ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P38278 | MHSRKSKSITGKRKQVGSNVTRVIKPQKTRRIIRRFHHLINKRQSICKFLCLKENLDDSNEEKNDKIIRLSIKGNVRLGKYYEDGKSQSFNDAMESQLLRLHSLIKNESKSKDTSDLAVMYTLLGYIMNQINKLGGLETYQIASQNGQLKERGGDTSKLLEKWIRSSFENCPGAVALEIGSLSSGNRISRCALFRNVVRIDLEEHEGVIKQDFMERPLPRNENDKFDLISCSLVLNFVKNHRDRGAMCHRMVKFLKPQGYIFIVLPQACVTHSRYCDKTLLQNLLGSIGLIMLNSHQSNKLYYCLYQLQVVPPQPSSFSK... | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of adenine 2142 in 25S rRNA. N(1)-methyladenine(2142) in 25S rRNA is present in helix 65, a region that accounts for most of the intersubunit surface of the large subunit.
Catalytic Activity: adenosine(2142) in ... |
Q5A846 | MFESDLSFYSALLILCCPISIVFFKKFPIKGYTGANKVSLFLQCLIAILNLNILYSFINSLTITLGHDGSSANTLTIDPITTTQQQGHVDYTPIKVSGYTFKNQVATKNLQCDSIVYDQDLDLQVSQAVDLNKPEDLKFFRDKLNELRSLNNIYDLFFQDNEDEVEESILERKWYKFCGSAVWLDKYGVYFMVNRIAYSKKGTRNNPTISVLAGQVFDKNWIELTGKKFPFSGLEFPTILPHYIDEGKEAEKVILGAEDPRVILHEYTNENGIRIQEPLIAFNALSTEVDWKRAMHIYRPLHDPHRIIRLSIENYAPREK... | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Required for addition of the second beta-mannose residue to acid-stable fraction of cell wall phosphopeptidomannan, and in elongation of beta-mannose chains on the phosphopeptidomannan acid-labile fraction.
Location Topology: Single-pass type II mem... |
Q5ABT8 | MTKSYMPLFRSPRQFKKIYFILIPLILAVIILHVFFDGFNKISEYSPTFISNRILNHQDQQQKSEKSSDVISSYFPSLAIYPKNFDNRVEFVNEPKNSKWIQYFGDSKTVLSNYITNQTYTNHSIGLYSSSTVRPPASSCKDILYERSFEITKYRTLHDDLYKLATTLLYQLENDPAFQDLSPFFNDRLPHIIMRGELHKHIYKFAGTSVWLEQHGVHLMLSRVIYSQQGKKNDPQLSLLYAQVYDENWNELNDIELIVPVINPNGERVYDSVKYPQFLAIPFYHNSEYIKSRWYGPEDTRLILTKNKFGDDEPVIIFNS... | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Required for the elongation of beta-mannose chains on the acid-labile fraction of cell wall phosphopeptidomannan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 90959
Sequence Length: 781
Subcellular Location: Membrane
E... |
F2QZ45 | MKLDTQQISHLLSRQMYHLAPRKKLLIWGGSLGFVLLLLIVASSHQRIRSTILHRTPISTLPVISQEVITADYHPTLLTGFIPTDSDDSDCADFSPSGVIYSTDKLVLHDSLKDIRDSLLKTQYKDLVTLEDEEKMNIDDILKRWYTLSGSSVWIPGMKAHLVVSRVMYLGTNGRSDPLVSFVRVQLFDPDFNELKDIALKFSDKPDGTVIFPYILPVDIPREGSRWLGPEDAKIAVNPETPDDPIVIFNMQNSVNRAMYGFYPFRPENKQVLFSIKDEEPRKKEKNWTPFFVPGSPTTVNFVYDLQKLTILKCSIITGI... | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Responsible for addition of a hexose to the beta-mannose chain (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 56665
Sequence Length: 503
Subcellular Location: Membrane
EC: 2.4.1.-
|
Q5ALW2 | MVQKQYRFAPKSIFTFVFLCFVAIVVIISTSSLVQVEESLDPIEVSDEIKKHDRKVVIFPSNFQSANNKLADFLTEAFGQRLNKGDIVYKNRDTYELPQTVYTWNTIDLFQSIGEKDNLKCEKIPLNFEISKIYNKNADLYKILRDFKNENSFYYKEVSVFFPDLGKQLRERTIEKHWFQLIGSSVWLEQYGVHLMISRVIYTKTGNKVQPVISLSYVQAFDRNWTELKNVTLVVPDSGKAKFKTVSYPSFIPIPVYHNVNQQRGKFYGVEDPRIMLVKNKEGYEEPLIVYNSFNRSPPNANYLEEIKNLVKLDTYRSIF... | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Required for beta-1,2-mannose transfer on phospholipomannan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 70896
Sequence Length: 612
Subcellular Location: Membrane
EC: 2.4.1.-
|
O94480 | MGKKARFKEARRLQKRNLNNAIGSSSINSQNSLTNDKIGKGKNKGPTERYVLPFEKNNRFLLLGEGNFSFAFSLLLHHVSSEGFVLATSYDSKEDLKQKYPDAAEYISKIEINGGKVMHEIDATKLHLHKKLKTQKFDTIFWNFPHSGKGIKDQDRNILDNQKMLLAFFKASKFLLSEKGVIVITLAETKPYTLWNLKGLAKDAGYTSLMTEKFDSSFYPEYSHRRTIGWIDGISERSPWKGELRDSRHYCFVVNGSNIKPYNQRKEKRKRSELSDDSSDSS | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(3) position of a uridine in 25S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine in 25S rRNA = H(+) + N(3)-methyluridine in 25S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32345
Sequence Length: 282
Subc... |
P40493 | MARKLKGKIGSKGLKGALLRHKAKVKLVRNIESKQKHELRKKNSSANNKTVKRNQEFQKLNQGKVMPFEKDETLMLCGEGDFSFARSIVEQNYIESDNLIITSYDNSVNELKLKYPHTFEENYQYLKDLNIPIFFQIDVTKLVKSFKISKNNTWFKIINRLSDHRWGNKPLQNIVFNFPHNGKGIKDQERNIREHQDLIFNFFQNSLQLFNLINTKIQNDTLRYTQGYDLNEDTPQAKKLTAEGYGNIILSLFDGEPYDSWQIKLLAKKNGLTLSRSSKFQWENFPGYHHRRTNSEQDTTKPAKERDARFYIFSKYVSNS... | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(3) position of uridine 2634 (m3U2634) in 25S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2634) in 25S rRNA = H(+) + N(3)-methyluridine(2634) in 25S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39402
... |
Q5ABU8 | MGNYKPSIKQYVVTVKAIKSSQFGRLGICAVVLLFVLGYPFYFISNNPFDTSIRYQYVDPYNDTTRKYTTIEKQHTDIGGNGTTILYPKNLQLDQTALSQLLNTTETTNPFVQYIGNSSSIAFSQLNQTLVNHSIQVFDPFSNSDNCSDLMTETQLTISQNIIIKESFEIMVKRLMHQLDTEPAFKELAPFFQNKLSLHLRMRSYHKHFYKFARTSVWLKDYGVHLMISRVIYSQKGKKGDPQISLLYTQLYDTNWQELTNTDLLVSMQDITGEYKLEKLQFPRFLPMPFYYNPKLTKGRWYGPEDARIMLVKNQLDMEE... | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Required for beta-1,2-mannose transfer on phospholipomannan. Required for pro-inflammatory response in macrophages through phospholipomannan-induced TNF-alpha production.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 74... |
Q12291 | MLLMRRFAFLTSSVYFKYIPIYSQYHYSSQFPINMNPKKVAQLPVHNKSTLPPQEIIDLFKITFLEELYPKDQDNEKSPLTEQIQAVKSDLYNRDYNAAFNNDSKRIAYCCRWSPSRATSYASVFAHFPELLKIIRCEIDDKDSNVLCIGGGAGGELVALASIFTLSRDFSSKFASALKIDNEVNKKPRNLNIQLVDIADWSTVVEKLTATIKSKWLYGDSEAESFNVNFTHKDCLQMTEPQDIKIYQGLDLITLLFTTNELFTQKKVESIKFLQRLNENCAPGCHLLILESAGSYSHITINNKKFPIQFLIDTILVGNR... | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(3) position of uridine 2843 (m3U2843) in 25S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2843) in 25S rRNA = H(+) + N(3)-methyluridine(2843) in 25S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42041
... |
Q19000 | MLSALLIRNIRNASKLASVAGPNSDRIVNVKWSDGKTGVFPLIWLRDTSPDPSTYTISPAMTARKLTMLEFDVEQNARKLWIDEDANCLKIEWESGVLSEFPSEWLKIRNPSDQEARRRRRKVYLFPEQTWGKAEIEGKLKKFSHEEFMKNEQVVHDFLQAVCIDGIAVLKGAPQGVRGAVEAIGDRIGMIKRTHFGLVFEVSLKADASNMAYASNGGLPFHTDFPSLSHPPQLQMLHMLQSAEEGGHSLFVDGFHVAEQLRVEKPEIFKILTTQSMEYIEEGYDVHEINGKTIRFDYDMCARHKVIRLNDDGKVNKIQF... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the formation of L-carnitine from gamma-butyrobetaine.
Catalytic Activity: 2-oxoglutarate + 4-(trimethylamino)butanoate + O2 = carnitine + CO2 + succinate
Sequence Mass (Da): 48436
Sequence Length: 421
Pathway: Amine and polyamine biosynthesis; carnitine bio... |
O75936 | MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKARKLLVEALDVNIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQARAKLQRELFFPECQYWGSELQLPTLDFEDVLRYDEHAYKWLSTLKKVGIVRLTGASDKPGEVSKLGKRMGFLYLTFYGHTWQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQKLKKNNPQAFQILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIFDVPVERVQPFYAALKEFVDL... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the formation of L-carnitine from gamma-butyrobetaine.
Catalytic Activity: 2-oxoglutarate + 4-(trimethylamino)butanoate + O2 = carnitine + CO2 + succinate
Sequence Mass (Da): 44715
Sequence Length: 387
Pathway: Amine and polyamine biosynthesis; carnitine bio... |
P80193 | NAIADYRTFPLISPLASAASFASGVSVTWADGRVSPFHNLWLRDNCPCGDCVYEVTREQVFLVADVPEDIQVQAVTIGDDGRLVVQWDDGHASAYHPGWLRAHAYDAQSLAEREAARPHKHRWMQGLSLPVYDHGAVMQDDDTLLEWLLAVRDVGLTQLHGVPTEPGALIPLAKRISFIRESNFGVLFDVRSKADADSNAYTAFNLPLHTDLPTRELQPGLQFLHCLVNDATGGNSTFVDGFAIAEALRIEAPAAYRLLCETPVEFRNKDRHSDYRCTAPVIALDSSGEVREIRLANFLRAPFQMDAQRMPDYYLAYRRF... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the formation of L-carnitine from gamma-butyrobetaine.
