ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
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
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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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
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 biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 5.3.1.1
|
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 diphosphate
Sequence Mass (Da): 29879
Sequence Length: 267
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.6.2
|
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 from thiamine: step 1/1.
EC: 2.7.6.2
|
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; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine: step 1/1.
EC: 2.7.6.2
|
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; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine: step 1/1.
EC: 2.7.6.2
|
Q6ZGP8 | MTNQDVVVSEMGIAAGAALPGGPAGPAGGLFACRSAAASMRQTYLDLAAAAVAARSASCTSWADAMRASSPTRSSRSASDVDEFTAWVRKHPSALSKFEEIAAKSRGKKIVMFMDYDGTLSPIVADPDTAYMSDAMRAAVREVAKTFPTAIVSGRCRDKVRNFVGLSDLYYAGSHGMDIKGPSSNPESALCQPASEFLPMIDEVYKTLVEKTKSTPGAKVENNKFCLSVHFRCVDEKRWNALGEQVKAVIKEYPKLKLTQGRKVLEIRPSIEWDKGKALEFLLESLGFANCGDVMPVYIGDDRTDEDAFKVLRKRGQGLGILVSKCPKDTNASYSLQDPTEVMEFLLRLVEWKRKSSSSSLMIRPRV | 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
Pathway: Glycan biosynthesis; trehalose biosynthesis.
EC: 3.1.3.12
|
Q7XT34 | MKISANFLLNNCARTYTKKKTLKKCKRELVEVVDGLVGVMMTSSNREKPDIESGYDGSSDEDSTENSRAEICPSALCFFDQIVASAQDKKVVLFLDYDGTLSPIVNDPEKAFMSSEMRATVKSVAKHFPTAIVSGRSRDKVFDFVKLTEIYYAGSHGMDILASFADSDSTIEKTKETKLFQPANEFLTMITEVSKSLIEVTKAIKGATVENNKFCVSVHYRNVDKKNWKLVAQVVNNVLKDFPSLKVSTGRKVLEVRPMINWDKGKAVEFLLRSLELDDSETVLPIYIGDDKTDEDAFKVLRERKNGCGILVSQVPKKSEAFFMLRGPSEVVILPVMLNFFAALLIMPS | 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
Pathway: Glycan biosynthesis; trehalose biosynthesis.
EC: 3.1.3.12
|
Q0DDI1 | MTNQDVVMPDIAAAAAMPGSSGRAPLFACRGAAAVSASSMLGGGGAAYQAAVVAHVAPVPAIRPCASWVVEAMRASSPTRPAAAAVDAEYDAWTQRKHPSALGSFEQVAAAASGKRVVVFLDYDGTLSPIVADPDMAFMSDEMRAAVRDVAEHFPAAIVTGRCVDKVQSFVGLPELYYAGSHGMDIKGPSSNEEEDTKILLQPAREFLPVINKAYKALMEKTKSTPGARVENNKFCLSVHFRCVDEKRWNPLAEQVKAVLRDYPELKLTQGRKVLEIRPSIMWDKGKAVEFLLKSLGFDDDRRDVLPVYIGDDRTDEDAFKVLRKRGQGLGILVSKCAKETDASYSLQDPAEKYTNAGAHVFVTMLLTVVFTAAVALALVNAVNSHDFAAHLAGVDCRMGLAGPVRCPASGFVELLVLALHVVRCVLAILDRLHACLMSPSLQLSIASPCHGVPCSIGAVEASAIIVSDAPEGLISTLTTDHIYYMTVFPAKLALTSEEV | 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
Pathway: Glycan biosynthesis; trehalose biosynthesis.
EC: 3.1.3.12
|
O64896 | MDMKSGHSSPVMTDSPPISNSRLTIRQNRLPYSSAAATAISQNNNLLLTVPRKKTGILDDVKSNGWLDAMKSSSPPPTILNKDNLSNDATDMTYREWMQLKYPSALTSFEKIMSFAKGKRIALFLDYDGTLSPIVEEPDCAYMSSAMRSAVQNVAKYFPTAIISGRSRDKVYEFVNLSELYYAGSHGMDIMSPAGESLNHEHSRTVSVYEQGKDVNLFQPASEFLPMIDKVLCSLIESTKDIKGVKVEDNKFCISVHYRNVEEKNWTLVAQCVDDVIRTYPKLRLTHGRKVLEIRPVIDWDKGKAVTFLLESLGLNNCEDVLPIYVGDDRTDEDAFKVLRDGPNHGYGILVSAVPKDSNAFYSLRDPSEVMEFLKSLVTWKRSMG | 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 biosynthesis; trehalose biosynthesis.
EC: 3.1.3.12
|
Q9C9S4 | MTNQNVIVSDRKPILGLKTITVSVSNSPLFSNSFPTYFNFPRRKLLKLLEAADKNNLVVAPKITSMIDSMRDSSPTRLRSSSYDSVSDNDDKTSWIVRFPSALNMFDEIVNAAKGKQIVMFLDYDGTLSPIVEDPDKAFITHEMREVVKDVASNFPTAIVTGRSIEKVRSFVQVNEIYYAGSHGMDIEGPTNENSNGQSNERVLFQPAREFLPMIEKVVNILEEKTKWIPGAMVENNKFCLSVHFRRVDEKRWPALAEVVKSVLIDYPKLKLTQGRKVLEIRPTIKWDKGQALNFLLKSLGYENSDDVVPVYIGDDRTDEDAFKVLRERGQGFGILVSKVPKDTNASYSLQDPSQVNKFLERLVEWKRKTVGEE | 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 biosynthesis; trehalose biosynthesis.
EC: 3.1.3.12
|
Q4WLM9 | MPSLENSTQNEARLLLVSNRLPITIKRSEDGKYDFSMSSGGLVSGLSGLSKSTTFQWYGWPGLEVPEEEIPVVKQRLKDEYGAIPVFIDDELADRHYNGFSNSILWPLFHYHPGEITFDESAWEAYKEANRLFAKAVAKEVQDGDLIWVHDYHLMLLPEMLREEIGDSKENVKIGFFLHTPFPSSEIYRILPVRNELLLGVLHCDLIGFHTYDYTRHFLSACSRLLGLATTPNGIEFQGKVIACGAFPIGIDPEKFQEGLKKEKVQKRIAQLEQKFQGVKLMVGVDRLDYIKGVPQKLHALEVFLSDHPEWVGKVVLVQVAVPSRQDVEEYQNLRAVVNELVGRINGKFGTVEFMPIHFLHKSVNFDELIALYAVSDACIVSSTRDGMNLVAYEYIASQQKRHGVLVLSEFAGAAQSLNGSIIINPWNTEELAGAYQEAVTMSDEQRALNFSKLDKYVNKYTSAFWGQSFVTELNRISAHSAGKFQSRKAKLPESADAEKPMNGSGESEESQTTQ | 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 trehalose as a protectant for cell integrity during thermal and oxidative stress .
Catalytic Activity: D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + H(+) + UDP
Sequence Mass (Da): 57919
Sequence Length: 515
Pathway: Carbohydrate biosynthesis.
EC: 2.4.1.15
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A0A348AUV5 | MASSQVGDMVNGNAEPTRHLAKFPPSLWGDRFTSFTLDKQLWDKYGNEIEVLKEQVRSMVVAGGRKAAEQINLINVLERLGVSYHFEKEIEEQLEQLFAKFEDNEDYDLFTIALHFRIFRQHGYKMSCDVFNKFRDSNGEFKETVSNDVQGMLSLYEATYLKIRGEGFLDEAHAFTIAQLESLVGGPHLSSDLSEQVMHALKQSIHRGFPRLEAKHFISFYEKDASRNETLLRLAKLDFNQLQLSHREELCHIFRWWKELDLISKVPYARDRAVECFFWSTCAYYEPQHSVGRAVLTKIMLLLSVTDDTYDAYGTYDELKLYTNAVQRWDVSAMDELPDYMKALYRALLNVYDEVERDLAKQGRDYGVHHSKEAFKEIVRSYEIEAEWFKEGYVASFEEYMKNALVTSTGRLHTTSCFMGLEADVATTEAFEWILTKPKMVAASGAIGRLVDDVMSHDEEQERGHVATGLDCYMKQRGVSKQEAIVELYKMIENAWRDINEEMLKPTAISMKLLIRVLNLSRISDVVYKYVDGYTHPEIIKDHVISLFEDPIPM | 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-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 4.2.3.204
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Q5M731 | MNSLGGIRSWPANWRSTTASMTTTESVRKVPQVLTVAGSDSGAGAGIQADLKVCAARGVYCASVITAVTAQNTRGVQSVHLLPPEFISEQLKSVLSDFEFDVVKTGMLPSTEIVEVLLQNLSDFPVRALVVDPVMVSTSGHVLAGSSILSIFRERLLPIADIITPNVKEASALLDGFRIETVAEMRSAAKSLHEMGPRFVLVKGGDLPDSSDSVDVYFDGKEFHELRSPRIATRNTHGTGCTLASCIAAELAKGSSMLSAVKVAKRFVDNALDYSKDIVIGSGMQGPFDHFFGLKKDPQSSRCSIFNPDDLFLYAVTDSRMNKKWNRSIVDALKAAIEGGATIIQLREKEAETREFLEEAKACIDICRSHGVSLLINDRIDIALACDADGVHVGQSDMPVDLVRSLLGPDKIIGVSCKTPEQAHQAWKDGADYIGSGGVFPTNTKANNRTIGLDGLKEVCEASKLPVVAIGGIGISNAGSVMQIDAPNLKGVAVVSALFDQDCVLTQAKKLHKTLKESKRGI | 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 pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Catalytic Activity: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Mass (Da): 55813
Sequence Length: 522
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Subcellular Location: Plastid
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Q9SYM4 | MPGNKYNCSSSHIPLSRTERLLRDRELREKRKSNRARNPNDVAGSSENSENDLRLEGDSSRQYVEQYLEGAAAAMAHDDACERQEVRPYNRQRLLVVANRLPVSAVRRGEDSWSLEISAGGLVSALLGVKEFEARWIGWAGVNVPDEVGQKALSKALAEKRCIPVFLDEEIVHQYYNGYCNNILWPLFHYLGLPQEDRLATTRSFQSQFAAYKKANQMFADVVNEHYEEGDVVWCHDYHLMFLPKCLKEYNSKMKVGWFLHTPFPSSEIHRTLPSRSELLRSVLAADLVGFHTYDYARHFVSACTRILGLEGTPEGVEDQGRLTRVAAFPIGIDSDRFIRALEVPEVIQHMKELKERFAGRKVMLGVDRLDMIKGIPQKILAFEKFLEENANWRDKVVLLQIAVPTRTDVPEYQKLTSQVHEIVGRINGRFGTLTAVPIHHLDRSLDFHALCALYAVTDVALVTSLRDGMNLVSYEFVACQEAKKGVLILSEFAGAAQSLGAGAILVNPWNITEVAASIGQALNMTAEEREKRHRHNFHHVKTHTAQEWAETFVSELNDTVIEAQLRISKVPPELPQHDAIQRYSKSNNRLLILGFNATLTEPVDNQGRRGDQIKEMDLNLHPELKGPLKALCSDPSTTIVVLSGSSRSVLDKNFGEYDMWLAAENGMFLRLTNGEWMTTMPEHLNMEWVDSVKHVFKYFTERTPRSHFETRDTSLIWNYKYADIEFGRLQARDLLQHLWTGPISNASVDVVQGSRSVEVRAVGVTKGAAIDRILGEIVHSKSMTTPIDYVLCIGHFLGKDEDVYTFFEPELPSDMPAIARSRPSSDSGAKSSSGDRRPPSKSTHNNNKSGSKSSSSSNSNNNNKSSQRSLQSERKSGSNHSLGNSRRPSPEKISWNVLDLKGENYFSCAVGRTRTNARYLLGSPDDVVCFLEKLADTTSSP | 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-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + H(+) + UDP
Sequence Mass (Da): 105976
Sequence Length: 942
Domain: The N-terminal part (1-88) has an inhibitory function on the enzymatic activity.
