ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9NV66 | MDPSADTWDLFSPLISLWINRFYIYLGFAVSISLWICVQIVIKTQGKNLQEKSVPKAAQDLMTNGYVSLQEKDIFVSGVKIFYGSQTGTAKGFATVLAEAVTSLDLPVAIINLKEYDPDDHLIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLEEASIDFRFGKTYLKGMRYAVFGLGNSAYASHFNKVGKNVDKWLWMLGAHRVMSRGEGDCDVVKSKHGSIEADFRAWKTKFISQLQALQKGERKKSCGGHCKKGKCESHQHGSEEREEGSHEQDELHHRDTEEEEPFESSSEEEFGGEDHQSLNSIVDVEDLGKI... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryoti... |
Q57705 | MIPEEIYKILRKQRYQIDGHTAVKLCGWVRKKMLEDKNCYKSKFYGIETHRCIQCTPSVIWCQQNCIFCWRVLPRDIGIDISQIKEPKWEEPEVVYEKILAMHKRIIMGYAGVLDRVGEKKFKEALEPKHVAISLSGEPTLYPYLDELIKIFHKNGFTTFVVSNGILTDVIEKIEPTQLYISLDAYDLDSYRRICGGKKEYWESILNTLDILKEKKRTCIRTTLIRGYNDDILKFVELYERADVHFIELKSYMHVGYSQKRLKKEDMLQHDEILKLAKMLDENSSYKLIDDSEDSRVALLQNENRKINPKL | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Component of the wyosine derivatives biosynthesis pathway that catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethy... |
Q8BJM7 | MGPLDVWDLSPLLSLWMNRFYIYMGCALGLTLCICVQIIKKQVTRSQEKRVPGAPDSSLSPQKKQTHVSGVKIFYGSQTGTAKGFAVVLAKAVTSLDLPVAIINLKEYDPDDSLIGEITSKTVCAFLVATYTDGCPTESAEWFCKWLEESANDFRFGKTYLKGLRYAVFGLGDSAYRSHFNKVSTNVDKWLWMLGAQRVLTRGEGDCNAVQSKHGSIEADFTAWKTKFISRLQALQRGEKKACGGNCKRGKCESAQHGPGEARPHPQGELHPGDAEEEEPCESSSEDELGTQDYQSLTSVVDVEDLGNIMNPVKREKREK... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryoti... |
Q8H8N3 | MPPPFPTATAAASTTSHLALLLLLSSSSVFFLYKSLRLRRNNPPSPPPGQGPAPTPTLLYASATGTSKALAAGLSRRLAEAGVTAHPADAAAFDPDDLPSLPLLLLVLPTHDGGAPPPAAAFLARWLEESAADFRAGAALLSGLRFAVFGVGSRAYGETFNAAARSFSRWLRALGAAEVVAVGEGDVDGGDLEVVFEEWCGRVVRVVKGEEIGEGHNGESDGFDELEEEESDDDDDEEEVDGGEVDMEDIAGKAPAARRRNGKVEGALSNGGENGVRDMVTPIIRTSLEKQGYKIIGSHSGVKICRWTKSQLRGRGGCYK... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryoti... |
O59412 | MMEMITIKPGKITVQANPNMPKEVAELFRKQHYEIVGRHSGVKLCHWLKKSLTEGRFCYKQKFYGIHSHRCLQMTPVLAWCTHNCIFCWRPMENFLGTELPQPWDDPAFIVEESIKAQRKLLIGYKGNPKVDKKKFEEAWNPTHAAISLSGEPMLYPYMGDLVEEFHKRGFTTFIVTNGTIPERLEEMIKEDKLPTQLYVSITAPDIETYNSVNIPMIPDGWERILRFLELMRDLPTRTVVRLTLVKGENMHSPEKYAKLILKARPMFVEAKAYMFVGYSRNRLTINNMPSHQDIREFAEALVKHLPGYHIEDEYEPSRV... | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Component of the wyosine derivatives biosynthesis pathway that catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine (imG-14) on guanosine-37 of tRNA(Phe).
Catalytic Activity: N(1)-methylguanosine(37) in tRNA... |
O59761 | MGYSLGYIGEHWEEYRAVLYIVLLLPVLIHFLIRRKTQLSNSDKSSEKKDEVKKQREVKRFKRVGKRGKIGSPSSSIRKQNDTIDWKNSPLCVFYSTLGGTAERYAKQVHEELSSLLQRDDIQLLNLDYVDLSEYFVSCPENAIYLVVLPSYEIESSIDYYLSSLQESFSDFRVPKDPLHGLSGYAVFGLGDMENYPGDKFCYQAIQADKWIKKLGARRLAPLGVVNTQLAPTAQIDALLQWTRSVAECLKNGTLLKIGNTDSLSSDVMDVEDMGSMMAKAKAEAALPVGTKEMVSTESPTYKALTKQGYSVVGSHSGVK... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryoti... |
O43818 | MSATAAARKRGKPASGAGAGAGAGKRRRKADSAGDRGKSKGGGKMNEEISSDSESESLAPRKPEEEEEEELEETAQEKKLRLAKLYLEQLRQQEEEKAEARAFEEDQVAGRLKEDVLEQRGRLQKLVAKEIQAPASADIRVLRGHQLSITCLVVTPDDSAIFSAAKDCSIIKWSVESGRKLHVIPRAKKGAEGKPPGHSSHVLCMAISSDGKYLASGDRSKLILIWEAQSCQHLYTFTGHRDAVSGLAFRRGTHQLYSTSHDRSVKVWNVAENSYVETLFGHQDAVAALDALSRECCVTAGGRDGTVRVWKIPEESQLVF... | Function: Component of a nucleolar small nuclear ribonucleoprotein particle (snoRNP) thought to participate in the processing and modification of pre-ribosomal RNA (pre-rRNA) . Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processom... |
O82383 | MRNVELIFIPTPTVGHLVPFLEFARRLIEQDDRIRITILLMKLQGQSHLDTYVKSIASSQPFVRFIDVPELEEKPTLGSTQSVEAYVYDVIERNIPLVRNIVMDILTSLALDGVKVKGLVVDFFCLPMIDVAKDISLPFYVFLTTNSGFLAMMQYLADRHSRDTSVFVRNSEEMLSIPGFVNPVPANVLPSALFVEDGYDAYVKLAILFTKANGILVNSSFDIEPYSVNHFLQEQNYPSVYAVGPIFDLKAQPHPEQDLTRRDELMKWLDDQPEASVVFLCFGSMARLRGSLVKEIAHGLELCQYRFLWSLRKEEVTKDD... | Function: Possesses quercetin 3-O-glucosyltransferase activity in vitro.
Catalytic Activity: a flavonol + UDP-alpha-D-glucose = a flavonol 3-O-beta-D-glucoside + H(+) + UDP
Sequence Mass (Da): 53000
Sequence Length: 467
EC: 2.4.1.-
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P0DO49 | MKKAELVFIPAPGAGHLVSALQFGKRLLQRDDRISITVLAIKSAAPSSLGSYTEALVASESRLQLIDVPQAELPPLEFAKSPAKFFILNIENHVPNVREALTNYVSSKQDSVSIVGVVLDFFCVSMIHVVNEFNLPSYLFMTSNAGYLSFEFHFPAQDSRTGRPPKDSDPDWLVPGIVPPVPTKVLPVSLTDGSYYNYLGVASRFREAKGIIANTCVELETHAFNSFAEDQTTPPVYPVGPVLDLNDGQARSNLNQAQRDKIISWLDDQPEESVVFLCFGSMGSFTEAQVKEIALGLEQSGQRFLWSLRLTPPKGSKSLT... | Function: Glycosyltransferase that catalyzes the glucosylation of diverse hydroxycoumarins, naphthols, flavonoids, acylphloroglucinols, and pelargonidin . Involved in fruit ripening by synthesizing acylphloroglucinol glucosides and anthocyanin .
Catalytic Activity: a 2-acylphloroglucinol + UDP-alpha-D-glucose = a 2-acy... |
Q9M156 | MEESKTPHVAIIPSPGMGHLIPLVEFAKRLVHLHGLTVTFVIAGEGPPSKAQRTVLDSLPSSISSVFLPPVDLTDLSSSTRIESRISLTVTRSNPELRKVFDSFVEGGRLPTALVVDLFGTDAFDVAVEFHVPPYIFYPTTANVLSFFLHLPKLDETVSCEFRELTEPLMLPGCVPVAGKDFLDPAQDRKDDAYKWLLHNTKRYKEAEGILVNTFFELEPNAIKALQEPGLDKPPVYPVGPLVNIGKQEAKQTEESECLKWLDNQPLGSVLYVSFGSGGTLTCEQLNELALGLADSEQRFLWVIRSPSGIANSSYFDSHS... | Function: Bifunctional O-glycosyltransferase and N-glycosyltransferase that can detoxify xenobiotics. Possesses high activity to metabolize the persistent pollutants 2,4,5-trichlorophenol (TCP) and 3,4-dichloroaniline (DCA). Also active on benzoates and benzoate derivatives in vitro.
