ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q02088 | MDKLREKINAARAETDEAVARAEAAEAKLKEVELQLSLKEQEYESLSRKSEAAESQLEELEEETKQLRLKADNEDIQKTEAEQLSRKVELLEEELETNDKLLRETTEKMRQTDVKAEHFERRVQSLERERDDMEQKLEEMTDKYTKVKAELDEVHQALEDL | Function: Forms part of the F-actin contractile ring during cytokinesis.
Sequence Mass (Da): 18964
Sequence Length: 161
Domain: The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity.
Subcellular Location: Cytoplasm
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Q2V0V2 | MDAIKKKMLAMKMEKEVATDKAEQTEQSLRDLEAAKNTIEEDLSTLQKKYSNLENDFDNAKENLTVANTNLEASEKRVNECESEIQGLNRRIQLLEEDLERSEERLTSAQSKLEDASKAADESERGRKVLENRSQGDEERIDLLEKQLEEAKWIAEDADRKFDEAARKLAITEVDLERAEARLEAAEAKIVELEEELKVVGNNMKSLEISEQEASQREDSYEETIRDLTHRLKEAENRAAEAERTVSKLQKEVDRLEDELLAEKERYKSISDELDQTFAELAGY | Function: Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.
PTM: The N-terminus is blocked.
Sequence Mass (Da): 32673
Sequence Length: 284
Domain: The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The s... |
P53099 | MNRDNMDTTKRKEDHTKHTTDVIEFYEEGTAASSLNIATEKANSSPSILRRIINRAAWLSKKVDAMGVESTGIQRISPYERGTSKKQFLHVAGLWLSATGGLSSMSSFLLGPLLFGLSFRESVASSLISVTIGCLIAAYCSIMGPQSGCRQMVTARYLFGWWFVKLVALASIIGVMGWSVVNSVVGGEMLAAISNDKVPLWVGIVIVTVCSFLVAIFGIKQVIKVETYLSVPVLTAFLLLYISSSDKYSFVNAYVSKGNLDSSTRKGNWMSFFSLCYSITATWGSITADYYILFPEDTPYIQIFCLTFFGTFLPTCFVGI... | Function: Thiamine-regulated, high affinity import carrier of pyridoxine, pyridoxal and pyridoxamine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64546
Sequence Length: 579
Subcellular Location: Membrane
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A0A385AJN0 | MDINKQKTKWDISIFKNENFTLPVIKSPFNTYYNKYIDSVINDIEEWHRECCFLGREKLKGYIESKPYLFSAYYYCHLNEKVLPFIIKFVDMFSIYDDEYLEKTNCSEDVINQFLDKNYKDKNIYGVEWFKIVEGLKKYGNKQSVNKFLKEFEFFIKNVHSIHLKENANYTNINFEEYTNTRSIDFGFDLVVSAAIIDCEEPSKEIRESSLFLTLNTKSSIICVLVNDIYSFVKESKQPDTMNYVKIMANKKKSIQKALNHTNKIINNTLKEIISIENQIKMQYKENNLYQYIERLNSVISATIYLHQNHKRYSVHNKNY... | Function: Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into the sesquiterpenes (E)-beta-farnesene and (E,E)-alpha-farnesene . TPS11 also converts geranylgeranyl diphosphate (GGPP) into the diterpene (S)-nephthenol .
Catalytic Activity: (2E,6E)-farnesyl diphosphate = (E)-beta-farnesene + dipho... |
B9RHP7 | MSMIGTKSFFISSSPKVPVGISWGPSSYRTNSSLSVRSPTLTCSISTISQPTRKEPATTKPEIMEELHEGTRKELLTSSSPIATMKLIDSIQRLGVGYYFEEEINTLLDRFLDLETTEDLLATALRFRLLRDNCFPAHSDVFGKFMNKDGKFKESLRKDVWGLLSLYEASYLGTKDEVELVEAMEFTKTCLEEQSIPLMAHKLSRHVSQALDLPRHLRMPRLEARNYIHEYSLESNNSPPLLELAKLEFNAVQSLHQKELIEIVRWWKQLGLVDKLGFARDRPLECYLWTVGIFPEPYNSTCRIELTKTIAILLVIDDIF... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Probable sesquiterpene synthase.
Sequence Mass (Da): 65426
Sequence Length: 572
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
EC: 4.2.3.-
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A0A385AJM6 | MYSLFKNIKFPNHWIPPIEFENKEQVKEKYFKRYCELGFYNENSIKDKVMNSSSVLLSYYFFSVAKNDQEFNLGYDIMAAFFSTDDFFDGKPENYNNQTAKERIFNIIKNEGNCSFSDFNQNEKFLIKYIIDSKEYSKNNSNKQILYYKILQGWIDYVESLGPYNLLENYSYNETIHLFIRRFDIAYLPACDLAIMMVIENLNISIMYHPKYCLMHLDLAKSLSLINDLHSFEKEFLDGQIKNNYLYKIIEKGNDNKSFDVGSFDIGVKKIFNDINKLNQSAENYEKELLEEFQLKLNEKQFDEFKKVITASLLINGGNL... | Function: Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into the sesquiterpenes beta-elemene, valencene; alpha-selinene, 7-epi-alpha-selinene and a yet unidentified sesquiterpene.
Catalytic Activity: (2E,6E)-farnesyl diphosphate = (1S,2S,4R)-beta-elemene + diphosphate
Sequence Mass (Da): 42307... |
B9T825 | MAINLFKVSNFYTMRSYVSPHVPVPNVNLQSVSCSAKAELPHLRPVIKRRSANYPPTIWTYNFVQSLNNHNADVLYKEKARKLEEEVRRLINNESQEMLTTLELIDGIQRLGLAYLFEKDIKGALDRFVSMGGCHVLPRKSLHAIALSFRLLRQHGYEVYQDDFKDFMDQKGELLKCFKKDVQGILSFYEASFCNLEGEDLLEKAKTETKVYLNDLQRNSKSDTVESISHALELPLCRRMVMLEARWYIEAYNKREDSNYTLLELAKLNFNMAQSILQRDLKDMSRWWNNLGLANKLSFSRDRLMECFFWTIGMAFEPQF... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Probable sesquiterpene synthase.
Sequence Mass (Da): 67929
Sequence Length: 587
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
EC: 4.2.3.-
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D5KXD2 | MASSSANKCRPLANFHPTVWGYHFLSYTHEITNQEKVEVDEYKETIRKMLVEAPEGSEQKLVLIDAMQRLGVAYHFDNEIETSIQNIFDASSKQNDNDNNLYVVSLRFRLVRQQGHYMSSDVFKQFINQDGKFKETLTNDVQGLLSLYEASHLRVRDEEILEEALTFTTTHLESTVSNLSNNNSLKAEVTEAFSQPIRMTLPRVGARKYISIYENNDAHNHLLLKFAKLDFNMLQKLHQRELSDLTRWWKDLDFANKYPYARDRLVECYFWILGVYFEPKYSRARKMMTKVIQMASFFDDTFDAYATFDELEPFNNAIQR... | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Sesquiterpene synthase involved in the biosynthesis of volatile compounds . Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (1E,4E,8E)-alpha-humulene and (-)-(E)-beta-caryophyllene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into beta... |
B9RXW4 | MALSSISIFIHCLVDPLPRKQTSKTLPSNHIDFKSAFNVANWSINQTLVSPLSAQCIHLTDEDVRIKERRTRAFKHILRKEGEGSHEVLAMIDAIQRLGIDHHFQDEIDEILQRQYTIPSYYNDNDLHGLALRFRLLRQGGYNVSAGVFDKFKDKEGNFDQKLSDDIRGLMELYEASQLSIGAEDHILDEAGDYSHQLLSSWMTRLDDSQARIIKNTLDHPHHKNLARFRATNFNRYFHMANIEGWMNELQELAKIDFQMVQSQNQQEIFQVAGWWKDLGISKELKFVRNQPLKWYIWSMATLSDPSLSQQRIDLTKPIS... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Probable sesquiterpene synthase.
Sequence Mass (Da): 65858
Sequence Length: 572
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
EC: 4.2.3.-
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A0A0M5L832 | MFMSSSSSSHARRPQLSSFSYLHPPLPFPGLSFFNTRDKRVNFDSTRIICIAKSKPARTTPEYSDVLQTGLPLIVEDDIQEQEEPLEVSLENQIRQGVDIVKSMLGSMEDGETSISAYDTAWVALVENIHHPGSPQFPSSLQWIANNQLPDGSWGDPDVFLAHDRLINTLACVIALKKWNIHPHKCKRGLSFVKENISKLEKENEEHMLIGFEIAFPSLLEMAKKLGIEIPDDSPALQDIYTKRDLKLTRIPKDIMHNVPTTLLYSLEGLPSLDWEKLVKLQCTDGSFLFSPSSTACALMHTKDGNCFSYINNLVHKFNG... | Function: Diterpene synthase that catalyzes the formation of (-)-kolavenyl diphosphate from geranylgeranyl diphosphate (GGPP).
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate = (-)-kolavenyl diphosphate
Sequence Mass (Da): 93935
Sequence Length: 815
Domain: The Asp-Xaa-Asp-Asp (DXDD) motif is important for t... |
P0DO46 | MSHLDVFRKFTDDQGNYNKELVNDTHGLLSLYEAAQFRVHDEEILDEAINFTTTHLKLLLPKLSNSLSMQVSYALKYPINKTIARVATRKYISFYQEEESSCDQVLINFAKLDFSILQKMHKRELCDITRWWKELDLANELAFARDRVVELYFWCLGVYFEPQYKVARNILTKVLCFVSITDDIYDTYGTLHELTLLTNAIERWNLDATENLTSYMKLFYTGLLHFYNEVEKELEKENKSFRVNFAISEMKKLVRAYFQEAKWYHGNTVPKMEEEYMKNGIQSSANPTLATASWLGMGDEATKEAFEWISTEPPILVASS... | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Sesquiterpene synthase involved in the biosynthesis of volatile compounds . No activity detected with geranyl diphosphate (GPP) and farnesyl diphosphate (FPP) as substrates .
Sequence Mass (Da): 50184
Sequence Length: 430
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu... |
G8H5N3 | MELCTQTVPADHEVEITRRVGSHHPTVWGDHFLAYANLSGASEEEEKQHEDLKEEVRKMLVMAPSNALEKLELINTIQCLGVAYHFEHEIESYMCTHYEEYWIGDLHAIALCFRLLRQQGYRVSCDAYKKFTDDQGNFKIELINDVHGMLSLYEAAQFRVHGEEILDEALNFTTTQLKLILPKLSNSPLAQQVANALKFPIKDGIVRVEARKYISFYQQNQNHNQLLLNFAKLDFNILQMLHKKELCDITRWWKELEIVKTLPYVRDRLAEVYFWSLGVYFEPQYSTARKILTKNISMISLIDDTYDIYGTLDELTLFTE... | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Sesquiterpene synthase involved in the biosynthesis of volatile compounds . No activity detected with geranyl diphosphate (GPP) and farnesyl diphosphate (FPP) as substrates .