Subcellular Location: Vacuole
EC: 2.4.1.15
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O88856 | MRLSVRKVLLAAGCALALVLAVQLGQQVLECRAVLGGTRNPRRMRPEQEELVMLGADHVEYRYGKAMPLIFVGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWTKSGREKLRLDEAGVTDEVLDAAMQAFILEVIAKHGEPARVLCNKDPFTLKSSVYLARLFPNSKFLLMVRDGRASVHSMITRKVTIAGFDLSSYRDCLTKWNKAIEVMYAQCMEVGRDKCLPVYYEQLVLHPRRSLKRILDFLGIAWSDTVLHHEDLIGKPGGVSLSKIERSTDQVIKPVNLEALSKWTGHIPRDVVRDMAQIAPMLARLGYDPYANPPNYGNPDPIVINNTHRVLKGDYKTPANLKGYFQVNQNSTSPHLGSS | 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'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein]
Sequence Mass (Da): 42067
Sequence Length: 376
Subcellular Location: Golgi apparatus membrane
EC: 2.8.2.20
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O77081 | MRKNRELLLVLFLVVFILFYFITARTADDPYYSNHREKFNGAAADDGDESLPFHQLTSVRSDDGYNRTSPFIFIGGVPRSGTTLMRAMLDAHPEVRCGEETRVIPRILNLRSQWKKSEKEWNRLQQAGVTGEVINNAISSFIMEIMVGHGDRAPRLCNKDPFTMKSAVYLKELFPNAKYLLMIRDGRATVNSIISRKVTITGFDLNDFRQCMTKWNAAIQIMVDQCESVGEKNCLKVYYEQLVLHPEAQMRRITEFLDIPWDDKVLHHEQLIGKDISLSNVERSSDQVVKPVNLDALIKWVGTIPEDVVADMDSVAPMLRRLGYDPNANPPNYGKPDELVAKKTEDVHKNGAEWYKKAVQVVNDPGRVDKPIVDNEVSKL | 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 type II membrane protein
Sequence Mass (Da): 43314
Sequence Length: 380
Subcellular Location: Golgi apparatus membrane
EC: 2.8.2.20
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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
Sequence Length: 259
EC: 2.8.2.20
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Q3EDG5 | MQMNSVWKLSLGLLLLSSVIGSFAELDFGHCETLVKKWADSSSSREEHVNKDKRSLKDLLFFLHVPRTGGRTYFHCFLRKLYDSSEECPRSYDKLHFNPRKEKCKLLATHDDYSLMAKLPRERTSVMTIVRDPIARVLSTYEFSVEVAARFLVHPNLTSASRMSSRIRKSNVISTLDIWPWKYLVPWMREDLFARRDARKLKEVVIIEDDNPYDMEEMLMPLHKYLDAPTAHDIIHNGATFQIAGLTNNSHLSEAHEVRHCVQKFKSLGESVLQVAKRRLDSMLYVGLTEEHRESASLFANVVGSQVLSQVVPSNATAKIKALKSEASVTISETGSDKSNIQNGTSEVTLNKAEAKSGNMTVKTLMEVYEGCITHLRKSQGTRRVNSLKRITPANFTRGTRTRVPKEVIQQIKSLNNLDVELYKYAKVIFAKEHELVSNKLISSSKRSIVDLPSELKSVLGEMGEEKLWKFVPVALMLLLIVLFFLFVNAKRRRTSKVKI | 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
Sequence Length: 500
Subcellular Location: Golgi apparatus membrane
EC: 2.8.2.20
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Q9VYB7 | MRLPYRNKKVTLWVLFGIIVITMFLFKFTELRPTCLFKVDAANELSSQMVRVEKYLTDDNQRVYSYNREMPLIFIGGVPRSGTTLMRAMLDAHPDVRCGQETRVIPRILQLRSHWLKSEKESLRLQEAGITKEVMNSAIAQFCLEIIAKHGEPAPRLCNKDPLTLKMGSYVIELFPNAKFLFMVRDGRATVHSIISRKVTITGFDLSSYRQCMQKWNHAIEVMHEQCRDIGKDRCMMVYYEQLVLHPEEWMRKILKFLDVPWNDAVLHHEEFINKPNGVPLSKVERSSDQVIKPVNLEAMSKWVGQIPGDVVRDMADIAPMLSVLGYDPYANPPDYGKPDAWVQDNTSKLKANRMLWESKAKQVLQMSSSEDDNTNTIINNSNNKDNNNNQYTINKIIPEQHSRQRQHVQQQHLQQQQQQHLQQQQHQRQQQQQQREEESESEREAEPDREQQLLHQKPKDVITIKQLPLAGSNNNNINNNINNNNNNNNIMEDPMADT | 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 membrane protein
Sequence Mass (Da): 58050
Sequence Length: 499
Subcellular Location: Golgi apparatus membrane
EC: 2.8.2.20
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Q6Q3H2 | MSTQVSASSLAQIPQPKNRPVANFHPNIWGDQFITYTPEDKVTRACKEEQIEDLKKEVKRKLTAAAVANPSQLLNFIDAVQRLGVAYHFEQEIEEALQHICNSFHDCNDMDGDLYNIALGFRLLRQQGYTISCDIFNKFTDERGRFKEALISDVRGMLGLYEAAHLRVHGEDILAKALAFTTTHLKAMVESLGYHLAEQVAHALNRPIRKGLERLEARWYISVYQDEAFHDKTLLELAKLDFNLVQSLHKEELSNLARWWKELDFATKLPFARDRLVEGYFWMHGVYFEPQYLRGRRILTKVIAMTSILDDIHDAYGTPEELKLFIEAIERWDINSINQLPEYMKLCYVALLDVYKEIEEEMEKEGNQYRVHYAKEVMKNQVRAYFAEAKWLHEEHVPAFEEYMRVALASSGYCLLATTSFVGMGEIATKEAFDWVTSDPKIMSSSNFITRLMDDIKSHKFEQKRGHVTSAVECYMKQYGVSEEQVYSEFQKQIENAWLDINQECLKPTAVSMPLLARLLNFTRTMDVIYKEQDSYTHVGKVMRDNIASVFINAVI | 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 five minor products.
Catalytic Activity: (2E,6E)-farnesyl diphosphate = (+)-valencene + diphosphate
Sequence Mass (Da): 64432
Sequence Length: 556
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.2.3.73
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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) motif is important for the catalytic activity, presumably through binding to Mg(2+).
EC: 3.1.7.11
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A0A343W969 | MVSIAAKSLPKLSGAVFGQFSRRKQLIQRHWLDTRTDQYYDVLRRIVVPECKNIASDVPEYPERIEKLLYYTNPAFSDAWNFTTELIYRTVADESHQTEENITKMYLIRATMDLLFTMSAVLDDISDRSEFRKGKKGWHMICQGGESTALYDGTQMGLFPLYLLKQYFKNDPGYSRLLETVVMTYIKLTIGQTIDVLGQFKKSPSMAEYKRINYYKAGQFVAAGSELAVIHAGITSQDLIDKTVEIFTIAGQIIQTWDDFNDYYSSSEQNGKLSCDFMNAGTTWVSAKAMEVFTPSQAVKFMECYGSDDQSKMKTVQELYDEIDMPKLYTEYVLENYNRCETLIKELPHDRLREACSSYMEWLVVRETPDEDSEHKVALCLNISG | 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 + diphosphate
Sequence Mass (Da): 44303
Sequence Length: 385
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Pheromone biosynthesis.
EC: 2.5.1.-
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A0A386JV86 | MAARAPVHLRGFIARVALNKKNLHARHKLDTDIDKYYYTLHNVIIPDFMDMVKEIPGYPERIKKCVAHTTPSYFEGWAFSTELIYKTVADKQHQTERNLEKCRIIRALMDMSYAMAGILDDYVDKGEFRRGKKVWASVCEGGQEAAIYDSIAVTYLMSLMVKRHFGTDPGYSKLIELFNMVPGTAAIGNTLDILDRHDTNYYDDTMWKHSVQNKAANTVFPAATAGLIHAGVLCDDLLDRTSEVFGYTGHLFQVWDDFMEHYAVKEQSGKGAPDTKYNAKTWATLTAMAHFNEAQAKEFKACYGSTDPAKRSRVRELYDEVNLRGLYIDYLRNTYMVVEEKISKIPDPRIQSACRSYMDWLLVEPPQDEEEAESVLNN | 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 Length: 378
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Pheromone biosynthesis.
