ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A8MFY0 | MRKPIIAGNWKMNKVSKEALDLVNQIKDEVHKTEVEVVVCCPFTVLSQVQKALVGTNLKLGAQNMHWEEDGAYTGEISANMLKDIGVEYVILGHSERRQYFNETDETVNKKVKKAIKENLKPIVCIGESLEEREANQTFDVIKKQLLGAFEGVPAEAMDNVVLAYEPIWAIGTGKTASSEEAQTVIAYIRSLIEEKYGVDISEEVRIQYGGSVKASNATEIMNETDIDGALVGGASLKAEEFLGIINF | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 27384
Sequence Length: 248
Pathway: Carbohydrate biosynthes... |
B3ER35 | MQRTIIAANWKMNKNFQEGLQLAKEITQFIQAEPLAGAQIILFPSFIHLEGISKLLTPEVKLHLGAQNCHDQIAGAFTGEVSAAMLASIDVRYVLVGHSERRQNFAEDNDLIAKKIDAILSCKLQPVFCCGEPLSVRESNQHYAFIEQQIAESLFHLTPDELQQVIIAYEPIWAIGTGLIPSLAEIEEMQQTIRNILKKQYNTVLADNMAILYGGSCNASNITKLISLPGINGVLIGGASLHFKEFIHILRSL | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 28021
Sequence Length: 253
Pathway: Carbohydrate biosynthes... |
O66686 | MRRLIAANWKMNKTVKETEEYINTFLKFVEHPESREILICPPFTSLYVAGKMLQGTGVKLGAQNCHYEKRGAFTGEISIPMLQEVGCEYVIVGHSERRHIFGESDELIHKKIVACLEMGIRPILCVGEKKEEREAGMTFKVIETQIKLALTGVEEHTDKIDIAYEPVWAIGTGTPATPEDAVEVHTFIRNLINQLNPKNEGKTRILYGGSVNPQNAKEFMKHEEINGLLVGTASLDPESFAKIVYSF | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 27765
Sequence Length: 247
Pathway: Carbohydrate biosynthes... |
P48491 | MARKFFVGGNWKCNGTAEEVKKIVNTLNEAQVPSQDVVEVVVSPPYVFLPLVKSTLRSDFFVAAQNCWVKKGGAFTGEVSAEMLVNLDIPWVILGHSERRAILNESSEFVGDKVAYALAQGLKVIACVGETLEEREAGSTMDVVAAQTKAIADRVTNWSNVVIAYEPVWAIGTGKVASPAQAQEVHDELRKWLAKNVSADVAATTRIIYGGSVNGGNCKELGGQADVDGFLVGGASLKPEFIDIIKAAEVKKSA | Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 27169
Sequence Length: 254
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
Q9HGY8 | MPRQFFVGGNFKMNGTAESITAIIKNLNEAKLDETTEVVVSPPALYLTLAQQVADEKKKVAVSSQNVFDKPNGAFTGEISVSQLQDAKIPWTIIGHSERRVILKETDEFIARKVKAAIDGGISVIFCIGETLEEREADKTIEVVTKQLNAAAKELTKEQWSKVVIAYEPVWAIGTGKVATTQQAQEVHAAIRKWLADAISPEASENTRIIYGGSVSEKNCRELAQERDVDGFLVGGASLKPAFVDIINARL | Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 27414
Sequence Length: 251
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 5.3.1.1
|
Q2NIS7 | MNYKPRTKVIAGNWKMHKCKDEALEFIQKVSLQVPDQTQVQTLIFPQLTLLDPLVQLQGANLQVGAQNMFYETEGAFTGEVSPQNLLSLGVKHVLLGHSERRTLFGETDQTVNLKLLSALKHKLVPTVCVGESLLTKENNQTQMFLDQQLTNIFAGVPEEALKNMIIAYEPVWAIGTGKSANPQDANKTIEQIREKVTALYSFQASCAIRIIYGGSLSVANIKSILEQPAIDGILAGKASLQTEDFLFFAQIASKQVLVSTKDIFQKNDCPFCY | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 30378
Sequence Length: 274
Pathway: Carbohydrate biosynthes... |
B6YRU5 | MRKNIVVGNWKMNKTLQEGVFLAKELELALKERKVNCDVIICVPFTHLVAIFETINTKIVKLGAQNNADRVSGAYTGEVSAAMIASIGVQYVILGHSERRAYYGETNIILKEKVKMALENNLIPIFCIGEVLKERVAGKQNIVVRKQIEESLFDFSAEDFRKIILAYEPVWAIGTGRTATPVQVQEMHIFIRQILIDNYGQAIANETSILYGGSCNAGNAKELFINPDVDGGLIGGASLKVDTFLSIIEAF | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 27753
Sequence Length: 251
Pathway: Carbohydrate biosynthes... |
A1K5A6 | MTTKLIAGNWKLNGSLAKNAALIDELRRAEMHCVVCVPYPYLAQAQALVAGSLIELGAQDVSEYEQGAYTGEVSAAMLVEFGCRYVIVGHSERRALFGDSDQVVGRKAASALAAGLTPIVCVGETLAERELGEVEAVIRRQLQAVADCVGGEALPTLVVAYEPVWAIGTGRSATPEQVAQTHGFIRAWFSARCDASAVRILYGGSVKPENAAVLFSTDDVDGGLIGGASLVGSDFVAICRAA | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 25360
Sequence Length: 242
Pathway: Carbohydrate biosynthes... |
Q81X76 | MRKPIIAGNWKMNKTLSEAVSFVEEVKGQIPAASAVDAVVCSPALFLERLVAATEGTDLQVGAQNMHFEKNGAFTGEISPVALSDLKVGYVVLGHSERREMFAETDESVNKKTIAAFEHGLTPIVCCGETLEERESGKTFDLVAGQVTKALAGLTEEQVKATVIAYEPIWAIGTGKSSSSADANEVCAHIRKVVAEVVSPAAAEAVRIQYGGSVKPENIKEYMAQSDIDGALVGGASLEPASFLGLLGAVK | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 26438
Sequence Length: 251
Pathway: Carbohydrate biosynthes... |
Q7NLT1 | MRRKVLAGNWKMYKTRGEARAFLEAFVPLISPGAENREVILCGPFTCLDLLSAQAGPYAVGAQNVHWADHGAYTGEIAPQMLVELGVHYVIVGHSERREYFNETDSTVNRRLNNAQDHDLVPILCVGETESVRKDGITEAHIRSQLDRDLELVDMRRLIIAYEPIWAIGTGKTCEANEANRVCAMIRKHVNFEGVPILYGGSVKPENIDELMAQSDIDGVLVGGASLEAKSFARIVNFEV | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 26608
Sequence Length: 240
Pathway: Carbohydrate biosynthes... |
A9HJ86 | MRQMIVGNWKMNGLGAPSRDLVGEIAEGLATIPSPPQVVVCPPFTQLAGIGPLLKGSGIALGAQDCHQAASGAHTGDISAAMLADLGVEYVVLGHSERRRDHGELDETVREKTQTALAAGLTPIVCIGETGDQKASGESRDAIGWQIQGSLPDGFSGVVAYEPVWAIGSGNPAASQDIADMMGFIRAELVRQFGAAGKTIRILYGGSVNGRDAASILPIAEVGGALVGSASLQADTFLPIVRAAVDL | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 25366
Sequence Length: 247
Pathway: Carbohydrate biosynthes... |
Q0BTX8 | MRQLIAGNWKMNGLRSTSESLLQALRDAAPHALRNCDMLICPPATLIAQAASVLAGSGIEVGAQDCHMARSGAHTGDLSAEMLVEAGAHWVILGHSERRRDHGELSETVREKVIAARQFGLTPIVCVGETEDERASGRETEIVGWQIKGSLPDGFAADSNGVIAYEPVWAIGTGRTATVEDVAMMHAFIREELVRQFGEAGRGVRILYGGSVKPENAASLLRVPEVGGALVGGASLSAQDFLAIAEASA | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 26280
Sequence Length: 249
Pathway: Carbohydrate biosynthes... |
P48492 | NWKCNLSKADIAELVSAFNAAPPIDAAHVQVVVAPPAVYLDSTRQALRADFDTSAQNAWISKGGAFTGELDAAMVKDVGAEWVILGHSERRHIAQLKESDHTIAMKAAYALQHASLGVIYCIGELLEERESGQTIAVCERQLQALSDAISDWSDVVIAYEPVWAIGTGKVATPEQAEQVHEAVRAWLANNVSPQVAASTRILYGGSVSPANCESLAKQPNIDGFLVGGASMKPTFLEIVDSYKATLAEAV | Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 26686
Sequence Length: 250
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
Q2SML7 | MRKKLIAGNWKSNGSLERNKALLEGIVNAKALGSVDVVVCPPFPYLQSVESAVSDSMIELGSQNCSATEDGAYTGEVSAKMCADMKCSWVILGHSERRALYAENDEVIACKVKRAVESGLAPILCVGETLADRESGRAEEVTLKQLDAVFMSVQPDDSWVVAYEPVWAIGTGKTASPEDAQSMHKALRNNIRKHFPQIADKIRILYGGSVKSSNAKELFSMPDVDGALVGGASLVSEEFVSIIEAAVE | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 26653
Sequence Length: 248
Pathway: Carbohydrate biosynthes... |
A1WXW9 | MRRKIIAGNWKMNGDQDLVRRVAERAADSAGDAELAVCPPYPLLAAAASQLPFGVALGAQDVSEYDSGAYTGEVSASMLLEAGCRYVIVGHSERRTLYGEDNGRVAGKFVAARNAGLTPILCVGETLAERDAERTESVVGEQLDAVMDAVGGATFQGAVIAYEPVWAIGTGRTATPEQAQAVHAFIRQRVQERDAGEIADQLPILYGGSMKADNAAELLAQPDIDGGLIGGASLDPDSFLSIYNAAAEG | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 26071
Sequence Length: 249
Pathway: Carbohydrate biosynthes... |
Q9HQS4 | MFVLVNLKAYPCDPVAIAEAAADVAETTPATIAVAPQPADIGRVADTGATTYAQHVSPTEHGSHTGSVLAESVADNGAVGTLLNHSEHRRRLADIDGSVAAAERAGLDTVVCANNPAQVAAAAALGPDAVAVEPPALIGTGTPVSQADPDIVSDAVAAAEAVDPSVDVYCGAGITTGEDVVSAGDLGASGVLLASGVAKADDPRAALADLVAPL | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 20928
Sequence Length: 214
Pathway: Carbohydrate biosynthes... |
A3PD39 | MRKSVIAGNWKMHMTCAEAKSYLEEFIPLIKNIKDDRKVVIAPPFTAISTFSDHSDFEYLDISSQNIHWEDQGAFTAEISPKMLLEHGVSYAIVGHSEPRKYFSESDEQINKRAVFAQSSGLTPIVCVGETLEQRERGEADRVITRQVEQGLENTDPSNLIVAYEPIWAIGTGKTCEAEDANKICSLIRKLIGFDDVIIQYGGSVKPNNIDEIMSMSDIDGVLVGGASLDPNSFARIANYQ | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 26779
Sequence Length: 241
Pathway: Carbohydrate biosynthes... |
Q7VC41 | MRKTVIAGNWKMHMTCSSAKEYIDKFIPFSKEFPSDRHVVIAPPFTAISTLASLLQGTNIQLSSQNVHWEDTGAFTAEISPSMLLEHDVRYAIVGHSEPRKYFSESDEQINLRARSAQSNGLIPIVCVGESIEQRERGEAERVIRRQVEQGLEQTDLTKLVIAYEPIWAIGTGKTCESNEANRICGLIREWAGFSDLIIQYGGSVKPANIDEIMSMSDIDGVLVGGASLDPENFARIANYQSI | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 26994
Sequence Length: 243
Pathway: Carbohydrate biosynthes... |
Q7V1N4 | MRKSVIAGNWKMHMTCADTKKYLEEFLPLIEEIPNDRKIVIAPPFTAISTFSNYTNFDYLNIASQNIHWEDKGAFTAEISPNMLIEHKVKYAIVGHSEPRKYFSESDEQINKRAVFAQSSGLTPIVCVGETLEQRERGEADRVITRQVEQGLENTDPSNLIVAYEPIWAIGTGKTCEASDANKICALIRSLIGFSDVIIQYGGSVKPNNIDEIMSMSDIDGVLVGGSSLDPISFSRIANFE | Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Mass (Da): 26828
Sequence Length: 241
Pathway: Carbohydrate biosynthes... |
B9DGU7 | MSAMDVMIHSSSFLLPCDETSTGTRYALVVLNQSLPRFTPLLWEHAKLRLCADGGANRIYDELPLFFPNEDALAIRNRYKPDVIKGDMDSIRRDVLDFYINLGTKVIDESHDQDTTDLDKCILYIRHSTLNQETSGLQILATGALGGRFDHEAGNLNVLYRYPDTRIVLLSDDCLIQLLPKTHRHEIHIQSSLEGPHCGLIPIGTPSAKTTTSGLQWDLSNTEMRFGGLISTSNLVKEEKITVESDSDLLWTISIKKTGLSIQDHTP | Function: Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate (TPP) . TPP is an active cofactor for enzymes involved in glycolysis and energy production . Plant leaves require high levels of TPP for photosynthesis and carbohydrate metabolism .
