ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P39205 | MESITFGVLTISDTCWQEPEKDTSGPILRQLIGETFANTQVIGNIVPDEKDIIQQELRKWIDREELRVILTTGGTGFAPRDVTPEATRQLLEKECPQLSMYITLESIKQTQYAALSRGLCGIAGNTLILNLPGSEKAVKECFQTISALLPHAVHLIGDDVSLVRKTHAEVQGSAQKSHICPHKTGTGTDSDRNSPYPMLPVQEVLSIIFNTVQKTANLNKILLEMNAPVNIPPFRASIKDGYAMKSTGFSGTKRVLGCIAAGDSPNSLPLAEDECYKINTGAPLPLEADCVVQVEDTKLLQLDKNGQESLVDILVEPQAG... | Function: Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.
Catalytic Activity: ATP + H(+) + molybdopterin = adenylyl-molybdopterin + diphosphate
Sequence Mass (Da): 6... |
A5Y5L5 | MNHHLIITPIFHLQIMLPVATLKRPPPPAATCSIYSFSRGTPSLVSKARLSTAAVGGMKNEPSPNHYSDISSSDLNLTRRSGNYGPTMWDFEYIQSIHNDYTEKKYMNRLNKLKEEMKKMIMAEGSQELEKLELIDNLQRLGVSYHFKHEIMQILSSIKQHSTPADSLYATALKFRLFREYGFHISQEIFGGLSETHTEDTKGMLYLYEASFLATEGESELEKARNWTEKHLREYLENKNDDQNVAELVHHALELPLHWRMLRIEARWFINFYKKKQDMIPLLLELAILDFNIVQAAHIEDLKYVARWWKETCLAENLPF... | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Monoterpene synthase involved in the biosynthesis of monoterpene natural products of the 'cineole cassette', volatile compounds present in floral scent . Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into 1,8-cineole and, as minor products, lim... |
P09948 | MTNGNNNNLEFAELKIRGKLFKLPILKASIGKDVIDISRVSAEADYFTYDPGFMSTASCQSTITYIDGDKGILWYRGYDIKDLAEKSDFLEVAYLMIYGELPSSDQYCNFTKKVAHHSLVNERLHYLFQTFCSSSHPMAIMLAAVGSLSAFYPDLLNFNETDYELTAIRMIAKIPTIAAMSYKYSIGQPFIYPDNSLDFTENFLHMMFATPCTKYKVNPIIKNALNKIFILHADHEQNASTSTVRIAGSSGANPFACISTGIASLWGPAHGGANEAVINMLKEIGSSENIPKYVAKAKDKNDPFRLMGFGHRVYKSYDPR... | Catalytic Activity: acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+)
Sequence Mass (Da): 49324
Sequence Length: 436
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.
EC: 2.3.3.16
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Q10306 | MMIILNAPRFMTNTRLASTRRLASSLLSQASLRSRQLNPLFTSSYSTRSSSLKDRLAELIPEKQAEIKKFRAEHGQDVIGEVTINQMYGGARGVRSLIWEGSVLDPNEGIRFRGYTIPECQKLLPSSPNGKQPLPESLFWLLVTGEIPTLSQVQALSADWAARSQLPKFVEELIDRCPPTLHPMAQFSLAVTALEHDSAFAKAYERGMNKHDYWKYEYEDCMDLIAKTVPIAGRIYRNLYRDGVVAPIQMDKDHSYNFANVLGFANNEEFVELMRLYLTIHADHEGGNVSAHTGHLVGSALSSPFLSMAASLNGLAGPLH... | Catalytic Activity: acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+)
Sequence Mass (Da): 54161
Sequence Length: 483
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.
Subcellular Location: Mitochondrion matrix
EC: 2.3.3.16
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P20903 | SDNSVVLRYGDGEYSYPVVD | Catalytic Activity: acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+)
Sequence Mass (Da): 2234
Sequence Length: 20
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.
EC: 2.3.3.16
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Q59939 | MAETNGLKDMIACDTRISAIKDNKLSYAGYDIADLMDNKARFEEVIYLLWNLHLPTAIELKQFEEKLRKNYAISDAIEQCILIQSRQHLHPMSVLRSTVSLLGVYNLKAEERSVEATYDQSIQLMAKIPTIIATFARLRQGLSPIAPRKDLGFAANFLYMLNGRLPSELEILAMNRALVLHAEHELNASTFAARVCASTLSDIYSCVTTAIGTLKGPLHGGANERVFDMLREIREYGDVDSYLQEKLNSKEKIMGFGHRVYQTQDPREKYLREMARELTKGTEHDIWYQLSKKVEICMKQKKNLIPNVDFYSATVYHVLG... | Catalytic Activity: acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+)
Sequence Mass (Da): 42711
Sequence Length: 372
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.
EC: 2.3.3.16
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Q59977 | MNYMMTDNEVFKEGLAGVPAAKSRVSHVDGTDGILEYRGIRIEELAKSSSFIEVAYLLIWGKLPTQAEIEEFEYEIRTHRRIKYHIRDMMKCFPETGHPMDALQTSAAALGLFYARRALDDPKYIRAAVVRLLAKIPTMVAAFHMIREGNDPIQPNDKLDYASNFLYMLTEKEPDPFAAKVFDVCLTLHAEHTMNASTFSARVTASTLTDPYAVVASAVGTLAGPLHGGANEEVLNMLEEIGSVENVRPYVEKCLANKQRIMGFGHRVYKVKDPRAIILQDLAEQLFAKMGHDEYYEIAVELEKVVEEYVGQKGIYPNVD... | Catalytic Activity: acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+)
Sequence Mass (Da): 44831
Sequence Length: 397
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.
EC: 2.3.3.16
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Q4S5X1 | MSFLTVNRLASKLLNSKNATYFLVAARNASASTTNLKDVLADLIPKEQNRIKNFKQQYGKTNIGQITVDMVYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAAGGQEPLPEGLFWLLVTGQVPTEEQVNWVSKEWAKRAALPSHVVTMLDNFPTNLHPMSQFSAAVTALNSESSFARAYSEGVHKSKYWEFAYEDSMDLIAKLPCIAAKIYRNLYREGSSIGAIDSGLDWSHNFTNMLGYSDAQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLAFSAAMNGLAGPLHGLANQEVLVWLTALQK... | Catalytic Activity: acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+)
Sequence Mass (Da): 52012
Sequence Length: 469
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.
Subcellular Location: Mitochondrion matrix
EC: 2.3.3.1
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P24118 | MRSINQLLKQASLSQKSQYNFSQTNLKKVIAEIIPQKQAELKEVKEKYGDKVVGQYTVKQVIGGMRGMKGLMSDLSRCDPYQGIIFRGYTIPQLKEFLPKADPKAADQANQEPLPEGIFWLLMTGQLPTHAQVDALKHEWQNRGTVNQDCVNFILNLPKDLHSMTMLSMALLYLQKDSKFAKLYDEGKISKKDYWEPFYEDSMDLIAKIPRVAAIIYRHKYRDSKLIDSDSKLDWAGNYAHMMGFEQHVVKECIRGYLSIHCDHEGGNVSAHTTHLVGSALSDPYLSYSAGVNGLAGPLHGLANQEVLKWLLQFIEEKGT... | Function: Structural protein involved in oral morphogenesis and in pronuclear behavior during conjugation. Respiratory enzyme.
Catalytic Activity: acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+)
Sequence Mass (Da): 52575
Sequence Length: 462
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate ... |
P21553 | MPETEEISKGLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIIASGAQDEEIQYLFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIRQLPRESDAVAMQMAAVAAMAASETKFKWNKDTDRDVAAEMIGRMSAITVNVYRHIMNMPAELPKPSDSYAESFLNAAFGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVEKWFNDNIINGKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEVHKVYEIATKLEDFGIKAFGSKGIYPNTDYF... | Catalytic Activity: acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+)
Sequence Mass (Da): 43072
Sequence Length: 385
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.
EC: 2.3.3.16
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B7LWM0 | MSDVITTDQPASATSLLQAKGIANLVERALLTEVRLTPKPGLVDIRNSGAHKDMDLALFEKSTLAVAPWMENFYQLGYDTSALEAELVLPMLRPIGMACEADMLQATGGVNTHRGAVFSFGLISAVTGRMVALEEELEQNRICYWVARMCRDLVAKELSSEATNAATSKSVEHFLHYGLSGARGEAESGFQTVRTVALPIFERIRAQNEDMNLALLQTLLHLMAWNNDTNLVSRGALKGLYYVQQQAQKMLWEGGVLMRGGLEALQAFDDELIARNLSPGGSADLLAVTWFLSHFPKGETFAD | Function: Catalyzes the formation of 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A, the precursor of the prosthetic group of the holo-acyl carrier protein (gamma chain) of citrate lyase, from ATP and dephospho-CoA.
Catalytic Activity: 3'-dephospho-CoA + ATP = 2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + ad... |
Q6D425 | MPTLRLPDGVLSAAVSRSVVSEYRERYSLLDIDQRVAHALTMEVMLTPKPGLVDRANNGSHRDMDVALFQTSIQAISPWFRHFTDAGYQHASVPLAQLLSQVRPIGIACEQAMLSATKGVNTHKGGIFAFGLLCTAAGWLTARGERVTQRSLCDSVAAMCHDLVRNELETCSGAATAGEHLYLRHGLTGARGEAASGFNTVCQHALPALQQAIAAGMDDETALLQTLLVLMAHNPDTNVVSRGGMDGLAFVQDYAQRLLAGPLDRQALIKMDEALIARNLSPGGSADLLALTWLLYHYPTE | Function: Catalyzes the formation of 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A, the precursor of the prosthetic group of the holo-acyl carrier protein (gamma chain) of citrate lyase, from ATP and dephospho-CoA.
