ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
B7XIB8 | MILITSGAEAEIYESENMIIKRRVKKNYRIDELDSMLNKTRTKREVNIIKKLNALNIPSPMFYTTNKYDIVMEKIKGIPVKNILNNESLTSNQFLNKICAKTHKDILIEIGNIVYAMHNNNIIHGDLTTLNFIYSDKIHIIDFGLSFYSNKDEDKAVDLYLFEKSLISVHNEEFVSYFYSGYIVNETLNKKLLEIRKRGRKRE | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
Q9UYB9 | MKLIKQGAEAKIYLAEFSELYFDYPIKVIVKERIKKRYRIPEIDLKLRKERTIREARILRRAKEFGVNVPYVFEVDTKNMIIVMEYIEGERLKELLEKLPMEERLKVCREVGRQIGKLHEAGIVHGDLTTSNMILREGKVYFIDFGLAEFDDTIEAQGVDLHLLKRAMESTHYKWFERGFEEVLKGYIEIRGEDKGREIREKIREIELRGRYRERSWITQ | Function: Component of the KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 gr... |
Q9P7N1 | MSEKPDLRQRCSDIYREIKEKKLTVVKQGAEAITIKTEFYPGEVCLLKCRPAKRWRHPILDQKLSRKRCLVEARLLAKCHYVGIKCPMLYFIDANRGQIYMEWIDGPCVRDYIREICECEIEKKLIPLMKRIGSEVAKMHKNDIVHGDLTTSNMMLESHNNPVPIFIDFGLGSVSESEEDKAVDIYVLERALSSTLPESESLFHHVLDSYAQSWKQSKATLRRFEEVRMRGRKRTMIG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
Q6C2A3 | MITLPEQLEKLSKQENLIAQGAESLVYSAQHPYLPQQECIVKYRPKKPYRLPELDAQLSKHRTLAEARVLQKLALGDVEVPHLVFIDAKNGLIYMEKIEGLSVKQWIWNEEGDTEGGAQEAGDKSRSLPDGDVSSLKDTLVLVGQEIGKLHKSDIVHGDLTTSNVMLRDGKPVIIDFGLASVSTLAEDKAVDLYVMERAVLSTHPVHSQQYCDWLFEGYLAVVGKSQKEVMRKLEDVRQRGRKRSMLG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
P53323 | MTQEFIDKVSSYLTPDVDIAPISQGAEAIVFTTTTHPYLPRAKDSHQKYIIKYRPPKRYRHPQIDQALTKHRTLNESRLLAKLYLIPGLCVPQLIACDPYNGFIWLEFLGEDLPGGHGFSNLKNFLWMHDQDPYSDLVATTLRKVGRQIGLLHWNDYCHGDLTSSNIVLVRDGARWTPHLIDFGLGSVSNLVEDKGVDLYVLERAILSTHSKHAEKYNAWIMEGFEEVYREQGAKGAKKLKEVTKRFEEVRLRGRKRSMLG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
P0C2K6 | ADSRKPDDRYDMSGNDALGDVKLATYEDNPWETFK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM... |
Q84TC2 | MAPTTATKDDSGYGDERRRELQAFDDTKLGVKGLVDSGVKSIPSIFHHPPEALSDIISPAPLPSSPPSGAAIPVVDLSVTRREDLVEQVRHAAGTVGFFWLVNHGVAEELMGGMLRGVRQFNEGPVEAKQALYSRDLARNLRFASNFDLFKAAAADWRDTLFCEVAPNPPPREELPEPLRNVMLEYGAAVTKLARFVFELLSESLGMPSDHLYEMECMQNLNVVCQYYPPCPEPHRTVGVKRHTDPGFFTILLQDGMGGLQVRLGNNGQSGGCWVDIAPRPGALMVNIGDLLQLVTNDRFRSVEHRVPANKSSDTARVSV... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-dependent dioxygenase required for hydroxylation in position C-7 of the benzoxazinoids. Can use 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucoside (DIBOA-glucoside) as substrate, but not aglucone DIBOA.
Catalytic Activity: 2-oxoglutarate + DIBOA be... |
B1P123 | MGHQAQHGTDDTEELLAAHRQLWCHALGYVKSMALKCALDLRIPDTIDRCGGSATLGELLAASEISASNHDYLRRVMRTLTAMRIFAASHDPAKADDAAAISYQLTPASRLLVSSSSSVDDAAGASKENTTTPSILPNIAHLVRPNTISLLFSMGEWMKDESAASVSLYETVHRQGMWACVEDDAANRASFYESMDADTRLVMQAVVRRCPHVFDGIKSLVDVGGGRGTAAAAVVAAFPHIQRCTVMDLPHVVAEAPAGTAGLSFHGGDMFEHIPSADALMLKWILHDWDEDKCIKIMERCKEAIGGKEAGGKVIIIDTV... | Function: O-methyltransferase involved in the benzoxazinoid glucoside biosynthesis. Can use 2,4,7-trihydroxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucoside (TRIBOA-glucoside) as substrate, but not aglucone TRIBOA, caffeic acid, ferulic acid, apigenin or quercetin.
Catalytic Activity: S-adenosyl-L-methionine + TRIBOA beta-D-... |
B4G072 | MASSRTGAGAGGRVVVFPFPFQGHFNPVMRLARALHARGLAITVFHSGALDPADYPADYRFVPVTVEADPKLLASEDIAAIVTTLNASCDAPFRARLSALLAAEGRDSVRCVFTDVSWNAVLTASSDLGVPALGMMTASAASLRDYMAYRTLIDKGYLPVKEERKEDPVPELPPYLVKDLLRVDTSDLEEFAELLARTVTAARRASGLIFNTFPLIETDTLAEIHKALSVPVFAVAPLNKLVPTATASLHGVVQADRGCLQWLDTQQPGSVLYVSFGSMAAMDPHEFVELAWGLADSKRPFVWVVRPNLIRGFESGALPD... | Function: Glucosyltransferase involved in the last step of benzoxazinoid glucoside biosynthesis. Catalyzes the glucosylation of hydroxamic acids utilizing UDP-glucose as glucose doner, reducing the toxicity of these natural insecticides for storage. Can use DIMBOA and DIBOA as substrates, HMBOA (2-hydroxy-7-methoxy-2H-... |
Q07021 | MLPLLRCVPRVLGSSVAGLRAAAPASPFRQLLQPAPRLCTRPFGLLSVRAGSERRPGLLRPRGPCACGCGCGSLHTDGDKAFVDFLSDEIKEERKIQKHKTLPKMSGGWELELNGTEAKLVRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKVEEQEPELTSTPNFVVEVIKNDDGKKALVLDCHYPEDEVGQEDEAESDIFSIREVSFQSTGESEWKDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKSQ | Function: Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial recept... |
P02746 | MMMKIPWGSIPVLMLLLLLGLIDISQAQLSCTGPPAIPGIPGIPGTPGPDGQPGTPGIKGEKGLPGLAGDHGEFGEKGDPGIPGNPGKVGPKGPMGPKGGPGAPGAPGPKGESGDYKATQKIAFSATRTINVPLRRDQTIRFDHVITNMNNNYEPRSGKFTCKVPGLYYFTYHASSRGNLCVNLMRGRERAQKVVTFCDYAYNTFQVTTGGMVLKLEQGENVFLQATDKNSLLGMEGANSIFSGFLLFPDMEA | Function: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc... |
P31721 | MKTQWSEILTPLLLLLLGLLHVSWAQSSCTGSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGLAGDHGELGEKGDAGIPGIPGKVGPKGPVGPKGAPGPPGPRGPKGGSGDYKATQKVAFSALRTVNSALRPNQAIRFEKVITNVNDNYEPRSGKFTCKVPGLYYFTYHASSRGNLCVNIVRGRDRDRMQKVLTFCDYAQNTFQVTTGGVVLKLEQEEVVHLQATDKNSLLGVEGANSIFTGFLLFPDMDV | Function: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc... |
P02747 | MDVGPSSLPHLGLKLLLLLLLLPLRGQANTGCYGIPGMPGLPGAPGKDGYDGLPGPKGEPGIPAIPGIRGPKGQKGEPGLPGHPGKNGPMGPPGMPGVPGPMGIPGEPGEEGRYKQKFQSVFTVTRQTHQPPAPNSLIRFNAVLTNPQGDYDTSTGKFTCKVPGLYYFVYHASHTANLCVLLYRSGVKVVTFCGHTSKTNQVNSGGVLLRLQVGEEVWLAVNDYYDMVGIQGSDSVFSGFLLFPD | Function: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc... |
Q02105 | MVVGPSCQPPCGLCLLLLFLLALPLRSQASAGCYGIPGMPGMPGAPGKDGHDGLQGPKGEPGIPAVPGTRGPKGQKGEPGMPGHRGKNGPRGTSGLPGDPGPRGPPGEPGVEGRYKQKHQSVFTVTRQTTQYPEANALVRFNSVVTNPQGHYNPSTGKFTCEVPGLYYFVYYTSHTANLCVHLNLNLARVASFCDHMFNSKQVSSGGVLLRLQRGDEVWLSVNDYNGMVGIEGSNSVFSGFLLFPD | Function: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc... |
P31722 | MVVGTSCQPQHGLYLLLLLLALPLRSQANAGCYGIPGMPGLPGTPGKDGHDGLQGPKGEPGIPAIPGTQGPKGQKGEPGMPGHRGKNGPMGTSGSPGDPGPRGPPGEPGEEGRYKQKHQSVFTVTRQTAQYPAANGLVKFNSAITNPQGDYNTNTGKFTCKVPGLYYFVHHTSQTANLCVQLLLNNAKVTSFCDHMSNSKQVSSGGVLLRLQRGDEVWLAVNDYNGMVGTEGSDSVFSGFLLFPD | Function: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc... |
Q8CFR0 | MALGLLIAVPLLLQAAPPGAAHYEMLGTCRMICDPYSVAPAGGPAGAKAPPPGPSTAALEVMQDLSANPPPPFIQGPKGDPGRPGKPGPRGPPGEPGPPGPRGPPGEKGDSGRPGLPGLQLTTSAAGGVGVVSGGTGGGGDTEGEVTSALSAAFSGPKIAFYVGLKSPHEGYEVLKFDDVVTNLGNHYDPTTGKFSCQVRGIYFFTYHILMRGGDGTSMWADLCKNGQVRASAIAQDADQNYDYASNSVVLHLDSGDEVYVKLDGGKAHGGNNNKYSTFSGFLLYPD | Function: May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses.
