ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
O46584 | SVVKSEDYALPSYVDRRDYPLPDVAHVRHLSASQKALKEKEKASWSSLSMDEKVELYRIQFKESFAEMNRGSNEWKTVVGAAMFFIGFTAILIILEKRYVYGPLPHTFDKEWVAMQTKRMLDLKVNPVDGLASKWDYDKKEWKK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
P13073 | MLATRVFSLVGKRAISTSVCVRAHESVVKSEDFSLPAYMDRRDHPLPEVAHVKHLSASQKALKEKEKASWSSLSMDEKVELYRIKFKESFAEMNRGSNEWKTVVGGAMFFIGFTALVIMWQKHYVYGPLPQSFDKEWVAKQTKRMLDMKVNPIQGLASKWDYEKNEWKK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
P19783 | MLASRALSLIGKRAISTSVCLRAHGSVVKSEDYAFPTYADRRDYPLPDVAHVTMLSASQKALKEKEKADWSSLSRDEKVQLYRIQFNESFAEMNRGTNEWKTVVGMAMFFIGFTALVLIWEKSYVYGPIPHTFDRDWVAMQTKRMLDMKANPIQGFSAKWDYDKNEWKK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
Q95283 | MLATRVFNLIGRRAISTSVCVRAHGSXVKSEDYALPVYVDRRDYPLPDVAHVKNLSASQKAXKEKEKASWSSLSMDEKVELYRLKFNESFAEMNRST | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
Q9TTT8 | MLPTRLLSFSGSRAISTSFCLRAHGSVVKSEDYALPSYVDRRDYPLPDVAHVKQLSAGQKALKEKEKAPWGSLTRDEKVELYRIQFNESFAEMNRGTNEWKTVVGTALFFIGFTALILIWEKHYVYGPIPHTFDKEWVAMQTKRMLDMKVSPIQGFSAKWDYNKNEWRK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
P10888 | MLATRALSLIGKRAISTSVCLRAHGSVVKSEDYALPSYVDRRDYPLPDVAHVKLLSASQKALKEKEKADWSSLSRDEKVQLYRIQFNESFAEMNKGTNEWKTVVGLAMFFIGFTALVLIWEKSYVYGPIPHTFDRDWVAMQTKRMLDMKVNPIQGFSAKWDYNKNEWKK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
O46582 | SVVKSEDYARPSYVDRRDYPLPDVAHVRHLSASQKALKEKEKASWSSLSMDEKVEKTVVGAAMFFIGFTAILVILEKRYVYGPLPHTFDKEWVAMQTKRMLDLKMNPIDGLASKWDYEKKEWKK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
O46581 | SVVKSEDFTLPAYVDRRDYPLPDVAHVKHLSASQKALKEKEKASWSSLSMDEKVELYRIKFKESFAEMNRRSNEWKTVVGTAMFFFGITALIVMWEKRYVYGPLPQTFDKEWVAMQTKRMLDMKVNPIQGLASKWDYEKNEWKK | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
Q9RM98 | MSVLDQNAVDINPRISEAEVGDYIALLKPRVMSLVIFTALVGMAMAPGHFHPVLAITSLLCIAVGAGASGALNMALEGDIDAKMSRTANRPIPRGRITRPEAMTFGMTLAFFSVMTLGILVNWIAGALLAFTIFFYVVIYTMWLKRWTAQNIVIGGAAGALPPVVAWAAVTGTVDVEPLLLFAIIFFWTPPHFWALALFRSDDYARAGIPMLPNVAGPDATRLQILLYTIVLIAVAAAPWALGYFDAVYGVVSLILGAGMLVLAINVYMRRERSQSLRATRKLFAFSILYLFALFATLLAEVVFRALAPMAGGA | Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
Location Topology: Multi-pass membrane protein
Sequence Mass (... |
Q829U3 | MLTTSSSRGQRPFGARVKAFVALTKPRIIELLLITTVPVMFLAEQGVPSLRLVLLTCLGGYLSAGGANALNMYIDRDIDALMERTSQRPLVTGMVSPRECLAFGITLAVVSTLLFGLTVNWLSAWLSLGALLFYVVVYTMILKRRTSQNIVWGGIAGCLPVLIGWSSVTDSMSWAPVILFLVMFFWTPPHYWPLSMKVKDDYARVGVPMLPVVASNKVVARQIVIYSWVMVGVSLLLTPLGYTGWFYTLVALLAGGFWLWEAHGLQNRAKAEVTGGKLKEMRLFHWSITYVSILFVAVAVDPFLR | Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
