plants, may have a detoxification role against certain herbicides (By similarity).
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 2552
... |
P30110 | MSPVKVFGHPMLTNVARVLLFLEEVGAEYELVPMDFVAGEHKRPQHVQLNPFAKMPGFQDGDLVLFESRAIAKYILRKYGGTAGLDLLGENSGIEELAMVDVWTEVEAQQYYPAISPVVFECIIIPFIIPGGGAAPNQTVVDESLERLRGVLGIYEARLEKSRYLAGDSITFADLNHIPFTFYFMTTPYAKVFDDYPKVKAWWEMLMARPAVQRVCKHMPTEFKLGAQY | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 25828
Sequence Length: 229
EC: 2.5.1.18
|
P46422 | MAGIKVFGHPASIATRRVLIALHEKNLDFELVHVELKDGEHKKEPFLSRNPFGQVPAFEDGDLKLFESRAITQYIAHRYENQGTNLLQTDSKNISQYAIMAIGMQVEDHQFDPVASKLAFEQIFKSIYGLTTDEAVVAEEEAKLAKVLDVYEARLKEFKYLAGETFTLTDLHHIPAIQYLLGTPTKKLFTERPRVNEWVAEITKRPASEKVQ | Function: Binds auxin, endogenous flavonoids and the phytoalexin camalexin and may be involved in regulating the binding and transport of small bioactive natural products and defense-related compounds during plant stress. Binds a series of heterocyclic compounds, including lumichrome, harmane, norharmane and indole-3-a... |
P84984 | LGKLLDVYESRLLDVYESRVLDIYESRLGKVLDIYESR | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. In plants, may have a detoxification role against certain herbicides (By similarity).
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 4519
... |
P04907 | MAPLKLYGMPLSPNVVRVATVLNEKGLDFEIVPVDLTTGAHKQPDFLALNPFGQIPALVDGDEVLFESRAINRYIASKYASEGTDLLPATASAAKLEVWLEVESHHFHPNASPLVFQLLVRPLLGGAPDAAVVEKHAEQLAKVLDVYEAHLARNKYLAGDEFTLADANHALLPALTSARPPRPGCVAARPHVKAWWEAIAARPAFQKTVAAIPLPPPPSSSA | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles . Involved in the detoxification of certain herbicides .
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 23849
Sequence Length: 222
EC: 2.5.... |
Q84TK0 | MDCLQMVFKLFPNWKREAEVKKLVAGYKVHGDPFSTNTRRVLAVLHEKRLSYEPITVKLQTGEHKTEPFLSLNPFGQVPVFEDGSVKLYESRAITQYIAYVHSSRGTQLLNLRSHETMATLTMWMEIEAHQFDPPASKLTWEQVIKPIYGLETDQTIVKENEAILEKVLNIYEKRLEESRFLACNSFTLVDLHHLPNIQYLLGTPTKKLFEKRSKVRKWVDEITSREAWKMACDQEKSWFNKPRN | Function: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Mass (Da): 28701
Sequ... |
P46420 | MATPAVKVYGWAISPFVSRALLALEEAGVDYELVPMSRQDGDHRRPEHLARNPFGKVPVLEDGDLTLFESRAIARHVLRKHKPELLGGGRLEQTAMVDVWLEVEAHQLSPPAIAIVVECVFAPFLGRERNQAVVDENVEKLKKVLEVYEARLATCTYLAGDFLSLADLSPFTIMHCLMATEYAALVHALPHVSAWWQGLAARPAANKVAQFMPVGAGAPKEQE | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the detoxification of certain herbicides. Most active with substrates possessing a chloroacetamide structure. Trans-cinnamic acid and 1-chloro-2,4-dinitrobenzene are not effective substrates.... |
P42760 | MAGIKVFGHPASTATRRVLIALHEKNVDFEFVHVELKDGEHKKEPFILRNPFGKVPAFEDGDFKIFESRAITQYIAHEFSDKGNNLLSTGKDMAIIAMGIEIESHEFDPVGSKLVWEQVLKPLYGMTTDKTVVEEEEAKLAKVLDVYEHRLGESKYLASDHFTLVDLHTIPVIQYLLGTPTKKLFDERPHVSAWVADITSRPSAQKVL | Function: Involved in camalexin biosynthesis by probably catalyzing the conjugation of GSH with indole-3-acetonitrile (IAN). May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Catalyt... |
Q96266 | MGAIQARLPLFLSPPSIKHHTFLHSSSSNSNFKIRSNKSSSSSSSSIIMASIKVHGVPMSTATMRVLATLYEKDLQFELIPVDMRAGAHKQEAHLALNPFGQIPALEDGDLTLFESRAITQYLAEEYSEKGEKLISQDCKKVKATTNVWLQVEGQQFDPNASKLAFERVFKGMFGMTTDPAAVQELEGKLQKVLDVYEARLAKSEFLAGDSFTLADLHHLPAIHYLLGTDSKVLFDSRPKVSEWIKKISARPAWAKVIDLQKQ | Function: In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and glutathione peroxidase activity toward cumene hydroperoxide and linoleic acid-13-hydroperoxide. May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobi... |
O80852 | MVLKVYGPHFASPKRALVTLIEKGVAFETIPVDLMKGEHKQPAYLALQPFGTVPAVVDGDYKIFESRAVMRYVAEKYRSQGPDLLGKTVEDRGQVEQWLDVEATTYHPPLLNLTLHIMFASVMGFPSDEKLIKESEEKLAGVLDVYEAHLSKSKYLAGDFVSLADLAHLPFTDYLVGPIGKAYMIKDRKHVSAWWDDISSRPAWKETVAKYSFPA | Function: In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC), and glutathione peroxidase activity toward cumene hydroperoxide and linoleic acid-13-hydroperoxide. May be involved in the conjugation of reduced glutathione to a wide number of e... |
O48843 | MDKFNPKKEKTVKKRALKVLTEISPTPLFSMLFLLHISQIATYLSLSDKETLNITVKTKQGGTDTCAGRYVYMHNLPSRFNEDLIKSCEAYIELRNKCKYLINSGFGPRILEEDHNHTTRVLTIETGSWYYTNQFMLEVIFREKMRHYECLTNDSSLSSVVFVPFYAGFDVRRFWGYNVKLRDELGEDLAQWLRERPEWRKMYGRDHFFVTGRVGRDFRRVTDQDSDWGNKLMRLPEFENITMLSIETNSRSNEFAVPYPTYFHPKSRTEVKRWQRQVTMMQRRYLFSFVGANRPKMEESIRGEIIRQCLASQGRCKFLD... | Function: Functions in xyloglucan synthesis by adding side chains to the xylosylated glucan backbone. Involved in the galactosylation of hemicellulose xyloglucan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 54837
Sequence Length: 468
Subcellular Location: Golgi apparatus membrane
EC: 2.4... |
Q9FLD7 | MKKLRSYYSNVRHHQNHHHHHHHHSNIVSSERKWIFFPLLIGSIFALFLLFLTTTLTSPTGGVRFLPFTRPVLLTGSGSSAFVESKIKPQQISSLPSPPRFAYLISGSAGDGKSLRRTLLALYHPNNRYVVHLDRESSREEREELHGYIKNSSLFRRFMNVHMIEKANLVTYRGPTMVANTLHAAAILLREGADWDWFINLSSSDYPLVTQDDLLHIFSHLPRDLNFIDHTSNIGWKASQRAKPVIIDPGLYLNKKSDVFWVTQRRSIPTAFKLFTGSAWMALSRPFVDYCIWGWDNLPRTVLMYYSNFLSSPEGYFHTV... | Function: Beta-glucuronosyltransferase involved in the biosynthesis of type II arabinogalactan (AG). Modifies both the beta-1,6-linked galactan and beta-1,3-linked galactan present in type II AG. Transfers glucuronate to beta-1,6-galactooligosaccharides with degrees of polymerization ranging from 3 to 11. Transfers glu... |
Q9LFQ0 | MKKLKSYYMQVRNQQQSLDRKWILPLAIGSICSLFLLLLTNLASSSGQTRLIPFSVYGFRSSVFVESKINPVSVSLTVSVSPPPPPRLAYLISGSSGDGQMLKRTLMALYHPNNQYVVHLDRESSPEERLDLSGFVANHTLFQRFQNVRMIVKANFVTYRGPTMVANTLHAAAILLREGGDWDWFINLSASDYPLVTQDDLLHTFSYLPRDLNFIDHTSNIGWKESHRAKPIIIDPGLYMSKKADVFWVSQKRSMPTAFKLFTGSAWMMLSRPFVDYFIWGWDNLPRIVLMYYANFLSSPEGYFHTVICNAREFTNTTVN... | Function: Beta-glucuronosyltransferase involved in the biosynthesis of type II arabinogalactan (AG). Modifies both the beta-1,6-linked galactan and beta-1,3-linked galactan present in type II AG.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 49583
Sequence Length: 434
Subcellular Location:... |