PTM: Glycosylated, but not with N-linked glycans.
Sequence Mass (Da): 29292
Sequence Length: 287
Subcellular Location: Secreted
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Q9NPY3 | MATSMGLLLLLLLLLTQPGAGTGADTEAVVCVGTACYTAHSGKLSAAEAQNHCNQNGGNLATVKSKEEAQHVQRVLAQLLRREAALTARMSKFWIGLQREKGKCLDPSLPLKGFSWVGGGEDTPYSNWHKELRNSCISKRCVSLLLDLSQPLLPSRLPKWSEGPCGSPGSPGSNIEGFVCKFSFKGMCRPLALGGPGQVTYTTPFQTTSSSLEAVPFASAANVACGEGDKDETQSHYFLCKEKAPDVFDWGSSGPLCVSPKYGCNFNNGGCHQDCFEGGDGSFLCGCRPGFRLLDDLVTCASRNPCSSSPCRGGATCVLG... | Function: Receptor (or element of a larger receptor complex) for C1q, mannose-binding lectin (MBL2) and pulmonary surfactant protein A (SPA). May mediate the enhancement of phagocytosis in monocytes and macrophages upon interaction with soluble defense collagens. May play a role in intercellular adhesion.
PTM: N- and O... |
O89103 | MAISTGLFLLLGLLGQPWAGAAADSQAVVCEGTACYTAHWGKLSAAEAQHRCNENGGNLATVKSEEEARHVQQALTQLLKTKAPLEAKMGKFWIGLQREKGNCTYHDLPMRGFSWVGGGEDTAYSNWYKASKSSCIFKRCVSLILDLSLTPHPSHLPKWHESPCGTPEAPGNSIEGFLCKFNFKGMCRPLALGGPGRVTYTTPFQATTSSLEAVPFASVANVACGDEAKSETHYFLCNEKTPGIFHWGSSGPLCVSPKFGCSFNNGGCQQDCFEGGDGSFRCGCRPGFRLLDDLVTCASRNPCSSNPCTGGGMCHSVPLS... | Function: Receptor (or element of a larger receptor complex) for C1q, mannose-binding lectin (MBL2) and pulmonary surfactant protein A (SPA). May mediate the enhancement of phagocytosis in monocytes and macrophages upon interaction with soluble defense collagens. May play a role in intercellular adhesion. Marker for ea... |
O46051 | MYLELFAILLATALAWDYMRKRRHNKMYAEAGIRGPKSYPLVGNAPLLINESPKTIFDMQFRLIAEFGKNIKTQMLGESGFMTADSKMIEAIMSSQQTIQKNNLYSLLVNWLGDGLLISQGKKWFRRRKIITPAFHFKILEDFVEVFDQQSATMVQKLYDRADGKTVINMFPVACLCAMDIIAETAMGVKINAQLQPQFTYVQSVTTASAMLAERFMNPLQRLDFTMKLFYPKLLDKLNDAVKNMHDFTNSVITERRELLQKAIADGGDADAALLNDVGQKRRMALLDVLLKSTIDGAPLSNDDIREEVDTFMFEGHDTT... | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57481
Sequence Length: 507
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9VLZ7 | MWILLGIAVLIMTLVWDNSRKQWRVNTFEKSRILGPFTIPIVGNGLQALTLRPENFIQRFGDYFNKYGKTFRLWILGECLIYTKDLKYFESILSSSTLLKKAHLYRFLRDFLGDGLLLSTGNKWTSRRKVLAPAFHFKCLENFVEIMDRNSGIMVEKLKNYADGKTCVDLFKFVSLEALDVTTETAMGVQVNAQNEPNFPYTKALKSVVYIESKRLASVSMRYNWLFPLAAPLVYRRLQKDIAIMQDFTDKVIRERRAILERARADGTYKPLIMGDDDIGGKAKMTLLDILLQATIDNKPLSDVDIREEVDVFIFAGDDT... | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 58265
Sequence Length: 511
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9VYY4 | MEVLKKDAALGSPSSVFYFLLLPTLVLWYIYWRLSRAHLYRLAGRLPGPRGLPIVGHLFDVIGPASSVFRTVIRKSAPFEHIAKMWIGPKLVVFIYDPRDVELLLSSHVYIDKASEYKFFKPWLGDGLLISTGQKWRSHRKLIAPTFHLNVLKSFIELFNENSRNVVRKLRAEDGRTFDCHDYMSEATVEILLETAMGVSKKTQDKSGFEYAMAVMRMCDILHARHRSIFLRNEFVFTLTRYYKEQGRLLNIIHGLTTKVIRSKKAAFEQGTRGSLAQCELKAAALEREREQNGGVDQTPSTAGSDEKDREKDKEKASPV... | Function: Probably involved in steroid hormones biosynthesis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65380
Sequence Length: 574
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q28GG3 | MTEFLFCFSCCIGEQPQPKRRRRIDRSMIGEPMNFVHTAHVGSGDTNAGFAMGGSFQDQMKSKGGYTPGISEVAL | Function: Probably involved in the organization of the actin cytoskeleton by acting downstream of CDC42, inducing actin filament assembly.
Location Topology: Lipid-anchor
Sequence Mass (Da): 8218
Sequence Length: 75
Subcellular Location: Cytoplasm
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Q54PT3 | MFLTSILYTIIIILIFYKGLEYLIEKRSFPLVHPIKGVMNGTKPYFIFGDLPFQRLLNLKPKLKELGSIYFRWFFWYPIVEIKDINAIQYVYNEKSNNYSLYWNLNKSSNFILTGSEIKRFFRIYYCAFNCKDSLQRIMPVIKSQVFDFIHSHKFQNSTLSTNDDVTNFMLKLLSRVYLGSSDEAYHCFKANYKKFNKSYLDFFHYLFPTLLKIPSKFSRKYIKNKNKRALYQVLAMKAYYGVVKQSSDDHIEESMINIIAETSYNDKEGLSLEEIKMPSYLLNASSIKGPMIMVENLMFQLIEKSEIESKIRKEIKLVF... | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 76315
Sequence Length: 657
Subcellular Location: Membrane
EC: 1.14.-.-
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P35720 | MAALLLRHVGRHCLRAHLSPQLCIRNAVPLGTTAKEEMERFWSKNTTLNRPLSPHISIYGWSLPMAMSICHRGTGIALSAGVSLFGLSALLVPGSFESHLEFVKSLCLGPALIHTAKFALVFPLMYHTWNGIRHLMWDLGKGLTISQLHQSGVAVLVLTVLSSVGLAAM | Cofactor: The heme b is bound between the two transmembrane subunits SDHC and SDHD.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
... |
P41955 | MINIPTSILCRLGARSAISRSFGTSVVTKSEAKTPIQKFGWEYLKKQRDMKRPIAPHLTIYQPQLTWMLSGFHRISGCVMAGTLLVGGLGFAVLPLDFTTFVEYIRGWNLPCAVTAVFKYIIAFPIIFHTLNGIRFLGFDLAKGVDNIGQVYKSGWLVFGVSAVIALAIVINSCQNKSKAVKTA | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Mediates resista... |
P41956 | MINIPTAILCRLGARSSISRSFGTSIVTKSEAKTPIQKFGWEYLLKQRSKNRPIAPHLTVYQPQLTWMLSGFHRISGCVMAGTLLVGGIGFAVLPFDFTAFVDFIRSWNLPCAVTAVFKYIIAFPIIFHTLNGIRFLGFDLAKGVNNVGQIYKSGYLVSGLSAILALAIVFNSCQNKSNKTA | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) (By similarity). ... |
P48934 | MFIKFKISNRPIAPHLLVYTPQLSSLFSIWHRISGVGLAFFFTTFLIFIRIILSSNFACNLLTLISFEISQWIIIYFNLFILLFLFYHLFNGTRHIIWDFGFLLDIKYLSKFSLFLLVSLSLILIFQ | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topolog... |
P70097 | MAALLLRHVGRHCLRAHLNSQICLRNAVPLGTTAKEEMERFWNKNTSSKRPVSPHLTIYRWSLPMVMSICHRGTGVALSGGVSLFGLSALLLPGNFESYLMFIKSLCLGPALIHSAKFVLVFPLMYHSLNGIRHLIWDLGKGLSISQVYQSGVAVLMLAVLSSVGLAAM | Cofactor: The heme b is bound between the two transmembrane subunits SDHC and SDHD.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
... |
P48935 | MFYKNRPLSPYVTIYSSQWTSISSIFHRLSGLYLVFFLFVLFCSIKFLFCFSTFWFVYKFVKTCFFFILSFFIVFIVFSMYSLFYHFFIGLRHLVWDEVILMEDNFVTMSTKLSLSLSLVLVLINCLRYFLV | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topolog... |
Q8T2T5 | MFGRTLNTFTSRNAPLVRNFDKFIVNNTLTSKNIYLSQTNTTNTPLSYSTQAKKPFTITEKRIDELKTPYQPTSPHLTIYKFPLPAVMSIMHRATGICLALGITGLAGVTLFAPHDAIHYIQLLHTQYPALVYPAKFAVALPLTYHFCTGVRHIIWDETVKGLSISQIESSGKVLLAVVAVLSTIFTFVSFK | Cofactor: The heme b is bound between the two transmembrane cytochrome b560 subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q)... |
Q99643 | MAALLLRHVGRHCLRAHFSPQLCIRNAVPLGTTAKEEMERFWNKNIGSNRPLSPHITIYSWSLPMAMSICHRGTGIALSAGVSLFGMSALLLPGNFESYLELVKSLCLGPALIHTAKFALVFPLMYHTWNGIRHLMWDLGKGLKIPQLYQSGVVVLVLTVLSSMGLAAM | Cofactor: The heme b is bound between the two transmembrane subunits SDHC and SDHD.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
... |
P35721 | MKINRPLSPHLTIYKPQLTSTFSIFHRISGAFLATMVLFSILFFKIGDLSLTFYHFYQYFFFLTFYLNWFIISLVNFTLLALCYHMSNGVRHLLWDLGFFLELSKVYTSGIIMLFCAAFLALLNIIRQHWSNGQIPY | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topolog... |
O48958 | MATTATPQLLGGSVPQQWQTCLLVLLPVLLVSYYLLTSRSRNRSRSGKLGGAPRLPPGPAQLPILGNLHLLGPLPHKNLRELARRYGPVMQLRLGTVPTVVVSSAEAAREVLKVHDVDCCSRPASPGPKRLSYDLKNVGFAPYGEYWREMRKLFALELLSMRRVKAACYAREQEMDRLVADLDRAAASKASIVLNDHVFALTDGIIGTVAFGNIYASKQFAHKERFQHVLDDAMDMMASFSAEDFFPNAAGRLADRLSGFLARRERIFNELDVFFEKVIDQHMDPARPVPDNGGDLVDVLINLCKEHDGTLRFTRDHVKA... | Function: Catalyzes the conversion of p-hydroxyphenylacetaldoxime to p-hydroxymandelonitrile. The dehydration of the oxime to the corresponding nitrile is followed by a C-hydroxylation of the nitrile to produce p-hydroxymandelonitrile.