Location Topology: Multi-pass membrane protein
Sequence Mass (... |
Q9XAC2 | MTAVESRPAGVIGTSQSPSHRPFGARVKAFVALTKPRIIELLLITTVPVMFLAEQGVPNLKLVLLTCVGGYLSAGGANALNMYIDRDIDALMDRTSQRPLVTGMVSPVECLVFGITLAIVSTLLFGFTVNWLSAWLSLGALLFYVVVYTMILKRRTSQNIVWGGIAGCLPVLIGWSAVTNSMSWAPVILFGVMFFWTPPHYWPLSMKVKEDYARVGVPMLPVIASNKVVARQIVIYSWVMVVVSLLLQPLGYTGWFYTAVALAAGGMWLWEAHGLQNRAKAEVTGGKLKEMRLFHWSITYVSVLFLAIAVDPFLR | Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
Location Topology: Multi-pass membrane protein
Sequence Mass (... |
Q67ML5 | MFAQARDRLQSGQVVRDYVALTKPRIVILLLITGFAAMWVAAGGPPPLGLTVVTMIGLALSCGAANAINMWYDRDIDAVMARTRRRPLPAGRLTPEQALRFGVITGALSFLVLLTVNLLTALLATAGLLFYVLVYTMWLKRSTVHNIVIGGAAGAAPPLVGWAAVTGRLDWAAVIMFLVVFLWTPPHFWALALFRSEDYERAGVPMLPVVRGERATKWQILLYSLLLIPSAALLYWTGTVGRLYLWTSVVLGCAMVSASVGLLRERAPQMDWAHRTYGWSLLYLFVIFLAMMLDVTRA | Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
Location Topology: Multi-pass membrane protein
Sequence Mass (... |
Q31JY9 | MTLSSDSRLRFPLEEVGAQLLAYWQLTKPRIILLLLITTAAGMGLAAQGPLDPRLAIATLIGGGLAAAAANTLNCLYDRDIDAIMERTRWRPLPSGRIQPFEAWAFALSLAALSFILLDWQANQLAAGLALAGIVFYVVIYTHGLKRHSSQNIVIGGAAGAIPPLVGWAAVTGELAWPAWILFAIVCLWTPPHFWALALMIRDDYAAVKVPMLPVVVGNAATAQQILAYAGLLLPTTLALAWPLGAAGPFYSATALLLGLELLRRSRQLCQAPDSRPLARSLFKFSIFYLMLLCGAIAMDCLPGAPSLSQAIAAWPGF | Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
Location Topology: Multi-pass membrane protein
Sequence Mass (... |
P9WPL7 | MTSTSIPTFPFDRPVPTEPSPMLSELRNSCPVAPIELPSGHTAWLVTRFDDVKGVLSDKRFSCRAAAHPSSPPFVPFVQLCPSLLSIDGPQHTAARRLLAQGLNPGFIARMRPVVQQIVDNALDDLAAAEPPVDFQEIVSVPIGEQLMAKLLGVEPKTVHELAAHVDAAMSVCEIGDEEVSRRWSALCTMVIDILHRKLAEPGDDLLSTIAQANRQQSTMTDEQVVGMLLTVVIGGVDTPIAVITNGLASLLHHRDQYERLVEDPGRVARAVEEIVRFNPATEIEHLRVVTEDVVIAGTALSAGSPAFTSITSANRDSDQ... | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43731
Sequence Length: 400
Subcellular Location: Cell membrane
EC: 1.14.-.-
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P9WPL5 | MTEAPDVDLADGNFYASREARAAYRWMRANQPVFRDRNGLAAASTYQAVIDAERQPELFSNAGGIRPDQPALPMMIDMDDPAHLLRRKLVNAGFTRKRVKDKEASIAALCDTLIDAVCERGECDFVRDLAAPLPMAVIGDMLGVRPEQRDMFLRWSDDLVTFLSSHVSQEDFQITMDAFAAYNDFTRATIAARRADPTDDLVSVLVSSEVDGERLSDDELVMETLLILIGGDETTRHTLSGGTEQLLRNRDQWDLLQRDPSLLPGAIEEMLRWTAPVKNMCRVLTADTEFHGTALCAGEKMMLLFESANFDEAVFCEPEK... | Function: Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain during infection . Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25R)-26-hydroxycholest-4-en-3-one (alcohol), (25R)-26-oxocholest-4-en-3-one (aldehyde),... |
