ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8EC35 | MKSWCKNLLAAGLSLAMLSACSSSDVEEEPVSELTAIQATVFPEVSWSASVGDGVGDYYSRLTPAVRYGKIFAADRYGAVMAFDEASGEQVWRKDFSEEFRDNALAKNKGARLAAGITAARNKLFIGGESGLLAALNAEDGQVLWHVIAGGELLSKPTVADDVVVVSTSSGSLEAYNVDTGAKLWVYDMQLPNLTLRGTGSAAYEAGGFFIGTADGKVAVVVKNNGQAAWEQAIYNPTGGNEFTRMADVDMTPLILGDNLYAVSYNGNLVSMELRTGRIIWTRKYSSFNELTTAGLSLFLVDDHSRIYSVDRRNGLELWS... | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 42690
Sequence Length: 395
Subcellular Location: Cell outer membrane
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C0HLZ9 | MKSFGLIALAICGVICVAAEPQHTYDGRNGPHVFGSPGNQVYIRGQNEGTYSVPGVGGQFQNAPQRGEHVYTDEAGNTFVNRKNAGGPASHTISGPNFSAKNLGPNGAKSVGIPQRARRSPQFHVERPGRTVDVGNGGFYIQRGRRSPQLHVARPDRTVTIGNGGVYIQRSRRSPQFHVERPDRTVDFGNGGFSAQRFRRGINDARVQGENFVARDDQAGIWDNNVSVWKRPDGRTVTIDRNGHTIVSGRGRPAQHY | Function: Secreted immune-induced peptides induced by Toll signaling . Has a significant role in resistance to infection by the entomopathogenic fungus B.bassiana R444 and weak antifungal activity against M.rileyi PHP1705 . In adult males, activity appears to be important for neuromuscular processes that mediate correc... |
O57878 | MVSMTKWDEIRKYTSKKIEKNLEIVKLDEKYIPRASGFKYYPMVIERSSGSRIWDKDGNEYIDFLTSAAVFNVGHTHPGVVKAVEEQIKKFFNYTMGYLYVEPPVRLAELLVEITPGNFEKKVTYGFSGSDAVDSSIKAARAYTKRVNIISFLHSYHGMTYGALSATGILDPKLKKLLHPMGNFHHVEFPDPYRNSWGIDGYEDPSELANRALDEIERKIKELNEDVAGIIIEPIQGDAGVVIPPEEFVRDLKKLTEEYGIVFIDEEVQTGMGRTGRWWGIEHFGVTPDLIVSAKALGGGMPISAVVGKAEIMDSVPVPF... | Function: Amino-acid racemase able to utilize a broad range of substrates . Can use Met, Leu, Phe, Ala, Ser, Ile, Val, Trp, Tyr and Thr . Is mostly active with Phe, Leu, Met and Tyr, followed by Ile, Thr and Trp. Has weaker activity with Val, Ser and Ala . Shows no activity toward Pro, Asp, Glu, Arg, His, Gln and Asn .... |
P0AEC7 | MTNYSLRARMMILILAPTVLIGLLLSIFFVVHRYNDLQRQLEDAGASIIEPLAVSTEYGMSLQNRESIGQLISVLHRRHSDIVRAISVYDENNRLFVTSNFHLDPSSMQLGSNVPFPRQLTVTRDGDIMILRTPIISESYSPDESPSSDAKNSQNMLGYIALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSMAMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTLK... | Function: Member of the two-component regulatory system UvrY/BarA involved in the regulation of carbon metabolism via the CsrA/CsrB regulatory system. Phosphorylates UvrY, probably via a four-step phosphorelay (By similarity).
PTM: Activation requires a sequential transfer of a phosphate group from a His in the primary... |
Q21209 | MFENTKKALETFRTAIECVKCKKPRGDLQYLGSSCKHAYCWECIATFQQKPSGKRSSVARHMCPSCAFPLDTSKITEAHMLKTCFDTLSELNDLLQKVGTTSLTQAEFACTQNIFNKEKTPADAVEKFLETQAHMPDEMGQLGEEDDDLMCKDENRENSNSPELDIFHDYSKEASPTRNSTKRPSTVSVHERKPKRSSILKTSVKNEPAAPVVDLFASQVPQRTHQNDLLTPFIERRSTAPAATGVATYAQAFGSSSNPVKAEIIEEDIFSKAIPLTKRQASMSASAKKQPKLEPEEPEEVPSTSRSRKNSIKSDKIERR... | Function: Constituent of the CeBCD complex that possesses E3 ubiquitin-protein ligase activity . When bound to chromatin, the brc-1-brd-1 heterodimer within the CeBCD complex is inactive during normal conditions, but in response to DNA damage, the brc-1-brd-1 heterodimer associates with other proteins such as the recom... |
Q99728 | MPDNRQPRNRQPRIRSGNEPRSAPAMEPDGRGAWAHSRAALDRLEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMIQLCSKLRNLLHDNELSDLKEDKPRKSLFNDAGNKKNSIKMWFSPRSKKVRYVVSKASVQTQPAIKKDASAQQDSYEFVSPSPPADVSERAKKASARSGKKQKKKTLAEINQKWNLEAEKEDGEFDSKEESKQKLVSFCSQPSVISSPQINGEIDLLASGSLTESECFGSLTEVSLPLAEQIESPDTKSRNEVVTPEKVCKNYLTSKKSLPLENNG... | Function: E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role ... |
P0C6N0 | MARFIAQLLLLASCVAAGQAVTAFLGERVTLTSYWRRVSLGPEIEVSWFKLGPGEEQVLIGRMHHDVIFIEWPFRGFFDIHRSANTFFLVVTAANISHDGNYLCRMKLGETEVTKQEHLSVVKPLTLSVHSERSQFPDFSVLTVTCTVNAFPHPHVQWLMPEGVEPAPTAANGGVMKEKDGSLSVAVDLSLPKPWHLPVTCVGKNDKEEAHGVYVSGYLSQ | Function: Plays diverse functions in immunomodulation and oncogenicity, maybe by acting as a functional receptor for human CSF1. May inhibit interferon secretion from mononuclear cells. Exhibits oncogenic activity in vitro (By similarity).
PTM: Phosphorylated on serine and threonine by host.
Sequence Mass (Da): 24471
S... |
A1BIZ8 | MRLAFWLYEGTALHGISRITNSMKGVHTVYHAPQGDDYITATYTMLERTPDFPGLSISVVRGRDLAQGVSRLPSTLQQVDHHYSPDLTVIAPSCSTALLQEDLNQLAAHSGVPSEKLLVYALNPFRVSENEAADGLFTELVKRYAVAQEKTPTPSVNLLGFTSLGFHLRANLTSLRRMLEALGIAVNVVAPWGSGIDDLAKLPAAWLNIAPYREIGATAAAYLDETCGMPAMYEAPIGVEPTTAWLRKLLDEINRIAGQKGLSRLAMPAPRAFSLDGLSAPSGVPWFARTADMESFSNKRAFVFGDATHTVALVKFLRDE... | Cofactor: Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophy... |
D5ANS3 | MSPRDDIPDLKGFDGDGEGSVQVHDSEDIGLDVGGARVFSVYGKGGIGKSTTSSNLSAAFSLLGKRVLQIGCDPKHDSTFTLTGRLQETVIDILKQVNFHPEELRPEDYVTEGFNGVMCVEAGGPPAGTGCGGYVVGQTVKLLKQHHLLEDTDVVVFDVLGDVVCGGFAAPLQHADRALIVTANDFDSIYAMNRIIAAVQAKSVNYKVRLAGCVANRSRETNEVDRYCEAANFKRIAHMPDLDSIRRSRLKKRTLFEMDDAEDVVMARAEYIRLAETLWRSTGEPGLTPEPLTDRHIFELLGFD | Cofactor: Binds 1 [4Fe-4S] cluster per dimer.
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique... |
P26236 | MPSDYAEIRNRVEHYFDRTATRAWARLTTADEKVSKVRQTVREGRDTMRAVMLSRLPDDLTGCRVMDAGCGTGLTTVELARRGADVVAVDISPQLIDIAKDRLPPELRGKVSFHVGDMADPALGQFDYVVAMDSLIYYRAPDIGRVLTELGKRTHSAIVFTVAPKTAFLMAFWWLGKLFPRSNRSPVMIPHALDKLQRHAGDSLIKIDRVARGFYISECLEYRP | Function: Converts Mg-protoporphyrin IX to Mg-protoporphyrin IX methylester using S-adenosyl-L-methionine as a cofactor.
Catalytic Activity: Mg-protoporphyrin IX + S-adenosyl-L-methionine = Mg-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25225
Sequence Length: 224
Pathway: Porph... |
P42333 | MAKKAKYPDVPIRFSETFSDTNLYIVLLIGVPLYGVITSYLFNREYAESTLKNLLTIPVSRISLIVSKLVLLLIWIMMLTLIAWVLTLLFGLIGQFEGLSSAVLIEGFKQFMIGGALLFFLVSPIIFVTLLFKNYVPTIIFTIIISMVSIMVYGTEYSALFPWSAVWVIASGTFFPEYPPEYSFISVAATTVLGLAATIVYFKKIDIH | Function: Part of the binding-protein-dependent transport system for bacitracin that confer resistance to this antibiotic; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23324
Sequence Length: 208
Subcellular Location: ... |
Q5WNX1 | MLNLISCELSKLKRSKMVLISVAGVLSTPLLMLIEALQTHFDKPEIIFTLSDIYSDSVLYIMLLVNMMIYVAIAAYLYSREYTENTLKTILPIPISRTKLLIGKFCTLLLWIVMLTLVTWAGIFIVCGLYHVVFTLEGYSLLVAISWLPKFLFGGILMFLTTSPFVFIAFKTKGFVAPVIASAVIVMGSVALSNQELGALYPWTATFFLIDGRIESTGYPLALAIGIIILVSAVGFFMTFHHFKKEDLK | Function: Essential for high-level bacitracin resistance . Part of the ABC transporter complex BcrAB. Probably responsible for the translocation of the substrate across the membrane (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27788
Sequence Length: 249
Subcellular Location: Cell membr... |
O87875 | MSAKTNPEVIKESSMVKQKEMIAGNYDRLTGTKESGEKVVSTFVPGNLNELIMCFDMVNNLPETNAIQNGMRKQSGGMIMDAEKAGHSEDVCTYVKADIGMMGRGNIAPNGKPMPAPDMLLLSYTGCFTFMKWFELLRHEYKCPTVMLQIPYQGDGKITKNMRDFVVKQLKEEVIPMFEQVSGVKFDIDRLREYLKNSAKAEDDLVWVLESAKNRPSPIDAYFGGVYYIGPMFTAFRGTADAVEYYGLLRGEIEQRIREGKGPITPEGDMKEEKYRLVVEGPPNWTSFREFWKLFYDEGAVVVASSYTKVGGLYDQGFRH... | Function: Catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring.