Catalytic Activity: 2-oxoglutarate + 4-(trimethylamino)butanoate + O2 = carnitine + CO2 + succinate
Sequence Mass (Da): 43322
Sequence Length: 383
Pathway: Amine and polyamine biosynthesis; carnitine bio... |
Q9QZU7 | MHCAILKAEAVDGARLMQIFWHDGAESLYPAVWLRDNCQCSDCYLHSAKARKLLLEALDVNIRMDDLTFDQKKVYITWPNGHYSEFEANWLKKRCFSQEARAGLQGELFLPECQYWGSELQLPTLNFEDVLNDDDHAYKWLSSLKKVGIVRLTGAADKRGEIIKLGKRIGFLYLTFYGHTWQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQKLKEKNPQAFSILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTVFDVPIERVQPFYAALKEFVDL... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the formation of L-carnitine from gamma-butyrobetaine.
Catalytic Activity: 2-oxoglutarate + 4-(trimethylamino)butanoate + O2 = carnitine + CO2 + succinate
Sequence Mass (Da): 44546
Sequence Length: 387
Pathway: Amine and polyamine biosynthesis; carnitine bio... |
P24282 | MEPIFIIGIILGLVILLFLSGSAAKPLKWIGITAVKFVAGALLLVCVNMFGGSLGIHVPINLVTTAISGILGIPGIAALVVIKQFII | Function: Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB-processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, prevent... |
O81851 | MAVQAHHMNIFSQFISPNRDCVKFQENMNHGEFEFTGGEVPLITGESFAVEPLAAKANFNKAESGLSYNFTVPPLSTKRQRDFQFSDSNAPVKRRSVAFDSSSPSLINVELVSQIQNQQQSEIDRFVAQQTEKLRIEIEARQQTQTRMLASAVQNVIAKKLKEKDDEIVRIRNLNWVLQERVKSLYVENQIWRDIAQTNEANANTLRTNLDQVLAQLETFPTASAVVEDDAESSCGSCCGDGGGEAVTAVGGGCKRCGEREASVLVLPCRHLCLCTVCGGSALLRTCPVCDMVMNASVHVNMSS | Function: E3 ubiquitin-protein ligase involved in the regulation of pathogen and abiotic stress responses by facilitating degradation of MYB108/BOI. Attenuates cell death by preventing caspase activation. Has no effect on the stability of the DELLA proteins. Not regulated by MYB108/BOI.
Catalytic Activity: S-ubiquitiny... |
Q6DC66 | MEMLRRSSVFAAEVMEVFDRSPTDKELVSQSKVLCRDYIHSRLHRAGIGWSKPEHGSGGTLAEVSSVLLWLGDELEYLRPNVYRNVARQLNITIASENIVSDAFLAVAAEIFSTEYSRKGLEKHKGVTWGKIVSLYAVAGALAVDCVRNGHPAMVHTIVDCMGEFVRKSLASWLKKRGGWADITKCVVSTDPSFHSHWLVTAACACGHYLKAVVFYLLREK | Function: May play a role in apoptosis. Does not appear to show pro-apoptotic activity when expressed ectopically in early embryos.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24599
Sequence Length: 221
Subcellular Location: Membrane
|
Q7T381 | MNVFARSSVLAAEMIDVFDRTHTEKELVFQSKELCRDFIHSRITREGLSWSKVELDLPEPRGVLVDVSVVLLKLGDELECMRPYVYRNIAKQLNISVSVEAVVSDAFLSVATEVIAMGITWGKVVAIYAVAAGLAVDCVRLGHPVMVHTIVDSLGEFVRRSLVPWLKKRGGWVDILKCVVNMDSRAHVHWLSTAVLTWREFIKTMYVYLTK | Function: May play a role in apoptosis. Does not appear to show pro-apoptotic activity when expressed ectopically in early embryos.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23834
Sequence Length: 211
Subcellular Location: Membrane
|
O35425 | MEVLRRSSVFAAEIMDAFDRSPTDKELVAQAKALGREYVHARLLRAGLSWSAPERASPAPGGRLAEVCTVLLRLGDELEQIRPSVYRNVARQLHIPLQSEPVVTDAFLAVAGHIFSAGITWGKVVSLYSVAAGLAVDCVRQAQPAMVHALVDCLGEFVRKTLATWLRRRGGWTDVLKCVVSTDPGFRSHWLVATLCSFGRFLKAAFFLLLPER | Function: Apoptosis regulator that functions through different apoptotic signaling pathways . Plays a roles as pro-apoptotic protein that positively regulates intrinsic apoptotic process in a BAX- and BAK1-dependent manner or in a BAX- and BAK1-independent manner . In response to endoplasmic reticulum stress promotes m... |
P47229 | MTALTESSTSKFVKINEKGFSDFNIHYNEAGNGETVIMLHGGGPGAGGWSNYYRNVGPFVDAGYRVILKDSPGFNKSDAVVMDEQRGLVNARAVKGLMDALDIDRAHLVGNSMGGATALNFALEYPDRIGKLILMGPGGLGPSMFAPMPMEGIKLLFKLYAEPSYETLKQMLQVFLYDQSLITEELLQGRWEAIQRQPEHLKNFLISAQKAPLSTWDVTARLGEIKAKTFITWGRDDRFVPLDHGLKLLWNIDDARLHVFSKCGHWAQWEHADEFNRLVIDFLRHA | Function: Catalyzes an unusual C-C bond hydrolysis of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (HOPDA) to produce benzoic acid and 2-hydroxy-2,4-pentadienoic acid (HPD).
Catalytic Activity: 2,6-dioxo-6-phenylhexa-3-enoate + H2O = 2-oxopent-4-enoate + benzoate + H(+)
Sequence Mass (Da): 32030
Sequence Length: 286
P... |
O05151 | MQSPINSFKKALAEGRTQIGFWLALGDAYSAEVCAGAGFDWLLIDGEHAPQDLRSVLAQLQVIGAYRDCHAAVRVPSADTTVIKQYLDLGAQSLLVPMVDTADEAAAVVRACRYPPGGIRGVGGARASRWGRYPRYLHEADEQVCVVVQAETALALSNLEAIAEVDGIDGVFIGTADLAASLGFPGNPAHPEVQDAILDALQRVRAAGKAPGVLTPVEDLAQKYLAHGAVFVAVGIDTHLLAKQTSALAARFAQVAYS | Function: Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2-oxovalerate to pyruvate and acetaldehyde.
Catalytic Activity: (S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate
Sequence Mass (Da): 27159
Sequence Length: 258
Pathway: Xenobiotic degradation; biphenyl degradation.
EC: 4.1.3.39
|
Q8R164 | MATATVRPAAQRLRLLLSPLKSRICVPQAEPVATFGTAVTSAKVAVNGVHLHYQRVGEGEHAILLLPGMLGSGKTDFAPQLQSLNKKRFTLVAWDPRGYGYSRPPDRDFPRDFFERDAKDAVDLMKALQFKQVSLLGWSDGGITALIAAAKYPSYIRKMVIWGANAYVTEEDSRIYQGIRDVSKWSEKARKPLEALYGYDYLAKTCEDWVDGISQFKQLPEGNICRHLLPLVQCPTLIVHGEKDPLVPRFHADFLLQHVKGSRLHLMPEGKHNLHLRFADEFNRLVEDFLQ | Function: Serine hydrolase that catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs such as valacyclovir and valganciclovir. Activates valacyclovir to acyclovir. May play a role in detoxification processes. It is a specific alpha-amino acid ester hydrolase that prefers small, hydropho... |
B4E8N5 | MTHPTELPLSPLSALQFYATAPYPCSYLDGRIARSQVATPSHLINSDIYTELVKAGFRRSGVFTYRPYCDGCRACVPVRVPVGEFAPTRTQRRMWKRHRALVATVSPLHYDEEHYALYMRYQSARHAGGGMDRDSRDQYEQFLLQSRINSRLVEFRDLDAPGGEPGKLRMVSMIDILGDGLSSVYTFFEPDDRHTSYGTYNILWQIEQAKSLGLPYVYLGYWIRESPKMAYKANFHPLEGLIDGRWKTLDPERVDLPPVDAALARAPLPGGHSGSG | 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] + ... |
Q9LY74 | MASLMLNGAITFPKGLGSPGSNLHARSIPRPTLLSVTRTSTPRLSVATRCSSSSVSSSRPSAQPRFIQHKKEAYWFYRFLSIVYDHVINPGHWTEDMRDDALEPADLSHPDMRVVDVGGGTGFTTLGIVKTVKAKNVTILDQSPHQLAKAKQKEPLKECKIVEGDAEDLPFPTDYADRYVSAGSIEYWPDPQRGIREAYRVLKIGGKACLIGPVYPTFWLSRFFSDVWMLFPKEEEYIEWFKNAGFKDVQLKRIGPKWYRGVRRHGLIMGCSVTGVKPASGDSPLQLGPKEEDVEKPVNNPFSFLGRFLLGTLAAAWFVL... | 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... |
P74388 | MPEYLLLPAGLISLSLAIAAGLYLLTARGYQSSDSVANAYDQWTEDGILEYYWGDHIHLGHYGDPPVAKDFIQSKIDFVHAMAQWGGLDTLPPGTTVLDVGCGIGGSSRILAKDYGFNVTGITISPQQVKRATELTPPDVTAKFAVDDAMALSFPDGSFDVVWSVEAGPHMPDKAVFAKELLRVVKPGGILVVADWNQRDDRQVPLNFWEKPVMRQLLDQWSHPAFASIEGFAENLEATGLVEGQVTTADWTVPTLPAWLDTIWQGIIRPQGWLQYGIRGFIKSVREVPTILLMRLAFGVGLCRFGMFKAVRKNATQA | Function: Involved in a key methylation step in both tocopherol (vitamin E) and plastoquinone synthesis. Catalyzes the conversion of 2-methyl-6-phytyl-1,4-hydroquinol (MPBQ) to 2,3-dimethyl-6-phytyl-1,4-hydroquinol (DMPQ, a substrate for tocopherol cyclase), and 2-methyl-6-solanyl-1,4-benzoquinol (MSBQ) to plastoquinol... |
O74510 | MSGSKCCSSSNTIKVSIYLFLHTLTYGLLNYHLNPRLLASTGVVESDIPYWMSYLSIIMHVGQSLLLQKFNLGYGWLLLTKYPVYVLLSTYYLTPLSQIAWAFIIDAISLLVARCFSRANPIKCSNQVNTQYSVSFLFTIMASVLISVLNYISQKIFLNGLILGNSHNVVTSLVAPPLPLQYLAHVPIGYVIQRVVFSERPIPQSLFLMIFLTLWNCFIPYSILFSMNWSAMFQVVGAYLSQIWIITFICWALSL | Function: Connects telomeres to the nuclear envelop (NE) during both vegetative growth and meiosis. This connection ensures clustering of telomeres to the spindle pole body (SPB) when cells enter meiotic prophase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28899
Sequence Length: 255
Subcellular ... |