Catalytic Activity: hydroquinone + ... |
A0A0D1CFE5 | MVVKRILPLPRPAGLAPPTEVPLDGQDLAMPKMVMHCIWFFLASSQPSLESTSLQELEQAFTLGMQLFLARFPAAGARTRHDKDTARWYLEYNDQGADLEVIQLDRPLQDDWKALDGKCDSVFAPRPVMIFDDDASIFSIKVTRLSCGSVAISTSTHHWLVDFVGYIDLMEELSHCVSIFLNDPNAQINIDEGATKFDWSRDLLAYSKQLEPESIPSATWFTERGSPPQMTRAPSSCHYASLLFTQESLEKLKRSLAEWALETAPTTATDRIVPSKDNWIATNDALHALLWAAITDARGLDLNATTQLHTPLDGRRLLSS... | Function: Acyltransferase; part of the gene cluster that mediates the biosynthesis of the glycolipid biosurfactant ustilagic acid (UA) . UA is a secreted cellobiose glycolipid that is toxic for many microorganisms and confers biocontrol activity to U.maydis . UA consists of 15,16-dihydroxypalmitic or 2,15,16-trihydroxy... |
Q9ZU75 | MIGLFKVKEKQREESQSNNGRGASTVKKQSAGELRLHKDISELNLPKSCKISFPNGKNDLMNFEVTIKPDEGYYLSGNFVFSFQVSNMYPHEAPKVKCKTKVYHPNIDLEGNVCLNILREDWKPVLNINTVIYGLFHLFTEPNYEDPLNHEAAAVLRDNPKTFEYNVRRAMMGGQVGQTSFPRCM | Function: Accepts the ubiquitin-like protein NEDD8/RUB1 from the ECR1-AXR1 E1 complex and catalyzes its covalent attachment to other proteins.
Sequence Mass (Da): 21133
Sequence Length: 185
Pathway: Protein modification; protein neddylation.
EC: 2.3.2.-
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Q77J49 | MFTHLTRAFRKMNNLVNRSFIDVHRVVAELSYPEFEEDVKNPESSIYRTPISLFQNKDIVTIVGDYILSPKTDSFQVLYPIKKVIEHFPVIFHCTHNNAPLWVHLLDERHHRLLQSLLTYEIVNAKYRGIVVIPYYRRPINYQTGKSLLMSKLASVKVLDILMRCGSYKFISLMCMINKKNNTNFLHCCASKWGEVGSKMMLHIAEMFFANPTTSQHLSDASSFPDAAAEDDKGKTPAHLAIQEDNADALLFLISLYGAPWFQDNNSYMKSALELKSNKCVKVLSFAADKYEILPNINNNQLEPDTMCGVCATSVEEDEN... | Function: Probable E3 ubiquitin-protein ligase which accepts ubiquitin from the E2 ubiquitin-conjugating enzyme UBE2E1/UBCH6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of host tumor-suppressor-like protein (TSL) targeting it for degradation. Migh... |
Q6DCJ1 | MSPAGCSHVNSFKVENWRQNLRVIYQCFVWSGTPETRKRKAKSCVCHMCGAHLNRLHSCLYCVYFGCFTKKHIHEHAKNKRHNLAIDLLYGGIYCFMCQDYIYDKDMEQVAKEEQRKAWKLQVFSPALVSPYQYTMTGVGEKYSTWEPTKRELELLQHNPKRRKITTNCTIGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHKCEMQSPNSCLVCEMSTLFQEFYSGHRSPHIPYRLLHLVWTHARHLAGYEQQDAHEFLIAALDVLHRHCKGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTID... | Function: Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a coactivator. Recruited to specific gene promoters by activators, where it is required for transcription (By similarity).
C... |
P51668 | MALKRIQKELSDLQRDPPAHCSAGPVGDDLFHWQATIMGPPDSAYQGGVFFLTVHFPTDYPFKPPKIAFTTKIYHPNINSNGSICLDILRSQWSPALTVSKVLLSICSLLCDPNPDDPLVPDIAQIYKSDKEKYNRHAREWTQKYAM | Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins . In vitro catalyzes 'Lys-48'-linked polyubiquitination . Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination... |
P62837 | MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDREKYNRIAREWTQKYAM | Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins . Catalyzes 'Lys-48'-linked polyubiquitination . Mediates the selective degradation of short-lived and abnormal proteins . Functions in the E6/E6-AP-induced ubiquitination of p53/TP53 . Mediates ubiquitination of PEX... |
Q06AA9 | MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDRDKYNRISREWTQKYAM | Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination o... |
P0CG53 | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC | Function: Exists either covalently attached to another protein, or free (unanchored) (By similarity). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear pol... |
P0CG54 | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGVYASPIF | Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via ... |
Q8MKD1 | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRFIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC | Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via ... |
P0CG47 | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC | Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via ... |
P0CG49 | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGY | Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via ... |
P35133 | MASKRILKELKDLQKDPPTSCSAGPVAEDMFHWQATIMGPSESPYAGGVFLVTIHFPPDYPFKPPKVAFRTKVFHPNINSNGSICLDILKEQWSPALTISKVLLSICSLLTDPNPDDPLVPEIAHMYKTDKNKYESTARSWTQKYAMG | Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Mediates the selective degradation of short-lived and abnormal proteins.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquit... |
P35134 | MASKRILKELKDLQKDPPSNCSAGPVAEDMFHWQATIMGPPESPYAGGVFLVSIHFPPDYPFKPPKVSFKTKVYHPNINSNGSICLDILKEQWSPALTISKVLLSICSLLTDPNPDDPLVPEIAHMYKTDRSKYESTARSWTQKYAMG | Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Mediates the selective degradation of short-lived and abnormal proteins.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquit... |
O00103 | MDSDMQNQNPHTNSKNSSSAGMAVDGHSVTKRLRSELMSLMMSNTPGISAFPDSDSNLLHWAGTITGPSDTYYEGLKFKISMSFPANYPYSPPTIIFTSPMWHPNVDMSGNICLDILKDKWSAVYNVQTILLSLQSLLGEPNNASPLNAQAAELWSKDPIEYKRLLMQRYKEIDEI | Function: Catalyzes the covalent attachment of ubiquitin to other proteins.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
Sequence Ma... |
P52492 | MAVEEGGCVTKRLQNELLQLLSSTTESISAFPVDDNDLTYWVGYITGPKDTPYSGLKFKVSLKFPQNYPFHPPMIKFLSPMWHPNVDKSGNICLDILKEKWSAVYNVETILLSLQSLLGEPNNRSPLNAVAAELWDADMEEYRKKVLACYEEIDDY | Function: Catalyzes the covalent attachment of ubiquitin to other proteins.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
Sequence Ma... |
Q76MR7 | MAVLAKFISKNHPSVPIIIISNAPESAAASVAAIPSISYHRLPLPEIPPDMTTDRVELFFELPRLSNPNLLTALQQISQKTRIRAVILDFFCNAAFEVPTSLNIPTYYYFSAGTPTAILTLYFETIDETIPVDLQDLNDYVDIPGLPPIHCLDIPVALSPRKSLVYKSSVDISKNLRRSAGILVNGFDALEFRAIGSHSQRPMHFKGPTPPVYFIGPLVGDVDTKAGSEEHECLRWLDTQPSKSVVFLCFGRRGVFSAKQLKETAAALENSGHRFLWSVRNPPELKKATGSDEPDLDELLPEGFLERTKDRGFVIKSWAP... | Function: Involved in the production of glucuronosylated baicalein, a flavonoid that shows antiallergic, anti-HIV and antitumor activities. Can use baicalein, scutellarein and wogonin as substrates, but not chrysin, apigenin, luteolin, quercetin, formononetin and daidzein. Highly specific for UDP-glucuronate (UDP-GlcUA... |