Catalytic Activity: ATP + thiamine = AMP + H(+) + thiamine d... |
P30636 | MSKKLKPFEILEDSCASVCIWLNGEPTAISNRAENLWNKAKYRVATDGAVNEILKRKSFVEWPHIICGDFDSINKQIDTKNAKVVHLPDQDYTDLSKSVQWCLEQKTLTSWEFENIVVLGGLNGRFDHTMSTLSSLIRFVDSQTPVIVLDSRNLVLAVPTGDSNLDVNLEMTTKMCGIIPIVQKETIVSSIGLKYEMENLALEFGKLISTSNEVTTSQVFLKSSSSLIFSIELENWVYKLDSL | Function: Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. Functions cell non-autonomously.
Catalytic Activity: ATP + thiamine = AMP + H(+) + thiamine diphosphate
Sequence Mass (Da): 27314
Sequence Length: 243
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate fr... |
Q9H3S4 | MEHAFTPLEPLLSTGNLKYCLVILNQPLDNYFRHLWNKALLRACADGGANRLYDITEGERESFLPEFINGDFDSIRPEVREYYATKGCELISTPDQDHTDFTKCLKMLQKKIEEKDLKVDVIVTLGGLAGRFDQIMASVNTLFQATHITPFPIIIIQEESLIYLLQPGKHRLHVDTGMEGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSNTYDGSGVVTVETDHPLLWTMAIKS | Function: Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. Can also catalyze the phosphorylation of pyrithiamine to pyrithiamine pyrophosphate.
Catalytic Activity: ATP + thiamine = AMP + H(+) + thiamine diphosphate
Sequence Mass (Da): 27265
Sequence Length: 243
Pathway: Cofactor biosynthesis; thiami... |
Q9R0M5 | MEHAFTPLEPLLPTGNLKYCLVVLNQPLDARFRHLWKKALLRACADGGANHLYDLTEGERESFLPEFVSGDFDSIRPEVKEYYTKKGCDLISTPDQDHTDFTKCLQVLQRKIEEKELQVDVIVTLGGLGGRFDQIMASVNTLFQATHITPVPIIIIQKDSLIYLLQPGKHRLHVDTGMEGSWCGLIPVGQPCNQVTTTGLKWNLTNDVLGFGTLVSTSNTYDGSGLVTVETDHPLLWTMAIKS | Function: Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. Can also catalyze the phosphorylation of pyrithiamine to pyrithiamine pyrophosphate.
Catalytic Activity: ATP + thiamine = AMP + H(+) + thiamine diphosphate
Sequence Mass (Da): 27068
Sequence Length: 243
Pathway: Cofactor biosynthesis; thiami... |
Q6ZGP8 | MTNQDVVVSEMGIAAGAALPGGPAGPAGGLFACRSAAASMRQTYLDLAAAAVAARSASCTSWADAMRASSPTRSSRSASDVDEFTAWVRKHPSALSKFEEIAAKSRGKKIVMFMDYDGTLSPIVADPDTAYMSDAMRAAVREVAKTFPTAIVSGRCRDKVRNFVGLSDLYYAGSHGMDIKGPSSNPESALCQPASEFLPMIDEVYKTLVEKTKSTPGAKVENNKFCLSVHFRCVDEKRWNALGEQVKAVIKEYPKLKLTQGRKVLEIRPSIEWDKGKALEFLLESLGFANCGDVMPVYIGDDRTDEDAFKVLRKRGQGLG... | Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance (By similarity).
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Mass (Da): 40018
Sequence Length: 367
Pathw... |
Q7XT34 | MKISANFLLNNCARTYTKKKTLKKCKRELVEVVDGLVGVMMTSSNREKPDIESGYDGSSDEDSTENSRAEICPSALCFFDQIVASAQDKKVVLFLDYDGTLSPIVNDPEKAFMSSEMRATVKSVAKHFPTAIVSGRSRDKVFDFVKLTEIYYAGSHGMDILASFADSDSTIEKTKETKLFQPANEFLTMITEVSKSLIEVTKAIKGATVENNKFCVSVHYRNVDKKNWKLVAQVVNNVLKDFPSLKVSTGRKVLEVRPMINWDKGKAVEFLLRSLELDDSETVLPIYIGDDKTDEDAFKVLRERKNGCGILVSQVPKKSE... | Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance (By similarity).
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Mass (Da): 39006
Sequence Length: 349
Pathw... |
Q0DDI1 | MTNQDVVMPDIAAAAAMPGSSGRAPLFACRGAAAVSASSMLGGGGAAYQAAVVAHVAPVPAIRPCASWVVEAMRASSPTRPAAAAVDAEYDAWTQRKHPSALGSFEQVAAAASGKRVVVFLDYDGTLSPIVADPDMAFMSDEMRAAVRDVAEHFPAAIVTGRCVDKVQSFVGLPELYYAGSHGMDIKGPSSNEEEDTKILLQPAREFLPVINKAYKALMEKTKSTPGARVENNKFCLSVHFRCVDEKRWNPLAEQVKAVLRDYPELKLTQGRKVLEIRPSIMWDKGKAVEFLLKSLGFDDDRRDVLPVYIGDDRTDEDAF... | Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance (By similarity).
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Mass (Da): 53443
Sequence Length: 500
Pathw... |
O64896 | MDMKSGHSSPVMTDSPPISNSRLTIRQNRLPYSSAAATAISQNNNLLLTVPRKKTGILDDVKSNGWLDAMKSSSPPPTILNKDNLSNDATDMTYREWMQLKYPSALTSFEKIMSFAKGKRIALFLDYDGTLSPIVEEPDCAYMSSAMRSAVQNVAKYFPTAIISGRSRDKVYEFVNLSELYYAGSHGMDIMSPAGESLNHEHSRTVSVYEQGKDVNLFQPASEFLPMIDKVLCSLIESTKDIKGVKVEDNKFCISVHYRNVEEKNWTLVAQCVDDVIRTYPKLRLTHGRKVLEIRPVIDWDKGKAVTFLLESLGLNNCED... | Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance.
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Mass (Da): 43192
Sequence Length: 385
Pathway: Glycan biosy... |
Q9C9S4 | MTNQNVIVSDRKPILGLKTITVSVSNSPLFSNSFPTYFNFPRRKLLKLLEAADKNNLVVAPKITSMIDSMRDSSPTRLRSSSYDSVSDNDDKTSWIVRFPSALNMFDEIVNAAKGKQIVMFLDYDGTLSPIVEDPDKAFITHEMREVVKDVASNFPTAIVTGRSIEKVRSFVQVNEIYYAGSHGMDIEGPTNENSNGQSNERVLFQPAREFLPMIEKVVNILEEKTKWIPGAMVENNKFCLSVHFRRVDEKRWPALAEVVKSVLIDYPKLKLTQGRKVLEIRPTIKWDKGQALNFLLKSLGYENSDDVVPVYIGDDRTDE... | Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance.