EC: 2.5.1.-
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P52177 | MESRVLLRATETVTGVPQLRRPIRAINRQFSTASSSFTAFAKPIGSIGEGGNLISGRQLRPLLLLDSLPEKREILKPVRAASAEGGDSAGETKVGFLGKYPWLVTGILLLMWYFLNVIFNILNKKIYNYFPYPYFVSVIHLFVGVVYCLVSWSVGLPKRAPVNSDILKVLIPVAVCHAIGHVTSNVSFAAVAVSFTHTIKALEPFFNASASQFLLGQPIPITLWLSLAPVVLGVAMASLTELSFNWLGFISAMISNISFTYRSIFSKKAMTDMDSTNVYAYISIIALFVCLPPAIIVEGPQLLKHGFNDAIAKVGMTKFISDLFWVGMFYHLYNQLATNTLERVAPLTHAVGNVLKRVFVIGFSIVIFGNKISTQTGIGTGIAIAGVALYSVIKAKIEEEKRQGKTA | 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 | MYKNMNSHELIEESNNSGTPATKSSSKPTKKIRPRNDLVHYSKALSKVLRHTAKANGLQIREDGYIEVDSILKLPQFRGMGMELLLSIVKGNDKKRFTMEEVEGVLYIRANQGHSIKAVQVPMARIDNASSIPKVVHGTKKELWPVISKQGLSRMKRNHIHCATGLYGDPGVISGIRKSCTLYIYIDSAKAMQDGVEFYRSENGVILTEGVNGLLSSKYFSRVETSDGEVLLDAKASPKNNRSDESDQSDPESIDPFCDNLQALSMHELELLEEKHSNFGYSEGIIKGKMQVAQSGFDDGFKHGSRLGFQMGKTIGTLKAKLYIFEENEQMEILKQELDRLQESAEFHIFVANHKEEILKCIREK | 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 (Da): 41028
Sequence Length: 365
EC: 2.7.1.160
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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 (Da): 26196
Sequence Length: 230
EC: 2.7.1.160
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Q9BVS5 | MLMAWCRGPVLLCLRQGLGTNSFLHGLGQEPFEGARSLCCRSSPRDLRDGEREHEAAQRKAPGAESCPSLPLSISDIGTGCLSSLENLRLPTLREESSPRELEDSSGDQGRCGPTHQGSEDPSMLSQAQSATEVEERHVSPSCSTSRERPFQAGELILAETGEGETKFKKLFRLNNFGLLNSNWGAVPFGKIVGKFPGQILRSSFGKQYMLRRPALEDYVVLMKRGTAITFPKDINMILSMMDINPGDTVLEAGSGSGGMSLFLSKAVGSQGRVISFEVRKDHHDLAKKNYKHWRDSWKLSHVEEWPDNVDFIHKDISGATEDIKSLTFDAVALDMLNPHVTLPVFYPHLKHGGVCAVYVVNITQVIELLDGIRTCELALSCEKISEVIVRDWLVCLAKQKNGILAQKVESKINTDVQLDSQEKIGVKGELFQEDDHEESHSDFPYGSFPYVARPVHWQPGHTAFLVKLRKVKPQLN | 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 of mitochondrial 16S ribosomal RNA and this modification is most likely important for mitoribosomal structure and function . In addition to tRNA N(1)-methyltransferase activity, also acts as a mRNA N(1)-methyltransferase by mediating methylation of adenosine residues at the N(1) position of MT-ND5 mRNA, leading to interfere with mitochondrial translation .
Catalytic Activity: adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 52965
Sequence Length: 477
Subcellular Location: Mitochondrion matrix
EC: 2.1.1.220
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P24082 | MKRILPLILALVAGMAQADSNSDYRAGSDFAHQIKGQGSSSIQGFKPQESIPGYNANPDETKYYGGVTAGGDGGLKNDGTTEWATGETGKTITESFMNKPKDILSPDAPFIQTGRDVVNRADSIVGNTGQQCSAQEISRSEYTNYTCERDLQVEQYCTRTARMELQGSTTWETRTLEYEMSQLPAREVNGQYVVSITSPVTGEIVDAHYSWSRTYLQKSVPMTITVLGTPLSWNAKYSADASFTPVQKTLTAGVAFTSSHPVRVGNTKFKRHTAMKLRLVVRVKKASYTPYVVWSESCPFSKELGKLTKTECTEAGGNRTLVKDGQSYSMYQSCWAYRDTYVTQSADKGTCQTYTDNPACTLVSHQCAFYSEEGACLHEYATYSCESKTSGKVMVCGGDVFCLDGECDKAQSGKSNDFAEAVSQLAALAAAGKDVAALNGVDVRAFTGQAKFCKKAAAGYSNCCKDSGWGQDIGLAKCSSDEKALAKAKSNKLTVSVGEFCSKKVLGVCLEKKRSYCQFDSKLAQIVQQQGRNGQLRISFGSAKHPDCRGITVDELQKIQFNRLDFTNFYEDLMNNQKIPDSGVLTQKVKEQIADQLKQAGQ | 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-reducing conditions, suggesting it has disulfide bonds; a dsbA deletion mutant has considerably less TraN that is still localized in the outer membrane.
Sequence Mass (Da): 65715
Sequence Length: 602
Domain: The first 350 residues are required for recognition of OmpA.
Subcellular Location: Cell outer membrane
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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 RNAs. Suppresses the host RNA silencing by inhibiting adenosine kinase 2 (ADK2), a kinase involved in a general methylation pathway. Also suppresses the host basal defense by interacting with and inhibiting SNF1 kinase, a key regulator of cell metabolism implicated in innate antiviral defense. Determines pathogenicity (By similarity).
PTM: Phosphorylated.
Sequence Mass (Da): 19551
Sequence Length: 172
Domain: The zinc finger and the transactivation region are involved in PTGS suppression.
Subcellular Location: Host nucleus
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Q8XDH7 | MKSPAPSRPQKMALIPACIFLCFAALSVQAEETPVTPQPPDILLGPLFNDVQNAKLFPDQKTFADAVPNSDPLMIRMQQNQSGFDLRHFVNVNFTLPKEGEKYVPPEGQSLREHIDGLWPVLTRSTENTEKWDSLLPLPEPYVVPGGRFREVYYWDSYFTMLGLAESGHWDKVADMVANFAHEIDTYGHIPNGNRSYYLSRSQPPFFALMVELLAQHEGDAALKQYLPQMQKEYAYWMDGVENLQAGQQEKRVVKLQDGTLLNRYWDDRDTPRPESWVEDIATAKSNPNRPATEIYRDLRSAAASGWDFSSRWMDNPQQLNTLRTTSIVPVDLNSLMFKMEKILARASKAAGDNAMANQYETLANARQKGIEKYLWNDQQGWYADYDLKSHKVRNQLTAAALFPLYVNAAAKDRANKMATATKTHLLQPGGLNTTSVKSGQQWDAPNGWAPLQWVATEGLQNYGQKEVAMDISWHFLTNVQHTYDREKKLVEKYDVSTTGTGGGGGEYPLQDGFGWTNGVTLKMLDLICPKEQPCDNVPATRPLSESTTQPVKQKEAEPTP | 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
Sequence Length: 561
Subcellular Location: Periplasm
EC: 3.2.1.28
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Q4J7W0 | MLGMKPLGFIGNGLTSALVDNGSIVWLTFPRFDSPSVFGKLLDDNAGEFSIRPVEDKFKVSQSYLVPNVLSTTFKSSNGKAEIVDLMPIGEKAIIRKVRTEIPLSFKIIPMFNYGLYRPIIRRKDDGIQFLNPVSRECLSLLSDVPTDEIKPPGTTLYLVYSSDCAYGPLDKGKQLENDLENSFNLTIDYWKDKIRSNDEVWRTSVGVLLGLIYSPSGSSIAAATTSLPEAVGDSRNWDYRFVWVRDSSMISEALLYSGYVVEARRILNFMLALVNFTAKPLLHPLYAVDGSDPPPEIEIPWLSGYMNSRPVRVGNAAASQIQLDIEGFLVDAIYKYYKYTSDRVFVEENWDKIKYIGDWVSKNWMLKDAGMWEDRGDPKHYTHSKVMMWVALDRIEKIMNVKIHEKDEIKEWVMRNCVKDGSFVRSSDSNDVDANLLTLPLYDFIDVKDPIFLKTLKRIEDELYVDGFVKRYSQDFMGEAKHPFALATIWLARVYIRLGRKERAMELLDKVLKPSGTLYLIGEHIDVENMEYTGNYPQAFVHAQLLLALKEVKGLST | 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 1/1.
EC: 3.2.1.28
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Q4J9D4 | MNYALLSNGITTALEKEGSIEWFPVPKFDSPSVFTKILDEDKGGYFLITPEKFNKVKQQYVEYSLILRTEFDDGNLILIDFLPLSLPAIIRLYEAKVPFNVEVKPLFNYGLVNAGTETRKDGIIYKNPESKEGLELLINGDYKIISPYRITVNSGKGYLYLLYSRDLRYGLFSQKGFVYSEPYEAYSKLLYYSRKELERARKPSIYENAFYRSLSVILGLIYKPSGGIIASPTTSIPEIVGDERNWDYRYVWVRDSSYAIEALVKANLLTHARRALDFLTNLLDPSSKSFDHPFYSVDGTPPPAEENLDWLSGFMNSKPVRIGNAAYLQIQMDIEGAYMNALYEYYKRTLDKDYISSIFWAVEAISDWVSSSWRGESTDIWEERGISRHYTHTKLMSWVALDRASKLAKDLGYNKLFEEWKSRANEIKIDILNNGVKDNHHFVRYYGGDEIDAALLTLPIYDFIPATDTLFMNTLKKIDEELRVADGLYLRYKKDFMGLAKNPFTLVTTWMARVYIRLKEFDRARWLLETLIKCNQDLGLIGEHVDPETCEARGNYPHLFPHSGMVLSILEFDEVR | 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 1/1.
EC: 3.2.1.28
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A0R0W9 | MVLQQTEPTDGADRKASDGPLTVTAPVPYAAGPTLRNPFPPIADYGFLSDCETTCLISSAGSVEWLCVPRPDSPSVFGAILDRGAGHFRLGPYGVSVPAARRYLPGSLILETTWQTHTGWLIVRDALVMGPWHDIDTRSRTHRRTPMDWDAEHILLRTVRCVSGTVELVMSCEPAFDYHRVSATWEYSGPAYGEAIARASRNPDSHPTLRLTTNLRIGIEGREARARTRLTEGDNVFVALSWSKHPAPQTYEEAADKMWKTSEAWRQWINVGDFPDHPWRAYLQRSALTLKGLTYSPTGALLAAPTTSLPETPQGERNWDYRYSWIRDSTFALWGLYTLGLDREADDFFSFIADVSGANNGERHPLQVMYGVGGERSLVEEELHHLSGYDNSRPVRIGNGAYNQRQHDIWGTMLDSVYLHAKSREQIPDALWPVLKNQVEEAIKHWKEPDRGIWEVRGEPQHFTSSKIMCWVALDRGSKLAELQGEKSYAQQWRAIAEEIKADVLARGVDKRGVLTQRYGDDALDASLLLAVLTRFLPADDPRIRATVLAIADELTEDGLVLRYRVEETDDGLAGEEGTFTICSFWLVSALVEIGEISRAKHLCERLLSFASPLHLYAEEIEPRTGRHLGNFPQAFTHLALINAVVHVIRAEEEADSSGVFVPANAPM | 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 methyl-alpha-D-glucopyranoside. Is also inactive on alpha,beta-trehalose, beta,beta-trehalose, alpha,alpha-trehalose-6,6'-dibehenate, trehalulose, nigerose, and trehalose dimycolate.