Q09444 | MTDAGSWCLIESDPGVFTEMLRGFGVDGLQVEELYSLDDDKAMTRPTYGLIFLFKWRQGDETTGIPSDKQNIFFAHQTIQNACATQALINLLMNVEDTDVKLGNILNQYKEFAIDLDPNTRGHCLSNSEEIRTVHNSFSRQTLFELDIKGGESEDNYHFVTYVPIGNKVYELDGLRELPLEVAEFQKEQDWIEAIKPVIQQRMQKYSEGEITFNLMALVPNRKQKLQEMMENLIQANENNELEEQIADLNKAIADEDYKMEMYRKENNRRRHNYTPFVIELMKILAKEGKLVGLVDNAYQAAKEKSKLNTDITKLELKRK... | Function: Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, pe... |
Q5ZKS8 | MGPAELVQKISINAESPRGGERNDCGAGAERGPAGGWRQKCAAYVLALRPWSFSASLTPVALGSALAYRAEGALDPRLLVGSAVAVLAVHGAGNLVNTYYDFSKGIDHKKSDDRTLVDQILEPQDVVRFGVFLYTVGCICAAGLYAVSTLKLEHLALVYFGGLSSSFLYTGGIGFKYVALGDVVILITFGPLAVMFAHAVQVGYLSVSPLLYAVPLALSTEAILHSNNTRDMESDQQAGIVTLAIIIGPAFSYVLYTVLLFLPYLIFCVLATRYTISMALPLLTIPMAFSLERQFRSQNFNKIPQRTAKLNLLLGLFYVF... | Function: Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10. MK-4 is a vitamin K2 isoform required for endothelial cell development. Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methyl-1,4-naphthoquin... |
E7FB98 | MQEMKPAALSGSNGLNGASGSSVRVPCSRLSRAGRMALDLQSKCAAYVLALRPWSFSASLTPVALGSALAYKLEGSVDLLLLLVCAVAVLLVHGAGNLVNTYYDFSKGIDHKKSDDRTLVDQILKPQDVVMFGAVLYSAGCLCATLLYFLSSLKLEHLALIYFGGLSSSFLYTGGIGLKYVALGDVVILITFGPLAVMFAHAVQVGYLSVLPLVYAVPLALNTEAILHSNNTRDMDSDKQAGIVTLAILLGPTLSYVIYNLLLFVPYLLFCILATRYTISMALPLLTLPMAFPLERQFRCRCYAKIPQKTAKLNLLMGLF... | Function: Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10 . MK-4 is a vitamin K2 isoform required for endothelial cell development (By similarity). Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methy... |
Q54K99 | MSTTINRNEKTKQVVNKTKEIKTESSQQQQQKPPISKLMGIILATRPWSLTISVTSVLVGSALAFREIREFDSIMLSIILVGAVSLQALGNVVNSFYDCKNGNDTKEKSADRTMFDFGLTEGNIINLIWYLLIQCAICLGLMIFRMDNIKCIVENILPLGAFGFILNISYTAAPIGLKYIGLGDLTIFLCFGPILVQSAFISQTHYHDSLAYFYSIPLALTIVAVLHVNNTRDIKADTEAGSITLASKLGFKNCYYIYAGLYLFAYIYLFKLSLDIDKYILNLPLILIPKIISLINQFKNKKLEDLTEKTGQLSFFFGGL... | Function: Prenyltransferase that mediates the formation of menaquinone-4 (MK-4), a vitamin K2 isoform.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate + menadiol = diphosphate + menaquinol-4
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36794
Sequence Length: 330
Pathway: Quinol/quinone ... |
Q5P5M0 | MIAPATLSSRLPLYLRLMRLDKPIGILLLMWPTLWALWLAADGFPPLHLIVIFALGTVLMRSAGCVINDYADRDFDGHVERTRTRPLTTGAVTVREALLLAAGLSLVSFVLILPLDPLVRWLSLPALFLAASYPYTKRFLAIPQAYLGIAFGFGIPMGFAAVQGEVPAIAWLLLLANIFWAVAYDTEYAMVDRPDDLKIGIKTSAITFGRFDVAAVMLCYAVAFGLIAAVGIATGRGPWFFGGIAIAAAIAIYHYTLIRDRDRARCFRAFLHNNWVGAVLFVALVIDYVAFPAA | Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-oct... |
Q494A7 | MSNRLFFIKKCYNLAQLMRINQPIGFFLLLWPTLWGLWLSHKGIPDKVVLIVFVAGALCMRSAGCIINDYVDYDIDGHVQRTKTRPLPSGMIRKKEALVALSILLFIAFILVLSLNFITIFLSVVALILSWIYPYLKRYIYFPQVMLGLLFSWPILMAFTAINNPINSTAWLLFLMNTVWTIVYDTQYAMIDREDDIYVGIKSSAVLFGDMDKFLIGILQLCIVFILGIIGWKERFTVVFYFFSLFGVIILFMWQQILINKRKRIRYFQAFLSNNYVGMLVFIGIASSFH | Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-oct... |
Q2SZ16 | MLARFPLYLRLIRMDKPIGSLLLLWPTLNALWIASDGHPAPSLVVIFVLGTLLMRSAGCAINDYADRDFDRHVKRTAERPLTSGKIRAWEAVAIAVGLALVSFLLILPLNALTKELSVVAVFVAATYPFMKRFFAIPQAYLGIAFGFGIPMAFAAVQDTVPALAWMLLAANVFWSVAYDTAYAMVDRDDDLKIGMRTSAITFGRYDVLAIMLCYAAMLGIYVWVGVTQHFGWPYWAGWAAAAGCSIYHYTLIKDRERMACFAAFRHNNWLGGALFAGIAAHYALSAL | Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-oct... |
A1WKC0 | MSGTPRSRLSLYLDLIRWNRPAGWLVCLWPTLSALWVAADGFPGWHLLLVFVLGTCIMRSAGCCVNDVADRDFDRHVKRTAQRPVTTGAVGVKEALAVGAVLALLAFGLVLSTNAATIAWSVPALLVAIAYPYAKRLVSMPQTVLGIAFNFGIVLAFAAVQGRVPAVAWWLWLGTMFWVLAYDTEYAMVDRDDDLKIGIKTSAITLGRLDVAAIMLCYLLFLSLWVWALHSRALGALFYIAIAAALAQALWHWRLIRQRTRAGCFAAFRVNHWLGCTVFAGIAGSYLVRHLQSNG | Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-oct... |
A5CXV6 | MRLDNPIGIYLLLWPTLWALFLASEGFPDLKLLLIFVLGVVLMRSAGCVINDYADRYIDKLVERTKHRPITSGEIHHRSALKFFVLLIMLAFLLVLLTNWLTIQLAMIAVLLAILYPFTKRWTYFPQFVLGLAFAMSVLMAFSATLNEIPITAWYVFAATVIWTVIYDTMYAMADREEDLKIGIKSSAILFAKFDRLIIGILQIIFLLILIKISNVFNLTISYHITLLLVTLLMIYHQYLIKNNENYSYLHGFLHNNYIGMVIFIGIVLSVGL | Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-oct... |
Q0A5V8 | MYRNKEASWWPRRHPSRRRVPRGLEAWLDEPGSLTARLRRSVPGGLEVTVLVERWGRPSIDEARAVELSDGRHARIREVLLGSRDQAWIYARTIMPPEALAGDGRRLARLGRTPLGGALFRGRTVARGPLSIARLGPRDPLAARVPGGGAGCWARRSRLWYGNAGLLVTEVFLPPLLQSLED | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 20280
Sequence Length: 182
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q5P5L9 | MRIRPHSETWLKRPPRPRVPARLRPWLTDPGSLTARIRSRCSLFSVNVLAQRLAVPHPDEAALLGLRRGELAWLREVLLVADGVPVVFARSILPRHDVRGAWILFQGLGSRPLGAALFADPRIGRKPLACACLDRRDARYHRASAAAAPRRLPLALWARRSLFGLRGRTLLVSEVFLPTILELPT | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 20742
Sequence Length: 185
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q2L1H6 | MTTKYQAPLAAGWLIRAPSLLSPTQRHWLFRPGALTAGLRQLGKVQLRVVSEHAEGASLDEARAMLIAPGSPVWVREVLMSVDGIDSVPARSLTPLAASHGSWQGMRRLLTRPLADMLYHDRGVTRSPFVCRRLSSPLPFYRMALPPNHDGSAIWARRSVFWRHGQPLLVAECFLPDFWRKVTLGRAIPPLKAHDRRA | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 22167
Sequence Length: 198
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q1QSG3 | MSPDRFPGWPHWLPIAAQRPRMSPDWWPWVASRDSLTARLRIASPRPFSVRLLTQGVTRPRLDEAQALGLPHRTHVWHREVLLRLGNASWVAARSVAPLEGLSGARLCTLGERSLGSWLFRQPNLERGPIEAIRAPAMTGLDAWRGDAGPWGRRSLLRVGRTRILVQEFFLAAMAADLSLPSR | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 20588
Sequence Length: 183
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q9CKD6 | MTDQHAFATEQVQLDPTLSPTTEETTHFGFKTVAKSEKQKMVANVFHSVAGKYDLMNDLLSFGIHRVWKRFTIDCSGVRKGHKVLDLAGGTGDFTAKFSRLVGPSGEVILADINDSMLRVGREKLRNLGVVGNVNYVQANAEALPFPDNTFDCVIISFGLRNVTDKDKALRSMFRVLKPGGRLLVLEFSKPILDPLSKIYNFYSFNILPKIGEVVVNDSESYRYLAESIRMHPAQDVLKQMMIDAGFEQVNYYNLSAGIVALHRGYKF | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol... |
B4RC42 | MTGPSATFGFRDVDAREKPGLVRGVFDRVARRYDLMNDLMSAGVHRLWKDAVAARLNPQPGETILDVAGGTGDMARRFARMARRAQERRGGDDAKVFVIDYNAEMIAAGRERGFEPEICWTVGDAQRLPLPDACADAYVISFGIRNVTDIPAALREARRVLKPGGRFLCLEFSRPVTEPLQRAYDLYSFKVIPEIGERVAGDRESYQYLVESIRRFPDQKRFAGMIGEAGFSRVGYTNFTAGVAALHTGRAI | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol... |
Q9A9X1 | MTQAASAAPSWSIDPADVARFSAIAAEWWDPKGKFAPLHVFNPCRLAFIREQALARFDRDGAARAPFEGLTLLDIGCGGGLLSEPMARLGFAVTAIDASEKNIKTAATHAAEQGLDIGYRPATAEQLLAEGAGPFDVVLTMEVIEHVADPGEFLRTCAKLLKPGGIMFVATLNRTLKALALAKIGAEYVLRWVPPGTHDWKQFLKPEELRAFLAGEPVAMQGPFGVAYNPLTGRWSRSSDTDINYMMTVTKD | Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic Activity: a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27245