O60158 | MTENEKSRSLPAERNPLYKDDTLDHTPLIPKCRAQVIEFPDGPATFVRLKCTNPESKVPHFLMRMAKDSSISATSMFRSAFPKATQEEEDLEMRWIRDNLNPIEDKRVAGLWVPPADALALAKDYSMTPFINALLEASSTPSTYATPSRPTAQKSETSEGEPESSTSATTTSVARRTRQRLAEHLENSKKTILQHDNKEEDKEIHSEENETKDEIKSEKKEPEIKKQEGGSSTEKVGQPSSSDDKAKGSTSKDQPSEEEEKTSDIQDRKIKTPIKPSLLGKIRSSVNKGMTDVASQVNRGMTDVASQVNKGVNGVASQVN... | Function: Connects telomeres to the nuclear envelop (NE) during both vegetative growth and meiosis. This connection ensures clustering of telomeres to the spindle pole body (SPB) when cells enter meiotic prophase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 47827
Sequence Length: 432
Subcellular ... |
A8KBY2 | MSKNCPECGSSRVVEDDLYSQKQWVCEDCGSVVSEGLLTTTLSEESHSRAVPFFTSTAAFKKPCRNLVSGFSRLRALCRIFRLSSSMEDASANLFERAYNHPNFLHISLSKKQILAGCCMFHICRQNSWPVFMGTIGYLLDADNYQMGTIYQELTKSLNLQTTQVCITRMLESFCYDFKLAPDEVEEVFSVAQQRLVDQTSALLELAADTWILTGRRPFPLFLAAVYVAWQSLNPLARMKYSLMKFCKIAKAPEQLWCKSKDTINKRLNELLEVLCKLGRELPWVRPTDIQMNTVTTLVEDILKHRKALLILAVKHYEKQ... | Function: General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites. Contributes to the regulation of gene expression; functions as activator in the absence of oxidative stress. Down-regulates ... |
Q9HAW0 | MPGRGRCPDCGSTELVEDSHYSQSQLVCSDCGCVVTEGVLTTTFSDEGNLREVTYSRSTGENEQVSRSQQRGLRRVRDLCRVLQLPPTFEDTAVAYYQQAYRHSGIRAARLQKKEVLVGCCVLITCRQHNWPLTMGAICTLLYADLDVFSSTYMQIVKLLGLDVPSLCLAELVKTYCSSFKLFQASPSVPAKYVEDKEKMLSRTMQLVELANETWLVTGRHPLPVITAATFLAWQSLQPADRLSCSLARFCKLANVDLPYPASSRLQELLAVLLRMAEQLAWLRVLRLDKRSVVKHIGDLLQHRQSLVRSAFRDGTAEVE... | Function: General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites . Contributes to the regulation of gene expression; functions as activator in the absence of oxidative stress . Down-regulate... |
Q4V8D6 | MPNGSRCPDCGSSELVEDSHYSQSQLVCSDCGCVVTEGVLTTTFSDEGNLREVTYSRSTGENEQVSRSQQRDLRRVRDLCRILKLPLTFEETAVSYYQKAYQLSGIRAARLQKKEVVVGCCVLITCRQHNWPLTMGAICTLLYADLDVFSSTYMQIVKLLGLDVPSLCLADLVKSYCSSFKLFQASPSMPAKYVEDKDKMLSRTLLLVELANETWLVTGRHPLPIITAATFLAWQSLRPSDRLTCSLARFCKLANVDLPYPAASRLQELLAVLLQMASQLAWLQVLRLDKRSVVKHIGDLLQHRHMLVRMAFQDGTAEVE... | Function: General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites. Contributes to the regulation of gene expression; functions as activator in the absence of oxidative stress. Down-regulates ... |
A4QNR3 | MSGAKQCPDCGSSDIVEDAHYSQDQVVCADCGCILSEGLITTTAAEESHLQAVRFADSTGENDSMTVSKLRGIVRVRNICRVLRLPDGFSDTAVSYYEQAYKHPLYHSVSIEKKEIIVGCCVYITCRQHQWPITMATICSLVYAKKELFASIFLSIVQVLKLDVPSVSLQNLVMSHCRSFKLFKDSCEVPSHYAEKLDTVSERTVQTVELAYETWLVTGRHPIPIITAAAYISWQSLLPARRLSCSLSRFCKLSDVDLPPPSAIRLRELQGTLIKLSVYLPWLKVLSLNKKTVVQHLGDLLRHRVFLLRKALAVTEAELS... | Function: General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites. Contributes to the regulation of gene expression; functions as activator in the absence of oxidative stress. Down-regulates ... |
Q9FHE4 | MAVEARHMNLFSSQYITNRECVKSQTNMNNGQQIAGGGFPVTIGDRNLQYIDPINSFNKSESELTAISKRQRDSTFDSDALIASQKRRAIAFSPASLIDAELVSQIQQQNSEIDRFVAQQTETLRIELEARQRTQTRMLASAVQNAILKKLKAKDEEIIRMGKLNWVLQERVKNLYVENQIWRDLAQTNEATANNLRSNLEQVLAQVDDLDAFRRPLVEEADDAESSCGSCDGGDVTAVVNGGCKRCGELTASVLVLPCRHLCLCTVCGSSALLRTCPVCDMVMTASVHVNMSS | Function: E3 ubiquitin-protein ligase involved in regulation of abiotic stress responses. Not involved in ubiquitination of MYB108/BOS1. Has no effect on the stability of the DELLA proteins.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conj... |
F4IDI6 | MAVDAHHLFLSPPQLFSNRELTMNNNTMEPTSGGFCNNNQTGYGVVSPFSVPNHTSTTTTATPPLLHVYGGSDTIPTTAGYYADGATNLDCEFFPLPTRKRSRDSSRSNYHHLLLQNPRSSSCVNAATTTTTTTLFSFLGQDIDISSHMNQQQHEIDRFVSLHLYQMERVKYEIEEKRKRQARTIMEAIEQGLVKRLRVKEEERERIGKVNHALEERVKSLSIENQIWRDLAQTNEATANHLRTNLEHVLAQVKDVSRGAGLEKNMNEEDDAESCCGSSCGGGGEETVRRRVGLEREAQDKAERRRRRMCRNCGEEESCV... | Function: Probable E3 ubiquitin-protein ligase. Has no effect on the stability of the DELLA proteins.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass ... |
Q9LDD1 | MAVEAHHLNPLFSSNREMIHPVEASGVVYNTQMRYGTVPTFNPTVECQTSLFNPIYNISPVDRLVHQSMKPTIQSVDSSLTFNSDNNVDFLRPVSSRKRSREESVVLNPSAYMQIQKNPTDPLMFLGQDLSSNVQQHHFDIDRLISNHVERMRMEIEEKRKTQGRRIVEAVEQGLMKTLRAKDDEINHIGKLNLFLEEKVKSLCVENQIWRDVAQSNEATVNALRSNLQQVLAAVERNRWEEPPTVADDAQSCCGSNDEGDSEEERWKLAGEAQDTKKMCRVGMSMCRSCGKGEASVLLLPCRHMCLCSVCGSSLNTCPI... | Function: Probable E3 ubiquitin-protein ligase. Has no effect on the stability of the DELLA proteins.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass ... |
Q9XF92 | MGFPVGYTEVFLPKLFVQTLSILGFIRTIVFSIFRFLGLSDFLEMDQTWPDYTSYPTRIPETRSPFSALLIREILPVIKFEELTNSGEDLPENCAVCLYEFEGEQEIRWLRNCRHIFHRSCLDRWMDHDQKTCPLCRTPFVPDEMQEEFNQRLWAASGVHDFHCPVTELL | Function: May be involved in the brassinosteroids (BRs) signaling pathway and regulate the growth and development of rosette leaves . Seems to prevent over development of leaves and inflorescence stems .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20060
Sequence Length: 170
Subcellular Location:... |
Q8WY22 | MGARASGGPLARAGLLLLLLLLLLLGLLAPGAQGARGRGGAEKNSYRRTVNTFSQSVSSLFGEDNVRAAQKFLARLTERFVLGVDMFVETLWKVWTELLDVLGLDVSNLSQYFSPASVSSSPARALLLVGVVLLAYWFLSLTLGFTFSVLHVVFGRFFWIVRVVLFSMSCVYILHKYEGEPENAVLPLCFVVAVYFMTGPMGFYWRSSPSGPSNPSNPSVEEKLEHLEKQVRLLNIRLNRVLESLDRSKDK | Function: Involved in tumorigenesis and may function by stabilizing p53/TP53.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27836
Sequence Length: 251
Subcellular Location: Mitochondrion outer membrane
|
P48582 | MKPYLFDLKLKDTEKLDWKKGLSSYLKKSYGSSQWRTFYDEKATSELDHLRNNANGELAPSSLSEQNLKYYSFLEHLYFRLGSKGSRLKMDFTWYDAEYSSAQKGLKYTQHTLAFEKSCTLFNIAVIFTQIARENINEDYKNSIANLTKAFSCFEYLSENFLNSPSVDLQSENTRFLANICHAEAQELFVLKLLNDQISSKQYTLISKLSRATCNLFQKCHDFMKEIDDDVAIYGEPKWKTTVTCKLHFYKSLSAYYHGLHLEEENRVGEAIAFLDFSMQQLISSLPFKTWLVEFIDFDGFKETLEKKQKELIKDNDFIY... | Function: Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. Fusion between endosomes and the vacuole will then target the cargo proteins to the vacuolar lumen. Acts as an adapter that recruits the DOA4 deubiquitinas... |
P12428 | MQESGGSSGQGGPSLCLEWKQLNYYVPDQEQSNYSFWNECRKKRELRILQDASGHMKTGDLIAILGGSGAGKTTLLAAISQRLRGNLTGDVVLNGMAMERHQMTRISSFLPQFEINVKTFTAYEHLYFMSHFKMHRRTTKAEKRQRVADLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYSVIKTLRHLCTRRRIAKHSLNQVYGEDSFETPSGESSASGSGSKSIEMEVVAESHESLLQTMRELPALGVLSNSPNGTHKKAAICSIHQPTSDIFELFTHIILMDGGRIVYQGRTEQ... | Function: ATP-dependent transporter of the ATP-binding cassette (ABC) family which transports various molecules including bioamines, neurotransmitters and metabolic intermediates . In the eye and probably in association with w/white, required for the transport of the eye red pigment precursor, guanine, into pigment cel... |
Q5VW32 | MTHWFHRNPLKATAPVSFNYYGVVTGPSASKICNDLRSSRARLLELFTDLSCNPEMMKNAADSYFSLLQGFINSLDESTQESKLRYIQNFKWTDTLQGQVPSAQQDAVFELISMGFNVALWYTKYASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHLPKLITPAEKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKADHTLSSLEPAYSAKWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKEYGETKGPGPTVKPSGHLFFRKLGNLVKNTL... | Function: Nuclear envelope-associated factor that is involved in the nuclear envelope ruptures during interphase (NERDI) repair, where it is locally recruited by CHMP5 and reduces cytoskeletal stress through its action on SYN2 to help reseal the ruptured membrane.