Catalytic Activity: alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose
Sequence Mass (Da): 74690
Sequence Length: 668
Pathway: Glycan degradation; trehalose degradation; D-glucose from alpha,alpha-trehalose: step 1/1.
EC: 3.2.1.28
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Q978S7 | MKKIPHELTHMAFHGLVKYSDITVEGYPKIQYHGFIGNNRTAMLVAMNGYIDWGCLPNFNSNAVFSSILDKNKGGYFAIFPSDTTDVYVDQYYKEMTNVLVTEFVKNGKIILRLTDFMPDSEYGKISFPEVHRFVESFSEPIDITIDFKPTFNYGQDKPIIEKDQHGFIFTTDKESIGISSEFPLRKNSDRIFGNVKMEPRSSSWIIALYGIHHLFRTTDYKSYLRLQETTDYWRKWASSSSYAGAYHSMVMRSALALKVLFYEPTGLMVAAPTASLPEAIGGERNWDYRFTWIRDTAYVIEALSSIGYKYEATEFLYDMMDMITRDNRIRTIYSIDDSNDLEERIIDYEGYRGSRPVRIGNKAVDQLQIDQYGSIVRAIHSMAKAGGIVNSYLWDFVEQVMAKIEYLWKYPDSSIWEFRTEPKQYVYSKVMSWAAFDSAISMAKDLGLSAPIKQWKSIQDEIKKEVLEKGFDTDTNSFVQYYGSKNIDAALLRLPILGFIPANDEKFLGTLSRIEKELMVDGYLFKRYREDDGLKGDEGSFLMLTFWYIEDLILMKRLKKAREVLESVLEKANHLGLYSEEIDEKSGDFLGNFPQALSHLGVIRVAPKLEEALLKRTSKINS | 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 1/1.
EC: 3.2.1.28
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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 tyrosine phosphorylation, activating multiple downstream mediators such as BTK, MAPK1, MAPK3 or phospholipase C-gamma. This cascade promotes the neutrophil- and macrophage-mediated release of pro-inflammatory cytokines and/or chemokines, as well as their migration and thereby amplifies inflammatory responses that are triggered by bacterial and fungal infections. By also promoting the amplification of inflammatory signals that are initially triggered by Toll-like receptor (TLR) and NOD-like receptor engagement, plays a major role in the pathophysiology of acute and chronic inflammatory diseases of different etiologies including septic shock and atherosclerosis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 25381
Sequence Length: 232
Subcellular Location: Cell membrane
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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 tyrosine phosphorylation, activating multiple downstream mediators such as BTK, MAPK1, MAPK3 or phospholipase C-gamma . This cascade promotes the neutrophil- and macrophage-mediated release of pro-inflammatory cytokines and/or chemokines, as well as their migration and thereby amplifies inflammatory responses that are triggered by bacterial and fungal infections . By also promoting the amplification of inflammatory signals that are initially triggered by Toll-like receptor (TLR) and NOD-like receptor engagement, plays a major role in the pathophysiology of acute and chronic inflammatory diseases of different etiologies including septic shock and atherosclerosis .
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 26387
Sequence Length: 234
Subcellular Location: Cell membrane
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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 tyrosine phosphorylation, activating multiple downstream mediators such as BTK, MAPK1, MAPK3 or phospholipase C-gamma. This cascade promotes the neutrophil- and macrophage-mediated release of pro-inflammatory cytokines and/or chemokines, as well as their migration and thereby amplifies inflammatory responses that are triggered by bacterial and fungal infections . By also promoting the amplification of inflammatory signals that are initially triggered by Toll-like receptor (TLR) and NOD-like receptor engagement, plays a major role in the pathophysiology of acute and chronic inflammatory diseases of different etiologies including septic shock and atherosclerosis (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 25409
Sequence Length: 230
Subcellular Location: Cell membrane
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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 tyrosine phosphorylation, activating multiple downstream mediators such as BTK, MAPK1, MAPK3 or phospholipase C-gamma. This cascade promotes the neutrophil- and macrophage-mediated release of pro-inflammatory cytokines and/or chemokines, as well as their migration and thereby amplifies inflammatory responses that are triggered by bacterial and fungal infections. By also promoting the amplification of inflammatory signals that are initially triggered by Toll-like receptor (TLR) and NOD-like receptor engagement, plays a major role in the pathophysiology of acute and chronic inflammatory diseases of different etiologies including septic shock and atherosclerosis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 26428
Sequence Length: 238
Subcellular Location: Cell membrane
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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 mediates microglial activation, proliferation, migration, apoptosis and expression of pro-inflammatory cytokines, such as IL6R and CCL3, and the anti-inflammatory cytokine ARG1 (By similarity). Acts as a receptor for lipoprotein particles such as LDL, VLDL, and HDL and for apolipoproteins such as APOA1, APOA2, APOB, APOE, APOE2, APOE3, APOE4, and CLU and enhances their uptake in microglia . Binds phospholipids (preferably anionic lipids) such as phosphatidylserine, phosphatidylethanolamine, phosphatidylglycerol and sphingomyelin . Regulates microglial proliferation by acting as an upstream regulator of the Wnt/beta-catenin signaling cascade (By similarity). Required for microglial phagocytosis of apoptotic neurons . Also required for microglial activation and phagocytosis of myelin debris after neuronal injury and of neuronal synapses during synapse elimination in the developing brain (By similarity). Regulates microglial chemotaxis and process outgrowth, and also the microglial response to oxidative stress and lipopolysaccharide (By similarity). It suppresses PI3K and NF-kappa-B signaling in response to lipopolysaccharide; thus promoting phagocytosis, suppressing pro-inflammatory cytokine and nitric oxide production, inhibiting apoptosis and increasing expression of IL10 and TGFB (By similarity). During oxidative stress, it promotes anti-apoptotic NF-kappa-B signaling and ERK signaling (By similarity). Plays a role in microglial MTOR activation and metabolism (By similarity). Regulates age-related changes in microglial numbers . Triggers activation of the immune responses in macrophages and dendritic cells . Mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages (By similarity). In dendritic cells, it mediates up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival . Involved in the positive regulation of osteoclast differentiation .
PTM: Undergoes ectodomain shedding through proteolytic cleavage by ADAM10 and ADAM17 to produce a transmembrane segment, the TREM2 C-terminal fragment (TREM2-CTF), which is subsequently cleaved by gamma-secretase.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 25447
Sequence Length: 230
Subcellular Location: Cell membrane
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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 mediates microglial activation, proliferation, migration, apoptosis and expression of pro-inflammatory cytokines, such as IL6R and CCL3, and the anti-inflammatory cytokine ARG1 . Acts as a receptor for lipoprotein particles such as LDL, VLDL, and HDL and for apolipoproteins such as APOA1, APOA2, APOB, APOE, APOE2, APOE3, APOE4, and CLU and enhances their uptake in microglia . Binds phospholipids (preferably anionic lipids) such as phosphatidylserine, phosphatidylethanolamine, phosphatidylglycerol and sphingomyelin (By similarity). Regulates microglial proliferation by acting as an upstream regulator of the Wnt/beta-catenin signaling cascade . Required for microglial phagocytosis of apoptotic neurons . Also required for microglial activation and phagocytosis of myelin debris after neuronal injury and of neuronal synapses during synapse elimination in the developing brain . Regulates microglial chemotaxis and process outgrowth, and also the microglial response to oxidative stress and lipopolysaccharide . It suppresses PI3K and NF-kappa-B signaling in response to lipopolysaccharide; thus promoting phagocytosis, suppressing pro-inflammatory cytokine and nitric oxide production, inhibiting apoptosis and increasing expression of IL10 and TGFB . During oxidative stress, it promotes anti-apoptotic NF-kappa-B signaling and ERK signaling . Plays a role in microglial MTOR activation and metabolism . Regulates age-related changes in microglial numbers . Triggers activation of the immune responses in macrophages and dendritic cells (By similarity). Mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages . In dendritic cells, it mediates up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival (By similarity). Involved in the positive regulation of osteoclast differentiation .