Catalytic Activity: 2 ADP + cycloh... |
P42334 | MSFSELNIDAFRFINDLGKEYSMLNPVVYFLAEYMMYFLALGLVVYWLTRTTKNRLMVIYAVIAFVVAEILGKIMGSLHSNYQPFATLPNVNKLIEHEIDNSFPSDHTILFFSIGFLIFLFHKKTGWLWLVLAFAVGISRIWSGVHYPLDVAAGALLGVLSALFVFWTAPKLSFIHQMLSLYEKVEQRIVPSKNKSNDKSKNF | Function: Part of the binding-protein-dependent transport system for bacitracin that confer resistance to this antibiotic; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23274
Sequence Length: 203
Subcellular Location: ... |
P94571 | MNYEIFKAIHGLSHHNSVLDSIMVFITEYAIVAYALILLAIWLFGNTQSRKHVLYAGITGIAGLVINYLITLVYFEPRPFVAHTVHTLIPHAADASFPSDHTTGALAISIAMLFRNRKIGWPLVIFGLLTGFSRIWVGHHYPVDVLGSLVVAIIIGFLFFRFSDLLRPFVDLVVRIYEAIINKLTKKPTDQNF | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21723
Seque... |
O87874 | MSTADIIARCEALYEDLDFTAARQWKEADPSRKVIAYMPVYVPREIIHAAGMLPLGIMGGGDGLEVIHGDAFYQSYICRIPRSTIELGLSKRMDFVDGMLFPSICDVIRNLSGMWKLMFPGKYVRYFDVPQNYRDDVGGNYYTAELNELREGLEHLSGRKITDDALRASIKVYNENRKLVQDVYGLRSREPWKVPSADVYLLMRAGLVLPVEEHNQMLKDYLAAAVKVEAQKRDNCRVIINGSFCEQPPLNLIKSIELSGCYIVDDDYMIVHRFLRNEVSTAGDPMQNLSLAFLHESISTAAKYDDKEEDKGKYLLEQVR... | Function: Catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring.
Catalytic Activity: 2 ADP + cycloh... |
O87877 | MTITAGIDIGTGAVKTVLFRVEGDKTEWLAKRNDRIRQRDPFKLAEEAYNGLLEEAGLKASDVDYVATTGEGESLAFHTGHFYSMTTHARGAVYLNPEARAVLDIGALHGRAIRNDERGKVETYKMTSQCASGSGQFLENIARYLGIAQDEIGSLSTQADNPEVVSSICAVLAETDVINMVSRGISAPNILKGIHISMAGRLAKLLKSVGARDGVVLCTGGLALDEGLLKTLNESIQEQKMAVVAYNHPDSPYAGAIGAALWGAFRHEKLARLGQQQVAEAA | Cofactor: The iron-sulfur cluster may be a [4Fe-4S] cluster.
Function: Catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substitu... |
Q5WNW9 | MEFNEKLQQLRTGKNLTQEQLAEQLYVSRTAISKWESGKGYPNMESLKCISKFFSVTIDELLSGEELITLAETENRSNLKKIYNYIYGILDMMAVAFIFLPLYGNSVGGYVYAVNLLSFTATTPFNLAVYWSAFAALIIIGIGKIISTHLDKEKWGGIATKCSLTITALAVCFFAAAREPYITVLVFLLLIGKIFVWIKQMGMK | Function: Functions as both a membrane-bound sensor and transducer of bacitracin availability to activates transcription of the bcrABD operon in the presence of bacitracin . Binds specifically to two inverted repeat sequences on the bcrABD promoter, irrespective of bacitracin concentration .
Location Topology: Multi-pa... |
P28246 | MTTRQHSSFAIVFILGLLAMLMPLSIDMYLPALPVISAQFGVPAGSTQMTLSTYILGFALGQLIYGPMADSFGRKPVVLGGTLVFAAAAVACALANTIDQLIVMRFFHGLAAAAASVVINALMRDIYPKEEFSRMMSFVMLVTTIAPLMAPIVGGWVLVWLSWHYIFWILALAAILASAMIFFLIKETLPPERRQPFHIRTTIGNFAALFRHKRVLSYMLASGFSFAGMFSFLSAGPFVYIEINHVAPENFGYYFALNIVFLFVMTIFNSRFVRRIGALNMFRSGLWIQFIMAAWMVISALLGLGFWSLVVGVAAFVGCV... | Function: Involved in sulfonamide (sulfathiazole) and bicyclomycin resistance . Probable membrane translocase. A transporter able to export peptides. When overexpressed, allows cells deleted for multiple peptidases (pepA, pepB, pepD and pepN) to grow in the presence of dipeptides Ala-Gln or Gly-Tyr which otherwise inhi... |
P45123 | MNQQKSTFIFILTLGILSMLPPFGVDMYLPSFLEIAKDLDVSPEQVQHTLTSFAYGMAFGQLFWGPFGDSFGRKPIILLGVIVGALTALVLTEINSVGNFTALRFVQGFFGAAPVVLSGALLRDLFSKDQLSKVMSTITLVFMLAPLVAPIIGGYIVKFFHWHAIFYVISLVGLLAAALVFFIIPETHKKENRIPLRLNIIARNFLLLWKQKEVLGYMFAASFSFGGLFAFVTAGSIVYIGIYGVPVDQFGYFFMMNIVTMIFASFLNSRFVTKVGAETMLRIALAIQFLSGMWLILTALLDLGFWPMAIGVAFFVGPNP... | Function: Involved in sulfonamide (sulfathiazole) and bicyclomycin resistance. Probable membrane translocase (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43459
Sequence Length: 398
Subcellular Location: Cell inner membrane
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Q54HY8 | MNHLKDQSKSIVLGISSGIGIFLISGGINIFKNVGQYILNRINSNIYYRIDVDSKDKSFEWLLYWLSENDSIKVSNHLNAETVYNLVGKNPKVILVPSVGKHRIVYKGKWIWIDRVRDQQFDMGAGAPFESISISTYKSNAQLINQLLQEAMTLSLNRDIGKTVIYINGGNGNWERFGNPRSIRSLSSVILADDLKSKLIEDIKSFITNESWYRNRGIPYRRGYLLYGEPGNGKSSLINAIAGELNLDICIVSLSSKDIDDKQINHLLNNAPPKSILLIEDIDAAFKSHRDNVDSNNNNSNNNNSLTYSGLLNALDGVAS... | Function: Chaperone necessary for the assembly of mitochondrial respiratory chain complex III.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 47356
Sequence Length: 421
Subcellular Location: Mitochondrion inner membrane
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Q54DY9 | MENVITNNNKGLPKSILKFIPEPIQPLFENPFFSAGFGLIGVGSILAMGRKGFQQAMIQSRRYFFVSVEVPSKDKSFHWLMEWLATKKNKNTRHVSVETTFHQHESGDIVSRINFVPSVGTHYVFYRGRVIKVERSREKNVIDMNSGNLWESITLTTLGTGRQVFQNLIEEAKEMALEKEEGKTLIYTSMGTDWRRFGHPRRKRPISSVILDKGKSELIIQDVKKFLNNSDWYNDRGIPYRRGYLLYGPPGTGKSSFITALAGELQLSICILNLAGKSVSDTSLNQLLATAPQRSIILLEDIDSAIQTGNHDLSAKSNSA... | Function: Chaperone necessary for the assembly of mitochondrial respiratory chain complex III.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 51361
Sequence Length: 458
Subcellular Location: Mitochondrion inner membrane
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Q5E9H5 | MPLSDFVLALKDNPYFGAGFGLVGVGTALALARKGAQLGLVAFRRHYMITLEVPARDRSYAWLLSWLTRHSTRTQHLSVETTYLQHESGRISTKFEFVPSPGNHFIWYQGKWIRVERSREMQMIDLQTGTPWESVTFTALGTDRKVFFNILEEARELALQQEEGKTVMYTAVGSEWRPFGYPRRRRPLNSVVLEQGVTERIVRDIREFIDNPKWYIDRGIPYRRGYLLYGPPGCGKSSFITALAGELQHSICLLSLTDSSLSDDRLNHLLSVAPQQSLVLLEDVDAAFLSRDLAAENPIKYQGLGRLTFSGLLNALDGVA... | Function: Chaperone necessary for the assembly of mitochondrial respiratory chain complex III. Plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): ... |
P50736 | MIQEKAIIIGGGPCGLSAAIHLKQIGIDALVIEKGNVVNSIYNYPTHQTFFSSSEKLEIGDVAFITENRKPVRIQALSYYREVVKRKNIRVNAFEMVRKVTKTQNNTFVIETSKETYTTPYCIIATGYYDHPNYMGVPGEDLPKVFHYFKEGHPYFDKDVVVIGGKNSSVDAALELVKSGARVTVLYRGNEYSPSIKPWILPEFEALVRNGTIRMEFGACVEKITENEVVFRSGEKELITIKNDFVFAMTGYHPDHQFLEKIGVEIDKETGRPFFNEETMETNVEGVFIAGVIAAGNNANEIFIENGRFHGGHIAAEIAK... | Function: S-bacillithiolation is the formation of mixed disulfide bonds between protein thiols and the general thiol reductant bacillithiol (BSH) under oxidative stress. BSH is an equivalent of glutathione (GSH) in Firmicutes. This protein is a NADPH-dependent bacilliredoxin reductase, which debacillithiolates (removes... |
Q08347 | MIGAFKRNRGSSQSFAKECQPSTLKANLEVAKELPFSDRRDFEDATQGYIGSLSDEQIIGPDGGVVWCMKSYGFLEPETPANTVNPSLWRQAQLNAIHGLFKITDNVYQVRGLDISNMTIIEGNTSLIIIDTLFTTETAQESLKLYYRHRPQKPVRTVIYTHSHSDHYGGVKGIVKEADVKSGEVQIIAPVGFMESVVAENILAGNAMHRRSQYQFGMLLSPSVKGHVDCGIGKAASHGTVTLIAPTIIIEEPVEERTIDGVDFVFQLAPGSEAPSEMLIYMPQQRVLNMAEDVTHHMHNLYALRGVEVRDGNQWAKYID... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Alkyl/aryl-sulfatase. Enables the use of SDS and 4-nitrocatechol as sulfur source.
