ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A4G5P1 | MPDIDKHKLSLSFSRAAAQYDAIAGFQQQVAARLAQLLPAIPATCVLDGGCGTGTSSALLTRHWPDALLLACDLSPEMVRQAHARQLTAVCGDLEQLPFSKACFDVVWSSLVLQWCQPQLAYPELQRVLKHGGRLLFSTLTSGSLHELESTFGEIDRHRRVLPFASEQQVVDALYAAGFEHVQCQAERWVTQHADLKTLLTSIRGIGANQTGAARRPGMMGKTQWQAAQVRYENLRDADGMLPLTYSLLFVSAEKSRAQD | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-... |
C1D5S5 | MTEAFYTDKSRVRASFDRAAATYDRAAVLQREVCDRMATRLDLIRHAPARVLDAGSGTGYGAGLLRARYPEAQVTELDLAPSMLRASRDKQLPQGRLRRLFARAPALVCADLEQLPLASGSLDMVWSSLALQWLNTPDAVLAEFHRVLRVDGLLMFATLGPDTLKELRQAFAGIDGATHVNQFIDMHDMGDALVRAGFATPVMDVERIVLTYDEVKAVMRDLKAIGAHNATAGRGRGLMGRQAWQRIEAAYDRLRQDGRLPATYEVVYGHAWRPAARPRRKLDDGRDIIEFHPHAPA | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-... |
Q5ZT34 | MTVNNEISKAFSKHADDYERVAKVQKEIGSRLFERLQYLKIAPRRILDLGCGPGFFSKELALLYPKAQIVGMDLSFAMLEQARKKQGWRRKWPLVSADMQKMPFATGAFDLVFANQVIHWSSSLGMVFRELNRVMNVNGCLMFTTLGPDTFKELQTAWSAANQYAHVNEFVDMHDIGDCLIAEHFMDPVIDMELLSIHYETLPQLLLALKTQGVRNINPKRNHGLTGKSAWKQFEAQYATMRTTTGKYPLTYEVVYGQAWKGAQRKMEQGIETWIPVSRVVKKS | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-... |
A0L3L9 | MNLPNRGEGNRNGRVGKNFGRALNYHRKALVQQHVADELAERLVDFPLPERPRVLEIGCGTGFLSRHLMRQWPGGSFLFTDISAPMLVRCQSHLSDLPGQRQFMVMDGEHCAVRGPFDLVVSSMAMQWFGDLPGALQGLSSLLKTNGMLAFATLGDETFREWRGVCAQYGSPFGRPDYPDVAQLQEMWPSGGEGDVEEDHIPVAHSSGHGFLRALREVGAHQPSGQHRPVSAALMRRMLQATRGGQHGFTVTYHVLYGFYTRSFDDRPIH | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-... |
A6W0X8 | MLITPDISALSYKRQLAKRFDRASQSYDSYADFQKVVLERLLAMLPLNQADVVLDLGTGTGQALGILSERLNPKCNIALDLSLQMLAVASERFSSLHNTHYVCADAERLPLQDRSCDLVFSSLAIQWCLSPLDLFKELYRVIKPGGYVVFSTLSQGSMPEISKAWFGLDNKEHVHQYMASDALLDSIRASELNLLSSQLSNISMWFDSPESAIYSLKKVGASLIASDGDPSVSPSKWKAFLLEYEKQRNELGIPLSYQVSFVVAQRPNSI | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-... |
Q609U9 | MNSLPRPDIGPFADTPEKRWVGVSFGAAAVGYDGVAALQREVGESLLAGIRHLGPPPARMLDLGAGTGHFSGLLVAAFPTAECLALDIAEGMLRFLRSHRPGADGMGLVVGDAEALPLADESVDLIFSNMAFQWCERLDRAISECCRVLRPGGRLAFSTFGEATLAELRMAWRAVDGYTHVNAFATRRSVEQELRAQGFTKIRLDARTLRRGYPSVLALMKELKALGARNLTRNRPRHLLSRHTLERVSEAYGRLPGMASAVTASFEVLTALVEK | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-... |
A1U4A9 | MAKHTFFVTGTDTGVGKTIVSAAILEAAKAAGKRTLAMKPIASGCDQTPEGLRNEDALMLQAAITEKLPYDTINPIALEPAIAPHVAAQQAGKQVTAQRIVGFCRGMQIRPADLLLIEGAGGWRVPLNDRETYAAVPGELKLPVILVVPLQLGCINHAMLSAEAIRADGLVVAGWVGNHPEEQVMSCEQDTLNYLSTHLGAPCLGVLPWLENTDTAEMPAILSRYLNITPLIEN | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 ... |
Q58695 | MIFITGTDTGIGKTYVSSILAENLKKMGINVGYLKPVETGGREDTLTLKNILNTDDDLDLMNPINLKLPLSPNIAFDVENSPLTLDEIKEKIKNAYETLKEKYDFLIVEGAGGVCVPIKEDFLMSDLIKFLGLDAVVVSRPNLGTINHTLLTVEHLRNKGINVRGVIINCITDLSEVLYYEKTFETIEKVGNIEIIGIVKSREDFEIDFEKILR | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 ... |
B8IBW1 | MSTLFVAGAGTEIGKTYVTAALTRALRASGRPVRALKPVASGVPDLSDPDFSASDTALLLAAQDLPVTPETVAAMTPWRFAAPLAPDLAAAREGRSLALADLVAWCETAIAAPAPGTAVLIEGVGGLMSPLTAEATGLAWLKALRLPVLLVSGSYLGAISHALTAIETLHHHAVDLRAVVVSETPGAPTPPETVAEAIARHAGVRVLCVARGGGFPAEGLDVVPA | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 ... |
B0JX07 | MNSLLIAATDTDAGKTVVTTGLVAYWQKYYPSKALGLMKLMQTGQGDREWYEGLFQGQLEMITPLQYQAPLAPPVAADLEGRDIPLGTVWQALLNLQKSQDLVLIEGLGGLGCPVTHELTLADLAAQWRLKTLLVVPVKLGAISQTVANIALAEQKKVNLGGIILNCLEPRTETEIEQLTPIDLIQSLTNCPVLGVFPFIEDRRDLDKLASVVASWPEIKLSSI | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring (By similarity). This cyanobacterium does not encode bioA (which catalyzes the formation of the p... |
B1MBZ5 | MTILLVTGTSTGVGKTVATAALAAAAVRQGIDVTVCKPVQTGDDHDAGEVARLSGVTRVQTLVRYPEPLAPVASASRAGLELLDHTQMATAIVALDRPGALTLVEGAGGLLVELAADGKTLRDLAMVLDAPVLVVTTADLGTLNHTALTLEALAVQSVPCAGLVVGSFPAEPDLAQRLNRENLANQFGTPVRAVIPEGAARLMPPVFAELSIELFEPQWVAGLVA | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 ... |
A0QX66 | MTVLAVTGTDTGVGKTVTTAALACAARLARRDVAVCKPVQTGTIDGDDDLGEVRRLSGVTALHGGWRYPEPLAPVAAAGRAGAPLPTRTELVGSVRAVDAAGRLTIVEGAGGLLVALGADGVTLRDLAHDLGAQVLIVVSPGLGTLNHTALTLEALAAHGLSCAGLVIGAWPAEPGVAELDNRTALEALAPVRAVLPAGAGAASPERFEALSAAAFDADWITSLS | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 ... |
C8V1D1 | MGDSPKCLRDSLREALRRREDKLCRRKLTILPSSSVDFSSNDFLSLSTSPAYRARFLDILQQAPPLHPFASGGSRLLDGNSAYAEELENFIAAFHNAPSGLLFNSGYDANVGVFSSIPQPGDLIVYDELIHASAHEGMRLSRAGKRIKFPHSSPDGLRAVLQAEITADPRLLQGRRNVFIAFESVYSMDGDVAPIREFVEIVDQLLPYGNGYFLVDEAHATGVFGPRGSGVVQELGLEDRMFVRVHTFGKALASHGAIVLCCADTRDYLINYARSLIYTTALGFPFLASIRAAYELLVEGKTEQLQHKLGQLIAHFRTGL... | Function: 8-amino-7-oxononanoate synthase; part of the cluster involved in the biosynthesis of biotin (also known as vitamin B8 or vitamin H), a water-soluble vitamin that functions as a prosthetic group of many carboxylases, such as acetyl-CoA carboxylase and pyruvate carboxylase . Catalyzes the decarboxylative conden... |
A7HMM1 | MFNYKILEDEMENLKNEGLYINIRTLESPQGAWIVVNGKRVLNLCSNNYLGFASDERLKQAAKKAIDEWGVGPGAVRTIAGTMKIHEELEKALAEFKGADATIFLQSGFIANQAAIPTVFGDENDAIISDELNHASIIDGVRLSKAKRYVYKHNDMNELEARLKEARDVQKARRILIITDGVFSMDGDIAPLPEIVELAEKYEAAVMVDDAHGEGVLGRGGRGIVDHFGLHGRVDMEIGTLSKAFGVLGGYIAGKETLIRYLKQKARPFLFSTGLTPADVAACLEAVKILQESDERVKRLWDNANYFKSEMKKLGFDLGV... | Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]
Sequence Mass (Da): 4... |
B9M8U3 | MQTFGEELESLRAAGLFRSMRLVEGEQSSRIILDGREVLLLCSNNYLGLADHPLLKEAAIRAVERFGVGSGAARLVSGNMELHFRLEERIAAFKGTEAALVFNSGYAANTGIISAIAGRGDLIFSDRLNHASIVDGALLSRAKVIRYSHNDMVALRRLLEENRSTSGRRIIVTDGVFSMDGDLAELAELAALKEEFGALLMVDDAHGTGVLGEHGRGSAELCGVMDRVDIHMGTLGKALGSFGAYAAASKEIIDYLVNRARSFIFSTSLPPAVLAASIAAFDLVDSQAGADLRKGLAANSTRFKDGLENAGFNTMGSETQ... | Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]
Sequence Mass (Da): 4... |
Q5KY23 | MKTELTVKLHEWEQKAQKRQLRRAEASGATVILNGKPMLNLASNNYLGLADDRRLIEAGCEAMRAYGAGAGASRLVVGNHPLYERAEAALKQWKKAEAALIFNSGYTANIGVLTALIGRDDLVFSDKLNHASLIDGIRLSKAACFRYRHHDIDQLESLLKQSPPAKRKWIVTDAVFSMDGDMAPLEELVELKRRYRAVLLVDEAHSGGVFGPNGEGLLHHFGLEKEEDVIAIGTFSKALGSFGAYVTGEPWLVDYLINSARSLIFTTALPPSVLAANEAAIHIVQAEPKRRERLHALSERFRTKLKRLGFDTGGSETPIV... | Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]
Sequence Mass (Da): 4... |