Catalytic Activity: (E)-4-hydroxyphenylacetaldehyde oxime + O2 + reduced [NADPH--hem... |
A0A3Q7HS74 | MDPFILYSLAFALVYISLYFIFKGNYSNNKHTNLPLGSNGWPILGENIDMAYSSSPEKFIHERMEKHSSQVFKTSLLGQKIAIFCGTSGNKFLFSNENKLLTTWWPPSLTKPLMCPTQSQSQNSVKEIALLNRGFLREILKPENLKQYIPFMDSMARDHLKQEWIPFKEVKIYPLVKKYTFSLACKLFLSIDDFRHVKKLSDPFVLVTSGMFTVPINLPGTPYNRAIKGGKMVHEELMKIIKERKINEKNNHSNDLLSQLISFSDENGQFMNDAEIYNNIIGLLVASYDTTSAAITFVLKYLAELPNIFNEVYKEQMEIA... | Function: Catalyzes the C-6 beta-hydroxylation of beta-amyrin to form daturadiol . Catalyzes the C-6 beta-hydroxylation of alpha-amyrin to form 6-beta-hydroxy-alpha-amyrin .
Catalytic Activity: beta-amyrin + O2 + reduced [NADPH--hemoprotein reductase] = daturadiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
... |
Q6XQ14 | MSVAILTSLPPQWLSILAVFLLPILTLLLFRGKDDNQKKGLKLPPGPRQLPLIGNLHQLGGQPYVDFWKMAKKYGPVMYLQLGRCPTVVLSSTETSKELMKDRDVECCSRPLSVGPGQLSYNFLDVAFSPYSDYWREMRKLFIFELLSMRRVQTFWYAREEQMDKMIEILDGAYPNPVNLTEKVFNMMDGIIGTIAFGRTTYAQQEFRDGFVKVLAATMDMLDNFHAENFFPVVGRFIDSLTGALAKRQRTFTDVDRYFEKVIEQHLDPNRPKPETEDIVDVLIGLMKDESTSFKITKDHVKAILMNVFVGGIDTSAVTI... | Function: Catalyzes the conversion of (E)-2-methylpropanal oxime (valox) to 2-hydroxy-2-methylpropanenitrile (acetone cyanohydrin) and of (E)-2-methylbutanal oxime (ilox) to 2-hydroxy-2-methylbutyronitrile. The reaction takes place in three steps. First, the oxime is isomerized to the (Z)- isomer, next the (Z)-isomer i... |
Q2QUC5 | MELTMASTMSLALLVLSAAYVLVALRRSRSSSSKPRRLPPSPPGWPVIGHLHLMSGMPHHALAELARTMRAPLFRMRLGSVPAVVISKPDLARAALTTNDAALASRPHLLSGQFLSFGCSDVTFAPAGPYHRMARRVVVSELLSARRVATYGAVRVKELRRLLAHLTKNTSPAKPVDLSECFLNLANDVLCRVAFGRRFPHGEGDKLGAVLAEAQDLFAGFTIGDFFPELEPVASTVTGLRRRLKKCLADLREACDVIVDEHISGNRQRIPGDRDEDFVDVLLRVQKSPDLEVPLTDDNLKALVLDMFVAGTDTTFATLE... | Function: Involved in serotonin biosynthesis. Catalyzes the conversion of tryptamine to serotonin . Accumulation of serotonin may play a role in innate immunity .
Catalytic Activity: O2 + reduced [NADPH--hemoprotein reductase] + tryptamine = H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + serotonin
Location Topo... |
W8JDE2 | MDQLMNFSLTSPIFLLLSSLFLIILLNKLMRGNKIQKGKKLPPGPKKIAIIGNLPSNGRFTSLIVFLNNLAEKYGPIMHLRIGQLSAVIISSAEKAKEILNTHGVRVADRPQTTVAKIMLYNSLGVTFAPYGDYLKQLRQIYAMELLSPKTVKSFWTIMDDELSTMITSIKSEVGQPMILHDKMMTYLYAMLCRATVGSVCNGRETLIMAAKETSALSASIRIEDLFPSVKILPVISGLKSKLTNLLKELDIVLEDIISAREKKLLSQPQQPLMLDEEDMLGVLLKYKNGKGNDTKFRVTNNDIKAIVFELILAGTLSSA... | Function: Involved in monoterpene indole alkaloids (MIAs) biosynthesis . Converts by aromatization the tetrahydro-beta-carboline alkaloids tetrahydroalstonine and ajmalicine to the corresponding beta-carboline alkaloids alstonine and serpentine, respectively .
Catalytic Activity: A + O2 + reduced [NADPH--hemoprotein re... |
A0A2Z5D854 | MDPAAIFLILAIPIASVYLLFYHKKRVNGLSSPPGPRGLPFIGHFYQIYKSECAHEYISNLSKQYGSLMTLHLGSVPALVVSSPKMAQEVLKTQDLVFCSRAQMTGSGKLSYNGLEMAFAPYGEHWRNVRKMCTLELFTQKRAQFNFRPVREDEVSRMVGRLSEAAAASEDVNAYECFTNFATSIISRVAFGKRYDEDNLGKEKFQRMVADIEAMFAAFFVSDFFPMFGWIDRLSGVKAVLDRNFNEMDTFYQELIDEHLKPDRPESLNGDLIDVMLKNKGSFLTMDSIKAILLNVFSGGIGTTGSALVFAMTALLRNQR... | Function: Involved in the biosynthesis of coumarins and furanocoumarins (FCs), natural products required for defense responses against attacks by predators with potential medical and agroindustrial usages such as anticoagulant, rodenticide and artificial vanilla substitutes . Catalyzes the conversion of psoralen into x... |
A0A1D6GQ67 | MEDKVLLAVAMVALIAVLSKLKSLLETKPKLNLPPGPWTLPLIGSIHHLVSSPLPYRAMRELAHKHGPLMMLWLGEVPTLVVSSPEAAQAITKTHDVTFADRHMNSTVDILTFNGNDIVFGTYGEQWRQLRKLSVLELLSVARVQSFQRIREEEVARFMRNLAASAGAGATVDLSKMISSFINDTFVRESIGSRCKHQDEYLDALHTGIRVAAELSVANLFPSSRLLQSLSTARRKAVAARDEMARILGQIIRETKEAMDWGDKASNESMISVLLRLQKEAGLPIELTDDIVMALMFDLFGAGSDTSSTTLTWCMTEMIR... | Function: Involved in the production of antifungal dolabralexin phytoalexins in response to biotic and abiotic stresses . Catalyzes the epoxidation of dolabradiene at C-16, followed by hydroxylation at C-3, to yield the epoxides 15,16-epoxydolabrene (epoxydolabrene) and 3b-hydroxy-15,16-epoxydolabrene (epoxydolabranol)... |
A3A871 | MEDKLILDLCLSALFVVVLSKLVSSAMKPRLNLPPGPWTLPLIGSLHHLVMTKSPQTHRSLRALSEKHGPIMQLWMGEVPAVVVSSPAVAEEVLKHQDLRFADRHLTATTEEVFFGGRDVIFGPYSERWRHLRKICMQELLTAARVRSFQGVREREVARLVRELAADAGAGGDAGVNLNERISKLANDIVMVSSVGGRCSHRDEFLDALEVAKKQITWLSVADLFPSSKLARMVAVAPRKGLASRKRMELVIRRIIQERKDQLMDDSAAGAGEAAAGKDCFLDVLLRLQKEGGTPVPVTDEIIVVLLFDMISGASETSPT... | Function: Enzyme of the diterpenoid metabolism involved in the biosynthesis of antibacterial oryzalides such as phytocassane.