Sequence Length: 252
Pathway: Cofactor biosynthesis; ubiquinone bi... |
Q9FIQ1 | MAEFSDPPPSNLSSSHKLTKPNQTLDESSPTAPIRDLVTNSLSLSSPIRQIQALSPAKPDGSSSSPPDKTLNFNPEENRDVNPDESSSSPSDKTLIAPPAQISPVSNNNHLRITNTSDSYLYRPPRRYIEYESDDDELNKMEPTKPLQLSWWYPRIEPTGVGAGLYNSGNTCFIASVLQCFTHTVPLIDSLRSFMYGNPCNCGNEKFCVMQALRDHIELALRSSGYGINIDRFRDNLTYFSSDFMINHQEDAHEFLQSFLDKLERCCLDPKNQLGSVSSQDLNIVDNVFGGGLMSTLCCCNCNSVSNTFEPSLGWSLEIE... | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by th... |
Q9UK80 | MPQASEHRLGRTREPPVNIQPRVGSKLPFAPRARSKERRNPASGPNPMLRPLPPRPGLPDERLKKLELGRGRTSGPRPRGPLRADHGVPLPGSPPPTVALPLPSRTNLARSKSVSSGDLRPMGIALGGHRGTGELGAALSRLALRPEPPTLRRSTSLRRLGGFPGPPTLFSIRTEPPASHGSFHMISARSSEPFYSDDKMAHHTLLLGSGHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPGGGRAQELTEAFADVIGALWHPDSCEAVNPTRFRAVFQKYVPSFSGYSQQDAQEFLKLLMERLHLEINRR... | Function: Deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator (By similarity). Deubiquitination of histone H2A releaves the repression of di- and trimethylation of histone H3 at 'Lys-4', resulting in regulation of transcriptional initiation (By similari... |
Q9LEW0 | MSARISFLKNPDPCNHLSDYKLRYGTDGYKSFNNLFRCFNDARIKIKLQGIDIPRCSYCSVYQKRLYICLICRSISCSSHILLHTQLNKGHDIAIDVERSELYCCACIDQVYDSEFDEVVVSKQLFGLGMSVKSGADVVAVRSNKKRRLDSQLIIGSNFLVSPRDRREKWTFPLGLRGLNNLGSTCFMNAVLQALVHAPPLRNFWLSGQHNRDLCPRRTMGLLCLPCDLDVIFSAMFSGDRTPYSPAHLLYSWWQHSTNLATYEQQDSHEFFISLLDRIHENEGKSKCLYQDNEECQCITHKAFSGLLRSDVTCTTCGST... | Function: Component of a deubiquitination module (DUB module) that specifically deubiquinates monoubiquinated histone H2B (H2Bub) . Does not seem to be a component of the TREX-2 complex . Seems to act independently of the SAGA multiprotein complex . The DUB module is responsible for the major H2Bub deubiquitinase activ... |
P0C8Z3 | MDAELVVTPPGCAHLGSFKVDNWKQNLRAIYQCFVWSGSAEARKRKAKSCVCHVCGLHLNRLHSCLHCVFFGCFTKKHIHEHAKSKRHNLAIELMYGGIYCFLCQDYIYDKDIEIIAKEEQRKAWKMQGVGEKFSTWEPTKRELELLKHNPKRRKITSNCTIGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGHRSPHIPYKLLHLVWTHARHLAGYEQQDAHEFLIAALDVLHRHCKGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDL... | Function: Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a coactivator. Recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Requi... |
A6H8I0 | MSPAGCSHVNGFKVDNWKQNLRVIYQCFVWSGSAETRKRKAKSCICHMCGAHLNRLHSCLHCVFFGCFSKKHIHEHAKNKRHNLAIDLLYGGIYCFVCQDYIYDKDMEQIAKEEQRKAWKLQGIGEKYSMWEPTKRELELLRHNPKRRKITANCTIGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHKCEMQSNSCLVCEMSQLFQEFYSGHRSPHIPFRLLHLVWTHARHLAGYEQQDAHEFLIAALDVLHRHCKDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSSTPFW... | Function: Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a coactivator. Recruited to specific gene promoters by activators, where it is required for transcription (By similarity).
C... |
Q9UPT9 | MVSRPEPEGEAMDAELAVAPPGCSHLGSFKVDNWKQNLRAIYQCFVWSGTAEARKRKAKSCICHVCGVHLNRLHSCLYCVFFGCFTKKHIHEHAKAKRHNLAIDLMYGGIYCFLCQDYIYDKDMEIIAKEEQRKAWKMQGVGEKFSTWEPTKRELELLKHNPKRRKITSNCTIGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGHRSPHIPYKLLHLVWTHARHLAGYEQQDAHEFLIAALDVLHRHCKGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTT... | Function: Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a coactivator. Recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Requi... |
Q9FPS4 | MEVATSSTEITIQTDRDPSSNNNGSCAVASSTASAVFRKIEFHPARKPFNGFSNGRSDFKIETLNPCSSNQRLLSAPSAKKPDSSDLLEHGFEPDLTFSITFRKIGAGLQNLGNTCFLNSVLQCLTYTEPLAATLQTAAHQKYCHVAGFCALCAIQKHVRTARQANGRILAPKDLVSNLRCISRNFRNCRQEDAHEYMINLLECMHKCSLPSGVPSESSDAYRRSLVHKIFGGSLRSQVKCEQCSHCSNKFDPFLDLSLDISKADSLQRALSRFTAVELLDNGAKVYQCERCKQKVKAKKQLTVSKAPYVLTVHLKRFEA... | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by th... |
Q9FPS3 | MSEKKVFVFGSFTEHETRSFFEQKPTKDPQNSKDKCVGSIQFGSLNLAAENSSVNTNGELKKGEADGTVKSAGSQERLDASRPASSDKNNDSDAKLPRKNSLRVPEHVVQNGIIKEISESNKSLNNGVAVKTDPIGLDNLSMSDGESDPVYKASSSKFQALDNEDFSSDSSSGSIQRKKNLKVPTESVPPVKDFTPRGLINAGNLCFLNATLQALLSCSPFVQLLQKIQLQDIPKADSPTLAAFSEFISELDVPSSSSIRNNVTVVEAGRPFRPAMFEGVLRNFTPDVLNNMSGRPRQEDAQEFLSFIMDQMHDELLKLK... | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by th... |
Q9FPS2 | MGFKLQMSWMPSLLSQKRRNGPPLGLRNLGNTCYLNSVLQCLTFTPPLANFCLTHKHSSHCDTYVDGERKRDCPFCIVEKRIARSLSVDLTTDAPNKISSCLKIFAEHFKLGRQEDAHEFLRYVIDACHNTSLRLKKLRYNGNEPFNGNSVVKEIFGGALQSQVKCLSCGAESNKADEIMDISLEILQSSSVKESLQKFFQSEILDGNNKYRCESCEKLVTARKQMSILQAPNILVIQLKRFGGIFGGKIDKAISFGEILVLSNFMSKASKDPQPEYKLFGIIVHSGFSPESGHYYAYVKDSLGRWYCCNDSFVSLSTLQ... | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by th... |
Q9BXU7 | MAALFLRGFVQIGNCKTGISKSKEAFIEAVERKKKDRLVLYFKSGKYSTFRLSDNIQNVVLKSYRGNQNHLHLTLQNNNGLFIEGLSSTDAEQLKIFLDRVHQNEVQPPVRPGKGGSVFSSTTQKEINKTSFHKVDEKSSSKSFEIAKGSGTGVLQRMPLLTSKLTLTCGELSENQHKKRKRMLSSSSEMNEEFLKENNSVEYKKSKADCSRCVSYNREKQLKLKELEENKKLECESSCIMNATGNPYLDDIGLLQALTEKMVLVFLLQQGYSDGYTKWDKLKLFFELFPEKICHGLPNLGNTCYMNAVLQSLLSIPSFA... | Function: Deubiquitinase regulating several biological processes through the deubiquitination of components of these processes . Involved in somatic cell reprogramming through the 'Lys-48'-linked deubiquitination and stabilization of CBX4 and CBX6, two components of the polycomb-repressive complex 1 (PRC1) . Also deubi... |
Q99MX1 | MEPILINAQVQMWSAKAGMSKSRNALIETCVGKREVKLILYFSTGKIKTLQLHDNIKSVVLQTYGEDQNYLHLTFKNNDFLFVEKLTTTDARRLKRFLDKTSQGSIRPARSDERCGEPSTSAQELNGSGSSCETNSECFESPKESEMCMFRELSLLPSSSTFLHNVGLLENQFIKRKRFFSDLAKNEKQSNLKDSIRDFEANLVVCISNEKGKERNVREVDISKPGFGFPFETNYPEDSGVDVRDLNDLITKLFSPVLLETHCIENGLEWHEYMKTYLLYPEKLWQGLPNVGNTCYINVVLQSLCSIPLFINDLFNQGFP... | Function: Deubiquitinase regulating several biological processes through the deubiquitination of components of these processes . Involved in somatic cell reprogramming through the 'Lys-48'-linked deubiquitination and stabilization of CBX4 and CBX6, two components of the polycomb-repressive complex 1 (PRC1) (By similari... |
Q9VC99 | MQDLRNADTLRLPNGDGAAANDEVKSPFLIGVAGGTASGKSTVCKKIMEQLGQAEMDHTQRQVVSISQDSFYRELTPAEKAKAQKGLFNFDHPDAFNEELMYSTLQNILKGHKVEIPSYDYRTNSLDFENVLVIYPADVVLFEGILVFYFPKIRELFHMKLFVDTDSDTRLARRVPRDINERGRDLDAVLTQYMTFVKPAFEEFCSPTKKFADVIIPRGADNTVAIDLIVHHIGEILATTNSAQHSNTVRVAASSMKRDH | Function: (Microbial infection) Required for optimal replication of E.chaffeensis in the immune tissues, hemocytes, and fat body.