Catalytic Activity: 3'-dephospho-CoA + ATP = 2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + ad... |
B9VVJ6 | MSVELRVGNRFRIGQKIGSGSFGEIFRGTNIQTGDPVAIKLEQVKTRHPQLAFEARFYRVLNAGGGVVGIPNVLYHGVEGEFNVMVIDLLGPSLEDLFSFCGRRLSLKTTLMLAEQMIARIEFVHSKSIIHRDIKPDNFLMGTGKKGHHVYIIDFGLAKKYRDARTHQHIPYKEGKSLTGTARYCSINTHIGIEQSRRDDLEGIGYILMYFLRGSLPWQGLKAHTKQEKYARISDRKQTTSVETLCRSFPAEFAAYLNYTRSLHFEDKPDYSYLKRLFRELFVREGYHVDYVFDWTLKRIHDTLQEGRADQQQQQQQQQQ... | Function: Serine/threonine protein kinase . May phosphorylate ZC3H11 during unstressed conditions, leading to proteasome-dependent degradation of ZC3H11 .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 38375
Sequence Length: 332
EC: 2.7.11.1
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Q9M9H6 | MAIKTKTSLIPSCSSPEDLKRVLQTLGSSWGDVVEDLERLEVVPLKGAMTNEVYQINWPTLNGEDVHRKVLVRIYGDGVDLFFNRGDEIKTFECMSHHGYGPKLLGRFSDGRLEEFIHARTLSADDLRVAETSDFIAAKLREFHKLDMPGPKNVLLWERLRTWLKEAKNLASPIEMDKYRLEGLENEINLLEERLTRDDQEIGFCHNDLQYGNVMIDEVTNAITIIDYEYSSFNPIAYDIANHFCEMAANYHSDTPHVLDYTLYPGEGERRRFISTYLGSTGNATSDKEVERLLKDAESYTLANHIFWGLWGIISGHVNK... | Function: Involved in phospholipid biosynthesis. Catalyzes the first step in phosphatidylcholine biosynthesis (By similarity).
Catalytic Activity: ATP + choline = ADP + H(+) + phosphocholine
Sequence Mass (Da): 40016
Sequence Length: 346
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphocholine... |
Q8L518 | MTMGGTEKNVENKQYRLPREVKEALQAIASEWEDVIDSKALQVIPLKGAMTNEVFQIKWPTREKGPSRKVLVRIYGEGVEIFFDREDEIRTFEFMSKHGHGPLLLGRFGNGRIEEFLHARTLSACDLRDPEISGRIATRMKEFHGLEMPGAKKALLWDRLRNWLTACKRLASPEEAKSFRLDVMEMEINMLEKSLFDNDENIGFCHNDLQYGNIMMDEETKAITIIDYEYSCYNPVAYDIANHFCEMAADYHTETPHIMDYSKYPGVEERQRFLKTYMSYSDEKPSDTMVKKLLEDVEKYTLASHLIWGLWGIISEHVNE... | Function: Involved in phospholipid biosynthesis. Catalyzes the first step in phosphatidylcholine biosynthesis (By similarity).
Catalytic Activity: ATP + choline = ADP + H(+) + phosphocholine
Sequence Mass (Da): 41017
Sequence Length: 350
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphocholine... |
Q9SZ92 | MAVGIFGLIPSSSPDELRKILQALSTKWGDVVEDFESLEVKPMKGAMTNEVFMVSWPRKETNLRCRKLLVRVYGEGVELFFNRDDEIRTFEYVARHGHGPTLLGRFAGGRVEEFIHARTLSATDLRDPNISALVASKLRRFHSIHIPGDRIMLIWDRMRTWVGQAKNLCSNEHSTEFGLDDIEDEINLLEQEVNNEQEIGFCHNDLQYGNIMIDEETNAITIIDYEYASYNPIAYDIANHFCEMAADYHSNTPHILDYTLYPGEEERRRFICNYLTSSGEEAREEDIEQLLDDIEKYTLASHLFWGLWGIISGYVNKIEF... | Function: Involved in phospholipid biosynthesis. Catalyzes the first step in phosphatidylcholine biosynthesis (By similarity).
Catalytic Activity: ATP + choline = ADP + H(+) + phosphocholine
Sequence Mass (Da): 40351
Sequence Length: 346
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphocholine... |
Q925N7 | MPSSAHLQDPPPLLSRTLTQNEGQTSLRQSSSCGPSAASASESLSGSTESRIPHSKMLQGKLPRNIPLEYPAGLYCCYVVIIVLSVAVVALSVALSVKKTAQISTINTYAACPRNWIGVGNKCFYFNEIPSNWTLSQTLCKEQGAELARFDTEEELNFLRRYKGSSGYWFGLHRESSAHPWKWTDNTEYNNSVSIGGDEKHGFLSDNGFSSGRGYIVRKSICRKPNSYTSQCL | Function: Lectin-type cell surface receptor.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 25686
Sequence Length: 233
Subcellular Location: Cell membrane
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O45824 | MAIFYDDPLERLNQPIKTKSYRKKQVVQRVHVFIFDNWKLILLGILNLIFLIIAIVFAILFFVGSADCAQLPDYTTSPASQLTTSAISSRTSEVQTNAITTTQGTPSNKTSTTTPSTSKVICASGFTLVGTKCGKLVSSNQPRTEADSICKGYGGSTLFSVRNEQETRDMLDFVKDSNIDFLWTGLVCNQTARTSCIWDVKSGTTADYNNFADGFPNVVYGYCIYFIVTGNSAGQWGSEQCSQLMNFVCELPTTIRDPDCKYNYNKNCYIRFDITLTIPQAQRFCNEKGADLVSIHSANENRFILTIYDIHGQILLGGLA... | Function: Involved in negative modulation of unc-40-mediated axon outgrowth . Required for proper presynaptic development in axons that have reached their targets . May function in concert with E3 ubiquitin-protein ligase rpm-1 in regulating axon outgrowth .
Location Topology: Single-pass type II membrane protein
Seque... |
P42916 | MLPLPLSILLLLTQSQSFLGEEMDVYSEKTLTDPCTLVVCAPPADSLRGHDGRDGKEGPQGEKGDPGPPGMPGPAGREGPSGRQGSMGPPGTPGPKGEPGPEGGVGAPGMPGSPGPAGLKGERGTPGPGGAIGPQGPSGAMGPPGLKGDRGDPGEKGARGETSVLEVDTLRQRMRNLEGEVQRLQNIVTQYRKAVLFPDGQAVGEKIFKTAGAVKSYSDAEQLCREAKGQLASPRSSAENEAVTQLVRAKNKHAYLSMNDISKEGKFTYPTGGSLDYSNWAPGEPNNRAKDEGPENCLEIYSDGNWNDIECREERLVICE... | Function: Lectin that binds to various sugars: mannose = ManNAc > fucose > GlcNAc > glucose = maltose > galactose > lactose > GalNAc. Could play a role in immune defense.
PTM: Hydroxylated.
Sequence Mass (Da): 33616
Sequence Length: 321
Subcellular Location: Secreted
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Q9UHP7 | MHDSNNVEKDITPSELPANPGCLHSKEHSIKATLIWRLFFLIMFLTIIVCGMVAALSAIRANCHQEPSVCLQAACPESWIGFQRKCFYFSDDTKNWTSSQRFCDSQDADLAQVESFQELNFLLRYKGPSDHWIGLSREQGQPWKWINGTEWTRQFPILGAGECAYLNDKGASSARHYTERKWICSKSDIHV | Function: Receptor for KLRB1 that protects target cells against natural killer cell-mediated lysis . Inhibits osteoclast formation . Inhibits bone resorption . Modulates the release of interferon-gamma . Binds high molecular weight sulfated glycosaminoglycans .
PTM: N-glycosylated.
Location Topology: Single-pass type I... |
Q91V08 | MCVTKASLPMLSPTGSPQEVEVGKILQGKRHGTISPESCAKLYCYYGVIMVLTVAVIALSVALSATKTEQIPVNKTYAACPQNWIGVENKCFYFSEYPSNWTFAQAFCMAQEAQLARFDNQDELNFLMRYKANFDSWIGLHRESSEHPWKWTDNTEYNNTIPIRGEERFAYLNNNGISSTRIYSLRMWICSKLNSYSLHCQTPFFPS | Function: Receptor for KLRB1B that protects target cells against natural killer cell-mediated lysis . Inhibits osteoclast formation . Binds high molecular weight sulfated glycosaminoglycans .