PTM: Farnesylation is required for nuclear envelope loc... |
A4IIL4 | MTHWFHRNPLKATAPVSFNFYGVASTQAASKICSDLRSTRARLLELFSDITCNHEMMKNATDAYFSLLLGFIDSLDGGTQDNKLRYIQNFKWTDTLQGNAPSAQQDAVFELVSMGFNVALWYTKYASRLAGKEDITEEEAKEVHRSLKIAAGVFKHLKENHIPKLITPVEKGRDLETRVIDAYTVQCQAEAQEVTIARAIELKHNPGLIAALAYETANYYQKVDHTLATLDPVYIAKWRSYTQLKMCFYMAYSYCYHGQTLLSADKCGEAIRSLQEAEKFYGKAEALCKEYGETKGPGTTAKPSGHLFFRKMGTLVRNTL... | Function: Nuclear envelope-associated factor that is involved in the nuclear envelope ruptures during interphase (NERDI) repair.
PTM: Farnesylation is required for nuclear envelope localization.
Location Topology: Lipid-anchor
Sequence Mass (Da): 46510
Sequence Length: 411
Subcellular Location: Nucleus membrane
|
F4I7Y4 | MGCCQSSFLKPSSLHDKKITSDDLSGRRGKGAKRGNRHRHANINEGRGWHFSDVPDFSEFSASVLRDATNNFNKNAVVSVCSDQEPNLVYQGCIRSDKDKRLIAVKKFSKTTWPDPKQFATEARAIGSLRHVRLVNLIGYCCEGDERLLVSEYMPNESLTKHLFHWEKQTMEWAMRLRVALYVAEALEYCRQSGLKLYHDLNTCRVLFDENGSPRLSCFGWMKNSKDGKNFSTNLAYTPPEYLRSGTLIPESVVFSFGTFLLDLLSGKHIPPSHAVGTIQKQNLNVLMDSHLEGNYPEEDAAMVFDLASKCLHNNPNERP... | Function: Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1.
PTM: Phosphorylated by BRI1, ASK7/BIN2 and ASK9/BIL2.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein... |
Q7XJT7 | MGCCYSLSSTVDPVQDHTTDASSEPRNGGGEDPPLTKFSFSALKTATNHFSPENIVSDQTSDVVFKGRLQNGGFVAIKRFNNMAWSDPKLFLEEAQRVGKLRHKRLVNLIGYCCDGDKRFLVADFMANDTLAKRLFQRKYQTMDWSIRLRVAYFVAEALDYCNTAGFASYNNLSAYKVLFDEDGDACLSCFGLMKEINNDQITTGSVNPENVIYRFGTVLVNLLSGKQIPPSHAPEMIHRKNVFKLMDPYLKGKFSIDEANVVYKLASQCLKYEGQESPNTKEIVATLETLQTRTEAPSYEVVEMTNQEKDASSSSNLSP... | Function: Probable inactive protein kinase that activates the YODA MAP kinase cascade, which regulates the asymmetric first division and embryo polarity, by promoting the elongation of the zygote and the development of its basal daughter cell into the extra-embryonic suspensor. Acts as an adapter at the plasma membrane... |
Q336V9 | MGCCGSSLRVGSHAPEKPPRRARPPPPPPQPHHPRRPSFTLNAHQAAASSSAASAAPAPAFAEFSLAELREATGGFAAANIVSESGEKAPNLVYRGRLQGAGGGGRAIAVKKFGKLAWPDPKQFAEEARGVGKLRHRRMANLIGYCCDGDERLLVAEFMPNDTLAKHLFHWENKAIEWAMRLRVAYNIAEALEYCSNEERPLYHDLNAYRVLFDENGDPRLSCFGLMKNSRDGKSYSTNLAYTPPEYLRNGRVTLESVVFSFGTILIDLLSGKRIPPTLALDMIRSRSIQAIMETNLEGKYSIEEATTLVDLASKCLQYE... | Function: Probable serine/threonine kinase that functions as a positive regulator of plant immunity. May be involved in the regulation of pattern-triggered immunity (PTI). Does not seem to be involved in responses to brassinosteroid (BR) signaling.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-... |
Q944A7 | MGCCQSLFSGDNPLGKDGVQPQPLSQNNHGGATTADNGGSGGASGVGGGGGGGGIPSFSEFSFADLKAATNNFSSDNIVSESGEKAPNLVYKGRLQNRRWIAVKKFTKMAWPEPKQFAEEAWGVGKLRHNRLANLIGYCCDGDERLLVAEFMPNDTLAKHLFHWENQTIEWAMRLRVGYYIAEALDYCSTEGRPLYHDLNAYRVLFDEDGDPRLSCFGLMKNSRDGKSYSTNLAYTPPEYLRNGRVTPESVTYSFGTVLLDLLSGKHIPPSHALDMIRGKNIILLMDSHLEGKFSTEEATVVVELASQCLQYEPRERPNT... | Function: Serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1. Mediates signal transduction from BRI1 by functioning as substrate of BRI1 . Functions as a positive regulator of plant immunity. May be involved in the regulation of pattern-trigg... |
Q9LS26 | MGCLHSKTANLPSSDDPSAPNKPESVNGDQVDQEIQNFKEFELNELRKATNGFSPSCIVSEGGEKAPNVVYRGKLEGNHLVAIKRFSRQSWPDAQQFVVEATGVGKLRNKRIVSLIGCCAEGDERLLVAEYMPNDTLSKHLFHWEKQPLPWDMRVRIADYIAEALDYCNIENRKIYHDLNAYRILFDEEGDPRLSTFGLMKNSRDGKSYSTNLAYTPPEFLRTGRVIPESVIFSYGTILLDLLSGKHIPPSHALDIIRGKNALLLMDSSLEGQYANDDATKLVDLASKCLQSEAKDRPDTKFLLSAVAPLQKQEEVASHV... | Function: Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1. Mediates signal transduction from BRI1 by functioning as substrate of BRI1.
PTM: Phosphorylated by BRI1 upon brassinolide (BL) treatment.
Location Topology: Lipid-anchor
C... |
Q8W4L3 | MGGQCSSLSCCRNTSHKTAVLEAPDVDNGESSEITDVPNFREYTLEQLKAATSGFAVEYIVSEHGEKAPNVVYKGKLENQKKIAVKRFTRMAWPDSRQFLEEARSVGQLRSERMANLLGCCCEGDERLLVAEFMPNETLAKHLFHWETQPMKWTMRLRVVLYLAQALEYCTSKGRTLYHDLNAYRVLFDEECNPRLSTFGLMKNSRDGKSYSTNLAFTPPEYLRTGRITPESVIYSFGTLLLDLLSGKHIPPSHALDLIRDRNLQTLTDSCLDGQFSDSDGTELVRLASRCLQYEARERPNTKSLVTALTPLQKETEVLS... | Function: Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1. Mediates signal transduction from BRI1 by functioning as substrate of BRI1 . Functions redundantly with BSK4, BSK6, BSK7 and BSK8 .
PTM: Phosphorylated by BRI1 upon brassi... |
Q4WUK5 | MSGPNRTYSFGEGDDSLAHPSSRTHAMHSQYDDVSPISDGARMNPMNGQGMDHGLASVLEDGRQGWGRSPEPSPSLLTGSSATPGMDNLGPGAVGGGISGIALSVANSHDRLSGVEALMGTDGQEANIPAERGLSTTGSDNPYVPEPPEHRYSYGSNIALGAAAAPAGQLTPGQSVSHLSSTNPSQRNLYDIPYQDVGGLNAGPYQRHSAYSSNDLPVDINPDEIVDDGDDGFVPAPNSGSGARKSQAIPAAAGGAAAGGVLGNLGGLFGGKSAADTSYGPVPGAGLEAGEKGRWVKPKPGGGNKKRGWIVGAILAFIII... | Function: Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation. Active on laminarin and lichenan (By similarity).
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (... |
A2QN74 | MAGVNRSFSYSRGDDALLRDDEREISPLRSAEDGLYSTSYGDVSPLSAGVQAQNRPFDRGLVSVPEGQTLERHMTSTPGMDNLGPASVGGGISGIALGVANSHNRQSGVDAFRETDVPVRNLPAERDFNTTGSDNPYIPAPPDGDIYPSSEAVRYRDSYSSHTGLGAGAPFAEHSTPGTTPSQRSFFDSPYQGVDAGPYQRHSAYSSHDYPLVINPDDIADDGDDGFPVHPKGAADYRSNANVPGTGVAGAAAAGGFLGKFRALFKREEPSPFYDSDIGGGLGGAEKAQGGRHIIGGGSRKRGWIVGLILAAVIVAAIVG... | Function: Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation. Active on laminarin and lichenan (By similarity).
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (... |
Q5B430 | MGDRSEQYGDIPPISSQHRMHGYGNNGEPAAMPGDGQQNWGSGPGIAHTHSMRTASTATPGMDNLGPSAVGGGISGIALGVANTHDRQSGIDAFRDADATLGYIPAERGYHTTGADNPYVPSPPSVGPGPDESSEGLRSHETFGSSAALSAAGAPAGNWTPPSGSRHSFLDGSYQGVASGPYQRHSAYSSQDYPADINPDDILDDGDDGFAAAPSNKPNAAGGAATGGAAGGLLGEFFGAKKAADASYDPVPGAGLPSVEKYAKPRPSGASRKRGWIIGGILAFIVIGAIVGGAVGGTLGNRRSETASESSEVSADDDTE... | Function: Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation. Active on laminarin and lichenan.
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glu... |
B0Y9Q9 | MRGAILATAAALAGTAMADVAHMRRHGHDSFHQRRSPLAEADATCGCTTEVVTVWGPPTLIPVASPTPSTVTSEAVTTLHSTSTTTVTVIASASTPAASPSPATDKVPLPTPAITNFPSTGVYTIPATTVTVFDTTTVCGATTTELPAGTHTYGGVTTVVETATTVVCPYATVEPSGTTVTSVIKTTTYVCPSAGTYTIAPTTTTVPTSTVIVYPTPAVITPGTYTQPEQTVTVTRTDYTYVCPFTGQDEPTSAPAAPSTTAVPATTTAAPETTTAAPDTTTAVPSTSSAAPSSSSTAPASTGAVSGQMGMTYTPYTKGG... | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-gl... |
Q5BD29 | MRGAILATAAAFAGTAVADMHMRRHAHEGLHHRALHASSAVPEEECGCTTEVITYWGEPTTIPLSVPTSTVTSETTETVHSTSYSTVTVTATSSAAPVETPSETPSPTPEVTLPTAGVTSYSETGTYTIPATTITVTDTTTVCGATTTELPSGTHTYGGVTTIVETATTITCPYATVKPTGSTVTSVIETTTYVCPSAGTYTIAPTTTFVPTSTVVVYPTPETVTPGTYTNPGTTITVTRTEDVYVCPYTNGNVPTSVPALPTTSAASTTTAVPSSSTTTSSATSVPTGASGNKMGMTFTPYNNDGSCMAKNDVLEQVGL... | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-gl... |
P08630 | MMGTKHRNSHVNGSIKSSSSLRSSSKSFQAKMDLMSERLYDVVKSGSMVKRAQNKKRFTPVNYKHRWFELTKRTFSYFDVENVERRRERGRIHLKGVRLVEEATVSGEGGDPFAPDGYPFQVGYCEISASANSHQLENGNGGGSGVGIEGQQSGRAVPQYTLYVIANSEKERSEWIRAIRQVCEDSNTPKSYRYHPGLWSGKKWSCCKGLSRTTFGCRAAAHWREANNNPSNGSSPAQNSTRSISPNSSTTNSQFSLQHNSSGSLGGGVGGGLGGGGSLGLGGGGGGGGSCTPTSLQPQSSLTTFKQSPTLLNGNGTLLD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Required for proper ring canal development. Also required for the development of male genitalia and for adult survival.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 87392
Sequence Length: 786
EC: 2.7.10.2... |
Q8JH64 | MASIILESIFLKRSQQKKKTSPLNFKKRLFLLTESKLSYYEYDFERGRRGSKKGSVDIEKITCVETVVPENNPPPERQVPKKGEDYNMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKSVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCKILESRNGSLKAGRSHRKTKKPLPPTPEEDTMVMKPLPPEPAPSAAGEMKKVVALYNYVPMNVQDLQLQKGEDYLILEESHLPWWKARDKNGREGYIPSNYVTATSNSLEIYEWYSKNITRSQAEQLLKQEGKEGGFIVRDSTSKTGKYTVSVYAK... | Cofactor: Binds 1 zinc ion per subunit.