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Mass (Da): 42449
Sequence Length: 374
Pathway: Glycan biosy... |
Q4WLM9 | MPSLENSTQNEARLLLVSNRLPITIKRSEDGKYDFSMSSGGLVSGLSGLSKSTTFQWYGWPGLEVPEEEIPVVKQRLKDEYGAIPVFIDDELADRHYNGFSNSILWPLFHYHPGEITFDESAWEAYKEANRLFAKAVAKEVQDGDLIWVHDYHLMLLPEMLREEIGDSKENVKIGFFLHTPFPSSEIYRILPVRNELLLGVLHCDLIGFHTYDYTRHFLSACSRLLGLATTPNGIEFQGKVIACGAFPIGIDPEKFQEGLKKEKVQKRIAQLEQKFQGVKLMVGVDRLDYIKGVPQKLHALEVFLSDHPEWVGKVVLVQV... | Function: Synthase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process . The disaccharide trehalose serves as a storage carbohydrate that is mobilized during conidial germination . Regulates the level of tr... |
A0A348AUV5 | MASSQVGDMVNGNAEPTRHLAKFPPSLWGDRFTSFTLDKQLWDKYGNEIEVLKEQVRSMVVAGGRKAAEQINLINVLERLGVSYHFEKEIEEQLEQLFAKFEDNEDYDLFTIALHFRIFRQHGYKMSCDVFNKFRDSNGEFKETVSNDVQGMLSLYEATYLKIRGEGFLDEAHAFTIAQLESLVGGPHLSSDLSEQVMHALKQSIHRGFPRLEAKHFISFYEKDASRNETLLRLAKLDFNQLQLSHREELCHIFRWWKELDLISKVPYARDRAVECFFWSTCAYYEPQHSVGRAVLTKIMLLLSVTDDTYDAYGTYDELK... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Terpene synthase that catalyzes the biosynthesis of the terpene valerianol, which is a volatile compound of floral scent.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O = diphosphate + valerianol
Sequence Mass (Da): 64124
Sequence Length: 554
Domain: The Asp-... |
Q5M731 | MNSLGGIRSWPANWRSTTASMTTTESVRKVPQVLTVAGSDSGAGAGIQADLKVCAARGVYCASVITAVTAQNTRGVQSVHLLPPEFISEQLKSVLSDFEFDVVKTGMLPSTEIVEVLLQNLSDFPVRALVVDPVMVSTSGHVLAGSSILSIFRERLLPIADIITPNVKEASALLDGFRIETVAEMRSAAKSLHEMGPRFVLVKGGDLPDSSDSVDVYFDGKEFHELRSPRIATRNTHGTGCTLASCIAAELAKGSSMLSAVKVAKRFVDNALDYSKDIVIGSGMQGPFDHFFGLKKDPQSSRCSIFNPDDLFLYAVTDSR... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Essential for thiamine biosynthesis. Bifunctional enzyme that catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP and condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidin... |
Q9SYM4 | MPGNKYNCSSSHIPLSRTERLLRDRELREKRKSNRARNPNDVAGSSENSENDLRLEGDSSRQYVEQYLEGAAAAMAHDDACERQEVRPYNRQRLLVVANRLPVSAVRRGEDSWSLEISAGGLVSALLGVKEFEARWIGWAGVNVPDEVGQKALSKALAEKRCIPVFLDEEIVHQYYNGYCNNILWPLFHYLGLPQEDRLATTRSFQSQFAAYKKANQMFADVVNEHYEEGDVVWCHDYHLMFLPKCLKEYNSKMKVGWFLHTPFPSSEIHRTLPSRSELLRSVLAADLVGFHTYDYARHFVSACTRILGLEGTPEGVEDQ... | Function: Required for normal embryo development, vegetative growth and transition to flowering. Regulates embryo growth, cell wall deposition, starch and sucrose degradation, but not cell differentiation. Involved in the regulation of glucose sensing and signaling genes during plant development.
Catalytic Activity: D-... |
O88856 | MRLSVRKVLLAAGCALALVLAVQLGQQVLECRAVLGGTRNPRRMRPEQEELVMLGADHVEYRYGKAMPLIFVGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWTKSGREKLRLDEAGVTDEVLDAAMQAFILEVIAKHGEPARVLCNKDPFTLKSSVYLARLFPNSKFLLMVRDGRASVHSMITRKVTIAGFDLSSYRDCLTKWNKAIEVMYAQCMEVGRDKCLPVYYEQLVLHPRRSLKRILDFLGIAWSDTVLHHEDLIGKPGGVSLSKIERSTDQVIKPVNLEALSKWTGHIPRDVVRDMAQIAPMLA... | Function: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate.
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: 3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine 3',5'-bisph... |
O77081 | MRKNRELLLVLFLVVFILFYFITARTADDPYYSNHREKFNGAAADDGDESLPFHQLTSVRSDDGYNRTSPFIFIGGVPRSGTTLMRAMLDAHPEVRCGEETRVIPRILNLRSQWKKSEKEWNRLQQAGVTGEVINNAISSFIMEIMVGHGDRAPRLCNKDPFTMKSAVYLKELFPNAKYLLMIRDGRATVNSIISRKVTITGFDLNDFRQCMTKWNAAIQIMVDQCESVGEKNCLKVYYEQLVLHPEAQMRRITEFLDIPWDDKVLHHEQLIGKDISLSNVERSSDQVVKPVNLDALIKWVGTIPEDVVADMDSVAPMLR... | Function: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate.
Catalytic Activity: 3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein]
Location Topology: Single-pass ... |
Q20351 | MRAILDAHPDVRCGGETMLLPSFLTWQAGWRNDWVNNSGITQEVFDDAVSAFITEIVAKHSELAPRLCNKDPYTALWLPTIRRLYPNAKFILMIRDARAVVHSMIERKVPVAGYNTSDEISMFVQWNQELRKMTFQCNNAPGQCIKVYYERLIQKPAEEILRITNFLDLPFSQQMLRHQDLIGDEVDLNDQEFSASQVKNSINTKALTSWFDCFSEETLRKLDDVAPFLGILGYDTSISKPDYSTFADDDFYQFKNFYS | Function: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate.
Catalytic Activity: 3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein]
Sequence Mass (Da): 29922
Seque... |
Q3EDG5 | MQMNSVWKLSLGLLLLSSVIGSFAELDFGHCETLVKKWADSSSSREEHVNKDKRSLKDLLFFLHVPRTGGRTYFHCFLRKLYDSSEECPRSYDKLHFNPRKEKCKLLATHDDYSLMAKLPRERTSVMTIVRDPIARVLSTYEFSVEVAARFLVHPNLTSASRMSSRIRKSNVISTLDIWPWKYLVPWMREDLFARRDARKLKEVVIIEDDNPYDMEEMLMPLHKYLDAPTAHDIIHNGATFQIAGLTNNSHLSEAHEVRHCVQKFKSLGESVLQVAKRRLDSMLYVGLTEEHRESASLFANVVGSQVLSQVVPSNATAKI... | Function: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides.
Catalytic Activity: 3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 56989
Sequen... |
Q9VYB7 | MRLPYRNKKVTLWVLFGIIVITMFLFKFTELRPTCLFKVDAANELSSQMVRVEKYLTDDNQRVYSYNREMPLIFIGGVPRSGTTLMRAMLDAHPDVRCGQETRVIPRILQLRSHWLKSEKESLRLQEAGITKEVMNSAIAQFCLEIIAKHGEPAPRLCNKDPLTLKMGSYVIELFPNAKFLFMVRDGRATVHSIISRKVTITGFDLSSYRQCMQKWNHAIEVMHEQCRDIGKDRCMMVYYEQLVLHPEEWMRKILKFLDVPWNDAVLHHEEFINKPNGVPLSKVERSSDQVIKPVNLEAMSKWVGQIPGDVVRDMADIAP... | Function: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides (By similarity). Has a role in protein secretion.
Catalytic Activity: 3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein]
Location Topology: Single-pass type II... |
Q6Q3H2 | MSTQVSASSLAQIPQPKNRPVANFHPNIWGDQFITYTPEDKVTRACKEEQIEDLKKEVKRKLTAAAVANPSQLLNFIDAVQRLGVAYHFEQEIEEALQHICNSFHDCNDMDGDLYNIALGFRLLRQQGYTISCDIFNKFTDERGRFKEALISDVRGMLGLYEAAHLRVHGEDILAKALAFTTTHLKAMVESLGYHLAEQVAHALNRPIRKGLERLEARWYISVYQDEAFHDKTLLELAKLDFNLVQSLHKEELSNLARWWKELDFATKLPFARDRLVEGYFWMHGVYFEPQYLRGRRILTKVIAMTSILDDIHDAYGTPE... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of valencene, a major volatile emitted from flowers of grapevine. Can use farnesyl diphosphate as substrate, but not geranyl diphosphate or geranylgeranyl diphosphate. Produces mainly (+)-valencene and (-)-7-epi-alpha-selinene along with ... |
A0A7D0AGU9 | MEGLVNNSGDKDLDEKLLQPFTYILQVPGKQIRAKLAHAFNYWLKIPNDKLNIVGEIIQMLHNSSLLIDDIQDNSILRRGIPVAHSIYGVASTINAANYVIFLAVEKVLRLEHPEATRVCIDQLLELHRGQGIEIYWRDNFQCPSEDEYKLMTIRKTGGLFMLAIRLMQLFSESDADFTKLAGILGLYFQIRDDYCNLCLQEYSENKSFCEDLTEGKFSFPIIHAIRSRPDDRQVIQILRQRTRDVEVKKYCVTLLEKFGSFSHTRETLAQLDREAREEVARLGGNPFLEAILNDLLNWDRTK | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Terpene synthase that is able to convert geraniol diphosphate to geraniol in tea leaves.