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 23647
Sequence Length: 207
Subc... |
Q8VI21 | MNAQCLKKPEEGESSPGTGDKILQRNSLRAISPESSAKLYCCCGVIMVLTVAVVALSVALPATKTEQILINKTYAACPKNWIGVGNKCFYFSEYTSNWTFAQTFCMAQEAQLARFDNEKELNFLKRHMNSSHWIGLHRDSSEHPWRWTDNTEYNNTFLIQGDGECGFLSDNGISSSRDYIPRKWICSRSSNYMLQC | Function: Lectin-type cell surface receptor.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 22205
Sequence Length: 196
Subcellular Location: Cell membrane
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Q8C1T8 | MNAAKVETSSMGMLQRADLTAADCLQEGEMGKKIQGKCFRIISTVSPVKLYCCYGVIMVLTVAVIALSVALSVRNKIPAMEDREPCYTACPSGWIGFGSKCFYFSEDMGNWTFSQSSCVASNSHLALFHSLEELNFLKRYKGTSDHWIGLHRASTQHPWIWTDNTEYSNLVLTRGGGECGFLSDNGISSGRSYTHRKWICSKFVSSCKSRVGSVPRHV | Function: Lectin-type cell surface receptor.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 24162
Sequence Length: 218
Subcellular Location: Cell membrane
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Q9WVF9 | MPDCLETGEKLFVHNMNAQCVQKPEEGNGPLGTGGKIVQGKCFRIISTVSPVKLYCCYGVIMVLTVAVIALSVALSTKKTEQIIINKTYAACSKNWTGVGNKCFYFSGYPRNWTFAQAFCMAQEAQLARFDNEEELIFLKRFKGDFDCWIGLHRESSEHPWKWTNNTEYNNMNPILGVGRYAYLSSDRISSSRSYINRMWICSKLNNYNLHCQTPPV | Function: Inhibits osteoclast formation. Receptor for KLRB1F. Enhances T-cell activation. Plays a role in splenocyte activation, T-cell responses and IL-2 production.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 24671
Sequence Length: 217
Subcellular Location: Cell membrane
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O04209 | MSAFEDDSFVILNDDASESVPVSGSFDATDSFSAFDGSLQVEDSVDDVFAAPSSDYGAYSNGDGIFGSNGDHDGPILPPPSEMESDEGFALREWRRQNAIQLEEKEKREKELLKQIIEEADQYKEEFHKKIEVTCENNKAANREKEKLYLENQEKFYAESSKNYWKAIAELVPKEVPTIEKRRGKKEQQDPKKPTVSVIQGPKPGKPTDLTRMRQILVKLKHNPPSHLKLTSQPPSEEAAAPPKNVPETKPTEAVTAA | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28837
Sequence Length: 258
Subcellular Location: Cell membrane
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Q5Z402 | MATAFDSPTASPAASPFDDDSFLRFDAAAPAPAPADAFPPSPEPYAFRPDAPSPFGMPEANGSLHDDPFAAPDNDNGPVLPPPNQMGADEGFLLREWRRQNAILLEEKEKKEKEMRNQIILDAKEFKKAFVEKRKLNVETSKDQNREREKLYLANQEKFHAGADKQYWKAISELIPHEIANIEKRGAKKDKDKEKKPGIVVIQGPKPGKPTDMSRMRQILLKLKHTPPPHMKPPPPPAAATGKDGAAGKDGAKVAAAASKDASANGSVPEMEKAAAAAAPAAAATEPIAAA | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31290
Sequence Length: 291
Subcellular Location: Cytoplasmic vesicle membrane
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F4J5M9 | MSSTLSNEESGLGDSNRSTEVDGGDGGNFTAYESRFQSQRFDSSFSNFDSQPEKESDLPCGDSSPRPETQSPPSINSFDDTNDSILPPPSAMEKEEGFALREWRRLNALRLEEKEKEEKEMVQQILEAAEQYKAEFYSKRNVTIENNKKLNREKEKFFLENQEKFYAEADKNNWKAIAELIPREVPVIENRGNKKKTATITVIQGPKPGKPTDLSRMRQVLTKLKHNPPTHMKPKLPSPSGADPNVSVSEQVTVTEKL | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29183
Sequence Length: 258
Subcellular Location: Cytoplasmic vesicle membrane
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Q6Z3A8 | MSSFDSVAAVAGDGDADDDDVLPPAPFDPAADGAQGGLGALRRGHRFATSYSSFGTAASEDDLAGAGAGTDGGVGAGIPLGSSSNGGAAYGYGGSGDVMNGHVDQIGDVMGGGVVVGDGGGIDDDLFAGAGDGDDGPVLPPPEAMKEEGILRREWRRQNALMLEEKERKERERRGEIIAEADEFKRSFAEKRKLNGDTNRAQNRDREKLFLAKQEKFHGEAEKQYWKAIAEMVPHEIPGLEKRGKRREKQSAEANAKAKQPGVVVVQGTKPGKPTDLSRMRQVLMKLKQTPPPHMAPPPPQPAKDTGGDTDANKDGEAEK... | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37773
Sequence Length: 363
Subcellular Location: Cytoplasmic vesicle membrane
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P04975 | MADDFGFFSSSESGAPEAAEEDPAAAFLAQQESEIAGIENDEGFGAPAGSQGGLAQPGPASGASEDMGATVNGDVFQEANGPADGYAAIAQADRLTQEPESIRKWREEQRKRLQELDAASKVMEQEWREKAKKDLEEWNQRQSEQVEKNKINNRIADKAFYQQPDADIIGYVASEEAFVKESKEETPGTEWEKVAQLCDFNPKSSKQCKDVSRLRSVLMSLKQTPLSR | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25082
Sequence Length: 228
Subcellular Location: Cytoplasmic vesicle membrane
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Q86AZ6 | MSNNYKAGTAINGNDYLLLNIDGNKDCDTDNGFFSGKNFFGGNQTSITHRRHHKMTTKTDRELMSHFESLDFNAIDNIIHRKYTFEKKKYQKILKTLGKWVICTLIGVVVGLVCYCLKESVDQLQSLKLTQVKKFYSTESTIFIPFLVYLGFNLCYGLISGLLVCIFGPMSSSSGLPEVKGYLNGIRISKAFNLKTVLGKLVSLIFSFSSGLVLGPEGPMFHIGAGIGSSMSQFKSKTLKFHLKSFWIFQNDSDKRDFISCGAAAGIAAAFGAPIGGVLFCLEEGSSFWSRQLTWRTFFSCLIATMTANLFLQGFTQQIH... | Function: Voltage-gated chloride channel. Chloride channels may have several functions including the regulation of cell volume, membrane potential stabilization and signal transduction (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 91016
Sequence Length: 815
Subcellular Location: Me... |
Q8N6F1 | MANSGLQLLGYFLALGGWVGIIASTALPQWKQSSYAGDAIITAVGLYEGLWMSCASQSTGQVQCKLYDSLLALDGHIQSARALMVVAVLLGFVAMVLSVVGMKCTRVGDSNPIAKGRVAIAGGALFILAGLCTLTAVSWYATLVTQEFFNPSTPVNARYEFGPALFVGWASAGLAVLGGSFLCCTCPEPERPNSSPQPYRPGPSAAAREPVVKLPASAKGPLGV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23229
Sequence Length: 224
Subcellular Location: Cell junction
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Q9ET38 | MANSGLQLLGYFLALGGWVGIIASTALPQWKQSSYAGDAIITAVGLYEGLWMSCASQSTGQVQCKLYDSLLALDGHIQSARALMVVAVLLGFVAMVLSVVGMKCTRVGDSNPTAKSRVAISGGALFLLAGLCTLTAVSWYATLVTQEFFNPSTPVNARYEFGPALFVGWASAGLAMLGGSFLCCTCPEPERANSIPQPYRSGPSTAAREPVVKLPASVKGPLGV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23343
Sequence Length: 224
Subcellular Location: Cell junction
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Q6L708 | MANAGLQLLGFILAFLGWIGSIVSTALPQWKVYSYASDNIVTAQAIYEGLWMSCVSQSTGQIQCKVFDSLLNLNSTLQATRALMVIGILLGLIAIFVATVGMKCMKCMEDDEAQKMRMAVFGGVIFLISGLAILVATAWYGNRIVQEFYDPMTPVNARYEFGQALFIGWAAASLCLLGGALLCCSCPRKTTSYPTPRPYPKPAPSSGKDYV | Function: Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members play essential roles in the formation of impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family membe... |
O88551 | MANAGLQLLGFILASLGWIGSIVSTALPQWKIYSYAGDNIVTAQAIYEGLWMSCVSQSTGQIQCKVFDSLLNLNSTLQATRALMVIGILLGLIAIFVSTIGMKCMRCLEDDEVQKMWMAVIGGIIFLISGLATLVATAWYGNRIVQEFYDPLTPINARYEFGQALFTGWAAASLCLLGGVLLSCSCPRKTTSYPTPRPYPKPTPSSGKDYV | Function: Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members play essential roles in the formation of impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family membe... |
O14249 | MSQVKVAVRSEEAANSYTQTFGMSWRQWRQACSEEYAKQCEREVLHTVDFIRENEKDPERLVEVVDSKIYDNDGLVHEVCVSDKATGKANKRSIVYMHGYGAGLGFYFRNMDGLTKGVTKDFNSYFVDWLGMGNSSRPPFDIKGQTASEKVEETERFFTESLETWRIGHGIEKMILVGHSMGGYLSAVYAMQYPERVEKLLLVSPVAIPENPFASNDDAEVYNSVASSAVHAVMDEPPLSNVTNEVLQTQEETTGLEPSRPSKPKNPLPRFITFLWEQNVTPFSLLRLSGPLGPKLMSFWSSRRFSTLPPETFRALHNYC... | Function: Mitochondrial cardiolipin-specific phospholipase which deacylates de novo synthesized cardiolipin (CL). Part of the remodeling process of cardiolipin, which involves deacylation-reacylation of premature cardiolipin.