Q01741 | KFLQIAVEEHYQSFDKNNIRDVTDSLWRSKKTKPRGAADPNEKIINLVNDIFGAGFDTVTTALSWSLMYLVTQPHSQKKIQESELDTAIGRERRSWLSERSMLPYKEAFILETVPTWQFVPFTIPHSTTRDTTLNGFHIPKECCVFVNQWQVNHEAELWEDPFVFRTERFLTDDSTAIDKTLSEKVMGKQVGLAWKSALGTRQWEVSFYLSTLTPNWSSAPGGESKKDRVRPIYGLSMKHKRCEHFQVKKRFSMKSSN | Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Catalytic Activity: an organic molecule + O2... |
P05177 | MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKNPHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDGQSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELMAGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFPILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGNLIPQEKIVNLVNDIFGAGFD... | Function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by N... |
Q92109 | MVLMILPIIGSVSASEGLVAMVTLCLVYMIMKYMHTEIPEGLKRLPGPKPLPIIGNMLEVHNNPHLSLTAMSERYGSVFQIQIGMRPVVVLSGNETVRQALIKQGEDFAGRSDLYSFKFINDGKSLAFSTDKAGVWRARRKLAMSALRSFATLEGTTPEYSCALEEHVLKEGEYLVKQLTSVMDVSGSFDPFRHIVVSVANVICGMCFGRRYSHDDQELLGLVNMSDEFGQVVGSGNPADFIPILRYLPNRTMKRFMDINDRFNNFVQKIVSEHYESYDKDNIRDITDSLIDHCEDRKLDENANIQVSDEKIVGIVNDLF... | Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Catalytic Activity: an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemopro... |
P79761 | MGPEEVMVQASSPGLISATEVLVAAATFCLLLLLTQTRRQHAPKGLRSPPGPRGLPMLGSVLELRKDPHLVLTRLSRKYGDVMEVTIGSRPVVVLSGLETIKQALVRQAEDFMGRPDLYSFRHITDGQSLTFSTDTGEMWKARRKLAQNALKNFSIAASPTASSSCLLEEHVSTEASYLVTKFLQLMEEKQSFDPYRYMVVSVANVICAICFGKRYDHDDQELLSVVNVVDEFVDVTAAGNPADFIPLLRYLPSRNMDSFLDFNKRFMKLLQTAVEEHYQTFDKNNIRDVTDSLIEQCVEKKAEANGATQIPNEKIINLV... | Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Catalytic Activity: an organic molecule + O2... |
Q16678 | MGTSLSPNDPWPLNPLSIQQTTLLLLLSVLATVHVGQRLLRQRRRQLRSAPPGPFAWPLIGNAAAVGQAAHLSFARLARRYGDVFQIRLGSCPIVVLNGERAIHQALVQQGSAFADRPAFASFRVVSGGRSMAFGHYSEHWKVQRRAAHSMMRNFFTRQPRSRQVLEGHVLSEARELVALLVRGSADGAFLDPRPLTVVAVANVMSAVCFGCRYSHDDPEFRELLSHNEEFGRTVGAGSLVDVMPWLQYFPNPVRTVFREFEQLNRNFSNFILDKFLRHCESLRPGAAPRDMMDAFILSAEKKAAGDSHGGGARLDLENV... | Function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by N... |