Sequence Mass (Da): 72646
Sequence Length: 646
EC: 3.1.6.-
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O13932 | MGSRFGRRKERNGDMLPLYESQSPQHLDSLENENDERISKLTGKVKSLKELTMNIGTEITSSTKLMESMNDSFDSTKSLLSGTMTRLKNVSKNGGISIWMWLAFFCLVALILVLVRF | Function: SNARE required for targeting and fusion of ER-derived transport vesicles with the Golgi complex.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 13251
Sequence Length: 117
Subcellular Location: Golgi apparatus membrane
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P22804 | MSSRFAGGNAYQRDTGRTQLFGPADGSNSLDDNVSSALGSTDKLDYSQSTLASLESQSEEQMGAMGQRIKALKSLSLKMGDEIRGSNQTIDQLGDTFHNTSVKLKRTFGNMMEMARRSGISIKTWLIIFFMVGVLFFWVWIT | Function: SNARE required for targeting and fusion of ER-derived transport vesicles with the Golgi complex.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 15720
Sequence Length: 142
Subcellular Location: Golgi apparatus membrane
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A0A0C6DWS6 | MPPTNGQTAIIQSKTCPTPTTLPLVVAHGRPLPPLPSSHHVRVRVLAVGLNPTDHKMVTHFFMQDNTTGCDFCGIIEEVGSASALPLGLRVCGADFPYRPSNPYNGAFAEYAVADSRHLLQIPDAISNIQAAAIGAIGWGTAALAMSDPTALNLPGTPSKPDARSLPVLVYGGATATGIIAIQMLKRSGYIPIAVCSAQSAPLCISLGAVGTACYTSTTCVQDIKALANGQSIKHALDCITDPESTTVCLASLARIGGRYACLEAVSDACITRRSVAVKVVMGFEGQNFDVDLGHPVYSRKANPALHAVAAQWAAELQPL... | Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of betaenones, phytotoxic polyketides involved in leaf spot disease in sugar beets . The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase bet1 and the enoyl reductase bet3 via condensat... |
A0A0C6E5D0 | MKSFATTVLLVTPGIYAAALSGRQGQAINSSCKVIPGDTAWPSRQIWSQLNDTLDGRLIQSTPQAAVCRPGGYGSISENGTECTTLKEDWDYAKAFLDSAVEIMNPWYQNTSCSPFYRVDQPCTLGNYVSYAIPVSGPEDVVTAINFTQTHNVRLVIKNTGHDYLGKSTGTGGLSLWTHNLQSKQIVNYTSPAYSGPAIKVGAGVTGGEALLHASQFGYRLVSGDCSTVGYAGGYSSGGGHSLLNSVHGMAADNVLEWEVVTADGRHLVASATQNSDLYWALSGGGAGNLAVVLSMTAKVHPDGLVGAATLSFNATSSPS... | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of betaenones, phytotoxic polyketides involved in leaf spot disease in sugar beets . The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase bet1 and the enoyl reductase bet3 via conde... |
A6X2G8 | MKAQPKASHFIGGAFVEDKTGKPSPVIYPATGEEIARLYSATPDVIEAAYAAALKAQGEWAALKPVERGRILRRTADILREKNKKLSKLETLDTGKALQETLVADAASAADALEFFGGIISGFNGEFVELGGSFAYTRREALGICVGIGAWNYPIQIAAWKSAPALAMGNAFIFKPSENTPLSALALAEAYKEAGLPDGLFNVVQGFGDVGAALVNHRLTAKVSLTGSVPTGKRIMAQAGEHLKHVTMELGGKSPIIVFDDADIESAIGGAMLGNFYSTGQVCSNGTRVFVHKNLRERFVERLVERTRKIRIGDPLDEAT... | Cofactor: Binds 2 potassium ions per subunit.
Function: Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid.
Catalytic Activity: betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH
Sequence Mass (Da): 52218
... |
Q9WTZ9 | MANVHQENEEMEQPLQNGQEDRPVGGGEGHQPAANNNNNNHNHNHNHHRRGQARRLAPNFRWAIPNRQMNDGLGGDGDDMEMFMEEMREIRRKLRELQLRNCLRILMGELSNHHDHHDEFCLMP | Function: May be a signaling adapter molecule involved in p75NTR-mediated apoptosis induced by NGF. Plays a role in zinc-triggered neuronal death.
PTM: Ubiquitinated (Probable). Degraded by the proteasome.
Sequence Mass (Da): 14542
Sequence Length: 124
Domain: The nuclear export signal is required for export from the n... |
Q9NWD9 | MESKEELAANNLNGENAQQENEGGEQAPTQNEEESRHLGGGEGQKPGGNIRRGRVRRLVPNFRWAIPNRHIEHNEARDDVERFVGQMMEIKRKTREQQMRHYMRFQTPEPDNHYDFCLIP | Function: May play a role in microtubule deacetylation by negatively regulating the SIRT2 deacetylase activity toward alpha-tubulin and thereby participate in the control of cell cycle progression and genomic stability.
PTM: Ubiquitinated and degraded by the proteasome.
Sequence Mass (Da): 14067
Sequence Length: 120
Su... |
Q9CWT2 | MASKFKQVILDLTVEKDKKDKKGGKASKQSEEEPHHLEEVENKKPGGNVRRKVRRLVPNFLWAIPNRHVDRNEGGEDVGRFVVQGTEVKRKTTEQQVRPYRRFRTPEPDNHYDFCLIP | Function: May play a role in microtubule deacetylation by negatively regulating the SIRT2 deacetylase activity toward alpha-tubulin and thereby participate in the control of cell cycle progression and genomic stability.
PTM: Ubiquitinated and degraded by the proteasome.
Sequence Mass (Da): 13820
Sequence Length: 118
Su... |
Q5R590 | MESKEELAANNLNGENAQQENEGREQAPTQNEETRHLGGGEGQKPGGNIRRGRVRRLVPNFRWAIPNRHIEHNEARDDVERFVGQMMEIKRKTREQQMRHYMRFQTPEPDNHYDFCLIP | Function: May play a role in microtubule deacetylation by negatively regulating the SIRT2 deacetylase activity toward alpha-tubulin and thereby participate in the control of cell cycle progression and genomic stability.
PTM: Ubiquitinated and degraded by the proteasome.
Sequence Mass (Da): 14051
Sequence Length: 119
Su... |
P22930 | MTTENAAIPTKKKKSFWKKMKPLFGLTVLIPTAFSAVYFGLFASDIYVSESSFVVRSPRSQSSLSGVGALLQSTGFSRSQDDTYSVQEYMRSRTALSALEQGLPLRTFYSEKGDLLSRFNGFGLNDTQEAFYRYFKERLSVDVDSISGIATLRVHAFDAEEGYQINERLLKEGESLINRLNERARKDTIEFAEQAVKDAEKNVNETAQALSQYRIKNKIFDLPAQSGVQLSLISSLKSELIRVETQLAQLVSITPDNPQVPALQMRQKSLKKEIDEQTRQLSGNGNSAATQTADYQRLMLANELAQQQLAAAMTSLQNTR... | Function: May form an ATP-driven capsule polysaccharide export apparatus, in association with the BexA, BexB and BexD proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42292
Sequence Length: 377
Subcellular Location: Cell inner membrane
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P9WQ26 | MNTSASPVPGLFTLVLHTHLPWLAHHGRWPVGEEWLYQSWAAAYLPLLQVLAALADENRHRLITLGMTPVVNAQLDDPYCLNGVHHWLANWQLRAEEAASVRYARQSKSADYPSCTPEALRAFGIRECADAARALDNFATRWRHGGSPLLRGLIDAGTVELLGGPLAHPFQPLLAPRLREFALREGLADAQLRLAHRPKGIWAPECAYAPGMEVDYATAGVSHFMVDGPSLHGDTALGRPVGKTDVVAFGRDLQVSYRVWSPKSGYPGHAAYRDFHTYDHLTGLKPARVTGRNVPSEQKAPYDPERADRAVDVHVADFVD... | Function: Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position (Probable). Is probably involved in the biosynthesis of 6-O-methylglucosyl lipopolysaccharides (MGLP) (By similarity).
Ca... |
Q5JDJ7 | MKGYLTFVLHTHIPYVRKHGKWPFGEEWVFEAISETYIPLLMEFERLRDSGVKFGIVINVTPVLAEQLTDEYMKKAFEEYMERKLKAMEEDLKSGKYDEKAVSYMLNYFRKVYDYWKAINGDIIGKLRELQDQGYVEVITSAATHGYLPLLGRDEAIRAQIANGVATYEKHFGMKPKGIWLPECAYRPAGEWELPGGRKVKRQGIEKFLEEFGLRYFFVESRLIDEGPASNVYGEVLIADTEKTTLRPYWIKGSNVAVFARNRETGHQVWSAHYGYPGDFWYREFHKKAPKSGGQYWRITSKEVGLGEKEFYDPDKAMER... | Function: Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position. The branch chain-length distribution of the reaction products shows degree of polymerization (DP) of 5 to 30, with two l... |
Q5SH28 | MARFALVLHAHLPYVRAHGMWPFGEETLYEAMAETYLPLIRVLERLRAEGVEAPFTLGITPILAEQLADARIKEGFWAYAKDRLERAQGDYQRYRGTALEASARHQVAFWELTLDHFQRLSGDLVAAFRKAEEGGQVELITSNATHGYSPLLGYDEALWAQIKTGVSTYRRHFAKDPTGFWLPEMAYRPKGPWKPPVEGPPEGVRPGVDELLMRAGIRYTFVDAHLVQGGEPLSPYGEAALGPVESQEATYHVHELESGLRVLARNPETTLQVWSADYGYPGEGLYREFHRKDPLSGLHHWRVTHRKADLAEKAPYDPEA... | Function: Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position. The branch chain-length distribution of the reaction products shows degree of polymerization (DP) of 3 to 13, with two l... |
P47113 | MSIRPLTLNGLDEPETSFEELNTTLPRFQSHETLTLEENVPPLSTSTYIPPPSSVGTSDTGTVFSNSTSAFWSNKQADDDQDMEVDQDDEFLNDFQEFQNKKDDFDDAIKTNFHLRNGCRTGPFKNDIFAEEFDRKLSLEDKPRLKQPRSMMELKPKRKLSNSVTSRNLRSGNSVRFKKSMPNLALVNPAIREEEEDEEREREDQREFNYKIDNDTQDTILAKFSSDDEGDFLTGFEELEGEAIDETISSNDKESADHPRFLKKSSSSLPLKISPAQYDIVKHDELLTPGLHRRQRDWNTQQELDSFKEKRSVRHCSNQN... | Function: Part of a checkpoint which monitors spindle integrity and prevents premature exit from mitosis. This cell-cycle arrest depends upon inhibition of the G-protein TEM1 by the BFA1/BUB2 complex.