PTM: Undergoes ectodomain shedding through proteolytic cleavage by ADAM10 and ADAM17 to produce a transmembrane segment, the TREM2 C-terminal fragment (TREM2-CTF), which is subsequently cleaved by gamma-secretase.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 24527
Sequence Length: 227
Subcellular Location: Cell membrane
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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 | MAPPHQFQSKPSDVIRRRLSSAVSSKRPNIPGYTSLTPMWAGIAGAVVNNNTQFEVAISIHDSVYNTDFASSVVPYSPNEPEAQAGIIEKHVLETLRKFSTEHMCKFLGAGVTVILLREAPNLCTRLWLDMDIVPIVFNIKPFHTDSITRPNVRHRISSTTGSYVPSGAETPTVYYDPAQLQDPNKLSANVQTRLPIPRTVDEQADSAARKCIMYFGPGNNPRLQIGPRNQVAVDAGGKIHLIDDIDEYRKTVGKGTWNSVIKLADELREKKIKIGFFSSTPQGGGVALMRHAIIRFFTALDVDAAWYVPNPSPSVFRTTKNNHNILQGVADPSLRLTKEAADNFDSWILKNGLRWTAEGGPLAPGGVDIAFIDDPQMPGLIPLIKRIRPDLPIIYRSHIEIRSDLVHVKGSPQEEVWNYLWNNIQHSDLFISHPVNKFVPSDVPLEKLALLGAATDWLDGLSKHLDAWDSQYYMGEFRNLCVKEKMNELGWPAREYIVQIARFDPSKGIPNVIDSYARFRKLCVDKVMEDDIPQLLLCGHGAVDDPDASIIYDQVLQLIHAKYKEYAPDIVVMRCPPSDQLLNTLMANAKFALQLSTREGFEVKVSEALHAGKPVIACRTGGIPLQIEHGKSGYLCEPGDNAAVAQHMLDLYTDEDLYDTMSEYARTHVSDEVGTVGNAAAWMYLAVMYVSRGVKLRPHGAWINDLMRTEMGEPYRPGEPRLPRGELHVQG | 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 Length: 732
EC: 2.4.1.231
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Q9UV63 | MSTPHHQFESKSSTAIRRRLSSSVSSKQRPNIMTTTFASLTPMWAGVAGTLVNNNTQYEIAVTVHDGVYSTDFASVIIPVTPGDTVKNSKDIEAQVLNLIRKFSAEHLCKFLGAGITLALLKECPNLCTRLWLDMDIVPIVFNIKPFHTDSVTRPNIKHRISSTTGSYVPSGSETPTVYVEASHLGDPSHLSPNAAQKLPIPRTLDEQSDSAARKCLMYFGPNNNPRLSIGARNPVTVDAGGKIHLIDDLEEYRMTVGAGTWNAVIKLADELREKKVKIGFFSSTPQGGGVALMRHALIRFLTALDVDVAWYVPNPSPQVFRTTKNNHNILQGVAAPDLRLTQEAKDAFDAWILKNGLRWTAEGGPLAPGGVDVVFIDDPQMPGLIPLIKKVRPEVPIVYRSHIEIRNDLVHVAWSPQEEVWKYLWNNIQLADLFISHPVSKFVPSDVPTEKLALLGAATDWLDGLNKDLDPWDSPFYMGEFRPRGSHLNRGEFRSLCAKEKMHELNWPARDYIVQVARFDPSKGIPNVVDSYYKFRNLLRTRSPDMDESEHPQLLICGHGAVDDPDASIIYDQIMALVNSDPYKEYAHDIVVMRLPPSDELLNAMMANSRIALQLSTREGFEVKVSEALHTGKPVIACRTGGIPLQIQHGKSGYLTTPGEKDAVAGHFYDFYTDEALYRKMSDFARTHVSNEVGTVGNAAAWLYLAVMYSRGEKIKPNGAWINDFFREETGEPYKEGETKLPRTKLDMQG | 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 Length: 751
EC: 2.4.1.231
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Q9CID5 | MTEKDWIIQYDKKEVGKRSYGQESLMSLGNGYLGLRGAPLWSTCSDNHYPGLYVAGVFNRTSTEVAGHDVINEDMVNWPNPQLIKVYIDGELVDFEASVEKQATIDFKNALQIERYQVKLAKGNLTLVTTKFVDPINFHDFGFVGEIIADFSCKLRIETFTDGSVLNQNVERYRAFDSKEFEVTKISKGLLVAKTRTSEIELAIASKSFLNGLAFPKIDSENDEILAEAIEIDLQKNQEVQFDKTIVIASSYESKNPVEFVLTELSATSVSKIQENNTNYWEKVWSDADIVIESDHEDLQRMVRMNIFHIRQAAQHGANQFLDASVGSRGLTGEGYRGHIFWDEIFVLPYYAANEPETARDLLLYRINRLTAAQENAKVDGEKGAMFPWQSGLIGDEQSQFVHLNTVNNEWEPDNSRRQRHVSLAIVYNLWIYSQLTEDESILTDGGLDLIIETTKFWLNKAELGDDGRYHIDGVMGPDEYHEAYPGQEGGICDNAYTNLMLTWQLNWLTELSEKGFEIPKELLEKAQKVRKKLYLDIDENGVIAQYAKYFELKEVDFAAYEAKYGDIHRIDRLMKAEGISPDEYQVAKQADTLMLIYNLGQEHVTKLVKQLAYELPENWLKVNRDYYLARTVHGSTTSRPVFAGIDVKLGDFDEALDFLITAIGSDYYDIQGGTTAEGVHIGVMGETLEVIQNEFAGLSLREGQFAIAPYLPKSWTKLKFNQIFRGTKVEILIENGQLLLTASADLLTKVYDDEVQLKAGVQTKFDLK | 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 | MSWSISSNQLNIENLLNEESLFFTGNGYIGVRGNFEEKYYDGASSIRGTYINAFHDITDINYGEKLYAFPETQQKLVNVIDAQTVQIYFGEEEERFSLFEGEVIQYERHLHMDKGFSERVIHWRSPGGKEVKLKFKRLTSFIYKELFIQEITIEPVNFFGKTKVVSTVNGDVSNFVDPSDPRVGSGHAKLLTVSDTVIEGDFVSIETKTKRSNLYAACTSTCRLNIDFQREYVKNEKSVETVLTFELTEKAIMTKINIYTDTLRHGDRPLRTGLDLCQKLSCLTFNDLKEQQKHYLDKFWLYADVEISGDQALQEGIRFNLFHLLQSAGRDRFSNIAAKGLSGEGYEGHYFWDTEIYMVPVFLMTNPELAKQLLIYRYSILDKARERAREMGHRKGALFPWRTISGGECSSYFPAGTAQYHISADIAYSYVQYYLVTKDLDFLKSYGAELLIETARLWMDTGHYHEGKFKIDAVTGPDEYTCIVNNNYYTNVMAKHNLRWAAKSVAELEKHAPDTLASLKAKLEITDEEIAEWIKAAEAMYLPYDPTLNINPQDDTFLQKQVWDFDNTPKEHYPLLLHYHPLTLYRYQVCKQADTVLAHFLLEDEQDESVIRDSYHYYEKITTHDSSLSSCVFSIMAAKIGELDKAYEYFIETARLDLDNTHGNTKDGLHMANMGGTWMAIVYGFAGLRIKESGLSLAPVIPKQWQSYRFSIQYLGRHISVSVDTKGTKVNLLNGEELTIKLYGKKHQLTKDEPLEITFNNGRVD | 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: 2.4.1.64
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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 = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 34653
Sequence Length: 297
Domain: The RING-type zinc finger domain is essential for its E3 ubiquitin-protein ligase activity, ability to positively regulate the NF-kappa-B signaling pathway and its antiviral activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q9BRZ2 | MVSHGSSPSLLEALSSDFLACKICLEQLRAPKTLPCLHTYCQDCLAQLADGGRVRCPECRETVPVPPEGVASFKTNFFVNGLLDLVKARACGDLRAGKPACALCPLVGGTSTGGPATARCLDCADDLCQACADGHRCTRQTHTHRVVDLVGYRAGWYDEEARERQAAQCPQHPGEALRFLCQPCSQLLCRECRLDPHLDHPCLPLAEAVRARRPGLEGLLAGVDNNLVELEAARRVEKEALARLREQAARVGTQVEEAAEGVLRALLAQKQEVLGQLRAHVEAAEEAARERLAELEGREQVARAAAAFARRVLSLGREAEILSLEGAIAQRLRQLQGCPWAPGPAPCLLPQLELHPGLLDKNCHLLRLSFEEQQPQKDGGKDGAGTQGGEESQSRREDEPKTERQGGVQPQAGDGAQTPKEEKAQTTREEGAQTLEEDRAQTPHEDGGPQPHRGGRPNKKKKFKGRLKSISREPSPALGPNLDGSGLLPRPIFYCSFPTRMPGDKRSPRITGLCPFGPREILVADEQNRALKRFSLNGDYKGTVPVPEGCSPCSVAALQSAVAFSASARLYLINPNGEVQWRRALSLSQASHAVAALPSGDRVAVSVAGHVEVYNMEGSLATRFIPGGKASRGLRALVFLTTSPQGHFVGSDWQQNSVVICDGLGQVVGEYKGPGLHGCQPGSVSVDKKGYIFLTLREVNKVVILDPKGSLLGDFLTAYHGLEKPRVTTMVDGRYLVVSLSNGTIHIFRVRSPDS | 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 the production of type I interferon IFN-beta (By similarity). Also mediate monoubiquitination of CGAS, thereby promoting CGAS oligomerization and subsequent activation . Promotes also TNFalpha-induced NF-kappa-B signaling by mediating 'Lys-63'-linked ubiquitination TAK1, leading to enhanced interaction between TAK1 and CHUK/IKKalpha . Independently of its E3 ubiquitin ligase activity, positive regulator of TLR3 signaling. Potentiates extracellular double stranded RNA (dsRNA)-induced expression of IFNB1 and interferon-stimulated genes ISG15, IFIT1/ISG56, CXCL10, OASL and CCL5/RANTES . Promotes establishment of an antiviral state by TLR3 ligand and TLR3-mediated chemokine induction following infection by hepatitis C virus . Acts as restriction factor of Zika virus through direct interaction with the viral RNA via its C-terminal region .
PTM: (Microbial infection) Preferentially ubiquitinated with 'Lys-48' and 'Lys-11'-linked ubiquitin chains by Salmonella effector SopA leading to proteasomal targeting and degradation.
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): 81488
Sequence Length: 755
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q8NG06 | MAWAPPGERLREDARCPVCLDFLQEPVSVDCGHSFCLRCISEFCEKSDGAQGGVYACPQCRGPFRPSGFRPNRQLAGLVESVRRLGLGAGPGARRCARHGEDLSRFCEEDEAALCWVCDAGPEHRTHRTAPLQEAAGSYQVKLQMALELMRKELEDALTQEANVGKKTVIWKEKVEMQRQRFRLEFEKHRGFLAQEEQRQLRRLEAEERATLQRLRESKSRLVQQSKALKELADELQERCQRPALGLLEGVRGVLSRSKAVTRLEAENIPMELKTACCIPGRRELLRKFQVDVKLDPATAHPSLLLTADLRSVQDGEPWRDVPNNPERFDTWPCILGLQSFSSGRHYWEVLVGEGAEWGLGVCQDTLPRKGETTPSPENGVWALWLLKGNEYMVLASPSVPLLQLESPRCIGIFLDYEAGEISFYNVTDGSYIYTFNQLFSGLLRPYFFICDATPLILPPTTIAGSGNWASRDHLDPASDVRDDHL | 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 nuclear polarization.
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): 54766
Sequence Length: 486
Domain: The RING finger is required for ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q5NCC9 | MATAPGERLQEEARCSVCLDFLQEPISVDCGHSFCLRCISEFCEKSDSAQGVYACPQCRGPFRPASFRPNRQLASLVDSVRQLGLGTGHAGSRQCARHGEDLSHFCEEDQTMLCWVCDTSPEHRSHRTETLQEAASRYQRMLRASLELVKKEMEEALTQEANVGKKTIIWKEKVEMQRQRFRLEFEKHRGFLAQEEQLQLRRLEEEERATLQRLRDSRNRLAQQNKALKELAEELEERSQRPAPGLLEGARGVLTRCEAITRLEPEAVPMDLKTVCRIPGMREMLRKFQVDVKLDPATAHPSLLLTADLRSVQDAEVWRDVPSNPERFDTWPCILGLQGFSSGRHYWEVIVGERAEWGLGVCRDSVLRKGETTPSPENGVWAMWLLRGNEYMVLSSPSVPVLQDERPRRIGIFLDYEAGEISFYNVTNGSYIYTFNHLFSGVLRPYFFVCDTTPLILPPMTEAAPGNWTPRGIFDLAAAARNEEY | 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 nuclear polarization.