Q8S8P3 | MKRSHISSPRSYSRPAISIFGVFLLFLLVLTLSSRKPSDSSSGLAPNRNLATKSTIPRFAYLVTGTKGDGKRVKRLLKAIHHPRNYYLLHLDLEASDEERMELAKYVRSEKKKFENVMVMGLADLVTEKGPTMLASTLHGVAILLKKAKDWDWFINLSASDYPLMPQDDILHIFSYLPRYLNFIEHTSNIGWKENQRARPIIIDPGFYHLKKSGVFWAKERRSLPASFKLFMGSTSVALTRPFLEFCIWGWDNLPRTLLMYYTNFLLSSEGYFQTVVCNNKDYQNTTVNHDLHYTKWDPLQQRTLNVTVENFRDMVQSGA... | Function: Beta-glucuronosyltransferase involved in the biosynthesis of type II arabinogalactan (AG). Modifies both the beta-1,6-linked galactan and beta-1,3-linked galactan present in type II AG.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 44459
Sequence Length: 384
Subcellular Location:... |
Q84R16 | MRPKNYSQMEKPISITTGKFRTNNNNNHNNVWFVVPLFFILCFVLLCFDYSALFTDTDETAFSIPDVTQKSTSSEFTKDDNFSRFPDDPSPDSSCSGRYIYVHELPYRFNGDLLDNCFKITRGTEKDICPYIENYGFGPVIKNYENVLLKQSWFTTNQFMLEVIFHNKMINYRCLTNDSSLASAVFVPFYAGLDMSRYLWGFNITVRDSSSHELMDWLVVQKEWGRMSGRDHFLVSGRIAWDFRRQTDNESDWGSKLRFLPESRNMSMLSIESSSWKNDYAIPYPTCFHPRSVDEIVEWQELMRSRKREYLFTFAGAPRP... | Function: Functions in xyloglucan synthesis by adding side chains to the xylosylated glucan backbone. Involved in the galactosylation of hemicellulose xyloglucan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 60991
Sequence Length: 521
Subcellular Location: Golgi apparatus membrane
EC: 2.4... |
Q8S1X8 | MAMRLSSAAVALALLLAATALEDVARGQDTERIEGSAGDVLEDDPVGRLKVYVYELPTKYNKKMVAKDSRCLSHMFAAEIFMHRFLLSSAIRTLNPEEADWFYTPVYTTCDLTPWGHPLPFKSPRIMRSAIQFISSHWPYWNRTDGADHFFVVPHDFGACFHYQEEKAIERGILPLLRRATLVQTFGQKDHVCLKEGSITIPPYAPPQKMKTHLVPPETPRSIFVYFRGLFYDTANDPEGGYYARGARASVWENFKNNPLFDISTDHPPTYYEDMQRSIFCLCPLGWAPWSPRLVEAVVFGCIPVIIADDIVLPFADAIP... | Function: Involved in the synthesis of glucuronoxylan hemicellulose in secondary cell walls.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 46902
Sequence Length: 415
Subcellular Location: Golgi apparatus membrane
EC: 2.4.-.-
|
Q5XF04 | MKNNNSSSVSIENHPWKKKPTTLLLFLSLLSISLLLLRLSQDKIILITTTKTTATTGTDHQRSHKSSEDDTCLGRYIYIHNLPSRFNLEIIKDCKSITRPKDKISMCKYLDNSGFGPLIGGKSSDYSPSWYATNQFMLEVIFHEKMKSYECLTRNSSLASAIYVPYYAGLDFRRHLRRRNVAARDAAGKELVKWLKKQPQWKDMSGKNHFLVTGRISRDFRRNSGSRSAWGTNFMLLSESLNLTFLSIERSLTSHNEFAIPYPTYFHPTSTPEILQWQEKIRLTNRTVLFSFAGAQRPSRNQNGVVRTEVIKQCKSSSKT... | Function: Functions in xyloglucan synthesis by adding side chains to the xylosylated glucan backbone. Involved in the galactosylation of hemicellulose xyloglucan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 54788
Sequence Length: 479
Subcellular Location: Golgi apparatus membrane
EC: 2.4... |
Q8S1X7 | MRRWVLAIAILAAAVCFFLGAQAQEVRQGHQTERISGSAGDVLEDDPVGRLKVYVYDLPSKYNKKLLKKDPRCLNHMFAAEIFMHRFLLSSAVRTFNPEEADWFYTPVYTTCDLTPSGLPLPFKSPRMMRSAIELIATNWPYWNRSEGADHFFVTPHDFGACFHYQEEKAIGRGILPLLQRATLVQTFGQKNHVCLKDGSITIPPYAPPQKMQAHLIPPDTPRSIFVYFRGLFYDTSNDPEGGYYARGARASVWENFKNNPLFDISTDHPPTYYEDMQRSVFCLCPLGWAPWSPRLVEAVVFGCIPVIIADDIVLPFADA... | Function: Involved in the synthesis of glucuronoxylan hemicellulose in secondary cell walls.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 47064
Sequence Length: 417
Subcellular Location: Golgi apparatus membrane
EC: 2.4.-.-
|
Q9SH31 | MSLSKHLQKLVHKRESKKQPNKKMPVSVSKLRRPRTSKKTETGNPEKTLKDPRTCCNNLFSIFSARSFLYRVPLTILFLFLIYLWSTSTTVISGNVVHICISSRKLTDLYCLTAGSQPALRAPVNNFTAPASEDVVTSKEEKNVFVLGKDGDKGFAENETFEGGKDSDKSTVGENLTINKNETFTGETSGERVSILNQDAKPIHEKNLDSVLDQDSLPKNEIDQDFIIDWDPETGEERYRYFKAKTEDEETGLKSTEEYIQIQRTWLSMGNNRKKPGSCEGKGVYVYDLPSKFNKDLLRECSDMVPWADFCNYFKNDAFG... | Function: Xyloglucan-specific galacturonosyltransferase that forms the beta-D-galactosyluronic acid-(1->2)-alpha-D-xylosyl linkage. Required for root hair development probably by providing important acidic xyloglucans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 76562
Sequence Length: 66... |
Q9CA34 | MTFNKRQVKINHWPEKNDKEKQKYSKNRETVKLTLLTLLLLCSICFLFLTLNFPFTIEFTASIPRTCDHNFTVYVYDLPKEFNIGLLQNCRHLNIYTNMCPHVANNGLGQPLHRGRTSWFSTHQFIAEMIFHARVENHPCRTYEPDTADIFYVPFYGGLYASSVFREQNLTKRDELAVRLVNYISGQRWWKRSNGRDHFLAIGRTAWDFMRSSDTDFGANMLMQMPRVMNMSVLTVERQPWNGDNHFGIPYPSYFHPYTSAEMVTWQDKMKNVERPNLFSFVGGPRKGLEKAAIRDELIKQCAESSHCELLKCENGGSRC... | Function: Functions in xyloglucan synthesis by adding side chains to the xylosylated glucan backbone. Involved in the galactosylation of hemicellulose xyloglucan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 52905
Sequence Length: 455
Subcellular Location: Golgi apparatus membrane
EC: 2.4... |
F4K6F1 | MLPVSNPSSPEHLLKKSRTPDSTTSIDRKNSFNSLHSVGNRSSYIAASRSHCTWLILSLLSLQLILFLTLRSIPFPHRHIPENFPSPAAVVTTTVTTTVISAASSNPPLSSSSSDERCDSGRVFVYDMPKIFNEVILQQCDNLNPWSSRCDALSNDGFGQEATSLSNVIPKDLVQSWFWTDQFVTEIIFHNRILNHRCRTLDPESATAFYIPFYAGLAVGQYLWSNYAAADRDRHCKMMTQWVKNQPYWNRSNGWDHFITMGRITWDFRRSKDEDWGSNCIYIPGMRNITRLLIERNSWDHFDVGVPYPTGFHPRSDSDV... | Function: Functions in xyloglucan synthesis by adding side chains to the xylosylated glucan backbone. Involved in galactosylating hemicellulose xyloglucan (XyG) at the second position of the XXXG motif to form XLXG . Associates with other xyloglucan-synthesizing enzymes to form multiprotein complexes for xyloglucan syn... |
Q9SUW1 | MASKSTVTTLTIFFFFFFFFIEPKVQSQQISAVDSECTNRWIHIRTLPSRFNLDLLSTCNRYPITDDLCPYLANHGLGPKTHTRTRSWYRTDPLLLELIFHRRILEYPCLTPDPNLASAIYLPYYAGIDSLRYLYGPDLNSSADHGSDLLEFLTRDQPEIWSRRSGHDHFLVMARPAWDFSQPLTVDPPIWGTSFLERREFFNLTALTLESRYWPWQEQAVPYPTSFHPHSLPFLESWIRRVRRSRRTSLMLFAGGGGTSSSPNIRRSIRLECTSINATQSDNKICDFVDCSNGICEHDPIRFMRPMLQSSFCLQPPGDT... | Function: Functions in xyloglucan synthesis by adding side chains to the xylosylated glucan backbone. Involved in the galactosylation of hemicellulose xyloglucan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 50361
Sequence Length: 435
Subcellular Location: Golgi apparatus membrane
EC: 2.4... |
J4VV61 | MSPSRSEPLIDNLVDRSNLKIVALASPADGHTFPLLRIVEELVLRGYDVTFLASEDYRARTAAVGAYFVPVPPYDDIQRITTELSVIADPGERMNAAMIELFITPTAGRMATLYAALEDVKREKPLHKVVLLTESFFLGDHPLFLGAPLPKGFTRRPRAINIHACSYGLSSVDSAPFGLTIIPDGTAESREKYRKLHSDMLTGSLAESVALQKKVLTELGATNMDEVEGRNPLDVIATTADVTLQMCPPSLEYRRSDIHPKVRFIGALPPRAPPKTFSAPPFWNTVINGSKRVVVVSQGTVAVRYDQLLVPAMHALADRD... | Function: UDP-glucosyltransferase; part of the pathway that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection . Targets the N-OH hydroxyl residue of 15-hydrox... |