PTM: Multiply phosphorylated in a cell-cycle-dependent manner with the major phosphorylation occurring in mitosis.
Sequ... |
A1DJ58 | MKFLLRRFIALAAASSVVAAPSVSHLSLQDAANRRELLQDLVTWDQHSLFVRGERLMIFSGEFHPFRLPVPGLWFDVFQKITSLGFNAVSFYTDWGLMEGNPGHVVTDGIWSLDEFFTAASEAGIYLIARPGPYINAETSAGGIPGWVLRLKGIIRSNSEDYLRATDTYMATLGKIIAKAQITNGGPVILVQPENEYTTWPNVSESEFPTTMNKEVMAYAEKQLRDAGVVVPTVVNDNKNLGYFAPGTGLGETDLYGIDAYPMRYDCGNPYVWPTYRFPRDWQHTHRNHSPTTPFAIMEFQGGSGDGWGGVTEDGCAILV... | Function: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 111421
Sequence Length: 1011
Subcellular Location: Secreted
EC: 3.2.1.23
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C8WV58 | MAKHAPIFPNVQGFLHGGDYNPDQWLAYPDVLEQDVQLMREAKWNVVSLGIFSWVSLEPEEGLFTFEWLDEAIERLTHAGVRILLATPSGARPAWLSAKYPEVLRVGPDGRRNRHGGRHNHCYTSPIYREKVRIINRKLAERYAHHPGVIGWHVSNEYGGECHCPLCQEAFREWLKRKYKTLDALNHAWWTPFWSHTYTDWSQIESPMPHGETSIHGLNLDWKRFVTDQTVDFCRHEIEPLKQVNPNLPVTTNFMGTYPGLNYWRFRDVLDVISWDSYPRWHAHETLVPEAVHTAMVHDLNRSILKKPFLLMESTPSVTN... | Function: Hydrolyzes o-nitrophenyl-beta-D-galactopyranoside (ONPG) and p-nitrophenyl-beta-D-fucopyranoside (PNPF), but not p-nitrophenyl-beta-D-glucopyranoside (PNPG), p-nitrophenyl-beta-D-xylopyranoside (PNPX) or p-nitrophenyl-beta-D-arabinopyranoside (PNPA). Also hydrolyzes lactose, including lactose in milk.
Catalyt... |
A1A399 | MSARRNFEWPELLTADGRGIAFGGDYNPDQWSEDIWDDDIRLMKQAGVNTVALAIFSWDRIQPTEDRWDFGWLDRIIDKLGNAGIVVDLASATATAPLWLYESHPEVLPRDKYGHPVNAGSRQSWSPTSPVFKEYALTLCRKLAERYGTNPYVTAWHMGNEYGWNNREDYSDNALEAFRAWCRRKYGTIDALNQAWGTTFWGQEMNGFDEVLIPRFMGADSMVNPGQKLDFERFGNDMLLDFYKAERDAIAEICPDKPFTTNFMVSTDQCCMDYAAWAKEVNFVSNDHYFHEGESHLDELACSDALMDSLALGKPWYVME... | Function: Involved in the hydrolysis of transgalactooligosaccharides (TOS). Highly active towards Gal(beta1-4)Gal and Gal(beta1-4)-Gal-containing oligosaccharides. Low activity towards Gal(beta1-3)Gal, lactose and Gal(beta1-3)GalOMe. No activity towards Gal(beta1-6)Gal, Gal(beta1-4)Man, Gal(alpha1-4)Gal, Gal(alpha1-3)G... |
Q93GI5 | MEHRAFKWPQPLAGNKPRIWYVGDYNPDQWPEEVWDEDVALMQQAGVNLVSVAIFSWAKLEPEEGVYDFDWLDRVIDKLGKAGIAVDLASGTASPPMWMTQAHPEILWVDYRGDVCQPGARQHWRATSPVFLDYALNLCRKMAEHYKDNPYVVSWHVSNEYGCHNRFDYSEDAERAFQKWCEKKYGTIDAVNDAWGTAFWAQRMNNFSEIIPPRFIGDGNFMNPGKLLDWKRFSSDALLDFYKAERDALLEIAPKPQTTNFMVSAGCTVLDYDKWGHDVDFVSNDHYFSPGEAHFDEMAYAACLTDGIARKNPWFLMEHS... | Function: Specific for beta-D-anomer-linked galactoside substrates. Hydrolyzes o-nitrophenyl-beta-D-galactopyranoside (ONPG), chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-gal) and to a lesser extent lactose. Hydrolyzes p-nitrophenyl-beta-D-galacturonide very slightly. Does not hydrolyze maltose, suc... |
P49676 | MKMKQFNLLSLFLILITSFGSANSTIVSHDERAITIDGQRRILLSGSIHYPRSTSDMWPDLISKAKDGGLDTIETYVFWNAHEPSRRQYDFSGNLDLVRFIKTIQSAGLYSVLRIGPYVCAEWNYGGFPVWLHNMPDMKFRTINPGFMNEMQNFTTKIVNMMKEESLFASQGGPIILAQIENEYGNVISSYGAEGKAYIDWCANMANSLDIGVPWIMCQQPHAPQPMIETCNGFYCDQYKPSNPSSPKMWTENWTGWFKNWGGKHPYRTAEDLAFSVARFFQTGGTFQNYYMYHGGTNFGRVAGGPYITTSYDYDAPLDE... | Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 93019
Sequence Length: 828
Subcellular Location: Secreted
EC: 3.2.1.23
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Q9TRY9 | MARPAAVRVLWALLLPLLLGSARGLRNASQRTFTIDYSHNRFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNAIQTYVPWNFHEPQPGQYQFSGEQDVEYFIKLAHELGLLVILRPGPYICAEWDMGGLPAWLLLKESIILRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPIITMQVENEYGSYFTCDYDYLRFLQKLFHHHLGNDVLLFTTDGANEKFLQCGALQGLYATVDFGPGANITAAFQIQRKSEPKGPLVNSEFYTGWLDHWGQPHSTVRTEVVASSLHDILAHGANVNLYMFIGGTNFAYWNG... | Function: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Sequence Mass (Da): 74992
Sequence Length: 668
Subcellular Location: Lysosome
EC: 3.2.1.23
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Q9RFN0 | MLQQKKLFYGGDYNPEQWSKAIILEDMRLMKKANVNYVSLNIFGWASIQPTEEGFDFSFLDEMLDLLWENGIGIDLANGTASPPAWLVKKHPEILPVTSQGTPLVHGSRQHYCPSNKVYRSYVIRLTEEVAKRYATHPGIVMWHVNNEYTCHISECYCESCEKSFRQWLQMKYKKINTLNECWSTKFWSQSYSQWDEIFLPKEMPTFKNPAHQLDYKRFISDQNLTLFKAEKKAIRSYSKDIPVMTNLMGLHKHVDGFAFAEEMDVVGWDSYPNPFEEKPYPQFLANDLTRSLKKKPFLVMEQAPSAVNWRRANGAKSPG... | Function: Capable of hydrolyzing the chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) at low temperatures. pNP-beta-galactoside, pNP-beta-fucoside and pNP-beta-galacturonide are also hydrolyzed, but not pNP-beta-galactosidase, pNP-alpha-galactoside, pNP-beta-mannoside, pNP-beta-arabanoside, pNP-bet... |
D9SM34 | MRIGVDYYPEHWDRQLWEKDAQLMKEIGVKVVRLAEFAWCKLEPIEGQYDFKWLDDVIEIFSVRNIEIVLGTPTNTPPLWLYEKYPDAIQVNESGERQFIGIRGHRCYNSSSMRKYTKAIVEAMTERYANNKAVIGWQIDNELDATHCCCDNCTEKFRGWLKNKYSTLENINKEYGNVVWSGEYSAWSQVTAPLGGSPFLNPSYLLDYNRFASDSMVEYIDFQREIIRKNCPSQFITTNTWFTGNLPNFYDAFENLDFVSYDNYPTTNEITDEEELHSHAFHCDLMRGIKKKNFWIMEQLSGTPGCWMPMQRTPKPGMIK... | Function: Involved in plant cell wall degradation in cooperation with cellulosome. Hydrolyzes both p-nitrophenyl-alpha-L-arabinopyranoside (pNPAp) and p-nitrophenyl-beta-D-galactopyranoside (pNPGp), with higher activity for pNPAp. Shows hydrolysis activity against p-nitrophenyl-beta-D-fucopyranoside (pNPFp), but not ag... |
Q8L7J2 | MGRIKSSSGRCSTARLEAVAVLVVVFGVASSSLRGCIAQQSGGGLTRGSFPEGFVFGTASAAYQYEGAVKEDGRGQTIWDTFAHTFGKITDFSNADVAVDQYHRFEEDIQLMADMGMDAYRFSIAWSRIYPNGVGQVNQAGIDHYNKLIDALLAKGIQPYVTLYHWDLPQALEDKYKGWLDRQIVDDFAAYAETCFREFGDRVKHWITLNEPHTVAIQGYDAGLQAPGRCSVLLHLYCKAGNSGTEPYVVAHHFILAHAAAASIYRTKYKATQNGQLGIAFDVMWFEPMSNTTIDIEAAKRAQEFQLGWFADPFFFGDYP... | Function: Hydrolyzes glycosides, oligosaccharides and hydrophobic glycosides . Possesses gibberellin ester beta-D-glucosidase activity. Can hydrolyze gibberellin A4 beta-D-glucosyl ester in vitro .