Sequence Mass (Da): 64521
Sequence Length: 553
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu... |
G5CV52 | MELCTQTVAADHEVIITRRSGSHHPTLWGDHFLAYADLRGANEGEEKQNEDLKEEVRKMLVMAPSKSLEKLELINTIQCLGLGYHFQSEIDESLSYMYTHYEEYSIGDLHAIALCFRLLRQQGYYVSCDAFKKFTNDQGNFKEELVKDVEGMLSLYEAAQFRVHGEQILDEALNFTIAQLKQILPKLSNSQLAQQITNALKYPIKDGIVRVETRKYISFYQQNQNHNEVLLNFAKLDFNILQTLHKKELSDMTRWWKKMELVNTLPYARDRLVECYFWCLGTYFEPQYSVARKMLTKISFYISIIDDTYDIYGKLDELTL... | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Sesquiterpene synthase involved in the biosynthesis of volatile compounds . Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into gamma-gurjunene, (E)-beta-farnesene and (+)-valencene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into (E)-alp... |
Q29VN3 | MAPKTVWGYFFIDYIPEPLQVSDKQRVVELKGEVARLFEDCNCKDVVERMNLVDVVQRLGIDHHFKEQIDTALKNIQGAEFNSSDLHEVSLRFRLLRQHGLWVPADQFDKFRRQEDGSFSSDIADDPKGLLGLYNAASLLIHGEEVLEEALLFARRHLESIRRGGGLHDSPYLSEQVGRSLKIPLPRTLKRLEAVSYIPEYSSADDTTYIHPEILELARLDFNLLQHVHQNELRTVTQWWKGLCDVIGPDYGRDRIVECYFWAFSMYYEEEHARARMILARLIMLASLLDDTFDDRATLQECRELNKAIERWDESDDISL... | Function: Converts farnesyl diphosphate to the bicyclic olefins alpha-copaene, (E)-beta-caryophyllene, and to the macrocyclic sesquiterpene germacrene D . Mediates also the biosynthesis of minor sesquiterpene hydrocarbons including delta-cadinene . Involved in indirect defense by producing volatile signals attracting n... |
J7LH11 | MNSTSRRSANYKPTIWNNEYLQSLNSIYGEKRFLEQAEKLKDEVRMLLEKTSDPLDHIELVDVLQRLAISYHFTEYIDRNLKNIYDILIDGRRWNHADNLHATTLSFRLLRQHGYQVSPEVFRNFMDETGNFKKNLCDDIKGLLSLYEASYLLTEGETIMDSAQAFATHHLKQKLEENMNKNLGDEIAHALELPLHWRVPKLDVRWSIDAYERRQDMNPLLLELAKLDFNIAQSMYQDELKELSRWYSKTHLPEKLAFARDRLVESYLWGLGLASEPHHKYCRMMVAQSTTLISIIDDIYDVYGTLDELQLFTHAVDRWD... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Sesquiterpene synthase involved in the biosynthesis of (+)-epi-alpha-bisabolol, a precursor of the natural sweetner hernandulcin.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O = (+)-epi-alpha-bisabolol + diphosphate
Sequence Mass (Da): 63782
Sequence Length:... |
A0A1L6Z3A0 | MSRFTSATHGLNLSIKMPISVSQVPSIRSNTSKYELQKLRSTGRSVLQTRRQLAIINMTKRSEADDNDGVERRKGVFHPNLWDDGFIQSLSTVYHEQASYRERAERLIGEVKAVFDSISMGDGDQFISPSAYDTAWVARVPAIDGSSRPQFPQAIDWILLNQQQDGSWGSQSHLSLTHRLTDTLACVIALASWKIESVQIDEGLDFITRGVEKLQSESVPAEFEIIFAELLNQAKSLQLSLPYEHSCLQSLWRKQEPILANGLMDSVAKRSLSSLEEMQDHRMNTDSDGTMHVESFLSSPAVAARVLMRTGNPICLAYLN... | Function: Converts geranylgeranyl diphosphate to an new 5,7-fused bicyclic diterpene, named pseudolaratriene . Catalyzes the first committed step in pseudolaric acid B (PAB) biosynthesis . PAB exhibits antiproliferative activity by inhibiting microtubule polymerization, and has demonstrated antitumor properties against... |
B9S1N2 | MAAEAKNDEQQDIARRLAKFPSTIWGCSFASFSLKDSEIESYTQQVEELKGKVKDMLMQSTKEITQNIEVINLLCRLGVSYHFESEIEQQLNLIFASLPSFLNDNGHLDLYTVALLFRVLRQHGRKVPCDVFNKYKDDNGEFKKDITSDVKGLLSLYEASVVSVHGEEILDEALVFTKQHLETLAAQVSPHFEQHIRNALLCPVHYGMERLQARLYISFYEEDESRNEILLKFAKLDFNRLQLLYREELAIVSRWWKDLDLTERLSYARDRIVEVYVWALGCVGSQPQFASSRLLVAKFTQTAMTVDDTYDAYGTIGELR... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Probable sesquiterpene synthase.
Sequence Mass (Da): 63820
Sequence Length: 551
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
EC: 4.2.3.-
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Q54YE2 | MYSLHDFKFPEDWIEPPANDKCIYTCYKEVVDFKLFEENKKTLEYYYGTISSTIYLYPLCNYEQLLVASRYLTVCFVVDDFLESKLTNPDDSRELIKKLEHIFMDGNFYDSNNISNIEKYVLYFRETTKQFVGEKIEFFNQFLKFIIDWINSINPFNRADNLNNYDSYNFFKRTNSGTYVSLSVAMLLYPNSKIDPKIWINPRFDRFATNGGYQMATMNDCASYAKEIRNNNHLTNPLHFLQNQVGSFDNVYKVILKFNDEIMNQICEDERILLLECPIEQRDDLKLLTRSMKLILGGNYLWSLQCSRYVDINSPFIEQR... | Function: Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into the sesquiterpene beta-barbatene as a major product as well as (E)-beta-farnesene as a minor product . Is also able to convert geranyl diphosphate (GPP) into a mixture of monoterpenes including (Z)-beta-ocimene, linalool, beta-myrcen... |
F0ZK52 | MSLSFKNIVFPEEWQVPPNDYIFIDDCYEEALQFNLFERGDEKSYTWMYHTISCCAYFWCKCSRSEMKLIGHLMLWTFLLDDILDSDKVNDAEAIEMIKRTEFIFIEGKLPENPTDLEKYTCYLRNEGLKIAGDREDMFNMFLTNSIQWILSIIPLNKSMEHKLPPHLQLHGYLRKLNVGVELCQGFTYLIFANNKVNPAIFNSPRYKKMLECTSMVVSHVNDMASYCKEVKNGGGFINSLLILQKRADPLSIEHSYQVIAEQTNAFIRDFIYQEKMLLESISDEQQNEVKVFLDHMKYLMKGNYLWSGTTARYASKSSP... | Function: Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into the sesquiterpenes beta-elemene, germacrene D and a yet unidentified sesquiterpene.
Catalytic Activity: (2E,6E)-farnesyl diphosphate = (1S,2S,4R)-beta-elemene + diphosphate
Sequence Mass (Da): 39801
Sequence Length: 341
Domain: Conta... |
B9RPM3 | MEIVFSSSLSSTLTVTKILRSPRHATTGNMQDYSRFPLFFTIASRSNASQAKHRRSANYHPTIWDPKAIECLRTPYTYDGVHGARLQKLKDEVRSLLTTFTKEPCGQLKLIDSMQRLGVSYHFREEIEEILNLVELDSDSDLYTTALHFRLLRQHGFTISKEVFEKFRNEDGKFKDSLKEDILGLLSLYDASYLGMHGEHILEEAKDFSTEQLKSLLGRSQGDIVTYQVKQALDVPLHWRMQRIENRNYINIYQKEDTNNLALLELAKLDYNLVQSVYQIELKELARWWIALGFREKLHFSRDRLMENYLWSMGMIFEPH... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Probable sesquiterpene synthase.
Sequence Mass (Da): 67734
Sequence Length: 584
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
EC: 4.2.3.-
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J9QS23 | MWELVETVRSMLNSLHDGEISVSAYDTAWVARVPALDGSNTPQFPMCLNWIMNNQLEDGSWGDRDLFLTYDRICSALACAIALKTWNTGDKIVHKALEFIRKTMPKMELEDSTHMPIGFEIVFPAMIEEAMALELDIDYTAPVLQTIYAERKKKLERIPMNVVQNYPTTLLHSLEGLHKTIDWDKVIKLQSPDGSLLFSPASTACALMHTGNEKCLQYLNNLVKRFNCAVPNVYPVDLFEHLWIVDRLQRLGISRYFTQEIKSALDYVYRYWTDKGIAWARGSPVQDADDTSMAFRLLRSHGYDISPDAFKTFQEGDSFV... | Function: Monofunctional diterpene synthase converting geranylgeranyl diphosphate to copalyl diphosphate.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate = (+)-copalyl diphosphate
Sequence Mass (Da): 84560
Sequence Length: 739
Domain: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic activity, ... |
Q9ZUH4 | MATLLQIGSGVIYSNALRKTLRRPQSSTCIIVTETTPCNKSPTVQRRSANYQPSRWDHHHLLSVENKFAKDKRVRERDLLKEKVRKMLNDEQKTYLDQLEFIDDLQKLGVSYHFEAEIDNILTSSYKKDRTNIQESDLHATALEFRLFRQHGFNVSEDVFDVFMENCGKFDRDDIYGLISLYEASYLSTKLDKNLQIFIRPFATQQLRDFVDTHSNEDFGSCDMVEIVVQALDMPYYWQMRRLSTRWYIDVYGKRQNYKNLVVVEFAKIDFNIVQAIHQEELKNVSSWWMETGLGKQLYFARDRIVENYFWTIGQIQEPQ... | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Involved in monoterpene (C10) biosynthesis. The major product is beta-myrcene (56%) followed by (E)-beta-ocimene (20%) and minor amounts (less than 5%) of the cyclic monoterpene (-)-limonene, (+)-limonene, 2-carene and tricyclene.
Catalytic Activity: (2E)-g... |
Q54K57 | MNENDNNLENETGFSGRLIVVSNRLPVSIKKESNGKWSCKMSSGGLVAALSGLKSNFIWVGWIGAEIEEDDRKEIKELLWKDYSCIPVFLSEKVANEHYNGFSNGVLWPLFHYLPGDLDYDDRIWNSYVEANEQFSSVVAEILKPNDLVWVHDYHMMLLPEILKQKKPDARIGFFLHIPFPSSEIFRVLPCRKEILLGILNCCLIGFHTYDYARHFLKSCTRIVGLETAPNGVYFKDRFVQVGVFPVGIDPDKFFESLKTTQVQNRIKELKESFEGTKVLIGIDRLDYIKGIPQKLQAIERLFQKYPEWKGKLVLIQVAV... | Function: Synthesizes trehalose 6-phosphate, the precursor for the production of trehalose, the main carbohydrate storage reserve of the dormant spore. Trehalose accumulates in both prestalk and prespore cells and then is rapidly metabolized during terminal differentiation of stalk cells, while being stored in spores, ... |
B1B1U4 | MEKQSLTFDGDEEAKIDRKSSKYHPSIWGDYFIQNSSLTHAKESTQRMIKRVEELKVQVKSMFKDTSDLLQLMNLINSIQMLGLDYHFENEIDEALRLIYEVDDKSYGLYETSLRFQLLRQHGYHVSADIFNKFKDDNGSFISSLNGDAKGLLSLYNVSYLGTHGETILDEAKSFTKPQLVSLMSELEQSLAAQVSLFLELPLCRRNKILLARKYILIYQEDAMRNNVILELAKLNFNLLQSLYQEELKKISIWWNDLAFAKSLSFTRDRVVEGYYWVLTIYFEPQHSRARVICSKVFAFLSIMDDIYDNYGILEECTLL... | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Involved in the biosynthesis of beta-eudesmol, a sesquiterpene with antifungal activity and responsible for resistance of plants to ant attack. Produces mainly beta-eudesmol, but also smaller amounts of 10-epi-gamma-eudesmol, alpha-eudesmol and aristolene.