Catalytic Activity: ATP + uridine = ADP + H(+) + UMP
Sequence Mass (Da): 29213
Sequence Length: 260
Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: s... |
B9TQX1 | MNWNQIIFISLIATVLILAIANEAESAAVRTDKSDIKREDGENMKKRIFMQESEATAFLKRRGRRSTKSKDEVNAENRQRLAADERRREYYEEQRNEFENYVEEERDEQQERNREKTEQWREYHYDGLYPSYQYNRHHI | Function: May be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells in peripheral zones of fetal cartilage and at the cartilage-bone interface.
PTM: Proteolytically cleaved by a furin-like convertase to generate a persistent C-terminal fragment found in almost the entire... |
Q6NWB6 | MSWTQPALLTCLLVLSAITLFDGADSAVSDKRDAVNPQGALRKIFMPEADAASFFKRRSRRAVKTQDEINAEQRQRLAADERRREYHEEQRNKYENYAEEENDEQDERTREKTEQWREFHYDGLDPSYEYNRHTI | Function: May be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells in peripheral zones of fetal cartilage and at the cartilage-bone interface.
PTM: Proteolytically cleaved by a furin-like convertase to generate a persistent C-terminal fragment found in almost the entire... |
B9TQX3 | MSWTRVVVLSSLTTLLILTFSSVVKSAAVRDDSKAGDPKGAARHVFMPESDASNFFKHRSRRSPRYYSERQAEQRVRLSANERRREYNEEQRNEFENYVEEERDEQNERSREKNEQVREYHYDGLYPRYHWFH | Function: May be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells in peripheral zones of fetal cartilage and at the cartilage-bone interface.
PTM: Proteolytically cleaved by a furin-like convertase to generate a persistent C-terminal fragment found in almost the entire... |
Q14BU0 | MSWRRVILLSSLLALVLLCMLQEGTSASVGSRQAAAEGVQEGVKQKIFMQESDASNFLKRRGKRSPKSRDEVNAENRQRLRDDELRREYYEEQRNEFENFVEEQRDEQEERTREAVEQWRQWHYDGLYPSYLYNRQNI | Function: May be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells in peripheral zones of fetal cartilage and at the cartilage-bone interface.
PTM: Proteolytically cleaved by a furin-like convertase to generate a persistent C-terminal fragment found in almost the entire... |
Q96RP3 | MTRCALLLLMVLMLGRVLVVPVTPIPTFQLRPQNSPQTTPRPAASESPSAAPTWPWAAQSHCSPTRHPGSRIVLSLDVPIGLLQILLEQARARAAREQATTNARILARVGHC | Function: Suppresses food intake, delays gastric emptying and decreases heat-induced edema. Might represent an endogenous ligand for maintaining homeostasis after stress.
PTM: Glycosylated.
Sequence Mass (Da): 12146
Sequence Length: 112
Subcellular Location: Secreted
|
P08067 | MLGIRSSVKTCFKPMSLTSKRLISQSLLASKSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAGAKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVKWQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDPQWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGDKVIVG | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehy... |
Q9SG91 | MGKQPVKLKAVVYALSPFQQKIMTGLWKDLPEKIHHKVSENWISATLLVTPVVGTYWYAQYFKEQEKLEHRF | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
Q9FLB7 | MGKQPVKLKAVVYALSPFQQKIMTGLWKDLPEKIHHKVSENWISTILLVAPVVGTYSYAQYFKEQEKLEHRF | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
Q94K78 | MAGTSGLLNAVKPKIQTIDIQAAAGWGIAAAAGAIWVVQPFGWIKKTFIDPPPTEEK | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
A0A411KUP5 | MIIQGNQLDSLPKAEDWEAFAESYKRIAEVAVMKPVQALLQCLDDRLPLSGAVGILDNGSGPGIIMSSLIERYGPQLPPDCVLTCVDYAPAMIDQVDKARIKAVEEDADSAWGRVEGKVLDALDLHSIADESQSHIAAGLLYNLTTDPAKCLSECKRTLQPGGVLAVSAWEGNDWIEMLRVVPLIKPDLKTAIQPKWSTVDAVRWDLELAGFREVHVQRIPIKIPFTSHALFVDTLMRYQPRMVAMLRTFTEDEKTELRRLLMNEMKVICPSQPGMMSGAVMVGAGVR | Function: Methyltransferase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused with a... |
A0A411KUP9 | MYPFFTYSPGRHYFEYKWYNLELLRLIGSAPYGGCDAAEFLELVASLKPNDADEWHHKFLALAERTQAKGEQMSEAGHEAVARGAYLRASNYFRCAQYMFPIMPAARQGEFLKLYHRSIRSFEQAAELMEHRVERVSIPFQPPEYRAPAVELPGWLHLPAAHQRLSGRKTPLLICVGGADSTQEELYFLSAAEGPGLGYAILTFDGPGQGLTLRESGVPLRPDGEVVIEAVLDFIESYAAEHPEADLDVDAISITGQSLGGYLALRGAADPRIKACVAVDPIYDFYDLAMSRMPRWFMWPWERNYMGDGFVDFAVIEHSK... | Function: Alpha/beta hydrolase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused wit... |
A0A411KUX1 | MSRNSGTTLEDGPLHADPTTEAPNNATVTTNVTANDENTEKEVDADAAAAAPAEAPKPNQGFRFWAIVAALAFTALLSSLEGTIITSALPKITADLGGGNSFIWVPNGYFLATIVMLPLMAQASNLFGRRWLTLISVATFTLGSGICGGANSQAMLIGGRVVQGFGGGGIALMINIILTDLVPLRERGKYMGIVQMVSAVGAALGPFLGGLLTSKSTWRWVFYINLPIGGTSLVALFFFLRVAKPPPTTLAEKISRIDFSGNAIFIASTVSVLIGVTWGGAVYPWSSFRVIVPLVLGFFGLGLFVVYEWTVAKNPSLPKD... | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused wit... |
A0A411KUU9 | MATRTADKLEKKLVVVVGGTSGLGFAVAQAAVDRKANVVVASSKQASVDDALSRLQAGLASDDDVARVRGLTLDLAAANVEEQIVALYDFASKNGQQKIDHIAVTAGDSLYPKALDQVKAEDFINASQVRVIGALLLAKHAAKYLAKSAASSFTLTSGVRDVRPAANFAPVAPVSAAVKSLAKTLAHDLAPIRVNSISPGAVRTEFFTKIAGEHADAVLQGLAEQTLTKSNGVAEDIAEIYLVVMTSAYIDGADLVADGGSLIA | Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone... |
A0A411KUQ7 | MGVPLLDVSQLQAGPEARKQYLQALVQSFRDYGFVRLTKHDVPAKRVQRIFDLSTQMFNLDIDSKLEFANIADGSPQRGYSAVGVEKTASLHGNLIGRRVDEKLTDAREHFDCGSPLDKSFANRWPEKLQGFQQELESFYFELEQVTAGILGSLEEALNCPPGTLNNMITKENNASELRLNHYPPVPAGTLRNGNVARIWPHFDLGVITLLFTSAVGGLEVEDRNAPGPQTFIPVEPETEAELIVNISETLQRWTDDHLPAGLHRVTIPKDLDTEIQNDANVEIPGRYSIAYLCKADREADVGTLPVFQTGEAPRYKAMT... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds sh... |
A0A411KUQ8 | MRNGAHRCESAMPGVTMTVLGCGKLGTAIIQGLLRSCPKASEAAPQKYLYPISTVIAAVRSKDRLESLIKSLVAEINDHTCPLDFVIANNVEAVRRADVVFLACHPNQATECLGGIGMQDAISGKLVISVLGGVSVATLEQAVYSSTRRPASGQAPCHIVQAIANTAAARQQSVTVVAEEETANSHEKGSLCEDVLRRLGQVSYVSPDLMPAVTALCASGTAFFTTYLDAMIQGAVSEGLGEDVATRLAALTMAGAANAVISGEHPAAVTSRVTTPGGVTAEGLKVLREGDLRTLTAKAISATTRRLRLVDEKSRKQS | Function: Pyrroline-5-carboxylate reductase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone c... |
A0A411KUQ1 | MARINRQTAYQKAQEIEFSTSSADPLAAWRISGIKGTAWEQWYFDSIADDGKSGIVLTMARDASYTVLGRGVLRVELDVTFEDGSHHNHVDWMNEAIVEDRSSPKSTGTIDGVWTAPGKSIRFQIAADGSAAKVEVDTPETKGHFTLAALSPPMYPNGETQNELESQGKVASTELLPKIHLVQVIPTATFEGDLMVNGRLLRFRGIGGHMHAWAQGAWFDTTLGWKVARGVAGPFSVTLMEYTDMEGIVHSSGYVVEDGVKRFGGLETYATPRSSATSQQVLKYRDEDRKGKQTVRWTPTYNTGFAGRFGDSSTGAILQF... | Function: Diels-Alderase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused with a ga... |
A0A411KUQ9 | MSPTDMKAVVFYGPHSIAIESRPIPKVQHDKDIVVKVSASGLCGSDLHYFRGHEVVDSAGFIMGHEFVGEVVEAGRAVTTVRPGDKVVSPFTVSCGDCFYCKLQNSSRCVHCQVFGSNGLDGAQAEYVRVPLADSTVVRAPPGLSDDALILMADIFPTGFFGARNAMAGLGAQDPTEAVVVVIGCGPVGLCAIVSALEYRPRVVFAIDSVDSRLGLAEKLGARPLDLKKGVPSIISAVQEVTEGRGADAVVEVVGQGPALRTAYDIIRPFGSISSIGAHHSAMPFSATDGYE | Cofactor: Binds 1 zinc ion per subunit.