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence... |
Q75I93 | MAARRANCALVLVLALALLAARDAGAAAVPKPNWLGGLSRAAFPKRFVFGTATSAYQVEGMAASGGRGPSIWDAFAHTPGNVAGNQNGDVATDQYHRYKEDVNLMKSLNFDAYRFSISWSRIFPDGEGRVNQEGVAYYNNLINYLLQKGITPYVNLYHYDLPLALEKKYGGWLNAKMADLFTEYADFCFKTFGNRVKHWFTFNEPRIVALLGYDQGTNPPKRCTKCAAGGNSATEPYIVAHNFLLSHAAAVARYRTKYQAAQQGKVGIVLDFNWYEALSNSTEDQAAAQRARDFHIGWYLDPLINGHYPQIMQDLVKDRL... | Function: Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl beta-D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-arabinoside, oligosaccharides, pyridoxine beta-D-glucoside and the cyanogenic glucosides amygdalin, prunasin and dhurr... |
Q75I94 | MGCAPAAHYLPGGGWRRLLVVVVALVVLDRAGARVRAADDDTGGLSRAAFPKGFVFGTATSAFQVEGMAASGGRGPSIWDPFVHTPGNIAGNGNADVTTDEYHRYKEDVDLLKSLNFDAYRFSISWSRIFPDGEGKVNTEGVAYYNNLIDYVIKQGLIPYVNLNHYDLPLALQKKYEGWLSPKIVGVFSDYAEFCFKTYGDRVKNWFTFNEPRIVAALGHDTGTDPPNRCTKCAAGGNSATEPYIVAHNIILSHATAVDRYRNKFQASQKGKIGIVLDFNWYEPLTNSTEDQAAAQRARDFHVGWFLDPLINGQYPKNMR... | Function: Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl beta-D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-arabinoside, cello-oligosaccharides, laminari-oligosaccharides, sophorose and gentiobiose.
Catalytic Activity: Hydroly... |
Q75C24 | MQNVASWLLALVVAVVQGELLPGKSAPALLWSYKLSEGIQEYQLAYNMTTVLPAPEFNAIALELLDHCNSHAYVFVNQPGLRLEDFDYEDAWTVLPNYLSRSSSALRFEQVEVSPSNVFENLIAHTKRRCDVQREIILRAEQTNQFEPYIDAQSRIIQVHFSPLPGDGRNERPSREDVLADHDQRLRRILGRLPSPAVTVIYTSLEPADRLSASPPRAGIFPEIFEHESRRIEYERNDRDLQVNRYFPSHHPKMEPIEEVELSLLDPKFIQSNLKLLKLIAVSAIGSLTWQLYSLFSPKLPVATPKGTAKRQKGQKKLVK... | Function: Required for normal beta-1,6-glucan synthesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 39105
Sequence Length: 344
Subcellular Location: Endoplasmic reticulum membrane
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Q59WG7 | MRLFVLLAYIIPFILCQLTPVLVASHKLVRGLKEEINPSNTLPHNVTSVTNMLKKLITECSSDAYLLINQPGLTYADLTTEKKDNWPFLRNYLYMSSTIVGLPRVENPIDLDFLEQYIISNCDAETINVWHDSEDEVVDYYDIRKRVIRIDLSPLSISNHDDRVKEIFEHDQLIRKILRKLPSAHYTIILTSLEPGIIHPVPRFLMEETPASFEIFDDIINDPFHNREIEKNDRFHKVEPNWNPIRDSNDRYYRNKKKDEIHLFDYELWEKNEKLITTIFVMVLSLFMMKIISFFNYLKQKIIQKKQQKSKRGIIADDKK... | Function: Required for normal beta-1,6-glucan synthesis, for hyphal morphogenesis, adhesion and virulence.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 38099
Sequence Length: 322
Subcellular Location: Endoplasmic reticulum membrane
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Q6FKH5 | MCGLIGIIIGLLTRVALASSLDVGTSPAILFSTRLSEGILEYYDMFDSGAVVPREDFNTVCKTLISHCNSDAVVFVNQPGLSLGDLSEYADQFQYLSSYVRHSSSAMNIERVSVSQDDQESQFESLVRYAMDTCNIYEKVVIEPYEADTYKAYIDAEKKVILIELPEFLNTQNETDRMALISSNDNRLRNILGQLPSPDISVIYTSFQPSNLAADEFAEILPAAFDVFDKNAAVERNIRLKDATRPGFINYRPKFGDFNSISQIKLDKQFLEENLGLLSAILVSTILYLFGQRLSSHSKSQNTTSNSAKNTTKKAERGN | Function: Required for normal beta-1,6-glucan synthesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 35559
Sequence Length: 319
Subcellular Location: Endoplasmic reticulum membrane
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Q6BHZ8 | MFISIRRLVALVAITQLVASFSAVPVLVASHRLAKGLKEELNGSGPQAPESATNLIKRLVTECSSDEYLVINQPGLVLEDMTVNEADNWPFLRRYIAMASSVVGIPWVRGALDLDFIEQYIISTCHAETMNVVHDDDQEVGNYIDTRTRVIKIDLSELPPRSDLELRYSVIREHDELIRKIIRKLPSPHYTIILTSDMPQNVHPIPNMVVESQPDKYQIFHDLVNDPSRELEIERNDRFHQTIEPYWSPDRNTINRYMENKKKDEIHFFDYDLWTRNEKLILTIIVMVLTLFTFQLTKLVKLLTETVFKKDKGLITHTKS... | Function: Required for normal beta-1,6-glucan synthesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 37170
Sequence Length: 321
Subcellular Location: Endoplasmic reticulum membrane
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Q6CMA4 | MQPSFMTMNELIVFALLLTPLLAARQQSVPGLLFSYNLAPGIVKYQDKYDNAQLPQDDFLKVAKDLISQCHSETYVFVNQPGLSRSDFKQHKQSMHKLYNYVLTSSTTVKFEKIDIVQNDDIYEELIAYTMDKCNIDDKIDIGGNVTDRYQPFVEARTRVLRVDFPPLPQQGQYVEGIGTRKDVLQANDEYLRYVMGTLPTPKHTVFYMSLEKSEVPDTETSLSYDIWPEIFTNPQRKVEIDRNDRVAKEMPKLVPYRPRIDTEDDKYLTVLDQEFIDNHYGIIVLIIGVTIAFILLQLGAVKVKKPSKPQITKDVTKEK... | Function: Required for normal beta-1,6-glucan synthesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 37243
Sequence Length: 323
Subcellular Location: Endoplasmic reticulum membrane
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Q6CB37 | MKLALLSLIGTALATPAVMLSHKELTAFEKYTNKQTSNSISAVELDRVARKLMHDCSANTYVVVNQPGLKAKDFQTESAFPFLKKLLERTSTMYTVPYADGGIELGKLANSVAKQCGAVKIDVNLDNNITPLEEYMDTTKRVIEINFEPLPNTYVSRLAALAANDEMLEKIVRATPSPFIALILTSQKGEEGDFETRNPDFKIFPGVARAKTVPGAKDKYKYHMELQNVPVDEKKLTAEALLKVKTPPTHAPEVRQTGDGELVDDKLLLMIVGSVVAILLSLLVFNGLMAAKPDVVKVDKTDAKVEKAVKKEVQKKERLV... | Function: Required for normal beta-1,6-glucan synthesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 36711
Sequence Length: 332
Subcellular Location: Endoplasmic reticulum membrane
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P38813 | MQTVLKYLLLIMCGSFCASEELQNQTNVPAIFFSYKLTPGILKYQEDYDRAVTLPRDTFIEAAEKFLGVCNADTYVFINQPGLRKLDFLEFETEFVSLQRYIRRSSTAIKFEKVDLLPQDLYYDLAEFVKEYCNVDQVLNLRGNNTEDFQPFIDSEKRVIIIEYPKLPEDTNERKEAFRHYDKYLRTILAQIPSPEQNVIYTSLNPGTTLAHESIIPIQIFPDIFDIKSRVGEVEQNNRVLDVPRLSFNDYTPRFSEPPSEYVSIFDSQLIENNRGLLQLIFTILVGYILIQFFFTKKTIVDEKITNKKDNVKQTSPQLL... | Function: Required for normal beta-1,6-glucan synthesis.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 39069
Sequence Length: 335
Subcellular Location: Endoplasmic reticulum membrane
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A1BCQ5 | MRPVPLHPDILQAYAVLETGEPVCRELAFALGELHGPDVLDLASLAHKVKLRHGGSSGSIHACSIMNARSGVCSENCRFCAQSAHHQAAIDVYGLVDVDAVLFHARQTASEGISHFGIVTSGFGYKTLSKEFRQILAMIDRLHQELPDLEICASLGVLGEEPALELARHGIAQYNINIQVAPRRYGELIADTHSVDDRIDTIKRLRRNNIDVCCGGIIGVGEQMKERVEMIFAFADLDVSVIPLNILVPIDGTPLEGSPGIPLDDIVKTFALCRLVHPRKIIKIAAGRETVMKDFQGLLMLSGADGLLTGGYLTTRGRAT... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [s... |
B5ECN1 | MEKMINDIAHRIIAGGSITEAEAIQLTQVQGTEVYDLFRAATRVKEHFVGNEVHLCSIINAKSGRCAENCAFCAQSAHHKTDAPVYPLVQEEEMLASARMAETNGSACFGIITSGTTVNGPELEQILTALRRIRKETTILPSCSLGIIDEETARKLKEAGMDTYHHNLETAASFFPQICTTHDYQDDVNTVRAVKKAGVKVCCGGIFGLGESAAQRVEMALTLKDLDVDSVPMNFLNPIEGTRLEGAANITAQECLKTIAIYRLILPGKRITVCGGREKNLRDLQSWIFFAGANGTMIGNYLTTLGRNVDTDLTMFSDLG... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [s... |