Catalytic Activity: a cardiolipin + H2O = 1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-g... |
P53264 | MFKSTLNSIIRRPLKGFQLLRGADSSNTRPQSPRASARDVTEKQILRTPSAPTAIPLREIIYRVPSLFPRPLEDSVKDFRDFIKNEDAFQTELLKTLPFYPTPSESKTARLIRTVVDDEGNYINEFCIRPRKTSVPEADLKHLVFIHGYGAGLGFFIKNFEDIPLLDNEWCIHAIDLPGYGFSSRPKFPFEYPRDNIHSVQDWFHERIHTWFSKRNLLNRPEKNIVMAHSLGSYLMALYLQKYKESPSFKKLILCSPAGVSYRDFNNTASEVEKWKPPPWWYVKLWDRNISPFTLVRNFRQLGSKITSGWSYRRFKHILN... | Function: Mitochondrial cardiolipin-specific phospholipase which deacylates de novo synthesized cardiolipin (CL). Part of the remodeling process of cardiolipin, which involves deacylation-reacylation of premature cardiolipin. Has a strong substrate preference for palmitic acid residues and generates monolysocardiolipin... |
P56880 | MASAGLQLLAFILALSGVSGVLTATLLPNWKVNVDVDSNIITAIVQLHGLWMDCTWYSTGMFSCALKHSILSLPIHVQAARATMVLACVLSALGICTSTVGMKCTRLGGDRETKSHASFAGGVCFMSAGISSLISTVWYTKEIIANFLDLTVPESNKHEPGGAIYIGFISAMLLFISGMIFCTSCIKRNPEARLDPPTQQPISNTQLENNSTHNLKDYV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23515
Sequence Length: 219
Subcellular Location: Cell junction
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Q8N7P3 | MALVFRTVAQLAGVSLSLLGWVLSCLTNYLPHWKNLNLDLNEMENWTMGLWQTCVIQEEVGMQCKDFDSFLALPAELRVSRILMFLSNGLGFLGLLVSGFGLDCLRIGESQRDLKRRLLILGGILSWASGVTALVPVSWVAHKTVQEFWDENVPDFVPRWEFGEALFLGWFAGLSLLLGGCLLHCAACSSHAPLASGHYAVAQTQDHHQELETRNTNLKH | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24509
Sequence Length: 220
Subcellular Location: Cell junction
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Q96B33 | MRTPVVMTLGMVLAPCGLLLNLTGTLAPGWRLVKGFLNQPVDVELYQGLWDMCREQSSRERECGQTDQWGYFEAQPVLVARALMVTSLAATVLGLLLASLGVRCWQDEPNFVLAGLSGVVLFVAGLLGLIPVSWYNHFLGDRDVLPAPASPVTVQVSYSLVLGYLGSCLLLLGGFSLALSFAPWCDERCRRRRKGPSAGPRRSSVSTIQVEWPEPDLAPAIKYYSDGQHRPPPAQHRKPKPKPKVGFPMPRPRPKAYTNSVDVLDGEGWESQDAPSCSTHPCDSSLPCDSDL | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31915
Sequence Length: 292
Subcellular Location: Cell junction
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Q9D7D7 | MRTPVVMTLGMVLTPCGLLLNLVSTLAPGWRLVKGFLDQPVDVVLYQGLWDICREQSSRERECGQPDEWNYFQTQPVQVARGLMITSLATTALGLLLASLGVRCWQDEPHYGLAGLSGVVFFVAGLFSLIPVSWYNHFLSDPDVLAAPSSPVTVQVSYSLVLGYLGSCLLLLGGFSLALSFAPWCEERCRRCRKAPPAGPRRSSISTVYVDWPEPALTPAIKYYSDGQHRPPPTAEHRDTSKLKVGFPMPRPPPKSYTNPMDVLEGEEKKTATSQGGSSSRSTRPCQNSLPCDSDL | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32461
Sequence Length: 296
Subcellular Location: Cell junction
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A6NM45 | MALIFRTAMQSVGLLLSLLGWILSIITTYLPHWKNLNLDLNEMENWTMGLWQTCVIQEEVGMQCKDFDSFLALPAELRVSRILMFLSNGLGFLGLLVSGFGLDCLRIGESQRDLKRRLLILGGILSWASGITALVPVSWVAHKTVQEFWDENVPDFVPRWEFGEALFLGWFAGLSLLLGGCLLNCAACSSHAPLALGHYAVAQMQTQCPYLEDGTADPQV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24421
Sequence Length: 220
Subcellular Location: Cell junction
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C9JDP6 | MAWSFRAKVQLGGLLLSLLGWVCSCVTTILPQWKTLNLELNEMETWIMGIWEVCVDREEVATVCKAFESFLSLPQELQVARILMVASHGLGLLGLLLCSFGSECFQFHRIRWVFKRRLGLLGRTLEASASATTLLPVSWVAHATIQDFWDDSIPDIIPRWEFGGALYLGWAAGIFLALGGLLLIFSACLGKEDVPFPLMAGPTVPLSCAPVEESDGSFHLMLRPRNLVI | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25394
Sequence Length: 229
Subcellular Location: Cell junction
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P57739 | MASLGLQLVGYILGLLGLLGTLVAMLLPSWKTSSYVGASIVTAVGFSKGLWMECATHSTGITQCDIYSTLLGLPADIQAAQAMMVTSSAISSLACIISVVGMRCTVFCQESRAKDRVAVAGGVFFILGGLLGFIPVAWNLHGILRDFYSPLVPDSMKFEIGEALYLGIISSLFSLIAGIILCFSCSSQRNRSNYYDAYQAQPLATRSSPRPGQPPKVKSEFNSYSLTGYV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
PTM: The disulfide bond is necessary for pore formation, but is not required for correct protein trafficking.
Location Topology: Multi-pass membrane protein
Sequence Mass ... |
P49761 | MPVLSARRRELADHAGSGRRSGPSPTARSGPHLSALRAQPARAAHLSGRGTYVRRDTAGGGPGQARPLGPPGTSLLGRGARRSGEGWCPGAFESGARAARPPSRVEPRLATAASREGAGLPRAEVAAGSGRGARSGEWGLAAAGAWETMHHCKRYRSPEPDPYLSYRWKRRRSYSREHEGRLRYPSRREPPPRRSRSRSHDRLPYQRRYRERRDSDTYRCEERSPSFGEDYYGPSRSRHRRRSRERGPYRTRKHAHHCHKRRTRSCSSASSRSQQSSKRSSRSVEDDKEGHLVCRIGDWLQERYEIVGNLGEGTFGKVVE... | Function: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistributio... |
O35492 | MPVLSARRKRLASTAGPRRGSGPSLAVRWVPPLGPEPSSDRGRAPMRPRGPTCSTTRRGAGRGPRLLPGPPGRDLHRCRPDPGGAGQSPRVCEFGARAVRPLGRVEPGPPTAASREGAVLPRAEARAGSGRGARSGEWGLAAAGAWETMHHCKRYRSPEPDPYLSYRWKRRRSYSREHEGRLRYPSRREPPPRRSRSRSHDRIPYQRRYREHRDSDTYRCEERSPSFGEDCYGSSRSRHRRRSRERAPYRTRKHAHHCHKRRTRSCSSASSRSQQSSKRSSRSVEDDKEGHLVCRIGDWLQERYEIVGNLGEGTFGKVVE... | Function: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistributio... |
Q9HAZ1 | MRHSKRTHCPDWDSRESWGHESYRGSHKRKRRSHSSTQENRHCKPHHQFKESDCHYLEARSLNERDYRDRRYVDEYRNDYCEGYVPRHYHRDIESGYRIHCSKSSVRSRRSSPKRKRNRHCSSHQSRSKSHRRKRSRSIEDDEEGHLICQSGDVLRARYEIVDTLGEGAFGKVVECIDHGMDGMHVAVKIVKNVGRYREAARSEIQVLEHLNSTDPNSVFRCVQMLEWFDHHGHVCIVFELLGLSTYDFIKENSFLPFQIDHIRQMAYQICQSINFLHHNKLTHTDLKPENILFVKSDYVVKYNSKMKRDERTLKNTDIK... | Function: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates SRSF1 an... |
P0DJL0 | FLVLLLVSLMCYAEIAEGSQPTECKYGRPCNSDRDCCWEYRCLSSGREYTCKQDPGP | Function: This recombinant peptide inhibits voltage-gated potassium channels mKv1.3/KCNA3 (IC(50)=1.70 uM), mKv1.1/KCNA1 (10 uM inhibits 40% of currents) and hKv1.2/KCNA2 (10 uM inhibits 42% of currents) . May also increase intracellular calcium release through the activation of nuclear inositol 1,4,5-trisphosphate rec... |