Function: Medium chain reductase/dehydrogenase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds shar... |
A0A411KUU5 | MTKKIFATGATGYIGGDAIYALLSASPEYEVSCLVRSGAKATELVARHPSVRIVDGTLDDLELLEEAAANADIVCNFAHATHEPSVSALAKGLARRQRPGHGYLIHTMGSGTMIYDDVIQRRFGEHSDKVFNDVEGLPEVLAVPDFAKARGAENAVRDVGVKNPDRVRTAVVCTGSAYGPGRGLVEYRTSAIHELVRCTLSRGHALQVGAGKSAWRNVYIRDLSDVFVKLITHATNDEQDSDNTDESVWGGSGGYYFVENGEHVWGELARAISDEAVAQGLIQGGDIESIDAAEAASLAPMCNFFWGCNARVEGRRAARG... | Function: Oxidase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused with a gamma-lac... |
A0A411KUQ5 | MALLNTPVLAAATAVSFGFYLAGLFVYRVFYHRLSHIPGPRLAAFTVYYQSYYDFFPHQGQFLWKLVELHKAYGPIIRIGPDEVHVNDARFYKEMYGSSVHKRNKSPIWYWMDGLGAVGDQSMFITLDHDHHRLRKAGLGTYFSKRKVQELEPRVKEKVLLLRQRLLERAGRGAINLKDAFGGMALDIITQYCFNQCMGALDRDDLGREWNQLMAAGVKINPFARTFPTVARTLLRLPKWVLGVSGMVSTTGEFLDLADRLSANARNEAIRDLQEGKYTLTDDADSRTVLHSMMRSDVLPEHEKGERRLQADGMTLIAAG... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core ... |
A0A411KUQ4 | MGSLIQTPSTQTAVVTTAEGRHQVAHGRRVPSCGPRSVLVRIKAVALNATDHKMPARVKREGLTSGCDFAGEVVAVGEQANDEPRRCELPRSWAPGDRVFGVVYGSNPGQPEWGAFAEYVEADPIMLCHVPDGWDWETAASVGGSVHGSVALCLFGDGNLALDYSNLKAQADSSSADAVTNQSPKPESFTKEELRKVVLVYGGSTACGTMALQLLRLAGYTPITTCSPRNFGLVESYGAVAAFDYHSETCATEMKTYTRSSLVAALDCLGNTQSAALCYAALGRAGGRYVALEKYPDSVSATRKLVKPSWVMGPVMFGRE... | Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused wi... |
A0A411KUQ2 | MKHADPLRADTLGTAPLSQAIEAHHHGKEREAHRQSLSSVPGDTVVEAPEKVVDLEINSVDNDKEHHRAPTRDEIQTLRKVPGSIPATAYLLCFVDFAERASWFGARSVSSNFMQFPLPEGGNGAGAPPSGSELPAGALGHGQRFSVALGLVFSFLSYVIPIFGAWLAEAKVGRYRTILIGVLIGGVAHIIMIAGAVPSILQAGKGTAPFLVSLFLLALGAGLFRPNVSPTVLDQHRHYQPFVKELPSGENVIIDPEATMQRIMLIFYALINVGAFYSLATVYSEKLVGYWLAFLLPGIIYLLLPLMLWYLNDKLIKVPP... | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties . These compounds share a hemiaminal-containing pyrrolizidinone core fused wit... |
P22309 | MAVESQGGRPLVLGLLLCVLGPVVSHAGKILLIPVDGSHWLSMLGAIQQLQQRGHEIVVLAPDASLYIRDGAFYTLKTYPVPFQREDVKESFVSLGHNVFENDSFLQRVIKTYKKIKKDSAMLLSGCSHLLHNKELMASLAESSFDVMLTDPFLPCSPIVAQYLSLPTVFFLHALPCSLEFEATQCPNPFSYVPRPLSSHSDHMTFLQRVKNMLIAFSQNFLCDVVYSPYATLASEFLQREVTVQDLLSSASVWLFRSDFVKDYPRPIMPNMVFVGGINCLHQNPLSQEFEAYINASGEHGIVVFSLGSMVSEIPEKKAM... | Function: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile . Essential for the elimination and detoxificatio... |
A8MRY9 | MRNNPVLPVSDPPLAGENDSDGKGVDDRLFKGSAMTKRGAYAALSYMACAVMLVLFNKAALSSYDFPCVNVITLFQMVSSSLFLYALRRRKIISFTAADSFSIDSASTFVPVKTLFHTLPLAIAYLLYMLASMASVRGVNVPMYTTLRRTTVAFTMVIEYMLTGQRYTRSIIGSVGIILLGAFFAGARDLSFDFYGYGVVFLANISTAVYLATIARTGKSSGLNSFGLMWSNGIICGPILMIWTFICGDLEKTINFPHLLTPGFMVVLLCSCVLAFVLNYCIFLNTTLNSALTQTICGNMKDLFTVGLGWMLFGGLPFDL... | Function: Mediates the transport of UDP-N-acetylglucosamine (UDP-GlcNAc) across the Golgi apparatus membrane . Delivers an essential substrate for the maturation of N-glycans and the GlcNAc-containing glycosyl inositol phosphorylceramide (GIPC) class of sphingolipids in the Golgi apparatus .
Location Topology: Multi-pa... |
Q9UTF8 | MNPYRPYVVVNNVEPTFSITPEPTFETQPTISKSEIFETLRSILVTKYLTTFFVQPLEVAKTVCQVEEYLPKRTKIERDGKQTKEPYDEDIPDGTEQEGLSDDEHEIYAYFETPTTEKAVTEQLAEKLCVDASGYVTDPSNLIERSYTIHSKRFSIKSIISELWEKEGARGLWKGHTISFLHNLLYSGLQSWLSATLSGALAIADPNIISPIDSVRPLLSLFIKSITSAISALILSPLDIARTKIILFPISSSSYLSSASETSGNSHKKFKPLTIRQCLKALPFYCPSSLILPTVCYVSLPPFVSSVLPLTFRNFLGSSP... | Function: Required for mitochondrial fusion as well as normal mitochondrial morphology. May coordinate fusion of inner and outer membranes during mitochondrial fusion (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46910
Sequence Length: 421
Subcellular Location: Mitochondrion outer ... |
Q03327 | MNNNNVTEATSRAQIRPYYDPDSFNAGYSAVFKPDEGVVDPHGYTIASKLNVINSSPTTKRMANALFKSSPMKKLSNSVNDGLSLEGSNGEITGLNNFEWAELVNIQKWRKIFEQLLDMFFRKYFQLLIQQPFDVARLLIQVGEFKIFKTTVDTNKPQAPIILRDEEGDGAAREGEEDAYDEEEIDFFPIERKIAEANSTAPIMAEETDHSHHEPTDISLTIAPQSLHTIDVINALFDQEGIRGLWKANNTTFIYNFLSLSIDTWFTGLLSSFLGVPDPYFMEVINSPDISKSFILALGAGVFTSIILLPVDLIRTRLIV... | Function: Required for mitochondrial fusion as well as normal mitochondrial morphology by bridging the essential interaction between FZO1 and MGM1. May coordinate fusion of inner and outer membranes during mitochondrial fusion.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 57543
Sequence L... |
P08800 | MTDTATSKATVERPKLQSTGSLHSLFKNVDLFSENDEELYPPLQHGARFAAPIEDSTLLALGMKPDELKAFQKQRHAYINKDQIYTDEIKIPNKTEMVDYHQLHLVSPIDQSNASRLLNKLVVIKLNGGLGNSMGCKTAKSTMEIAPGVTFLDMAVAHIEQINQDYNVDVPLVIMNSYKTHNETNKVIEKYKTHKVSIKTFQQSMFPKMYKDTLNLVPKPNTPMNPKEWYPPGSGDIFRSLQRSGLIDEFLAAGKEYIFISNVENLGSIIDLQVLNHIHLQKIEFGLEVTNRINTDSTGGILMSYKDKLHLLELSQVKPE... | Function: Plays a central role as a glucosyl donor in cellular metabolic pathways. During development the lack of the enzyme activity leads to cell death and lysis. Strains which lack UDPG pyrophosphorylase accomplish early developmental events but are unable to culminate. The enzyme affects the growth rate of the cell... |
Q8SSC5 | MQESRSKESTLSGDEDKDVHRFLDEFDDKCTCKLLKEMKETLEGLKKSHPNPTNLDEFYRLFERYLRTRHEKIVWEKIRSPKDRIVQYNEIPEPTEKSKELLRKLAILKLNGGLGTTMGCVGPKSAITIKDGKNFIDLVVKQIRYLNSKYKIDVPLILMNSFNTEGMTDKIIFRYDGIKKFSQSKFPRISSETLLPVSPSHGDKGMYPPGHGDLFYSMKNSGMLEELLEGGYEYLFVSNIDNLASTVDLKLLEYFATNELGFLMEVTDKTRADVKGGTLIEYKGALRLLEIAQVPSNKKSEFTSFKKFTIFNTNNLWINL... | Function: Plays a central role as a glucosyl donor in cellular metabolic pathways.