Catalytic Activity: (2E)-geranyl diphosphate + H2O = (2E)-geraniol + diphosphate
Sequence Mass (Da): 34983
Sequence Length: 303
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) moti... |
A0A343W969 | MVSIAAKSLPKLSGAVFGQFSRRKQLIQRHWLDTRTDQYYDVLRRIVVPECKNIASDVPEYPERIEKLLYYTNPAFSDAWNFTTELIYRTVADESHQTEENITKMYLIRATMDLLFTMSAVLDDISDRSEFRKGKKGWHMICQGGESTALYDGTQMGLFPLYLLKQYFKNDPGYSRLLETVVMTYIKLTIGQTIDVLGQFKKSPSMAEYKRINYYKAGQFVAAGSELAVIHAGITSQDLIDKTVEIFTIAGQIIQTWDDFNDYYSSSEQNGKLSCDFMNAGTTWVSAKAMEVFTPSQAVKFMECYGSDDQSKMKTVQELY... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Sesquiterpene alcohol synthase that catalyzes the formation of (1S,6S,7R)-sesquipiperitol, a terpene intermediate in murgantiol biosynthesis, a male-released aggregation pheromone.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O = (1S,6S,7R)-sesquipiperitol + ... |
A0A386JV86 | MAARAPVHLRGFIARVALNKKNLHARHKLDTDIDKYYYTLHNVIIPDFMDMVKEIPGYPERIKKCVAHTTPSYFEGWAFSTELIYKTVADKQHQTERNLEKCRIIRALMDMSYAMAGILDDYVDKGEFRRGKKVWASVCEGGQEAAIYDSIAVTYLMSLMVKRHFGTDPGYSKLIELFNMVPGTAAIGNTLDILDRHDTNYYDDTMWKHSVQNKAANTVFPAATAGLIHAGVLCDDLLDRTSEVFGYTGHLFQVWDDFMEHYAVKEQSGKGAPDTKYNAKTWATLTAMAHFNEAQAKEFKACYGSTDPAKRSRVRELYDE... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Sesquiterpene alcohol synthase that catalyzes the formation of the pheromone precursor (Z)-alpha-bisabolene from (2Z,6E)-farnesyl diphosphate.
Catalytic Activity: (2Z,6E)-farnesyl diphosphate = (Z)-alpha-bisabolene + diphosphate
Sequence Mass (Da): 43223
Sequence Len... |
P52177 | MESRVLLRATETVTGVPQLRRPIRAINRQFSTASSSFTAFAKPIGSIGEGGNLISGRQLRPLLLLDSLPEKREILKPVRAASAEGGDSAGETKVGFLGKYPWLVTGILLLMWYFLNVIFNILNKKIYNYFPYPYFVSVIHLFVGVVYCLVSWSVGLPKRAPVNSDILKVLIPVAVCHAIGHVTSNVSFAAVAVSFTHTIKALEPFFNASASQFLLGQPIPITLWLSLAPVVLGVAMASLTELSFNWLGFISAMISNISFTYRSIFSKKAMTDMDSTNVYAYISIIALFVCLPPAIIVEGPQLLKHGFNDAIAKVGMTKFI... | Function: Mediates the export of fixed carbons from the chloroplasts into the cytosol in the form of triose phosphates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44487
Sequence Length: 407
Subcellular Location: Plastid
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O14045 | MYKNMNSHELIEESNNSGTPATKSSSKPTKKIRPRNDLVHYSKALSKVLRHTAKANGLQIREDGYIEVDSILKLPQFRGMGMELLLSIVKGNDKKRFTMEEVEGVLYIRANQGHSIKAVQVPMARIDNASSIPKVVHGTKKELWPVISKQGLSRMKRNHIHCATGLYGDPGVISGIRKSCTLYIYIDSAKAMQDGVEFYRSENGVILTEGVNGLLSSKYFSRVETSDGEVLLDAKASPKNNRSDESDQSDPESIDPFCDNLQALSMHELELLEEKHSNFGYSEGIIKGKMQVAQSGFDDGFKHGSRLGFQMGKTIGTLKA... | Function: Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
Catalytic Activity: 2'-phospho-[ligated tRNA] + NAD(+) = ADP-alpha-D-ribose 1'',2''-cyclic phosphate + mature tRNA + nicotinamide
Sequence Mass (D... |
Q12272 | MRQVLQKDKRDVQLSKALSYLLRHTAVKEKLTIDSNGYTPLKELLSHNRLKTHKCTVDDIHRIVKENDKQRFHIKTLGADEEWICATQGHSIKSIQPSDEVLVPITEASQLPQELIHGTNLQSVIKIIESGAISPMSRNHVHLSPGMLHAKGVISGMRSSSNVYIFIDCHSPLFFQTLKMFRSLNNVYLSSSIPVELIQKVVVKGNLKDEEKLDTLRRILHERNIPLEKI | Function: Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
Catalytic Activity: 2'-phospho-[ligated tRNA] + NAD(+) = ADP-alpha-D-ribose 1'',2''-cyclic phosphate + mature tRNA + nicotinamide
Sequence Mass (D... |
Q9BVS5 | MLMAWCRGPVLLCLRQGLGTNSFLHGLGQEPFEGARSLCCRSSPRDLRDGEREHEAAQRKAPGAESCPSLPLSISDIGTGCLSSLENLRLPTLREESSPRELEDSSGDQGRCGPTHQGSEDPSMLSQAQSATEVEERHVSPSCSTSRERPFQAGELILAETGEGETKFKKLFRLNNFGLLNSNWGAVPFGKIVGKFPGQILRSSFGKQYMLRRPALEDYVVLMKRGTAITFPKDINMILSMMDINPGDTVLEAGSGSGGMSLFLSKAVGSQGRVISFEVRKDHHDLAKKNYKHWRDSWKLSHVEEWPDNVDFIHKDISGA... | Function: Methyltransferase that catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in various tRNAs in mitochondrion, including tRNA(Leu) (deciphering codons UUA or UUG), tRNA(Lys) and tRNA(Ser) (deciphering codons UCA, UCU, UCG or UCC) . Catalyzes the formation of 1-methyladenosine at position 947 o... |
P24082 | MKRILPLILALVAGMAQADSNSDYRAGSDFAHQIKGQGSSSIQGFKPQESIPGYNANPDETKYYGGVTAGGDGGLKNDGTTEWATGETGKTITESFMNKPKDILSPDAPFIQTGRDVVNRADSIVGNTGQQCSAQEISRSEYTNYTCERDLQVEQYCTRTARMELQGSTTWETRTLEYEMSQLPAREVNGQYVVSITSPVTGEIVDAHYSWSRTYLQKSVPMTITVLGTPLSWNAKYSADASFTPVQKTLTAGVAFTSSHPVRVGNTKFKRHTAMKLRLVVRVKKASYTPYVVWSESCPFSKELGKLTKTECTEAGGNRT... | Function: Essential for F plasmid conjugative transfer. May interact with the recipient cell surface to stabilize mating pairs initiated by F-pili. May interact with TraG (Probable). Transfer requires OmpA and lipopolysaccharide (LPS), which are possibly receptors for TraN .
PTM: Has higher gel mobility under non-reduc... |
P0CK38 | MESRFKLKEEYHQSCCAIQVRVPVIKTSSTKRKTELYTTGPFIMRSSSPSQPPSIKAQHRIAKHKAIRRRRIDLNCGCSIFYHIKCADHGFTHRGEHHCASGREFRFYLGGTKSPLFQDHAGGRSSIHTDKDIPHPSQVQSQPQESTGSPQSIPELPSLDDIDSSFWDDIFK | 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... |
Q8XDH7 | MKSPAPSRPQKMALIPACIFLCFAALSVQAEETPVTPQPPDILLGPLFNDVQNAKLFPDQKTFADAVPNSDPLMIRMQQNQSGFDLRHFVNVNFTLPKEGEKYVPPEGQSLREHIDGLWPVLTRSTENTEKWDSLLPLPEPYVVPGGRFREVYYWDSYFTMLGLAESGHWDKVADMVANFAHEIDTYGHIPNGNRSYYLSRSQPPFFALMVELLAQHEGDAALKQYLPQMQKEYAYWMDGVENLQAGQQEKRVVKLQDGTLLNRYWDDRDTPRPESWVEDIATAKSNPNRPATEIYRDLRSAAASGWDFSSRWMDNPQQL... | Function: Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system.
Catalytic Activity: alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose
Sequence Mass (Da): 63272
Se... |
Q4J7W0 | MLGMKPLGFIGNGLTSALVDNGSIVWLTFPRFDSPSVFGKLLDDNAGEFSIRPVEDKFKVSQSYLVPNVLSTTFKSSNGKAEIVDLMPIGEKAIIRKVRTEIPLSFKIIPMFNYGLYRPIIRRKDDGIQFLNPVSRECLSLLSDVPTDEIKPPGTTLYLVYSSDCAYGPLDKGKQLENDLENSFNLTIDYWKDKIRSNDEVWRTSVGVLLGLIYSPSGSSIAAATTSLPEAVGDSRNWDYRFVWVRDSSMISEALLYSGYVVEARRILNFMLALVNFTAKPLLHPLYAVDGSDPPPEIEIPWLSGYMNSRPVRVGNAAAS... | Function: Catalyzes the hydrolysis of alpha,alpha-trehalose into two molecules of D-glucose.
Catalytic Activity: alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose
Sequence Mass (Da): 63575
Sequence Length: 558
Pathway: Glycan degradation; trehalose degradation; D-glucose from alpha,alpha-trehalose: step 1/... |
Q4J9D4 | MNYALLSNGITTALEKEGSIEWFPVPKFDSPSVFTKILDEDKGGYFLITPEKFNKVKQQYVEYSLILRTEFDDGNLILIDFLPLSLPAIIRLYEAKVPFNVEVKPLFNYGLVNAGTETRKDGIIYKNPESKEGLELLINGDYKIISPYRITVNSGKGYLYLLYSRDLRYGLFSQKGFVYSEPYEAYSKLLYYSRKELERARKPSIYENAFYRSLSVILGLIYKPSGGIIASPTTSIPEIVGDERNWDYRYVWVRDSSYAIEALVKANLLTHARRALDFLTNLLDPSSKSFDHPFYSVDGTPPPAEENLDWLSGFMNSKPV... | Function: Catalyzes the hydrolysis of alpha,alpha-trehalose into two molecules of D-glucose.
Catalytic Activity: alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose
Sequence Mass (Da): 66574
Sequence Length: 576
Pathway: Glycan degradation; trehalose degradation; D-glucose from alpha,alpha-trehalose: step 1/... |
A0R0W9 | MVLQQTEPTDGADRKASDGPLTVTAPVPYAAGPTLRNPFPPIADYGFLSDCETTCLISSAGSVEWLCVPRPDSPSVFGAILDRGAGHFRLGPYGVSVPAARRYLPGSLILETTWQTHTGWLIVRDALVMGPWHDIDTRSRTHRRTPMDWDAEHILLRTVRCVSGTVELVMSCEPAFDYHRVSATWEYSGPAYGEAIARASRNPDSHPTLRLTTNLRIGIEGREARARTRLTEGDNVFVALSWSKHPAPQTYEEAADKMWKTSEAWRQWINVGDFPDHPWRAYLQRSALTLKGLTYSPTGALLAAPTTSLPETPQGERNWD... | Cofactor: Shows an absolute requirement for Mg(2+) for activity. Mg(2+) cannot be replaced by Ca(2+), Mn(2+) or Zn(2+).