Q64429 | MATSLSADSPQQLSSLSTQQTTLLLLFSVLAAVHLGQWLLRQWQRKPWSSPPGPFPWPLIGNAAAVGQASHLYFARLARRYGDVFQIRLGSCPVVVLNGESAIHQALVQQGSIFADRPPFASFRVVSGGRSLAFGHYSEHWKTQRRSAYSTMRAFSTRHPRSRGLLEGHALAEARELVAVLVRRCAGGAFLDPTQPVIVAVANVMSAVCFGCRYNHDDAEFLELLSHNEEFGRTVGAGSLVDVLPWLQLFPNPVRTTFRKFEQLNRNFSNFVLDKFLRHRESLVPGAAPRDMTDAFILSAEKKASGAPGDDSSGLDLEDV... | Function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (By similarity). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electron... |
P98187 | MSLLSLSWLGLRPVAASPWLLLLVVGASWLLARILAWTYAFYHNGRRLRCFPQPRKQNWFLGHLGLVTPTEEGLRVLTQLVATYPQGFVRWLGPITPIINLCHPDIVRSVINTSDAITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKSANIMHAKWQRLAMEGSTCLDVFEHISLMTLDSLQKCIFSFDSNCQEKPSEYITAIMELSALVVKRNNQFFRYKDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSQGVDDFLQAKAKSKTLDFIDVLLLSEDKNGKELSDEDIRA... | Function: A cytochrome P450 monooxygenase involved in the metabolism of endogenous polyunsaturated fatty acids (PUFAs) and their oxygenated derivatives (oxylipins). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provid... |
Q9HCS2 | MSLLSLPWLGLRPVATSPWLLLLLVVGSWLLARILAWTYAFYNNCRRLQCFPQPPKRNWFWGHLGLITPTEEGLKNSTQMSATYSQGFTVWLGPIIPFIVLCHPDTIRSITNASAAIAPKDNLFIRFLKPWLGEGILLSGGDKWSRHRRMLTPAFHFNILKSYITIFNKSANIMLDKWQHLASEGSSRLDMFEHISLMTLDSLQKCIFSFDSHCQERPSEYIATILELSALVEKRSQHILQHMDFLYYLSHDGRRFHRACRLVHDFTDAVIRERRRTLPTQGIDDFFKDKAKSKTLDFIDVLLLSKDEDGKALSDEDIRA... | Function: A cytochrome P450 monooxygenase involved in the metabolism of endogenous polyunsaturated fatty acids (PUFAs). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CP... |
Q6NT55 | MLPITDRLLHLLGLEKTAFRIYAVSTLLLFLLFFLFRLLLRFLRLCRSFYITCRRLRCFPQPPRRNWLLGHLGMYLPNEAGLQDEKKVLDNMHHVLLVWMGPVLPLLVLVHPDYIKPLLGASAAIAPKDDLFYGFLKPWLGDGLLLSKGDKWSRHRRLLTPAFHFDILKPYMKIFNQSADIMHAKWRHLAEGSAVSLDMFEHISLMTLDSLQKCVFSYNSNCQEKMSDYISAIIELSALSVRRQYRLHHYLDFIYYRSADGRRFRQACDMVHHFTTEVIQERRRALRQQGAEAWLKAKQGKTLDFIDVLLLARDEDGKEL... | Function: A cytochrome P450 monooxygenase involved in epidermal ceramide biosynthesis. Hydroxylates the terminal carbon (omega-hydroxylation) of ultra-long-chain fatty acyls (C28-C36) prior to ceramide synthesis . Contributes to the synthesis of three classes of omega-hydroxy-ultra-long chain fatty acylceramides having... |
Q9GLL1 | MLELSVSRLGFGLVAASPWLLLLVVGASWLLARVLAWTYTFYNNCRLLQCFPQPPKQNWFFAHLYLVPPTEQGLRKSTQLAANYSHGYLIWFGPITPMIVFCHPDMLRSIANASAAVAPKNMDFYKFLKPWLGDGLLLSAGDKWSRHRHLLTPTFHFNILKPYMKIFTKSTDIMHTKWERLITQGHTRLDMFEHLSLLTLDSLQKCVFSFDSNCQELSSCRKPSKYITAILELSELVAKRNRQIFLHADFLYFLTLDGWRFLRACRLVHDFTDAVIQERCRTLPENVDDFLKAKAKTKTLDFIDVLLLTKDEDGKRLSDE... | Function: A cytochrome P450 monooxygenase that catalyzes the omega-hydroxylation of prostaglandin E2. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemo... |