I1S104 | MLATPTLSNFDKPSLPSSEGGDPALAARLQPLYSRFLTDLDLQPEYRRHESEKLMEEVLKFAKSTGVPHDLNSHSYQSLMVGYTYADNCLPYHDIEVKVYVAIYTWLATICDDAEALGIIDDVQLFEQRFILGEEQPTVLLRAFADQLKLTYKLYHPLVANLILCSSLNLLTSTSLVARKGIKEKGDHPSKGGNYFAWYIRERDGVGEAYSWFTFPKRQFPNLDIPIEAIEDMTRFIAYLNDVLSFYKESLAGETHNYINHTAAYEGVDSDAALHKTAQDTIDCARRIESVLAGKGEYEKAWRLHASGYLQMHVQRGRYR... | Function: Terpene cyclase involved in the biosynthesis of culmorin, a tricyclic sesquiterpene diol reported to have antifungal activity and some phytotoxicity to wheat coleoptile tissue, contributing to Fusarium head blight disease (Probable). The terpene cyclase CLM1 is responsible for the cyclization of farnesyl dip... |
Q8TDQ1 | MPLLTLYLLLFWLSGYSIVTQITGPTTVNGLERGSLTVQCVYRSGWETYLKWWCRGAIWRDCKILVKTSGSEQEVKRDRVSIKDNQKNRTFTVTMEDLMKTDADTYWCGIEKTGNDLGVTVQVTIDPAPVTQEETSSSPTLTGHHLDNRHKLLKLSVLLPLIFTILLLLLVAASLLAWRMMKYQQKAAGMSPEQVLQPLEGDLCYADLTLQLAGTSPQKATTKLSSAQVDQVEVEYVTMASLPKEDISYASLTLGAEDQEPTYCNMGHLSSHLPGRGPEEPTEYSTISRP | Function: Acts as an inhibitory receptor for myeloid cells and mast cells . Positively regulates the phagocytosis of apoptotic cells (efferocytosis) via phosphatidylserine (PS) recognition; recognizes and binds PS as a ligand which is expressed on the surface of apoptotic cells. Plays an important role in the maintenan... |
Q6SJQ7 | MHLSLLVPFLFWITGCCTAEDPVTGPEEVSGQEQGSLTVQCRYTSGWKDYKKYWCQGVPQRSCKTLVETDASEQLVKKNRVSIRDNQRDFIFTVTMEDLRMSDAGIYWCGITKGGLDPMFKVTVNIGPAIQVPITVPTMPPITSTTTIFTVTTTVKETSMFPTLTSYYSDNGHGGGDSGGGEDGVGDGFLDLSVLLPVISAVLLLLLLVASLFAWRMVRRQKKAAGPPSEQAQSLEGDLCYADLSLKQPRTSPGSSWKKGSSMSSSGKDHQEEVEYVTMAPFPREEVSYAALTLAGLGQEPTYGNTGCPITHVPRTGLEE... | Function: Acts as an inhibitory receptor for myeloid cells and mast cells . Positively regulates the phagocytosis of apoptotic cells (efferocytosis) via phosphatidylserine (PS) recognition; recognizes and binds PS as a ligand which is expressed on the surface of apoptotic cells . Plays an important role in the maintena... |
A0A098D1J7 | MLLIIVVLVGTLIYFLSFHNKKRHGLPPGPKPLPIIGNIKDMPPKGVAAFRHWLKHKDTYGPVSSVSVLGQPLILIHDREAAHYLFDKSSGKSSGRPSANFGGRLCGFDQILSLQQYGDTFKRHRKLVHRQMGTRAGAAKFRQIQDVESHRFLLRSLDNPGNLMEHIRKEAGGVILKATYGYSIEPHKPDPLVHLVEFMVEGISIVVVPMKFVVDFLPWLEYIPECLPGMSFKARARRWRTILNNTIEAPYQFVRQQMAKGIQFESYVSSLLTQEKLKGGNDTLDETYEADIKRTAAIMYAGGADTTVSTIQSFVLAMMV... | Function: Cytochrome P450 monooxygenase involved in the biosynthesis of culmorin, a tricyclic sesquiterpene diol reported to have antifungal activity and some phytotoxicity to wheat coleoptile tissue, contributing to Fusarium head blight disease . The terpene cyclase CLM1 is responsible for the cyclization of farnesyl ... |
Q496F6 | MWLLPALLLLCLSGCLSLKGPGSVTGTAGDSLTVWCQYESMYKGYNKYWCRGQYDTSCESIVETKGEEKVERNGRVSIRDHPEALAFTVTMQNLNEDDAGSYWCKIQTVWVLDSWSRDPSDLVRVYVSPAITTPRRTTHPATPPIFLVVNPGRNLSTGEVLTQNSGFRLSSPHFLLVVLLKLPLLLSMLGAVFWVNRPQWAPPGR | Function: Probably acts as an activating receptor.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 22918
Sequence Length: 205
Subcellular Location: Cell membrane
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Q831Y7 | MNIEKMTTTLQEAIAEAQKVAVTRQHQEIDIAHLWKIFLQPNHFGRNFYTDAGLDVDAFEREVDNALDEYPSVAGGNVQYGQNLSQNLFHLLQEADSLREEFQDEFLSTEIVLLALMKLKNYRLTKYLMQQGITEKELRKNIEEMRGGDRVTSQNQEEQYKALEKYGVDLVQQVKAGKQDPIIGRDEEIRDVIRILSRKTKNNPVLIGEPGVGKTAIVEGLAQRIVRKDVPENLKDKTIFSLDMGALIAGAKFRGEFEERLKAVLKEVKKSDGKIILFIDEIHNIVGAGKTEGSMDAGNLLKPMLARGELHLIGATTLDE... | Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein... |
Q8RHQ8 | MNPNQFTENTISAINLAVDISKGNMQQSIKPEALALGLLMQNNGLIPRVIEKMGLNLQYIISELEKEMNNYPKVEVKVSNENISLDQKTNSILNRAEKIMNEMEDSFLSVEHIFKAMIEEMPIFKRFGISLEKYMEVLMNIRGNRKVDNQNPEATYEVLEKYAKDLVELAREGKIDPIIGRDSEIRRAIQIISRRTKNDPILIGEPGVGKTAIVEGLAQRILNGDVPESLKNKKIFSLDMGALVAGAKYKGEFEERMKGVLKEVEESNGNIILFIDEIHTIVGAGKGEGSLDAGNMLKPMLARGELRVIGATTIDEYRKY... | Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein... |
P71404 | MNLFEKMTDQLHETLDSALALALHHKNAEVTPMHMLFAMLNNSQGILIQALQKMPVDIQALRLSVQSELNKFAKVSQISKQNIQLNQALIQSLENAQGLMAKRGDSFIATDVYLLANMGLFESVLKPYLDAKELQKTLESLRKGRTIQDKNDDSNLESLEKFGIDLTQKALENKLDPVIGRDEEIIRMMQILIRKTKNNPILLGEPGVGKTAVVEGLAQRIMNKEVPKTLLNKRVIALDLSLLVAGAKYRGEFEERLKKVIEEVKKSANVILFIDEIHTIVGAGASEGGMDAANILKPALARGELHTIGATTLKEYRKYF... | Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein... |
Q9H078 | MLGSLVLRRKALAPRLLLRLLRSPTLRGHGGASGRNVTTGSLGEPQWLRVATGGRPGTSPALFSGRGAATGGRQGGRFDTKCLAAATWGRLPGPEETLPGQDSWNGVPSRAGLGMCALAAALVVHCYSKSPSNKDAALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGDDFSSVYKTAKEQGIHSLEDGGQDGASRHITNQWTSALEFRRWLGLPAGVLITREDDFNNRLNNRASFKGCTALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYAREGEVMKLLRTSEA... | Function: Functions as a regulatory ATPase and participates in secretion/protein trafficking process. Has ATP-dependent protein disaggregase activity and is required to maintain the solubility of key mitochondrial proteins . Involved in mitochondrial-mediated antiviral innate immunity, activates RIG-I-mediated signal t... |
O68185 | MDIEKMTTTMQEALGSAQQIAQVRHHQVIEVPHLWRIFVQPNSFGANFYKDLGIDLDDFTNLIEKEIDKINSVEGSNITYGQNLSPDLFQVFTEADKIAQKMGDEYLSTEIILLALFELKQNPLTEYLVSHGLTKAKAQAAIEKLRGGDKVTSQNAEETYKALEKYGVDLVAQVKSGNQDPVIGRDEEIRDVIRVLSRKTKNNPVLIGEPGVGKTAIVEGLAQRIVRKDVPENLKDKTIFSLDMGALIAGAKYRGEFEERLKAVLNEVKKADGQIILFIDELHTIVGAGKTEGSMDAGNLLKPMLARGELHLIGATTLDE... | Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein... |
Q8F509 | MKLDKLTSKLNEAIYNAQASAEKLGNPEISEEHILKEVLSQPDGLVPLLISKLNLSPKSFLESTENALGKQPKVGGNTSADVGFSRSAVSLLKAADEVRKELKDEYLSTDHILLGLMKNGTGSLKTEFLKLGLEYHKLLKITLENRKGKTIMDDSPEGKTDALAKYAKNLNELAKQGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLANKIVQGEVPEGIKNKTLYTLDLGSMIAGAKYRGEFEDRLKALLDEVKSSDGEVILFIDEIHTLVGAGATEGALDASNMLKPMLARGELRCIGATTLKE... | Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein... |