Function: Catalyzes the hydrolysis of alpha,alpha-trehalose into two molecules of D-glucose. Does not hydrolyze maltose, isomaltose, sucrose, cellobiose, p-nitrophenyl-alpha-D-glucopyranoside, and met... |
Q978S7 | MKKIPHELTHMAFHGLVKYSDITVEGYPKIQYHGFIGNNRTAMLVAMNGYIDWGCLPNFNSNAVFSSILDKNKGGYFAIFPSDTTDVYVDQYYKEMTNVLVTEFVKNGKIILRLTDFMPDSEYGKISFPEVHRFVESFSEPIDITIDFKPTFNYGQDKPIIEKDQHGFIFTTDKESIGISSEFPLRKNSDRIFGNVKMEPRSSSWIIALYGIHHLFRTTDYKSYLRLQETTDYWRKWASSSSYAGAYHSMVMRSALALKVLFYEPTGLMVAAPTASLPEAIGGERNWDYRFTWIRDTAYVIEALSSIGYKYEATEFLYDM... | Function: Catalyzes the hydrolysis of alpha,alpha-trehalose into two molecules of D-glucose.
Catalytic Activity: alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose
Sequence Mass (Da): 71827
Sequence Length: 623
Pathway: Glycan degradation; trehalose degradation; D-glucose from alpha,alpha-trehalose: step 1/... |
Q6QUN5 | MRKAGVWGLLWMLFIEEIQAAAEVFEEKCTLAEGQTLKVSCPTNTNIYSNSQKAWQRLKDNGEVQTLAITEGSSQVRVGKYFLEDIPSEGMLQIQMANLQVEDSGLYRCVILGPSDPIILFHPVRLVVTKNSLGTPASDEYPCQVSVQNPTPLPVTTKLRPRPRPRPKPVTQPIPTSADRLSSPGFTVTPTNVTHVNRAPGISIIIPAACGLLSKTLVFIGLFAVTHRSFAS | Function: Cell surface receptor that plays important roles in innate and adaptive immunity by amplifying inflammatory responses. Upon activation by various ligands such as PGLYRP1, HMGB1 or HSP70, multimerizes and forms a complex with transmembrane adapter TYROBP/DAP12. In turn, initiates a SYK-mediated cascade of tyro... |
Q9NP99 | MRKTRLWGLLWMLFVSELRAATKLTEEKYELKEGQTLDVKCDYTLEKFASSQKAWQIIRDGEMPKTLACTERPSKNSHPVQVGRIILEDYHDHGLLRVRMVNLQVEDSGLYQCVIYQPPKEPHMLFDRIRLVVTKGFSGTPGSNENSTQNVYKIPPTTTKALCPLYTSPRTVTQAPPKSTADVSTPDSEINLTNVTDIIRVPVFNIVILLAGGFLSKSLVFSVLFAVTLRSFVP | Function: Cell surface receptor that plays important roles in innate and adaptive immunity by amplifying inflammatory responses . Upon activation by various ligands such as PGLYRP1, HMGB1 or HSP70, multimerizes and forms a complex with transmembrane adapter TYROBP/DAP12 . In turn, initiates a SYK-mediated cascade of ty... |
Q9JKE2 | MRKAGLWGLLCVFFVSEVKAAIVLEEERYDLVEGQTLTVKCPFNIMKYANSQKAWQRLPDGKEPLTLVVTQRPFTRPSEVHMGKFTLKHDPSEAMLQVQMTDLQVTDSGLYRCVIYHPPNDPVVLFHPVRLVVTKGSSDVFTPVIIPITRLTERPILITTKYSPSDTTTTRSLPKPTAVVSSPGLGVTIINGTDADSVSTSSVTISVICGLLSKSLVFIILFIVTKRTFG | Function: Cell surface receptor that plays important roles in innate and adaptive immunity by amplifying inflammatory responses. Upon activation by various ligands such as PGLYRP1, HMGB1 or HSP70, multimerizes and forms a complex with transmembrane adapter TYROBP/DAP12. In turn, initiates a SYK-mediated cascade of tyro... |
Q6TYI6 | MRSARLGRLLWMLFITEIQAATELPEEKYILAEGETLNVNCPVTVGVYSNSRKAWQKLNRNGKFQTLAITERVSGQVSKVQVGKIFLTDEPSEGMLHVQMTNVQAEDSGLYRCVIYQPPKDPIILFYPVRLVVTNYSSGTPASAETPTQSCSPTTTLPPTTTTNRHRPRPRTVRTVTQFLTDFTTSLSSPGLKVTLTNVTDITRDTEISLILPAVCGLLSKSLVFIVLFVVTRMSFTP | Function: Cell surface receptor that plays important roles in innate and adaptive immunity by amplifying inflammatory responses. Upon activation by various ligands such as PGLYRP1, HMGB1 or HSP70, multimerizes and forms a complex with transmembrane adapter TYROBP/DAP12. In turn, initiates a SYK-mediated cascade of tyro... |
Q9NZC2 | MEPLRLLILLFVTELSGAHNTTVFQGVAGQSLQVSCPYDSMKHWGRRKAWCRQLGEKGPCQRVVSTHNLWLLSFLRRWNGSTAITDDTLGGTLTITLRNLQPHDAGLYQCQSLHGSEADTLRKVLVEVLADPLDHRDAGDLWFPGESESFEDAHVEHSISRSLLEGEIPFPPTSILLLLACIFLIKILAASALWAAAWHGQKPGTHPPSELDCGHDPGYQLQTLPGLRDT | Function: Forms a receptor signaling complex with TYROBP which mediates signaling and cell activation following ligand binding . Acts as a receptor for amyloid-beta protein 42, a cleavage product of the amyloid-beta precursor protein APP, and mediates its uptake and degradation by microglia . Binding to amyloid-beta 42... |
Q99NH8 | MGPLHQFLLLLITALSQALNTTVLQGMAGQSLRVSCTYDALKHWGRRKAWCRQLGEEGPCQRVVSTHGVWLLAFLKKRNGSTVIADDTLAGTVTITLKNLQAGDAGLYQCQSLRGREAEVLQKVLVEVLEDPLDDQDAGDLWVPEESSSFEGAQVEHSTSRNQETSFPPTSILLLLACVLLSKFLAASILWAVARGRQKPGTPVVRGLDCGQDAGHQLQILTGPGGT | Function: Forms a receptor signaling complex with TYROBP which mediates signaling and cell activation following ligand binding . Acts as a receptor for amyloid-beta protein 42, a cleavage product of the amyloid-beta precursor protein APP, and mediates its uptake and degradation by microglia . Binding to amyloid-beta 42... |
Q9JKE1 | MSPLLLWLGLMLCVSGLQAGDEEEHKCFLEGENLTLTCPYNIMLYSLSLKAWQRVRSHGSPETLVLTNTRKADFNVARAGKYLLEDYPTESVVKVTVTGLQRQDVGLYQCVVYLSPDNVIILRQRIRLAWCQGKPVMVIVLTCGFILNKGLVFSVLFVFLCKAGPKVLQPSKTSKVQGVSEKQ | Function: Forms a receptor signaling complex with TYROBP/DAP12 which mediates activation of macrophages as part of the innate immune response.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 20452
Sequence Length: 183
Subcellular Location: Cell membrane
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O75003 | MAPPHQFQSKPSDVIRRRLSSAVSSKRPNIPGYTSLTPMWAGIAGAVVNNNTQFEVAISIHDSVYNTDFASSVVPYSPNEPEAQAGIIEKHVLETLRKFSTEHMCKFLGAGVTVILLREAPNLCTRLWLDMDIVPIVFNIKPFHTDSITRPNVRHRISSTTGSYVPSGAETPTVYYDPAQLQDPNKLSANVQTRLPIPRTVDEQADSAARKCIMYFGPGNNPRLQIGPRNQVAVDAGGKIHLIDDIDEYRKTVGKGTWNSVIKLADELREKKIKIGFFSSTPQGGGVALMRHAIIRFFTALDVDAAWYVPNPSPSVFRTT... | Function: Reversibly catalyzes the synthesis and degradation of trehalose from glucose and alpha-D-glucose 1-phosphate. The equilibrium lies in the direction of trehalose synthesis.
Catalytic Activity: alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate
Sequence Mass (Da): 81582
Sequence L... |
Q9UV63 | MSTPHHQFESKSSTAIRRRLSSSVSSKQRPNIMTTTFASLTPMWAGVAGTLVNNNTQYEIAVTVHDGVYSTDFASVIIPVTPGDTVKNSKDIEAQVLNLIRKFSAEHLCKFLGAGITLALLKECPNLCTRLWLDMDIVPIVFNIKPFHTDSVTRPNIKHRISSTTGSYVPSGSETPTVYVEASHLGDPSHLSPNAAQKLPIPRTLDEQSDSAARKCLMYFGPNNNPRLSIGARNPVTVDAGGKIHLIDDLEEYRMTVGAGTWNAVIKLADELREKKVKIGFFSSTPQGGGVALMRHALIRFLTALDVDVAWYVPNPSPQV... | Function: Reversibly catalyzes the synthesis and degradation of trehalose from glucose and alpha-D-glucose 1-phosphate. The equilibrium lies in the direction of trehalose synthesis.
Catalytic Activity: alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate
Sequence Mass (Da): 83653
Sequence L... |
Q9CID5 | MTEKDWIIQYDKKEVGKRSYGQESLMSLGNGYLGLRGAPLWSTCSDNHYPGLYVAGVFNRTSTEVAGHDVINEDMVNWPNPQLIKVYIDGELVDFEASVEKQATIDFKNALQIERYQVKLAKGNLTLVTTKFVDPINFHDFGFVGEIIADFSCKLRIETFTDGSVLNQNVERYRAFDSKEFEVTKISKGLLVAKTRTSEIELAIASKSFLNGLAFPKIDSENDEILAEAIEIDLQKNQEVQFDKTIVIASSYESKNPVEFVLTELSATSVSKIQENNTNYWEKVWSDADIVIESDHEDLQRMVRMNIFHIRQAAQHGANQ... | Function: Catalyzes the conversion of trehalose 6-phosphate into glucose 1-phosphate and glucose 6-phosphate.