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): 55371
Sequence Length: 485
Domain: The RING finger is required for ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q5ZMD4 | MHQFEEELTCSICYSLFEDPRVLPCSHTFCRSCLEGVIQLSSNFSIWRPLRVPLKCPNCRSIVEIPASGTESLPINFALKAIIEKYRQEDHSDVATCSEHYRQPLNVYCLLDKKLVCGHCLTIGKHNGHPIDDLHSAYLKEKESSGKILEQLTDKHWSDVCLLIEKLKEQKAQCESIVQDDKKVVVQYFKKLSETLEHKKQVLLAALDEINRQILEEYEPHIEKLKKIREEQLELMSLNTSIQKEESPLVFLEKVDNVHQRIKALKEKELPDVKPVEVYPRVGHLLKDVWSKTEIGQINKILTPKIKLVPKRKLHSKNSEKERGKPEELLQAANPLSVTFIFTVIIAIAVLSFHKPISSVVIESIPTHISDFFGFLYQDFCTCMQNTVDVVCHKLNSLAEFLGGIVPF | 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 | MHNFEEELTCPICYSIFEDPRVLPCSHTFCRNCLENILQASGNFYIWRPLRIPLKCPNCRSITEIAPTGIESLPVNFALRAIIEKYQQEDHPDIVTCPEHYRQPLNVYCLLDKKLVCGHCLTIGQHHGHPIDDLQSAYLKEKDTPQKLLEQLTDTHWTDLTHLIEKLKEQKSHSEKMIQGDKEAVLQYFKELNDTLEQKKKSFLTALCDVGNLINQEYTPQIERMKEIREQQLELMALTISLQEESPLKFLEKVDDVRQHVQILKQRPLPEVQPVEIYPRVSKILKEEWSRTEIGQIKNVLIPKMKISPKRMSCSWPGKDEKEVEFLKILNIVVVTLISVILMSILFFNQHIITFLSEITLIWFSEASLSVYQSLSNSLHKVKNILCHIFYLLKEFVWKIVSH | 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 transcription and the ubiquitination of BECN1 . On the one hand, regulates the transcription of BECN1 through negatively modulating the NF-kappa-B pathway. On the other hand, regulates TRAF6-mediated 'Lys-63'-linked ubiquitination of BECN1, thus affecting the formation of the BECN1-PIK3C3 complex. In addition, mediates 'Lys-48'-linked ubiquitination of TRAF6 and thereby promotes TRAF6 proteasomal degradation . Acts also as a critical regulator for early embryo development from blastocyst stage to gastrula through modulating F-actin assembly and WASH1 'Lys-63'-linked ubiquitination (By similarity).
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 47114
Sequence Length: 403
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.2.27
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Q9C030 | MTSPVLVDIREEVTCPICLELLTEPLSIDCGHSFCQACITPNGRESVIGQEGERSCPVCQTSYQPGNLRPNRHLANIVRRLREVVLGPGKQLKAVLCADHGEKLQLFCQEDGKVICWLCERSQEHRGHHTFLVEEVAQEYQEKFQESLKKLKNEEQEAEKLTAFIREKKTSWKNQMEPERCRIQTEFNQLRNILDRVEQRELKKLEQEEKKGLRIIEEAENDLVHQTQSLRELISDLERRCQGSTMELLQDVSDVTERSEFWTLRKPEALPTKLRSMFRAPDLKRMLRVCRELTDVQSYWVDVTLNPHTANLNLVLAKNRRQVRFVGAKVSGPSCLEKHYDCSVLGSQHFSSGKHYWEVDVAKKTAWILGVCSNSLGPTFSFNHFAQNHSAYSRYQPQSGYWVIGLQHNHEYRAYEDSSPSLLLSMTVPPRRVGVFLDYEAGTVSFYNVTNHGFPIYTFSKYYFPTTLCPYFNPCNCVIPMTLRRPSS | 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 autophosphorylation of IKBKE leading to stimulation of an antiviral response . Ubiquitinates also MYC and inhibits its transcription activation activity, maintaining the pluripotency of embryonic stem cells (By similarity). Promotes the association of unanchored 'Lys-48'-polyubiquitin chains with DHX16 leading to enhanced RIGI-mediated innate antiviral immune response .
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): 56400
Sequence Length: 488
Domain: The B-box zinc finger and the linker region between the coiled coil and B30.2/SPRY domains contribute to higher order self-association.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q9C029 | MAAVGPRTGPGTGAEALALAAELQGEATCSICLELFREPVSVECGHSFCRACIGRCWERPGAGSVGAATRAPPFPLPCPQCREPARPSQLRPNRQLAAVATLLRRFSLPAAAPGEHGSQAAAARAAAARCGQHGEPFKLYCQDDGRAICVVCDRAREHREHAVLPLDEAVQEAKELLESRLRVLKKELEDCEVFRSTEKKESKELLKQMAAEQEKVGAEFQALRAFLVEQEGRLLGRLEELSREVAQKQNENLAQLGVEITQLSKLSSQIQETAQKPDLDFLQEFKSTLSRCSNVPGPKPTTVSSEMKNKVWNVSLKTFVLKGMLKKFKEDLRGELEKEEKVELTLDPDTANPRLILSLDLKGVRLGERAQDLPNHPCRFDTNTRVLASCGFSSGRHHWEVEVGSKDGWAFGVARESVRRKGLTPFTPEEGVWALQLNGGQYWAVTSPERSPLSCGHLSRVRVALDLEVGAVSFYAVEDMRHLYTFRVNFQERVFPLFSVCSTGTYLRIWP | 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 specific viral proteins for ubiquitination and degradation including norovirus NTPase protein or SARS-CoV-2 NSP5 and NSP8 proteins . Mechanistically, recognizes the C-terminal glutamine-containing motif usually generated by viral proteases that process the polyproteins and trigger their ubiquitination and subsequent degradation . Mediates 'Lys-63'-linked polyubiquitination and stabilization of the JUN coactivator RNF187 in response to growth factor signaling via the MEK/ERK pathway, thereby regulating JUN transactivation and cellular proliferation . Promotes the TLR4-mediated signaling activation through its E3 ligase domain leading to production of pro-inflammatory cytokines and type I interferon (By similarity). Also plays a negative role in the regulation of exogenous cytosolic DNA virus-triggered immune response. Mechanistically, enhances the 'Lys-48'-linked ubiquitination of STING1 leading to its proteasome-dependent degradation . Mediates the ubiquitination of the SIN3-HDAC chromatin remodeling complex component BRMS1 . Modulates NCOA4-mediated ferritinophagy and ferroptosis in glioblastoma cells by ubiquitinating NCOA4, leading to its degradation .
PTM: Phosphorylated at Ser-107 by RPS6KA5/MSK1, which stimulates the ubiquitin ligase activity.
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): 56631
Sequence Length: 511
Domain: The B30.2 domain mediates interaction with GYG1.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q923T7 | MATVGPRTGPNAGAEALALAAELQGEATCSICLEFFREPVSVECGHSFCRACIMRCWERPGAGTGTATRTLPCPLPCPQCREPARPSQLRPNRQLAAVVSLLRRFSLPPTAPGERGTPAVPARAAAARCSQHGEQLKLYCQDDGRAICVVCDRAREHRSHAVLPLEEAVQEAKELLDSRLRALKKVLEDYEAFRSTEERESKELLKQMAAEKEKVGAEFQALRAFLVEQEGRLLSRLEVLSREVTQKQNENLAQLEGEITQLSKLSGQIQETAQKPDLDFLQEFKSTLSKCSSVPSSKPTTVSSEMKNKVWNVSLKSFVLKGLLKKFKEDLQGELEKEEKVELTLDPDTANPRLILSLDLKSVRLGQRAQDLPNHPRRFDTNTRVLASCGFSSGRHHWEVEVGSKDGWAFGVARESVRRKGLTPFTPEEGVWAMQLNNGQYWAVTSPERTQLNCGHLSRVRVALDLEVGAVSFYAVEDMRHLYTFRVNFQERVFPLFSVCSTGTYLRIWP | 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 specific viral proteins for ubiquitination and degradation including norovirus NTPase protein. Mechanistically, recognizes the C-terminal glutamine-containing motif generated by viral proteases that process the polyproteins and trigger their ubiquitination and subsequent degradation . Mediates 'Lys-63'-linked polyubiquitination and stabilization of the JUN coactivator RNF187 in response to growth factor signaling via the MEK/ERK pathway, thereby regulating JUN transactivation and cellular proliferation (By similarity). Promotes the TLR4-mediated signaling activation through its E3 ligase domain leading to production of pro-inflammatory cytokines and type I interferon . Also plays a negative role in the regulation of exogenous cytosolic DNA virus-triggered immune response. Mechanistically, enhances the 'Lys-48'-linked ubiquitination of STING1 leading to its proteasome-dependent degradation. Mediates the ubiquitination of the SIN3-HDAC chromatin remodeling complex component BRMS1. Modulates NCOA4-mediated ferritinophagy and ferroptosis in glioblastoma cells by ubiquitinating NCOA4, leading to its degradation .
PTM: Phosphorylated at Ser-106 by RPS6KA5/MSK1, which stimulates the ubiquitin ligase activity.
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): 57021
Sequence Length: 510
Domain: The B30.2 domain mediates interaction with GYG.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q9BZR9 | MAENWKNCFEEELICPICLHVFVEPVQLPCKHNFCRGCIGEAWAKDSGLVRCPECNQAYNQKPGLEKNLKLTNIVEKFNALHVEKPPAALHCVFCRRGPPLPAQKVCLRCEAPCCQSHVQTHLQQPSTARGHLLVEADDVRAWSCPQHNAYRLYHCEAEQVAVCQYCCYYSGAHQGHSVCDVEIRRNEIRKMLMKQQDRLEEREQDIEDQLYKLESDKRLVEEKVNQLKEEVRLQYEKLHQLLDEDLRQTVEVLDKAQAKFCSENAAQALHLGERMQEAKKLLGSLQLLFDKTEDVSFMKNTKSVKILMDRTQTCTSSSLSPTKIGHLNSKLFLNEVAKKEKQLRKMLEGPFSTPVPFLQSVPLYPCGVSSSGAEKRKHSTAFPEASFLETSSGPVGGQYGAAGTASGEGQSGQPLGPCSSTQHLVALPGGAQPVHSSPVFPPSQYPNGSAAQQPMLPQYGGRKILVCSVDNCYCSSVANHGGHQPYPRSGHFPWTVPSQEYSHPLPPTPSVPQSLPSLAVRDWLDASQQPGHQDFYRVYGQPSTKHYVTS | 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 positive role in the TNFalpha and IL-1beta signaling pathways. Mechanistically, induces the 'Lys-63'-linked polyubiquitination of MAP3K7/TAK1 component leading to the activation of NF-kappa-B . Modulates also STAT3 activity through negative regulation of PIAS3, either by degradation of PIAS3 through the ubiquitin-proteasome pathway or exclusion of PIAS3 from the nucleus . Negatively regulates TLR3/4-mediated innate immune response by catalyzing 'Lys-6'- and 'Lys-33'-linked polyubiquitination of TICAM1 and thereby disrupting the TICAM1-TBK1 interaction .