Q749W3 | MTRSIAGELQQLREQGLYRSLRTVAGSQGSRVVAEGREVVLLCSNNYLGLADHPSLKRAAVEAVERYGTGSGASRLVSGTMELHAALEERLARFKGTEAALVFNSGYAANSGIIPALVGRGDVVFSDRLNHASIVDGCLLSRARFVRYPHNDMNALERLLAEHRGAGRMLIVTDGVFSMDGDLAPLPALVALKRQYGALLMVDDAHGTGVLGESGRGSAEQFEVAADIDLQMGTLGKALGGFGAYVAASAEVVELLINRARSFIFSTSLPPAVLAAARAALDLVDSPEGKALRRRLARSAALFRDALQEAGFDTMGSETQ... | Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]
Sequence Mass (Da): 4... |
A5G6I9 | MQTFAEELAALRMEGLFRSMRLVEGNQSKRAVLDGREVLLLCSNNYLGLADHPLLKEAAIRAVERYGVGSGASRLVSGTMELHEALEARIAAFKGTNSALVFNSGYAANTGIISAIAGRGDVIFSDRLNHASIVDGALLSRARFVRYPHNNISVLRRLLEDTEVASGRRLIVTDGVFSMDGDLAKLSELVALKKEFDALLMVDDAHGTGVLGDGGRGSAEQCGVMAEVDIHMGTLGKALGSFGAYAAASREIIDYLVNRARSFIFSTSLPPAVLAASQAAFELVDSPSGAALRLALAANTIRFKAGLQAVGFDTMGSETQ... | Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]
Sequence Mass (Da): 4... |
Q5NZF6 | MNRPDLVLLHGWGLGPQVWSALTPYLPAGLRVRTPALPGHGGTPARGPTLEAWSDALLPELPDDAVVCGWSLGGLVALDLARRHPHKVARLVLIGTSPCFVTRPENAAAPWPYGLAASTVTGFIDDFAHDPAATLRRFVALQALGDARRRTVSNALNAALANLEQCRPAALGAGLELLADTDWRAALDDVRQPVQLIHGAGDALMPLAAAEWLATRLPDARLARFDDCGHAPFLSHPEDCAVLIEDVVRG | Function: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] methyl e... |
Q89A54 | MNKKLHWKSLGTGTTNLILIHGWGVNSKIWSILVQSQLYQHFKLHFVDLPGFGHSNQLLPMTLNDTAELLSVYIPKNSILLGWSMGGLIASKIALNYPQKIKGIISVCSSPCFIVRPNWPGIPKKIFLKFYNKLNINFDRTISEFITLQSHNTNYLEIKNLKQQILSQPYPTIYTLKKNLETIFKTDLRTKIKKLKIPMLRIYGSLDTFVPKKIREILDILWPKTKSITIAHASHIPFVSHQKEFYESIINFKNYLNTLKITCQK | Function: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] methyl e... |
Q7NPW5 | MNLFVETLGQGPDVVMLHGWGLHGGVFARVAEQLATRFCVHLVDLPGHGASPALPRFDADAVADLLAAHFPLPAQVVGWSLGGLIAQHWAARHPDKVKSLALVATSPRFVRDETWPHAQARASIEAVAQSLDGAFEQTLERFLALQMMGAPSARDTLKALRGELFSHGRPQGLLPALGLLLEADARALAGRIQCPAALFYGARDAITPIGAGRWLAESLPDAVLYEFPQASHAPFLSHEQDFVRALAEHLETQA | Function: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] methyl e... |
O07631 | MKLRNDLRNIAIIAHVDHGKTTLVDQLLHQAGTFRANEQVAERAMDSNDLERERGITILAKNTAINYKDTRINILDTPGHADFGGEVERIMKMVDGVVLVVDAYEGCMPQTRFVLKKALEQNLNPVVVVNKIDRDFARPEEVIDEVLDLFIELDANEEQLEFPVVYASAINGTASLDPKQQDENMEALYETIIKHVPAPVDNAEEPLQFQVALLDYNDYVGRIGIGRVFRGTMKVGQQVSLMKLDGTAKSFRVTKIFGFQGLKRVEIEEAKAGDLVAVSGMEDINVGETVCPVDHQDPLPVLRIDEPTLQMTFVVNNSPF... | Function: A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribos... |
O25225 | MKNIRNIAVIAHVDHGKTTLVDGLLSQSGTFSEREKVDERVMDSNDLERERGITILSKNTAIYYKDTKINIIDTPGHADFGGEVERVLKMVDGVLLLVDAQEGVMPQTKFVVKKALSFGICPIVVVNKIDKPAAEPDRVVDEVFDLFVAMGASDKQLDFPVVYAAARDGYAMKSLDDEKKNLEPLFETILEHVPSPSGSVDEPLQMQIFTLDYDNYVGKIGIARVFNGSVKKNESVLLMKSDGSKENGRITKLIGFLGLARTEIENAYAGDIVAIAGFNAMDVGDSVVDPANPMPLDPMHLEEPTMSVYFAVNDSPLAGL... | Function: A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribos... |
H9L427 | MIENLRNIAIIAHVDHGKTTLVDKLLQQSGTFDARAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIIYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPLQMQISQLDYNNYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRNAKVGKVLTHLGLERIDSNIAEAGDIIAITGLGELNISDTICDPQNVEALPALSVDEPTVSMFFCVNTSPFCG... | Function: A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribos... |
Q44056 | MYVLSVEKPTLRNKFAAGIGVVLVCVVASFIPTPVFALDTTKLIQAVQSEESALHARVGMTVFDSNTGTTWNYRGDERFPLNSTHKTFSCAALLAKVDGKSLSLGQSVSISKEMLVTYSPITEKSLSPETVTFGKICQAAVSYSDNTAANVVFDAIGGATGFNAYMRSIGDEETQLDRKEPELNEGTPGDVRDTTTPNAMVNSLRKILLGDALSASSRSQLTQWMLDDQVAGALLRASLPSDWKIADKTGAGGYGSRSIVAVIWPPSKQPLVVGIYITQTKASMQASNQAIARIGVVLKDTVAP | Function: Hydrolyzes carbenicillin. Methicillin and oxacillin are weakly hydrolyzed.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 32428
Sequence Length: 304
EC: 3.5.2.6
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P10424 | MKNKKMLKIGMCVGILGLSITSLVTFTGGALQVEAKEKTGQVKHKNQATHKEFSQLEKKFDARLGVYAIDTGTNQTIAYRPNERFAFASTYKALAAGVLLQQNSTKKLDEVITYTKEDLVDYSPVTEKHVDTGMTLGEIAEAAVRYSDNTAGNILFHKIGGPKGYEKALRKMGDRVTMSDRFETELNEAIPGDIRDTSTAKAIARNLKDFTVGNALPHQKRNILTEWMKGNATGDKLIRAGVPTDWVDADKSGAGSYGTRNDIAIVWPPNRSPIIIAILSSKDEKEATYDNQLIKEAAEVVIDAIK | Function: Acts preferentially on penicillins.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 33596
Sequence Length: 306
Subcellular Location: Secreted
EC: 3.5.2.6
|
Q59514 | MQRRHFLQKTLLALPIIFSGNLLTGCKTNLSDDYLPDDKITNNPNLLQNKLKEILPIWENKFNAKIGMTIIADNGELSSHRGNEYFPVNSTIKAFIASHILLLVDKEKLDLNEKIIIKESDLIEYSPVCKKYFDENKPISISELCEATITLSDNGSANILLDKIGGLTAFNQFLKEIGADMVLANNEPLLNRSHYGETSDTAKPIPYTKSLKALIVGNILSNQSKEQLITWLINDKVADNLLRKYLPKNWRIGDKTGTGSESKNIIAVIWNENNKPYFISLFITQPHDGKSLDFKNQKDEIMAQIGKEIYPFL | Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Location Topology: Lipid-anchor
Sequence Mass (Da): 35383
Sequence Length: 313
Subcellular Location: Cell membrane
EC: 3.5.2.6
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P52700 | MRSTLLAFALAVALPAAHTSAAEVPLPQLRAYTVDASWLQPMAPLQIADHTWQIGTEDLTALLVQTPDGAVLLDGGMPQMASHLLDNMKARGVTPRDLRLILLSHAHADHAGPVAELKRRTGAKVAANAESAVLLARGGSDDLHFGDGITYPPANADRIVMDGEVITVGGIVFTAHFMAGHTPGSTAWTWTDTRNGKPVRIAYADSLSAPGYQLQGNPRYPHLIEDYRRSFATVRALPCDVLLTPHPGASNWDYAAGARAGAKALTCKAYADAAEQKFDGQLAKETAGAR | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 30801
Sequence Length: 290
... |
Q9S169 | MRYIRLCIISLLATLPLAVHASPQPLEQIKLSESQLSGRVGMIEMDLASGRTLTAWRADERFPMMSTFKVVLCGAVLARVDAGDEQLERKIHYRQQDLVDYSPVSEKHLADGMTVGELCAAAITMSDNSAANLLLATVGGPAGLTAFLRQIGDNVTRLDRWETELNEALPGDARGTTTPASMAATLRKLLTSQRLSARSQRQLLQWMVDDRVAGPLIRSVLPAGWFIADKTGAGERGARGIVALLGPNNKAERIVVIYLRDTPASMAERNQQIAGIGAALIEHWQR | Function: Hydrolyzes ampicillin. Can also hydrolyze cephaloridine, aztreonam and ceftazidime with a low catalytic rate.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 31166
Sequence Length: 286
EC: 3.5.2.6
|
P04190 | MKKNTLLKVGLCVGLLGTIQFVSTISSVQASQKVEKTVIKNETGTISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHSTALTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVWLPQYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVPGHGEVGDKGLLLHTLDLLK | Cofactor: Binds 2 Zn(2+) ions per subunit. The enzyme can also function with only 1 Zn(2+) ion .