Q9FHD8 | MVSKRKSRTSKTIEDSCIHLCSVFFRFLYYTLPALFLFFFLLYLCLSFTTGISYNNFHMCIFSRKFNDPYCNTAGSKPGFQIISEENVTFAGEIAGDRVSKDHNKILNSVPVQEHKTKNKVDLNSLIELKAEEEYSKYIKPTSEDEGYALRAAIKYLYLQRSWLSPGDENLNKPRSCEGKGVYVYDLPSKFNSDLLVGCNDILPGVNLCSYFKNEGFGEAIKNLGKGWFATHMYSLEPILHSRVLKHPCRVYNETQAKLFFVPYYGGYDVLRWHYRNVSEDVKDRLGIEVLKWLNSKESWRRNAGKDHVFVLGKITWDFR... | Function: Functions in xyloglucan synthesis by adding side chains to the xylosylated glucan backbone. Involved in the galactosylation of hemicellulose xyloglucan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 65208
Sequence Length: 561
Subcellular Location: Golgi apparatus membrane
EC: 2.4... |
A5PK45 | MAAAPRACKGHGRPLPVLLLLLLLALPPLGGPPGAAAYFPEERWSPESPLQAPRVLIALLARNAAHALPATLGALERLRHPRERTALWVATDHNADNTSAVLREWLVAVKGLYHSVEWRPSEEPRSYPDEEGPKHWSDSRYEHVMKLRQAALKSARDMWADYILFVDADNLILNPDTLTLLIAENKTVVAPMLDSRAAYSNFWCGMTSQGYYKRTPAYIPIRKRERRGCFAVPMVHSTFLIDLRKAASRNLAFYPPHPDYTWSFDDIIVFAFSCKQAEVQMYVCNKEVYGFLPVPLRSHSTLQDEAESFMHVQLEVMVKH... | Function: Beta-galactosyltransferase that transfers beta-galactose to hydroxylysine residues of type I collagen. By acting on collagen glycosylation, facilitates the formation of collagen triple helix. Also involved in the biosynthesis of collagen type IV.
PTM: N-glycosylated.
Catalytic Activity: (5R)-5-hydroxy-L-lysyl... |
A5PMF6 | MHLLCFFFLLLWTGPARSYFPEERWSPESALLAPRVLVALVCRNSAHSLPHVLGAIDRLNYPKDRMAVWVATDHNSDNTTEILREWLVNVQNFYHYVEWRPQDEPSVYEGESGPKHWTNLRYEHVMKLRQAALETAREMWADYFMLVDCDNLLTNRDVLWKLMRENKTIVAPMLESRAAYSNFWCGMTSQGYYKRTPAYMPIRRQERKGCFAVPMVHSTLLLDLRKEASRQLAFFPPHPDYTWAFDDIIIFAFSARMAEVQMYICNRETYGYFPVPLRSQNSLQDEAESFLHSQLEVMVRNPPIEPSVYLSLMPKQTDKM... | Function: Beta-galactosyltransferase that transfers beta-galactose to hydroxylysine residues of type I collagen. By acting on collagen glycosylation, facilitates the formation of collagen triple helix.
Catalytic Activity: (5R)-5-hydroxy-L-lysyl-[collagen] + UDP-alpha-D-galactose = (5R)-5-O-(beta-D-galactosyl)-5-hydroxy... |
Q8NBJ5 | MAAAPRAGRRRGQPLLALLLLLLAPLPPGAPPGADAYFPEERWSPESPLQAPRVLIALLARNAAHALPTTLGALERLRHPRERTALWVATDHNMDNTSTVLREWLVAVKSLYHSVEWRPAEEPRSYPDEEGPKHWSDSRYEHVMKLRQAALKSARDMWADYILFVDADNLILNPDTLSLLIAENKTVVAPMLDSRAAYSNFWCGMTSQGYYKRTPAYIPIRKRDRRGCFAVPMVHSTFLIDLRKAASRNLAFYPPHPDYTWSFDDIIVFAFSCKQAEVQMYVCNKEEYGFLPVPLRAHSTLQDEAESFMHVQLEVMVKHP... | Function: Beta-galactosyltransferase that transfers beta-galactose to hydroxylysine residues of type I collagen . By acting on collagen glycosylation, facilitates the formation of collagen triple helix . Also involved in the biosynthesis of collagen type IV .
PTM: N-glycosylated.
Catalytic Activity: (5R)-5-hydroxy-L-ly... |
P22732 | MEQQDQSMKEGRLTLVLALATLIAAFGSSFQYGYNVAAVNSPALLMQQFYNETYYGRTGEFMEDFPLTLLWSVTVSMFPFGGFIGSLLVGPLVNKFGRKGALLFNNIFSIVPAILMGCSRVATSFELIIISRLLVGICAGVSSNVVPMYLGELAPKNLRGALGVVPQLFITVGILVAQIFGLRNLLANVDGWPILLGLTGVPAALQLLLLPFFPESPRYLLIQKKDEAAAKKALQTLRGWDSVDREVAEIRQEDEAEKAAGFISVLKLFRMRSLRWQLLSIIVLMGGQQLSGVNAIYYYADQIYLSAGVPEEHVQYVTAG... | Function: Functions as a fructose transporter that has only low activity with other monosaccharides . Can mediate the uptake of 2-deoxyglucose, but with low efficiency . Essential for fructose uptake in the small intestine (By similarity). Plays a role in the regulation of salt uptake and blood pressure in response to ... |
Q9WV38 | MEEKHQEETGELTLVLALATLIAAFGSSFQYGYNVAAVNSPSEFMQQFYNDTYYDRNEENIESFTLTLLWSLTVSMFPFGGFIGSLMVGTLVNKLGRKGALLFNNIFSILPAILMGCSQIAQSFELIIISRLLVGICAGISSNVVPMYLGELAPKNLRGALGVVPQLFITVGILVAQLFGLRSLLANEDGWPVLLGLTGVPAGLQLLLLPFFPESPRYLLIQKKDEAAAERALQTLRGWKDVHLEMEEIRKEDEAEKAAGFISVWKLFTMQSLRWQLISMIVLMAGQQLSGVNAIYYYADQIYLSAGVKSDDVQYVTAGT... | Function: Functions as a fructose transporter that has only low activity with other monosaccharides . Can mediate the uptake of deoxyglucose, but with low efficiency (By similarity). Essential for fructose uptake in the small intestine . Plays a role in the regulation of salt uptake and blood pressure in response to di... |
Q9UGQ3 | MQEPLLGAEGPDYDTFPEKPPPSPGDRARVGTLQNKRVFLATFAAVLGNFSFGYALVYTSPVIPALERSLDPDLHLTKSQASWFGSVFTLGAAAGGLSAMILNDLLGRKLSIMFSAVPSAAGYALMAGAHGLWMLLLGRTLTGFAGGLTAACIPVYVSEIAPPGVRGALGATPQLMAVFGSLSLYALGLLLPWRWLAVAGEAPVLIMILLLSFMPNSPRFLLSRGRDEEALRALAWLRGTDVDVHWEFEQIQDNVRRQSSRVSWAEARAPHVCRPITVALLMRLLQQLTGITPILVYLQSIFDSTAVLLPPKDDAAIVGA... | Function: Probable sugar transporter that acts as a regulator of glycolysis in macrophages (Probable). Does not transport glucose .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54539
Sequence Length: 507
Subcellular Location: Lysosome membrane
|
Q3UDF0 | MQEPLLRTEGLDYDTFPEVPATPGERERAGALKNRRVFLATFAAVLGNFSFGYALVYTSPVIPELKLSSDPALHLDKIQASWFGSVFTLGAAAGGLSAMLLNDLLGRKLSIMFSAVPSAIGYAIMAGARGLWMLLLGRMLTGFAGGLTAACIPVYVSEIAPPDVRGALGATPQLMAVFGSLSLYALGLLLPWRWLAVAGEGPVLIMILLLSFMPNSPRFLLSKSRDEEALQALTWLRADSEVHWEFEQIQDNVRRQSSRVSWAEAREPRVYRPVLIAVLMRFLQQLTGITPILVYLQTIFDNTSVVLPSQQDAAIVGAVR... | Function: Probable sugar transporter that acts as a regulator of glycolysis in macrophages . Does not transport glucose (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54433
Sequence Length: 497
Subcellular Location: Lysosome membrane
|
Q6PXP3 | MENKEAGTPPPIPSREGRLQPTLLLATLSAAFGSAFQYGYNLSVVNTPHKVFKSFYNETYFERHATFMDGKLMLLLWSCTVSMFPLGGLLGSLLVGLLVDSCGRKGTLLINNIFAIIPAILMGVSKVAKAFELIVFSRVVLGVCAGISYSALPMYLGELAPKNLRGMVGTMTEVFVIVGVFLAQIFSLQAILGNPAGWPVLLALTGVPALLQLLTLPFFPESPRYSLIQKGDEATARQALRRLRGHTDMEAELEDMRAEARAERAEGHLSVLHLCALRSLRWQLLSIIVLMAGQQLSGINAINYYADTIYTSAGVEAAHS... | Function: Probable sugar transporter . Even if its physiological substrate is subject to discussion, it is able to transport glucose and fructose . Does not transport galactose, 2-deoxy-d-glucose and xylose .