Q97MI6 | MKNQWNNILSIGEKVLNGEKITADEALTLSKSNGSDIFLLCSFANKLREKFNGNHVDLCSVINAKSGNCSEDCAFCAQSAHHKANVSCYPLLNEDKILEMAKQREAYGARHCDIATSGLGYTGDEKDFQTILKAFKKMKENTNLKLCACLGTLTEKAMNSLAAVGVERYNHNLETAKSFYKNIVSTHGYDERIKTINYAKNAKMEVCSGMIVGLGETMEQRIEHALLLRDLNVDAVPVNILNPVKGTKLENAKPLSPMEIIKTFAIIRFILPDKIIRYAGGREKNLRSLQPLGFLSGLNGMLIGNYLTTNGQSVNDDFNM... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [s... |
A7GFJ9 | MSNIIKYKKKILNGDLLTKEEVEEILEEDITDLAATANEIRESLCGNKFDLCTIINGKSGRCQENCKYCAQSAHFDTDIIEYNILNSDRIINSAISNYNKGVHRFSVVTSGRALNNNEVDTLCKTYSKLKETCSIRLCASHGLLKYEDLKRLKDSGVTRYHNNLETSRKFFTKICTTHKYDDKIETIKNAKKAGLEICSGGIIGLGETMEDRIDMAFTLRELSVESVPVNILNPIKGTPLENQEILSYEEIIKTLALFRFILPTVQIRLAGGRTIISDNGKKALESGVNGAISGDMLTTLGIETSEDIKMIKNLGFEV | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [s... |
A1SM80 | MQTSFDHLADRILAGGDATPADALAVLRADEKDLLHVVAAAGRLRRARFGNTVKVNYLVNLKSGLCPEDCHYCSQALGSRAPILKYNWLSSEEVLEQAGAGLRGGATRVCLVSSGRGPSDRDVDRVAAMAQELKGEQPGVEICACLGLLKDGQAERLRAAGVDAYNHNINTAESHHDTIVSTHSYSDRVDTIEKAAAAGLSPCSGLIAGLGETDEQLVEALFALKALGADSIPVNFLMPFDGTPSERTFELTPIRCVQILAMTRFVCPDTEIRIAGGREMHLRSLQALALHVANSIFLGDYLTSEGQDARADLEMLRDNG... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [s... |
A6LD84 | MTIEEAKQHILEGGKITEEQALSLANHPDKEALYEAAHQITRHFMGNKFDTCSIINAKSGNCSEDCKWCAQSGHYKTLVNLYPLLPAKECVYHAVYNRKQGIRRFALVTSGKRVSDKELEQITDTIRQIKRQSDIKCCASMGLLTRSQLQSLYDSGVENYHCNIETAPSYFRQLCSTHTIEQKMETIHTAREIGFRICCGGIIGMGETMKERIEMACFLQKEGVLSIPLNLLQPIPGTPMENTQILEEEEWLTTIALFRLINPNAFLRFSGGRAQLSEVTQRKSLHIGINSAIIGDLLTTIGSKVEEDKVLFTSEGYSLT... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [s... |
A5D4Y6 | MFNELVKKIKSGLEITFEEALALGGLDEDRLNELFLAALQVNRHFHGNRVDLCSIVNARSGRCSEDCAFCAQSGHYRTEAPVYPLLSKEEILERAREMELRGARRFALVTSGRGISESDFEKVLDIYQMLKEKTGLGLCASLGIIGYDKAVRLKEAGVGMYHHNLETCRSYFPHICTTHSFDERVETVKAAKEAGLEVCSGGIIGLGESWRHRVEMAFHLKELGVASVPINILTPVKGTPLWGRPLLEPVEVLRTAAMFRLVLPGALIRLCGGREAALRDLQPLALLAGVNALMVGNYLTTSGRRVEDDLQMVADLKLSV... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic Activity: (4R,5S)-dethiobiotin + [s... |
P32451 | MMSTIYRHLSTARPALTKYATNAAVKSTTASSEASTLGALQYALSLDEPSHSWTKSQLKEIYHTPLLELTHAAQLQHRKWHDPTKVQLCTLMNIKSGGCSEDCKYCAQSSRNDTGLKAEKMVKVDEVIKEAEEAKRNGSTRFCLGAAWRDMKGRKSAMKRIQEMVTKVNDMGLETCVTLGMVDQDQAKQLKDAGLTAYNHNIDTSREHYSKVITTRTYDDRLQTIKNVQESGIKACTGGILGLGESEDDHIGFIYTLSNMSPHPESLPINRLVAIKGTPMAEELADPKSKKLQFDEILRTIATARIVMPKAIIRLAAGRY... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine +... |
Q818W9 | MSGFFITATDTEVGKTVVAGAIAGVFRELGYNVGVYKPLQSGHVASNPEGDAARLKSLSGVPTQENEICPYSIEEPLAPRLAMKRAGRVVKLKEITDYYNGLLKEFNSLFVEGAGGLAVPYTEDALVIDFAKELQLPLIVVARPTLGTVNHTVLTIAYAKAHGLTVAGVILSGCKECEMERVQENKEMIEELSGVPVLGLLPFFAGEFTKEEVLESAKEHIMISKLEEFIQNESNVAGAPSM | 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 ... |
P53558 | MRGFFVTGTDTEVGKTVISSGLAALLKDNNRHVGVYKPFLSGISRHHPDSDTSLLKDMSQTSLSHEDITPFAFKAPLAPYVAGKLEGKTVTMEEVLSHWGRIREKHECFIVEGAGGISVPLGEDYLVSHVIKALQLPMIIVARPRLGTINHTFLTVKYAESMGLPIAGIIINGISDSPDEDEKTNPEMIERLCGVPILGVTPKLANVTKETVLHMVKDHINLSLLMNQVGV | 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 ... |
Q9AMS4 | MNKRIVVTGTDTGVGKTVFSAGLAGLLGANYWKPVQAGLEQEIDSECIRRLGGLSSDRIVPELYRLRTPASPHHSAEIDGVRIDTETLGLPDSGERRLVIEGAGGLMVPLTARTLYIDIFERWQLPVVLCARTGLGTINHSLLSIEALRKRQIRILGIAFIGERNAETESAVCEIGRVRWLGRLPWLVPLTNDRLQAAFKDSFVSSDFLNL | 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 ... |
C0QVL9 | MAKAIFITATGTDIGKTYVSGLIAKHMKDKGLNIGYYKAALSGSLDITDSDAWYVKQQADLLDSYDEMVSYTYKHAYSPHLAAQIEGNPPDIKVIKNAYENINKKHDYMIVEGSGGIICPIRYDNNQKIFLEDIIKELNIPSLIIADAGLGTINSAVLTIEYMRSKNLKVNGVILNRFEMANEMHDDNKKMIEEMTGVKIIGIVIDGILKLDEKNIETLFE | 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 ... |
Q9I614 | MPAFFVTGTDTEIGKTTIAAGLLHAARSAGLSTAAAKPVASGCEPTAQGLRNGDALVLLGQCSLALAYEQVNPLAFAPAIAPHLAAREAGVELSAARLHEAVREVLALQADFTLVEGAGGWRVPLLGRENLSDLARLLALPVVLVVGVRLGCINHALLSAEAILGDGLALAGWVANVVDPATSRLEENLATLAERLPAPCLGRVPRLEEATPAAVAAHLDLRPLGIGL | 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 ... |
Q3IGS9 | MKEFFITGTDTDAGKTHVTSLLLKLLAQHKKQAIGFKPLASGCEMAFDQLVNADALILMESATVSAKYDIINPFAFAPAIAPHIAAEQAGVTITADKLSSAYKNVKQQGADYILTEGAGGWALPISNTDYLYNWVKAEQLPVILVVGMKLGCLNHALLTAAHMQSMGINCIGWIANQVDPNMDEYQANLDSLKLRLPFPILAISPYSEQTPKLQIYKTLLENFALNT | 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 ... |
Q7URG0 | MASLYFVTGTDTEVGKTYCTAKTVERMRECGQRVGVYKPVASGCELRADGQRYSVDAATLWQAAGRPKNIDAVCPQRFLAALSPPQSAAREGVKVDTRQLRDGLAIWCDGDFDVVMIEGAGGLFSPISDDWLNVDLAIEMKRWSDQNGHSFELLLVAPDRLGVLHHVISTSRAAESAGIPIAGLILNRMDDHADESTQTNAEDLRRWCGIPMVASVRQPSGPLVVFSGPNGRNASGETSRETAGGVNFLNQTTIRR | 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 ... |
Q0AE73 | MLPDLAEALQQRRQEGLYRFRQVLEGPQSPRVTIDGRDFLAFCSNDYLGLANHPALIEAVAAGAQRYGVGSGASHLISGHSRAHHELEEALAEFVGLPRTLLFSTGYMANMAVVTALMGREDAIFADRLNHASLNDAALLSRARFIRYPHLDLVTLEKQLKTIQARRRLIVTDAVFSMDGDRAPVAELLALCQRFDAWLLLDDAHGFGVLGEQGKGSLYDPQEVERNVPHLIYMATLGKAAGVSGAFVAAQASMIETLIQHSRTYGYTTAAAPLLAHALLTSLQLISQGVWRRERLVQLIEQLRQKLQSLPWQLLLSDTP... | 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... |
Q81ZZ4 | MLADLSEALRERQQEGLYRSRPVLEGPQSPHVTIDGRDFLAFCSNDYLGLANHPALIEAAAEGARCYGVGSGASHLISGHFRAHHELEEALAAFVGLPRTLLFSTGYMANMAVVTALAGRGDAIFADRLNHASLNDAALLSRARFIRYPHLDLDTLARQLETTKARRRLVVTDAVFSMDGDMAPVAELLTLCQRFDAWLLLDDAHGFGVLGERGKGSLYHSQRIERDTPYLIYMATLGKAAGVSGAFVAAQAPVVETLIQHGRTYGYTTAAPPLLAHTLLTSLQLISQESWRRERLALLIERLRQRLHSLPWPLLLSETP... | 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... |
A1AQT1 | MGRTVQDELEQIRAKGLFRSTRLIQGRQSARVTMEGRQLLLLCSNNYLGLAEHPALIAASMAAAEQFGSSSGASRLVSGSMEPHEALETAVAAFKRTESALAFNSGYAANTGIIQALVGRGDVIFCDRLNHASIIDGALLSGARLVRYPHNDAVALAGLMEKQRGTGRCLIVSDGVFSMDGDLAPLAELAELRRRHDALLMVDDAHGCGVLGEQGRGSAELLGVLSHIDIHVGTFGKALGSFGAYAALSRELRDLLVNRARSFIFSTSLPPAVLAVSTAALELVQAAEGDELRKRLRDNTSLFRGLLRDAGFFLGEGNTQ... | 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... |
A9BGL0 | MDFYEQLREELKKLEDSGLLITIRTLESAQGAWININGKKVLNMCSNNYLGLANNERLKEAAINAIKNWGVGPGAVRTIAGTMKIHEELEKKLAEFKKVEATLVVQSGFNANQAVIPTITNEEDGILSDELNHASIIDGVRLSKAKRYIWKHKDLNSLEEQLVKAQRDNCRRKLIITDGVFSMDGDIAPLPGIVELAKKYDALVMVDDAHGEGVLGENGRGIADHFNLTEEVDIEIGTLSKAFGVVGGFIAGKKVLIDYLKQQARPFLFSSSLSPAETAAALEATKILYESDDLVKKLWDNAKYFQSKIKEMGYDIGGTE... | 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... |
Q6LPR3 | MPLSNRRFNHKIKHALEARETQGLYRQRACLSRADQSVYHQGTSLLNFSSNDYLGLAQDPAILSAWQEGLTLFGAGSGASPLVTGFHSAHKALEDQLADWLGYDRALLFNSGFSANQAVLFTIPDKHDVLIQDKLNHASLMEAGLLSPATMRRFAHNDLSALTRLLHQTNDKFPSINPLVITEGVFSMDGDLSPLANISEQCSQHDAWLMVDDAHGCGVLGDKGRGSCDLAGVKADILIVTFGKAFGLSGAAVMCNNDTAEYLIQFARHFIYSTSMPPSQAHALSAACRLIQSDDWRREKLHDLGYLLFENVESSIQLVD... | 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... |