... |
O48935 | MATNGVVISCLREVRPPMTKHAPSMWTDTFSNFSLDDKEQQKCSETIEALKQEARGMLMAATTPLQQMTLIDTLERLGLSFHFETEIEYKIELINAAEDDGFDLFATALRFRLLRQHQRHVSCDVFDKFIDKDGKFEESLSNNVEGLLSLYEAAHVGFREERILQEAVNFTRHHLEGAELDQSPLLIREKVKRALEHPLHRDFPIVYARLFISIYEKDDSRDELLLKLSKVNFKFMQNLYKEELSQLSRWWNTWNLKSKLPYARDRVVEAYVWGVGYHYEPQYSYVRMGLAKGVLICGIMDDTYDNYATLNEAQLFTQVL... | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Involved in the production of (E)-beta-farnesene, an aphid alarm pheromone. Can use both farnesyl diphosphate and geranyl diphosphate as substrate, but not geranylgeranyl diphosphate. Produces mainly (E)-beta-farnesene, but also smaller amounts of (Z)-beta-... |
Q54NU9 | MTIIQRSTSLNNIINEKLGKIIVASNTLPITVTKFNETPLFGSPLSASRESITSSFGMSEPSRDRESKIQIQINGHPFPTQSALETLKAKDEIEDWLWIGWSHCEVNEDEEPMLNQAIKEFSPHFEHVFLNPRQFENYYKGYCKNGLWLLLHYQMNFIRMQSEWWEEYVGVNQMFAEKIASVWRPSDIIWIHDYHLMLVPQMLRQLLPPEASIGFFFHAPFPSYELFRILPNRKELLKGILSSNLIGFQSFEYVRHFKSSCARLLDLEVHPKGLEIFEDGSTHFTKLQVYPIGVDYNDFAKNLNLPEVSSRVESLRKIFK... | Function: Synthesizes trehalose 6-phosphate, the precursor for the production of trehalose, the main carbohydrate storage reserve of the dormant spore. Trehalose accumulates in both prestalk and prespore cells and then is rapidly metabolized during terminal differentiation of stalk cells, while being stored in spores, ... |
O81086 | MAGVSAVSKVSSLVCDLSSTSGLIRRTANPHPNVWGYDLVHSLKSPYIDSSYRERAEVLVSEIKAMLNPAITGDGESMITPSAYDTAWVARVPAIDGSARPQFPQTVDWILKNQLKDGSWGIQSHFLLSDRLLATLSCVLVLLKWNVGDLQVEQGIEFIKSNLELVKDETDQDSLVTDFEIIFPSLLREAQSLRLGLPYDLPYIHLLQTKRQERLAKLSREEIYAVPSPLLYSLEGIQDIVEWERIMEVQSQDGSFLSSPASTACVFMHTGDAKCLEFLNSVMIKFGNFVPCLYPVDLLERLLIVDNIVRLGIYRHFEKE... | Cofactor: Binds 3 divalent metal cations per subunit . Can use either Mg(2+) or Mn(2+) .
Function: Converts farnesyl diphosphate to alpha-bisabolene . Involved in defensive oleoresin formation in conifers in response to insect attack or other injury . Involved in sesquiterpene (C15) olefins biosynthesis .
Catalytic Act... |
Q7M707 | MEHLLKRTFDITENILLIILFIELIIGLIGNGFTALVHCMDWVKRKKMSLVNKILTALATSRIFLLWFMLVGFPISSLYPYLVTTRLMIQFTSTLWTIANHISVWFATCLSVFYFLKIANFSNSPFLYLKRRVEKVVSVTLLVSLVLLFLNILLLNLEINMCINEYHQINISYIFISYYHLSCQIQVLGSHIIFLSVPVVLSLSTFLLLIFSLWTLHKRMQQHVQGGRDARTTAHFKALQAVIAFLLLYSIFILSLLLQFWIHGLRKKPPFIAFCQVVDTAFPSFHSYVLILRDRKLRHASLSVLSWLKCRPNYVK | Function: Putative taste receptor which may play a role in the perception of bitterness.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36750
Sequence Length: 316
Subcellular Location: Membrane
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O00220 | MAPPPARVHLGAFLAVTPNPGSAASGTEAAAATPSKVWGSSAGRIEPRGGGRGALPTSMGQHGPSARARAGRAPGPRPAREASPRLRVHKTFKFVVVGVLLQVVPSSAATIKLHDQSIGTQQWEHSPLGELCPPGSHRSEHPGACNRCTEGVGYTNASNNLFACLPCTACKSDEEERSPCTTTRNTACQCKPGTFRNDNSAEMCRKCSRGCPRGMVKVKDCTPWSDIECVHKESGNGHNIWVILVVTLVVPLLLVAVLIVCCCIGSGCGGDPKCMDRVCFWRLGLLRGPGAEDNAHNEILSNADSLSTFVSEQQMESQEP... | Function: Receptor for the cytotoxic ligand TNFSF10/TRAIL . The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) m... |
O14763 | MEQRGQNAPAASGARKRHGPGPREARGARPGPRVPKTLVLVVAAVLLLVSAESALITQQDLAPQQRAAPQQKRSSPSEGLCPPGHHISEDGRDCISCKYGQDYSTHWNDLLFCLRCTRCDSGEVELSPCTTTRNTVCQCEEGTFREEDSPEMCRKCRTGCPRGMVKVGDCTPWSDIECVHKESGTKHSGEVPAVEETVTSSPGTPASPCSLSGIIIGVTVAAVVLIVAVFVCKSLLWKKVLPYLKGICSGGGGDPERVDRSSQRPGAEDNVLNEIVSILQPTQVPEQEMEVQEPAEPTGVNMLSPGESEHLLEPAEAERS... | Function: Receptor for the cytotoxic ligand TNFSF10/TRAIL . The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) m... |
Q9QZM4 | MEPPGPSTPTASAAARADHYTPGLRPLPKRRLLYSFALLLAVLQAVFVPVTANPAHNRPAGLQRPEESPSRGPCLAGQYLSEGNCKPCREGIDYTSHSNHSLDSCILCTVCKEDKVVETRCNITTNTVCRCKPGTFEDKDSPEICQSCSNCTDGEEELTSCTPRENRKCVSKTAWASWHKLGLWIGLLVPVVLLIGALLVWKTGAWRQWLLCIKRGCERDPESANSVHSSLLDRQTSSTTNDSNHNTEPGKTQKTGKKLLVPVNGNDSADDLKFIFEYCSDIVPFDSWNRLMRQLGLTDNQIQMVKAETLVTREALYQML... | Function: Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) me... |
O14798 | MARIPKTLKFVVVIVAVLLPVLAYSATTARQEEVPQQTVAPQQQRHSFKGEECPAGSHRSEHTGACNPCTEGVDYTNASNNEPSCFPCTVCKSDQKHKSSCTMTRDTVCQCKEGTFRNENSPEMCRKCSRCPSGEVQVSNCTSWDDIQCVEEFGANATVETPAAEETMNTSPGTPAPAAEETMNTSPGTPAPAAEETMTTSPGTPAPAAEETMTTSPGTPAPAAEETMITSPGTPASSHYLSCTIVGIIVLIVLLIVFV | Function: Receptor for the cytotoxic ligand TRAIL. Lacks a cytoplasmic death domain and hence is not capable of inducing apoptosis. May protect cells against TRAIL mediated apoptosis by competing with TRAIL-R1 and R2 for binding to the ligand.
PTM: N-glycosylated and O-glycosylated.
Location Topology: Lipid-anchor
Sequ... |
Q9UBN6 | MGLWGQSVPTASSARAGRYPGARTASGTRPWLLDPKILKFVVFIVAVLLPVRVDSATIPRQDEVPQQTVAPQQQRRSLKEEECPAGSHRSEYTGACNPCTEGVDYTIASNNLPSCLLCTVCKSGQTNKSSCTTTRDTVCQCEKGSFQDKNSPEMCRTCRTGCPRGMVKVSNCTPRSDIKCKNESAASSTGKTPAAEETVTTILGMLASPYHYLIIIVVLVIILAVVVVGFSCRKKFISYLKGICSGGGGGPERVHRVLFRRRSCPSRVPGAEDNARNETLSNRYLQPTQVSEQEIQGQELAELTGVTVELPEEPQRLLEQ... | Function: Receptor for the cytotoxic ligand TRAIL . Contains a truncated death domain and hence is not capable of inducing apoptosis but protects against TRAIL-mediated apoptosis . Reports are contradictory with regards to its ability to induce the NF-kappa-B pathway. According to PubMed:9382840, it cannot but accordin... |
Q8GQQ1 | MYLYTSYGTYQFLNQIKLNHQERSLFQFSTNDSSIILEESEGKSILKHPSSYQVIDSTGEFNEHHFYSAIFVPTSEDHRQQLEKKLLHVDVPLSNFGGFKSYRLLKPTEGSTYKIYFGFANRTAYEDFKASDIFNENFSKDALSQYFGASGQHSSYFERYLYPIEDH | Function: Contributes to virulence and biofilm formation.
PTM: Each of the three conserved histidine residues contributes to TRAP phosphorylation. Phosphorylation is essential for TRAP activity (By similarity).
Sequence Mass (Da): 19529
Sequence Length: 167
Subcellular Location: Membrane
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P03562 | MRNSSSSTPPSIKAQHRAAKRRAIRRRRIDLNCGCSIYIHIDCRNNGFTHRGTYHCASSREWRLYLGDNKSPLFQDNQRRGSPLHQHQDIPLTNQVQPQPEESIGSPQGISQLPSMDDIDDSFWENLFK | Function: Strong activator of the late viral genes promoters. Enhances the expression of the capsid protein and nuclear shuttle protein. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral... |
A1Z8N1 | MSGRDNRGAGGGGGGHQPLSNAMGKLKEKLTRVGDELGYHRVESNLSTSNTATSLDTILPEDPFLFPQVSPQRHPQNTVRTQRLLEDEPPLSFRPLLEDDDINEPPTQQQQRTPLRASGSLELTPLPPPPTSLEIREHRDRQQRGAQGDELQRSKQSLKGSRVSFERRDTGNSNTNSNKAAESSDEDSFEEKRTGFQQQKATSVDHKGILKDLKHILANDNRRQFQAKKHVSLDVKGTRFLQDLLKESSSEEEFHKTRREFQGRKHQSLDPRVTFKLDKVLQGSSTDSDEEGEDAEHKRLIHRPKDITKPVIIDLKDLES... | Function: Low-capacity facilitative transporter for trehalose. Does not transport maltose, sucrose or lactose. Mediates the bidirectional transfer of trehalose. Responsible for the transport of trehalose synthesized in the fat body and the incorporation of trehalose into other tissues that require a carbon source, ther... |
Q8MKK4 | MKILMRADTHVSFSVPADGLKANFTFSQVLAALSVSLCSLVVGFVSAYTSPALVSMTDRTITSFEVTKDAGSWVGGIMPLAALAGGITGGPLIEYLGRRSTILATAVPFIVSSLLIACAVNVIMILCGRFLTGFCVGIASLSLPVYLGETLQPEVRGTLGLLPTALGNIGILVCYVAGSFMNWSMLAFLGAALPVPFLILMIIIPETPRWFVNRGQEERARKALKWLRGKEADVEPELKELMQSQADADRQATQNTCLELFKRNNLKPLSISLGLMFFQQFSGINAVIFYTVQIFKDAGSTIDSNLSTIIVGVVNFFATF... | Function: Fails to transport trehalose.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53088
Sequence Length: 488
Subcellular Location: Cell membrane
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Q9SU50 | MKSYKLNNPNLLISTHTHNKLFLSSSPFNLLFSFPSFIYLKQQRSLFFFFFFFLCFSFTTSMLDSDTDTDSGPVVATTKLVTFLQRVQHTALRSYPKKQTPDPKSYIDLSLKRPYSLSTIESAFDDLTSESHDQPVPVETLEKFVKEYFDGAGEDLLHHEPVDFVSDPSGFLSNVENEEVREWAREVHGLWRNLSCRVSDSVRESADRHTLLPLPEPVIIPGSRFREVYYWDSYWVIKGLMTSQMFTTAKGLVTNLMSLVETYGYALNGARAYYTNRSQPPLLSSMVYEIYNVTKDEELVRKAIPLLLKEYEFWNSGKHK... | Function: Involved in the regulation of trehalose content by hydrolyzing trehalose to glucose.