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): 61489
Sequence Length: 551
Domain: The coiled coil domain is required for homodimerization.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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M9MRI4 | MEDELRCPTCKQLYANPVLLPCFHALCLGCALDIQTPYSPGSALPGAVNGAGAASAAGHNGLHGNGGGAGGGAAAPVTNPNGPGTRHSSHSSAASTASSNTGSESVTSDQDQSDKVSIFSEADSGVVCCSNTSRPVSYAGTGLLPGVGNVVAPPGAAYCLTCPLCRKLVFFDDGGVRNLPTYRAMEAIVDRFCAREALRCQMCETDPKVASLICEQCEIRYCDACRELTHPARGPLAKHTLVKPRGAAQQRESVCGEHEETLSQYCLSCKAPACGLCIGELRHQAHDVQSINVTCKAQKTELSHNLQQLSEKARSTTEFIQRLKGMSDKVTESCMEFERLVHAQCEALIQAIHDRREYLLEAIRMDKDTKIRILKDQQSNCTGKLQQTTGLIQFCIEALKETDSAAFLQVGSMLINRVTNTDMTWHQEVTNAAPRVSPIVDLTLDDAALARAIDNLNFIQMRAVKDGDERCPAAPMTPTILPSDCSAENNSVTVAWQPPNHSFVEGYVLELDDGSGGEFREVYCGKETICTVDGLHFNSMYNARVKAFNSAGEGEYSELIGLQTAEVAWFTFDPVLSGGAGSGLIFSKNNATVSVEGWEHRVALGSVGFSRGVHYWEFTIDNYTADTDPAFGVARIDVARNKMLGKDEKSFAMYIDRQRSWFQHNSIHERRVEGGITTGSTIGVLLDLERHTLSFLVNEMPQGSVAFRDLYGVFYPAVSINRGVTLTMHTAMDAPKMDYF | 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 eye development, consolidates the attachment of R8 photoreceptor growth cones to the target medulla layer, probably downstream of fra .
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): 80192
Sequence Length: 740
Domain: The fibronectin type-III, SPRY and coil-coil domains are necessary for C4da axon patterning.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cell projection
EC: 2.3.2.27
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Q9C026 | MEEMEEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTPESESPQSHRAAGSGVSDYDYLDLDKMSLYSEADSGYGSYGGFASAPTTPCQKSPNGVRVFPPAMPPPATHLSPALAPVPRNSCITCPQCHRSLILDDRGLRGFPKNRVLEGVIDRYQQSKAAALKCQLCEKAPKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPPAQGRVSRRLSPRKVSTCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWKLHKSQLSQALNGLSDRAKEAKEFLVQLRNMVQQIQENSVEFEACLVAQCDALIDALNRRKAQLLARVNKEHEHKLKVVRDQISHCTVKLRQTTGLMEYCLEVIKENDPSGFLQISDALIRRVHLTEDQWGKGTLTPRMTTDFDLSLDNSPLLQSIHQLDFVQVKASSPVPATPILQLEECCTHNNSATLSWKQPPLSTVPADGYILELDDGNGGQFREVYVGKETMCTVDGLHFNSTYNARVKAFNKTGVSPYSKTLVLQTSEVAWFAFDPGSAHSDIILSNDNLTVTCSSYDDRVVLGKTGFSKGIHYWELTVDRYDNHPDPAFGVARMDVMKDVMLGKDDKAWAMYVDNNRSWFMHNNSHTNRTEGGITKGATIGVLLDLNRKNLTFFINDEQQGPIAFDNVEGLFFPAVSLNRNVQVTLHTGLPVPDFYSSRASIA | 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 neurodegenerative disorders. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation.
PTM: Auto-ubiquitinated. Poly-ubiquitinated in cultured cells, whereas it is monoubiquitinated in vitro.
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): 79177
Sequence Length: 710
Domain: The coiled coil domain mediates the interaction with the N-terminal t-SNARE domain of SNAP25.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q8C7M3 | MEEMEEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTPESESPQSRRASGSGVSDYDYLDLDKMSLYSEADSGYGSYGGFASAPTTPCQKSPNGVRVFPPAMPPPPTHLSPALAPVPRNSCITCPQCHRSLILDDRGLRGFPKNRVLEGVIDRYQQSKAAALKCQLCEKAPKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPPAQGRVSRRLSPRKVSTCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWKLHKSQLSQALNGLSDRAKEAKEFLVQLRTMVQQIQENSVEFEACLVAQCDALIDALNRRKAQLLARVNKEHEHKLKVVRDQISHCTVKLRQTTGLMEYCLEVIKENDPSGFLQISDALIRRVHLTEDQWGKGTLTPRMTTDFDLSLDNSPLLQSIHQLDFVQVKASSPVPATPILQLEECCTHNNSATLSWKQPPLSTVAADGYILELDDGSGGQFREVYVGKETMCTVDGLHFNSTYNARVKAFNKTGVSPYSKTLVLQTSEAAGAHETKPMKDTDSEEQTLPFPVPSERLPLRRMSPFSSTLNLQPSFPGRSYFDFRSSPHQLSLHSSLQSLNAPGCNFETQSASYSQLVDIKKLLAVAWFAFDPGSAHSDIIFSNDNLTVTCSSYDDRVVLGKTGFSKGVHYWELTIDRYDNHPDPAFGVARIDVMKDMMLGKDDKAWAMYVDNNRSWFMHNNSHTNRTEGGITKGATIGVLLDLNRKTLTFFVNNEQQGPIAFENVEGLFFPAVSLNRNVQVSLWAPGLRACSGCYFKVCPGAVKSPQAPAP | 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 for the SNARE complex formation.
PTM: Auto-ubiquitinated.
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): 90870
Sequence Length: 817
Domain: The coiled coil domain mediates the interaction with the N-terminal t-SNARE domain of SNAP25.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
|
Q8N9V2 | MSTADLMENLREELTCFICLDYFSSPVTTECGHSFCLVCLLRSWEEHNTPLSCPECWRTLEGPHFQSNERLGRLASIARQLRSQVLQSEDEQGSYGRMPTTAKALSDDEQGGSAFVAQSHGANRVHLSSEAEEHHREKLQEILNLLRVRRKEAQAVLTHEKERVKLCQEETKTCKQVVVSEYMKMHQFLKEEEQLQLQLLEQEEKENMRKLRNNEIKLTQQIRSLSKMIAQIESSSQSSAFESLEEVRGALERSEPLLLQCPEATTTELSLCRITGMKEMLRKFSTEITLDPATANAYLVLSEDLKSVKYGGSRQQLPDNPERFDQSATVLGTQIFTSGRHYWEVEVGNKTEWEVGICKDSVSRKGNLPKPPGDLFSLIGLKIGDDYSLWVSSPLKGQHVREPVCKVGVFLDYESGHIAFYNGTDESLIYSFPQASFQEALRPIFSPCLPNEGTNTDPLTICSLNSHV | 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 Mass (Da): 53002
Sequence Length: 468
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
|
Q8BVP1 | MSNHEKMSTTDLMENLREELTCFICLDYFSSPVTTECGHSFCLMCLLKSWEEHNTPLSCPECWRTLGAPHFQANERLGRLANIGRQLRSQVLQSEDEQSICGRMPGPSWVFSDDEQSVINVSPPSQGTNKACFSSEAEEQHKEKLQDIINILRKKKKEVQAILNHEKERVMLCKEETKTCKQVVVSEYMKMHQFLKEEEQLQLQLLEREEKANMKKLRENEIQLTQQIRRLGKMIGRIESTCQNLTLESFEEVKGAMDRYESLLFQSPETTITELSLCHITGMREMLRKFSTDITLDPATANAYLLLSEDLKSVRYGGTRQQLPDNPERFDQSATVLGAQIFTCGRHYWEVEVGKKTEWEVGICKDSVNRKGNLPKPPGDLFSLIGLKIGDDYSLWVSSPLKGQHVREPVHKVGVFLDYDSGHIAFYNATDESLIYSFPPTPFHEALRPIFSPCLPNEGTNTDPLIICHI | 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 enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 53787
Sequence Length: 470
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
|
Q8N7C3 | MSKRLSPQLQHNITEDAYCETHLEPTRLFCDVDQITLCSKCFQSQEHKHHMVCGIQEAAENYRKLFQEILNTSREKLEAAKSILTDEQERMAMIQEEEQNFKKMIESEYSMRLRLLNEECEQNLQRQQECISDLNLRETLLNQAIKLATELEEMFQEMLQRLGRVGRENMEKLKESEARASEQVRSLLKLIVELEKKCGEGTLALLKNAKYSLERSKSLLLEHLEPAHITDLSLCHIRGLSSMFRVLQRHLTLDPETAHPCLALSEDLRTMRLRHGQQDGAGNPERLDFSAMVLAAESFTSGRHYWEVDVEKATRWQVGIYHGSADAKGSTARASGEKVLLTGSVMGTEWTLWVFPPLKRLFLEKKLDTVGVFLDCEHGQISFYNVTEMSLIYNFSHCAFQGALRPVFSLCIPNGDTSPDSLTILQHGPSCDATVSP | 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
|
H9JAQ7 | MDITKENYYEELDNIAKNIKDSCFISFDAEFSAILTKESFKYSLFDTNEERYNKYKTQISTMKMMQVGLTMFQYDRELDAYLATGYTFHLCPQLIGTINQSLIFQASTLKFLCKHNFDFNKFIYEGLPYLSKSDEALLNRYRIENNLFDYVSESLEFDEEKQINQCSSEVSKWLSSSIEDTMYLDIDNAICRYLLHLELRQRYPGILTTDSLGNSKKILIYRDKNVEGAKNAPIAILEDNLIAYLLGFLHVIKLLETHKKPIVGHNMFLDMLFLHNQFIGPLPDSYTMFKKNINSVFPTIFDTKYISHAMSKKLTFSESWKSNALQDLYEFFAERKCKKLEYGINIVRLTTPFDIKQSYHEAGWDAYCSGYCFIRLGHWAACENRGKSHVIGPREKLAALAPYCNKVNVIRGGVSYMNFSENDPPRNRPVLLHVKCLKDTVIDVEKVASLLGSFGSIDIKPCGKRAALVATGAQFMVDKILKTYENNRDYRISKYSVYKHSVAGRFAIWSGSIVTGGLALYLIHKKFKSILL | 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 elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 61318
Sequence Length: 532
Subcellular Location: Mitochondrion outer membrane
EC: 3.1.13.-
|
Q973J1 | MTITKRKNTFYTSQFISYMKGYYLHPDIRGNLVAFTSDDDVWLMTLEDMKPIRVTSGQGVAIRPKISPDGKKIAYTIIWLRKGKGGGDIFITGNGETKRITFFGSMNTRVLGWLSDDEILVLTDFHTPFPQWSETYKININDGTMEKIPFGPISNIAISGDIIVIARGYQDLPFWKGYKGGTKGEFLISYDKGNT | Function: Degrades oligopeptides in a sequential manner.