Catalytic Activity: D-glucose(out) = D-glucose(in)
Location Topology: Multi-pass membrane protein
Sequence Mass... |
P0C6A1 | MEDKEIGTPLPLPHSEARLQPTLVLTTLSAAFGSVFQYGYNIAVINTPHKVFKSFYNDTHFERHGTFMDESTLLLLWSCTVSMFPLGGLLGSLVVGLMVNKWGRKGTLLINNVFAITSAVLMGVSKVARAFELIILSRVLVGICAGIAYSTLPMYLGELAPQNLRGALGTMTEVFVIIGVLLAQIFSLQAILGNATGWPILLALTGVPAVIQLLSLPFFPESPRYTLIEKGDEETARQALRRLRGQNYNVEAEMEEMRTEERTEQAEGRLSVLNLFTFRPLRWQLISIVVLMAGQQLSGINAVNYYADVIYTSAGVDPTQ... | Function: Probable sugar transporter. Even if its physiological substrate is subject to discussion, it is able to transport glucose and fructose. Does not transport galactose, 2-deoxy-d-glucose and xylose.
Catalytic Activity: D-glucose(out) = D-glucose(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (D... |
P58354 | MTPEDQEETQPLLRPPGGSAPRGRRVFLAAFAAALGPLSFGFALGYSSPAIPSLRRAAPPAPHLDEDAASWFGAIVTLGAAAGGVLGGWLLDRAGRKLSLVLCALPFVAGFAVITAAQNLWMLLGGRLLTGLACGIASLVAPVYISEIAYPEVRGLLGSCVQLMVVTGILLAYLAGWVLEWRWLAVLGCVPPSFMLLLMCFMPETPRFLLSQHKHQEAMAAMQFLWGYAQGWEEPPLGAQHQDFHVAQLRRPGVYKPFIIGISLMAFQQLSGVNAVMFYAETIFEEAKFKDSSLASVVVGVIQVLFTATAALIMDRAGRR... | Function: Insulin-regulated facilitative hexose transporter that mediates the transport of glucose and fructose. Also able to mediate the transport of dehydroascorbate.
Catalytic Activity: D-glucose(out) = D-glucose(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51417
Sequence Length: 478
Subcel... |
Q9NY64 | MTPEDPEETQPLLGPPGGSAPRGRRVFLAAFAAALGPLSFGFALGYSSPAIPSLQRAAPPAPRLDDAAASWFGAVVTLGAAAGGVLGGWLVDRAGRKLSLLLCSVPFVAGFAVITAAQDVWMLLGGRLLTGLACGVASLVAPVYISEIAYPAVRGLLGSCVQLMVVVGILLAYLAGWVLEWRWLAVLGCVPPSLMLLLMCFMPETPRFLLTQHRRQEAMAALRFLWGSEQGWEDPPIGAEQSFHLALLRQPGIYKPFIIGVSLMAFQQLSGVNAVMFYAETIFEEAKFKDSSLASVVVGVIQVLFTAVAALIMDRAGRRL... | Function: Insulin-regulated facilitative hexose transporter that mediates the transport of glucose and fructose. Also able to mediate the transport of dehydroascorbate.
Catalytic Activity: D-glucose(out) = D-glucose(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50819
Sequence Length: 477
Subcel... |
Q9JIF3 | MSPEDPQETQPLLRPPEARTPRGRRVFLASFAAALGPLSFGFALGYSSPAIPSLRRTAPPALRLGDNAASWFGAVVTLGAAAGGILGGWLLDRAGRKLSLLLCTVPFVTGFAVITAARDVWMLLGGRLLTGLACGVASLVAPVYISEIAYPAVRGLLGSCVQLMVVTGILLAYVAGWVLEWRWLAVLGCVPPTLMLLLMCYMPETPRFLLTQHQYQEAMAALRFLWGSEEGWEEPPVGAEHQGFQLALLRRPGIYKPLIIGISLMVFQQLSGVNAIMFYANSIFEEAKFKDSSLASVTVGIIQVLFTAVAALIMDRAGRR... | Function: Insulin-regulated facilitative hexose transporter that mediates the transport of glucose and fructose . Also able to mediate the transport of dehydroascorbate .
Catalytic Activity: D-glucose(out) = D-glucose(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51508
Sequence Length: 477
Subc... |
Q9NRM0 | MARKQNRNSKELGLVPLTDDTSHAGPPGPGRALLECDHLRSGVPGGRRRKDWSCSLLVASLAGAFGSSFLYGYNLSVVNAPTPYIKAFYNESWERRHGRPIDPDTLTLLWSVTVSIFAIGGLVGTLIVKMIGKVLGRKHTLLANNGFAISAALLMACSLQAGAFEMLIVGRFIMGIDGGVALSVLPMYLSEISPKEIRGSLGQVTAIFICIGVFTGQLLGLPELLGKESTWPYLFGVIVVPAVVQLLSLPFLPDSPRYLLLEKHNEARAVKAFQTFLGKADVSQEVEEVLAESRVQRSIRLVSVLELLRAPYVRWQVVTV... | Function: High-capacity urate transporter, which may play a role in the urate reabsorption by proximal tubules . May have a residual high-affinity, low-capacity glucose and fructose transporter activity . Transports urate at rates 45- to 60-fold faster than glucose . Does not transport galactose . May mediate small upt... |
Q3T9X0 | MDSRELALASLMCDTGGPGELSVGHQQRRTKKWSFSLVVAALVGAFGSSFLYGYNLSVVNAPTPYIKAFYNGTWYRRHGQPIDPDTLTLLWSVTVSIFAIGGLVGTLMVKMIGKFLGRKSTLLVNNGFAISAALLMACSLRAGTFEMLIVGRFIMGVDGGIALSALPMYLNEISPKEIRGSLGQVTAIFICIGVFSGQLLGLPELLGRESTWPYLFGVIIVPALVQLASLPFLPESPRYLLFEKHDEAGAMKAFQTFLGKADVSQELEEALAESRVQRNLRLVSVLELLRAPFVRWQVITVIITMASYQLCGLNAIWFYT... | Function: High-capacity urate transporter, which may play a role in the urate reabsorption by proximal tubules. May have a residual high-affinity, low-capacity glucose and fructose transporter activity. Transports urate at rates 45- to 60-fold faster than glucose. Does not transport galactose. May mediate small uptake ... |
Q5RB09 | MARKQNRNSKELGLAPLADDTSHAGPPGPGRALLECDHLRSGLPDGRRRKDWSCSLLVASLAGAFGSSFLYGYNLSVVNAPTPYIKAFYNESWERRHGRPIDPDTLTLLWSVTVSIFAIGGLVGTLMVKMIGKVLGRKHTLLANNGFAISAALLMACSLQAGAFEMLIVGRFIMGIDGGIALSVLPMYLSEISPKEIRGSLGQVTAIFICIGVFTGQLLGLPELLGKESTWPYLFGVIVVPAVVQLLSLPFLPDSPRYLLLEKRNEARAVKAFQTFLGKADVSREVEEVAESRVQRSIRLVSVLELLRAPYVRWQVVTVI... | Function: High-capacity urate transporter, which may play a role in the urate reabsorption by proximal tubules. May have a residual high-affinity, low-capacity glucose and fructose transporter activity. Transports urate at rates 45- to 60-fold faster than glucose. Does not transport galactose. May mediate small uptake ... |