Function: Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Active on cephalosporin and penicillin.
Catalytic Activity: a bet... |
O07293 | MQRSLSMSGKRHFIFAVSFVISTVCLTFSPANAAQKLSCTLVIDEASGDLLHREGSCDKAFAPMSTFKLPLAIMGYDADILLDATTPRWDYKPEFNGYKSQQKPTDPTIWLKDSIVWYSQELTRRLGESRFSDYVQRFDYGNKDVSGDPGKHNGLTHAWLASSLKISPEEQVRFLRRFLRGELPVSEDALEMTKAVVPHFEAGDWDVQGKTGTGSLSDAKGGKAPIGWFIGWATRDDRRVVFARLTVGARKGEQPAGPAARDEFLNTLPALSENF | Function: Has a broad substrate profile, hydrolyzes amoxicillin, ticarcillin, cephalothin, ceftazidime, cefotaxime, and aztreonam, but not imipenem or cephamycins.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 30602
Sequence Length: 275
EC: 3.5.2.6
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P13661 | MKNTIHINFAIFLIIANIIYSSASASTDISTVASPLFEGTEGCFLLYDASTNAEIAQFNKAKCATQMAPDSTFKIALSLMAFDAEIIDQKTIFKWDKTPKGMEIWNSNHTPKTWMQFSVVWVSQEITQKIGLNKIKNYLKDFDYGNQDFSGDKERNNGLTEAWLESSLKISPEEQIQFLRKIINHNLPVKNSAIENTIENMYLQDLDNSTKLYGKTGAGFTANRTLQNGWFEGFIISKSGHKYVFVSALTGNLGSNLTSSIKAKKNAITILNTLNL | Function: This is an oxacillin-hydrolyzing beta-lactamase.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 30880
Sequence Length: 276
EC: 3.5.2.6
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O84955 | MIIRFLALLFSAVVLVSLGHAQEKTHESSNWGKYFSDFNAKGTIVVVDERTNGNSTSVYNESRAQQRYSPASTFKIPHTLFALDAGAVRDEFHVFRWDGAKRSFAGHNQDQNLRSAMRNSTVWVYQLFAKEIGENKARSYLEKLNYGNADPSTKSGDYWIDGNLAISANEQISILKKLYRNELPFRVEHQRLVKDLMIVEAKRDWILRAKTGWDGQMGWWVGWVEWPTGPVFFALNIDTPNRMEDLHKREAIARAILQSVNALPPN | Function: This is an oxacillin-hydrolyzing beta-lactamase.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 30449
Sequence Length: 266
EC: 3.5.2.6
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Q00982 | MKTIAAYLVLVFYASTALSESISENLAWNKEFSSESVHGVFVLCKSSSNSCTTNNAARASTAYIPASTFKIPNALIGLETGAIKDERQVFKWDGKPRAMKQWEKDLKLRGAIQVSAVPVFQQIAREVGEIRMQKYLNLFSYGNANIGGGIDKFWLEGQLRISAFNQVKFLESLYLNNLPASKANQLIVKEAIVTEATPEYIVHSKTGYSGVGTESSPGVAWWVGWVEKGTEVYFFAFNMDIDNESKLPSRKSISTKIMASEGIIIGG | Function: Hydrolyzes both oxacillin and methicillin.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 29432
Sequence Length: 267
EC: 3.5.2.6
|
P0A3M4 | MKKILLLHMLVFVSATLPISSVASDEVETLKCTIIADAITGNTLYETGECARRVSPCSSFKLPLAIMGFDSGILQSPKSPTWELKPEYNPSPRDRTYKQVYPALWQSDSVVWFSQQLTSRLGVDRFTEYVKKFEYGNQDVSGDSGKHNGLTQSWLMSSLTISPKEQIQFLLRFVAHKLPVSEAAYDMAYATIPQYQAAEGWAVHGKSGSGWLRDNNGKINESRPQGWFVGWAEKNGRQVVFARLEIGKEKSDIPGGSKAREDILVELPVLMGNK | Function: Oxacillin-hydrolyzing beta-lactamase. Confers resistance to beta-lactam antibiotics but at a significantly lower level than the TEM bla gene product.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 30568
Sequence Length: 274
EC: 3.5.2.6
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A1KXI1 | MKVLVLFCLVSLAAAGPLKDALNKAQVDAFYAEGYIVDGSNAADGDAPYQVSLQRTSHFCGGSIIADNYILTAAHCIQGLSASSLTIRYNTLRHNSGGLTVKASRIIGHEKYDSNTIDNDIALIQTASKMSTGTTNAQAIKLPEQGSDPKASSEVLITGWGTLSSGASSLPTKLQKVTVPIVDRKTCNANYGAVGADITDNMFCAGILNVGGKDACQGDSGGPVAANGVLVGAVSWGYGCAQAKYPGVYTRVGNYISWIKGKGVPV | Catalytic Activity: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Sequence Mass (Da): 27555
Sequence Length: 266
Subcellular Location: Secreted
EC: 3.4.21.4
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Q03170 | MKFLLAFSLLIPSVVFASSSKFQQVEQDVKAIEVSLSARIGVSVLDTQNGEYWDYNGNQRFPLTSTFKTIACAKLLYDAEQGKVNPNSTVEIKKADLVTYSPVIEKQVGQAITLDDACFATMTTSDNTAANIILSAVGGPKGVTDFLRQIGDKETRLDRIEPDLNEGKLGDLRDTTTPKAIASTLNKFLFGSALSEMNQKKLESWMVNNQVTGNLLRSVLPAGWNIADRSGAGGFGARSITAVVWSEHQAPIIVSIYLAQTQASMAERNDAIVKIGHSIFDVYTSQSR | Function: Hydrolyzes penicillin, ampicillin and carbenicillin but not other antibiotics including oxacillin, methicillin and cloxacillin.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
Sequence Mass (Da): 31348
Sequence Length: 288
EC: 3.5.2.6
|
A0A3B7TNM4 | MHCTVFFLLIACAKSSYGQTRSVSTAKSESKSDEYSYNSDAIDQSRLLRGAVNPVSENMALRKFIFDMPEMLRPEHFEPIFINPAAVKEVIKDYLAYGEALCGSGYDPRLLALFGVRPTVLKQELMKAKGVTLSVMPSSRKRPRALDEVESEVENFRNVLKDFFIPPTTTNPSKLIPDDIETLVPEHVSAHFNSLVYLMYFAVLHFDSQELATMSSSVLLKYALQKNLLLREKIESGTLGEWERDFRLMRVLNVYKSEQT | Function: Secreted effector that triggers a robust hypersensitive response (HR) in Lactuca serriola LS102. The response to BLN06 was visible as strong necrosis . Although effector recognition is frequently associated with single dominant R gene loci, the recognition of BLR38 requires 2 unlinked loci that display incomp... |
P25916 | MHRTTRIKITELNPHLMCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRPLLNIRSDKTLQDIVYKLVPGLFKNEMKRRRDFYAAHPSADAANGSNEDRGEVADEEKRIITDDEIISLSIEFFDQSRLDRKVNKEKPKEEVNDKRYLRCPAAMTVMHLRKFLRSKMDIPNTFQIDVMYEEEPLKDYYTLMDIAYIYTWRRNGPLPLKYRVRPTCKRMKMSHQRDGLTNAGELESDSGSDKANSPAGGVPSTSSCLPSPSTPVQSPHPQFPHISSTMNGTSNSPSANHQSSFASRPRKSSLNGSSA... | Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitinatio... |
Q53HL2 | MAPRKGSSRVAKTNSLRRRKLASFLKDFDREVEIRIKQIESDRQNLLKEVDNLYNIEILRLPKALREMNWLDYFALGGNKQALEEAATADLDITEINKLTAEAIQTPLKSAKTRKVIQVDEMIVEEEEEEENERKNLQTARVKRCPPSKKRTQSIQGKGKGKRSSRANTVTPAVGRLEVSMVKPTPGLTPRFDSRVFKTPGLRTPAAGERIYNISGNGSPLADSKEIFLTVPVGGGESLRLLASDLQRHSIAQLDPEALGNIKKLSNRLAQICSSIRTHK | Function: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Majo... |
Q8BHX3 | MAPKKRSSRGTRTNTLRSRKLASFLKDFDREVQVRTKQIESDRQTLLKEVENLYNIEILRLPKALQGMKWLDYFALGGNKQALEEAAKADRDITEINNLTAEAIQTPLKSVKKRKVIEVEESIKEEEEEEEEGGGGGGRTKKSHKNLRSAKVKRCLPSKKRTQSIQGRGRSKRLSHDFVTPAMSRLEPSLVKPTPGMTPRFDSRVFKTPGLRTPAAKEQVYNISINGSPLADSKEISLSVPIGGGASLRLLASDLQRIDIAQLNPEALGNIRKLSSRLAQICSSIRTGR | Function: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. In t... |