Catalytic Activity: ent-isokaurene + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = ent-isokaurene-2beta,3beta-diol + 2 H(+) + 2 H2O + 2 oxidized [NADPH--hemoprotein reductase]
Location Topol... |
B8AV52 | MVGGELVLAALVILLALLLTLVLSHFLPLLLNPKAPKGSFGWPLLGETLRFLSPHASNTLGSFLEDHCSRYGRVFKSHLFCTPTIVSCDQELNHFILQNEERLFQCSYPRPIHGILGKSSMLVVLGEDHKRLRNLALALVTSTKLKPSYLGDIEKIALHIVGSWHGKSKDKGMVNVIAFCEEARKFAFSVIVKQVLGLSPEEPVTAMILEDFLAFMKGLISFPLYIPGTPYAKAVQARARISSTVKGIIEERRNAGSSNKGDFLDVLLSSNELSDEEKVSFVLDSLLGGYETTSLLISMVVYFLGQSAQDLELVKREHEG... | Function: Involved in brassinosteroid biosynthesis (By similarity). Involved in internode elongation and seed development (By similarity). Catalyzes the conversion of campesterol (CR) to (22S)-22-hydroxycampesterol (22-OHCR, 22-hydroxyCR) (By similarity).
Catalytic Activity: campesterol + O2 + reduced [NADPH--hemoprote... |
H1A988 | MDASSTPGAIWVVLTVILAAIPIWVCHMVNTLWLRPKRLERHLRAQGLHGDPYKLSLDNSKQTYMLKLQQEAQSKSIGLSKDDAAPRIFSLAHQTVHKYGKNSFAWEGTAPKVIITDPEQIKEVFNKIQDFPKPKLNPIAKYISIGLVQYEGDKWAKHRKIINPAFHLEKLKGMLPAFSHSCHEMISKWKGLLSSDGTCEVDVWPFLQNLTCDVISRTAFGSSYAEGAKIFELLKRQGYALMTARYARIPLWWLLPSTTKRRMKEIERGIRDSLEGIIRKREKALKSGKSTDDDLLGILLQSNHIENKGDENSKSAGMTT... | Function: Involved in the biosynthesis of Glycyrrhetinic acid (GA), a natural product which exhibits anti-inflammatory activity . Involved in the biosynthesis of the triterpenoid saponin glycyrrhizin . Catalyzes three sequential oxidation steps at C-30 of 11-oxo-beta-amyrin . Also able to catalyze C-30 monohydroxylatio... |
A0A481NR20 | MEISVASVTVSVVIAVVTWWVWRTLKWVWFQPKMLESYLRRQGLSGTPYTPLVGDLKRNSKMLTEAISKPIRLNDDITQRVVPYPLQMLKTYGRTHFTWLGPIPAITIMDPELIKEVFNRVYDFQKARLFPLARLIATGLVRYDGDKWAKHRKIINPAFHLEKLKNMVPAFHQCCSEVVGAWDKLVSDKRSSCEVDVWPGLVSMTADMISRTAFGSSYKEGQRIFELQEEIKELLIQSLGKAFIPGYHYLPTKGNRRMKAADREIKVILRGIVNKRLRAREAGEAPSEDLLGILLESNLGQAKGNGMSIEDVMEECKLFY... | Function: Catalyzes the oxidation of oleanolate at the C-23 position to form hederagenin.
Catalytic Activity: O2 + oleanolate + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + hederagenin + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58607
Sequence L... |
Q50EK6 | MADQISLLLVVFTAAVALLHLIYRWWNAQRGQKRTSNEKNQELHLPPGSTGWPLIGETYSYYRSMTSNRPRQFIDDREKRYDSDVFVSHLFGSQAVISSDPQFNKYVLQNEGRFFQAHYPKALKALIGDYGLLSVHGDLQRKLHGIAVNLLRFERLKFDFMEEIQNLVHSTLDRWVDKKEIALQNECHQMVLNLMAKQLLDLSPSKETNEICELFVDYTNAVIAIPIKIPGSTYAKGLKARELLIRKISNMIKERRDHPHIVHKDLLTKLLEEDSISDEIICDFILFLLFAGHETSSRAMTFAIKFLTTCPKALTQMKEE... | Function: Multifunctional and multisubstrate cytochrome P450 that oxidizes the respective carbon 18 of abietadienol, abietadienal, levopimaradienol, isopimara-7,15-dienol, isopimara-7,15-dienal, dehydroabietadienol, and dehydroabietadienal.
Catalytic Activity: abieta-7,13-dien-18-ol + 2 O2 + 2 reduced [NADPH--hemoprote... |
A0A517FNC5 | MAPVVILFFLFPTLLVLVVAVLGLRGGDDSWKKRGLKVPPGSMGWPLLGETIAFRRLHPCTSLGEYMEEHVNKYGKIYRSNLFGAPTIVSADAELNRFVLMNDERLFEPCFPKSVADILGHTSMLVLTGEMHRYMKSLSVNFMGIARLRNNFLGDSELYITQNFNRWKENIPFPAKEEACKVTFNLMVKNILSLNPGEPESEHLRKLYMSFMKGVVAIPLNLPGTAYKKAIQSRATILKMIEKLMEERIRNKKAGTDKIGEADLLGFILEQSNLDAEQFGDLLLGLLFGGHETSATAITLVIYFLYDCPKAVDHLREEHL... | Function: Involved in the biosynthesis of spiroketal steroid and saponin natural products from cholesterol such as diosgenin and analogs (e.g. furostanol and spirostanol), plant defense compounds used as main precursors for the industrial production of steroid hormones . During the 5,6-spiroketalization of cholesterol,... |
A0A1D6HSP4 | MELASTMSVAMALAAAIFVVLCSVVASARGRREKALKLPPGPRGWPVLGSLGALAGALPPHRALAALAARHGPLMHLRLGSYHTVVASSADAARLVLRTHDSALADRPDTAAGEITSYGYLGIVHTPRGAYWRMARRLCATELFSARRVESFQDVRAQEMRALARGLFGCAAGRRAVAVREHVAGATMRNILRMAVGEKWSGCYGSPEGEAFRRSLDEAFAATGAVSNVGEWVPWLGWLDVQGFKRKMKRLHDLHDHFYEKILVDHEERRRLAQASGGEFVATDLVDVLLQLSEESTKLESESEARLPRDGVKALIQDII... | Function: Involved in the biosynthesis of homoterpenes, attractants of herbivores parasitoids and predators (e.g. predatory mites and parasitoid wasps) (By similarity). Component of the volatile terpenes biosynthesis pathways . Converts mainly nerolidol to dimethylnonatriene (DMNT) and, to a lower extent, geranyllinalo... |
Q42798 | MAYQVLLICLVSTIVFAYILWRKQSKKNLPPSPKALPIIGHLHLVSPIPHQDFYKLSTRHGPIMQLFLGSVPCVVASTAEAAKEFLKTHEINFSNRPGQNVAVKGLAYDSQDFLFAFAPFGPYWKFMKKLCMSELLSGRMMDQFLPVRQQETKRFISRVFRKGVAGEAVDFGDELMTLSNNIVSRMTLSQKTSENDNQAEEMKKLVSNIAELMGKFNVSDFIWYLKPFDLQGFNRKIKETRDRFDVVVDGIIKQRQEERRKNKETGTAKQFKDMLDVLLDMHEDENAEIKLDKKNIKAFIMDIFVAGTDTSAVSIEWAMA... | Function: Cytochrome P450 involved in the biosynthesis of the phytoalexin glyceollin. Stereospecific for (6aR,11aR)-3,9-dihydroxypterocarpan.
Catalytic Activity: (6aR,11aR)-3,9-dihydroxypterocarpan + O2 + reduced [NADPH--hemoprotein reductase] = (6aS,11aS)-3,6a,9-trihydroxypterocarpan + H(+) + H2O + oxidized [NADPH--he... |
P93149 | MEPQLVAVSVLVSALICYFFFRPYFHRYGKNLPPSPFFRLPIIGHMHMLGPLLHQSFHNLSHRYGPLFSLNFGSVLCVVASTPHFAKQLLQTNELAFNCRIESTAVKKLTYESSLAFAPYGDYWRFIKKLSMNELLGSRSINNFQHLRAQETHQLLRLLSNRARAFEAVNITEELLKLTNNVISIMMVGEAEEARDVVRDVTEIFGEFNVSDFIWLFKKMDLQGFGKRIEDLFQRFDTLVERIISKREQTRKDRRRNGKKGEQGSGDGIRDFLDILLDCTEDENSEIKIQRVHIKALIMDFFTAGTDTTAISTEWALVEL... | Function: Catalyzes the formation of licodione and 2-hydroxynaringenin from (2S)-liquiritigenin and (2S)-naringenin, respectively . Can also convert eriodictyol to luteolin .