Q7NHC2 | MTSSPTAAARTEGEAAPTVPTQVESGTAQRPGLAREMVAILDFGSQYSELIARRIRETKVYSEVLSYQTPIAEIRRLAPKGIILSGGPNSVYEAYAPQCDPALWELGIPILGVCYGMQLMVQQLGGAVERAERAEYGKASLFINDPTDLFTNVEDGTTMWMSHADSVLRMPEGFELLAHTENTPCAAIAHHSRHLYGVQFHPEVVHSRGGMALLRNFVYHICGCEPEWTTAAFIEEAIREVRARVGDKRVLLALSGGVDSSTLAFLLHRAIGDNLTCMFIDQGFMRKNEPERLVKLFKEQFHIPVAYVDAAERFIVRLEG... | 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): 61532
Sequence Length: 551
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
|
P44335 | MTNIHYHKILILDFGSQYTQLIARRVREIGVYCELWAWDVTEQQIREFAPTGIILSGSPESTTEENSPRAPEYVFNAGVPVLGICYGMQTMAMQLGGLTETSDHREFGYASVSLENSTALFANLNDNLTASEPKLDVWMSHGDKVTRLPENFKVTGTTLTCPIAAMSDESRRFYGVQFHPEVTHTKKGLELLTNFVVNICGCETKWTAENIIEDAVARIKEQVGDDEVILGLSGGVDSSVVALLLHRAIGKNLHCVFVDNGLLRLHEGDQVMEMFGDKFGLNITRVDAESRFLGELAGVSDPEAKRKIIGKVFVDVFDDE... | 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): 58186
Sequence Length: 523
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
|
O25165 | MILVLDFGSQYTQLIARRLRERGIYTEIVPFFESIENIQKKAPKGLILSGGPASVYAKDAYKPSGKIFDLNVPILGICYGMQYLVDFFGGVVVGANEQEFGKAVLEITQNSVIFEGVKIKSLVWMSHMDKVIELPKGFTTLAKSPNSPHCAIENGKIFGLQFHPEVVQSEEGGKILENFALLVCGCEKTWGMQHFAQREIARLKEKIANAKVLCAVSGGVDSTVVATLLHRAIKDNLIAVFVDHGLLRKNEKERVQAMFKDLKIPLNTIDAKEVFLSKLKGVSEPELKRKIIGETFIEVFEKEAKKHHLKGKIEFLAQGT... | 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): 56824
Sequence Length: 508
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
|
Q2S0V0 | MHDKIVVLDFGSQYTQLIARRVRETGVYSEIRPCTVEADAIDALNPSGVILSGGPCSVYDEAGPALDPALLELERPDGTPVPLLGICYGLQAMAHQFGGEVARADRREFGRAQLQVPPDGQEKSLLFEGVPSGSTVWMSHSDHLTDLPDGYEVIARTDNAPVAAVRDTDGPYYGVQFHPEVVHTDYGRQILENFAHAICGCSGDWTPASFVEEQTETIRDRVGDRHVILGLSGGVDSSVAAALLQRALGDQLHCIFVNNGLLRKGEWNQVQDTFRGHFEMDLRTTDATDRFLERLDGVTDPEEKRTIVGNTFIEVFEEQT... | 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): 58103
Sequence Length: 526
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
|
Q9P772 | MSSTEVPGEVSTSVSSYFDTILILDFGSQYSHLIARRLREIHVYAELLPCTQKIEALPFKPIGVILSGGPYSVYDDIAPHVDPAVFELGVPVLGICYGMQEIAWLNGRCVEPGIEREYGPATVSMEPEIKTEVFKSFFNSMPKEFEVWMSHGDRLSALPNGYETIGRTKNSPFAVIAHVTKPIIGLQFHPEVTHTPLGLQLIKNFAIEICHAKPNWSMENFVDKEILRIRKMIGPSDHVIGAVSGGVDSTVASKVLKEAIGDRFHAIMVDNGLLRLNEAEIVRETLNKHLGIQLTVVDASEEFIGKLKGVTDPEKKRKII... | Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 60044
Sequence Length: 539
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.5.2
|
Q83SM9 | MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFSMASALASFDILTAVHKHFSVEEWQAFINNSSADVLKHVMVSTGTSDADFEKTKQILDLNPALNFVCIDVANGYSEHFVQFVAKAREAWPTKTICAGNVVTGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGMIVSDGGCTTPGDVAKAFGGGADFVMLGGMLAGHEESGGRIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGQVENTARDILGGLRSACTYVG... | Function: Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.
Catalytic Activity: IMP + NADP(+) + NH4(+) = GMP + 2 H(+) + NADP... |
B0CS18 | MEEFPCDVIRYEAYVYGVCEFRLPFFLPSRNFSIIAHIDHGKSTLADRLLELTGTIQKKQAGKNEQVLDKLKVERERGITGKSNHSMIDKFKGKDYLLNLIDTPGHVDFAWEVSRSLAACQGALLLVDASQGVQAQSISVFHNAKERGLKIIPILNKIDLPAAQPERIAAQMQATFGIDPSDILHISAKTGQGTQEVLEAIISRIPPPSGRIHAPLKAFLFDSFYDRYRGVISLINVQEGVLRKGDKISSCHTRKKYEITELGILHPEEVPTQSLNPGQVGYIACNMKQSSEAHIGDTLHRAGEPVEPMEGFQETKAMVF... | Function: Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate... |
Q4Q3F0 | MKLCGVRGSGVSLMRSSNFPCFRAAHNGGAPTATRHQSLCGRCLDSHMGAGKRWCFRPLLAEPRRYGSASSASTTDAATAPVHGEDLYVSHYAIPEDARRLVGTPQLLPRNPAEEVAFKKNLIRSFPQACIRNVSVVAHVDHGKTTLSDAMLRFSNLLPADGATGTFTDRLKVEKERGITIKAQTCSVLLTVRETGTQYLVNLIDTPGHVDFQYEVSRSLCASEGAALLVDVRQGVEAQTMAQFYAALEQNLTILPVLTKMDNVMSDAEVEKTLLQLEDSTGLLSREVILTSAKSKQGIEQLFQQIIDKVPPPRGREGFS... | Function: Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate... |
A4QV78 | MSCCKGLTPQCVRVRLPRRPALSHPARLYSSSSSSNSHSSPSRPRLLSRPQPHNAILHLPRPNLGSGRYDRIPQARSSHHSSAPMTDLEQRIAAIPIERYRNFCVIAHVDHGKSTLSDRLLELTGTISASDENKQILDKLDVERERGITVKAQTCTMLYRYRGEDYLLHLVDTPGHVDFRAEVTRSYASCGGALLLVDASQGVQAQTVANFYLAFAEGLTLVPVVNKIDLPTADPERALKQLRDTFELDVNEDGTGAVLVSAKAGTNVEKVLPAVIEQIPHPTGDPNAPLRLLLVDSWYDTFRGVVLLVRIFNGTVRPGD... | Function: Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate... |
Q8C3X4 | MWALVGRALAPWAAGARHAAASEPRAACRLFSAAELKEKPDMSRFPVEDIRNFSIIAHVDHGKSTLADRLLELTGTIDKTKKNKQVLDKLQVERERGITVKAQTASLFYSFGGKQYLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVGKQIEKVFDIPSEECIKISAKLGTNVDSVLQAVIERIPPPKVHRENPLKALVFDSTFDQYRGVIANIALFDGVVSKGDKIVSAHTKKAYEVNEVGILNPNEQPTHKLYAGQVGFLIAGMKDVTEAQIGDTLY... | Function: Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate... |