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + phosphate = beta-D-glucose 1-phosphate + D-glucose 6-phosphate
Sequence Mass (Da): 87267
Sequence Length: 769
EC: 2.4.1.216
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Q8GRC3 | MSWSISSNQLNIENLLNEESLFFTGNGYIGVRGNFEEKYYDGASSIRGTYINAFHDITDINYGEKLYAFPETQQKLVNVIDAQTVQIYFGEEEERFSLFEGEVIQYERHLHMDKGFSERVIHWRSPGGKEVKLKFKRLTSFIYKELFIQEITIEPVNFFGKTKVVSTVNGDVSNFVDPSDPRVGSGHAKLLTVSDTVIEGDFVSIETKTKRSNLYAACTSTCRLNIDFQREYVKNEKSVETVLTFELTEKAIMTKINIYTDTLRHGDRPLRTGLDLCQKLSCLTFNDLKEQQKHYLDKFWLYADVEISGDQALQEGIRFN... | Function: Catalyzes the reversible phosphorolytic cleavage of trehalose. Phosphorolysis is specific for trehalose.
Catalytic Activity: alpha,alpha-trehalose + phosphate = beta-D-glucose 1-phosphate + D-glucose
Sequence Mass (Da): 87952
Sequence Length: 765
Pathway: Glycan degradation; trehalose degradation.
EC: 2.4.1.6... |
Q11RM1 | MKDYQILLYYCYTHIADPDAYREEHHLKCLELGLLGRIIIASEGLNGTVSGTEEGCRQYMEYVKADPRFEALEFKIEAHEGHAFQKLYVRVKPEIVHSSLKHVDPTKRTGKHLEPAEFKAMKDRDDVVVLDVRSNYEHQVGRFKNAVTIDMENFRDFPEKIKELDHLKGKKVLTYCTGGIKCEKASAFLLEQGFEDVYQLHGGIIKYGIEQGGEDFEGKCYVFDGRVIADVNKVNPSIISTCYVCGTLSDRMVNCSNPVCNRHEPMCEACGEKMQGACSEECKCHPEKRPYDGTGAYPKELNGYDPYLHVKR | 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): 35553
Sequence Length: 312
EC: 1.14.-.-
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Q9RVC9 | MPEPHPAPQPYTVAALYQFRALPDPAALRAELLALGERLELCGTLIVADEGINGTVAGSAAAIAELHAFLLASGFDRLEYKESQASEKPFKRYKVRLKKEIVTLGVPVAPREQVGTYLDPQAWNDLLADPEVIVVDTRNRYEVKAGTFQGAVDPEIDSFREFPAWVDEHLAGAEGKKIAMFCTGGIRCEKSTSLLLQKGFQDVYHLKGGILKYLEDVPQAQSRWDGECFVFDGRVTVGHGLQEGDAVMCHSCGWPLTAQERAHPQFEEGVSCEHCFDETTDVQKAAFRERQRMYEAGHLT | 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): 33239
Sequence Length: 300
EC: 1.14.-.-
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A9C0A8 | MSDILNISCYKFTPLPDAAALRDTLAERAQALALKGTILLAEEGINFFLAGPAQAVHSFVDQLRADDRFADLAPKESWSDTVPFRKMLVKVKREIIRMDHPTIRPAEGRAPSVSPATLRRWLEQGHDDEGREVVTLDTRNDFEVDAGAFKDTIDWRITKFTEFPPALRAHKAELADKTVVSYCTGGIRCEKAAILMRDEGLEHVYQLEGGILKYFEETDGAFYDGGCFVFDERRAVGADLAITPLAPAEPLEPIQPTSPPGKA | 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): 29146
Sequence Length: 263
EC: 1.14.-.-
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Q31LZ7 | MSLVLINFYRFVALGDCDRWRQWLQDLCTALGLRGTILLAPEGINAGLAGNTEAIAQFLSELQQHPPFANLSFKSATVTDWPFARLKVKVKPEIVSLGCPELNPAERTGTLVAPQDWNQLLQDPEVVLIDVRNRFEIALGSFPRAIDPQTDRFRDFPRFVQEQLLPQPPAKVAMFCTGGIRCEKASAYLLEQGIETVYQLEGGILNYLEAIAPEENHWQGDCFVFDERIAVDRQLQTPQHQLCPACGQPVVATTCSHCQDSVQASSSPK | 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): 29967
Sequence Length: 269
EC: 1.14.-.-
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Q3AX81 | MSRLQVAAFYAFTPLNEQQRASLLSDLPDMAMTNSVLGSILVAHEGVNGTISGPEAGVEALLQSLRTSLALGCEHFERLEVKRSWADQAVFRRFKARAKKEIVTMGVTSVNPRQNVGTYVDPKDWNDLVDDPDTLVIDTRNSYETAIGSFEGSLDPSTESFRDFPAWAEASLRPLMNDQSPKRIAMFCTGGIRCEKASSYLQSNGFGEVLHLRGGILNYLGEIPEQESRWQGECFVFDQRVALNHQLEPGVHSLCHACGLPLSPSDRADPSYIKGVQCIHCIDRFSESDRARFLMRQQQFDQTPT | 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): 33993
Sequence Length: 305
EC: 1.14.-.-
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Q96A61 | MAGYATTPSPMQTLQEEAVCAICLDYFKDPVSISCGHNFCRGCVTQLWSKEDEEDQNEEEDEWEEEEDEEAVGAMDGWDGSIREVLYRGNADEELFQDQDDDELWLGDSGITNWDNVDYMWDEEEEEEEEDQDYYLGGLRPDLRIDVYREEEILEAYDEDEDEELYPDIHPPPSLPLPGQFTCPQCRKSFTRRSFRPNLQLANMVQIIRQMCPTPYRGNRSNDQGMCFKHQEALKLFCEVDKEAICVVCRESRSHKQHSVLPLEEVVQEYQEIKLETTLVGILQIEQESIHSKAYNQ | Function: E3 ubiquitin-protein ligase . Positively regulates the NF-kappa-B signaling pathway .
PTM: Autoubiquitinated . Polyubiquitinated . Undergoes extremely rapid proteolytic degradation by the proteasome .
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine ... |
Q9BRZ2 | MVSHGSSPSLLEALSSDFLACKICLEQLRAPKTLPCLHTYCQDCLAQLADGGRVRCPECRETVPVPPEGVASFKTNFFVNGLLDLVKARACGDLRAGKPACALCPLVGGTSTGGPATARCLDCADDLCQACADGHRCTRQTHTHRVVDLVGYRAGWYDEEARERQAAQCPQHPGEALRFLCQPCSQLLCRECRLDPHLDHPCLPLAEAVRARRPGLEGLLAGVDNNLVELEAARRVEKEALARLREQAARVGTQVEEAAEGVLRALLAQKQEVLGQLRAHVEAAEEAARERLAELEGREQVARAAAAFARRVLSLGREAE... | Function: E3 ubiquitin-protein ligase that plays a key role in innate antiviral immunity by mediating ubiquitination of CGAS and STING1 . In response to pathogen- and host-derived double-stranded DNA (dsDNA), targets STING1 to 'Lys-63'-linked ubiquitination, thereby promoting its homodimerization, a step required for t... |
Q8NG06 | MAWAPPGERLREDARCPVCLDFLQEPVSVDCGHSFCLRCISEFCEKSDGAQGGVYACPQCRGPFRPSGFRPNRQLAGLVESVRRLGLGAGPGARRCARHGEDLSRFCEEDEAALCWVCDAGPEHRTHRTAPLQEAAGSYQVKLQMALELMRKELEDALTQEANVGKKTVIWKEKVEMQRQRFRLEFEKHRGFLAQEEQRQLRRLEAEERATLQRLRESKSRLVQQSKALKELADELQERCQRPALGLLEGVRGVLSRSKAVTRLEAENIPMELKTACCIPGRRELLRKFQVDVKLDPATAHPSLLLTADLRSVQDGEPWR... | Function: E3 ubiquitin ligase induced during late erythropoiesis. Directly binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. May participate in the erythroblast enucleation process through regulation of nucl... |
Q5NCC9 | MATAPGERLQEEARCSVCLDFLQEPISVDCGHSFCLRCISEFCEKSDSAQGVYACPQCRGPFRPASFRPNRQLASLVDSVRQLGLGTGHAGSRQCARHGEDLSHFCEEDQTMLCWVCDTSPEHRSHRTETLQEAASRYQRMLRASLELVKKEMEEALTQEANVGKKTIIWKEKVEMQRQRFRLEFEKHRGFLAQEEQLQLRRLEEEERATLQRLRDSRNRLAQQNKALKELAEELEERSQRPAPGLLEGARGVLTRCEAITRLEPEAVPMDLKTVCRIPGMREMLRKFQVDVKLDPATAHPSLLLTADLRSVQDAEVWRD... | Function: E3 ubiquitin ligase induced during late erythropoiesis. Directly binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. May participate in the erythroblast enucleation process through regulation of nucl... |
Q5ZMD4 | MHQFEEELTCSICYSLFEDPRVLPCSHTFCRSCLEGVIQLSSNFSIWRPLRVPLKCPNCRSIVEIPASGTESLPINFALKAIIEKYRQEDHSDVATCSEHYRQPLNVYCLLDKKLVCGHCLTIGKHNGHPIDDLHSAYLKEKESSGKILEQLTDKHWSDVCLLIEKLKEQKAQCESIVQDDKKVVVQYFKKLSETLEHKKQVLLAALDEINRQILEEYEPHIEKLKKIREEQLELMSLNTSIQKEESPLVFLEKVDNVHQRIKALKEKELPDVKPVEVYPRVGHLLKDVWSKTEIGQINKILTPKIKLVPKRKLHSKNSE... | Function: May serve as a multifunctional regulator for innate immune signaling pathways.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 46775
Sequence Length: 408
Subcellular Location: Endoplasmic reticulum membrane
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Q8IWR1 | MHNFEEELTCPICYSIFEDPRVLPCSHTFCRNCLENILQASGNFYIWRPLRIPLKCPNCRSITEIAPTGIESLPVNFALRAIIEKYQQEDHPDIVTCPEHYRQPLNVYCLLDKKLVCGHCLTIGQHHGHPIDDLQSAYLKEKDTPQKLLEQLTDTHWTDLTHLIEKLKEQKSHSEKMIQGDKEAVLQYFKELNDTLEQKKKSFLTALCDVGNLINQEYTPQIERMKEIREQQLELMALTISLQEESPLKFLEKVDDVRQHVQILKQRPLPEVQPVEIYPRVSKILKEEWSRTEIGQIKNVLIPKMKISPKRMSCSWPGKD... | Function: E3 ubiquitin ligase involved in different processes such as development and immune response . Serves as a negative regulator for innate immune signaling pathways by suppressing RLR-induced activation of IRF3/7 and NF-kappa-B via interaction with adapter ECSIT . Regulates autophagy through modulating both the ... |