Catalytic Activity: (2S)-liquiritigenin + O2 + reduced [NADPH--hemoprotein reductase] = 2 H(+) + H2O + licodione + oxidized [NADPH--hemoprotein r... |
Q9SXS3 | MLVELAITLLVIALFIHLRPTLSAKSKSLRHLPNPPSPKPRLPFVGHLHLLDKPLLHYSLIDLSKRYGPLYSLYFGSMPTVVASTPELFKLFLQTHEASSFNTRFQTSAIRRLTYDNSVAMVPFGPYWKFIRKLIMNDLLNATTVNKLRPLRSQEIRKVLRVMAQSAESQVPLNVTEELLKWTNSTISRMMLGEAEEIRDIARDVLKIFGEYSLTDFIWPLKKLKVGQYEKRIDDIFNRFDPVIERVIKKRQEIRKKRKERNGEIEEGEQSVVFLDTLLDFAEDETMEIKITKEQIKGLVVDFFSAGTDSTAVATDWALS... | Function: 2-hydroxyisoflavanone synthase, which catalyzes the hydroxylation associated with 1,2-aryl migration of flavanones. Converts liquiritigenin and naringenin into highly unstable precursors of the isoflavones daidzein and genistein. Acts only on substrates with (2S)-chirality.
Catalytic Activity: (2S)-liquiritig... |
Q9XHC6 | MLDIKGYLVLFFLWFISTILIRSIFKKPQRLRLPPGPPISIPLLGHAPYLRSLLHQALYKLSLRYGPLIHVMIGSKHVVVASSAETAKQILKTSEEAFCNRPLMIASESLTYGAADYFFIPYGTYWRFLKKLCMTELLSGKTLEHFVRIRESEVEAFLKRMMEISGNGNYEVVMRKELITHTNNIITRMIMGKKSNAENDEVARLRKVVREVGELLGAFNLGDVIGFMRPLDLQGFGKKNMETHHKVDAMMEKVLREHEEARAKEDADSDRKKDLFDILLNLIEADGADNKLTRESAKAFALDMFIAGTNGPASVLEWSL... | Function: Heme-containing cytochrome P450 involved in the biosynthesis of soyasaponins. Hydroxylates specifically the C-24 methyl group of the triterpenes beta-amyrin and sophoradiol. No activity with lupeol, butyrospermol, tirucalla-7,21-dien-3beta-ol, taraxasterol, psi-taraxasterol, bauerenol, alpha-amyrin and multif... |
P0C8U3 | ITCCTRGTCAQHC | Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
Sequence Mass (Da): 1397
Sequence Length: 13
Domain: The cysteine framework is I (CC-C-C). Alpha4/3 pattern.
Subcellular Location: Secreted
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P0C8U5 | NGRCCHPACAKYFSCGR | Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
Sequence Mass (Da): 1873
Sequence Length: 17
Domain: The cysteine framework is I (CC-C-C). Alpha3/5 pattern.
Subcellular Location: Secreted
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P0DPM2 | IMYDCCSGSCSGYTGRC | Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
Sequence Mass (Da): 1806
Sequence Length: 17
Domain: The cysteine framework is I (CC-C-C). Alpha3/5 pattern.
Subcellular Location: Secreted
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P0C8U9 | MFTVFLLVILATTVVPFPSDRDPASNHENSKGSNRNAWLTPEECCAAPACREMILEFCLAGEAFAAALDGFRRLPYRLSSE | Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them (By similarity). Has possibly a distinct nAChR binding mode from other alpha-conotoxins, due to a different three residue motif (lacks the Ser-Xaa-Pro motif) (By similarity).
Sequen... |
P58782 | GCCGPYPNAACHPCGCKVGRPPYCDRPSGG | Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin binds with high affinity to both fetal (alpha-1/beta-1/epsilon/delta subunits) and adult (alpha-1/beta-1/gamma/delta subunits) mammalian muscle nicotinic acetylcholine r... |
P69746 | CCGVPNAACHPCVCKNTC | Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks the fetal muscle subtype (alpha-1/beta-1/gamma/delta subunits) (IC(50)=0.51 nM) with 600-fold greater affinity than the adult subtype (IC(50)=310 nM). It blocks t... |
P0C828 | MGMRMMFTVFLLVVLATTVVSTPSDRASDGRNAAVHERQKSLVPSVITTCCGYDPGTMCPPCRCTNSCG | Function: Neurotoxin with probable activity on sodium channel (Probable). Induces intense repetitive firing of the frog neuromuscular junction, leading to a tetanic contracture in muscle fiber (spastic paralysis) . In vivo, shows the same effect as the whole venom when injected on fish . Intraperitoneal injection into ... |
P0C1W8 | CCGVPNAACPPCVCNKTCG | Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks the fetal muscle subtype (alpha-1/beta-1/gamma/delta subunits) (IC(50)=66 nM) with 1500/2000-fold greater affinity than the adult (alpha-1/beta-1/epsilon/delta) s... |
P0DQY7 | APALVVTATTNCCGYTGPACHPCLCTQTC | Function: Probable neurotoxin with ion channel inhibitor activity.
PTM: O-linked glycans consist of Hex4-HexNAc2 hexasaccharides.
Sequence Mass (Da): 2900
Sequence Length: 29
Domain: The cysteine framework is IV (CC-C-C-C-C).
Subcellular Location: Secreted
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P0C2C5 | DCCGVKLEMCHPCLCDNSCKNYGK | Function: Probable neurotoxin with ion channel inhibitor activity (Probable). In vivo, elicits dose-dependently excitatory activity upon injection into fish. Its action is slowly reversible .
Sequence Mass (Da): 2664
Sequence Length: 24
Domain: The cysteine framework is IV (CC-C-C-C-C).
Subcellular Location: Secreted
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P27521 | MATVTTHASASIFRPCTSKPRFLTGSSGRLNRDLSFTSIGSSAKTSSFKVEAKKGEWLPGLASPDYLTGSLAGDNGFDPLGLAEDPENLKWFVQAELVNGRWAMLGVAGMLLPEVFTKIGIINVPEWYDAGKEQYFASSSTLFVIEFILFHYVEIRRWQDIKNPGSVNQDPIFKQYSLPKGEVGYPGGIFNPLNFAPTQEAKEKELANGRLAMLAFLGFVVQHNVTGKGPFENLLQHLSDPWHNTIVQTFN | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phos... |
P0DUR2 | GCCSHPPCNVNNPHICG | Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
Sequence Mass (Da): 1752
Sequence Length: 17
Domain: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
Subcellular Location: Secreted
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Q9ULX7 | MLFSALLLEVIWILAADGGQHWTYEGPHGQDHWPASYPECGNNAQSPIDIQTDSVTFDPDLPALQPHGYDQPGTEPLDLHNNGHTVQLSLPSTLYLGGLPRKYVAAQLHLHWGQKGSPGGSEHQINSEATFAELHIVHYDSDSYDSLSEAAERPQGLAVLGILIEVGETKNIAYEHILSHLHEVRHKDQKTSVPPFNLRELLPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSTEEEPSKLLVQNYRALQPLNQRMVFASFIQAGSSYTTGEMLSLGVGILVGCLCLLLAVYFIARKIRKKRL... | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 37668
Sequence Length: 337
Subcellular Location: Membrane
EC: 4.2.1.1
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Q9WVT6 | MLFFALLLKVTWILAADGGHHWTYEGPHGQDHWPTSYPECGGDAQSPINIQTDSVIFDPDLPAVQPHGYDQLGTEPLDLHNNGHTVQLSLPPTLHLGGLPRKYTAAQLHLHWGQRGSLEGSEHQINSEATAAELHVVHYDSQSYSSLSEAAQKPQGLAVLGILIEVGETENPAYDHILSRLHEIRYKDQKTSVPPFSVRELFPQQLEQFFRYNGSLTTPPCYQSVLWTVFNRRAQISMGQLEKLQETLSSTEEDPSEPLVQNYRVPQPLNQRTIFASFIQAGPLYTTGEMLGLGVGILAGCLCLLLAVYFIAQKIRKKRL... | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 37505
Sequence Length: 337
Subcellular Location: Membrane
EC: 4.2.1.1
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Q99N23 | MWALDFLLSFLLIQLAAQVDSSGTWCYDSQDPKCGPAHWKELAPACGGPTQSPINIDLRLVQRDYTLKPFIFQGYDSAPQDPWVLENDGHTVLLRVNSCQQNCPAIRGAGLPSPEYRLLQLHFHWGSPGHQGSEHSLDEKHGSMEMHMVHMNTKYQSMEDARSQPDGFAILAVLLVEEDRDNTNFSAIVSGLKNLSSPGVAVNLTSTFALASLLPSALRLLRYYRYSGSLTTPGCEPAVLWTVFENTVPIGHAQVVQFQAVLQTGPPGLHPRPLTSNFRPQQPLGGRRISASPEASVRSSVSTLPCLHLALVGLGVGLRL... | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 35482
Sequence Length: 324
Subcellular Location: Secreted
EC: 4.2.1.1
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P20507 | MARTGALLLVALALAGCAQACIYKFGTSPDSKATVSGDHWDHGLNGENWEGKDGAGNAWVCKTGRKQSPINVPQYQVLDGKGSKIANGLQTQWSYPDLMSNGTSVQVINNGHTIQVQWTYNYAGHATIAIPAMHNQTNRIVDVLEMRPNDAADRVTAVPTQFHFHSTSEHLLAGKIYPLELHIVHQVTEKLEACKGGCFSVTGILFQLDNGPDNELLEPIFANMPSREGTFSNLPAGTTIKLGELLPSDRDYVTYEGSLTTPPCSEGLLWHVMTQPQRISFGQWNRYRLAVGLKECNSTETAADAGHHHHHRRLLHNHAH... | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 41628
Sequence Length: 377
Subcellular Location: Periplasm
EC: 4.2.1.1
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P00917 | MAHSDWGYDSPNGPZEWVKLYPIANGNNQSPIDIKTSETKHDTSLKPFSVSYDPATAKEIVNVGHSFQVKFEDSDNRSVLKDGPLPGSYRLVQFHFHWGSTDDYGSEHTVDGVKYSAELHLVHWNSSKYSSFDEASSQADGLAILGVLMKVGEANPKLQKVLDALNEVKTKGKKAPFKNFDPSSLLPSSPDYWTYSGSLTHPPLYESVTWIVCKENISISSQQLSQFRSLLSNVEGGKAVPIQHNNRPPQPLKGRTVRAFF | Function: Catalyzes the reversible hydration of carbon dioxide. Can hydrate cyanamide to urea.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 29025
Sequence Length: 261
Subcellular Location: Cytoplasm
EC: 4.2.1.1
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P00915 | MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASF | Function: Catalyzes the reversible hydration of carbon dioxide . Can hydrate cyanamide to urea .