A1VUJ6 | MLIDYLNHQLREREAQGLTRQRRIAESPCAPRQRVSQRGQPARDLLAFCSNDYLGLANHPALVRALAEGAQLYGAGSGASHLISGHSEAHAALEADLAAWLAPCIPNAQALYFCTGYMANLALLTALGGANATIFADKLNHASLVDGALLAKATLQRYAHKSLAVLARQLAACDTPIKLIVTDAVFSMDGDVADLPELLALAERFDAWLVVDDAHGFGVLGEEGRGSLSHFGLCSERLICMGTLGKAAGVGGAFVAAHPSIIDWLVQTARPYIYTTAAPPAVAHALRESLRLIGGTEGDQRRKQLQQLISQLRSQLAELI... | 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... |
Q8D1X1 | MKPFFWRIIGSGSVNLVFIHGWGLNSCIWNNIIIILSNYFKLHLVDLPGYGKNILYKEYSFSKITEIIACKSPKKSILIGWSLGGLIATNISIVYPEKFKGLIIVSSSPCFCEKKDWPGIKKEILNNFSFQLKNDFHNTVKKFFNIQFLGTKKNNNEIKKLKNIFFRQKEPSYKTLSSGLKILKNIDIRNYLKYIKIPTLRIYGNLDVIVPVKIIPIIKKLQNFNINKNIIIPSASHAPFLSHPFLFCKIIKYFIKKFN | 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... |
Q9PDM3 | MYIEVTGYGPALVLIHGWAMHSGVFAPLVEQLRAHHTLYLVDLPGHGYNHTTLTPLALPHVVHAIAAATPPAVWLGWSLGGLFALHAAATLPQVRGLIMLAATPCFVRREDWPHAVEVSIFTQFAEDLKQNYTETINRFLALDTLGSTYAQSELRQLRQILNARHTPNTATLQAGLELLAHTDLRRAVIDLTPPSLWIAGQRDRLVPAASIHAATALAPSGQTELLTITGGGHAPFLSHANQMTAALQHFIATLP | 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... |
A7FNV8 | MKQLYWYTCGEGDCDLVLLHGWGLNSGVWHCIIDRLAPHFRLHLVDLPGYGRSQDYGAMSLADMAERVAQQAPKQALWLGWSMGGLVASQIALSQPECVRGLITVSSSPCFTARDEWPGIKPEVLAGFQHQLSDDFHRTVERFLALQTLGTESSRQDARLLKSVVLQHQMPDVEVLTGGLAILRTADLRTALAGFTLPFMRVYGHLDSLVPRKVASLLDSAWPQTQSVVMQGAAHAPFISHPNDFAKLILNFAEENKK | 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... |
Q89VI2 | MIHAISAVNRHLYEDVLEQHFRLRHDIFVEERHWETLRRPDGREVDSYDDEDTVYLLALEGRRVVGGHRLYPTTKPSMMSEVFPHLAAVRGCPSDPLIWEWSRYFVVRDRRDGALNLQLMAAVQEFCLDQGIAQVSAIMETWWLPRFHEAGFVVTPLGLPALVENAWTMAATVDIRRQTLDVLHDRIGMPSIVQQDGPRLDAVARANLCGLAAAQRKSA | Function: Catalyzes the synthesis of IV-HSL (isovaleryl-homoserine lactone), a quorum-sensing (QS) autoinducer molecule which binds to BjaR1 transcriptional regulator to activate expression of QS-dependent genes. Is active with isovaleryl-CoA but cannot use isovaleryl-ACP as acyl donor.
Catalytic Activity: 3-methylbuta... |
P9WIS2 | MGEGSRRPSGMLMSVDLEPVQLVGPDGTPTAERRYHRDLPEETLRWLYEMMVVTRELDTEFVNLQRQGELALYTPCRGQEAAQVGAAACLRKTDWLFPQYRELGVYLVRGIPPGHVGVAWRGTWHGGLQFTTKCCAPMSVPIGTQTLHAVGAAMAAQRLDEDSVTVAFLGDGATSEGDVHEALNFAAVFTTPCVFYVQNNQWAISMPVSRQTAAPSIAHKAIGYGMPGIRVDGNDVLACYAVMAEAAARARAGDGPTLIEAVTYRLGPHTTADDPTRYRSQEEVDRWATLDPIPRYRTYLQDQGLWSQRLEEQVTARAKH... | Function: Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched-chain alpha-ketoacids to acyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+... |
P9WIS0 | MTQIADRPARPDETLAVAVSDITQSLTMVQAINRALYDAMAADERVLVFGEDVAVEGGVFRVTEGLADTFGADRCFDTPLAESAIIGIAVGLALRGFVPVPEIQFDGFSYPAFDQVVSHLAKYRTRTRGEVDMPVTVRIPSFGGIGAAEHHSDSTESYWVHTAGLKVVVPSTPGDAYWLLRHAIACPDPVMYLEPKRRYHGRGMVDTSRPEPPIGHAMVRRSGTDVTVVTYGNLVSTALSSADTAEQQHDWSLEVIDLRSLAPLDFDTIAASIQRTGRCVVMHEGPRSLGYGAGLAARIQEEMFYQLEAPVLRACGFDTP... | Function: Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched-chain alpha-ketoacids to acyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+... |
O06159 | MSGEDSIRSFPVPDLGEGLQEVTVTCWSVAVGDDVEINQTLCSVETAKAEVEIPSPYAGRIVELGGAEGDVLKVGAELVRIDTGPTAVAQPNGEGAVPTLVGYGADTAIETSRRTSRPLAAPVVRKLAKELAVDLAALQRGSGAGGVITRADVLAAARGGVGAGPDVRPVHGVHARMAEKMTLSHKEIPTAKASVEVICAELLRLRDRFVSAAPEITPFALTLRLLVIALKHNVILNSTWVDSGEGPQVHVHRGVHLGFGAATERGLLVPVVTDAQDKNTRELASRVAELITGAREGTLTPAELRGSTFTVSNFGALGVD... | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched-chain alpha-ketoacids to acyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2-methylpropanoyl-CoA = (R)... |
Q9FMZ0 | METNLQQVKNSSQTFSEKQNPKQEASPSPISSTCSSPSHDFSFTISLQPLSSSSKHISPTLRSPSKTTSSYQQTDPFAVDLSPADEIFFHGHLLPLHLLSHLPVSPRTSTGSYNDGFTLPVKDILPDQPTNNNNNTENAITNISTEAKDDNTEDKAEGEIRVKTKPIKSFSLFGLSKWRKGFESNEREQEQQQQKIKKPMSLDLSHAVKKYIRMLFQKRGNGTQFWNRRQTSSYSFSSSLMGPNGNSKTMINGSYNKRDLIRGRRGELFSAPASMRTSPTNSGHLRVSTAGLSSSSGSTSSSSSDSTMEELQAAIQAAIA... | Function: Negative regulator of brassinosteroid signaling. When associated to the membrane, limits the interaction of BRI1 with BAK1 by binding to the kinase-inactive form of BRI1.
PTM: Phosphorylated on Tyr-211 in response to brassinosteroid perception, leading to its inactivation: once phosphorylated, displaced into ... |
Q9LFL7 | MGNCLKHFKQQLPSIAPKPLIIPPIFSARKRESESLQIRGLKKATKKFRQDRVVECEDYSVRKFYKGYIDETTFAPSRAGTGIAVSVMECDSSRSLQDWMAVVRSLGQLSHQNLVNFLGYCCEDNKPFFLVFEYSHKGSLDSHIFGKEEEALPWEIRVKIAIGTAQGLAFLHSIKNSPLNRELRMHNIMLDEQYNAKLFYLEPTKRSLVDEGLKRGRFTYLSPEWGSLGILDMTTDVYIFGMILLELLMGSKDRKKIKEEQGLVDYWTSSFLPDNYKIEEIIDPRLGSDYSANAATQMGTLINRCTAHNTKKRPLMQQVL... | Function: Collaboratively with BKN2/SZE2, involved in compatible pollen-stigma interactions.
Location Topology: Lipid-anchor
Sequence Mass (Da): 37870
Sequence Length: 331
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Cell membrane
|
Q9LFL6 | MGNCLKPLKEQPPSASPKPLTIPSSSVEPVKENLKEFRFAELNKATKRFRKYMVIKGNDNGFTRTFYEGCINETTFAPSRTGITVSVMECYQDNSQTLQDWKEEVKSLGRISHPNLVKLLGYCCEENKSFLVFEYLHKGSLNRYIFGKEEEALPWETRVKIAIGAAQSIAFLHWVKNSALYRELRMYNILLDEHYNTKLFYLGSKKLCLLEESVTTAFIGRTVYIPPEYVISGHLGTKSDVYTFGVILLEILTGLKASDGKKNENMQSLHVWTKPFLSDQSKIREIIDPRLGNDYPVNAATQMGKLIKRCIKLDTRKRPS... | Function: Together with SZE1 and ZED1, required for effector-triggered immunity (e.g. Pseudomonas syringae type III effector HopZ1a) via the activation of ZAR1, thus being essential for resistance against P. syringae pv. tomato DC3000 expressing HopZ1a . Collaboratively with BKN1, involved in compatible pollen-stigma i... |
Q5U5M8 | MESSQGRRRRPGTVVPGEAAETDSELSASSSEEELYLGPSGPTRGRPTGLRVAGEAAETDSEPEPEPTVVPVDLPPLVVQRDPAETWGTEETPAMAPARSLLQLRLAESQTRLDHDVAAAVSGVYRRAGRDVAALAGRLAAAQATGLAAAHSVRLARGDLCALAERLDIVAGCRLLPDIRGVPGMEPEQDPGPRA | Function: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for... |
Q94KL5 | MGLATTTSSMSQDYHHHQGIFSFSNGFHRSSSTTHQEEVDESAVVSGAQIPVYETAGMLSEMFAYPGGGGGGSGGEILDQSTKQLLEQQNRHNNNNNSTLHMLLPNHHQGFAFTDENTMQPQQQQHFTWPSSSSDHHQNRDMIGTVHVEGGKGLSLSLSSSLAAAKAEEYRSIYCAAVDGTSSSSNASAHHHQFNQFKNLLLENSSSQHHHHQVVGHFGSSSSSPMAASSSIGGIYTLRNSKYTKPAQELLEEFCSVGRGHFKKNKLSRNNSNPNTTGGGGGGGSSSSAGTANDSPPLSPADRIEHQRRKVKLLSMLEEV... | Function: Transcription factor that establishes leaf shape by repressing growth in specific subdomains of the leaf. Negatively regulates knox homeobox gene KNAT1/BP expression.