Q9C030 | MTSPVLVDIREEVTCPICLELLTEPLSIDCGHSFCQACITPNGRESVIGQEGERSCPVCQTSYQPGNLRPNRHLANIVRRLREVVLGPGKQLKAVLCADHGEKLQLFCQEDGKVICWLCERSQEHRGHHTFLVEEVAQEYQEKFQESLKKLKNEEQEAEKLTAFIREKKTSWKNQMEPERCRIQTEFNQLRNILDRVEQRELKKLEQEEKKGLRIIEEAENDLVHQTQSLRELISDLERRCQGSTMELLQDVSDVTERSEFWTLRKPEALPTKLRSMFRAPDLKRMLRVCRELTDVQSYWVDVTLNPHTANLNLVLAKNR... | Function: E3 ubiquitin ligase that plays a crucial role in the activation of the IKBKE-dependent branch of the type I interferon signaling pathway . In concert with the ubiquitin-conjugating E2 enzyme UBE2K, synthesizes unanchored 'Lys-48'-linked polyubiquitin chains that promote the oligomerization and autophosphoryla... |
Q9C029 | MAAVGPRTGPGTGAEALALAAELQGEATCSICLELFREPVSVECGHSFCRACIGRCWERPGAGSVGAATRAPPFPLPCPQCREPARPSQLRPNRQLAAVATLLRRFSLPAAAPGEHGSQAAAARAAAARCGQHGEPFKLYCQDDGRAICVVCDRAREHREHAVLPLDEAVQEAKELLESRLRVLKKELEDCEVFRSTEKKESKELLKQMAAEQEKVGAEFQALRAFLVEQEGRLLGRLEELSREVAQKQNENLAQLGVEITQLSKLSSQIQETAQKPDLDFLQEFKSTLSRCSNVPGPKPTTVSSEMKNKVWNVSLKTFV... | Function: E3 ubiquitin-protein ligase that have both tumor-promoting and tumor-suppressing activities and functions in several biological processes including innate immunity, regulation of ferroptosis as well as cell proliferation and migration . Acts as an antiviral effector against multiple viruses by targeting speci... |
Q923T7 | MATVGPRTGPNAGAEALALAAELQGEATCSICLEFFREPVSVECGHSFCRACIMRCWERPGAGTGTATRTLPCPLPCPQCREPARPSQLRPNRQLAAVVSLLRRFSLPPTAPGERGTPAVPARAAAARCSQHGEQLKLYCQDDGRAICVVCDRAREHRSHAVLPLEEAVQEAKELLDSRLRALKKVLEDYEAFRSTEERESKELLKQMAAEKEKVGAEFQALRAFLVEQEGRLLSRLEVLSREVTQKQNENLAQLEGEITQLSKLSGQIQETAQKPDLDFLQEFKSTLSKCSSVPSSKPTTVSSEMKNKVWNVSLKSFVL... | Function: E3 ubiquitin-protein ligase that have both tumor-promoting and tumor-suppressing activities and functions in several biological processes including innate immunity, regulation of ferroptosis as well as cell proliferation and migration. Acts as an antiviral effector against multiple viruses by targeting specif... |
Q9BZR9 | MAENWKNCFEEELICPICLHVFVEPVQLPCKHNFCRGCIGEAWAKDSGLVRCPECNQAYNQKPGLEKNLKLTNIVEKFNALHVEKPPAALHCVFCRRGPPLPAQKVCLRCEAPCCQSHVQTHLQQPSTARGHLLVEADDVRAWSCPQHNAYRLYHCEAEQVAVCQYCCYYSGAHQGHSVCDVEIRRNEIRKMLMKQQDRLEEREQDIEDQLYKLESDKRLVEEKVNQLKEEVRLQYEKLHQLLDEDLRQTVEVLDKAQAKFCSENAAQALHLGERMQEAKKLLGSLQLLFDKTEDVSFMKNTKSVKILMDRTQTCTSSSL... | Function: E3 ubiquitin-protein ligase that participates in multiple biological processes including cell survival, differentiation, apoptosis, and in particular, the innate immune response . Participates in the activation of interferon-gamma signaling by promoting proteasomal degradation of the repressor SOCS1 . Plays a... |
M9MRI4 | MEDELRCPTCKQLYANPVLLPCFHALCLGCALDIQTPYSPGSALPGAVNGAGAASAAGHNGLHGNGGGAGGGAAAPVTNPNGPGTRHSSHSSAASTASSNTGSESVTSDQDQSDKVSIFSEADSGVVCCSNTSRPVSYAGTGLLPGVGNVVAPPGAAYCLTCPLCRKLVFFDDGGVRNLPTYRAMEAIVDRFCAREALRCQMCETDPKVASLICEQCEIRYCDACRELTHPARGPLAKHTLVKPRGAAQQRESVCGEHEETLSQYCLSCKAPACGLCIGELRHQAHDVQSINVTCKAQKTELSHNLQQLSEKARSTTEFI... | Function: E3 ubiquitin-protein ligase activity (By similarity). During embryonic and larval development, regulates the pattern of axonal projections of class IV nociceptive sensory neurons (C4da) downstream of netrin receptor fra . Regulates fine-scale topography of C4da axon terminals upon neuronal activity . During e... |
Q9C026 | MEEMEEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTPESESPQSHRAAGSGVSDYDYLDLDKMSLYSEADSGYGSYGGFASAPTTPCQKSPNGVRVFPPAMPPPATHLSPALAPVPRNSCITCPQCHRSLILDDRGLRGFPKNRVLEGVIDRYQQSKAAALKCQLCEKAPKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPPAQGRVSRRLSPRKVSTCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWKLHKSQLSQALNGLSDRAKEAKEFLVQLRNMVQQIQENSVEFEACLVAQC... | Function: E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions and may also participate in the formation or breakdown of abnormal inclusions in neurodegenerati... |
Q8C7M3 | MEEMEEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTPESESPQSRRASGSGVSDYDYLDLDKMSLYSEADSGYGSYGGFASAPTTPCQKSPNGVRVFPPAMPPPPTHLSPALAPVPRNSCITCPQCHRSLILDDRGLRGFPKNRVLEGVIDRYQQSKAAALKCQLCEKAPKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPPAQGRVSRRLSPRKVSTCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWKLHKSQLSQALNGLSDRAKEAKEFLVQLRTMVQQIQENSVEFEACLVAQC... | Function: E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25... |
Q8N9V2 | MSTADLMENLREELTCFICLDYFSSPVTTECGHSFCLVCLLRSWEEHNTPLSCPECWRTLEGPHFQSNERLGRLASIARQLRSQVLQSEDEQGSYGRMPTTAKALSDDEQGGSAFVAQSHGANRVHLSSEAEEHHREKLQEILNLLRVRRKEAQAVLTHEKERVKLCQEETKTCKQVVVSEYMKMHQFLKEEEQLQLQLLEQEEKENMRKLRNNEIKLTQQIRSLSKMIAQIESSSQSSAFESLEEVRGALERSEPLLLQCPEATTTELSLCRITGMKEMLRKFSTEITLDPATANAYLVLSEDLKSVKYGGSRQQLPDN... | Function: Probable E3 ubiquitin-protein ligase which plays an important role in blastocyst development.
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 Mas... |
Q8BVP1 | MSNHEKMSTTDLMENLREELTCFICLDYFSSPVTTECGHSFCLMCLLKSWEEHNTPLSCPECWRTLGAPHFQANERLGRLANIGRQLRSQVLQSEDEQSICGRMPGPSWVFSDDEQSVINVSPPSQGTNKACFSSEAEEQHKEKLQDIINILRKKKKEVQAILNHEKERVMLCKEETKTCKQVVVSEYMKMHQFLKEEEQLQLQLLEREEKANMKKLRENEIQLTQQIRRLGKMIGRIESTCQNLTLESFEEVKGAMDRYESLLFQSPETTITELSLCHITGMREMLRKFSTDITLDPATANAYLLLSEDLKSVRYGGTR... | Function: Probable E3 ubiquitin-protein ligase which plays an important role in blastocyst development. Involved in progression of blastocyst stage and subsequent embryo development.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating ... |
Q8N7C3 | MSKRLSPQLQHNITEDAYCETHLEPTRLFCDVDQITLCSKCFQSQEHKHHMVCGIQEAAENYRKLFQEILNTSREKLEAAKSILTDEQERMAMIQEEEQNFKKMIESEYSMRLRLLNEECEQNLQRQQECISDLNLRETLLNQAIKLATELEEMFQEMLQRLGRVGRENMEKLKESEARASEQVRSLLKLIVELEKKCGEGTLALLKNAKYSLERSKSLLLEHLEPAHITDLSLCHIRGLSSMFRVLQRHLTLDPETAHPCLALSEDLRTMRLRHGQQDGAGNPERLDFSAMVLAAESFTSGRHYWEVDVEKATRWQVGI... | 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 Mass (Da): 49893
Sequence Length: 437
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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H9JAQ7 | MDITKENYYEELDNIAKNIKDSCFISFDAEFSAILTKESFKYSLFDTNEERYNKYKTQISTMKMMQVGLTMFQYDRELDAYLATGYTFHLCPQLIGTINQSLIFQASTLKFLCKHNFDFNKFIYEGLPYLSKSDEALLNRYRIENNLFDYVSESLEFDEEKQINQCSSEVSKWLSSSIEDTMYLDIDNAICRYLLHLELRQRYPGILTTDSLGNSKKILIYRDKNVEGAKNAPIAILEDNLIAYLLGFLHVIKLLETHKKPIVGHNMFLDMLFLHNQFIGPLPDSYTMFKKNINSVFPTIFDTKYISHAMSKKLTFSESW... | Function: 3'-5' exonuclease that specifically cleaves precursor piRNAs (pre-piRNAs) at their 3' ends . Trims pre-piRNAs to their mature size, a process required for piRNAs maturation and stabilization, and subsequent pre-piRNAs 2'-O-methylation . The piRNA metabolic process mediates the repression of transposable eleme... |
Q973J1 | MTITKRKNTFYTSQFISYMKGYYLHPDIRGNLVAFTSDDDVWLMTLEDMKPIRVTSGQGVAIRPKISPDGKKIAYTIIWLRKGKGGGDIFITGNGETKRITFFGSMNTRVLGWLSDDEILVLTDFHTPFPQWSETYKININDGTMEKIPFGPISNIAISGDIIVIARGYQDLPFWKGYKGGTKGEFLISYDKGNT | Function: Degrades oligopeptides in a sequential manner.