Sequence Mass (Da): 22013
Sequence Length: 195
Subcellular Location: Cytoplasm
EC: 3.4.21.-
|
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: Cytoplasm
EC: 2.1.1.206
|
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: Cytoplasm
EC: 2.1.1.206
|
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: Cytoplasm
EC: 2.1.1.206
|
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: Cytoplasm
EC: 2.1.1.206
|
Q9HJN6 | MITVLRINHRPYRDKRITTHVALTARAFGASAILVDERDETLENTIRGVISNFGGSFSIKTGCNWIQEFKHFQGIRVHLTMYGRRINDVIDEIRNSGKDVMVLVGSEKVPIEAYEIADYNVSVTNQPISEVSALAIFLDRYFQGKEFEFEFRGRINVQPAERGKIVKIIPDEIECLDLLKKYGASEQLIEHVKAVEGLALKIAERCNADKRVIVAGSLLHDIGRTRTNGIDHAVAGAEILRSENIHDSVVSAVERHIGAGITREEAARLGLPEKDYVPETLEEMIVAQADNLFAGNKRLRLEEVLNIYRKRGLDSAAERIKELHRRISAIAGIDIDEIR | 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: Cytoplasm
EC: 2.1.1.206
|
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: Cytoplasm
EC: 2.1.1.206
|
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: Cytoplasm
EC: 2.1.1.206
|
Q58293 | MPLCLKINKKHGEQTRRILIENNLLNKDYKITSEGNYLYLPIKDVDEDILKSILNIEFELVDKELEEKKIIKKPSFREIISKKYRKEIDEGLISLSYDVVGDLVILQISDEVDEKIRKEIGELAYKLIPCKGVFRRKSEVKGEFRVRELEHLAGENRTLTIHKENGYRLWVDIAKVYFSPRLGGERARIMKKVSLNDVVVDMFAGVGPFSIACKNAKKIYAIDINPHAIELLKKNIKLNKLEHKIIPILSDVREVDVKGNRVIMNLPKFAHKFIDKALDIVEEGGVIHYYTIGKDFDKAIKLFEKKCDCEVLEKRIVKSYAPREYILALDFKINKK | 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
|
Q9V0Q0 | MTLAVKVPLKEGEIVRRRLIELGALDNTYKIKREGNFLLIPVKFPVKGFEVVEAELEQVSRRPNSYREIVNVPQELRRFLPTSFDIIGNIAIIEIPEELKGYAKEIGRAIVEVHKNVKAVYMKGSKIEGEYRTRELIHIAGENITETIHRENGIRLKLDVAKVYFSPRLATERMRVFKMAQEGEVVFDMFAGVGPFSILLAKKAELVFACDINPWAIKYLEENIKLNKVNNVVPILGDSREIEVKADRIIMNLPKYAHEFLEHAISCINDGGVIHYYGFGPEGDPYGWHLERIRELANKFGVKVEVLGKRVIRNYAPRQYNIAIDFRVSF | 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
|
Q16VC0 | MLFRRFLNLTTKTPHLQTFRARHYFRNMSCPELIPPPTVRGMTVLDKGAFDKRISAPRLIVPRQLNFQQICSSVKKLLLKMECFKPVVSGEYKITLHPSAVKTWEDLKEIGLEDKGLTEENLVWEQMKLGYDNWRYDEILKAVLPEDKEALSAFSKVGHIVHLNLKEHLLPYKNLIGTVIKDKVVGCRAVVNKLVTIDNTYRNFQMELLCGEEDYQVSLKENGCIFEFDFSKVYWNSRLSTEHGRVVEMLKKGDVLLDVYAGVGPFSIPAAKKGYSVLANDLNPDSYKALVHNCAKNKVQGRITCFNKNGIDFIKEEIKQFIISKNQDDTFTGTIHITMNLPALAVEHLENYVGLLKDEQIELKHFPLVHVYCFAKGVEDNKLLARGLVEKNMGIPLGNNLKEIAFVRNVAPNKDMMRVSFYLTRQILCHNDIQLKRPTSETSHQDAKRKCNVLRKIATMGKRNIKNRNQQKQTAKKVKNVFAVNQSKKGNVKKAKEVTSKLKKINVQDKREKADKKFQDLHAHIVAKKPEKKPLPAKPASKKNKNQANTKQVEAGLDKMQM | 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 and required for accurate decoding.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 64310
Sequence Length: 562
Subcellular Location: Mitochondrion matrix
EC: 2.1.1.228
|
E3WPP8 | MCADLLPPATVRGMEQLDRDAFAKTVRVPHLIIPEATNLNSAARALKQYLLKMEHYKPIRSEERKITLHPIPVKQWEDLPVEPLKELGIEKDCLVWEEIKLSYENYKYDLILKAVLPENQEGLSAFSKIGHIIHLNLKNHLMPYRRLIGEVLMDKVADCRTVVNKSNSIQNTYRNFEMELICGVPEYEVSIKENGCTYKFNFSRVYWNPRLSTEHQKITDMLEEGDLLYDLYAGVGPFTVPAAKRGCTVIANDLNPDSYSALVINCGLNKVMRNVKCYNMDAVDFIKVELRNDLLAKLADDKFQGNIHITMNLPAMAVEHLVHFPGLFSGESIELRIKPLVHVYCFAQGADDKKPIAQQKVEQWLGVEVTDMLKEITFVRNVAPNKDMMRVRNPSALGMAKKANKLKDQPKQLAKKAKNVFAVSQTKKGNLKKTKEVAAKLKKINVQDKREKVDANFKTLHAQIVAKKTPKPAPRPLPAKNKTTPDTNKMETDLTKLEMK | 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 and required for accurate decoding.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 56886
Sequence Length: 500
Subcellular Location: Mitochondrion matrix
EC: 2.1.1.228
|
Q7Q5Z3 | MIITTKALTVLPHSGLRTTHRSLLARLRHYFKNMLCPDLHPPATVRGMKLLDRSAFSKTIKVPHLLVPKDKNLNDICRASKKYLLKMERYKPVITEQYKITLHPLAVQKWEDLADLNLEKLDIGSEALVWEEIQLKYENWKYDEIFKAVLPADKEALSSFSKIGHIIHLNLKDHLLPYKELIGQVICDKIADCRTVVNKSLSIDNTYRNFQMELLCGEPDYRVSVKENACLFEFDFSKVYWNPRLSTEHEKIVKMLAKTDTLFDLYAGVGPFTVPAARRGCKVLANDLNPDSYEALVNNCALNKVSKHVTCHNKDAVDFIKHEVKQALLEKCTDESMEGDIHITMNLPAMAVEHLVHFPGLLKDEDVVLRKQPLVHVYCFAKGVEDKKQIARELVEHWLGTDVTDKLKEIAFVRNVAPNKDMMRVSFYLTEDLLLGRTAVKKRQHEEEDLPQLEEAKRPSNKMKDQRKQLAKKAKTVFSVSQVKKGNLKKTKEVSSNLKKIQVNDKREKVDKKFENLHAQIVSKKAAKPAPKPLPAKNKSKPDTKKIEADLNEMQM | 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 and required for accurate decoding.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 63813
Sequence Length: 556
Subcellular Location: Mitochondrion matrix
EC: 2.1.1.228
|
Q4WX30 | MDSMTDSSNSLRSSDLPEMFRPPVNRAMRVLDRSFFRKTVPLSAAAVFQNSDISKVRAELHKSRDLLAVPRLNCIRDVADQEGQIKKALLLRETVKHDDKETWSPKISELVEKGRIAMRPYDLTLDYDFWTYADIISSILPEDELQEIPQGFTQVGHVLHLNLREQYLPYKYLIAEILKDKNKVIRTVINKTEDVGSHSEFRTFPFELLAGDNDLNVVQHEQDCEFRFDYSRVYWNSRLETEHRRLVEKFNKGEMVCDVMAGVGPFAVPAGKKKIFVWANDLNPHGYEVMQDAIKRNKVEGFVTPFNMDGREFIRWSAKELLETEPVTVTIHPKVRRDRKSGNKVEQAPPPHPEEYHRPVFFDHYVMNLPATAIEFLDAFPGIYAGKESLFAPHTSQRLPMVHVYCFSGHSENELDDHIDICQRISERIGYTITPEDRIGGSGNQSVELSIHNVRLVSPKKQMFCASFRLPAEVAFKKV | 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 and required for accurate decoding.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 55196
Sequence Length: 479
Subcellular Location: Mitochondrion matrix
EC: 2.1.1.228
|
F4NUJ6 | MKYIFAPPANKGLQQLNHALFESSHTLPALKIPAHASGIAMETLRSHILVAPRLRTIVDDPTDKKWRLLLLDPSMEASEINDLPNPLKEFALKHEAKLVKHTIELKYDYWTSDQVLRSILPDEMETPGAFETVGHIAHLNLRDRYQPFKHIIGQVILDKSSHIKTVVNKLDNIDHTFRFFQMEILAGINDMNAKLKEGGCFFHFDFSKVYWNSRLQGEHDRIIKLFGQNDLICDVFAGVGPFALPAAKHKRCVVFANDLNPQSFKYLMENIKLNKLETRILPFNMDGRQFIKQSLEDLNNPAIWNKITKQKPTSNDKKRNRKVESPTVAPLTDQPAISGIRHFKHYVMNLPATAIEFLDAFHGLYSGMRDVIMDSDLPTIHCHCFSNAKDVKADVIERVERVIGMPLGSNLIMVHSVRTVAPNKDMLCISFRLPSALAFAEPKILGKRKGLETEENLVSQSDVSKSSDNILEKDT | 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 and required for accurate decoding.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 53947
Sequence Length: 475
Subcellular Location: Mitochondrion matrix
EC: 2.1.1.228
|
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