Catalytic Activity: alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71355
Sequence Length: 626
Subcellular Location: Cell membrane
EC: 3.2.1.28... |
B0KTG9 | MDLLANVPSWSDIERSLDQKFSAVNQSIHQGLQSANDSWHGFSRRVSDGAGQAYGYLGGHRIDNVQQALAMSYPIFQEDLKRKWASIGIEQILPVLLQLVKEVSMILGGSIAVGSAAGGAIGALAFGVGAAPGAVAGAGIGLEVGNLILLALGLSAIAEYFIKGLPVCLATLQEGIATAWNAEEGVKPAGLDPTGGSVAVIQERTERAARQLARGQEQLVLLLLMAIVTYLLRGQMKAGIMGSMENIATRSAKLQADIANKQFGAWLAKNEAKLLAHPDLQIKGPTPVKKPEPLQPARQPEKASAPKPVAKPAVMSLREA... | Function: Toxic component of a contact-dependent interbacterial competition system (also called effector-immunity systems). Acts by ADP-ribosylating a number of target proteins in target cells; E.coli target proteins include FtsZ, EFTu, RNase E, Fis, YegQ, GuaB and IF2.
Catalytic Activity: L-arginyl-[protein] + NAD(+) ... |
A8GG78 | MSELSAARELDEIAHTASEGWMIAGLIGGAIVGAALIAVTGGTAAVAVAAVVAGASAGGGLGEVLGSMSWAPRHVTGVLADGSPNVYINGRPAIRAHISTGECSEDGPAKKVVAQGSAKVYINDFPAARINDLLACSAEIHTGSPNVIIGGEKEQTDDIEPEIPDWVNWTLLAAGAGAAAVLATPAIAILGTLGGLGGGFAGSLIGGAFFGEGSDGQKWSMLAGGFVGGFAGGKGGAKFDAWRNTKIVEPPPRVTTKVDPISPPRMTLAEAVGQEQAKVWTQTARANAEKNNAQLSTLLTDDQIGAIYGYTTNEGYTALN... | Function: Toxic component of a contact-dependent interbacterial competition system (also called effector-immunity systems). Acts by ADP-ribosylating a number of target proteins in target cells; E.coli target proteins include FtsZ, EFTu, RNase E, Fis, RL9, SucB, and LolD. FtsZ is thought to be the physiologically releva... |
P74130 | MASIAHCSGGLVGAGNFDFILGGSDPVGRHGLMELQPWHWCCLPLEGRTGSEIFSQLFGHQGIATLLESPYPASPDHPHLGRYSLCAGQPRKGRLWTPKPEEIFSFLNQLCPCNHDVNLTKNIPEHLPFHGGWLGWLGYDTAWAIEKLPYSKADDLPFPVAYWYEPENFVILDHQEQLLWLATTDQEKIKFFQTQLADKINSVSSPQVPPLNLTYTTDQDQYETMVNQAKQYIKAGDIFQANLTLRFIAKTEQKLNSWQVYQHLQTINPSPFASYWRSPWGDVVSCSPERLVKLEGNVAQTRPIAGTRARGKNLAEDEQL... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 54271
Sequence Length: 485
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
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Q08693 | MRSSYQPVSTTNFEHENAIPTASSSHNLLMSQRFDDSPPSSNDNSIETNITPPPEPPSYEFDIEDPHDDLHKRTHLQRVSIGFQEKILEPLMENIIHPLLQISKFVPDKADYYLSKIGNPFILRRFFYIIFMSFIAYYVLSSGYLFNEKASGSKGMFSQHDILFEYAKKSVDLAKFERDLEYISSMPHGSGTKGDAAIYRYIQESFDNNGLKLVKEMGYSVYSNYPGNVSISYYDNKNEKHDLELSKENFNPLSSNGKLSKVSLIYGGKGTTYDLQHLKDSKTIEDGKDYVLLLQYDKLVSQQVLIAEKFGAKAVIFISE... | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 91995
Sequence Length: 809
Subcellular Location: Membrane
EC: 3.-.-.-
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A8J4S9 | MASSCSIRCGSRNILVNAAATFLALLVVLRCFANAEKPSPCQSDVYCRGELLHTIQMASIYKDSKTFVDMKMKRPPDETLKSFREFMERHEQMPTRYQIERFVNDTFDPEGSEFEDWDPDDWTFRPKFLSRILDDDLRNFASELNGIWKMLGRKMKDDVRVNEELYSIIYVPHPVIVPGGRFREFYYWDSYWIVKGLLLSEMYTTVKGMLTNFVSLVDKIGFIPNGGRIYYTMRSQPPMLIPMVDEYLKITHDYEWLENNLYLLEKEFDFWMTNRTVEIEVDGVNYVLARYNEQSSGPRPESYKEDYLTSQSFRTNEEKD... | PTM: Glycosylated; contains 3.1% carbohydrates.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose
Sequence Mass (Da): 72817
Sequence Length: 626
Subcellular Location: Membrane
EC: 3.2.1.28
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P32358 | MRLFLLLVGLTTVIADDLPPTCIRPVYCNSTLLHYVQMARLYPDSKTFVDFQMRKDENATLSAFQELLDRTNHNPTKEDLQEFVVDFFDETSELEEWKPDDHKENPPFLAKIRDQGFREFAKALNDIWPTLARRVKPSVLEKPEQSSLVPMTHGFIVPGGRFKEIYYWDAYWIIEGLLITDMTETAKGMIENLIELLYKFGHIPNGSRWYYQERSQPPLLAAMIKLYYEKTKDIEFIRKYISALEKELEYWLDTHLIAFNKDDRVYTLLRYYIPSAGPRPESYYEDYELAQKLDKNTDPNDIYADLKSAAESGWDFSTRW... | Function: Involved in uptake of hemolymph trehalose into epithelial cells in the midgut of feeding larvae.
Catalytic Activity: alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose
Sequence Mass (Da): 66542
Sequence Length: 579
Subcellular Location: Basolateral cell membrane
EC: 3.2.1.28
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P52494 | MFTKNHRRMSSTSSDDDPFDVAEKYYGEERKKKLNRVRTFSAFESTKYGAGPISPLRPTYEPPPVIKETSEPLSSSSSTSSPPTLTPQTSQVQFNLGVGKTKNGSAIHSDSEEEEEDEDPVSNTKKGEADEKDPFDTTDSKLENENSTPSSITGKEIIPHPTGFRGSSEESAIRRKPSIIPIYHDNISQESVIRNANTPTTYNREKFHLRRGSLDESTFIRPKKYYINDVQGTLRELLANEDTDNNCQITIEDTGPKVLRLGTANSLGINQSSIRGTYRLSNLLQELTIASRFGRHQIVLDEARLSENPVDRMKRLISTS... | Function: Hydrolyzes intracellular trehalose to glucose.
Catalytic Activity: alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose
Sequence Mass (Da): 104023
Sequence Length: 907
Pathway: Carbohydrate degradation.
Subcellular Location: Cytoplasm
EC: 3.2.1.28
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O58762 | MMYEVKEFSSGKRKLEDYKSIIGEEEVSKIQEKAEKLKGRSFVHVNSTSFGGGVAEILHSLVPLLRSIGIEARWFVIEGPTEFFNVTKTFHNALQGNESLKLTEEMKELYLNVNRENSKFIDLSSFDYVLVHDPQPAALIEFYEKKSPWLWRCHIDLSSPNREFWEFLRRFVEKYDRYIFHLPEYVQPELDRNKAVIMPPSIDPLSEKNVELKQTEILRILERFDVDPEKPIITQVSRFDPWKGIFDVIEIYRKVKEKIPGVQLLLVGVMAHDDPEGWIYFEKTLRKIGEDYDVKVLTNLIGVHAREVNAFQRASDVILQ... | Function: Synthesizes trehalose from ADP-, UDP- or GDP-glucose and glucose.
Catalytic Activity: an NDP-alpha-D-glucose + D-glucose = a ribonucleoside 5'-diphosphate + alpha,alpha-trehalose + H(+)
Sequence Mass (Da): 48069
Sequence Length: 415
EC: 2.4.1.245
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Q1ARU5 | MLQRVNPGHKALADYRSIIRRELYGELQELAGRLRGARVLHINATSFGGGVAEILYTLVPLARDAGLEVEWAIMFGAEPFFNVTKRFHNALQGADYELTIEDRAIYEEYNRRTAQALAESGEEWDIVFVHDPQPALVREFSGGLGEGTRWIWRCHIDTSTPNRQVLDYLWPYIADYDAQVYTMREYTPPGVEMPGLTLIPPAIDPLSPKNMALSRDDASYIVSQFGVDVERPFLLQVSRFDPWKDPLGVIDVYRMVKEEVGEVQLVLVGSMAHDDPEGWDYWYKTVNYAGGDPDIFLFSNLTNVGAIEVNAFQSLADVVI... | Function: Synthesizes trehalose from ADP-glucose and glucose. The reaction is reversible, the equilibrium strongly favors trehalose synthesis.
Catalytic Activity: an NDP-alpha-D-glucose + D-glucose = a ribonucleoside 5'-diphosphate + alpha,alpha-trehalose + H(+)
Sequence Mass (Da): 46557
Sequence Length: 416
EC: 2.4.1.... |
Q91XB0 | MGSQTLPHGHMQTLIFLDLEATGLPSSRPEVTELCLLAVHRRALENTSISQGHPPPVPRPPRVVDKLSLCIAPGKACSPGASEITGLSKAELEVQGRQRFDDNLAILLRAFLQRQPQPCCLVAHNGDRYDFPLLQTELARLSTPSPLDGTFCVDSIAALKALEQASSPSGNGSRKSYSLGSIYTRLYWQAPTDSHTAEGDVLTLLSICQWKPQALLQWVDEHARPFSTVKPMYGTPATTGTTNLRPHAATATTPLATANGSPSNGRSRRPKSPPPEKVPEAPSQEGLLAPLSLLTLLTLAIATLYGLFLASPGQ | Cofactor: Binds 2 Mg(2+) per subunit. The second magnesium ion interacts with only one residue. Substitution with Mn(2+) results in partial activity.