Sequence Mass (Da): 69271
Sequence Length: 627
Domain: The SR/KY and BELL domains are responsive for the interaction between the TALE/BELL prot... |
Q9SJJ3 | MDMIKPDFQQIRRDKFRVEQMNDFPNTWTQQQHQNIRIPNNLDLIGILQNQISVPVQTDLYQDSAATFMNMPQSIHRDPQGPSNWRISDLSQPSTVNHGYDQAGIRPNNVADLLSDHFSSRNQILDRPLYVGRDSIPQSSMIRRSEVSCLDDNQKGCVTVACSGTGNEILRSSYDQGSSSGSYRGEFSFLPSLENQSVAHNASNWNHGPVNVTATSHTNSKKGFPLSLLSDIPPSRDVGNAAVLSTMNIHGPLGPFTGYASILKSSRFLEPAQKMLEEFCISYASKIISRSESTSMEDDDDDDDNLSGFSSSSEPLEPKN... | Function: Required for specifying floral primordia and establishing early internode patterning events during inflorescence development.
Sequence Mass (Da): 65775
Sequence Length: 584
Domain: The SR/KY and BELL domains are responsive for the interaction between the TALE/BELL proteins and the TALE/KNOX proteins.
Subcellu... |
Q9LZM8 | MADAYEPYHVLQQSRRDKLRIPSLDSHFHFHPPPPPSSGGGGGVFPLADSDFLAAGGFHSNNNNNHISNPSYSNFMGFLGGPSSSSSTAVAVAGDHSFNAGLSSGDVLVFKPEPLSLSLSSHPRLAYDLVVPGVVNSGFCRSAGEANAAAVTIASRSSGPLGPFTGYASILKGSRFLKPAQMLLDEFCNVGRGIYTDKVIDDDDSSLLFDPTVENLCGVSDGGGGDNGKKKSKLISMLDEVYKRYKQYYEQLQAVMGSFECVAGLGHAAPYANLALKALSKHFKCLKNAITDQLQFSHNNKIQQQQQCGHPMNSENKTDS... | Function: Transcription factor that is involved in the preservation of the spiral phyllotactic arrangement leading to a regular pattern of organ initiation. Required for maintenance of stem cell fate in the shoot apical meristem, and is essential for specifying floral primordia and establishing early internode patterni... |
Q9HNE6 | MGASPVALTPLTARARRTLARPALALGWVAISIAALPAITGVSLSPTARYAPLVASAVVFGMPHGAIDYLALPRAVTGTVTVRWLAVVGVLYLVLGGGYAAAWFFAPVPAAFAFVAITWLHWGQGDLYPLLDFLDVDYLDTRPRRAATVLIRGGLPMLVPLLGFPERYRSVVDAFAAPFGGSVGDLAVFDPRVRLWLGVAFAAATVAVLAAGRRRTHSPGAWRVDAAETLLLWVFFFVVPPVFAVGVYFCVWHSVRHVARAIAVDGSVHPSLRAGDILGPLARFGVEAAPMTAAALALGGVLWWAVPNPPTTLESGAALY... | Function: Appears to partially substitute for Brp function in retinal biosynthesis during bacteriorhodopsin production. Probably catalyzes the cleavage of beta-carotene at its central double bond (15,15') to yield two molecules of all-trans-retinal.
Catalytic Activity: all-trans-beta-carotene + O2 = 2 all-trans-retinal... |
Q4PNI0 | MGLMLIDWCALALVVFIGLPHGALDAAISFSMISSAKRIARLAGILLIYLLLATAFFLIWYQLPAFSLLIFLLISIIHFGMADFNASPSKLKWPHIIAHGGVVTVWLPLIQKNEVTKLFSILTNGPTPILWDILLIFFLCWSIGVCLHTYETLRSKHYNIAFELIGLIFLAWYAPPLVTFATYFCFIHSRRHFSFVWKQLQHMSSKKMMIGSAIILSCTSWLIGGGIYFFLNSKMIASEAALQTVFIGLAALTVPHMILIDFIFRPHSSRIKIKN | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the cleavage of beta-carotene at its central double bond (15,15') to yield two molecules of all-trans-retinal. Exhibits the highest activity for beta-carotene, followed by beta-cryptoxanthin, beta-apo-4'-carotenal, alpha-carotene, and gamma-carotene in decre... |
Q09457 | MVKSYTLAGLAAIACLLLAIGAVISTVYILNDISDFYSEAQEELVEFKDIANNIWEEMVFELTPEEMREAEDNDREKRSYEPEGPYQSETTTPSTTTSTAATTTEAAEDESGYDFVNDNGPPSSRPRKPEPPTMPRTIQGFRAPPPAATSTYRPPHGSNYDNYGREPASSRRPYPPQQPPSTSAPHSSPNNRTSLYNPQPPPKTGYPTNPRVPYNPPQPNYTRQPTYPEDNRAPYKPTRSPNTPPPRQPSGGYDSDGQTPPSSPRIYNTRRPNNHGPGYPEDQVPTAPPVPGQQRVPPTQTRNPPNPTNTRQPSRPVPPT... | Function: Probable cuticular collagen-like protein (Probable). Nematode cuticles are composed largely of collagen-like proteins (Probable). The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment (Probable). Acts downstream of the Wnt signaling pathway; perhaps in the form... |
Q5ADQ9 | MDKFIQSFSHQYLDSSSSLKLTARRKRKLTILGLFLFSLISLMIIISYSNNNILPGLSGISISSTFSDYYSNPKQQNKFEQQIQDHQTTKKGKRTIIFPNNFNHVHDHKGSYMMKDSELVKYYVETMEQALDPEDLIYRNRFTYKLPNIPYTEQKIEMFSDGGGGGGDTSDSNTDMCPKLSTTIKVEASPAMNKNGDLKKILKTFLQEDSFYYRELSPFFPDLKKHFDEDTIDKHWYQFIGSTVWLEQYGVHLMVSRIIYTEKDQGSPKFSLAYLQVFDRNWKELDNVELIVPDPENISTTNNKNKNKKPYGYKSVLYPT... | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Required for addition of the first beta-mannose residue to acid-stable fraction of cell wall phosphopeptidomannan. Plays a key role in reducing host inflammatory response.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 7... |
F2QZ65 | MVDLFQWLKFYSMRRLGQVAITLVLLNLFVFLGYKFTPSTVIGSPSWEPAVVPTVFNESYLDSLQFTDINVDSFLSDTNGRISVTCDSLAYKGLVKTSKKKELDCDMAYIRRKIFSSEEYGVLADLEAQDITEEQRIKKHWFTFYGSSVYLPEHEVHYLVRRVLFSKVGRADTPVISLLVAQLYDKDWNELTPHTLEIVNPATGNVTPQTFPQLIHVPIEWSVDDKWKGTEDPRVFLKPSKTGVSEPIVLFNLQSSLCDGKRGMFVTSPFRSDKVNLLDIEDKERPNSEKNWSPFFLDDVEVSKYSTGYVHFVYSFNPLK... | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Involved in the beta-mannosylation of outer chains of N-glycans (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 74338
Sequence Length: 652
Subcellular Location: Membrane
EC: 2.4.1.-
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Q59MA6 | MLAWLRHRIRSYNTSTYSSILPSASFGKVYKIGTKLNFTLLALCLLLACSVFFNYFYLADNNGLDIDTKGEEEENVFKDRKMVIFPNNFEITDKNLLEYYLKTLEEPLHPQDTIYRNRFIYKVPDVSYTSQTINLFSGLSQNSQSSKCEDLSSSYSFDVSGPQNKNCDLYKVLGKFLNDDSEYFQEISPLFPKLKEMLVKKEIEKHWFQLIGSSVWLEQYGVHLMTSRIFYSSTGDKVKPVVSLTYVQVFDHEWREIENVELIVPDGEGKYKPMTYPTFLPMSVYHNEKQQQGRFYGVEDPRITLVRNKLGYDEPIIVYN... | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Required for the addition of beta-mannose to the acid-labile fraction of cell wall phosphopeptidomannan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 75813
Sequence Length: 654
Subcellular Location: Membrane
EC: 2.4.1.... |
C4R7X8 | MRTRLNFLLLCIASVLSVIWIGVLLTWNDNNLGGISLNGGKDSAYDDLLSLGSFNDMEVDSYVTNIYDNAPVLGCTDLSYHGLLKVTPKHDLACDLEFIRAQILDIDVYSAIKDLEDKALTVKQKVEKHWFTFYGSSVFLPEHDVHYLVRRVIFSAEGKANSPVTSIIVAQIYDKNWNELNGHFLDILNPNTGKVQHNTFPQVLPIATNFVKGKKFRGAEDPRVVLRKGRFGPDPLVMFNSLTQDNKRRRIFTISPFDQFKTVMYDIKDYEMPRYEKNWVPFFLKDNQEAVHFVYSFNPLRVLKCSLDDGSCDIVFEIPK... | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Initiates the beta-mannosylation of core N-linked glycans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 74561
Sequence Length: 644
Subcellular Location: Membrane
EC: 2.4.1.-
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Q9UUH2 | MRPIPVKNRIGKNNIDNAKGLKGNKLIRHYHNLLKEKSRLIASSAPIEKIKNVESELENIGIDAYQRASRSGQAEGKGGDSSKILIKWIRTTPCFSYCARLKEPKDLLEIGSVSVDNKCSTCGLFRVSRIDLHSVHPLIKQQDFLERTPEEGLFTGISCSLVLNFAPPELRAKMLLHCTGLLMPPNKEQPPWLFLVLPSPCITNSRYMDEKTLHSIMIQFGFICRQKSISKKIAYYLYSYECFPMKEIDWKKKIVNDGATRNNFFIPCIL | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of an adenine present in helix 65 in 25S rRNA.
Sequence Mass (Da): 30760
Sequence Length: 270
Subcellular Location: Nucleus
EC: 2.1.1.-
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