Function: Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling . Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation (By similarity). After BCR engagement and activ... |
Q06187 | MAAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYEYDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIPRRGEESSEMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILENRNGSLKPGSSHRKTKKPLPPTPEEDQILKKPLPPEPAAAPVSTSELKKVVALYDYMPMNANDLQLRKGDEYFILEESNLPWWRARDKNGQEGYIPSNYVTEAEDSIEMYEWYSKHMTRSQAEQLLKQEGKEGGFIVRDSSKAGKYTVSVF... | Cofactor: Binds 1 zinc ion per subunit.
Function: Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling . Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation . After BCR engagement and activation at the pl... |
Q05619 | MSYKLLIINPGSTSTKIGVYEGEKELFEETLRHTNEEIKRYDTIYDQFEFRKEVILNVLKEKNFDIKTLSAIVGRGGMLRPVEGGTYAVNDAMVEDLKVGVQGPHASNLGGIIAKSIGDELNIPSFIVDPVVTDELADVARLSGVPELPRKSKFHALNQKAVAKRYGKESGQGYENLNLVVVHMGGGVSVGAHNHGKVVDVNNALDGDGPFSPERAGSVPIGDLVKMCFSGKYSEAEVYGKAVGKGGFVGYLNTNDVKGVIDKMEEGDKECESIYKAFVYQISKAIGEMSVVLEGKVDQIIFTGGIAYSPTLVPDLKAKV... | Function: Catalyzes the conversion of butyryl-CoA through butyryl phosphate to butyrate.
Catalytic Activity: ATP + butanoate = ADP + butanoyl phosphate
Sequence Mass (Da): 38434
Sequence Length: 355
Pathway: Lipid metabolism; butanoate metabolism.
Subcellular Location: Cytoplasm
EC: 2.7.2.7
|
Q9RVA9 | MSMIAHVINPGISGVKLACAVIEPGQNPAFPSHLQVSLTREELPLEAAPDELGLDALAERILEQTAAWPAPDAVVGRGGLMGRVPAGTYHVTPELARYVLENVSGSQPADDPNPGIGAPLALRVAQARGVPAYIVDPQSVDELLPEAHMTGVPGVRREARFHALNARAVARRAAYEVGKQFREARVVVAHLGVTTSVTAFDQGRAIDTTGTAPDGGPMGARQSGPLPTRAVIRLLQTQSESELLRLLTRGSGFFALTGTADLSEIERRQEQGEDSVVQTAIAAFVHQVCKAIGEQTAALPGRPDAVALTGGIARWDAVVD... | Catalytic Activity: ATP + butanoate = ADP + butanoyl phosphate
Sequence Mass (Da): 40533
Sequence Length: 383
Subcellular Location: Cytoplasm
EC: 2.7.2.7
|
B2KEH0 | MEHNILVINPGSTSDDIGYYKGPKTVFEESARYSQEELDSFAGKELSEQIPLRRKFLLDVLKKHEINLNEIDAVIGRGGLLKHIEGGIYTINEAMLADLKRGYNGHHPSNLGGILAREIAESLGKPCFIADPVVVDEMEPLARYTGFKEIKRKSIFHALNQKRVAITAAKELGKKYKECNFIVMHGGGGVSVGAHKKGKVIDVSDGFEGAGPMTPQRSGVLPSLELVEMCFSGQYTIQELRKKMRGRGGMIAHTGTSDIADLYNYISSGKKKPGSTINCSREAAQEAFDAMIYQISKEIGAMATVLKGDVDAIILTGGLA... | Catalytic Activity: ATP + butanoate = ADP + butanoyl phosphate
Sequence Mass (Da): 40599
Sequence Length: 370
Subcellular Location: Cytoplasm
EC: 2.7.2.7
|
Q9RPS7 | METVLVINPGSTSTKLALFANHDCLAEETLRHSVQELAPFENVVSQTSFRKQMIAEFLETHNIIQLAAVVGRGGLLKPIPGGTYLVDQQMLEDLRTERFNTHASNLGAILANEFAEKYHVPAFIVDPVVVDELQPLARISGLKGIQRRSVGHALNQKAVARKIAEDLGKTYEQSNFIVVHLGGGISLGAHQKGRMVDVVNGLDGEGPYTPERSGALPLVEFAQWILEQELTISQVKKLIAGNSGLKSYLGETDLRHIQAQIAAGDQTANYYLKGMCYQIAKSIGEMAVVLEGTIDAIILTGGAAYSQTVVQEISQKVTWI... | Catalytic Activity: ATP + butanoate = ADP + butanoyl phosphate
Sequence Mass (Da): 39256
Sequence Length: 360
Subcellular Location: Cytoplasm
EC: 2.7.2.7
|
P54621 | MQEQKFRILTINPGSTSTKIGVFENERAIVEKTIRHEGRCFGNIKR | Catalytic Activity: ATP + butanoate = ADP + butanoyl phosphate
Sequence Mass (Da): 5334
Sequence Length: 46
Subcellular Location: Cytoplasm
EC: 2.7.2.7
|
I1RV18 | MSWKAIAKAAQAEVLDAIPTKWKLDPAKYRTLTDVTSVPRECGILSDAQLSITDLTALEVVKRIESRELTAVQALEAFGARTAIAHQLVNCLMDWFYEDGLRQAEELDKSFKATGKLKGPLHGVPVALKDFHFVAGRPTTTGYVSRRDFRPEHDSALVKTLRDAGAVFYCKTTMPQSGMAIETVSNLWGRTLNPYNTALSAGGSSGGDAVLVALKGTPITPSTDLGGSIRVPAAFNGLYAIRPTSDRIPKGGMDNINSGQISIKLSCGPICHSMEDLESFTKLINAYPENQNDPTSVPVPWKTVKPIEGKLTIGLMKWDK... | Function: Amidase; part of the gene cluster that mediates the biosynthesis of butenolide, a mycotoxin that shows antibiotic activity but does not seem to play a major role in the spread of head blight in wheat . Butenolide is derived from glutamic acid via a 4-acetamido-2-butenoic acid intermediate (Probable). The pred... |
I1RV19 | MAMFTVLPLIWLAPLGLISLFFYYIIPYFWNYRHLRSIPGPLFARLSNWWLVYACREKSRWKYVNDAHTRYGPVVRIQPNHVSIANEEVINAIYGHGNGMLKSSFYDASVITTYSIFTSRDRAEHSRKRKVVSHSFAPQSMRNFEPFIQQHLNVFLQKWDAMAANEAKFDGYADVESRVWLNYLVLDIIGDLAFGAPFGVLAKGSEVVDFETEKGPSSLPVITSLSTRSEIAATVGALPELKPYLKWSPDPFFRTGFNGMINLRTLGTSRITDRLNNPPGDEREKDLLERVREGRDHKGQPFGKGELIAEALTVLIAGTD... | Function: Cytochrome P450 monooxygenase FG08079; part of the gene cluster that mediates the biosynthesis of butenolide, a mycotoxin that shows antibiotic activity but does not seem to play a major role in the spread of head blight in wheat . Butenolide is derived from glutamic acid via a 4-acetamido-2-butenoic acid int... |
I1RV21 | MTASSRPAEYRDVRTANLNTITFDNLFDKDEAELKRLIESCEKDGFFYLDLKSAASQKFWNDLYTIDSTTKDWFKQPIEKKLQTPTVSLAHGFKAVGNQSGSIESKKDGFEALKIGKSELDGRWALPDVVSDNLPLFDQFASSCHFISKLLLDCLSDGLNLKGDARFETHHRDDCRSKSTLYFLHYPPGAQDPNKVGQNMHTDIGTLTILYAPQWGLQVFSPADGAWEYVEPRPNQIIVNVGDTLRFLSGKRFKSALHRVLPLGGIQIEDRYSISYFLRASDSTEFKDSDEDESNAKQWYTKKYAMYEMPHVIQKQQTTL... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of butenolide, a mycotoxin that shows antibiotic activity but does not seem to play a major role in the spread of head blight in wheat . Butenolide is derived from glutamic a... |
I1RV22 | MINITKPQNWTRGDYLVSTDPALLQVDAINAALSSDMVWWAGDLPADALWDALRSSICFGLYRKRSSEMNGTGPTVEYKIEEWEQVGLVRMITDGVTFGYLTDVYILPEHQGGGRGRWMLQILNEALQGWPHLRRVMLLTTDKMHLFGKNLGMKDYREFDGMKGVSIAMVEGPGAQH | Function: Putative acetyltransferase; part of the gene cluster that mediates the biosynthesis of butenolide, a mycotoxin that shows antibiotic activity but does not seem to play a major role in the spread of head blight in wheat . Butenolide is derived from glutamic acid via a 4-acetamido-2-butenoic acid intermediate (... |
I1RV23 | MDNGLSRRHEISELLQLVDSTTTRAFHTSNGSPKSDCRNDSKPLKRYEELFGSFPAEGLGTSGFKDAIDLISRNSVDNASPGFLGKLVSAPSAPGIASDLFLSILNNNGHVQRAGPALTAIEKHTSLELARLFDLQGPHAGGVTVPGGAAGNLMAMLVARNIVAPESKQRGLTPGEYAIFVSDAAHYSVSNSANVIGLGNDSIIRVPALDDGTMDADALQRAVDQAGKDGKKPLLIAATSGSTVNGAFDPLDKIGEIAHRVGAWFHVDACWGGGVVFSDKLKHLMKGSHLADSIAFNPHKLLGVPLVCAFLLVNDLRTLW... | Function: Glutamate decarboxylase-like protein; part of the gene cluster that mediates the biosynthesis of butenolide, a mycotoxin that shows antibiotic activity but does not seem to play a major role in the spread of head blight in wheat . Butenolide is derived from glutamic acid via a 4-acetamido-2-butenoic acid inte... |
I1RV24 | MPPQQEQDTDSDAIRSYNEESKSETPGCIPDAMLSSDETSNDVASDISPPPDGGWNAWLCTLCGHFLFMNTWGFINSFGIFQTYYTTFLDRDPSDISWIGSIQVFLSFFVGAFVGRYIDSGHLRLVLSCGTILVLIGIFTASLSTQYWQLILSQGICCGLGNGFLVTPAVSVTSTYFAKRRSLAIGISTCGSVTGALVFNSMARQLLPTAGFGWTMRAIGFVQAATLLFVVVAMKTRLPPTKSGRLVEWVAFKQLDYTFFTIGMFFNFWAVFFGYYYIAPYSRDIITPTLTYTQSLNLLLILNGVGVFGRMIANHYADTF... | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of butenolide, a mycotoxin that shows antibiotic activity but does not seem to play a major role in the spread of head blight in wheat.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48062
Sequence Length: 441
Su... |
Q5HJP2 | MTNNKVALVTGGAQGIGFKIAERLVEDGFKVAVVDFNEEGAKAAALKLSSDGTKAIAIKADVSNRDDVFNAVRQTAAQFGDFHVMVNNAGLGPTTPIDTITEEQFKTVYGVNVAGVLWGIQAAHEQFKKFNHGGKIINATSQAGVEGNPGLSLYCSTKFAVRGLTQVAAQDLASEGITVNAFAPGIVQTPMMESIAVATAEEAGKPEAWGWEQFTSQIALGRVSQPEDVSNVVSFLAGKDSDYITGQTIIVDGGMRFR | Function: Catalyzes the irreversible reduction of 2,3-butanediol to (S)-acetoin in the presence of NADH.