Q8NN01 | MTVFMSDIRMAAQGGPGFGNDVFDRLLSERIIFLGSQVDDEIANKLCAQILLLSAEDPTRDISLYINSPGGSVTAGMAIYDTMKYSPCDIATYGMGLAASMGQFLLSGGTKGKRFALPHARIMMHQPSAGVGGTAADIAIQAEQFAATKREMAQLIAEHTGQTFEQISKDSDRDRWFTAQEAKDYGLVDHVITLAEGPISN | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q6A7E9 | MSHNTSIASQGMPAMAGPETGGAGMTDNVYQSLLRNRIVFLGSEVKDENANALCAQMLLLNAEDPEADIYLYINSPGGSVTGGMAIYDTMQWISNDVATVTMGMAASMGQFLLTAGTPGKRYALPHAKILMHQPLGGVGGTATEIAINAKMLKDTKRELSQLNADHSGHTLEQILEDSDRDHWFTAQEALEYGLIDHVYSNASQLRGDAPNQ | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q2JDQ8 | MRHEQARQAAAQPQGRYVLPNIIEKTSRGEYGMDPYSKLLKERIVFLGVQIDDVSANDVMAQLLFLESEDPDRDISIYINSPGGSFTSLTAIYDTMQFVRPDISTICMGQAASAAAVLLAAGTPGKRFALENSRILIHQPSAQGEGQSSDIEIQAREILRMRSLLERMLAVHTGKKEEDIRKDIERDKIFSADEAKEYGLIDEVIKTRKSSRLATAR | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q7NEW1 | MSELANYGPGAIRAAYSGDYGFRTPPPDLPSLLLNERIVYLGTPINDVVAELLIAQLLYLESEDNAKPIEIYINSPGVAGFETSAFAVYDTMRHVRMPIKTICLGLAGGFSALLMAAGTKGQRMSLPNSRIILYQPYGGARGQATDINIRAQELLTTKRTLNQLLSIHTGKTVEQIDKDTERLFYMSPQEAVSYGLIDKVLEPSANKLAKLKAVGAPV | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q5FQT4 | MHAGSGNDMDITRMTPTRLDDEPDAPEPETREDDNKTLNSPISELEGRLFDQRKVLIFGGINDKIARDVTGRLLALAGTSDKPIDVYVNSPGGHVESGDTIHDMIRFVDSIAPINMIGTGWVASAGALIYAAGRPERRVCLPNTRFLLHQPMGGVRGPATDIDIEAREIIKMRERLNRIFAKETGQTYEKVAKDTDRNYWMSANEAIAYGLVNRIIHSATELK | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q72R01 | MPETEKIAEVFEELTGSKISKNFLDHRKIFLWGPVTDESSKDLVGKLLYLEMKDPGKKITFYINSPGGVVTSGMTVFDTIKMISSPVHTVCMGMAASMGSVLLAAGTKGERSIWPNGKVMIHQPSIGGQIVAPATDLKIHAEEILKTKTKLNQILADACGHPISKLEEDTDRDYYMDAEEAIKYGIVDKLATKIDFN | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
P42380 | MPIGVPRIIYCWGEELPAQWTDIYNFIFRRRMVFLMQYLDDELCNQICGLLINIHMEDRSKELEKKEMEKSGLFKSGTAKTKGKDTVKKENLSGGASAKRQSVEDLLTSDNDFGIEENHLLEQYTLQKITTEWLNWNAQFFDYSDEPYLYYLADILSKDFSPNQDKDSANLNFAKSSANKQAFQNPAEMTKLIKNLKNLKNFSTGSKNVKQNLDVYSPFRLLANFAPQNYNLEHPNQNLAEIYSLLKTSTQNTNQPFTKKLIDNLSHKELMNRLQSPEKLVASSEKALGRRRLKQRYVQERLGSGGLSNSKALKAYNYLD... | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity).
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the ... |
Q7NUY9 | MKSMMEPQGLGLVPMVVEQSGRGERAYDIYSRLLKERIVFLVGPVTDESANLVVAQMLFLESENPDKDIHFYINSPGGSITAGMSIYDTMNFIKPDVSTLCIGQAASMGAFLLAAGTHGKRFALENSRVMIHQPLLYGGGLSGQVTDIEIHARELVKVKAKMNELLAKHSGQTLERVQSDTERDNFMSAEEARAYGMIDKVLSSRRDVTA | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q2G3T3 | MLDLFGASSAPTFGNQGKFTTDPVTGALIPVVVEQSSRGERSFDIYSRLLRERIIFVTGEVEDHMASVIIAQLLFLESENPSKDISMYINSPGGVVTAGLAIYDTMQYIRPRVSTVCIGQAASMGSFLLAAGEPGMRIALPNARIMIHQPSGGARGMASDIEIQAREILRIRKRMNDLYVKFTGRSLDEIEKAMDRDTFLEAEEAMKFGLVDKVFESRPATDSVGEGEGSGGAPA | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q9MTJ8 | MPIGMPKIPFLLDGDEEDEEEDDATWVDLYNVLYRTRSIFLGDAIHFEVANHIAGLMIFLTIQDATQNLYFFINSPGGLAVAGLLIYDTMQYVTPPVYTLGLGVLASMASFLLVGGETSKRLMGPNGRVMIHQPESDYTHKDQSLEVQLDSGEVEDIRKMVIRVYLERTRLPREVLNDHLERNYFMTATEAKYYGIVDDIGIQNLLARLRAESASQDNSLDPDAPDESASQDNSLDPDAPDETRPPKLR | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q0P3P4 | MPIGVPKVAYRLPGESTPQWVDLYNRLYRERVLFLGSGLDDELANQLNGIMLYLSAEDASRSLFLYINSPGGSVTAGLSVFDIMNYVQASVTTIGIGFAASMASFILAGGERGSRIALPHCRVMIHQPQGGMEGQASEVVLEKEEIVRLRRLIGRLYVDLTGQPLSTIANDLDRDKYLSAREAREYGLVDLVATTETATV | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
P54414 | MTTSAARKGLRTRGSACPRATRSASSISSRAQVIVAGPITDKLAQRTVAHLLALAEDSDEPINMLISSPGGHVESGDMIHDVIKFIRPTVRTIGLAWVASAGALIFVGADKENRYCLPNTRFLIHQPSVGIGGTSTDMMIQAEQVRLMRDRLNQIFAEATGQPVERIEKDTQRDFWLNTQEALDYGLLGKVIRSVDELK | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q9CJM2 | MSVIPMVVEQTARGERSYDIYSRLLKERVIFLGGEVEDRMANLIVAQLLFLESEDPEKDINIYINSPGGSVTAGMAIYDTMQFVKPDIRTLCVGQACSMGAFLLAGGTAGKRIALPSARVMIHQPLGGFRGQASDIQIHAQEILKIKQTLNERLAFHTGQTIERIERDTDRDNFMSAEEAKAYGLVDEVLASR | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q81V75 | MKKPIIQLLLIFTIVSIVPFLLNTSYISLYTFVGVLWSITIVGISFVIFIENRSPQSTLAWFLVLALLPVVGVLLYSIFGRSRWRRKKHLHRSEEQRKLFREILEGRRLELSLKVPLSERSVHLTEVVQKFGGGPAADRTTTKLLTNGDQTFSEILQAIEQAKHHIHIQYYIYKSDEIGTKVRDALIKKAKDGVIVRFLYDGLGSNTLRRRFLQPMKEAGIEIVEFDPIFSAWLLETVNYRNHRKIVIVDGEIGFTGGLNVGDEYLGRSKKFPVWRDSHLKVEGKALYKLQAIFLEDWLYASSGLNTYSWDPFMNRQYFP... | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
Location Topology: Multi-pass membrane protei... |
P45860 | MLKRRLEFFFLYMMLIGAYVIWFFPVSRLEFYGGLLCYISIILFSIYSLILENRTSQHTLLWIHILVFFPIVGYVFYLFSGQLYVKGKLFKTKRMYNREKLRKLFDKEETPEVTGLKDNQERFFTYSIRAAHMNINTKSNIKVLKNGEETFPDIFKAMRKAESYIHIEYYMFKSDMLGRGMMDIMMEKARQGVEVRFLYDAAGSMKLARRDIMRMKQAGVDIVPFSPLKYGFFNQKLNFRNHRKIVIIDGKTGFVGGLNVGKEYISRDPYIGFWRDTHLRLEGEIVQTLHAIFMLDWEYVSNEVLIDQEEYNTPVPVEGG... | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol (By similarity). May have a role in the heat shock response since the level of the transcript of ywiE increases after a heat shock.
Catalytic Ac... |
Q8CPD8 | MNFGFLGTILTILLVVGFITNVVLAFVIIFLERDRRTASSTWAWLFVLFVLPVIGFILYLFLGRTVSKKKMEKNNGDELNAFEDLVQDQIDSFDKHNYGYINDQVIKHRDLIRMLLMKQDAFLTENNKIDLFTDGHKLYEKVLEDIYNAQDYIHLEYYTFELDGLGKRILDALETKLKEGLEVKLLYDDVGSKKVRLSKFKHFRALGGEVEAFFPSKVPLINFRMNNRNHRKIIIIDGQIGYVGGFNVGDDYLGLGKLGYWRDTHTRVQGEGIDALQLRFILDWNSQSHRPQFKFDQKYFPKKIGDKGNAAIQIASSGPA... | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
Location Topology: Multi-pass membrane protei... |
P71040 | MSISSILLSLFFILNILLAIIVIFKERRDASASWAWLLVLFFIPVLGFILYLLFGHNLRRKHLFQWEDRKKIGIERLLKHQLEDLETKQFQFNNRATFDNKDLIYMLIMNNHAVFTEDNSVDVITDGRDKFQRLLSDISKAKDHIHLQYYIYKGDELGKKLRDALIQKAKEGVQVRVLYDELGSRTLRKKFFKELREAGGHVEVFFPSKLRPINLRLNYRNHRKLVIIDGMTGYVGGFNVGDEYLGLNPKFGYWRDTHIRLQGTAVHAIQTRFILDWNQASHHHTLTYIPNHFPDYGPKGNVGMQIVTSGPDSEWEQIKN... | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
Location Topology: Multi-pass membrane protei... |
P17698 | ISGKELQEMSTEGSKYVNKEIKNALKEVLQIKLVMEQGREQSSVMNVMPFPLLEPLNFHDVFQPFY | Function: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partia... |
P05482 | RDCCTPPKKCKDRRCKPLKCCA | Function: Mu-conotoxins block voltage-gated sodium channels (Nav). This toxin shows potent activity on Nav1.4/SCN4A (IC(50)=286 nM), and weak activity on mNav1.6/SCN8A.