Function: Major cellular 3'-to-5' DNA exonuclease which digests single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) with mismatched 3' termini . Prevents cell-int... |
Q9BQ50 | MSEAPRAETFVFLDLEATGLPSVEPEIAELSLFAVHRSSLENPEHDESGALVLPRVLDKLTLCMCPERPFTAKASEITGLSSEGLARCRKAGFDGAVVRTLQAFLSRQAGPICLVAHNGFDYDFPLLCAELRRLGARLPRDTVCLDTLPALRGLDRAHSHGTRARGRQGYSLGSLFHRYFRAEPSAAHSAEGDVHTLLLIFLHRAAELLAWADEQARGWAHIEPMYLPPDDPSLEA | Cofactor: Binds 2 Mg(2+) per subunit. The second magnesium ion interacts with only one residue. Substitution with Mn(2+) results in partial activity.
Function: Exonuclease with a preference for double-stranded DNA with mismatched 3' termini. May play a role in DNA repair.
Catalytic Activity: Exonucleolytic cleavage in ... |
Q44315 | MRTPVSTYRLQIRKGFTLFDAAKTVPYLHSLGVDWVYLSPVLTAEQGSDHGYDVTDPSAVDPERGGPEGLAAVSKAARAAGMGVLIDIVPNHVGVATPAQNPWWWSLLKEGRQSRYAEAFDVDWDLAGGRIRLPVLGSDDDLDQLEIRDGELRYYDHRFPLAEGTYAEGDAPRDVHARQHYELIGWRRADNELNYRRFFAVNTLAGVRVEIPAVFDEAHQEVVRWFREDLADGLRIDHPDGLADPEGYLKRLREVTGGAYLLIEKILEPGEQLPASFECEGTTGYDALADVDRVLVDPRGQEPLDRLDASLRGGEPADYQ... | Function: Catalyzes the conversion of maltooligosaccharide into the non-reducing saccharide, maltooligosyl trehalose (alpha-maltooligosyl alpha-D-glucoside) by intramolecular transglycosylation.
Catalytic Activity: 4-[(1->4)-alpha-D-glucosyl](n-1)-D-glucose = 1-[(1->4)-alpha-D-glucosyl](n-1)-alpha-D-glucose
Sequence Ma... |
P9WQ20 | MAFPVISTYRVQMRGRSNGFGFTFADAENLLDYLDDLGVSHLYLSPILTAVGGSTHGYDVTDPTTVSPELGGSDGLARLSAAARSRGMGLIVDIVPSHVGVGKPEQNAWWWDVLKFGRSSAYAEFFDIDWELGDGRIILPLLGSDSDVANLRVDGDLLRLGDLALPVAPGSGDGTGPAVHDRQHYRLVGWRHGLCGYRRFFSITSLAGLRQEDRAVFDASHAEVARWFTEGLVDGVRVDHLDGLSDPSGYLAQLRELLGPNAWIVVEKILAVDEALEPTLPVDGSTGYDVLREIGGVLVDPQGESPLTALVESAGVDYQE... | Function: Catalyzes the conversion of maltooligosaccharide into the non-reducing saccharide, maltooligosyl trehalose (alpha-maltooligosyl alpha-D-glucoside) by intramolecular transglycosylation.
Catalytic Activity: 4-[(1->4)-alpha-D-glucosyl](n-1)-D-glucose = 1-[(1->4)-alpha-D-glucosyl](n-1)-alpha-D-glucose
Sequence Ma... |
Q44316 | MTHTYPREAAKPVLGPARYDVWAPNAESVTLLAGGERYAMQRRAETGPEDAGWWTAAGAPTDGNVDYGYLLDGDETPLPDPRTRRQPDGVHALSRTFDPSAYSWQDDAWQGRELQGAVIYELHLGTFTPEGTLEAAAGKLDYLAGLGVDFIELLPVNAFNGTHNWGYDGVQWFAVHEAYGGPEAYQRFVDAAHAAGLGVIQDVVYNHLGPSGNYLPRFGPYLKQGEGNTWGDSVNLDGPGSDHVRRYILDNLAMWLRDYRVDGLRLDAVHALKDERAVHILEDFGALADQISAEVGRPLTLIAESDLNNPRLLYPRDVNG... | Catalytic Activity: hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-[(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-alpha-D-glucan.
Sequence Mass (Da): 65832
Sequence Length: 598
Pathway: Glycan biosynthesis; trehalose biosynthesis.
Subcellular Location: Cytoplasm
EC: 3.2.1.141
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Q9RX51 | MTQTQPVTPTPPASFQTQHDPRTRLGATPLPGGAGTRFRLWTSTARTVAVRVNGTEHVMTSLGGGIYELELPVGPGARYLFVLDGVPTPDPYARFLPDGVHGEAEVVDFGTFDWTDADWHGIKLADCVFYEVHVGTFTPEGTYRAAAEKLPYLKELGVTAIQVMPLAAFDGQRGWGYDGAAFYAPYAPYGRPEDLMALVDAAHRLGLGVFLDVVYNHFGPSGNYLSSYAPSYFTDRFSSAWGMGLDYAEPHMRRYVTGNARMWLRDYHFDGLRLDATPYMTDDSETHILTELAQEIHELGGTHLLLAEDHRNLPDLVTVN... | Catalytic Activity: hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-[(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-alpha-D-glucan.
Sequence Mass (Da): 66910
Sequence Length: 600
Pathway: Glycan biosynthesis; trehalose biosynthesis.
Subcellular Location: Cytoplasm
EC: 3.2.1.141
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Q142P9 | MSIVNLSSYQFATIEDTAAWRPFVTERCNALGLKGTVLLAPEGINLFVAGTRENTDAFIHYIRHDALFEGKFADLQFKESLSDKQPFTRMLVKLKREIITMKKPAIRPELGRAPFVDAPTLKSWLDRGHDDEGRPVVMLDTRNAFEVDVGTFDNALDYRITKFSEFPEVIEQNRADLEGKTIVSFCTGGIRCEKAAIHMKDVGIENVYQLEGGILKYFEEVGGAHYHGDCFVFDYRTALNPQLEPSKTTQCFGCRAVVTPEAQQSPLYVAGKTCPECHPDSKAARAA | Function: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Catalytic Activity: AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA + A + H2O
Sequence Mass (Da): 32108
Sequence Length: 287
EC: 1.14.-.-
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Q4FLR0 | MFDVFGFYKFKKLTSLKKNKILLQDYLIKKNIRGTIIIANEGVNATISGKANDLKSTITKIKKILNFKKFDSENISKSKFQPFHKPKVKIKKEVVPMGLSLSSKNKKNNHIDPKKWNKLINDKDTLVLDSRKPFEYNVGTFKRSVNPDVANFREFPKYLNKLKKTKPIAMFCTGGIRCEKASVFLEKKGFKNVYQLKGGILNYLKNIKKKESLWNGECFVFDNRISVKHGLITGTYSMCSGCRKPVSPKDKKSKKYEEGVSCVNCHDNLTQTQKERFRMRQKQINLAKKTGSKHIFQKEFK | Function: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Catalytic Activity: AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA + A + H2O
Sequence Mass (Da): 34811
Sequence Length: 301
EC: 1.14.-.-
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Q7N5W3 | MPVLHNRISNKELKARMLAETQPRTTISFYKYFNILNPLDFRNSLYQQFTDLSVFGRVYIAKEGINAQISLPTHNLEAFKALLYSVDPALDNLRLNIALDDDGKSFWVLRMKVRDRVVADGIDDETFDPSKTGEYLKAEQVNQMLDNPDTLFVDMRNHYEYEVGHFENAIEVPSDTFREQLPMVAEMLQDNKDKNIVMYCTGGIRCEKASAYMLHNGFKNVYHVEGGIIEYARKAREQGLPVRFVGKNFVFDERMGERISDDVIAHCHQCGVSCDSHTNCKNEGCHLLFIQCPECATKFEGCCSEMCREEVRLPETEQRA... | Function: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Catalytic Activity: AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA + A + H2O
Sequence Mass (Da): 40418
Sequence Length: 352
EC: 1.14.-.-
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Q6LSS4 | MAQYVVCALYKFVALEDFEAIRQPLTDVMEKNKIRGTLLLASEGINGTVASTREGIDALLAWFKQDQRLTDVVYKESFDENQPFNRTKVKLKKEIVTMGVEGIDPRHVVGTYVKPKDWNALIADPDVFVVDTRNDYEIEIGTFKHAVNPETESFREFPEYVEKNLDPEKHKKVAMFCTGGIRCEKSTAYLKEQGFDEVYHLEGGILKYLEEVPEKESLWEGECYVFDGRVAVDHQLEKGQYSVCNACRLPITDAA | Function: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Catalytic Activity: AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA + A + H2O
Sequence Mass (Da): 29104
Sequence Length: 255
EC: 1.14.-.-
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A2BX81 | MKKNNYKIVSLYSFFSFQENSIIELKQNLLRIEKENDLSGLLIIASEGINGTICAEEKIIENILNLIKNIVGNNQLNIKVSYSKEKIFKKLKLKIKNEIVTMGVPEINPLEDAGTYIDSFNWNKLIKDKDTIVIDTRNHYEVSIGSFKKSINPNTKNFSEFPQWVDNNLDNHLGNENSKNIAMFCTGGIRCEKATTLLKNKGYKNIFHLKGGILKYLEDISKEESLFEGECFVFDKRVALDHELKKGSYSICHACGMPISIEDQTKVEYIEGIQCHFCINKFTDEDRKRFEERQKQINKLKVKNQEISNN | Function: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Catalytic Activity: AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA + A + H2O
Sequence Mass (Da): 35765
Sequence Length: 310
EC: 1.14.-.-
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Q7V6T9 | MNLQDDQTSADLFQVATFYSFTAWTEVTIACLLHDLLSLGDEHQLMGTVLLAEEGVNGTICGSVDGVSALLERLESDLIEGLFELKISWTPEQAFRRFKVRRKAEIVTMGLAGLNPSKTVGTYVDAHEWNDLIDDPDTLLIDTRNDYEVAIGEFKGAINPQTKCFRDFPAWVEQQLRSMVKAQTPARIAMYCTGGIRCEKATSYLIEKGFTNVHHLRGGILRYFEEVSQTESRWQGECFVFDQRVALNHQLSPGVHCLCHACGMPLTPEDQTMNSYLPGVQCRHCVDQFSDTDRIRFAERQRQMEHSSRK | Function: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Catalytic Activity: AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA + A + H2O
Sequence Mass (Da): 35122
Sequence Length: 310
EC: 1.14.-.-
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Q55613 | MAYQVTTFYHFTRLNCLAEKQSRWQELGDRLGLKGTILLAEEGVNATIAGESAAIEEMVKIMAADLGLTSVPQRHSWAKTIPFQRMKVKIKPEIVSLGQPQVNPEKQVGTYVSPQQWNQLLQDPDVVVIDTRNDYEVAIGTFQGAVNPCTKKFRQFPDYVKNNLDQQKNKKVAMFCTGGIRCEKASAYLLEEGFAEVYHLRGGILHYLETIAPEESLWQGECFVFDERVAVQEGLKVGSHALCDHCGYPLRVGDLAEIRYAVRHCPQCGLTVAVSNEL | Function: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Catalytic Activity: AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA + A + H2O
Sequence Mass (Da): 31166
Sequence Length: 278
EC: 1.14.-.-