Catalytic Activity: (S)-acetoin + NAD(+) = diacetyl + H(+) + NADH
Sequence Mass (Da): 27216
Sequence Length: 258
EC: 1.1.1.304
|
Q8CQD2 | MSKTAIITGAAGGLGKGIAERLANDGFNIVLQDINEALLLETEKEFKEKGYQAVAYKSDVSKKKEQEELVQFAVTEFGQLDVMVNNAGVDAVTPILEIGEEELSKLFNINVFGTLFGIQAAANQFIKQKSKGKIINACSIAGHESYEVLGTYSATKHSVRSFTQTAAKELADKGITVNAYCPGVAKTEMWDRIDEEMVKLDDSLEIGDAFEAFSSEIKLGRYQEPSDVANLVSFLASNDSDYITGQSILTDGGLVYR | Function: Catalyzes the irreversible reduction of 2,3-butanediol to (S)-acetoin in the presence of NADH.
Catalytic Activity: (S)-acetoin + NAD(+) = diacetyl + H(+) + NADH
Sequence Mass (Da): 27917
Sequence Length: 257
EC: 1.1.1.304
|
P56685 | SIVPIRCRSNRDCRRFCGFRGGRCTYARQCLCGY | Function: Active against both Gram-positive and Gram-negative bacteria.
PTM: Contains three disulfide bonds.
Sequence Mass (Da): 3975
Sequence Length: 34
Subcellular Location: Secreted
|
Q8S307 | MTSDGATSTSAAAAAAAAAAARRKPSWRERENNRRRERRRRAVAAKIYTGLRAQGDYNLPKHCDNNEVLKALCVEAGWVVEEDGTTYRKGCKPLPGEIAGTSSRVTPYSSQNQSPLSSAFQSPIPSYQVSPSSSSFPSPSRGEPNNNMSSTFFPFLRNGGIPSSLPSLRISNSCPVTPPVSSPTSKNPKPLPNWESIAKQSMAIAKQSMASFNYPFYAVSAPASPTHRHQFHTPATIPECDESDSSTVDSGHWISFQKFAQQQPFSASMVPTSPTFNLVKPAPQQMSPNTAAFQEIGQSSEFKFENSQVKPWEGERIHDV... | Function: Transcriptional repressor that binds to the brassinosteroid (BR) response element (BRRE) 5'-CGTG(T/C)G-3' in gene promoter. Regulates positively the brassinosteroid-signaling pathway . Mediates downstream growth responses and negative feedback regulation of brassinosteroid biosynthesis. Promotes growth. Modul... |
B8B7S5 | MTSGAAAAGRTPTWKERENNKRRERRRRAIAAKIFTGLRALGNYNLPKHCDNNEVLKALCREAGWVVEDDGTTYRKGCKPPPSSAGGASVGMSPCSSTQLLSAPSSSFPSPVPSYHASPASSSFPSPSRIDNPSASCLLPFLRGLPNLPPLRVSSSAPVTPPLSSPTASRPPKIRKPDWDVDPFRHPFFAVSAPASPTRGRRLEHPDTIPECDESDVSTVDSGRWISFQMATTAPTSPTYNLVNPGASTSNSMEIEGTAGRGGAEFEFDKGRVTPWEGERIHEVAAEELELTLGVGAK | Function: Positive brassinosteroid-signaling protein. Mediates downstream brassinosteroid-regulated growth response and feedback inhibition of brassinosteroid biosynthetic genes. May act as transcriptional repressor by binding the brassinosteroid-response element (5'-CGTGCG-3') in the promoter of GRAS32 (AC Q9LWU9), an... |
Q9LN63 | MTSDGATSTSAAAAAAAMATRRKPSWRERENNRRRERRRRAVAAKIYTGLRAQGNYNLPKHCDNNEVLKALCSEAGWVVEEDGTTYRKGHKPLPGDMAGSSSRATPYSSHNQSPLSSTFDSPILSYQVSPSSSSFPSPSRVGDPHNISTIFPFLRNGGIPSSLPPLRISNSAPVTPPVSSPTSRNPKPLPTWESFTKQSMSMAAKQSMTSLNYPFYAVSAPASPTHHRQFHAPATIPECDESDSSTVDSGHWISFQKFAQQQPFSASMVPTSPTFNLVKPAPQQLSPNTAAIQEIGQSSEFKFENSQVKPWEGERIHDVA... | Function: Positive regulator of brassinosteroid (BR) signaling. Transcription factor that activates target gene expression by binding specifically to the DNA sequence 5'-CANNTG-3'(E box) through its N-terminal domain. Can bind individually to the promoter as a homodimer or synergistically as a heterodimer with BIM1, BI... |
O44220 | MWKFAIHSQQPFCWQQLCNRRHLYVGNVQQQTHLELLDAAPTRSDDEWLQAKPYEKVPGPGTWQVLSYFLPGGKQYNTNLIQMNRRMREWYGDIYRFPGLMGKQDVIFTYNPNDFELTYRNEGVWPIRIGLESFTYYRKVHRPEVFGSIGGLVSEQGKDWAHIRNKVNPVQMRVQNVRQNLPQIDQISREFVDKLDTLRDPVTHILNDNFHEQLKMWAFESISFVALNTRMGLLSDRPDPNAARLAEHMTDFFNYSFKYDVQPSIWPYYKTPGFKKFLQTYDKITEITTAYIDEAIKRFEIEKDSGNECVLQQLLSLNKK... | Function: Probably involved in steroid hormones biosynthesis.
Sequence Mass (Da): 62031
Sequence Length: 532
Subcellular Location: Mitochondrion
EC: 1.14.-.-
|
Q6IDS6 | MSDRILCKFFVHGSCLKGENCEFSHDSKDPPNNVCTFYQKRICLYGSRCRYDHVRAASNLPLSSDSESLDRSISTTPSRHLQQQGDNNDGDKSSNVYCIHPREYPICSFAAAGDCPRGNQCPHMHGDLCNTCGKKCLHPFRPEEREEHTKECEKKQKHIEALKQSQDIECSVCLDRILSKATPGERKFGLLTECDHPFCIQCIRNWRSSAPVSGMDVNSTLRACPICRKLSYFVVPSVVWYSSPEEKKEIIDIYKAKLRSIDCKHFNFGNGNCPFGASCFYKHAYSDGHLEEVVLRHLGSQEGETVITDSIRLSEFLGGL... | Function: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequ... |
Q94AD9 | MRTPMSDTQHVQSSLVSIRSSDKIEDAFRKMKVNETGVEELNPYPDRPGERDCQFYLRTGLCGYGSSCRYNHPTHLPQDVAYYKEELPERIGQPDCEYFLKTGACKYGPTCKYHHPKDRNGAQPVMFNVIGLPMRLGEKPCPYYLRTGTCRFGVACKFHHPQPDNGHSTAYGMSSFPAADLRYASGLTMMSTYGTLPRPQVPQSYVPILVSPSQGFLPPQGWAPYMAASNSMYNVKNQPYYSGSSASMAMAVALNRGLSESSDQPECRFFMNTGTCKYGDDCKYSHPGVRISQPPPSLINPFVLPARPGQPACGNFRSYG... | Function: Possesses RNA-binding and ribonuclease activities in vitro.
Sequence Mass (Da): 44704
Sequence Length: 404
Subcellular Location: Nucleus
EC: 3.1.-.-
|
P75925 | MSFTNTPERYGVISAAFHWLSAIIVYGMFALGLWMVTLSYYDGWYHKAPELHKSIGILLMMGLVIRVLWRVISPPPGPLPSYSPMTRLAARAGHLALYLLLFAIGISGYLISTADGKPISVFGWFDVPATLADAGAQADFAGALHFWLAWSVVVLSVMHGFMALKHHFIDKDDTLKRMLGKSSSDYGV | Cofactor: Binds 2 heme b (iron-protoporphyrin IX) groups per molecule.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20736
Sequence Length: 188
Subcellular Location: Cell inner membrane
|
Q8RN05 | MFEEKNALRGTEIHRRERFDPGPELRALMAEGRMSVMESEESPGGRTGWLATGYEETRQVLGSDKFSAKLLFGGTAAGRIWPGFLNQYDPPEHTRLRRMVASAFTVRRMRDFRPRIEAVVKATLDDIEATGGPVDFVPRFAWPIATTVICDFLGIPRDDQAELSRVLHASRSERSGKRRVAAGNKYWTYMGQVAAKTRRDPGDDMFGAVVREHGDDITDAELLGVAAFVMGASGDQVARFLSAGAWLMVEHPEQFAVLRDDPDSVPDWLNEVARYLTSDEKTTPRIALEDVRIGDQLVKKGDAVTCSLLASNRHRFPDPE... | Function: Involved in the coupling of aromatic side chains of the heptapeptide of vancomycin.
Sequence Mass (Da): 43829
Sequence Length: 391
Pathway: Antibiotic biosynthesis; vancomycin biosynthesis.