D2VRR7 | MLSSSLSNDNENNRRNYVSKSNKNGLVFECSELKEELKRLSIMNRNNIYSNVWMRNIGFSKQQQVRNYSVLPTNAKKIKEHNKSALDLSGFTPEYIRNFCIIAHIDHGKSTLADYLLKETNTITAELLKDNAQFLDRLQVERERGITVKAQSCAMFYEYNGKKYLLNLIDTPGHVDFSYEVSRSMGACDGALLLVDSGQGVQAQTLANYFLALEENLEIIPIMTKIDQQTAQPELVEEDMTGILGVEKDEIIKVSAKTGLNCQKIIPAVIEKIPAPEPPKVSEGETPGALKSLIFDSWYDEYFGVVSLVYIAQGSVEVGD... | Function: Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate... |
Q7S0P6 | MRGALCRPDVLMRPCLRPCARLPRLPPSRRLPFSITTSCQQLPRTSPGRAGFSSLASLESRQNDRTRCFSALRSLSSSQLLPTTAPVLARHNSTTATSQMPLERKAIEIEKRIAAIPLERYRNFCIVAHIDHGKSTLSDRLLEHTGTITAGDGNKQVLDKLDVERERGITVKAQTCTMIYKHRDGLDYLLHLVDTPGHVDFRAEVTRSYSSCSGALLLVDASQGVQAQTVANFYLAFAQGLSLVPVVNKIDMASADVPRVLEQLETVFELDTSTAVKVSAKTGQGVGEILPAVISNVPAPVGDAKKPLRMLLVDSWYDTF... | Function: Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate... |
Q5VQ69 | MAGAAALRRSARRVVLPGAYALSRALQHPERLLSSQASPDRGGVLGSELGLYPPERVRNFSIIAHVDHGKSTLADRLLELTGTIKKGHGQPQYLDKLQVERERGITVKAQTATMFYRHANNQLPASDQPDAPSYLLNLIDTPGHVDFSYEVSRSLAACQGALLVVDAAQGVQAQTIANFYLAFESNLSIIPVINKIDQPTADPDNVKAQLKRLFDIDPSEALLTSAKTGQGLSQVLPAVIERIPSPPGKCDSPVRMLLLDSYYDEYKGVICHVAVVDGALHKGDKIASAATGRTYEVLDVGIMHPELTPTGVLYTGQVGY... | Function: Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate... |
A4S3R2 | MALRRVLVDRIVRSCAARAFASTSASYASARDALKEERPPTADELAAIPRERTRNFSIIAHVDHGKSTLADRLLELTGAIKRDGSNKQVLDTLPVERRRGITVKAQAVSILHREPSDGQAYLLNLIDTPGHADFSFEVSRSLSACDGAVMLVDATQGVEAQTIATFYLALDRNLAIVPAANKVDMTSADVERVAKQMERAFGVEREDVLEVSGKTGHNAEKVLSAVVKHVPHPSGDPNGPLRVLLLDCHYDDYRGAVNIVQVADGVIRKGDKVSSCASGQHFEVLELGMMTPERTKTDAMYAGQVGYMITNVRDVRSSKV... | Function: Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate... |
P0C2S3 | MVSFKAGINLGGWISQYQVFSKEHFDTFITEKDIETIAEAGFDHVRLPFDYPIIESDDNVGEYKEDGLSYIDRCLEWCKKYNLGLVLDMHHAPGYRFQDFKTSTLFEDPNQQKRFVDIWRFLAKRYINEREHIAFELLNEVVEPDSTRWNKLMLEYIKAIREIDSTMWLYIGGNNYNSPDELKNLADIDDDYIVYNFHFYNPFFFTHQKAHWSESAMAYNRTVKYPGQYEGIEEFVKNNPKYSFMMELNNLKLNKELLRKDLKPAIEFREKKKCKLYCGEFGVIAIADLESRIKWHEDYISLLEEYDIGGAVWNYKKMDF... | Function: This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 40954
Sequence Length: 343
Pathway: Glycan me... |
P23658 | MKKVLVNQVGFLCNAPKKAVLNFQANEFSVVDGNGKKAFDGKVEHFGTDEISGEDTYVADFSALTEEGKYKIVADGQESVLFSISNDAYDKLMKDICKCFYYLRCGDALSKEFAGEYYHKPCHMTKATVYGEDVEPVDVTGGWHDAGDYGRYSTAGAVAVAHLLYGVRFFKGLLDVHYDIPKVAGDKGNLPEILAEVKVELDFLMKMQRENGSVWHKVTTFNHAPFLMPEDDREELFLFSVSSLATADIAAVFALAYTVYKEYDAEYADKLMQKSLLAYKWLLDNPDELLFFNPDGSNTGQYDEAEDISNRFWAACALYE... | Function: Glycoside hydrolase that rapidly hydrolyzes short-chain cellodextrins to yield either cellobiose or cellobiose and glucose as end products; cellobiose is not hydrolyzed further. Also shows limited activity against endoglucanase specific substrates (carboxymethylcellulose (CMC), lichenan, laminarin and xylan).... |
P37699 | MIKGSSLKRFKSLVMAAIFSVSIISTAIASSAADQIPFPYDAKYPNGAYSCLADSQSIGNNLVRSEWEQWKSAHITSNGARGYKRVQRDASTNYDTVSEGLGYGLLLSVYFGEQQLFDDLYRYVKVFLNSNGLMSWRIDSSGNIMGKDSIGAATDADEDIAVSLVFAHKKWGTSGGFNYQTEAKNYINNIYNKMVEPGTYVIKAGDTWGGSNVTNPSYFAPAWYRIFADFTGNSGWINVANKCYEIADKARNSNTGLVPDWCTANGTPASGQGFDFYYDAIRYQWRAAIDYSWYGTAKAKTHCDAISNFFKNIGYANIKD... | 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-glucosi... |
P0C2S4 | SLTGVFPSGLIETKVSAAKITENYQFDSRIRLNSIGFIPNHSKKATIAANCSTFYVVKEDGTIVYTGTATSMFDNDTKETVYIADFSSVNEEGTYYLAVPGVGKSVNFKIAMNVYEDAFKTAMLGMYLLRCGTSVSATYNGIHYSHGPCHTNDAYLDYINGQHTKKDSTKGWHDAGDYNKYVVNAGITVGSMFLAWEHFKDQLEPVALEIPEKNNSIPDFLDELKYEIDWILTMQYPDGSGRVAHKVSTRNFGGFIMPENEHDERFFVPWSSAATADFVAMTAMAARIFRPYDPQYAEKCINAAKVSYEFLKNNPANVFA... | Function: This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 69707
Sequence Length: 625
EC: 3.2.1.4
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P50400 | MHSASRTRARTRVRTAVSGLLAATVLAAPLTLVAAPAQAATGDDWLHVEGNTIVDSTGKEAILSGVNWFGFNASERVFHGLWSGNITQITQQMAQRGINVVRVPVSTQLLLEWKAGTFLKPNVNTYANPELEGKNSLQIFEYWLTLCQKYGIKVFLDVHSAEADNSGHVYNMWWKGDITTEDVYEGWEWAATRWKDDDTIVGADIKNEPHGTQGSTERAKWDGTTDKDNFKHFAETASKKILAINPNWLVFVEGVEIYPKPGVPWTSTGLTDYYGTWWGGNLRGVRDHPIDLGAHQDQLVYSPHDYGPLVFDQKWFQKDF... | Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 78937
Sequence Length: 747
Pathway: Glycan metabolism; cellulose degradation.
EC: 3.2.1.4
|
P28623 | MIKHLLSRGKLLLFVSVMATSSIIAGGNAYGSTAFTGVRDVPAQQIVNEMKVGWNLGNTMDAIGGETNWGNPMTTHAMINKIKEAGFNTLRLPVTWDGHMGAAPEYTIDQTWMKRVEEIANYAFDNDMYVIINLHHENEWLKPFYANEAQVKAQLTKVWTQIANNFKKYGDHLIFETMNEPRPVGASNEWTGGSYENREVVNRYNLTAVNAIRATGGNNATRYIMVPTLAASAMSTTINDLVIPNNDSKVIVSLHMYSPYFFAMDINGTSSWGSDYDKSSLDSEFDAVYNKFVKNGRAVVIGEMGSINKNNTAARVTHAE... | Function: Has endoglucanase activity on carboxymethyl-cellulose (CMC), cellobiosidase activity on p-nitrophenyl-cellobioside (p-NPC), and partial hydrolytic activity on crystalline cellulose (Avicel).