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 28870
Sequence Length: 261
Subcellular Location: Cytoplasm
EC: 4.2.1.1
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B3A0P2 | MKLQGAGCVVAAVLGALFIVNVESHFHKPELQLCKAFGEPCISYDVRSTIGPRCWFKLEFPREKCCNENGKRQSPIDIPDVKSIYKVPQKLRYSSRKFVGHLENTGIQPAFKRKVGADKVYLEGIGSPVGKRYFIENVHFHVGVRHKERQTENTLNGRSFDGEAHIVHIREDFGDLKEAANHPQGLLVISIFLSTSKGERRRDGFDDLIEMIQDVQEFEEEDGPCANVKIPDIFKFKQLIPFHPVWPICKKTFPVADDSDNSGSGVVCNFYLPNGLCGEKKESKINPNELLADDPEYYVFNGGLTTPPCSESVLWLVAKQ... | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 44718
Sequence Length: 395
Subcellular Location: Secreted
EC: 4.2.1.1
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Q8HY33 | MANLNWSYEGENGPEHWSKLYPIANGDNQSPIDIKTKEVKHDASLKPISVSYNPATAKEIVNVSHNFQVNFEDKDNQSVLKGGPFTGSFRLRQFHFHWGTADDHGSEHTVDGVKYSSELHIVHWNSEKYSSFSEAAEKPDGLAIIAVFIKAGQANPGLQKVIDALSSIKTKGKKAPFANFDPSLLIPQSSDYWSYHGSLTHPPLHESVTWIIYREPISASSEQLAKFRSLLSTAEGEKASSILHNHRLPQPLKGRQVKASFK | Function: Catalyzes the reversible hydration of carbon dioxide. Can hydrate cyanamide to urea.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 29175
Sequence Length: 262
Subcellular Location: Cytoplasm
EC: 4.2.1.1
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Q8XA34 | MDIIGGQHLRQMWDDLADVYGHKTALICESSGGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQFYPMYQQIQQEDATQLRHICLTDVALPADDGVSSFTQLKNQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATITECIPMMIRTLMVQPPSANDRQHRLREVMFYLNLSEQEKDTFCERFGVRLLTSYG... | Function: Catalyzes the transfer of CoA to carnitine, generating the initial carnitinyl-CoA needed for the CaiB reaction cycle. Also has activity toward crotonobetaine and gamma-butyrobetaine.
Catalytic Activity: 4-(trimethylamino)butanoate + ATP + CoA = 4-(trimethylamino)butanoyl-CoA + AMP + diphosphate
Sequence Mass ... |
P60977 | CISARYPCSNSKDCCSGNCGTFWTCFIRKDPCSKECLAP | Function: Causes paralysis to insect larvae (H.virescens). This toxin is active only on insects.
Sequence Mass (Da): 4296
Sequence Length: 39
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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A0A1V6PBC8 | MDEVTRTAQRSPSITETHAGETKLAGPGEKEGDVESPVDPSADSEQNRQQITGLQLFAILASVTLSAFLMLLDGSIIGVAIPNITSQFHSIDDIGWYTAAYQLASAALQPLSGKIYSSFSTKWTYLFFFGLFELGSLICGVANSSSMLIGGRAVAGLGSSGLLNGGMTIIAGAVPLEKRPVYTGIYLGISQLGIVCGPLIGGALTEYTTWRWCFYINLPVGAVTAILLLFLQVPELTEKPRFTFALVRRVIPELDLIGFTLFAPAAIMVLLALYYGGNDFPWDSSQVIGLFCGAGVTIIVFALWERRVGDRAMIPPSMVS... | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of calbistrin A and related compounds. Calbistrin A is a secondary metabolite with an interesting structure that was recently found to have bioactivity against leukemia cells. It consists of two polyketides linked by an ester bond: ... |
O86447 | MSILGLNGAPVGAEQLGSALDRMKKAHLEQGPANLELRLSRLDRAIAMLLENREAIADAVSADFGNRSREQTLLCDIAGSVASLKDSREHVAKWMEPEHHKAMFPGAEARVEFQPLGVVGVISPWNFPIVLAFGPLAGIFAAGNRAMLKPSELTPRTSALLAELIARYFDETELTTVLGDAEVGALFSAQPFDHLIFTGGTAVAKHIMRAAADNLVPVTLELGGKSPVIVSRSADMADVAQRVLTVKTFNAGQICLAPDYVLLPEESLDSFVAEATRFVAAMYPSLLDNPDYTSIINARNFDRLHRYLTDAQAKGGRVIE... | Function: Catalyzes the NAD(+)-dependent oxidation of coniferyl aldehyde to ferulic acid and which is induced during growth with eugenol as the carbon source.
Catalytic Activity: (E)-coniferaldehyde + H2O + NADP(+) = (E)-ferulate + 2 H(+) + NADPH
Sequence Mass (Da): 51987
Sequence Length: 481
EC: 1.2.1.68
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Q9NYX4 | MVKLGCSFSGKPGKDPGDQDGAAMDSVPLISPLDISQLQPPLPDQVVIKTQTEYQLSSPDQQNFPDLEGQRLNCSHPEEGRRLPTARMIAFAMALLGCVLIMYKAIWYDQFTCPDGFLLRHKICTPLTLEMYYTEMDPERHRSILAAIGAYPLSRKHGTETPAAWGDGYRAAKEERKGPTQAGAAAAATEPPGKPSAKAEKEAARKAAGSAAPPPAQ | Function: Interacts with clathrin light chain A and stimulates clathrin self-assembly and clathrin-mediated endocytosis.
PTM: Glycosylated.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23434
Sequence Length: 217
Subcellular Location: Cytoplasmic vesicle membrane
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P58821 | MVKLGCSFSGKPGKETGDQDGAAMDSVPLISPLDVSQLQPSFPDQVVIKTQTEYQLTSADQPKKFADLEGQRLACSHPEEGRRLPTARMIAFAMALLGCVLIMYKAIWYDQFTCPDGFLLRHKICTPLTLEMYYTEMDPERHRSILAAIGAYPLSRKHGTEMPAIWGNSYRAGKEEHKGTTPAAMTVSTAAAAAAAEGNEPSGKPLDMREKEDPQKAEDVPSQSPK | Function: Interacts with clathrin light chain A and stimulates clathrin self-assembly and clathrin-mediated endocytosis.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24718
Sequence Length: 226
Subcellular Location: Cytoplasmic vesicle membrane
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G5EGK5 | MSPRPEDDDLVIEPADDEGLHYGNASMEGTSTGQRPYIRLTSQLRNATKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAASVNTTSVLRVNNVPDAVKLSQKKGSHHSTKHIAFDEYEDYEMMDRGRLPDEEDADLYRVPDSAAGSNYAPVAVSERWLDGIKYRVGDCVQYRGEACRQYLSNKFVMMTNESREEMYDIDRNLRAAMLFINGAPTISQKCRQLSQAVACHHMYKVCESDSNNQIVSICKHDCDVIQNDECPSELALAAQHELVGDTPKALFPLC... | Cofactor: Can use both Mg(2+) and Mn(2+) in vitro and shows higher activity with Mn(2+) but Mg(2+) is likely to be the in vivo cofactor.
Function: Tyrosine-protein kinase receptor for Wnt ligands egl-20, mom-2 and cwn-1 . Involved in the final positioning of migrating ALM, CAN, BDU and HSN neurons during development . ... |
P16640 | MNANDNVVIVGTGLAGVEVAFGLRASGWEGNIRLVGDATVIPHHLPPLSKAYLAGKATAESLYLRTPDAYAAQNIQLLGGTQVTAINRDRQQVILSDGRALDYDRLVLATGGRPRPLPVASGAVGKANNFRYLRTLEDAECIRRQLIADNRLVVIGGGYIGLEVAATAIKANMHVTLLDTAARVLERVTAPPVSAFYEHLHREAGVDIRTGTQVCGFEMSTDQQKVTAVLCEDGTRLPADLVIAGIGLIPNCELASAAGLQVDNGIVINEHMQTSDPLIMAVGDCARFHSQLYDRWVRIESVPNALEQARKIAAILCGKV... | Function: The oxidation of camphor by cytochrome P450-CAM CamC requires the participation of the flavoprotein, putidaredoxin reductase CamA, and the iron-sulfur protein, putidaredoxin CamB, to mediate the transfer of electrons from NADH to P450 for oxygen activation.