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
Sequence Mass (Da): 55910
Sequence Length: 492
EC: 2.7.7.9
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P32861 | MSTKKHTKTHSTYAFESNTNSVAASQMRNALNKLADSSKLDDAARAKFENELDSFFTLFRRYLVEKSSRTTLEWDKIKSPNPDEVVKYEIISQQPENVSNLSKLAVLKLNGGLGTSMGCVGPKSVIEVREGNTFLDLSVRQIEYLNRQYDSDVPLLLMNSFNTDKDTEHLIKKYSANRIRIRSFNQSRFPRVYKDSLLPVPTEYDSPLDAWYPPGHGDLFESLHVSGELDALIAQGREILFVSNGDNLGATVDLKILNHMIETGAEYIMELTDKTRADVKGGTLISYDGQVRLLEVAQVPKEHIDEFKNIRKFTNFNTNN... | Function: Plays a central role as a glucosyl donor in cellular metabolic pathways.
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
Sequence Mass (Da): 55988
Sequence Length: 499
EC: 2.7.7.9
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Q9M9P3 | MAATTENLPQLKSAVDGLTEMSESEKSGFISLVSRYLSGEAQHIEWSKIQTPTDEIVVPYEKMTPVSQDVAETKNLLDKLVVLKLNGGLGTTMGCTGPKSVIEVRDGLTFLDLIVIQIENLNNKYGCKVPLVLMNSFNTHDDTHKIVEKYTNSNVDIHTFNQSKYPRVVADEFVPWPSKGKTDKEGWYPPGHGDVFPALMNSGKLDTFLSQGKEYVFVANSDNLGAIVDLTILKHLIQNKNEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKKLVEADALKMEIIPN... | Function: Converts glucose 1-phosphate to UDP-glucose, which is the major glycosyl donor for polysaccharides. Acts redundantly with UGP1 and is essential for the synthesis of sucrose, starch and cell wall, and callose deposition.
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-g... |
Q54YZ0 | MMKPDLNSPLPQSPQLQAFGSRSSDLATEDLFLKKLEAISQTAPNETVKNEFLNKEIPSINKLFTRFLKNRKKVIDWDKINPPPADMVLNYKDLPAITEQRTSELASKLAVLKLNGGLGTTMGCTGPKSVIEVRSEKTFLDLSVQQIKEMNERYNIKVPLVLMNSFNTHQETGKIIQKYKYSDVKIHSFNQSRFPRILKDNLMPVPDKLFGSDSEWYPPGHGDVFFALQNSGLLETLINEGKEYLFISNVDNLGAVVDFNILEAMDKNKVEYIMEVTNKTRADVKGGTLIQYEGKAKLLEIAQVPSSKVEEFKSIKKFKI... | Function: Plays a central role as a glucosyl donor in cellular metabolic pathways.
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
Sequence Mass (Da): 56268
Sequence Length: 502
EC: 2.7.7.9
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O59819 | MLHRRIHFKSQSTLDFDSVAVSISASTMKNELDKLVLNSRVSDKKTFGIQMDNFFALYRRYLLHTVKGYECDWDSIRPLGPEDMIDYGDLPLCKNAGKYLNRLAVVKLNGGMGNALGVNYPKAMIEVRDNQSFLDLSIRQIEYLNRRYDVSVPFILMNSYDTNDETCKVLRKYAGCKIDISTFEQSRYPRVFVDSQLPVPKAAPSPIEEWYPPGHGDIFDALVHSGTIERLLAQGKDYLFVSNIDNLGASVDLNILSHVIDNQIEYSMEITDKTKADIKVGILVNQDGLLRLLETNQVPEQHREEFMSDKVFKYINTNNV... | Function: Plays a central role as a glucosyl donor in cellular metabolic pathways.
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
Sequence Mass (Da): 56740
Sequence Length: 499
Subcellular Location: Cytoplasm
EC: 2.7.7.9
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P38709 | MTVFSGVNKIEFEGTFEGIGKDVVMSQMIRALQKHFPSIRDKNYEFSLFLHIFQRYVLENTSITHDLVCDKIRLPIIDEVVELDDIKNYGLLEGKLLSKLAILKLTGKANPIIGKESPLFEVKNGMSSLDVIVRQTQNLNVRYNSDVPLIFMTSLETESQVSNFLEEHYSSSKVRWKTVVQSSFPQIDKDRLLPIDLQINSHENDFWYPCGTGNLTDTLYFSGELDKLIAQGKEILFVSNVDNLGATGDLNILNFIINEKIEYLVEVVERTANVSNTGVLATYKGKLRSVYYNCLSNESASTCRIVNTNNIWIDLKKLKV... | Function: Plays a central role as a glucosyl donor in cellular metabolic pathways.
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
Sequence Mass (Da): 56000
Sequence Length: 493
EC: 2.7.7.9
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F4IY62 | MANPQASPILHHPQNHLSLFHFRTTTSPRSFSSLHFRKPLLFLSSSSSFSSKLQQSEQQCNNHQVRHVSTVPVEYSTPTPPESDDFLSEIDRLKSLLSKLDVSKDLRRKDAVIDADSRVRRFFSENRGGLSKVFGYLGLNSNEMFLVKCVIAAGQEHALCMNYEEAFGEEEEEYTVRSSVKNALYALVEMIERFDVNSSGYKGRREMGTVLDSEEIAHFRKFLTFLEEIEQFYDCIGGIIGYQVMVLELLHQSSKRRNTNRSQLVEESLGCQYLEMHTPSVLDLTQEEDYASQAALWGIEGLPDLGEIYPLGGAADRLGL... | Function: Involved in the biosynthesis of sulfolipids in the chloroplast. Catalyzes the first committed step in sulfolipid biosynthesis. Converts glucose 1-phosphate to UDP-glucose, the precursor of the polar head of sulfolipid. In addition to glucose 1-phosphate, can use galactose 1-phosphate, but with much lower acti... |
Q7CRU3 | MQSVVFPNKILPYLLVAPQIILTVIFFFWPASQALYQSTMREDAFGLSSNFVGLANFSAVLSDESYLNSLKVTVIFSVLTALVSMGLALLLATAADRVVRGKGFYRTMMIMPYAVAPAVAGMLWLFMFNPAMGTLSYILRRNGIMWDPLLDGNQAMLLVVAAAAWKQISYNFLFFVAGLQAIPKSLLEAASIDGARGSRRFWTIVFPLLAPTTFFLLVVNTVYAFFDTFGIIHAVTGGGPAKATETLVYKVYNDGFVNLNLGSSAAQSVILMVIVIALTAFQFRFVEKRVHYG | Function: Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32198
Sequence Length: 293
Subcellular Location: Cell inner membrane... |
Q18081 | MLLRILTFLAVCQVTTSHKILMFSPTASKSHMISQGRIADELANAGHEVVNFEPDFLNLTDKFVPCKKCRRWPVTGLNNYKFKKIQNGLSGDVFQQSSIWSKIFNTDSDPYQDEYTNMCEEMVTNKELIEKLKKEKFDAYFGEQIHLCGMGLAHLIGIKHRFWIASCTMSVSMRDSLGIPTPSSLIPFMSTLDATPAPFWQRAKNFVLQMAHIRDEYRDVVLTNDMFKKNFGSDFPCVEFLAKTSDLIFVSTDELLEIQAPTLSNVVHIGGLGLSSEGGGLDEKFVKIMEKGKGVILFSLGTIANTTNLPPTIMENLMKI... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59627
Sequence Length: 526
Subcellular Location: Membrane
EC: 2.4.1.17
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A0A291PQG3 | MTLLRDLLLLYINSLLFINPSIGENILVFLPTKTYSHFKPLEPLFQELAMRGHNVTVFSGFSLTKNISNYSSIVFSAEIEFVNIGMGNLRKQSRIYNWIYVHNELQNYFTQLISDNQLQELLSNKDTQFDLIFIELYHVDGVFALSHRFNCPIIGLSFQPVLPIYNWLIGNPTTFSYIPHVYLPFTDIMSFWKRIINAVFSIFTAAFYNFVSTKGYQKHVDLLLRQTESPKLNIEELSESLSLILAEFHFSSAYTRPNLPNVIDIAGIHIQSPKPLPQDLLDFLDQSEHGVIYVSLGTLIDPIHTDHLGLNLINVFRKLR... | Function: Catalyzes the transfer of a glycosyl group from a UDP-sugar to an acceptor molecule.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 58644