EC: 1.14.-.-
|
P30992 | MASMNFSPPEYPDYGTATLDPNIFVDESLNTPKLSVPDMIALVIFVMVFLVGVPGNFLVVWVTGFEVRRTINAIWFLNLAVADLLSCLALPILFSSIVQQGYWPFGNAACRILPSLILLNMYASILLLTTISADRFVLVFNPIWCQNYRGPQLAWAACSVAWAVALLLTVPSFIFRGVHTEYFPFWMTCGVDYSGVGVLVERGVAILRLLMGFLGPLVILSICYTFLLIRTWSRKATRSTKTLKVVVAVVVSFFVLWLPYQVTGMMMALFYKHSESFRRVSRLDSLCVAVAYINCCINPIIYVLAAQGFHSRFLKSLPAR... | Function: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a . The ligand interacts with at least two sites on the receptor: a high-affinity site on the extracellular N-terminus, and a second site in the transmembrane region which activates downstream signaling events. Receptor activation stimulate... |
P21730 | MDSFNYTTPDYGHYDDKDTLDLNTPVDKTSNTLRVPDILALVIFAVVFLVGVLGNALVVWVTAFEAKRTINAIWFLNLAVADFLSCLALPILFTSIVQHHHWPFGGAACSILPSLILLNMYASILLLATISADRFLLVFKPIWCQNFRGAGLAWIACAVAWGLALLLTIPSFLYRVVREEYFPPKVLCGVDYSHDKRRERAVAIVRLVLGFLWPLLTLTICYTFILLRTWSRRATRSTKTLKVVVAVVASFFIFWLPYQVTGIMMSFLEPSSPTFLLLKKLDSLCVSFAYINCCINPIIYVVAGQGFQGRLRKSLPSLLR... | Function: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a . The ligand interacts with at least two sites on the receptor: a high-affinity site on the extracellular N-terminus, and a second site in the transmembrane region which activates downstream signaling events . Receptor activation stimulat... |
Q6UNA4 | MDDMCSILTEEELSLYNITDCEFVKPGGLGPVLGPRHLSALVFYGLVFLLGVPGNALVVWVTGFRMPRSVTSLWFLNLALADLLCCLSLPLLMVPLAMDQHWPFGPVACKLLKGLLYLIMFCSVLLLVLISLDRFLLVSWPVWCQNWRRPRKAGWVCVGVWLLALLGSIPQFVYVKEVQLSTSKSECLGLYTVASAWANTTARFLVGFVLPFITIVTCHWVVYSRARRGSGVGPGRVSEARSRRTLRVIVAVSLSFFLCWFPLHILDFLVLSTPRHSSHSANIQLAHTLALCLAYCNSCLNPLLYVCLGRGFKQNINRSL... | Function: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a. This receptor stimulates chemotaxis, granule enzyme release and superoxide anion production.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39323
Sequence Length: 350
Subcellular Location: Cell membrane
|
Q9TUE1 | APMENSTYDYTNYDSLGTLDPSTPVDNTVRRLRPTTIVALVIYMAVFLVGVPGNALVVWVTALEAKRTVNAIWFLNLAVADLLSCLALPILFVSIIQEGHWPFGRAACSVLPSLILLNMYASILLLATISADRFLLVFNPIWCQNTRGAGLAWLACCVAWGLALLLTIPSFLYRKVLQDDYPPKTTCGVDYGHEGVRAERAVAIVRLVVGFLLPLFTLSVCYTFLLLRTWSRNGTRSTKTLKVVVAVVVSFFIFWLPYQVMGMILALLHPSSATFRWAIRLDPLCIALAYVNCCINPIIYVVAGKGFQGQLRKSLPSLLR... | Function: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a . The ligand interacts with at least two sites on the receptor: a high-affinity site on the extracellular N-terminus, and a second site in the transmembrane region which activates downstream signaling events. Receptor activation stimulate... |
A0A0S1TPC7 | MQVLILLSLAFLASCVVAYSRRRPGGRGAGDLPPGPPRLPIIGNMLQLGQNPHKSLAHLAKTYGPLMSLKLGNQFVVVVSSPEMAREVLQRHGLVFSRPFTPIAVQILGHGEVSMNMLPATSPIWKKIRKIAREKLFSNQALHATRAVRRERLRKLADYVGRCSGAMNVGEATFTTMSNLMFATLFSVEITQYADSDSDSGVNKKFREHVNAITRYMGVPNIADFFPIFAPFDPQGLRRKLTYHLGSLLELVQSLIEQRLRARNAATYRKKDDFLEMLLDLSEGDEYDLSVNEIKHLCVDLIIAGSDTSAATTEWAMVEL... | Function: Monooxygenase involved in the biosynthesis of carnosate, a potent antioxidant labdane-related diterpene natural product . Catalyzes the oxidation of 11-hydroxyferruginol to produce carnosate . Mediates the conversion of miltiradien into miltiradien-20-al (By similarity). Also involved in the production of pis... |
Q6YTF5 | METRELWVLAAALAVSLLYYLAALMRYAGGGCSRSSRPPLPPGPTPLPLIGNLLSLRGVLHHRLASLARVHGPVMALRLGLTTAVVVSSRDAAAEAFTKHDRRLAARVVPDSNRAHGFSDRSIIWLPSSDPRWKALRGIQATHLFSPRGLAAVRSVRESKVRDIVAYFRSRAGEEVVFGEAIYSGVLNLVSSSFFSVNMAGVGSEEAHGLRELVEDLVEAIAKPNVSDLFPFLRQLDLQGLRRRTEERMARAFGILDGIIDRRLANRTHGDRHGDFLDALLDLVSEGKMARDHVTIMLFEVFGAGSDTMSVSLEWAMAEL... | Function: Enzyme of the diterpenoid metabolism involved in the biosynthesis of the oryzalexin class of phytoalexins. Hydroxylates ent-sandaracopimaradien.
Catalytic Activity: ent-sandaracopimaradien-3beta-ol + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + oryzalexin E + oxidized [NADPH--hemoprotein reducta... |
Q6YTF1 | MENSQMWLLWGALSVALFFYFSTLRRRYAGGKPLPPGPTPLPLIGNLHLVGGGTFHHKLRDLARVHGPVMTLKLGLATNVVISSREAAIEAYTKYDRHLAARATPDTFRACGFADRSMVFIPSSDPQWKALRGIHASHVFTPRVLAAVRPIRERKVGDLIAYLRAHAGEEVLVGHAMYTGILNMVSFSYFSVDIVDMGSQMARELREVVDDIILVVGKPNVSDFYPFLRPLDLQGLRRWTTKRFNRVFSIMGDIIDRRLAHIRDNKPRHDDFLDSILELMAAGKIDRVNVLNMLFEAFVAGADTMALTLEWVMAELLKNP... | Function: Enzyme of the diterpenoid metabolism involved in the biosynthesis of both phytocassane and the oryzalexin class of phytoalexins. Can hydroxylate syn-pimaradiene, ent-pimaradiene, ent-sandaracopimaradiene, ent-isokaurene, ent-kaurene, and ent-cassadiene, but no activity with syn-stemodene, syn-stemarene, syn-l... |
Q9LZ31 | MFPLISFSPTSLDFTFFAIIISGFVFIITRWNSNSKKRLNLPPGPPGWPVVGNLFQFARSGKPFFEYAEDLKKTYGPIFTLRMGTRTMIILSDATLVHEALIQRGALFASRPAENPTRTIFSCNKFTVNAAKYGPVWRSLRRNMVQNMLSSTRLKEFGKLRQSAMDKLIERIKSEARDNDGLIWVLKNARFAAFCILLEMCFGIEMDEETIEKMDEILKTVLMTVDPRIDDYLPILAPFFSKERKRALEVRREQVDYVVGVIERRRRAIQNPGSDKTASSFSYLDTLFDLKIEGRKTTPSNEELVTLCSEFLNGGTDTTG... | Function: Catalyzes the epoxidation of physiological unsaturated fatty acids in vitro. Can use laurate, oleate, linoleate, linolenate and vernolate as substrate.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58138
Sequence Length: 512
Subcellular Location: Membrane
EC: 1.14.-.-
|
O22203 | MSWFLIAVATIAAVVSYKLIQRLRYKFPPGPSPKPIVGNLYDIKPVRFRCYYEWAQSYGPIISVWIGSILNVVVSSAELAKEVLKEHDQKLADRHRNRSTEAFSRNGQDLIWADYGPHYVKVRKVCTLELFTPKRLESLRPIREDEVTAMVESVFRDCNLPENRAKGLQLRKYLGAVAFNNITRLAFGKRFMNAEGVVDEQGLEFKAIVSNGLKLGASLSIAEHIPWLRWMFPADEKAFAEHGARRDRLTRAIMEEHTLARQKSSGAKQHFVDALLTLKDQYDLSEDTIIGLLWDMITAGMDTTAITAEWAMAEMIKNPR... | Function: Cytochrome P450 which catalyzes 3'-hydroxylation of p-coumaric esters of shikimic/quinic acids to form lignin monomers. Can use p-coumarate, p-coumaraldehyde, p-coumaroyl methyl ester, 5-O-(4-coumaroyl) D-quinate and 5-O-(4-coumaroyl) shikimate as substrates, but not p-coumaryl alcohol, p-coumaroyl CoA, 1-O-p... |
Q9CA61 | MIIYLISLLPIIVATLMLYQRWWRSNIPPGPKPKFLLGNLHQMKPLWTHSFSEWSETYGPIISVWIGSQLTVVVSSSDLARQVLRDKDHQLSNRHRIARMTQTGTDLVWSDYSPHYVKLRKLCTLELFSLKSIENFRSLREMEARSMVVSILKDLMSNSGDDQERKPVIVRKYLAAVVLNTISRLMIGKEFGSEEGKEFKAIVEKEHLLSGSGTILDHVWWLKWVSSWFFSDKEFLAHKDRRTKWFRGAIMVEEDIEIEDHRGFVRKLLVLKEQKELSEETVGGLVWNMLTAGADTTAVVIEWAMAEMIKCPTVQEKAQQ... | Function: Acts redundantly with CYP98A9 as tricoumaroylspermidine meta-hydroxylase. Catalyzes also the meta-hydroxylation of the three triferuloylspermidine phenolic rings. Unable to use 5-O-(4-coumaroyl) D-quinate or 5-O-(4-coumaroyl) shikimate as substrates.
Location Topology: Single-pass membrane protein
Sequence Ma... |
Q0JF01 | MMEINSEATVTLVSVVTLPILLALLTRKSSSKKRRPPGPWNLPLVGGLLHLLRSQPQVALRDLAGKYGPVMFLRTGQVDTVVISSPAAAQEVLRDKDVTFASRPSLLVSEIFCYGNLDIGFAPYGAYWRMLRKLCTVELLSTKMVRQLAPIRDGETLALVRNIEAAAGGKKPFTLATLLISCTNTFTAKAAFGQACGGELQEQFLTALDEALKFSNGFCFGDLFPSLRFIDAMTGLRSRLERLRLQLDTVFDKIVAQCESNPGDSLVNVLLRIKDQGELDFPFSSTHVKAIILDMFTGGTETTSSTTEWLMSELMRNPEV... | Function: Involved in momilactone phytoalexins biosynthesis; acts as a multifunctional diterpene oxidase. Participates in the biosynthetic steps between 9-beta-pimara-7,15-diene and 3-beta-hydroxy-9-beta-pimara-7,15-dien-19,6-beta-olide. Catalyzes also consecutive oxidations at C19 of syn-stemod-13(17)-ene.