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Q3SKY5 | MSIVNISCYKFVTLNDREALKADLGARCLQLGLRGTILLAPEGINVFLAGTRAAIDAIVAGLRADPRFADLEPKLSLSAEAPFTRMRVRLKKEIITMKMPVVRPEEGRAPAVAAATLKRWLDQGCDDEGRPVVMLDTRNDYEVAAGSFENAVDYGIGVFSEFPPQLQRRRDDYAGKTVVSFCTGGIRCEKAAIHMQEIGVERVYQLEGGILKYFEEVGGAHYRGGCFVFDAREAVGADLQPLGGRVHC | Function: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Catalytic Activity: AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA + A + H2O
Sequence Mass (Da): 27168
Sequence Length: 248
EC: 1.14.-.-
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Q87FT1 | MSQYVVCALYKFVELNNYQELREPLLALMEKHHIRGTLLLAGEGINGTVASDRAGIDTLLEWLNTEPRLTGTVYKESYSETQPFNRTKVKLKKEIVTLGVEGIDPRHVVGTYVKPQDWNDLIADPEVFVVDTRNDYEIEIGTFKGAVNPNTETFREFPDYVKENMDPAKHKKVAMFCTGGIRCEKSTAYMKEQGFEEVYHLEGGILKYLEEVPQEESMWEGDCYVFDGRVAVNHQLEKADYDLCNACRLPITDEDKQSELFEQGVSCPKCHGKHSEEQVERFREREKQVSLANQRGEQHVGGESAKQRAQRREAKLAKKA... | Function: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Catalytic Activity: AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA + A + H2O
Sequence Mass (Da): 37300
Sequence Length: 326
EC: 1.14.-.-
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Q8D3D6 | MSCNIIKKISNKRYYSINYKKKTKTISFYKYCKIENIDCIQEKLFEICKKLEILGRIYISYEGINAHISIKKHKIEELKIFIKKTFDYLTDIRFNLYSDNKKQPFKKLKIKKKLNILNCGIKDCSFDIKNTGHKLTANDFNAILMKNDFILVDMRNSYEYEIGHFENALKISSKTFRQQLKLLINNLKFYKSKNIIMYCTGGIRCEAASAWMMHNGFKYVSFLDGGIIEYVNFIKKNNYPMKFLGKIFVFDDRLYEKVTSDVLSLCHQCKIQPCDNYINCKNKKCNSLFIQCIYCNKTLNEFCSNFCNEYYQSKN | Function: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Catalytic Activity: AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA + A + H2O
Sequence Mass (Da): 37378
Sequence Length: 315
EC: 1.14.-.-
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Q9H8W5 | MSENRKPLLGFVSKLTSGTALGNSGKTHCPLCLGLFKAPRLLPCLHTVCTTCLEQLEPFSVVDIRGGDSDTSSEGSIFQELKPRSLQSQIGILCPVCDAQVDLPMGGVKALTIDHLAVNDVMLESLRGEGQGLVCDLCNDREVEKRCQTCKANLCHFCCQAHRRQKKTTYHTMVDLKDLKGYSRIGKPILCPVHPAEELRLFCEFCDRPVCQDCVVGEHREHPCDFTSNVIHKHGDSVWELLKGTQPHVEALEEALAQIHIINSALQKRVEAVAADVRTFSEGYIKAIEEHRDKLLKQLEDIRAQKENSLQLQKAQLEQL... | Function: E3 ubiquitin-protein ligase that plays a role in the regulation of inflammatory response . Mechanistically, mediates the 'Lys-48'-linked polyubiquitination of TAB2, a regulatory protein of the kinase TAK1, leading to its degradation via the proteasomal pathway and inhibition of the TLR-mediated inflammatory i... |
Q6PFY8 | MSEIRKPLLGFVHKLQDANASGSSGKTHCPTCLRLFKVPRLLPCLHTVCTTCLEKLDPFSVVDIRGGDSDTSSEGSVFQDPELCSLQPQIGILCPVCDAQVDLPLGGVKALTVDHLAMNDVLLENLRGEGQGLVCDLCSDREVEKRCQTCKANLCHFCCQAHRRQKKTTYHTMVDLKDLKGYSQVGKPILCPSHPAEELRLFCELCDRPVCRDCVVGEHREHPYDFTSNVIHKHGDSVRELLRDTQPHVEALEDALAQIKSVNNALQERVEAVAADVRTFSEGYIKAIEEHRDKLLQQLDDIRIQRETALQLQKAQLEQL... | Function: E3 ubiquitin-protein ligase that plays a role in the regulation of inflammatory response . Mechanistically, mediates the 'Lys-48'-linked polyubiquitination of TAB2, a regulatory protein of the kinase TAK1, leading to its degradation via the proteasomal pathway and inhibition of the TLR-mediated inflammatory i... |
Q96LD4 | MDGSGPFSCPICLEPLREPVTLPCGHNFCLACLGALWPHRGASGAGGPGGAARCPLCQEPFPDGLQLRKNHTLSELLQLRQGSGPGSGPGPAPALAPEPSAPSALPSVPEPSAPCAPEPWPAGEEPVRCDACPEGAALPAALSCLSCLASFCPAHLGPHERSPALRGHRLVPPLRRLEESLCPRHLRPLERYCRAERVCLCEACAAQEHRGHELVPLEQERALQEAEQSKVLSAVEDRMDELGAGIAQSRRTVALIKSAAVAERERVSRLFADAAAALQGFQTQVLGFIEEGEAAMLGRSQGDLRRQEEQRSRLSRARQN... | Function: E3 ubiquitin-protein ligase that mediates the ubiquitination and proteasomal degradation of CYLD.
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.
Sequence... |
Q8C0E3 | MDGSGPFSCPICLEPLREPVTLPCGHNFCLACLGALWPHRSAGGTGGSGGPARCPLCQEPFPDGLQLRKNHTLSELLQLRQGSVPGPMSAPASGSTRGATPEPSAPSAPPPAPEPSAPCAPEQWPAGEEPVRCDACPEGAALPAALSCLSCLASFCSAHLAPHERSPALRGHRLVPPLRRLEESLCPRHLRPLERYCRVERVCLCEACATQDHRGHELVPLEQERALQEVEQSKVLSAAEDRMDELGAGIAQSRRTVALIKSAAVAERERVSQMFAEATATLQSFQNEVMGFIEEGEATMLGRSQGDLRRQEEQRSRLSK... | Function: E3 ubiquitin-protein ligase that mediates the ubiquitination and proteasomal degradation of CYLD.
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.
Sequence... |
Q8IWZ4 | MSRRIIVGTLQRTQRNMNSGISQVFQRELTCPICMNYFIDPVTIDCGHSFCRPCFYLNWQDIPILTQCFECIKTIQQRNLKTNIRLKKMASLARKASLWLFLSSEEQMCGIHRETKKMFCEVDRSLLCLLCSSSQEHRYHRHCPAEWAAEEHWEKLLKKMQSLWEKACENQRNLNVETTRISHWKAFGDILYRSESVLLHMPQPLNLALRAGPITGLRDRLNQF | Function: E3 ubiquitin-protein ligase which promotes K48-linked polyubiquitination of protein methyltransferase PRMT1, leading to PRMT1 degradation . This suppresses methylation of the PRMT1 substrate MAP3K5/ASK1, promoting its activation and increasing MAP3K5-dependent cell death induced by oxidative stress . TRIM48-m... |
Q12612 | MVDQDWIKALVNIPISHAVGVVAASTVIYFLSSCFYNLYLHPLRKIPGPKLAAIGPYLEFYHEVIRDGQYLWEIAKMHDKYGPIVRVNDKEVHIRDPSYYSTIYTAGARKTNKDPATVGAFDVPTATAATVDHDHHRARRGYLNPYFSKRSITNLEPFIHERVTKLLSRFQEHLDNDQVLSLDGAFCALTADVITSRFYGKHYNYLDLPDFHFVVRDGFLGLTKVYHLARFIPVLVTVLKRLPYSCLRLIAPSVSDLLQMRNEIHERGGDEFLSSKTSEAKSSILFGALADTHIPPVERTVERMLDEGTVILFAGTETTS... | Function: Cytochrome P450 monooxygenase; part of the core gene cluster that mediates the biosynthesis of trichothecenes, a very large family of chemically related bicyclic sesquiterpene compounds acting as mycotoxins, including T2-toxin . The biosynthesis of trichothecenes begins with the cyclization of farnesyl diphos... |
Q86XT4 | MAWQVSLPELEDRLQCPICLEVFKEPLMLQCGHSYCKGCLVSLSCHLDAELRCPVCRQAVDGSSSLPNVSLARVIEALRLPGDPEPKVCVHHRNPLSLFCEKDQELICGLCGLLGSHQHHPVTPVSTVYSRMKEELAALISELKQEQKKVDELIAKLVNNRTRIVNESDVFSWVIRREFQELHHLVDEEKARCLEGIGGHTRGLVASLDMQLEQAQGTRERLAQAECVLEQFGNEDHHKFIRKFHSMASRAEMPQARPLEGAFSPISFKPGLHQADIKLTVWKRLFRKVLPAPEPLKLDPATAHPLLELSKGNTVVQCGL... | Function: E3 ubiquitin-protein ligase that ubiquitinates Beclin-1/BECN1 in a 'Lys-63'-dependent manner enhancing its binding to ULK1 . In turn, promotes starvation-induced autophagy activation. Interacts also with p62/SQSTM1 protein and thereby induces the formation and the autophagy clearance of aggresome-associated p... |
Q810I2 | MAWRLTVPELQDQLQCPICLEVFKEPLMLQCGHSYCKDCLDNLSQHLDSELCCPVCRQSVDCSSSPPNVSLARVIDALRLPGDIEPTVCVHHRNPLSLFCEKDQEFICGLCGLLGSHQHHRVTPVSTVYSRMKEELAGRISELKEEHRNVEEHIGKLVNNRTRIINESDVFSWVIRREFQELHHLVDEEKARCLEGLEGHTRGLVASLDMQLEQAQGTQERLAQAEQVLEQFGNESHHEFIRFHSVASRAEVQQARPLEGVFSPISFKPALHQADIKLTVWKRLFRKVLPAPASLKLDPATAHPLLELSKGNTVVHCGLL... | Function: E3 ubiquitin-protein ligase that ubiquitinates Beclin-1/BECN1 in a 'Lys-63'-dependent manner enhancing its binding to ULK1 . In turn, promotes starvation-induced autophagy activation. Interacts also with p62/SQSTM1 protein and thereby induces the formation and the autophagy clearance of aggresome-associated p... |
B2B9D9 | MGKKDASTTRTPVDQYRKQIGRQDYKKNKPVLKATRLKAEAKKAAIGIKEVILVTIAILVLLFAFYAFFFLNLTKTDIYEDSNN | Function: Plays a role in cell growth and maintenance of cell morphology.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9584
Sequence Length: 84
Domain: Both the conserved triple repeat of the QXXK/R motif and the hydrophobic region are essential for its activity. The hydrophobic region contribute... |
Q9BQ61 | MAARGRRAEPQGREAPGPAGGGGGGSRWAESGSGTSPESGDEEVSGAGSSPVSGGVNLFANDGSFLELFKRKMEEEQRQRQEEPPPGPQRPDQSAAAAGPGDPKRKGGPGSTLSFVGKRRGGNKLALKTGIVAKKQKTEDEVLTSKGDAWAKYMAEVKKYKAHQCGDDDKTRPLVK | Function: Exoribonuclease that is part of the telomerase RNA 3' end processing complex and which has the ability to all four unpaired RNA nucleotides from 5' end or 3' end with higher efficiency for purine bases .