O14613 | MSTKVPIYLKRGSRKGKKEKLRDLLSSDMISPPLGDFRHTIHIGSGGGSDMFGDISFLQGKFHLLPGTMVEGPEEDGTFDLPFQFTRTATVCGRELPDGPSPLLKNAISLPVIGGPQALTLPTAQAPPKPPRLHLETPQPSPQEGGSVDIWRIPETGSPNSGLTPESGAEEPFLSNASSLLSLHVDLGPSILDDVLQIMDQDLDSMQIPT | Function: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts in a CDC42-dependent manner.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22484
Seque... |
Q8JZX9 | MSTKVPIYLKRGSRKGKKEKLRDLLSSDMISPPLGDFRHTIHIGSGGGDDMFGDISFLQGKFHLLPGTAVEEAEEDGSFDLPFQFTRTTTVCGRELPDGLSPLLKNAISLPVIGGPQALTLPTAQAPPKPPRLHLESPQPSPQPSPQGAGNVDVWRIPEAGSPHNGMSPEPEAEEPFLSHASSLLSLHVDLGPSILDDVLQIMDHDLGRVQIPT | Function: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts in a CDC42-dependent manner (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (... |
B1VN94 | MILVTGATGAVGREVAGRLADAGPVRILARRPERLTVRGTGVEVVQGAYGDRAALDRALRGVDAVFLVTNDPTEPDDERVAAAAAAAGVRHLVKLSMMAVEEPDAEDFITRRQRENEQAVRDSGVPWTFVRPRTFMSNTLSWAPGIRSAGVVRALYGDAPVACVDPRDVAAVAVAALTGTGHEGRAYAVSGPEAITAREQTAQLSRVLGRPLRFEELGVDAARTALMAKYPPPVAEAFLQSAERQRTGAKASVVPTVQELTGRPARPFRDWSAEHAEAFAPE | Function: Involved in the biosynthesis of A factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone), a gamma-butyrolactone autoregulator that triggers secondary metabolism and morphogenesis in Streptomyces . Catalyzes the reduction of the butenolide phosphate produced by nonenzymatic intramolecular condensation of... |
Q5JIZ3 | MREIIERVKEKTTIPVYERTIENVLSAIQASGDVWRIVDLSEEPLPLVVAVVTALYELGYVAFENNQVILTRKGKELVEKYGIGPRADYTCSHCQGRTVEIDAFSELLEQFKEITRDRPEPAHQFDQAYVTPETTVARVALMHSRGDLENKEVFVLGDDDLTSVALMLSGLPKRIAVLDIDERLTKFIEKAADEIGYENIEIFTFDLRKPLPDYALHKFDTFITDPPETVEAIRAFVGRGIATLKGPGCAGYFGITRRESSLDKWREIQRVLLNEFGVVITDIIRNFNEYVNWGYVEETRAWRLLPIKVKPSYNWYKSYM... | Function: Involved in the biosynthesis of branched-chain polyamines, which support the growth of thermophiles under high-temperature conditions. Catalyzes the sequential condensation of spermidine with the aminopropyl groups of decarboxylated S-adenosylmethionines to produce N(4)-bis(aminopropyl)spermidine via N(4)-ami... |
P25125 | MNKEALVQVAEEVRRATGLPVGWRDVERTLGALRATRDLWEAVRLSRVPLRFLVPIWEGLARRGLLRVEEGLDLLAEVPAPRPGEAACPACEGRGLVGERLPGRAAERFLAWAKERPEAIQDFDQGYVTPESTLARVALAWNWGDLEGKEVLVLGDDDLTGLAAALTGLPKRVVVLDADPRIVRFLERAAKAEGLPLEAHVHDLREPLPEAWVHAFHTFFTDPVEGPLGLQAFVGRGLLALEGEGCAGYVGLTHVEASLAKWADFQRFLLENGAVITELRDGFHVYENWGYIEQMRAWPWLPVKRRPEKPWYTSALIRLE... | Function: Involved in the biosynthesis of branched-chain polyamines, which support the growth of thermophiles under high-temperature conditions. Catalyzes the sequential condensation of spermidine with the aminopropyl groups of decarboxylated S-adenosylmethionines to produce N(4)-bis(aminopropyl)spermidine via N(4)-ami... |
Q8DAR7 | MSSDIHQIKIGLTDNHPCSYLPERKERVAVALEADMHTADNYEVLLANGFRRSGNTIYKPHCDSCHSCQPIRISVPDIELSRSQKRLLAKARSLSWSMKRNMDENWFDLYSRYIVARHRNGTMYPPKKDDFAHFSRNQWLTTQFLHIYEGQRLIAVAVTDIMDHCASAFYTFFEPEHELSLGTLAVLFQLEFCQEEKKQWLYLGYQIDECPAMNYKVRFHRHQKLVNQRWQG | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-glutamyl-[protein] = H(+) + N-terminal L-leucyl-L-glutamyl-[protein] + ... |
Q3BW59 | MAIHADTHDDLRLFQTGEHACGYWSDRQARDLVLDPHDPRLGAIYPQALAWGFRRSGDLVYRPHCERCRACVPVRIAVAAFHPDRSQRRCLARNQDLVVRVVAAERTDEQLALYRHYLKHRHPGGGMDEHGATEFDQFLIGGWSHGRFLEIREPAIAHLPGRLLAVAVTDVTGHALSAVYTFYTPEAAARSLGTFAILQQIQWAQRERRAHLYLGYWIDGHAKMNYKRRFSALEAYDGRHWRGLPAHASVD | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-glutamyl-[protein] = H(+) + N-terminal L-leucyl-L-glutamyl-[protein] + ... |
A7INB9 | MSEHPRDTPQFYLTAPSPCPYLPGREERKVFTHLVGDKAASLNDVLTQGGFRRSQSIAYRPACEGCKACVSVRICVDDFTPGRSFRRVQADNSDLIGQIKPATPTSEQYALFRSYVTGRHGTGGMADMSVLDYAMMVEDTHVHTRLVEYRKRGPDSRIIPRGTGDLMAVALTDVLTDGLSMVYSFYNPQVHDRSLGTFLILDHITRARQMGLPYVYLGYWVQGSRKMDYKRRYLPQERLTPHGWERVEK | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-glutamyl-[protein] = H(+) + N-terminal L-leucyl-L-glutamyl-[protein] + ... |
Q6ZLD3 | MKEMVSSSTFRAPGGLGFLGPSKIGLIPLRNRSGVRSRVKYIAPKCAVSSARPASQPRFIQHKKEAFWFYRFLSIVYDHVINPGHWTEDMRDDALEPAELYHHGLKVVDVGGGTGFTTLGIVKHVDNENVTLLDQSPHQLEKARQKVALNGVNIIEGDAEDLPYPTDTFDRYVSAGSIEYWPDPQRGIREAYRVLKLGGVACLIGPVHPTFWLSRFFADMWMLFPKEEEYIEWFQKAGFQDVKIKRIGPKWYRGVRRHGLIMGCSVTGVKRSSGDSPLQLGPKAEDVEKPVNPFTFIFRFVMGTICASYYVLVPIYMWMK... | Function: Involved in a key methylation step in both tocopherols (vitamin E) and plastoquinone synthesis. Catalyzes the conversion of 2-methyl-6-phytyl-1,4-hydroquinone (MPBQ) to 2,3-dimethyl-6-phytyl-1,4-hydroquinone (DMPQ, a substrate for tocopherol cyclase), and 2-methyl-6-solanyl-1,4-benzoquinone (MSBQ) to plastoqu... |
Q07457 | MTAEPATKKIKLELSDPSEPLTQSDVIAFQKEALFRCINRRRVDFEALRKQYELSRRECIDVSRKLANIMALIVTLARFIETFCTDANEKQLCREIAQGDETLIVQRSDSFMKLLTKYGKPNTTDSNTNSNASDHIQELTTELKNLRKSKEELFYENSQLTEEISALKEYYTNIIRKYDRDESFTIKRVFKEDKTDAVKELREDEKESNENNIKSGNKDSSAINGDNTSKKSEKGDELVQAEDERKEDAENEKLELDLKFSDLRAEINSLSSTIKDLENIRRENEEELIKTRSEVSNLKKQQIAAADQDPDFKSYDHESL... | Function: E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H2B to form H2BK123ub1 in association with the E2 enzyme RAD6/UBC2. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and... |
A8Y3H3 | MRQNRRASMIVNRILITLIVLVSLSFLFLRAGPKFSEADRACIQDEWQENKSLNVSSEINNETYQIVFADVQKEFKWIFLPKEISGNPDILMIVSSNRDNFARRNVIRKSWMNSDKNKIVAEKRMKILFLVGVNSENEKENTVVLKEAEVFGDIIVVDLEDNYQNLPYKSLTILLYGQSKTAESVKLIGKIDEDVIFYPDQLTPLINDGTINMSISAIYGEKWNAGVEVSNKDETNKWFIPKYSFKCQLLPSYLSGPFYLTTRKAAERILKSTKHRKFISVEDVFITGLLAGDVGVEKKQLPSMYMYDETTTDTAKAEIL... | Function: Transfers N-acetylgalactosamine onto carbohydrate substrates. Involved in susceptibility to pore-forming crystal toxins in conjunction with bre-1, bre-3, bre-4, and bre-5. Involved in resistance to the nematotoxic C.cinerea galectin Cgl2.