Catalytic A... |
Q6DBW9 | MEKTLWTWTLLAVFSLLVVKGMSDGLDLADALGDDDDDEPTTKPPKADPGAGGAGGAAVKPTLKPVKPTVKEPAKPKPKQTGLDDFDLADALNPDNDIKGKGKDSGKGDKEVGGGSRDDGTPNSRGSQFSDDDLLDVGNDNSYKPDKGKGGKGGSSSNVGDLDPADDNNYDTMAETGTIAGIVSAVAMALVGAVSSYISYQKKKLCFSIQQSLNADMVKADAPDAVVAQEPQVQQTLLQPPNAEPPTEENAV | Function: May function as a homophilic adhesion molecule.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 26102
Sequence Length: 252
Subcellular Location: Cell membrane
|
Q8TCZ2 | MVAWRSAFLVCLAFSLATLVQRGSGDFDDFNLEDAVKETSSVKQPWDHTTTTTTNRPGTTRAPAKPPGSGLDLADALDDQDDGRRKPGIGGRERWNHVTTTTKRPVTTRAPANTLGNDFDLADALDDRNDRDDGRRKPIAGGGGFSDKDLEDIVGGGEYKPDKGKGDGRYGSNDDPGSGMVAEPGTIAGVASALAMALIGAVSSYISYQQKKFCFSIQQGLNADYVKGENLEAVVCEEPQVKYSTLHTQSAEPPPPPEPARI | Function: Plays a role in a late step of leukocyte extravasation helping cells to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1 (By similarity). Homophilic adhesion molecule, but these interactions may not be required for cell aggregation (By similarity).
PTM: O-glyc... |
Q8BIF0 | MVARLTAFLVCLVFSLATLVQRGYGDTDGFNLEDALKETSSVKQRWDHFSTTTRRPVTTRAPANPAERWDHVATTTTRRPGTTRAPSNPMELDGFDLEDALDDRNDLDGPKKPSAGEAGGWSDKDLEDIVEGGGYKPDKNKGGGGYGSNDDPGSGISTETGTIAGVASALAMALIGAVSSYISYQQKKFCFSIQQGLNADYVKGENLEAVVCEEPQVTYSKQETQSAEPPPPEPPRI | Function: Plays a role in a late step of leukocyte extravasation helping cells to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1. Homophilic adhesion molecule, but these interactions may not be required for cell aggregation.
PTM: O-glycosylated.
Location Topology: Sin... |
Q5RE35 | MVAWRSAFLVCLAFSLATLVQRGSGDFDDFNLKDAVKETSSVKQRWNHVTTTTKRPVTTRAPANTLGNDFDLADALDDRNDRDDGRRKPIAGGGGFSDKDLEDIVGGGEYKPDKGKGDGRYGSNDDPGSGMVAETGTIAGVASALAMALIGAVSSYISYQQKKFCFSIQHAAEGQEGLNADYVKGENLEAVVCEEPQVKYSALHTQSAEPPPSEPARI | Function: Plays a role in a late step of leukocyte extravasation helping cells to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1 (By similarity). Homophilic adhesion molecule, but these interactions may not be required for cell aggregation (By similarity).
PTM: O-glyc... |
Q8R1R5 | MVARLTTLLVCLVFSLATLVQRGYGDFDDFNLEDALKETSSVKQSHFSTTTRRTGTTRAPANPAERWDHMTTTTTKRPGTTRAPSNPLELDGFDLEDALDDRNDLDGPKKPSTGEGGGLSDKDLEDILGGGGYKPDKNKGGGGGYGSQDDPGSGAVTDPGTIAGLVSALAAALLGAVSGYLSYQHRKFCFSVQRGLDAAYVKGENLEAVVCEEPRVEAAMCEAPPVTDSTQHSQPTEPLAPERPRI | Function: Plays a role in a late step of leukocyte extravasation helping cells to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1 (By similarity). Homophilic adhesion molecule, but these interactions may not be required for cell aggregation (By similarity).
PTM: O-glyc... |
E9KBR8 | MISESLLLVFLIVFISASLLKLLFVRENKPKAHLKNPPSPPAIPIIGHLHLLKPLIHHSFRDLSLRYGPLLSLRIGSVKFIVASTPSLAQEFLKTNELTYSSRKMNMAINMVTYHNATFAFAPYDTYWKFMKKLSTTELLGNKTLGHFLPIRTREVHDIIQFLFHKSKAQESVNLTEALLSLSNNVISQMMLSIKSSGTDSQAEQARTLVREVTQIFGEFNVSDFLGFCKNLDLQGFRKRALDIHKRYDALLEKIISDREELRRKSKVDGCEDGDDEKVKDFLDILLDVAEQKECEVQLTRNHVKSLILDYFTAATDTTA... | Function: Functions as flavone synthase II (FNSII) that catalyzes the direct conversion of flavanones to flavones . In vitro, can convert liquiritigenin, naringenin and eriodictyol to 7,4'-dihydroxyflavone, apigenin and luteolin, respectively .
Catalytic Activity: a flavanone + O2 + reduced [NADPH--hemoprotein reductas... |
A0A517FNB9 | MEGLLLLLPTAIIALYLYISLIRRSRKKHNLPPGSDGWPFLGETFSYLKPHSAISIGRFMEDHISRYGKIYRSNLFGEPTIVSADAELNRFVLQNEGRLFECSYPRSIGGILGKWSMLVLVGDMHRDMRMISLNFMSAARLRTRLMPEVERQTLLVLRSWREGSTFSAQEEAKKFTFNLMAKHIMSMDPGEPETEMLRREYITFMKGVVSAPLNFPGTPYWKALKSRSSILAVIERKMEERIGRRDRGDGGVEDDDLLGWAMNQSNLLKEQILDLLLSLLFAGHETSSMALALAIYFLESCPEAVRDLRDEHLAISMSGK... | Function: Canonical brassinosteroid (BR)-biosynthetic enzyme capable of converting cholesterol to 22S-hydroxycholesterol via sterol-C22 hydroxylation.
Catalytic Activity: cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (22S)-22-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Locati... |
C7S340 | LPTLSHEAFGDIYLFEGELPNTLTTSNNNQLSLSKQHAKDGEQSLKWQYQPQATLTLNNIVNYQDDKNTATPLTFMMWIYNEKPQSSPLTLAFKQNNKIALSFNAELNFTGWRGIAVPFRDMQGSATGQLDQLVITAPNQAGTLFFDQIIMSVPLDNRWAVPDYQTPYVNNAVNTMVSKNWSALLMYDQMFQAHYPTLNFDTEFRDDQTEMASIYQRFEYYQGIRSDKKITPDMLDKHLALWEKLVLTQHADGSITGKALDHPNRQHFMKVEGVFSEGTQKALLDANMLRDVGKTLLQTAIYLRSDSLSATDRKKLEERY... | Function: Broad-specificity glycosaminoglycan lyase, which acts in an exolytic fashion, and preferentially degrades the tetra- and hexasaccharide derivatives of chondroitin sulfate and dermatan sulfate produced by the chondroitin sulfate ABC endolyase, to yield the respective disaccharides. To a lesser extent, is also ... |
Q9ESJ1 | MAAATATAGTAACSSSSSSRGGSTDAAATSGVQPPPPPPATAPPEPLRKPRMDPRRRQAALSFLTNISLDGRPPLQDHEWGGGEEGGGTKPGARARLSLLAAGCNAFSAPGTAAAPWTAGSGSSPCPLPPSLVPRVLGEPSQPPRSAPAVTGAQLQLPDGPGGAGQEELEEDDAFTNVQVPSASFLGSGTPGSTSGSRGRLNSFTQGILPIAFSRQNSQNYCALEQSGQGGSTSALEQLQRSRRRLISQRSSLETLEDIEENAPLRRCRTLSGSPRPKNFKKIHFIKNMRQHDTKNGRDLKLDGGRQSAGAMSLKEIIGL... | Function: Cyclin-dependent kinase binding protein. Enhances cyclin-dependent kinase tyrosine phosphorylation by nonreceptor tyrosine kinases, such as that of CDK5 by activated ABL1, which leads to increased CDK5 activity and is critical for neuronal development, and that of CDK2 by WEE1, which leads to decreased CDK2 a... |
P84783 | VRTPVTVQTKVDNIKXY | Function: Hydrolysis of carbamoyl and sulfocarbamoyl esters of paralytic shellfish toxins. Ester hydrolysis is unaffected by the presence or absence of a hydroxyl moiety at the N-1 postion of the substrate toxin but is significantly affected by the stereochemistry of sulfate esters at C-11 of the substrate toxin.
PTM: ... |
P38505 | MAEALFKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDADGNGEIDQNEFAKFYGSIQGQDLSDDKIGLKVLYKLMDVDGDGKLTKEEVTSFFKKHGIEKVAEQVMKADANGDGYITLEEFLEFSL | Function: Calcium-binding protein which probably acts as a calcium sensor and modulator, contributing to cellular Ca(2+)-mediated signaling . Activates endogenous kinase(s) in a Ca(2+)-dependent manner . Plays a role in regulating actin cytoskeleton dynamics . Regulates the association of actin filaments in a bundle bu... |
Q9NZU7 | MGGGDGAAFKRPGDGARLQRVLGLGSRREPRSLPAGGPAPRRTAPPPPGHASAGPAAMSSHIAKSESKTSLLKAAAAAASGGSRAPRHGPARDPGLPSRRLPGSCPATPQSSGDPSSRRPLCRPAPREEGARGSQRVLPQAHCRPREALPAAASRPSPSSPLPPARGRDGEERGLSPALGLRGSLRARGRGDSVPAAASEADPFLHRLRPMLSSAFGQDRSLRPEEIEELREAFREFDKDKDGYINCRDLGNCMRTMGYMPTEMELIELSQQINMNLGGHVDFDDFVELMGPKLLAETADMIGVKELRDAFREFDTNGDG... | Function: Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling . Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels . Causes calcium-dependent facilitation and... |
O88751 | MSSHIAKSESKTSLLKAAAASGGSRAPRHSSARDPGLRGRRLPGPCPDSPATCGDPSSRRPLCRPVPRDEGARGSRRGLPQAHCRPRETLPPARGRDGEERGLAPALSLRGSLRSRGRGDPAPAGTPEADPFLHQLRPMLSSAFGQDRSLRPEEIEELREAFREFDKDKDGYINCRDLGNCMRTMGYMPTEMELIELSQQINMNLGGHVDFDDFVELMGPKLLAETADMIGVKELRDAFREFDTNGDGEISTSELREAMRKLLGHQVGHRDIEEIIRDVDLNGDGRVDFEEFVRMMSR | Function: Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling (By similarity). Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels . Causes calcium-dependent f... |
Q9NPB3 | MGNCAKRPWRRGPKDPLQWLGSPPRGSCPSPSSSPKEQGDPAPGVQGYSVLNSLVGPACIFLRPSIAATQLDRELRPEEIEELQVAFQEFDRDRDGYIGCRELGACMRTLGYMPTEMELIEISQQISGGKVDFEDFVELMGPKLLAETADMIGVRELRDAFREFDTNGDGRISVGELRAALKALLGERLSQREVDEILQDVDLNGDGLVDFEEFVRMMSR | Function: Required for sound encoding at inner hair cells (IHCs) synapses, likely via inhibition of the inactivation of voltage-gated calcium channel of type 1.3 (Cav1.3) in the IHCs . Required for the normal transfer of light signals through the retina (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.