Sequence Length: 504
Subcellular Location: Microsome membrane
EC: 2.4.1.-
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Q22295 | MHYSQMRWMFFCLTALLHGSFIVNAAKILVYCPSISKSHVLLCSKYADLLHNAGHDTVLFIPSYSKLLDNYDGAKHAKVWRLHNVTEAYDTKLGTLANVMENSHIGFIDRLTFDADFWIDMCADLLGKLPEMQHIIDYKFDLVIYNEIDPCTPAIVRLFNIPKTVLLSSEAIMDKVAWNLGLPTLPSYVPSVEENPNHDRMSFFERMSNVYKFFQSIVVHYLQDIHVLNLFRKEVSSDFPSIAEIIRNVSLVLVNTDEIFDLPRSYSSKFVYVGMLEAGKDENVTLPKKQDDYFKKGKSGSVFVSFGTVTPFRSLPERIQ... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 60286
Sequence Length: 523
Subcellular Location: Membrane
EC: 2.4.1.17
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Q22180 | MQLLTLPTLIFIFLNYGTPCLSLRILVYSPRMIPSHVAFVANIANLLGQRGHNVVVVDNVLRSDISNKLDLKVIEKVVKVETSANVAKLLADQSIPINFWSMRNEPEEQKKVMKQLGIIFLEQCKYLVSKEETVFNELKHLEFDFGIHEVFDICGIGIFEKLGIRKSVILSSTGMRDIVNEALGISSQLQDASILSDYGNSIPFYGIRRNLKFHSAWRNFFEVQSKTLEPLFETTSSFENLLRFSNLMFLNTHELADAHRPWSRRVHEIGGISFKFPMPLKNEYINLFNKYNSIILVSFGTTTPSFLMPEKYKNTLINTF... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58929
Sequence Length: 512
Subcellular Location: Membrane
EC: 2.4.1.17
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Q22181 | MLWAFIVWLGALCIYGSAFDILIYAPRMMQSHVYFTARIANVLAARGHKVTVIDNVFRYDVDNELSSDIHEIISVEPSPEVTKLLNTGSLPTILWNSKASPEEQRTIMEGLGHVHRLQCTHLIENSTLIPKLQEIKFDFAIHEVFDSCGVGILEVIGVQKTVIVSSTGPMDVVPITLGISDTLNTPSLLSDYGSYLSFFEKRRNLKFLSGMLNFHEMQDSMISPLFKKYYGLKKPTGEIMRQANLLFYNIHEGSDGMRMRGRRSFDIGGIAFKDQKNLTMEYQTLLSDPRPKVLVSFGTAATSSHMPQNLKNSLMTAMKQ... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59284
Sequence Length: 524
Subcellular Location: Membrane
EC: 2.4.1.17
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Q20086 | MKSWLLLLGTIGWVTAGDVLFIPSTLYPVHAQTMSVLARELAERGHKVTWLEIGPERSDIVLHQQVSREFWPAQFGDRTLQEIYQFKNHTSHSELWNPQYTNENEQTTGWLASIRLCDSVLSRSKSKFDKMVEKQFSTVIVDDLYNSCGVLMAGLKKSVYIYWSMTGLRTESAWANQSPSPPSYLPVAGTGLTDDLTFSQRLYNVASYFKQLYIHQHIVQPRIDAVFQKYYPGVESTFEIERNASINFVNTPPIFDFSRPYMPRVNFIGAIQCRKPKELPKEFTSWISAYPDGFVVLSTGFTVQWNKSPEHIRQAYLDTF... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 61143
Sequence Length: 533
Subcellular Location: Membrane
EC: 2.4.1.17
|
A0A291PQF1 | MIFFYFLTLTSFISVAFSYNILGVFPFQAKSHFGFIDPLLVRLAELGHNVTIYDPYPKSEKLPNYNEIDVSECFVFNTLYEEIDTFIKTAASPFSSLWYSFEETLAVFQKENFDKCAPLRELLNSTVKYDLLITETFLTDITLLFVNKFKIPFITSTPNVPFPWLADRMGNPLNPSYIPNLFSDYPFDKMTFFNRLWNTLFYVMALGGHNAIILKNEEKINKYYFGSSVPSLYNIARETSIMLINAHETLNPVIPLVPGMIPVSGIHIKQPAALPQNIEKFINESTHGVVYFCMGSLLRGETFPAEKRDAFLYAFSKIPQ... | Function: Catalyzes the transfer of a glycosyl group from a UDP-sugar to an acceptor molecule.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 60071
Sequence Length: 526
Subcellular Location: Microsome membrane
EC: 2.4.1.-
|
P34317 | MYLPIFCIFLSVVDSLRILQIVPGFTNSHVLFNYRLAETLRFLGHDVKMWTQMEMAMLDTGNNKLPEGVSEYRIPIHFTDTLKTEGLKVFQSMMFESGDAHDLWWTGQEFKDMRVEACEQMLRHDESVYEDFRKDGFDVAIAHFHDLCPLAIAKKMNVKRVIWITHGTSIYEFSAVQLGLRTIPSTIPHPLSSAGFSQLFLDRVQNTLWHLSLLDFVNLPQNLLVDENLFYREFVGADQDDLWDLAKTTVPSLLINGDRMLDFPRPLPIHIAFSGELGVSKGKKLVMEKWLEDIIEKPSDGLIVFSLGTVSNTTNMPAQM... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57727
Sequence Length: 507
Subcellular Location: Membrane
EC: 2.4.1.17
|
F8WLS6 | MGSLSSSDYSKKPHAVCIPYPAQGHINPMLKLAKLLHYKGFHITFVNTEFNHKRLLKSRGSDSLKGLHSFQFKTIPDGLPPSDVDATQDIPSLCESTTTHCLVPFKQLLQKLNDTSSSEVPPVSCVVSDAVMSFTISAAQELDIPEVLFWTPSACGVLGYMHYAQLIDKGLTPLKDASYFSNGFLDQVLDWIPGMEGIRLRDLPTFLRTTNPDEYMIKFILQETERSKKASAIVLNTFQELESEVIDSLSTLLPPIYPIGPLQILQNQVDDESLKVLGSNLWKEEPECLEWLDTKDPNSVVYVNFGSITVMTNDQLIEFA... | Function: Iridoid glucosyltransferase acting exclusively on 7-deoxyloganetin. No activity with 7-deoxyloganetic acid.
Catalytic Activity: 7-deoxyloganetin + UDP-alpha-D-glucose = 7-deoxyloganin + H(+) + UDP
Sequence Mass (Da): 54611
Sequence Length: 487
EC: 2.4.1.324
|
F8WKW8 | MFPWLAYGHISPYLELAKRLTDRGFAIYICSTPINLGFIKKRITGKYSVTIKLVELHLPDTPELPPHYHTTNGLPPHLMATLKRALNGAKPELSNILKTLKPDFVIYDATQTWTAALTVAHNIPAVKFLTSSVSMLAYFCHLFMKPGIEFPFPAIYLSDFEQAKARTAAQDARADAEENDPAAERPNRDCDSIFLVKSSRAIEGKYIDYLFDLMKLKMLPVGMLVEEPVKDDQGDNSNELIQWLGTKSQRSTVLVSFGTEYFLTKEEMEEIAHGLELSEVNFIWVVRFAMGQKIRPDEALPEGFLERVGDRGRIVEGWAP... | Function: Glucosyltransferase catalyzing the beta 1-6 glucosylation of the sugar moiety of crocetin glucosyl esters to produce crocetin gentiobiosyl esters. Weak activity toward curcumin glucosides, but no activity with flavonoid glucosides, coumarin glucosides, 4-nitrophenyl glucoside or crocetin. Involved with UGT75L... |
E7CQW6 | MSPSSHKPLILACGLPLSGHIMPVLSLVHGLTDDGYEATVVTGRAFEQKVRDVGADFVPLEGNADFDDHTLDDLVPGRKDMAPSFDRTVQDVEHMMVATLPEQFAAIQRAFKKLSASGRPVVLVSEVLFFGAHPISLGAPGFKPAGWICLGVLPLLIRSDHTLGLDNDRSPEAHAKKLAMNHALEHQIFVKATAKHKEICRELGCTEDPKFIWEHSYIAADKFLQLCPPSLEFSRDHLPSNFKFAGSTPKHRTQFTPPSWWGDVLSAKRVIMVTQGTFAVSYKHLIVPTLEALKDEPDTLTVAILGRRGAKLPDDVVVPE... | Function: Catalyzes the first glycosylation step of sophorolipid biosynthesis, the coupling of glucose to a hydroxylated fatty acid to give rise to a glucolipid . Can glycosylate all hydroxyl fatty acids generated by cytochrome P450 monooxygenases CYP52M1, CYP52N1 and CYP52E3 into their corresponding glucolipids. Main ... |
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