Sequence Mass (Da): 2553
Sequence Length: 22
Domain: The cysteine framework is III (CC-C-C-CC). Classified in the M-4 branch, since 4 residues stand be... |
P0DPJ2 | CCAFPQWCGAGCIVPCC | PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 1761
Sequence Length: 17
Domain: The cysteine framework is III (CC-C-C-CC). Classified in the M-3 branch, since 3 residues stand between the fourth and the fifth cysteine residues.
Subcellular Location: Secreted
|
A0A7M4DUE8 | RGCCNGRGGCSSRWCRDHARCC | Function: Mu-conotoxins block voltage-gated sodium channels (Nav). This toxin potently inhibits hNav1.4/SCN4A (IC(50)=15.11 nM). It also displays lower activities on other human subtypes (Nav1.1/SCN1A; IC(50)=132 nM, Nav1.2/SCN2A; IC(50)=363.8, Nav1.3/SCN3A; IC(50)=89.4, Nav1.6/SCN3A; IC(50)=124.9, Nav1.7/SCN7A; IC(50)... |
P0DPJ3 | LCCPPQXCGPDCASPCC | PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 1708
Sequence Length: 17
Domain: The cysteine framework is III (CC-C-C-CC). Classified in the M-3 branch, since 3 residues stand between the fourth and the fifth cysteine residues.
Subcellular Location: Secreted
|
G3J454 | MECTTVKLSVALGEEVVQLSTLDQQAQRAYANLLLVFKLSQNADADHVFSSLKRGLGAALTEVPDFASLVVPVPGSKKNELQLRLGPDSGVPFKLVRQDALASHLEKHSSGGTYAELARDNFPLASVPTELLFNQLPASELACARGLPGLLAQASVVDGGLIMGLSWHHTVSDARGINTLLSSWARHTKMWAGQGTIGSPSAAPEPTRDRWRLTCGPRDVHVSHFSDYQINAAARTPLSPAAAHLLDRPDTTNATAGLSTWYFSKKALSSLRGELGRAAADGSDAVQFTSGEAVSALVWKHLSLARLLHQQLAHETSLFA... | Function: Acyltransferase; part of the gene cluster that mediates the biosynthesis of beauveriolides I and III, cyclodepsipeptides acting as inhibitors of the acyl-CoA:cholesterol acyltransferase . The HR-PKS cm3B initiates the biosynthesis of beauveriolides by iteratively catalyzing the formation of the linear polyket... |
A0A4Y7TJF3 | MIGASLAKKGQLTIVGSGIASISHLTLQAVSAIENADIVCYVVADGATEAFIRKKNPNSLDLYHLYGEDKQRTDTYIQMAEFMLIRVRQGQNVVGVFYGHPGVFVCPTHRALYIARSEGYKARMLPGLSAEDCLFADLGIDPSSVGCVTYEATDLLVFKRPINPASHLVLYQVGIVGKSNFKFDYTSDENIHFTKLLDRLEEAYGPEHSVTHYIAPLFPTEDPIAEEYTIAQLRLPEIRDKIHTISTFYVPPKTSESLIYDEVLLASLGVTHKPSVPYPWNPEATPYGPREKKAIELLAEHEPPKGYRPLKERSGLLAVL... | Function: Fusion protein of the methyltransferase cmiM and a type I borosin core peptide; part of the gene cluster that mediates the biosynthesis of a type I borosin, a highly methylated cyclic peptide with potent biological activities . Type I borosins derive from the C-terminus of the fusion protein, and it is the sa... |
A5EVQ4 | MNEFFRDDIFNRPQNVVDFRFDERTAAVFPDMIHRSIPAYASLLHMLGVIAGTYVQEGDHIYDLGCSLGGATLSLSRFIPKTAHITAVDSSPAMVQRFRAYVEGAALHHIEVLEADIIHLPLKSSRVIVMNFVLQFIPPPARDALIAKIYQALTEGGILLLAEKTQPEDDLLRTWHEAFKASQGYSALAIAQKREALENVMKIETETAERVRLQAAGFRRVLPYFQGMMFKAWVAIK | Function: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
Catalytic Activity: prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O
Sequence Mass (Da): 26674
Sequence Length: 237
EC: 2.1.3.-
|
A7ZMZ5 | MSHRDTLFSAPIARLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLAERFVQPGTQVYDLGCSLGAATLSVRRNIHHDNCKIIAIDNSPAMIERCRRHIDAYKAPTPVDVIEGDIRDIAIENASMVVLNFTLQFLEPSERQALLDKIYQGLNPGGALVLSEKFSFEDAKVGELLFNMHHDFKRANGYSELEISQKRSMLENVMLTDSVETHKARLHKAGFEHSELWFQCFNFGSLVALKAEDAA | Function: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
Catalytic Activity: prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O
Sequence Mass (Da): 27791
Sequence Length: 247
EC: 2.1.3.-
|
Q5HMV4 | MNYNPFQWTFKSEQTANEFNEHVEKSVPFYKEIHKIVKIIGGFFVEENTNVYDIGSSTGNLLKGMSNILKRNANYIGIDNSIYMNQVAMNDADSDNIKIISEDVQDFKFTNASYITSILTLQFINIEDREKTIKNVYQGLNKGGAFILVEKVNGEFVQSHEIMNQIYHDFKLENGLTYEEVIKKSQSIRGVLKPLTLKQNKRMLEKAGFKDIDTWFKWNNFVGIIAVK | Function: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
Catalytic Activity: prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O
Sequence Mass (Da): 26332
Sequence Length: 228
EC: 2.1.3.-
|
Q3A8E8 | MTKDSLFSRPQKPVPPFEFNASVVEVFDDMLNRSVPCYRELIHRQAQLAAHFYQPKTRIYDLGCSTGNLDLAICSAMDAARPFELVGVDNSEPMLKVCRERMRETPPEANISFACSDIRNLEMSNASVIILNLTLQFIPPADRQNILNRIFQALVPGGILLLTEKTVHAHAGLSELQQDFYYRFKAENGYSQMEISQKREALENVLIPETMESHRKRLDQAGFKAVDTWLKWFNFASFIALKEKS | Function: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
Catalytic Activity: prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O
Sequence Mass (Da): 27992
Sequence Length: 245
EC: 2.1.3.-
|
Q119M3 | MTEPLETELYLSSEKDELFEKGPWPKPFAFNAEVVKVFDNMVCRSVPLYREVVAGAVHWTRAYYQPKTRIIDIGCSTGTFLELLGRFLKQPAILVGIDNSSDMLDKAKEKLAQVEQIHQIELICESAENCSFEKSSVVVMNYTLQFLSLPQRQKLLRAIYQGLVPGGLLFISEKIRSDCPQFQETITHHYEAFKAKNGYAQNEIERKKEALENVLIPLSEAEQLQMLKQSGFSYIESLIKLHNFVSFVAFKSD | Function: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
Catalytic Activity: prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O
Sequence Mass (Da): 28924
Sequence Length: 253
EC: 2.1.3.-
|
Q7MJ72 | MNPKSNPDTIFSAPIDKIGDFTFDERVAEVFPDMIQRSVPGYSNIISAIGMLAERFVKPHSNVYDLGCSLGAATLSMRRHIKQEGCQIIAVDNSKAMVERCKLHVNAYRSDTPVNVIEADIRNIDIENASVVVLNFTLQFLSPEDRYVLLEKIYAGLRPGGILILSEKYVFEDQVSNELLIDLHHDFKRANGYSELEISQKRSAIENVMRPDSKKQHKERFAQIGFSSYDVWFQCFNFGSMFAIK | Function: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
Catalytic Activity: prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O
Sequence Mass (Da): 27835
Sequence Length: 245
EC: 2.1.3.-
|
P39660 | MNEFQPVNRRQFLFTLGATAASAILLKGCGNPPSSSGGGTSSTTQPTAAGASDLEVKTIKLGYIPIFEAAPLIIGREKGFFAKYGLDVEVSKQASWAAARDNVILGSAGGGIDGGQWQMPMPALLTEGAISNGQKVPMYVLACLSTQGNGIAVSNQLKAQNLGLKLAPNRDFILNYPQTSGRKFKASYTFPNANQDFWIRYWFAAGGIDPDKDIELLTVPSAETLQNMRNGTIDCFSTGDPWPSRIAKDDIGYQAALTGQMWPYHPEEFLALRADWVDKHPKATLALLMGLMEAQQWCDQKANRAEMAKILSGRNFFNVP... | Function: Part of the ABC transporter complex CmpABCD involved in bicarbonate transport. Binds bicarbonate with high affinity.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Location Topology: Peripheral membrane protein
Sequence Mass (Da... |