Q9V3S0 | MAVEVVQETLQQAASSSSTTVLGFSPMLTTLVGTLVAMALYEYWRRNSREYRMVANIPSPPELPILGQAHVAAGLSNAEILAVGLGYLNKYGETMKAWLGNVLLVFLTNPSDIELILSGHQHLTKAEEYRYFKPWFGDGLLISNGHHWRHHRKMIAPTFHQSILKSFVPTFVDHSKAVVARMGLEAGKSFDVHDYMSQTTVDILLSTAMGVKKLPEGNKSFEYAQAVVDMCDIIHKRQVKLLYRLDSIYKFTKLREKGDRMMNIILGMTSKVVKDRKENFQEESRAIVEEISTPVASTPASKKEGLRDDLDDIDENDVGA... | 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): 62971
Sequence Length: 556
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9V558 | MIILWLILALSALLYWLHRANKDYHILSFFTKRIRLKDGTPVEIIAPIAKGKTIFGNTLDLYGRDHAGVFNYSRERAKEMGTSYIEYVFGKAIYNIIDADSAENVLNHPNLITKGLVYNFLHPFLRTGLLTSTGKKWHARRKMLTPTFHFNILNQFQEIFKTESQKFLLQFEGQDEVTITLHDVIPRFTLNSICETAMGVKLDEMAEKGDRYRENFSQIEECFIRRLSNPLLWGDKLFEMFAAKDFASALDVVHRFSSEIIAKRRDLLKDELDKSSSTADDDGFVSKKRFAMLDTLIYAEKDGLIDHIGICEEVDTLMFE... | 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): 59433
Sequence Length: 513
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9V557 | MMICLLWISVAILVVIHWIYKVNKDYNILAFFARRVQTKDGKPLDSLVPMIKGRTVFANCFDLLGKDTDQVFTHLRQLAKNSGDSYLQYSMGFSNFNVIDAHNAANILNHPNLITKGVIYNFLHPFLRTGVLTATEKKWHTRRSMLTRTFHLDILNQFQEIFIAESLKFVSQFQGQNEVVVSLKDRISRFTLNSICETAMGIKLDEMAEKGDRYRANFHIIDEGLTRRIVNPLYWDDCVYNMFTGHKYNAALKVVHEFSREIIAKRRVLLEEELENRRATQTADDDICVIRKKRFAMLDTLICAEKDGLIDDIGISEEVD... | 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): 60459
Sequence Length: 520
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9VXY0 | MSTLALVAFVLWAAFLRYLPKILNFLRLQRFAKTLPGPTIGELIANVKKGEILNWLKELREKHGPVFRIWFGKDLMVMFTDPEDIKQLLGNNQLLTKSRNYELLEPWLGKGLLTNGGESWHRRRKLLTPGFHFRILSEFKEPMEENCRILVRRLRTKANGESFDIYPYITLFALDAICETAMGIKKHAQLQSDSEYVQAVQSICRVMHKQSFSFWQRLNVFFKHTKPGKEREAALKVLHDETNRVIRLRREQLIQERNEWKPEAEQDDVGAKRRLAFLDMLLLTQMEGGAELSDTDIREEVDTFMFEGHDTTSSAIAFAL... | 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): 57189
Sequence Length: 495
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q6ZWL3 | MAGLWLGLVWQKLLLWGAASALSLAGASLVLSLLQRVASYARKWQQMRPIPTVARAYPLVGHALLMKPDGREFFQQIIEYTEEYRHMPLLKLWVGPVPMVALYNAENVEVILTSSKQIDKSSMYKFLEPWLGLGLLTSTGNKWRSRRKMLTPTFHFTILEDFLDIMNEQANILVKKLEKHINQEAFNCFFYITLCALDIICETAMGKNIGAQSNDDSEYVRAVYRMSEMIFRRIKMPWLWLDLWYLMFKEGWEHKKSLQILHTFTNSVIAERANEMNANEDCRGDGRGSAPSKNKRRAFLDLLLSVTDDEGNRLSHEDIR... | Function: A cytochrome P450 monooxygenase involved in fatty acid metabolism in the eye. Catalyzes the omega-hydroxylation of polyunsaturated fatty acids (PUFAs) docosahexaenoate (DHA) and its precursor eicosapentaenoate (EPA), and may contribute to the homeostasis of these retinal PUFAs . Omega hydroxylates saturated f... |