Location Topology: Single-pass type II membrane protein
Sequence Mass (... |
Q6QMT2 | MRQSRRASSRVNRLVVIFIIVASGFLLLYKNTQQFTQIDRECIQDEWQENNNLGNTIDDGSNFRIAFTDIQQNYTWLHLPNFLENSEILMIVSSNCDNFARRNILRKTWMNPENSQIIGDGRMKALFLVGINGADEKLNAVVLEEAKVFGDMIVIDLEDNYLNLSYKTISLLLYSISKTKSPNLIGKIDEDVLFYPDQLTPLINDKTINTSTFSIYGEKYEAGVAVNHGEDNAKWQISKNSFKCSVYPSYLSGPTYFLTRKAAKRIVEATKHRKFISVDVEDVFITGLLAGDVGIKKNQLPFMYMIEEATNDRESYEILA... | Function: Transfers N-acetylgalactosamine onto carbohydrate substrates (By similarity). Involved in susceptibility to pore-forming crystal toxins in conjunction with bre-1, bre-3, bre-4, and bre-5 . Involved in resistance to the nematotoxic C.cinerea galectin Cgl2 .
Location Topology: Single-pass type II membrane prote... |
Q9GUM2 | MAFRHLAVARLKSLLVLCAVLLLVHAMIYKIPSLYENLTIGSSTLIADVDAMEAVLGNTASTSDDLLDTWNSTFSPISEVNQTSFMEDIRPILFPDNQTLQFCNQTPPHLVGPIRVFLDEPDFKTLEKIYPDTHAGGHGMPKDCVARHRVAIIVPYRDREAHLRIMLHNLHSLLAKQQLDYAIFIVEQVANQTFNRGKLMNVGYDVASRLYPWQCFIFHDVDLLPEDDRNLYTCPIQPRHMSVAIDKFNYKLPYSAIFGGISALTKDHLKKINGFSNDFWGWGGEDDDLATRTSMAGLKVSRYPTQIARYKMIKHSTEAT... | Function: Catalyzes the transfer of galactose onto proteins or lipids. Required for susceptibility to pore-forming crystal toxins in conjunction with bre-1, bre-2, bre-3 and bre-5.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 43914
Sequence Length: 383
Pathway: Protein modification; prote... |
Q95US5 | MFLCVRILKRKYHELSSFQKLLIFTITIFLLWVLGVVDKFRETSFGDFSWPLETRNLQLRSKFTKYPQCKFSGNGQKIIIIIIKSSAKNGPMRESVRKTWGVFRMIDGVEVMPIFIVGRVENMEIMRRIDVESEKYKDILAISDIDSYRNNTLKLFGAIDYAANPNQCSSPDFTFLVDDDYLVHIPNLVKFAKTKQKEELVYEGFVFDTSPFRLKIHKHSISLNEYPFSRYPPYVSAGAVFLTSETIARFRNSIRKLKMFPFDDVFTGILAKTVNVAATHNENFIFWCRRVSQKEWDDGVIAVHGYARKDLEYEYSQLNG... | Function: Transfers N-acetylgalactosamine onto mannose groups of carbohydrate substrates. Required for susceptibility to pore-forming crystal toxins in conjunction with bre-1, bre-2, bre-3, and bre-4. Involved in resistance to the nematotoxic C.cinerea galectin Cgl2 .
Location Topology: Single-pass type II membrane pro... |
A0A068ACU9 | MPGRELAPRQNVEFQTLDGLTLRGWLFPAQSRGPAVIITPGFNCVKEMFVSEVAESFQHSDVTALVYDPRTLGDSGGLPRNNIDPLAQVSDYSDALTFLKTLPIVDQTNISFWGMSFSALVALNAAALDKRARCCIAVCPLTGMQPEPDMLPKVLARCMQDRESQVVGNPPVTISVLTEQGRNPAGMGIGADKMEYDYMVNAKFRGAPNYENRTTLQSYYKMMAWQPFEIMKYLSKTRVLMIIPENDTISPADKQQVLFDGLPEPKTAHIAKGKGHLDVLSGADYEILAEMQAYFIKGPRGKGNAPSA | Function: Thiohydrolase; part of the gene cluster that mediates the biosynthesis of brefeldin A (BFA), a protein transport inhibitor that shows antiviral, antifungal, and antitumor properties . The proposed biosynthesis of BFA involves formation of an acyclic polyketide chain that is differentially tailored throughout ... |
A0A068A9T2 | MFDIYDYSPRLVALGLIAATIIIYSFTLTVYRLFFHPLARIPGPKLCAITGWYEIFWDVLVGGQFTFKIEEWHKTYGPVMRIGPNEVHFNDPDFYNELYPTIGATYEKPAQWRWRFGCGTAIFDTIGHEHHAQRKAPVAAFFSRQKILQFSGFIQDQTDILVKRIRDDHRGQVICANEAFDALTMDIIGYYAFGLSYNSLQYPGFKAPYRNVTADIARMVHVGAHFPWVFTILNALPEKYITRLLPPMSKIFMFRKEISSQIRRIKDNKEYLDKNVNEHRTVFHEILNSNQPACELNEGRIYHEALSLVGAALETSKRTT... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of brefeldin A (BFA), a protein transport inhibitor that shows antiviral, antifungal, and antitumor properties . The proposed biosynthesis of BFA involves formation of an acyclic polyketide chain that is differentially tail... |
A0A068AA98 | MYHLIPFAAILGMTYALSLAIYRLFLSPLAKFPGPKLAAVTGWVETYYQLFYGEGGQFIFLYKEWHQKYGPIIRINPWEVHISDSCFFEILYSTNRPLKKLPHLAKVFDNELSGFSTVSPELHRIRRKAVSHLFSKGEVLKRGAQIQSAMDRLSERLKLDFLGHGNRVICMNDMWSVYTADLIAEYAFGRHYGFIDQPNFEADFTKALVHLLEPTHLAQQFPWLTDILKALPTSVLEFLHPHMAAFNKFKAANQVRIAKANFAKDLSKGGTMFSAIFNSDLPDEEKSIERAHQEALAFAAAGAETVAATLSVASFHLLHD... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of brefeldin A (BFA), a protein transport inhibitor that shows antiviral, antifungal, and antitumor properties . The proposed biosynthesis of BFA involves formation of an acyclic polyketide chain that is differentially tail... |
A0A068AA78 | MANDVSGLGPTAFVRLLAFHLIGLFVSITVYRLFFHNLSGFRGPFIARLSSFYLAWLSAKRLHLHDEIDDLHSLYGDYVRTGPRELSIIDPQCVQVIYGSQTKCIKGPIYTLLDPRTNLSSTRDKTEHAKRRRAWDRGFSTTALHTYEPMVQELTEELMTIIDELSENPINITEWVDKYAFEVMGQLTFGKPFNMLKERKEAYFLELIRQDMNAIGYLLNLPWLSYLFLRTPGLNQNHLNFWRWIENEFAQRIARGQRRPDVFNWLHQAYLQGPQTKSDTLKLHGDGYLVIVAGSDTTASTITHLLFYLACNKALTQKLQ... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of brefeldin A (BFA), a protein transport inhibitor that shows antiviral, antifungal, and antitumor properties . The proposed biosynthesis of BFA involves formation of an acyclic polyketide chain that is differentially tail... |
Q45340 | MYLDRFRQCPSSLQIPRSAWRLHALAAALALAGMARLAPAAAQAPQPPVAGAPHAQDAGQEGEFDHRDNTLIAVFDDGVGINLDDDPDELGETAPPTLKDIHISVEHKNPMSKPAIGVRVSGAGRALTLAGSTIDATEGGIPAVVRRGGTLELDGVTVAGGEGMEPMTVSDAGSRLSVRGGVLGGEAPGVGLVRAAQGGQASIIDATLQSILGPALIADGGSISVAGGSIDMDMGPGFPPPPPPLPGAPLAAHPPLDRVAAVHAGQDGKVTLREVALRAHGPQATGVYAYMPGSEITLQGGTVSVQGDDGAGVVAGAGLL... | Function: Inhibits the classical pathway of complement activation and prevents accumulation of deposited C4.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 103377
Sequence Length: 1010
Domain: The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic sp... |
P71345 | MFSRKDIIVLGMMIFALFLGAGNIIFPPMEGFSSGQHWTSASLGFVLTGVLMPFITLVVVAILGRGEELTKDLPKWAGTGFLVILYLTIGSTFAMPRITNVAYEMAWLPLGLTENNANVRFVFSLIFNLIAMGFMISPNTIISSVGKFMTPALLVLLIAVAITVFISPLSEIQAPSNAYENSHSLLIGLTSGYQTMDVLAAIAFGGIVARALSAKNVTKTKDIVKYTISAGFVSVILLAGLYFSLFYLGATSAAVAEGATNGGQIFSRYVNVLFGSAGTWIMAGIIVLASLTTLVGVTSASADYFSKFSVRFSYPFWAAL... | Function: Branched chain amino acid transport system, which transports leucine, valine and isoleucine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47039
Sequence Length: 436
Subcellular Location: Cell inner membrane