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucan... |
P25472 | MKKILALIISCSIIMSFLPMSVYGAINSQDMVKKMGIGMNLGNTFDAPTEGSWSKAAQEYYFDDFKQAGFKHVRIPIRWDQHTLANSPYTVDSNFLNRIETVIDWSLSRGFVTVINSHHDTWLMDNYSQNIGRFEKIWEQIAQRFKGKSENLVFEILNEPHGNITDSQINDMNKRILNIIRKTNPTRNVIIGAGYWNSYNSLSQLEIPNDPNLIATFHYYDPYSFTHQWQGTWGTKNDMDAIAMVFNHVKKWSDKNNIPVYLGEYGVMGHSDRTSAVKWFDFVSDQAISHGFSCGAWDNGVFGSVDNDMAFYNRDTRQFD... | 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-glucosi... |
Q05622 | MRKRITSMITVISLTLCGTIGTYPHNANASAKEAFEDISKRSECTKVFDNDNGTYTAYSNTAPIHYLNNDEWKEIDNTLIEDSDDYYRNKDNSFNIYIPKEYSLGKNIKNPVIMNYDTFSLSTSITDIKMPDRPEEETFSEGVYADINNEVYTTIDNSAIAEGMKAALKKSASMATYHSIVEDIDLDIAVHNASVSESIIINKLESLPETITYSISVEDAIIKKTEDNRLQLIKDNEAVLILSPFTISDSSENVNVMQVEYDLTESEEGYEVTLYPAETVNRMSSPVMPLSLGSEYSYDRPFSTVYNSQASLHPSIIIIT | Function: Hydrolyzes both carboxymethylcellulose and xylan. Probably has a role in hydrolyzing oligosaccharides derived from cellulose, which are transported across the cell wall.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da)... |
P26224 | MKKILAFLLTVALVAVVAIPQAVVSFAADFNYGEALQKAIMFYEFQRSGKLPENKRNNWRGDSALNDGADNGLDLTGGWYDAGDHVKFNLPMAYAVTMLAWSVYESRDAYVQSGQLPYILDNIKWATDYFIKCHPSPNVYYYQVGDGALDHSWWGPAEVMQMPRPSFKVDLTNPGSTVVAETAAAMAASSIVFKPTDPEYAATLLRHAKELFTFADTTRSDAGYRAAEGYYSSHSGFYDELTWASIWLYLATGDQSYLDKAESYEPHWERERGTTLISYSWAHCWDNKLYGSLLLLAKITGKSYYKQCIENHLDYWTVGF... | Function: This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 82089
Sequence Length: 739
EC: 3.2.1.4
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Q05332 | MKKAKAIFSLVVALMVLAIFCFAQNTGSTATTAAAAVDSNNDDWLHCKGNKIYDMYGNEVWLTGANWFGFNCSENCFHGAWYDVKTILTSIADRGINLLRIPISTELLYSWMIGKPNPVSSVTASNNPPYHVVNPDFYDPETDDVKNSMEIFDIIMGYCKELGIKVMIDIHSPDANNSGHNYELWYGKETSTCGVVTTKMWIDTLVWLADKYKNDDTIIAFDLKNEPHGKRGYTAEVPKLLAKWDNSTDENNWKYAAETCAKAILEVNPKVLIVIEGVEQYPKTEKGYTYDTPDIWGATGDASPWYSAWWGGNLRGVKDY... | Function: This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 63199
Sequence Length: 566
EC: 3.2.1.4
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P37700 | MLKTKRKLTKAIGVALSISILSSLVSFIPQTNTYAAGTYNYGEALQKSIMFYEFQRSGDLPADKRDNWRDDSGMKDGSDVGVDLTGGWYDAGDHVKFNLPMSYTSAMLAWSLYEDKDAYDKSGQTKYIMDGIKWANDYFIKCNPTPGVYYYQVGDGGKDHSWWGPAEVMQMERPSFKVDASKPGSAVCASTAASLASAAVVFKSSDPTYAEKCISHAKNLFDMADKAKSDAGYTAASGYYSSSSFYDDLSWAAVWLYLATNDSTYLDKAESYVPNWGKEQQTDIIAYKWGQCWDDVHYGAELLLAKLTNKQLYKDSIEMN... | 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-glucosi... |
P16218 | MKKRLLVSFLVLSIIVGLLSFQSLGNYNSGLKIGAWVGTQPSESAIKSFQELQGRKLDIVHQFINWSTDFSWVRPYADAVYNNGSILMITWEPWEYNTVDIKNGKADAYITRMAQDMKAYGKEIWLRPLHEANGDWYPWAIGYSSRVNTNETYIAAFRHIVDIFRANGATNVKWVFNVNCDNVGNGTSYLGHYPGDNYVDYTSIDGYNWGTTQSWGSQWQSFDQVFSRAYQALASINKPIIIAEFASAEIGGNKARWITEAYNSIRTSYNKVIAAVWFHENKETDWRINSSPEALAAYREAIGAGSSNPTPTPTWTSTPP... | Function: This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 102416
Sequence Length: 900
EC: 3.2.1.4
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Q9HI16 | MTNESRKRKVRGSQIRSSRGDKKQGRSQSRDDKEIERLERQNDARGQESSTHVDEGFVPEEQSFIETESVNRVESRMERWLDVGRPVHLIGPTGCGKTSLAMHVARERDRPVVWINGDAELTTSDLVGEYAEKERISEHDQFIHNVVKSKDIIRDRWVDNPLTLAVQEGATLVYNEFSRTKPVANNVLLSVFEEGVLELPGKRGKSRYVDVHPEFRTILTSNSVEYAGVHEPQDALLDRLIGIYMDFYDLDTEIEIVRAHVDKSADTNVEDIVRVLRELRERLDITVGTRAAIMANEGATTVDTVDQAVLTDICTDVLAS... | Function: An ATPase that functions in gas vesicle formation (By similarity). A minor component of the gas vesicle, also found in soluble extracts . Probably enhances gas vesicle formation (Probable). Gas vesicles are hollow, gas filled proteinaceous nanostructures found in several microbial planktonic microorganisms. T... |
Q9RH29 | MTSEAASKDPISVLSGFGAGTATSASKNGGRTTPSALTPRPRSGFVETEQVRDLTRRGLGFLNAGYPLHFRGPAGTGKTTLALHVAAQLGRPVIIITGDNELGTADLVGSQRGYHYRKVVDQFIHNVTKLEETANQHWTDHRLTTACREGFTLVYDEFTRSRPETHNVLLGVFEERMLFLPAQAREECYIKVHPEFRAIFTSNPQEYAGVHASQDALADRLATIDVDYPDRAMELAVASARTGMAEASAARIIDLVRAFRASGDYQQTPTMRASLMIARVAALEGLDVSVDDPRFVQLCSDALESRIFSGQRAEAVAREQ... | Function: An ATPase that functions in gas vesicle formation (By similarity). A minor component of the gas vesicle, also found in soluble extracts (By similarity). Gas vesicles (GV) are hollow, gas filled proteinaceous nanostructures. During planktonic growth they allow positioning of the organism at a favorable depth f... |
P55150 | MTTTKVNHKRAVLRLRPGQFVVTPAIERVAIRALRYLKSGFPVHLRGPAGTGKTTLAMHLANCLDRPVMLLFGDDQFKSSDLIGSESGYTHKKVLDNYIHSVVKLEDEFKQNWVDSRLTLACREGFTLVYDEFNRSRPEVNNVLLSALEEKILSLPPSSNQPEYLSVNPQFRVIFTSNPEEYAGVHSTQDALMDRLVTISMPEPDEITQTEILIQKTNIDRESANFIVRLVKSFRLATGAEKTSGLRSCLMIAKVCADNNIPVTTESLDFPDIAIDILFNRSHLSMSESTNIFLELLDKFSAEELEILNNRVTGDNDFLI... | Function: An ATPase that functions in gas vesicle formation (By similarity). A minor component of the gas vesicle, also found in soluble extracts (By similarity). Gas vesicles (GV) are hollow, gas filled proteinaceous nanostructures. During planktonic growth they allow positioning of the organism at a favorable depth f... |
A4GWX9 | MGNRIGGRRKAGVEERYTRPQGLYEHRDIDQKKLRKLILEAKLAPCYMGADDAAAAADLEECPICFLYYPSLNRSKCCSKGICTECFLQMKPTHTAQPTQCPFCKTPSYAVEYRGVKTKEERSIEQFEEQKVIEAQMRMRQQALQDEEDKMKRKQNRCSSSRTITPTKEVEYRDICSTSFSVPSYRCAEQETECCSSEPSCSAQTSMRPFHSRHNRDDNIDMNIEDMMVMEAIWRSIQEQGSIGNPVCGNFMPVTEPSPRERQPFVPAASLEIPHGGGFSCAVAAMAEHQPPSMDFSYMAGSSAFPVFDMFRRPCNIAGG... | Function: E3 ubiquitin-protein ligase involved in the regulation of grain size. May limit grain width and weight by restricting cell proliferation of the spikelet hull. Possesses E3 ubiquitin-protein ligase activity in vitro.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor pro... |
Q67UR2 | MVETTTMMKVLVRVREFDVEKDLPAVEELERRCQVGLSGDMAAVHDHADDGDGAAAKEKKKTKTKTKKKKASMSLCVEQIGDPLARVRHAPEHVMLVAEYGEEEEKKKVVGVIKACVKTVSRGGKQEKPFVKVANLLGLRVSPSHRRLGIGTALVRRAEEWCVARGAEHATMATTESNAASLALFTGRFGYAPFRRPEFIGHPVHAHRLPVARGHRVFQLPPEVAAAAYARLLPPQDAEFLPADMPALLAHKLTLGTFVAVAADGASFAVLSVWDSTRSLSLRVSGAPALLRASLAALRALDRGAPWLHLPSIPDIFRPF... | Function: Possesses intrinsic histone acetyltransferase activity and acts as positive regulator of grain weight, hull size, yield, and plant biomass . Regulates postitively grain weight and yield by enlarging spikelet hulls via increasing cell number and accelerating grain filling . In vitro, catalyzes the acetylation ... |