Catalytic Activity: H(+) + NAD(+) + 2 reduced [2Fe-2... |
O80673 | MGICHGKPVEQQSKSLPVSGETNEAPTNSQPPAKSSGFPFYSPSPVPSLFKSSPSVSSSVSSTPLRIFKRPFPPPSPAKHIRAFLARRYGSVKPNEVSIPEGKECEIGLDKSFGFSKQFASHYEIDGEVGRGHFGYTCSAKGKKGSLKGQEVAVKVIPKSKMTTAIAIEDVSREVKMLRALTGHKNLVQFYDAFEDDENVYIVMELCKGGELLDKILQRGGKYSEDDAKKVMVQILSVVAYCHLQGVVHRDLKPENFLFSTKDETSPLKAIDFGLSDYVKPDERLNDIVGSAYYVAPEVLHRTYGTEADMWSIGVIAYIL... | Function: May play a role in signal transduction pathways that involve calcium as a second messenger (By similarity). Serine/threonine kinase that phosphorylates histone H3. Confers thermotolerance; involved in the heat-shock-mediated calmodulin-dependent signal transduction leading to the activation of heat-shock tran... |
Q9LJL9 | MGGCTSKPSSSVKPNPYAPKDAVLQNDDSTPAHPGKSPVRSSPAVKASPFFPFYTPSPARHRRNKSRDGGGGESKSVTSTPLRQLARAFHPPSPARHIRDVLRRRKEKKEAALPAARQQKEEEEREEVGLDKRFGFSKELQSRIELGEEIGRGHFGYTCSAKFKKGELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDERLNDIVGSAYYVAPEV... | Function: May play a role in signal transduction pathways that involve calcium as a second messenger.
PTM: Autophosphorylated.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 67207
Sequence Length: 599
Domain: There are 3 contigu... |
Q9ZUZ2 | MGQCYGKVNQSKQNGEEEANTTTYVVSGDGNQIQPLTPVNYGRAKNTPARSSNPSPWPSPFPHGSASPLPSGVSPSPARTSTPRRFFRRPFPPPSPAKHIKASLIKRLGVKPKEGPIPEERGTEPEQSLDKSFGYGKNFGAKYELGKEVGRGHFGHTCSGRGKKGDIKDHPIAVKIISKAKMTTAIAIEDVRREVKLLKSLSGHKYLIKYYDACEDANNVYIVMELCDGGELLDRILARGGKYPEDDAKAIVVQILTVVSFCHLQGVVHRDLKPENFLFTSSREDSDLKLIDFGLSDFIRPDERLNDIVGSAYYVAPEVL... | Function: May play a role in signal transduction pathways that involve calcium as a second messenger (By similarity). Serine/threonine kinase that phosphorylates histone H3 an GLN1-1.
PTM: Autophosphorylated.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[p... |
Q94AH1 | MRVLSEIAESPFVISRLSPDSTATGGFIGGWVGKCHGFLHNTVLVLASILFVAYLAYEAKKSLSKLSNRRSYIMIAYYGFLWLVSLLNLAWCCLQAWECTPGKEVIWNLLTLFTTSGMLFLEVSLVAFLFQGNYASGAEALTRTFLISGLVIGLDLLLKAIYLFGFGVPLFIDNNEHIHKFKWGLWVIHKLLLAGIYGMIFFMYNSKWRERLPARPAFYKYITVMLALNGLSLFACALTANGAHFGLWLYGITSVCYHAFYLPLLYVTFLADFFQEEDLNLENVYYSEMKDAGFFDADWE | Function: Plays a role in plants and microbes interactions . G-protein coupled melatonin receptor involved in root growth mediated by the bacterial quorum-sensing signals N-acyl-homoserine lactones (AHLs) . Binds to melatonin . Phytomelatonin receptor required, in collaboration with GPA1, for melatonin-mediated stomata... |
Q9LZ39 | MTILPFLAAVFVLQLLSTLTVAEIKSFTISNDSRPVILLEKFGIIEIGHVTVSVSSVSVLSPILDSSKLGFFVLSEESLPHVLLELQQNFSFCVLDSHYILHFFTFVDLSPPPRSQFSKSYPITSPNDYSLFFANCVPETRVSMKVHTEIYHDLYPNGSRDYLLAGSAQLPGLYLVFFLCYLSFLCFWLCFCWNHKQIVKRIHLLMTALLLVKSLTLICAAVYKHYVKVTGTAHGWNIVFYIFQFISVVLLFMVIVLIGNGWSFLKPKLHVKEKKLLVIVVPLQVLANIASIVIGETGPYTQDWVSWNQIFFLADITCCC... | Function: G-protein coupled receptor . Plays a role in plants and microbes interactions (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48883
Sequence Length: 428
Subcellular Location: Membrane
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F4JY11 | MAKMPLSVVVFLLFSAAFLAVSMAEIKSLVISDDARPMILFEKFGFTHTGHVTVSISSVSVVSTSSDPNPEASRLGFFLLSEESLLQVLLEIQQNPRFCVLDSHYVTHLFTFRDLSPPPNSRFNQSYPVTSPNEYSLFFANCVPETKVSMAVRTEMYNKDPNGSKDYLPAGSTQLPTLYSFFFLCYVAFLGFWSYTCWTNKQTVHRIHLLMAGLLLIKSLNLICAAEDKHYVKITGTPHGWDILFYIFQFIRVVLLFTVIILIGTGWSFLKPFLQEKEKNVLIIVIPLQVLANIASIVIGETGPFIKDWVTWNQVFLLVD... | Function: Plays a role in plants and microbes interactions . G-protein coupled receptor involved in root growth mediated by the bacterial quorum-sensing signals N-acyl-homoserine lactones (AHLs) .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50245
Sequence Length: 440
Subcellular Location: Membran... |
F4K2U8 | MRVLDEIAESPFLISPLNPNSTANGYRWVDKCHGFLHNTVLVAASLFFVAYLAYEAKKSLSKLSNRRSYIMIAYYGCLWLVSLLNLAWCCLQGWECTPGKEVVWNLLTLFTTSGMLFLEVSLVAFLFQGNYASGAEALTRTFLISGFIVALDLLLKAIFLFGFGVPLFIDNNENGKTFKWGLWIIHKLLLTGVYGMVFLMYNSRWREKLPARPAFYNYIIIMFALYSLYLVASAFTANNAHFGFWLYGIMSVCYHALYLPLLYITFLADFFQEEDLNLENVYYSEMKDAGFFDSDWE | Function: G-protein coupled receptor . Plays a role in plants and microbes interactions (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34138
Sequence Length: 297
Subcellular Location: Membrane
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P0DPE4 | MAILQIGAGGVGWVVAHKAAQNNDVLGDITIASRTVGKCEKIIESIQKKNNLKDSTKKLEARAVNADDVDSLVALIKEVQPDLVINAGPPWVNMSIMEACYQAKVSYLDTSVAVDLCSEGQQVPQAYDWQWGYREKFEEAGITGILGAGFDPGVVSVFAAYAVKHLFDEIDTIDVMDVNAGDHGKKFATNFDPETNMLEIQGDSFYWENGEWKQVPCHSRMLEFEFPNCGSHKVYSMAHDEVRSMQEFIPAKRIEFWMGFGDRYLNYFNVMRDIGLLSPDPLTLHDGTVVQPLHVLKALLPDPTSLAPGYTGLTCIGTWV... | Function: Involved in norspermidine biosynthesis. Catalyzes the synthesis of carboxynorspermidine from L-aspartate 4-semialdehyde and 1,3-diaminopropane. Is also slightly active with putrescine as a substrate.
Catalytic Activity: carboxynorspermidine + H2O + NADP(+) = H(+) + L-aspartate 4-semialdehyde + NADPH + propane... |
Q8WVQ1 | MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLCSHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQEENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSVDDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDVVNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPRRASQERYSEKDDERKGANLL... | Function: Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP . Involved in proteoglycan synthesis .
PTM: N-glycosylated.
Location Topolog... |
Q8VCF1 | MPIQPFDQREWNEPMHSLRISVGGLPVLASMTKATDPRFRPRWRVILTSFVGAALLWLLYSHHQGPVPGRPPTHNAHNWRLSQQRISHYNDTYPLSPPQRTPGGIRYRIAVIADLDTGSRAQEENTWFSYLKKGYLTLSDSGDRVSVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSVDDRTGVIYQIEGTKAVPWVILSDGDGTVEKGFKAEWLAVKDEHLYVGGLGKEWTTTTGEVMNENPEWVKVVGHRGSVDHENWVSSYNALRAAAGIRPPGYLIHESACWSDTLQRWFFLPRRASHERYSEKDDERKGSN... | Function: Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > IDP >> UTP > CDP = GTP = ITP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis.
Catalytic Activity: ... |
P00789 | MMPFGGIAARLQRDRLRAEGVGEHNNAVKYLNQDYEALKQECIESGTLFRDPQFPAGPTALGFKELGPYSSKTRGVEWKRPSELVDDPQFIVGGATRTDICQGALGDCWLLAAIGSLTLNEELLHRVVPHGQSFQEDYAGIFHFQIWQFGEWVDVVVDDLLPTKDGELLFVHSAECTEFWSALLEKAYAKLNGCYESLSGGSTTEGFEDFTGGVAEMYDLKRAPRNMGHIIRKALERGSLLGCSIDITSAFDMEAVTFKKLVKGHAYSVTAFKDVNYRGQQEQLIRIRNPWGQVEWTGAWSDGSSEWDNIDPSDREELQL... | Cofactor: Binds 3 Ca(2+) ions.