Sequence Mass (Da): 22013
Sequence Length: 195
Subcellular Location: Cytoplasm
EC: 3.4.21.-
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O58214 | MIVVLRLGHRPERDKRVTTHVALTARAFGADGIIIASEEDEKVKESVEDVVKRWGGPFFIEFNRNWRKVMKEFTGVKVHLTMYGLHVDDVIEELKEKLKKGEDFMIIVGAEKVPREVYELADYNVAIGNQPHSEVAALAVLLDRLLEGKGLKKEFKGAKIKIVPQARGKKVVEVQGYAEQDKAEGKATPGKNWENSGFTGDNP | 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): 22767
Sequence Length: 203
Subcellular Location: ... |
Q980M4 | MTTHVILVARAFGAKGVYIEGKDEKMVKSILKVIDSWGGSSYFLVKEIENGKSIVNEWKEKGGTIIHLTMYGININDFQDRFEKIKYPLLIIVGAEKVEGWYYHNADYNIAIGNQPHSEVAALAIFLDRIYKGRELYMEFEDAKIKILPQKAGKKVIRSG | 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): 18185
Sequence Length: 160
Subcellular Location: ... |
Q877H6 | MEVWGGKSYFKVEFVDNPKKIVKSWREKGGLVVHLTMYGKMIDDMIDEITKASKNFTLPLLVVIGSEKVEGWYYYNSDYNIGIGNQPHSEVSALAIFLDRIYKGEELYIHFSDAKFYIIPQLKGKRVVKTDK | 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): 15261
Sequence Length: 132
Subcellular Location: ... |
Q975T9 | MHHRPERDKRVTTHVALVARAFGAKGIFIHGEDMNLLKTIEKVKANWGGKYFSIEFVKNPKKVVRDWRNSGGIVVHLTMYGIPIDNIMEKIINKNTKILVVVGSEKVEGWYYYNSDYNIAIGNQPHSEVAALAIFLDRIYKGGELNIQFSDAKLSIIPQERGKKVRKNE | 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): 19294
Sequence Length: 169
Subcellular Location: ... |
Q9HJN6 | MITVLRINHRPYRDKRITTHVALTARAFGASAILVDERDETLENTIRGVISNFGGSFSIKTGCNWIQEFKHFQGIRVHLTMYGRRINDVIDEIRNSGKDVMVLVGSEKVPIEAYEIADYNVSVTNQPISEVSALAIFLDRYFQGKEFEFEFRGRINVQPAERGKIVKIIPDEIECLDLLKKYGASEQLIEHVKAVEGLALKIAERCNADKRVIVAGSLLHDIGRTRTNGIDHAVAGAEILRSENIHDSVVSAVERHIGAGITREEAARLGLPEKDYVPETLEEMIVAQADNLFAGNKRLRLEEVLNIYRKRGLDSAAERI... | 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): 38120
Sequence Length: 339
Subcellular Location: ... |
Q5JEG5 | MRKMIAVLRLGHRPERDKRITTHVALTARAFGADKIIIAAEEDEHVKESVEDVVNRWGGPFEIEFNPSWKKILREWKDRGIIVHLTMYGIHIDDAIPRIKDELKSGKDLLIVVGAEKVPREVYEMADYNVAVGNQPHSEVAALAVFLDRLLDGAGLRKEFHNAKLKIVPQERGKKVLQLE | 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): 20503
Sequence Length: 180
Subcellular Location: ... |
A1RY31 | MSTGRRVFVLRIGHRPVRDHRVTTHVGLVARAFGADGIFLEESVEESVIRTLRNVVENWGGDFKVLTTRDPRETVANWKKNGGIVVHLTMYGENISEELINLISGQGKDILVVVGGEKVPRWLFEEADFNVAIGNQPHSEVAALAVFLDRLFKGEELRREFPGAKLSIIPSKRGKIVVRRE | 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): 20308
Sequence Length: 181
Subcellular Location: ... |
Q58293 | MPLCLKINKKHGEQTRRILIENNLLNKDYKITSEGNYLYLPIKDVDEDILKSILNIEFELVDKELEEKKIIKKPSFREIISKKYRKEIDEGLISLSYDVVGDLVILQISDEVDEKIRKEIGELAYKLIPCKGVFRRKSEVKGEFRVRELEHLAGENRTLTIHKENGYRLWVDIAKVYFSPRLGGERARIMKKVSLNDVVVDMFAGVGPFSIACKNAKKIYAIDINPHAIELLKKNIKLNKLEHKIIPILSDVREVDVKGNRVIMNLPKFAHKFIDKALDIVEEGGVIHYYTIGKDFDKAIKLFEKKCDCEVLEKRIVKSY... | Function: Specifically methylates the N1 position of guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39000
Sequence Length: 336
Subcellular Location: Cytoplasm
EC: 2.1.1.228
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Q9V0Q0 | MTLAVKVPLKEGEIVRRRLIELGALDNTYKIKREGNFLLIPVKFPVKGFEVVEAELEQVSRRPNSYREIVNVPQELRRFLPTSFDIIGNIAIIEIPEELKGYAKEIGRAIVEVHKNVKAVYMKGSKIEGEYRTRELIHIAGENITETIHRENGIRLKLDVAKVYFSPRLATERMRVFKMAQEGEVVFDMFAGVGPFSILLAKKAELVFACDINPWAIKYLEENIKLNKVNNVVPILGDSREIEVKADRIIMNLPKYAHEFLEHAISCINDGGVIHYYGFGPEGDPYGWHLERIRELANKFGVKVEVLGKRVIRNYAPRQY... | Function: Specifically methylates the N1 position of guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 37852
Sequence Length: 330
Subcellular Location: Cytoplasm
EC: 2.1.1.228
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Q16VC0 | MLFRRFLNLTTKTPHLQTFRARHYFRNMSCPELIPPPTVRGMTVLDKGAFDKRISAPRLIVPRQLNFQQICSSVKKLLLKMECFKPVVSGEYKITLHPSAVKTWEDLKEIGLEDKGLTEENLVWEQMKLGYDNWRYDEILKAVLPEDKEALSAFSKVGHIVHLNLKEHLLPYKNLIGTVIKDKVVGCRAVVNKLVTIDNTYRNFQMELLCGEEDYQVSLKENGCIFEFDFSKVYWNSRLSTEHGRVVEMLKKGDVLLDVYAGVGPFSIPAAKKGYSVLANDLNPDSYKALVHNCAKNKVQGRITCFNKNGIDFIKEEIKQ... | 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... |
E3WPP8 | MCADLLPPATVRGMEQLDRDAFAKTVRVPHLIIPEATNLNSAARALKQYLLKMEHYKPIRSEERKITLHPIPVKQWEDLPVEPLKELGIEKDCLVWEEIKLSYENYKYDLILKAVLPENQEGLSAFSKIGHIIHLNLKNHLMPYRRLIGEVLMDKVADCRTVVNKSNSIQNTYRNFEMELICGVPEYEVSIKENGCTYKFNFSRVYWNPRLSTEHQKITDMLEEGDLLYDLYAGVGPFTVPAAKRGCTVIANDLNPDSYSALVINCGLNKVMRNVKCYNMDAVDFIKVELRNDLLAKLADDKFQGNIHITMNLPAMAVEH... | 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... |
Q7Q5Z3 | MIITTKALTVLPHSGLRTTHRSLLARLRHYFKNMLCPDLHPPATVRGMKLLDRSAFSKTIKVPHLLVPKDKNLNDICRASKKYLLKMERYKPVITEQYKITLHPLAVQKWEDLADLNLEKLDIGSEALVWEEIQLKYENWKYDEIFKAVLPADKEALSSFSKIGHIIHLNLKDHLLPYKELIGQVICDKIADCRTVVNKSLSIDNTYRNFQMELLCGEPDYRVSVKENACLFEFDFSKVYWNPRLSTEHEKIVKMLAKTDTLFDLYAGVGPFTVPAARRGCKVLANDLNPDSYEALVNNCALNKVSKHVTCHNKDAVDFI... | 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... |
Q4WX30 | MDSMTDSSNSLRSSDLPEMFRPPVNRAMRVLDRSFFRKTVPLSAAAVFQNSDISKVRAELHKSRDLLAVPRLNCIRDVADQEGQIKKALLLRETVKHDDKETWSPKISELVEKGRIAMRPYDLTLDYDFWTYADIISSILPEDELQEIPQGFTQVGHVLHLNLREQYLPYKYLIAEILKDKNKVIRTVINKTEDVGSHSEFRTFPFELLAGDNDLNVVQHEQDCEFRFDYSRVYWNSRLETEHRRLVEKFNKGEMVCDVMAGVGPFAVPAGKKKIFVWANDLNPHGYEVMQDAIKRNKVEGFVTPFNMDGREFIRWSAKE... | 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... |
F4NUJ6 | MKYIFAPPANKGLQQLNHALFESSHTLPALKIPAHASGIAMETLRSHILVAPRLRTIVDDPTDKKWRLLLLDPSMEASEINDLPNPLKEFALKHEAKLVKHTIELKYDYWTSDQVLRSILPDEMETPGAFETVGHIAHLNLRDRYQPFKHIIGQVILDKSSHIKTVVNKLDNIDHTFRFFQMEILAGINDMNAKLKEGGCFFHFDFSKVYWNSRLQGEHDRIIKLFGQNDLICDVFAGVGPFALPAAKHKRCVVFANDLNPQSFKYLMENIKLNKLETRILPFNMDGRQFIKQSLEDLNNPAIWNKITKQKPTSNDKKRN... | 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... |
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