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P54104 | MKEKLTHAESLTISSMLFGLFFGAGNLIFPAYLGEASGANLWISLLGFLITGVGLPLLAIASLGMTRSEGLLDLSGRVSHKYSYFFTCLLYLTIGPFFAIPRSFTVPFETGISALLPSGMAKSTGLFIFSLIFFAIMLFFSLRPGQIMDWIGKFLTPAFLLFFFFIMIMALLHPLGNYHAVKPVGEYASAPLISGVLAGYNTMDALAGLAFGIIVISSIRTFGVTKPEKVASATLKTGVLTCLLMAVIYAITALVGAQSRTALGLAANGGEALSQIARHYFPGLGAVIFALMIFVACLKTAIGLITACSETFAEMFPKTL... | Function: Branched chain amino acid transport system which is involved in the uptake of leucine, valine and isoleucine . The proton motive force is probably the driving force for transport .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47869
Sequence Length: 446
Subcellular Location: Cell membrane... |
A2RJ04 | MKEKLAGKDYLFIGSMLFGLFFGAGNLIFPIHMGQEAGDAISQANFGFLVTAVGFPFLGIIALGISQSNGVFELATRVNRIYAYIFTILLYLVIGPFFALPRLATTSFEIGISPFLSNKLQTPLLALFSILFFGTAWFLSRKPTKLLDYIGKFLNPLFLVLLGLILIIAFSHPLGSVHQAEVGKLYQSSAFMNGFTQGYNTLDALAALAFGIIIITTIRQRGVKNSKIIAKETIKAGLISVGLMAIIYTCLSYLGAMSVGKFAISENGGIALAQISNYYLGTFGMIILALIVIIACLKTAVGLMSAFSETFVELFPKREY... | Function: Branched chain amino acid transport system which is involved in the uptake of leucine, valine and isoleucine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48900
Sequence Length: 449
Subcellular Location: Cell membrane
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P0A1W9 | MTHQLKSRDIIALGFMTFALFVGAGNIIFPPMVGLQAGEHVWTAAIGFLITAVGLPVLTVVALAKVGGGVDSLSTPIGKVAGLLLATVCYLAVGPLFATPRTATVSFEVGIAPLTGDSAMPLLIYSVVYFAIVILVSLYPGKLLDTVGNFLAPLKIIALVILSVAAIVWPAGPISNALDAYQNAAFSNGFVNGYLTMDTLGAMVFGIVIVNAARSRGVTEARLLTRYTVWAGLMAGVGLTLLYLALFRLGSDSATLVDQSANGAAILHAYVQHTFGGAGSFLLAALIFIACLVTAVGLTCACAEFFAQYIPLSYRTLVFI... | Function: Liv-II branched chain amino acid transport system, which transports leucine, valine and isoleucine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46221
Sequence Length: 439
Subcellular Location: Cell inner membrane
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Q24157 | MQSKHRKLLLRCLLVLPLILLVDYCGLLTHLHELNFERHFHYPLNDDTGSGSASSGLDKFAYLRVPSFTAEVPVDQPARLTMLIKSAVGNSRRREAIRRTWGYEGRFSDVHLRRVFLLGTAEDSEKDVAWESREHGDILQAEFTDAYFNNTLKTMLGMRWASDQFNRSEFYLFVDDDYYVSAKNVLKFLGRGRQSHQPELLFAGHVFQTSPLRHKFSKWYVSLEEYPFDRWPPYVTAGAFILSQKALRQLYAASVHLPLFRFDDVYLGIVALKAGISLQHCDDFRFHRPAYKGPDSYSSVIASHEFGDPEEMTRVWNECR... | Function: Neurogenic protein essential for the development and maintenance of epithelial structure. Required in the germline for establishing the follicular epithelium and for determining the dorsal-ventral polarity. Collaborates with Notch on the apical surface of follicle cells to mediate germline-follicle cell adhes... |
Q63K32 | MAEKTEKPTAKKLRDAAKKGQTFKARDIVALIVIATGALAAPALVDLTRIAAEFVRIASTGAQPNPGAYAFAWAKLFLRIAAPFVLLCAAAGALPSLVQSRFTLAVESIRFDLTALDPVKGMKRLFSWRSAKDAVKALLYVGVFALTVRVFADLYHADVFGLFRARPALLGHMWIVLTVRLVLLFLLCALPVLILDAAVEYFLYHRELKMDKHEVKQEYKESEGNHEIKSKRREIHQELLSEEIKANVEQSDFIVANPTHIAIGVYVNPDIVPIPFVSVRETNARALAVIRHAEACGVPVVRNVALARSIYRNSPRRYSF... | Function: Part of the bsa type III secretion system, is involved in the intracellular replication of invading bacteria inside the host cell. Probably necessary for the lysis of the vacuole membrane and escape into the host cell cytoplasm.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44458
Sequence... |
D1MX89 | MIFLAPFEFLDPLRHALPLTCTGLIIIFAFYLSRHHSPKPAPNIPIHSYDREEYFRRGYELVQEGQKKHPSCFQLRTATGWKILVPIRFVEELRKNPSLSFARGNDKDAFIEYPGFEAMEAACHDDYFMQEVVRVKLTQTLNLLYSSVIDESAVAMSEVLGEDKIWRTLRIKDDINHIVARVTSRVFLGFPLCRNQKWLDIVVNHTKAVFMAQKRMRQTPPALRPLIHYFLPETKLLRQHLHAARTLISPELAKRRAAVEEALRHGKIPKESANAISWMVEVSQAQGRKIDVAVHVVSLSMTAIQTTSEVMTNCILQLCE... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isope... |
D1MX85 | MEMATTFTHDVTTSGKPLLLFLILITLTYSLGIVFYRLFRHPLAKFPGPRIAAATYLYEIAFDYFGNGAYLFEIERMHHKYGPIVRLNPAELSIKDGEFYDKVYVNGNVRRTEALPSFGDGMDFNNSHGMTVDHHQHRQRRKPLEPFFSKAGVARFESNLASVVSTLVDRLRDYEGTGSVLRLDHAFAALAGDIITTMCIDSTSMTFLDDKDFSRGWYELFHTLIISMPVFMNFPWIIRLVRLIPTSILKRVDPRSQMFRDWSDMSVAEIKKSLQRKATGEMLTYQKGIIKAPTLFDHLVNSDLPTSDMSVERLASEAQV... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isope... |
D1MX86 | MESAQIHSTRDSLFILWLTTLLVSVLATAAYIKFQSRPRPYSGFPLVTLGGPSETDSSHAANWFRRGRALVNKGLSELSGAFQISNGSGYWIILPSKYMDELRNHPDMSLRDALREENFPNYRGFDGFRQAFKDSTFTQEVIRVKVTQSLGLITANLANECQHALQENLGESREWQQRFIIEDILNIVAQLTSRVFLGERLCRDKEWLQITKEYARNSFMGSEELRQCLPLTRPLMQFFMPACTQLRKFSAAARRLIDPEVQARKRRAEEAIKLGKKPPKVEDTIGWMVEVARGRQVDYVGGQLALSIAAIHSSTDNLSK... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isope... |
E0D7H5 | MSQSTLVIIGAGGIGEAIARRVGPGKEVLLGDWSNALLQEATQRMKRDGFRVTSQHVNISSHDSVIQFAEKAQSLGQVMHVVISAGLSPVSSTRETILAVNLAGTGFCIAEFGKLIGHGGTCVVISSLAGYTLAQDVPHGVIQHLARTSPSDVLGLPLLRETVLDQWSAYGVSKRVNYVQVQDASLSWARRGARINSISPGAIQTPMLSLESQASKEEVVHDLAQNVPCKRVGDSGEVAHVAAFLLGSESSFVTGTDILVDGGALAYLSRDTSS | Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts... |
D1MX87 | MLEGTLQDCWTSISKMQLHWTVLGLLPVLFIAILGPRVRQIWVNYVHLTKIPSPHKKDYFCFVTETTRAEFLNECARLLRKGFASGDVIRLHASWDHIVVLSPSYAECLRADEKFSPDTFSDKEMFGAVPGFEPYRFLCTHRDLVRNVISMRLNRCFVPATRYLSEAIDDALRKQMGNDSEWREVPLGNAVLKILTQSSFRALQGPELCYDDEWLDIATQYIVTSVTGVTALRKLPKFLVPLIHWFHPDAIKSRRLLSRARAKLIPFYEKRKKELYQARRNGTYRPEDADAFGWYEELADGRDYDPVVAQLTVAVAATHS... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isope... |
C9K2Q2 | MAVQETDLDKQLLQLSIQVADLAARTDSRGSQKIQDFLIKTQQSLESPWETLMRYYDLDFQHVAIRIGCDMQVFTTLTTADKPMKLQDIANVNGASERLLGRVLRYLASINTIEEVGKDTFEANHITRTLSKPGIEGGIRLSSACQRPTNSALPDLLVERGFQDITSATETAFNKAWASREPFFTWVRSQPKIFEYLRLALDVQFREDWLNAFPLESHLGDFASRADPEKVLFVDVGGNLGIQCRGLKAKFPHLSGRIILEDLQETIDVALALEGVETLAQDYLTEQKVKGAKFYYYRNIFHDNPDDRCRLILDALKPAM... | Function: 16-O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isopentenyl ... |
Q08280 | MDASSVPPKVDDYGMYTTEISHHNPIELKNLLSSSDSRRNSQDEDSLPNNTNLIKEIDWQGEKVKTYPLNYQTVPLVKLQVIACLIMFVVFGMNDQTVGALLPTLIEYYHISRVDVSNVFIVQLCGYVMASLSKERLNKHFGMRGGMLLAAGLCIVFLIILATAPSSFYVCMFCGLPLGLGIGILDSTGNVLMGSLLVHKNELMGIMHGLYGAAAMVTPPLVSYFVEWGHWSLFFLIPLFFSIIGMIVIFPAFKFETASKYDYLCSVENKESNNDVEEAGDNSLMESTKASPGFFELLRNPAIFLYSLYLFLYLGAEITT... | Function: Probable transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55084
Sequence Length: 497
Subcellular Location: Golgi apparatus