O33926 | MPEILINKPVEDELVESYLLYSMSVIVGRAIPDVRDGLKPVQRRILYGMYELGLKHNSPTKKSARIVGEVMGKYHPHGDAPVYDALVRMAQPFTMRYPLIEGQGNFGSIDRDPPAAMRYTEARLTRLAEEMLEDIEKNTVNMIDNFDGTLKEPEVLPSKVPNLIINGASGIAVGMATNIPPHNLSETVDALIYLIDHPEATVEELMQFIKGPDFPTGAVVVNASELKKVYEEGRGRIIVRGKVHVEDGKRVKRIVITEIPYGVSKAGLIEQIAKIAKDDESLPIRNIRDESDKRGMRIVIEIPKDANEEVIINNLYKRTA... | 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 ... |
Q5SIL4 | MAQVLPVEITEELKQSFINYAMSVIVDRALPDVRDGLKPVQRRILFGAYQEGVLPGRKHVKSAKIVGEVMGKYHPHGDAAIYDALVRMAQPWNLRYPLIDGQGNFGSIDGDPPAAQRYTEARLSPIGAEMLLDIDKDTVDFRPNYDGSLKEPEVLPAAIPNLLVNGASGIAVGMATSLPPHNLSEVVDALVAMIENPAITLEEVMRHLPGPDFPTGGKLSKKGIKEAYATGRGSLKVRAKVRVEEKGQRPVLVVTEIPYQVNKASLIAQIAALVKAKKIEDIVGLRDESDRQGLRIAIELKRGANPQVVLNQLYKHTALQ... | 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 . It probably also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including ... |
O83051 | MEEISTPEGGVLVPISIETEVKRAYIDYSMSVIVSRALPDVRDGLKPVHRRILYAMEEKGLRFSGPTRKCAKIVGDVLGSFHPHGDASVYDALVRLGQDFSLRYPVIHPQGNFGTIGGDPPAAYRYTEAKMARIAESMVEDIKKETVSFVPNFDDSDVEPTVLPGRFPFLLANGSSGIAVGMTTNMPPHNLREIAAAISAYIENPNLSIQELCDCINGPDFPTGGIIFGKNGIRQSYETGRGKIVVRARFTIETDSKGRDTIIFTEVPYQVNTTMLVMRIGELARAKVIEGIANVNDETSDRTGLRIVVELKKGTPAQVV... | 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 ... |
Q94BZ7 | MALLQRASYLRLYYLRLMGSRPRLFSSSLSPALHRHSSTLSSPPFSSPSPSFRLKFQLTSVLSQRLIQRNAISSRFLSTEASQETTTSKGYSSEQIQVLEGLDPVRKRPGMYIGSTGSRGLHHLVYEILDNAIDEAQAGYASKVDVVLHADGSVSVVDNGRGIPTDLHPATKKSSLETVLTVLHAGGKFGGTSSGYSVSGGLHGVGLSVVNALSEALEVSVWRDGMEHKQNYSRGKPITTLTCRVLPLESKGTKGTSIRFWPDKEVFTTAIEFDHNTIAGRIRELAFLNPKVTISLKKEDDDPEKTQYSEYSFAGGLTEY... | Cofactor: Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner.
Catalytic A... |
Q9SS38 | MALVQRQHSYLLRYFRLMASRPRPRLFSHSLYPSLHRHSSALSSSTPRIKFQLANVFSQRLVQRNAVSPKSFMSSTMESLQESSTSKDYSSEHIQVLEGLDPVRKRPGMYIGSTGSRGLHHLVYEILDNAIDEAQAGFASKIDVVLHSDDSVSISDNGRGIPTDLHPATGKSSLETVLTVLHAGGKFGGKSSGYSVSGGLHGVGLSVVNALSEALEVIVRRDGMEFQQKYSRGKPVTTLTCHVLPPESRGTQGTCIRFWPDKEVFTTAIQFDHNTIAGRIRELAFLNPKVTISLKKEDDDPERDVYSEYFYAGGLTEYVS... | Cofactor: Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner.
Catalytic A... |
P50074 | MTTYDTRTATDTRGSEQPGHVGTASYDANAITVLDGLDAVRKRPGMYIGSTGERGLHHLVQELVDNSVDEALAGVADRIDVTVLADGGVRVVDNGRGIPVGMHPVEKRPAVEVVLTVLHAGGKFGGGGYGVSGGLHGVGLSVVNALSTRLSAEIWTDGHRWTQDYRDGAPTAPLARHEATSRTGTSLTFWADGDIFETTEYSFETLARRHQEMAFLNGGLTLTLTDERSSARATAAVDEADSDPTAKTVSYRYDGGITDFVVHLNARKGEPAHPSVITIAAEDTERLLSAEIALQWNGQYTDSVYSYANAIHTHEGGTHE... | Cofactor: Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modu... |
Q43947 | DNSYKVSGGLHGVSVSVVNALSSKLHLMISRAGQVHEQEYQHGDPQYPLRVIGETDKSGTTVRFWPSELTFTQTIFNVEILARRLRELSFLNAGVRIVLRDERINLEHVYDYEGGLSEFVKYINEGKTHLNEIFHFTADTDSGIGVEVALQWNESYQENVRCFTNNIPQKDGGSHLAGFRAALTRGLNQYLENENILKKEKVNVTGDDAREGLTAIISVKVPDPKFSSQTKEKLVSSEVKPAVEQAMNKEFSAYLLENPQAAKSIAGKIIDAARARDAARKAREMTRRKSALDIAGLPGKLADCQEKDPALSELYLVEGD... | 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 ... |
P02253 | MSETAPAAPAAAPPAEKTPVKKKAAKKPAGARRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAATGEAKPKAKKAGAAKPKKAAGAAKKTKKATGAATPKKTAKKTPKKAKKPAAAAVTKKVAKSPKKAKAAKPKKAAKSAAKAVKPKAAKPKVAKPKKAAPKKK | Function: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin rem... |
P15864 | MSEAAPAAPAAAPPAEKAPAKKKAAKKPAGVRRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGILVQTKGTGASGSFKLNKKAASGEAKPQAKKAGAAKAKKPAGAAKKPKKATGAATPKKAAKKTPKKAKKPAAAAVTKKVAKSPKKAKVTKPKKVKSASKAVKPKAAKPKVAKAKKVAAKKK | Function: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin rem... |
P35064 | MSTTGKGGKAKGKTASSKQVSRSARAGLQFPVGRISRFLKHGRYSERVGTGAPVYLAAVLEYLAAEVLELAGNAAKDNKKTRIVPRHILLAIRNDEELNKLMANTTIADGGVLPNINPMLLPSKSKKTESRGQASQDL | Function: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. 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... |
Q6GM86 | MSGRGKAVSKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAHRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKSRIIPRHLQLAVRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKSSGGVSTSGKKSSQQSQEY | Function: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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... |
A0A0D2UG83 | MAKSKKIVAATSGSRSRSSRAGLAFPVGRVHRLLRKGHFADRIGSGSAVYLAAVLEYLTAEILELAGNAARDNRKTRINPRHIQLAVRNDEELSKLFTGVVIPSGGTLPHIWPALIPNEAKDSSTASASFNAPAKSATVKALAAAKSAGKKPAAVSSSSAAASSSSSASSSSSVAPKKPVRGFTILSKKTLHLGQTLYVVNGDLTEVRCDAVVHPTNGTMSFAGQVGGAIRAAAGAGVDAEVNSYMSEHSQLQVTKAAITSGHNLPSKWIVHVHSPNYSNAATATDALTQTIRNALTLADTKSIKTIAFPSIGSGNNHFP... | Function: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. 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 regula... |
O93327 | MSSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAIITPPPAKKAKSPSQKKTVSKKTGGKKGARKSKKKQGEVSKSASADSTTEGTPADGFTVLSTKSLFLGQKLQVVQADIATIDSDAVVHPTNSDFYTGGEVGSTLEKKGGKEFVEAVIELRKKNGPLDIAGAVVSAGHGLPAKFVIHCNSPGWGSDKCEELLEKTVKNCLALADEKKLKSIAFPSIGSGRNGFPK... | Function: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. 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 regula... |
O75367 | MSSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAIITPPPAKKAKSPSQKKPVSKKAGGKKGARKSKKKQGEVSKAASADSTTEGTPADGFTVLSTKSLFLGQKLQVVQADIASIDSDAVVHPTNTDFYIGGEVGNTLEKKGGKEFVEAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPK... | Function: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription . 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 regu... |
Q02874 | MSSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAIITPPPAKKAKSPSQKKPVAKKTGGKKGARKSKKQGEVSKAASADSTTEGAPTDGFTVLSTKSLFLGQKLQVVQADIASIDSDAVVHPTNADFYIGGEVGSTLEKKGGKEFVEAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALADDRKLKSIAFPSIGSGRNGFPKQ... | Function: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. 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 regul... |
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