Function: Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.
PTM: The N-terminus is blocked.
Catalytic Activity: Broad endopeptidase specificity.
Sequence Mass (Da): 80352
Sequence Le... |
P43920 | MTQEYSTLRNNISMLGRFLGETINDAQGEDILELIENIRKLSRNSRAGDDKARQALLDTLGSISNENIIPVARAFSQFLNLTNIAEQYQTISREHSLAQSSSQSLSELFKRLKEQNASVEEVHKTVEKLLIELVLTAHPTETTRRSLIHKHIEINKCLSKLEHHDLTEKERNIIERLLLRLIAEAWHTNEIRTVRPTPFDEAKWGFAMLENSLWQAVPEFLRQLNETAREFLGYDLSVGLKPVRISSWMGGDRDGNPFVTAQITKKVLYFARWKAADLFLQDISKLADELSMMKCSDEFRDKYGEHLEPYRFVVKNLRNQ... | Function: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Mass (Da): 100055
Sequence Length: 879
EC: 4.1.1.31
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A1U2U4 | MTELHPDLRENVRLLGDLLGQSILRFPGQDCYDRIEEIRAAAKADRRQESGSGQRLVKLLGQLSDDELLPVTRAFNQFLNLANLAEQYHGIRRKQGHPSDLMVESLGEVFDRLKSGGIDPQELHRKVADLRIEFVLTAHPTEVARRTLILKYDEMSDCLSRLDHDDLMPGEREEIVDRLSLLIAEAWHTDEIRHERPTAVDEAKWGFAVIENSLWQALPKFLRSLDTSLSEATGQGLPLQVSPIRIASWMGGDRDGNPNVTHEVTREVFLLGRWMAADLYLRDIQALRAELSMWQASDELRAEVGDSREPYRQVLAQLRE... | Function: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Mass (Da): 99626
Sequence Length: 881
EC: 4.1.1.31
|
Q49136 | MTKTLHARPSAATDTTFAPPVITGTATEDALEILFHALLDVARRHDPELEDVLHGRADISSFTPEMLARALQVQGIWFQLVSIAEQNAAMRRRRHVERDQGREALNGSFAKVLAEASARGIGPQQIHALLKDLRIRPTITAHPTEGKRVTVLEKLRRIYLVLRELELPRWTERERNGLMNELRDQIELIWMTGELHLEKATVEREVAWGLHFFDETLFEMLPEMLLSLEESLAQYYPDETFEVPPFFQFGSWIGGDRDGNPYVTASVTRETLQRNALASLRRYRDGITHLGRVLSITERSLPVPETFRSELAHMLAESGD... | Function: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Mass (Da): 103021
Sequence Length: 922
EC: 4.1.1.31
|
P46710 | MVEFSDAILEPIGAVQRTRVGREATEPMRADIRLLGTILGDTLREQNGDEVFDLVERVRVESFRVRRSEIDRADMARMFSGLDIHLAIPIIRAFSHFALLANVAEDIHRERRRHIHLDAGEPLRDSSLAATYAKLDLAKLDSATVADALTGAVVSPVITAHPTETRRRTVFVTQRRITELMRLHAEGHTETADGRSIERELRRQILTLWQTALIRLARLQISDEIDVGLRYYSAALFHVIPQVNSEVRNALRARWPDAELLSGPILQPGSWIGGDRDGNPNVTADVVRRATGSAAYTVVAHYLAELTHLEQELSMSARLI... | Function: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Mass (Da): 102516
Sequence Length: 934
EC: 4.1.1.31
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Q9JGF1 | MAGGATAPAGAKPKQPKQKQKKPSSQARKKPSQKQKAMKPVKQELRKVEKQVRVLKARTNGPKVNDTMKTTVTVGTLVGQTQSGLNRQLRVSFNPLLMKSTEGGSTTPLSIRASMYEMWKPLSVEIFATPLSGFSSVVGSVGFMVITLNGLEASADSIDTIKARRHVQMALGRPYRLKLSARELAGPREGWWLVDTSEAPADAYGPAVDLMLAYATENLLGTSSGSTTSYTGTLWQVEMRVTYAFSTYNPKPGLQTLVSQSITGGQTVTIQPSPDDGSLIMTTNSQQVLALLTPRVAGQRKGKSQTIWAIAGSAVDAAAT... | Function: Capsid polyprotein VP90: self-assembles to form an icosahedral T=3 capsid.
PTM: Specific enzymatic cleavages in vivo yield mature protein(s). VP90 undergoes a cascade of proteolytic cleavages presumably mediated by host caspases and extracellular proteases (By similarity).
Sequence Mass (Da): 73909
Sequence L... |
P69466 | MDKSESTSAGRNRRRRPRRGSRSAPSSADANFRVLSQQLSRLNKTLAAGRPTINHPTFVGSERCRPGYTFTSITLKPPKIDRGSYYGKRLLLPDSVTEYDKKLVSRIQIRVNPLPKFDSTVWVTVRKVPASSDLSVAAISAMFADGASPVLVYQYAASGVQANNKLLYDLSAMRADIGDMRKYAVLVYSKDDALETDELVLHVDIEHQRIPTSGVLPV | Function: Capsid protein. Probably binds RNA and plays a role in packaging (By similarity).
Sequence Mass (Da): 24141
Sequence Length: 218
Domain: The N-terminal arginine-rich stretch does not seem to be the major RNA-binding region that allows formation of an infectious ribonucleoprotein complex.
Subcellular Location:... |
Q06934 | MDKSGSPNASRTSRRRRPRRGSRSASGADAGLRALTQQMLKLNKTLAIGRPTLNHPTFVGSESCKPGYTFTSITLKPPEIEKGSYFGRRLSLPDSVTDYDKKLVSRIQIRINPLPKFDSTVWVTVRKVPSSSDLSVAAISAMFGDGNSPVLVYQYAASGVQANNKLLYDLSEMRADIGDMRKYAVLVYSKDDNLEKDEIVLHVDVEHQRIPISRMLPT | Function: Capsid protein. Probably binds RNA and plays a role in packaging (By similarity).
Sequence Mass (Da): 24202
Sequence Length: 218
Domain: The N-terminal arginine-rich stretch does not seem to be the major RNA-binding region that allows formation of an infectious ribonucleoprotein complex.
Subcellular Location:... |
P10470 | MSTVVVKGNVNGGVQQPRRRRRQSLRRRANRVQPVVMVTASGQPRRRRRRRGGNRRSRRTGVPRGRGSSETFVFTKDNLMGNSQGSFTFGPSLSDCPAFKDGILKAYHEYKITSILLQFVSEASSTSSGSIAYELDPHCKVSSLQSYVNKFQITKGGAKTYQARMINGVEWHDSSEDQCRILWKGNGKSSDTAGSFRVTIRVALQNPK | Function: Major capsid protein that self-assembles to form an icosahedral capsid with a T=3 symmetry, about 23 nm in diameter, and consisting of 180 capsid proteins monomers. Most of the 180 monomers are the major capsid protein, but a small percentage contain the minor capsid protein, which has a long C-terminal exten... |
P0DQM5 | MVRLLAKLLRSTIHGSNGVSLDAVSSTHGTPGFQTPDARVISRFGFN | Function: Peptide antibiotic that functions through inhibition of the bacterial DNA-dependent RNA polymerase (RNAP) . Inhibits transcription by binding in RNAP secondary channel, where it sterically blocks the folding of the trigger loop, which is essential for efficient catalysis . In contrast to MccJ25, does not rest... |
P54654 | MSEATIVELLKRLDQATTRLEAVEKSIASGVASSSSSSSPSSGAAGPSSASVKEFQNLVDQHITPFVALSKKLAPEVGNQVEQLVKAIDAEKALINTASQSKKPSQETLLELIKPLNNFAAEVGKIRDSNRSSKFFNNLSAISESIGFLSWVVVEPTPGPHVAEMRGSAEFYTNRILKEFKGVNQDQVDWVSNYVNFLKDLEKYIKQYHTTGLTWNPKGGDAKSATPAPASSAPAAPVAPAVSSTPVESKKGPGLGAVFGELSKGDGVTSGLKKVTNDMKSKNFTDKSSVVKAADTKVAKVDAPSRPAVFALQGNKWSIE... | Function: May have a regulatory bifunctional role. Binds G-actin and PIP2. Involved in microfilament reorganization near the plasma membrane in a PIP2-regulated manner.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 49641
Sequence Length: 464
Domain: The C-terminus is responsible for sequestering G-... |
P40122 | MEQLVSRLEAVTNRLEAVASRGGGSTIKAAVDDDPAWFDDFKVFNAKFLSGFVNDTIALGGELEQMGKFVNEAFHCHLVLMEVAARHNRPSQTDLEGLLKPLSEAISKVQDFREKNRSSKQFNHLSAISEGLPFLGWVGVAPKPVLYIQQMEESAQFYTNKLLKEFRESDPKQANWATSFIQLLKGFAAYVKDHHQAGLMWNKEKSAATPAALAVSAHKPPVPPPPSGFAPPPPPPIQAPTVTHAVTGSHSSEDSRSQLFAQLSKGSEVTAGLKKVTDDMKTHKNPELRNQPPLKSSALDPRPYTPPNLKKFSAPVSKPA... | Function: May have a regulatory bifunctional role.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53144
Sequence Length: 481
Subcellular Location: Cell membrane
|
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