Q55106 | MVTARETRRNGSRPSGLKKWRQKLDGILLPLAGILGFLIIWQIFSSSGATRLPGPLSLFTEERTRELLLYPFLDRGGLDKGLFWQTIASLTRVAQGFSIAAIIGISVGILVGLNRQLNAMLDPLFQFLRMIAPLAWVPIALVAFQQNQPAAIFVIFITAVWPILINTAEGVRQIPQDYNNVARVLRMSKSKYLMKVVLPAALPYIFTGLRIAIGLSWLAIIAAEIVMSGIVGIGFFIWDAYQQNYVSDIILAVIYIGAVGLLLDRFVAWLQRWILRNM | Function: Part of the ABC transporter complex CmpABCD involved in bicarbonate transport. Probably responsible for the translocation of the substrate across the membrane (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31041
Sequence Length: 278
Subcellular Location: Cell inner membrane
|
Q55107 | MSLFVAVENIEKSFPLSGGNEYLALKGIDLEIKQGEFISLIGHSGCGKSTLLNLIAGLELPTDGAVSLEGQQITAPGPDRMVVFQNYSLFPWLTVRENIALAVDEVLRDLPKEERQAIVEEHIQLVGLGHAADKPPAQLSGGMKQRVAIARGLATRPKLLLLDEPFGALDALTRGNLQEKLMQICEENHVTAVMVTHDVDEAVLLSDRIVMLTNGPGSKIGGILEVDIPRPRKRMDVVHHPSYYSLRSEIIYFLNQQKRVKKLNARKVTTVARHGLEKVNLEIGYVPLMACAPLVVAQEKAFFAKHGLDEVSLVRETSWR... | Function: Part of the ABC transporter complex CmpABCD involved in bicarbonate transport. Responsible for energy coupling to the transport system (Probable).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 73492
Sequence Length: 663
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
|
O67085 | MEELKELRKEIDRIDEEILRLLNERAKLAKRIGEIKSKANLPIHVPEREREIFEKILRLNKEVYGGVFPQEALVHIYREIISACLSLEKKIKVAYLGPKATFTHQAALEFFGFSAHYTPCSTIRDVFVEVETKRADYGVVPVENTIEGVVNYTLDMFLESDVKIAGEIVIPITLHLLSASDSIENVEKVYSHKMALAQCRSWLEKNLPSVQVIEVESTAKACEIALEDERAGAVASEVAAYTYHLNILARNIQDSGDNFTRFLVIAKRDLKPTGSDKTSILFGVKDEPGALYKALEVFYKHGINLTKIESRPSKKKAWDY... | Function: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Catalytic Activity: chorismate = prephenate
Sequence Mass (Da): 41187
Sequence Length: 362
Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from pr... |
P57472 | MPANNSLLIFRDEINNIDKKIVKLLAERKNLVFKIAQSKIENNQAIRDIEREKKMLQKLIFLGKKYNLKSEYITQLFQLIIEESVATQKKLLKKFCNHNKLIPANFSFLGPKGSYSHIAAYKYADLNFQKCITNECSTFEEVVLSVENNQSDYAVLPIENTCSGSINEVFDILKKTNLFIIGEINIFINHNLLTLKKIELNKIKTIYSHPQPFQQCSDFIKKFPEWKIKYTKSTADAMKKIKKYNDVTNAALGSEIGSKIYGLEILMKNLANKENNITRFILLNRNPKKISKNIPTTTTLIFTTGQEAGSLSKVLSILQE... | Function: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Catalytic Activity: chorismate = prephenate
Sequence Mass (Da): 44338
Sequence Length: 385
Domain: The regulatory domain shows changes in the ESRP sequence, which is involved in... |
Q89AE5 | MTLKNALLAFRNAINILDKNLINLLAKRKQLSLNIAHTKVKNNYPVRDIEREQMLLKNLTILGEKHFLNKKYIESLFSIILEDSVLTQKKWIKKYNLNKYKLEKISFLGSFGSYSHLAAQKYAKKHSKILTDKIYKNFSDVITSVEQQQSTYAILPIENQSSGLIIEVYKLLQKTPLFIIGNIYIHANHCLLAKKYTPILKIQKIYSHIQPFKQCSKFISLFPNWKLSNTTSTSEAIQHVAKENDNTIAALGNESYGELNKLEVIAKNISNKRNNITQFIILAQKKTYITNKKTHLKTIILISKKNENCEKIIRNILHKN... | Function: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Catalytic Activity: chorismate = prephenate
Sequence Mass (Da): 43136
Sequence Length: 371
Domain: The regulatory domain shows changes in the ESRP sequence, which is involved in... |
P43900 | MALELSDIRQQITQIDRSLLKLLSERHRLAFDVVRSKEISQKSLRDVEREQQLLQELVQFAENENYQLEAQYITSIFQKIIEDSVLTQQVYLQNKLNEQRNQNLHIAFLGKRGSYSNLAARNYAARYQKQFVELGCQSFEQVFEKVQTGEADFGVLPLENTTSGAINEVYDLLQHTDLSLVGELAYPIKHCVLVNDKTDLNQIDTLYSHPQVIQQCSQFIHSLDRVHIEYCESSSHAMQLVASLNKPNIAALGNEDGGKLYGLSVLKTNIANQENNITRFIVVAKEPREVSSQIPTKTLLLMTTSQQAGALVDALLVFKK... | Function: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Catalytic Activity: chorismate = prephenate
Sequence Mass (Da): 44001
Sequence Length: 385
Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from pr... |
Q9ZHY3 | MSQTIDELLIPHRNAIDTIDAEILRLLNERAQHAHAIGELKGTGAVYRPEREVAVLRRIQDLNKGPLPDESVARLFREVMSECLAVERPLTIAYLGPQGTFTQQAAIKHFGHAAHTMACPTIDDCFKQVETRQADYLVAPVENSTEGSVGRTLDLLAVTALQACGEVVLRIHHNLLRKNNGSTEGIAKVFSHAQALAQCNDWLGRRLPNAERIAVSSNAEAARLVAESDDGTVAAIAGRTAAEIYGLDMVAECIEDEPNNTTRFLVMGHHETGASGSDKTSLAVSAPNRAGAVASLLQPLTESGISMTKFESRPSKSVLW... | Function: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Catalytic Activity: chorismate = prephenate
Sequence Mass (Da): 39354
Sequence Length: 362
Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from pr... |
Q9HZ67 | MADQDQLKALRLRIDSLDEKLLELISERARCAQDVARVKTQTLGEGEAPVFYRPEREAWVLKHIMQLNKGPLDNEEVARLFREIMSSCLALEQPLKVAYLGPEGTFTQAAALKHFGNAVISTPMAAIDEVFREVAAGAVNFGVVPVENSTEGAVNHTLDSFLEHDMVICGEVELRIHHHLLVGETTKTDNITRIYSHAQSLAQCRKWLDSHYPSVERVAVSSNADAAKRVKSEWNSAAIAGDMAASLYDLSKLHEKIEDRPDNSTRFLIIGNQEVPPTGDDKTSIIVSMRNKPGALHELLVPFHNNGIDLTRIETRPSRS... | Function: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Catalytic Activity: chorismate = prephenate
Sequence Mass (Da): 40632
Sequence Length: 365
Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from pr... |
P53996 | MSSNECFKCGRSGHWARECPTGGGRGRGMRSRGRGGFTSDRGFQFVSSSLPDICYRCGESGHLAKDCDLQEDEACYNCGRGGHIAKDCKEPKREREQCCYNCGKPGHLARDCDHADEQKCYSCGEFGHIQKDCTKVKCYRCGETGHVAINCSKTSEVNCYRCGESGHLARECTIEATA | Function: Single-stranded DNA-binding protein that preferentially binds to the sterol regulatory element (SRE) sequence 5'-GTGCGGTG-3', and thereby mediates transcriptional repression (By similarity). Has a role as transactivator of the Myc promoter . Binds single-stranded RNA in a sequence-specific manner (By similari... |
Q09KQ6 | MPDAVVFSPGGYRYIPAVFQYSAGIAAEPGFEIERVRFHRPVPLAEAFVAVESHLRAIGRPTTSFAQCELRSPDPFNDQGFIDFNTEYVKTLERWGIYKDRVNPVARTNVCPMYDKPTTPSMFAFSYTVPTTSAAKRPSFQLAGGGDARGGSAPYKDRIVAFGDTSPEGLREKVVFVIEEMESRLKTLGLGWADAVSTQLYTVQNIGHLVGPELARRGCGAGGLVWNYTRPPVIGLEYEMDVRGAVRETVL | Function: Involved in the biodegradation of xenobiotic compounds, such as nitrobenzene and 4-chloronitrobenzene (4-CNB) . CnbZ preferentially catalyzes the deamination of 2-amino-5-chloromuconate (2A5CM) to yield 2-hydroxy-5-chloromuconate (2H5CM). Also able to catalyze the deamination of 2-aminomuconate to yield 2-hyd... |
P22571 | MSDNTVLAPPTSNQGPTTPRKGPPKFKQRQTRQFKSKPPKKGVKGFGDDIPGMEGLGTDITVICPWEAFSHLELHELAQFGII | Function: Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones.
Catalytic Activity: 3',5'-cyclic GMP + H2O = GMP + H(+)
Sequence Mass (Da): 9102
Sequence Length: 83
Domain: The C-termin... |
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