Sequence Mass (Da): 18419
Sequence Length: 176
Domain: The C-terminus contains a key domain which is respo... |
Q9D735 | MAARGRRAEPPGREAPGPAGSGRSRWAESGPGTSPESGDDEVSGSSPVSSGVNLFANDGSFLELFKRKMEEEQRQRQEEPPPGPQRPDPPASAAAGPGNPKRKGGPGPTLSFVGKRRGGNKLALKTGIVAKKQKTEDEVLTSKGDAWAKYMAEVKKYKAHQCGDDDKTRPLVK | Function: Exoribonuclease that is part of the telomerase RNA 3' end processing complex and which has the ability to all four unpaired RNA nucleotides from 5' end or 3' end with higher efficiency for purine bases (By similarity).
Sequence Mass (Da): 18377
Sequence Length: 173
Domain: The C-terminus contains a key domain... |
Q9VML9 | MIMTMMQTVRAWQQESDVEHRKQHKQRWRPDGAHISAAYDLNSDNDDGHHRVVHNQNNGSPNSSPNQSTSAFRQRQPHHPPTGQQPPRLPCTVTHFSAHWKTLLILLTLLSASTLTASANVTSTISPPINGSSTDYILLYGESTTSLVPALTTGLSGDGSGAVIEDEEDAEKASEYIFDRTDVRIIFITLYTLVFCCCFFGNLLVILVVTLSRRLRSITNFFLANLAFADFCVGLFCVMQNLSIYLIESWVFGEFLCRMYQFVHSLSYTASIFILVVICMERYFAIVHPITCKQILTAARLRMVIVTVWITSAVYSTPKF... | Function: G-protein coupled receptor which is activated by the Trissin peptide in vitro, leading to increased intracellular calcium ion levels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74486
Sequence Length: 669
Subcellular Location: Cell membrane
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O76997 | MRGPRRFRLWTRANVLTVISILTSILSGAGCSPLSQLPSDNPAHVGVQDGVTTERVDRSKNHRNTTASSGAHRVTSGEPLGDRVTTRSTTAPDQVPGDASRNTTMAGTKCSLQVDLSTFACPADCQCNATSEGMVVSCVTPDTLREFPVIAREVARAVIKLELRGQSKLTSLKTELKFFTCLKHLTIENCGLNNIQGIAFKTLTSLETINLRHNHLTEFPQELLRTLNLRELWLEGNALTCSCTNLWLRSVDVAADRSEMTCSTRDGVSKMKMTQFKCEPCGIPDIRNMTLVFEPKNGMFLLRFVISGCPKPKIDLLRNH... | Function: May bind an endogenous invertebrate neurotrophin. Binds human NT-3, but not NGF or BDNF.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 89054
Sequence Length: 794
Subcellular Location: Membra... |
P47946 | MVLNYIQRWFKWVIPTFGFLAIHYIYIISLTIIASILLFTGGTTTKIKYIDALFLASSATTQTGLNSVDLNSLSIWQQFILYGFTAITVPIWMHGSISFIRLYWFRRKFKDVVRQNRTRKFQRKLRKSLMKKSEDDEEQGVRGRKIRVMLPYLHSLRSPTSLKNFSRFDTHDSTNNPYFPDNPPSPKADISKDEYFGKYLPKKSDTLDMDLESHNMTFHDYEPSIENKNYDFGSSHSASMQMYEMDDLHPRLRRQSSFISSVNPLEADDTRETLSEGALVQESLPMAYSYSDTNLVVSRDSFTLTGDDNLFPEGGLRPAN... | Function: Together with TRK2, defines the major, high-affinity potassium influx transport system. Involved in maintenance of the proper sodium/potassium ratio in the cell and in regulating the plasma membrane potential.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96045
Sequence Length: 841
Subcel... |
Q10065 | MQLSGFSTNGSGSLNTIVCEKLLFKPNFVQDSFIIGMTILCSVILYGSGNLRYIDALLLASGSCTQTGLQPVDLTQISIYQQLTILLFGVLSTPITVNLGLTLFKLYFYNKRYDMVITNNKLRMTYTYHTVRRRDTPEPSKVGNRKIRVLLDQGNQMHRPVAPETKAEEAEHQENEKHHRHHFRLRKFANAIDRPSFFRGNTMPALPSYAGVRNSQENEDRTEALSPALGKRRMASIDNGSLSVVQNNARNNPVDFYIPSSFEESSFQTIPEDFEPQVHDHENQTQLNHHLDNNSSISSHNPSLETANDGNQETVSSSNS... | Function: Together with TRK1, defines the major, high-affinity potassium influx transport system. Involved in maintenance of the proper sodium/potassium ratio in the cell and in regulating the plasma membrane potential.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 99848
Sequence Length: 880
Subcel... |
P28584 | MPTAKRTSSRASLALPFQLRLVHKKSWGHRLRDFISGFLKSCRPIAKYVFPNFIVVHYIYLITLSIIGSILLYPCKNTAFIDVLFLAAGASTQGGLATKSTNDFNLYQQIVVYVITLLSTPILIHGFLAFVRLYWFERYFDNIRDISKQNFKLRRTMTLQQRELSGSSGNAARSRSFKDNLFRGKFVSREDPRQSASDVPMDSPDTSALSSISPLNVSSSKEESSDTQSSPPNFSSKRQPSDVDPRDIYKSIMMLQKQQEKSNANSTDSFSSETNGPAFIVQERHERRAPHCSLKRHSVLPSSQELNKLAQTKSFQKLLG... | Function: This protein is required for low-affinity potassium transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 101087
Sequence Length: 889
Subcellular Location: Membrane
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Q04856 | MKVVICGAGQVGFGIAERLASEQNDVSIVDASPRRIQIATDQLDVRGVVGHGSHPDVLARAGIEQADMLIAVTLHDEVNMVACQVGHSLFNVPTKVARIRAQTYLQPEWRSMLSRDHMPIDVVISPEIEVGEMVLRRLSLPGAVDTVSFGDGSVVIAGVLCGEACPVVDTPLTQLTQLFPDLPATIVAINRNGKVMATRSSDQIQTGDIAYFVAPADQVGRTLSIFGHDEIPAKRIIIGGGGNIGLYVAQELEKRNAAARIKVVESNRERAQAIAEGLSRSVVLHGDSLAREILDEAGVADSDTMIALTNDDRVNILSCL... | Function: Part of a potassium transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 49334
Sequence Length: 458
Domain: The RCK N-terminal domain binds NAD and possibly other effectors. This is expected to cause a conformation change that regulates potassium transport (By similarity).
Subc... |
O28105 | MKRVQNLLVAVGLSPNYHRRTYPSGKKSLVVRFYATLTPGLEDVAAKEVESFGCKVEEIRERRGRIFFSGEKSAIPLLNHFSRTLERLNVLLLRCEVEGLDDIYAAVKGLDFSFVKGKSFAIRSLRVGEHDFTSMDIARVAGQAVIDSFMESYGERLKVNLNQPDVIIRVELVDSELFVGVDTTGDDAMHKRWWRVYNHPAHLNAAIACGMLRIADWKVDESLIDPMCGSGTIPIEAALMVRNVPNLRDFAYKKLCEWELAFEPNEVRLKLYGMEKFRKHLVGAIRNAVNAGVADTIEFRQGDATEMTGEYDVIITNPPY... | Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the methylation of the guanosine nucleotide at position 6 (m2G6) in tRNA.
Catalytic Activity: guanosine(6) in tRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(6) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 44374
Sequenc... |
Q57880 | MDYYVTLSPGLEKISKNEIESFGGKIKEIRENKGRIFFSGDLKLIPKINYLSRTIERMNILLHREEIPNIALDDIYKRVYNIDWTEWIKENQSFAIRPLRAGEHNFTSIDIGRVAGEAVIKSYQRDKNIRLKVNLDEPDVIVRVEVIFDELIVGIDTTGDIALDKRGYRVFNHPAHLNATIASSLVYLSDWKDDEMLLDPMCGSGTIPIEGALMKRNIPPGKFRENKYGFKFIDIFGYELLDKIKKEIVENKNIYKIIGLDKNQKYLDGAKDNAKNAEVLDTIEFICGDATKLHEKFNESDVIIANPPYGIRIGSKRSVK... | Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the methylation of the guanosine nucleotide at position 6 (m2G6) in tRNA(Cys).
Catalytic Activity: guanosine(6) in tRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(6) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 43738
Se... |
Q8U248 | MKFLLTTAQGIEDIAKREVSLLLKKLGISFQIEEKPLGIEGRLLLEAEKAYYVDEKGRKRELSISTYLNENSRLLHRVIIEIASEKFNGIEKDESEEALKRIKDFVSSLPVEQFVKVSETFAVRSFRKGDHNITSIDIARTVGEAIFERLSRFGTPLVNLDHPAVIFRAELIKDVFFLGIDTTGDSSLHKRPWRVYDHPAHLKASIANAMIELAELDGGSVLDPMCGSGTILIELALRRYSGEIIGIEKYRKHLIGAEMNALAAGVLDKIKFIQGDATQLSQYVDSVDFAISNLPYGLKIGKKSMIPDLYMKFFNELAKV... | Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the methylation of the guanosine nucleotide at position 6 (m2G6) in tRNA(Phe).