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D1MX88 | MASILWTTSLKVLLALIVWIGTTIIYNIYFHPLHSFPGPVLARATRLYSAYIRAVGLSERKSLQWHNQYGGIVRIAPDELSFNTGSAWNDIYGTKSRKSQRLQKDPHFYMGATAPNGEKNMGAVGDEDHSRIRSVLAHAFTDTALHAQESLIRAHVDRLVQRLQDLHGKPTDIVRWMHHHSYDVIAHLCFGQDLDALGSKDWFPPARVVFEGIREGVTLIEVLRFVPFKATVLDILVQAFGKARRENFNASVARAMLRLRLAETTSIDFISYILRVKESAKELTRSELTANVALLIDAGSETTATMLSGCLFYLSLNRTT... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isope... |
C9K2Q3 | MKYQFSIIVDPATYDNEGLSNGIDLRKNNFTHLEDRGAIRAQQDWATHIAPIKQFKGTLGHDYSFMTVCVPECIPIRLEIISYANEFAFMYDDDTELDTENNTSAENDKLMGTFLAGTQGWSPPQDQSSSGKTRILKQLFSEMMEIDKECAIATMKAWAEFLRVGSSRQHGTVFTRLKDYLPYRIKDVGEMFWFGVVTFGMALHIPDHEMDACHKLMEPAWIAVGLANDVFSWPKERDASQRLGRTHVVNAVWVVMQEHGFSQEQARQYCRELAAQFVAQYLDNIRNIKNEESISPDLRTYVEAMQYSISGNVIWSKFCP... | Function: Multifunctional diterpene synthase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts ... |
D7UTD1 | MASTSSTSTDGHLNIRPMVHGSDKKLNFGAYITGLDLNNASDAEVDQLREAILRHKIVVIKGQQAEKPDKNWEMIKKLDPMHHMITQEEFGQLFHPTGEGLIAMLKLATVPTTEHGHIHLMGKGYQGDDHYGLKKLNLGEAFAGNYYSKPLAEEDFRAGVTRFQSWHMDGPLYKVHPPYISSLRFIQLPDGEQTVEWADGSGLSLKTKPGRTAFFSTSQLYDMLTDEERAMVDNSAVEYMYYPYEWIRGCRGNPNGLNVADEGREKPLDAMEEIARDERWTKTYPMVWFNELTKEKSLQVQPNCVRRLLIRRSADQKEPE... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Alpha-ketoglutarate dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C . In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl tr... |
Q6WRU0 | MAPTFYHYHPLPMDQKEPGCGIRWRCLAAASVLILVALVIPLIIFAVKANSEACRDGLRAQEECSNTTRLLQRQLTRSQDNLAQAEAQASTCNRTVVTLQDSLEKKVSQIQEKQALIQEQEAQIKEQEAQIKEQEAQIKEQKAHIQEQQVRIQKLEGEVEEFEQKLKKLRTAEEASITSKQNSAGSMAVSSLLVLAVPLFLLF | Function: IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The teth... |
Q10589 | MASTSYDYCRVPMEDGDKRCKLLLGIGILVLLIIVILGVPLIIFTIKANSEACRDGLRAVMECRNVTHLLQQELTEAQKGFQDVEAQAATCNHTVMALMASLDAEKAQGQKKVEELEGEITTLNHKLQDASAEVERLRRENQVLSVRIADKKYYPSSQDSSSAAAPQLLIVLLGLSALLQ | Function: IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The teth... |
Q8R2Q8 | MAPSFYHYLPVPMDEMGGKQGWGSHRQWLGAAILVVLFGVTLVILTIYFAVTANSVACRDGLRAQAECRNTTHLLQRQLTRTQDSLLQAETQANSCNLTVVTLQESLEKKVSQALEQQARIKELENEVTKLNQELENLRIQKETSSTVQVNSGSSMVVSSLLVLKVSLFLLF | Function: IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The teth... |
Q811A2 | MAPSFYHYLPVAMDERWEPKGWSIRRWWLVAAILVVLIGVVLVCLIVYFANAAHSEACKNGLRLQDECRNTTHLLKHQLTRAQDSLLQTEMQANSCNQTVMDLRDSLKKKVSQTQEQQARIKELENKIERLNQELENLRTQKEISTTVQVNSGGSVVVSSLLVLVAVLFLHF | Function: IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The teth... |
K4JY29 | MGPAVVFDCMTADFLNDDPNNAELSSLEMEELESWGAWSDDTDQSV | Function: Bottromycin D is a ribosomally synthesized and post-translationally modified peptide (RiPP) that displays antibiotic activity against methicillin-resistant S.aureus (MRSA).
PTM: The precursor peptide is first ribosomally synthesized and then highly tailored by specific enzymes to yield the final natural produ... |
Q9LR78 | MAPDQSYQYPSPSYESIQTFYDTDEDWPGPRCGHTLTAVFVNNSHQLILFGGSTTAVANHNSSLPEISLDGVTNSVHSFDVLTRKWTRLNPIGDVPSPRACHAAALYGTLILIQGGIGPSGPSDGDVYMLDMTNNKWIKFLVGGETPSPRYGHVMDIAAQRWLVIFSGNNGNEILDDTWALDTRGPFSWDRLNPSGNQPSGRMYASGSSREDGIFLLCGGIDHSGVTLGDTYGLKMDSDNVWTPVPAVAPSPRYQHTAVFGGSKLHVIGGILNRARLIDGEAVVAVLDTETGEWVDTNQPETSASGANRQNQYQLMRRCH... | Cofactor: Binds 2 manganese ions per subunit.
Function: Phosphatase that acts as a positive regulator of brassinosteroid (BR) signaling . Dephosphorylates BES1, a transcription factor that regulates the expression of BR-response genes, thereby playing an important role in the regulation of response to BRs . Inactivates... |
P33532 | MASKIASLFSPSETASKDQHENVAEDLELGTASSQSDGIHETNSEYDEKKREESPEVIDISNLISSDHPAHPQNWHWAKRWSIVFMFCLMQIYVIWTSNGFGSIEYSVMAQFNVSAQVATLCLSMNILGSGLGPMFLGPLSDIGGRKPVYFCSIFVYTVFNISCALPRNIVQMIISHFIIGVAGSTALTNVAGGIPDLFPEDTAGVPMSLFVWACAGGAIGAPMATGVDINAKYGWRWLYYINIIVGGFFLIVILIIPETLPIKVITRYENAKGRIVEGIPKNNLKEVLKKCKFVTTMGFRMMLTEPIILSMGLYNFYAY... | Function: Thiamine-regulated, high affinity import carrier of pyridoxine, pyridoxal and pyridoxamine. Also imports, but does not export, amiloride and so confers sensitivity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58484
Sequence Length: 526
Subcellular Location: Membrane
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O67791 | MENLKKYLEVAKIAALAGGQVLKENFGKVKKENIEEKGEKDFVSYVDKTSEERIKEVILKFFPDHEVVGEEMGAEGSGSEYRWFIDPLDGTKNYINGFPIFAVSVGLVKGEEPIVGAVYLPYFDKLYWGAKGLGAYVNGKRIKVKDNESLKHAGVVYGFPSRSRRDISIYLNIFKDVFYEVGSMRRPGAAAVDLCMVAEGIFDGMMEFEMKPWDITAGLVILKEAGGVYTLVGEPFGVSDIIAGNKALHDFILQVAKKYMEVAV | Function: Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, and both D and L isomers of inositol-1-phosphate (I-1-P).
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 29336
Sequence Length: 264
EC: 3.1.3.11
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O30298 | MDERDALRISREIAGEVRKAIASMPLRERVKDVGMGKDGTPTKAADRVAEDAALEILRKERVTVVTEESGVLGEGDVFVALDPLDGTFNATRGIPVYSVSLCFSYSDKLKDAFFGYVYNLATGDEYYADSSGAYRNGERIEVSDAEELYCNAIIYYPDRKFPFKRMRIFGSAATELCFFADGSFDCFLDIRPGKMLRIYDAAAGVFIAEKAGGKVTELDGESLGNKKFDMQERLNIVAANEKLHPKLLELIK | Cofactor: Magnesium. Can also use manganese.
Function: Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, inositol-2-phosphate, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phos... |
Q57573 | MKWDEIGKNIAKEIEKEILPYFGRKDKSYVVGTSPSGDETEIFDKISEDIALKYLKSLNVNIVSEELGVIDNSSEWTVVIDPIDGSFNFINGIPFFAFCFGVFKNNEPYYGLTYEFLTKSFYEAYKGKGAYLNGRKIKVKDFNPNNIVISYYPSKKIDLEKLRNKVKRVRIFGAFGLEMCYVAKGTLDAVFDVRPKVRAVDIASSYIICKEAGALITDENGDELKFDLNATDRLNIIVANSKEMLDIILDLL | Function: Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate, fructose-6-phosphate, NAD(+) or 5'-AMP. May be involved in t... |
O26957 | MEESDIYYWKGVAVRMAEQVERAVSPLVGTEDAGEIIKMGADGTPTKLIDLVAEDEAVGVLESTGRPVTIISEEIGVLHINSEGDEPGIIFVVDPLDGTSNAIRNIPFYGISVAVAERHPDGAAPTLNNVLMGFVKNFATGDLYWAIKGQGAFLNEKAISSSSQSSLDRTSLGAFIYGTRFRRVDSICRVIRRMRILGSVALELAYVASGSYDAFMDLRENLRIVDIAASKLIVEEAGGVVTNERGGEIDGLLNVKARTSLVAAGNLELHEKIMQTLEVI | Function: Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, and both D and L isomers of inositol-1-phosphate (I-1-P).