Catalytic Activity: guanosine(6) in tRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(6) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 41000
Se... |
Q9YDY7 | MPVPSPMRLAVTHEGRSIIYIPSPEYAVASGRLEPAWLEVFYNPAMEFNRDVSVVAASALRRTGLLTRSGVAFDAHAGVGVRGVRYAVEAGYVKVIMNDINPKASMLAALNARANGLEPGSYMIFNKESNSLMFHLSRERPTPVSLIDIDPYGSPAPFVDAALALSGKGTVVAMTATDLAVLEGGKARAAVRRYMLRSVSKTPVSKETGLRVLLGYVARVAAAHDKAVKPLLAYYADHYYRVYVAVERGARRSDSMLEENLGRLVYCPETGVALALSYAEDPASACGGSYVVAADPAWIGSLGDQAFLEAMLNIAVEAVW... | Function: Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
Catalytic Activity: guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine
Sequence Mass (Da): 43643
Seq... |
O67010 | MEIVQEGIAKIIVPEIPKTVSSDMPVFYNPRMRVNRDLAVLGLEYLCKKLGRPVKVADPLSASGIRAIRFLLETSCVEKAYANDISSKAIEIMKENFKLNNIPEDRYEIHGMEANFFLRKEWGFGFDYVDLDPFGTPVPFIESVALSMKRGGILSLTATDTAPLSGTYPKTCMRRYMARPLRNEFKHEVGIRILIKKVIELAAQYDIAMIPIFAYSHLHYFKLFFVKERGVEKVDKLIEQFGYIQYCFNCMNREVVTDLYKFKEKCPHCGSKFHIGGPLWIGKLWDEEFTNFLYEEAQKREEIEKETKRILKLIKEESQL... | Function: Dimethylates the guanine residues at position 26 and 27 of one or more tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
Catalytic Activity: guanosine(26)/guanosine(27) in tRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(2)-dimethylguanosine(26)/N(2)-dimethylguanosine(27) in tRNA + 4 S-adenosyl-... |
Q9LFU5 | METDLNDYTVIKEGEAEVLMHKKNQVFFNKAQVNNRDMSIAVLRAFIIKRKQEHEAMLSKRARSSGKVVEKDVSETSKEETPTENGDDNGKTNGEHEVTTQDGPKEAAKTAYESARRELKPPRVLEALSASGLRALRYAREVEGIGQVVALDNDPASVEACQRNIKFNGLMSTSKVESHLTDARVHMLSHPKDFDVVDLDPYGAPSIFLDSAVQSVADGGLLMCTATDMAVLCGANGEVCYSKYGSYPLKGKYCHEMALRILLASIESHANRYKRYIVPVLSVQMDFYVRVFVRVYTSASAMKNTPLKLSYVYQCIGCDS... | Function: Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
Catalytic Activity: guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine
Sequence Mass (Da): 65845
Sequence L... |
O29443 | MEVEEGRARVKVEGVFYNPRMRFCRDLDMLVFATMDSKEYFDALSASGIRGIRAALEAGKKAVFNDVSPKAVKVIEENLRENGVSGEVINGDAAAVMRQRAFEHIDIDPFGSPAPFMDSACFSAKRYLSVTATDTAALCGSATNSGLKKYGAFAVKTDVYHEVGLRMLIGFVVREATKYEKALFPLISWVREHYYRVHFKIKKSTAMSAKVYEKMGYLAYCSTCLRKKVLGMGEGAERCECGGKFSLIGPIWLGELKQRDFAEKVAEKAEGKLRAFLEKILAEIDAPTAYSLPALAKIHSLTLPPTDVVVEELKKLGYEA... | Function: Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
Catalytic Activity: guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine
Sequence Mass (Da): 38808
Seq... |
Q23270 | MTENVNSSGDSAIKSEDKEEVTVIQEGQAKVGFHGPVFYNPVQEFNRDLTVTVLRQFSADHQKWAEEQKQLKTEEEPPKKKNKLAINEDGKIRILDALSASGLRALRFSKEVPNVGFIMANDFSDNAVASIQENVKLNGVEDIVEAHFGDAVMTMMEHRGIDKRFHAVDLDPYGTASTFLDSAVQCVADRGILMVTCTDMAVLCGNTPEACYNKYDAVTTRMKCCHEVGLRILLRAIDSAANRYTRYIEPLVSISVDFYVRVFVRVHTGAFQAKQSGTKVGTVLVCSGCHSMEPLVLLKRGEGNQQSKYSIPTVRHSISG... | Function: Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
Catalytic Activity: guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine
Sequence Mass (Da): 58400
Sequence L... |
Q9VK89 | MEVDEEKPQIIAENPNENVIRERNAEIVSGGNVFYNPVQEFNRDLSIAALNVYRQRLTKERSEKALKKQRKKVKEQEDEKTTPVPEDPPVYEAGTRYEDGLRILEALAATGLRSIRYAQEIAGVRQIVANDLSRQAVASINTNIRHNKVEELIEPSHSDAMTLMYLSTQPEKRFDAVDLDPYGCPNRFLDGAMQCLVDGGLLLVTATDMAVLAGNAPEACYVKYGSVPLRMKCCHEMALRILLHCIESHANRYGKYIEPLLSISADFYIRIFVRVYVGQAQCKLSMSKQSWIYQCTGCETFTLQPLGITKPNPTAGNPQQ... | Function: Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
Catalytic Activity: guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine
Sequence Mass (Da): 64957
Sequence L... |
B7FTW3 | MLDPVEASSVPVVDDSTIRSLSDFPDRNVFRREDRYPALNIPVRRTAELRKTLKHVLWRRPKTKNVYDDETDPQRRILVLANIDEDAFRDETVQRLIQHEDCRKASYTVTTAYENYTVEEILKQLLPNESEIPSAFEMVGHLAHVNLRSSQLPFKYWIGKVMLDKNQPRIRTVVNKLGTIETEYRTFGMEVIAGYQGENWSVVTVKEERCTFRLDFTKVYWNSRLAGEHRRLVQQILKESQTKPLVVADLMAGVGPFAVPLTASHGRRNQVTVYANDLNPESYKYLLQNVQSNKCTNIHCYNQCGRAMVHQLQAENIEVD... | Function: Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs an... |
Q4CNL4 | MSGEERHQGKGEKGPMDHDEPPSYRTRVEASVELMALRVKPVHLLGEVLKALRGCLYDMRGVRNVMDAPQPTSDPGEAHKLLLLDPQVIPPPSPAAKNASTAPTQPLWVEANHASVPPVVRERLQSFLLGKRSVAQSLRVAVAQHIVRLSHRNFTMPELLQRILPPGTIPLSGFEQVGHIAHVNLSAAHLPYRADIGAVILDCNPTVRVVVNKVDNIASVFREFKMEVIARRTTHSDMKGSPAEENSGDEEKLHRLLLATVRQHGCIFRVPYDRVYWNSRLSHEHARVVGMMQSGDMLYDAMAGVGPFAIPAAVAGVKTY... | Function: Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs an... |
F6H2F8 | MVTKLFLRPHSLSFTLLSGIHLFPKTSLSKPITLCLLSTTATTPILTLTQTLDPNLSYGPSLHKGTKPLNHQNHQLIAATPGEEECVFDKEAFTRVFNLTAIRVPSKDCFALENRLRGHLLNWPRIRNVARVPGDEVEDGLVKLLGEKRNSSDGSESEGDFDSLNRRIYGKAEGDGEILSPVLYRDTLAKTFDSQGFANFRNLAKLSRPKKKKRRKEEERSEGKKRTGKNEFAMVEVVEDGEEGEDLRGLLGEEFKRKRWRGSTRLLLLDERYADKGVEELPEAIKAVLKEDTGQSMTSTFELVKCKLTLFYNYWQMNEI... | Function: Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs an... |
Q6NQ64 | MVSKLSLFRANSLPFPVISSYSARFILKPYPKPKTLIFCVFSSNLSSTTFPYGPSLLKGKKPVLDDIRLASIGRDRDAHRGKIGEFDESIEKDVLLNEDEFTRVFEISAIRVPAKDCFALENRLRGHLLNWPRIRNIARVPGDEIEEDVVKLLGRETDEEEEDEDSVVDSVNRRIRGKAEGDGERLSSVLHRDKLARTFNSTGYLKFRNLAKISRPKRKRKTERTREGKEKEIASRRNEMAVVEVVETRGGEEDFEGLLGEGYGSRGRWRGSTRLLLLDEKYSGEEVQDLPEAIKVLFAEAKMADASLSFELVKCRLTLF... | Function: Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs an... |
B7G5J1 | MTTRVTGNERRGRQLLLRFSGFLSAALTVMALITATRALAPVVAYIAPQRVRSHFMRRAFASGNCRSRRFSVLRSTVGTETRNENNITTPYHSPLPTSRYVYQSSRTLSSRNPALPLESTLMHSNANELTDVELKNLVAHWRDHPVLNPMVTFRSWVVPIKGKMIQAILNSKSLQPYLASRHELLQEMHVRLKIVRDYTDSTDGTEKLILLHPDTPPLSELPADVQQLLRNCQIHENGPVMPTKFTYKDFTASYILSQLLPIAVHPPPTAFETIGHVAHLNLKERHWPYRFLIGQVLLETLPLIESVINKVGEVSGPYRT... | Function: Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs an... |
F6HH45 | MLLDESKFDLQLKLWALRIPSQLCKVASRILNGYLLDKPRVKPITEDPTCETNRYIILSERIKNPDLSDIPEDKRDELKVLCKIEVVPYSLTLGYSYWSADHVLKQILPDGVEVPSSFETITFSLCHIAHLNITGELLPYKDVIAKVIYDKNYPRIKTVVNKVGTITNEFRVPKFEILVGKDDMVTEVKQYRATFKLDYSLVYWNSRLEHEHMRLVSQFRPGQIICDMFSGVGPFAIPAAQKGCLVYANDLNPDSIRYLKINAKINKVDDNIWAYNMDARKFISQLMEVPVHEILPEPDVPVLKATEECSIQANVQTESQ... | Function: Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs an... |
Q5V3R4 | MKDSPQVTVLRLGHRPGRDERMTTHVGLTARALGADKVVLANAARNQADTVIDITDRFGGPFDVASTEEPKRLIRDFEGRVVHLTMYGEPVQEVEADVREANTAEPLLVVVGAEKVPFEVYEHADWNVGVTNQPHSEVASLAVFLDRLFEGRELDREWENPDRVVVPQETGKRVVDPDEE | Function: Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Catalytic Activity: cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 20120
Sequence Length: 180
Subcellular Location: ... |
Q18HD7 | MKRSCENDVSVLRYGHRPGRDDRMTTHVGLTARALGADQVIFPDNATQSAETVSDIVSRFGGPFDVERTDGLNATIREWSGTVIHLTMYGERVQDVTEVIRETCLHHQPLLIIIGGEKVPSDVYEWADWNIAVTNQPHSEVAGLAVFLDRLFMGQELEQEWAGAEHVVVPQACGKRVVDAELTTEADEMNAEK | Function: Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Catalytic Activity: cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 21458
Sequence Length: 193
Subcellular Location: ... |
A2BLW3 | MSYSHPASRYERVYVLRIGHRPERDKRITTHVGLVARAFGANGFILGDTCDEKVMESLKDVIDRWGGSMELACGVNSRRYVLEWKRAGGEVIHLTMYGLHVDDVIEEIKRSSKPKLIIVGAEKVPPFFYEYADYNVAIGHQPHSEVAALAIFLHKLYEGKELYIDFPRAKLRIVPSARGKKVVSREA | Function: Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Catalytic Activity: cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 21243
Sequence Length: 187
Subcellular Location: ... |
A8ABJ8 | MKVYVLRIGHRPDRDKRITTHVGLVARAFGAHGFVLSPCDEKVLEKLRDVEERWGRLLEEIACTNSPLKYVKTWDGTVVHLTMYGLPVDSVIDEIRQKDKILVIVGAEKVPREYYELAHYNVAIGNQPHSEVAALAIFLDRLYGGAELYRQPVGGKLRIIPTEKGKKVVKVGEEGPSGGAPGVRAERGRGGRGEGVQGADEVRGHKRGATDRDLGDET | Function: Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Catalytic Activity: cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24058
Sequence Length: 218
Subcellular Location: ... |
Q8TL02 | MKRIVLLRLGHRPERDKRITTHVGLTARMLGAEGMLLASDDQGIVHSLEDVVRRWGGDFYIKNNVNFKQEIRAWKEEGGKVCHLSMYGVNLPDVTGELKKCKKLMIVVGAEKVPPEIYQLANWNVAVGSQPHSEVAAVAITMDRIAEGEPLEKEFPGAELTIVPAERGKHVIENIRE | Function: Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Catalytic Activity: cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 19801
Sequence Length: 177
Subcellular Location: ... |
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