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 30173
Sequence Length: 280
EC: 3.1.3.11
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Q5JH93 | MEFNWSEIALNTAKELEEKIMPLFGTKKAGENVGTNVSGDVTKYVDKVAEDIILKRLVPLGVNVVSEEVGTVDSGSDYTVVVDPLDGSYNFSAGIPIFAFSLGIFKGKKPVYGAIYEFLPENFYEAKPGKGAYLNGERIRVNEPEPGKEALSFYTRGRCLGLVKKVKRVRVLGAIAVELAYVARGSLDGVFDIRNYVRPTDVAAGVLLVREAGGIVTDERGREFEVKLSATEKTNIIAVANERLLNTILEAMKDEP | Function: Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate (FBP) and inositol-1-phosphate (IMP). However, while possessing a high FBPase activity in vitro, does not participate in gluconeogenesis in vivo.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-... |
O33832 | MDRLDFSIKLLRKVGHLLMIHWGRVDNVEKKTGFKDIVTEIDREAQRMIVDEIRKFFPDENIMAEEGIFEKGDRLWIIDPIDGTINFVHGLPNFSISLAYVENGEVKLGVVHAPALNETLYAEEGSGAFFNGERIRVSENASLEECVGSTGSYVDFTGKFIERMEKRTRRIRILGSAALNAAYVGAGRVDFFVTWRINPWDIAAGLIIVKEAGGMVTDFSGKEANAFSKNFIFSNGLIHDEVVKVVNEVVEEIGGK | Function: Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P) but displaying a 20-fold higher rate of hydrolysis of D-I-1-P than of the L isomer, 2'-AMP, pNPP, inositol-2-phosphate, beta-glycerol phosphate, and alpha-D-glucose-1-phos... |
P18892 | MAVFPNSCLAGCLLIFILLQLPKLDSAPFDVIGPQEPILAVVGEDAELPCRLSPNVSAKGMELRWFREKVSPAVFVSREGQEQEGEEMAEYRGRVSLVEDHIAEGSVAVRIQEVKASDDGEYRCFFRQDENYEEAIVHLKVAALGSDPHISMKVQESGEIQLECTSVGWYPEPQVQWRTHRGEEFPSMSESRNPDEEGLFTVRASVIIRDSSMKNVSCCIRNLLLGQEKEVEVSIPASFFPRLTPWMVAVAVILVVLGLLTIGSIFFTWRLYKERSRQRRNEFSSKEKLLEELKWKRATLHAVDVTLDPDTAHPHLFLYE... | Function: May function in the secretion of milk-fat droplets. May act as a specific membrane-associated receptor for the association of cytoplasmic droplets with the apical plasma membrane. Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion (... |
Q13410 | MAVFPSSGLPRCLLTLILLQLPKLDSAPFDVIGPPEPILAVVGEDAELPCRLSPNASAEHLELRWFRKKVSPAVLVHRDGREQEAEQMPEYRGRATLVQDGIAKGRVALRIRGVRVSDDGEYTCFFREDGSYEEALVHLKVAALGSDPHISMQVQENGEICLECTSVGWYPEPQVQWRTSKGEKFPSTSESRNPDEEGLFTVAASVIIRDTSAKNVSCYIQNLLLGQEKKVEISIPASSLPRLTPWIVAVAVILMVLGLLTIGSIFFTWRLYNERPRERRNEFSSKERLLEELKWKKATLHAVDVTLDPDTAHPHLFLYE... | Function: May function in the secretion of milk-fat droplets. May act as a specific membrane-associated receptor for the association of cytoplasmic droplets with the apical plasma membrane (By similarity). Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies, T-cell metabolism and IL2 and ... |
Q9FMK7 | MAITATQNDGVSLNANKISYDLVETDVEIITSGRRSIPAHSGILASVSPVLTNIIEKPRKIHGGSSKKVIKILGVPCDAVSVFVRFLYSPSVTENEMEKYGIHLLALSHVYMVTQLKQRCTKGVGERVTAENVVDILQLARLCDAPDLCLKCMRFIHYKFKTVEQTEGWKFLQEHDPFLELDILQFIDDAESRKKRRRRHRREQNLYLQLSEAMECIEHICTEGCTLVGPSSNLDNKSTCQAKPGPCSAFSTCYGLQLLIRHFAVCKKRVDGKGCVRCKRMIQLLRLHSSICDQSESCRVPLCRQYKNRGEKDKKMVEDT... | Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Also targeted for degradation by the 26S proteasome pathway. May be involved in gametophyte development.
Sequence Mass ... |
Q9KSL2 | MDFHRLLQHKQQRWQRSSYLLIGLFLSVCVLYLLVGELWLSPFSAWSSLEQQLVWELRLPRLLAAAVIGASLAVAGATLQVLLGNVLAEPGVVGVSGGASVAMVILLLFFPSLNSPVAFMAAAVLGALLFTLLLVVMARKLRLTTARLLLVGVALGILSGAVVTWAFYFSDDLGLRQLMYWLMGSVAGVSWYQHLLSLVAVPVVIWLVLQGGVLDKLMLGEGHAKQLGIDIHRVRWRLILAIALLVGASVALGGVIGFVGLVVPHLLRLTLGSENRLLLPLSALCGALLLVSADLIARLALGSGELPLGVVTTTLGAPIF... | Function: Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35497
Sequence Length: 331
Subcellular Location: Cell inner membrane
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B0R5G4 | MTLDVTGLDVELAGTRILDDVHASIRDGHLVGVVGPNGAGKSTLLRAMNGLITPTAGTVLVAGDDVHALSSAAASRRIATVPQDASVSFEFTVRQVVEMGRHPHTTRFGTDTDTAVVDRAMARTGVAQFAARDVTSLSGGERQRVLLARALAQAAPVLLLDEPTASLDVNHQIRTLEVVRDLADSEDRAVVAAIHDLDLAARYCDELVVVADGRVHDAGAPRSVLTPDTIRAAFDARVAVGTDPATGAVTVTPLPDRTSAAADTSVHVVGGGDSATPVVRRLVSAGASVSVGPVVEGDTDHETARRVGCPCTSVAPFTRL... | Function: Required for corrinoid utilization. Probably part of the ABC transporter complex BtuCDF involved in cobalamin (vitamin B12) import. Probably responsible for energy coupling to the transport system (By similarity).
Catalytic Activity: an R-cob(III)alamin(out) + ATP + H2O = ADP + an R-cob(III)alamin(in) + H(+) ... |
Q2HGY8 | MAAADDAQFPPPKVLTYPASTPPTLITQGAEGRLYKTTHLTRDRPCALKYRPPKPYRHPVLDARLTKARLSSEAKVLERCWREGVPVPAVYAMDPAAGWMMMEWIEGIPVRVGINEWLGDRPEEGAEIPQVADETPIVDLMKRIGAAIGALHKTGVVHGDLTTSNMMLRPRGFNPVDGAPGDEGKAGSVEGDVVLIDFGLATQSMSDEDRAVDLYVLERAFASTHPRAERLFATLLESYKSTFKKASSVLIKLEDVRMRGRKRSMLG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
P0CP73 | MAASTPLLSRGTLIKQGAEAKVYALPSLFPEPTTYHPGSSSSFSAASPTPVILKHRFTKTYRHPTLDASLTSQRLTFEARALARAAKAGVTVPKVVWVDEKAGVIGMERIEGWSVREILGGGAEGEVEVIEEQEIEEDVENKAEDSAVREEPEGPESEGLKALKNLGVTQEHLMRSIGAALARLHKTMIIHGDLTTSNMMVRLTPGGSGPYEIVLIDFGLSSQAQFPENYAVDLYVLERAFASTHPRSEKLYAGVLETYAEGLGEKKWKPIQIKLKDVRRRGRKRDMTG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
Q6BHA8 | MTDHIVKKAQECLPNIPLTVISQGAEALVFYTDVHPYANEPYLQNRGKYVIKYRPSKPYRHPKVDSSITKSRTVGEVKFMYKLNKLNINSPRIISADYNNGIIWMEYIGYSLPNGDVSSFKNWLWYLERNNQDCTSESVEKMCFKVGQLIGKLHLHEMIHGDLTSSNILLNDDEPVLIDFGLSSYSGLAEDRAVDLYVLERAITSTHSVYAKEYNQWLLQGYEDVHKHKEFGKQGQKKLVEVLKKLDDVRLRGRKRSMLG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
Q54W07 | MDANECSNSENSATTTIPKSASPSTTISTKVVKLDEIGILISQGAEAKTYETDLYGLKCIVKERFSKAYRHPILDQKISSKRILQEVRSLNKCKKKGIQVPSLYLVDIGNNRIYMEFIKGETVKHYLYKNQESTQHQNQIESIMKELGNQIGIIHEMNVIHGDLTTSNMLLRESTNELVFIDFGLSYTSNSVEDKAVDLYVLERAFISTHPNSEQLFQTILSNYELTSSNSKIVIQKLNQVRLRGRKKTCFG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
Q5BAB7 | MPPTNRPPPFSTILSSASLPSYSSTDELTPIYQGAEAHLYKTTFLSPSQPAALKIRPSKPYRHPILDRRLTRARILQEARCLQKLVKEGVSVPALLGVDWEPSAGDGSSWLVMEWIEGEPVRVILEEWEAYLKGIEREKRLGLGEGVQGSEEEKVRGLMRRIGRAVGGLHRAGVIHGDLTTSNLMLRPLGSADTTETIEERDQSPSMAGEVVMIDFGLAMQSSQDEDRAVDLYVLERAFGSSHPRTERFFEEVLVGYRESYKGAVSALKRLEDVRMRGRKRSMIG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
Q8SVD9 | MGFHFQGAESIISADGETVVKKRARKAYRIEALDLKIINGRTKREAKILRKLEALGIPAPRLISTYGDTIVMEKVEGTVLKEMIDSSDNPGALFRDLGALVSRLHIADIIHGDLTTSNFIHGSKIYAIDFGLSYISRKDEDKAVDLYVFEKAVGCAHDAKFLEDFYCGYMGEGSESVLKKLGTVRLRGRKREAMAFG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
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