Q9DBW0 | MLWLWLGLSGQKLLLWGAASAVSLAGATILISIFPMLVSYARKWQQMRSIPSVARAYPLVGHALYMKPNNAEFFQQLIYYTEEFRHLPIIKLWIGPVPLVALYKAENVEVILTSSKQIDKSFLYKFLQPWLGLGLLTSTGSKWRTRRKMLTPTFHFTILENFLDVMNEQANILVNKLEKHVNQEAFNCFFYITLCALDIICETAMGKNIGAQSNNDSEYVRTVYRMSDMIYRRMKMPWLWFDLWYLVFKEGRDHKRGLKCLHTFTNNVIAERVKERKAEEDWTGAGRGPIPSKNKRKAFLDLLLSVTDEEGNRLSQEDIR... | Function: A cytochrome P450 monooxygenase involved in fatty acid metabolism in the eye. Catalyzes the omega-hydroxylation of polyunsaturated fatty acids (PUFAs) docosahexaenoate (DHA) and its precursor eicosapentaenoate (EPA), and may contribute to the homeostasis of these retinal PUFAs. Omega hydroxylates saturated fa... |
Q8N118 | MEFSWLETRWARPFYLAFVFCLALGLLQAIKLYLRRQRLLRDLRPFPAPPTHWFLGHQKFIQDDNMEKLEEIIEKYPRAFPFWIGPFQAFFCIYDPDYAKTLLSRTDPKSQYLQKFSPPLLGKGLAALDGPKWFQHRRLLTPGFHFNILKAYIEVMAHSVKMMLDKWEKICSTQDTSVEVYEHINSMSLDIIMKCAFSKETNCQTNSTHDPYAKAIFELSKIIFHRLYSLLYHSDIIFKLSPQGYRFQKLSRVLNQYTDTIIQERKKSLQAGVKQDNTPKRKYQDFLDIVLSAKDESGSSFSDIDVHSEVSTFLLAGHDT... | Function: A cytochrome P450 monooxygenase that selectively catalyzes the epoxidation of the last double bond of the arachidonoyl moiety of anandamide, potentially modulating endocannabinoid signaling. Has no hydroxylase activity toward various fatty acids, steroids and prostaglandins. Mechanistically, uses molecular ox... |
Q86W10 | MEPSWLQELMAHPFLLLILLCMSLLLFQVIRLYQRRRWMIRALHLFPAPPAHWFYGHKEFYPVKEFEVYHKLMEKYPCAVPLWVGPFTMFFSVHDPDYAKILLKRQDPKSAVSHKILESWVGRGLVTLDGSKWKKHRQIVKPGFNISILKIFITMMSESVRMMLNKWEEHIAQNSRLELFQHVSLMTLDSIMKCAFSHQGSIQLDSTLDSYLKAVFNLSKISNQRMNNFLHHNDLVFKFSSQGQIFSKFNQELHQFTEKVIQDRKESLKDKLKQDTTQKRRWDFLDILLSAKSENTKDFSEADLQAEVKTFMFAGHDTTS... | Function: A cytochrome P450 monooxygenase that catalyzes the in-chain oxidation of fatty acids . Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates lauric and myristic acids predominantly at the omega-4 and omega-2 positions, respectively . Catalyzes the epoxidation of double bonds of polyunsaturated fa... |
Q56686 | MFKNKLAVLFTCLSVFSFSAQSGSFDTVTLGSKGGIQDGNLTAFLIKSEADSNFVMLDAGSVVNGLIVSEQKGAFKDITVPDSSPYTKVGYLLKDRIKGYFISHAHLDHVAGLIISSPDDSKKPIYGLAATNKDLMKNYFNWSAWPNFGNKGEGFKLNKYNYVDLQPGVWSPVAETTMSVVSLPLSHSGGQSTVFILKDSEGDVFAYFGDTGPDEVEKSSAMRTAWSVLAPFVKQGKLKGIIIEVSFTNETPDKSLFGHLTPNWLVKELSVLEDMNGKGSLKDLNVAISHIKYSLKNSEDPKVIIKKQLVEVNDLGVNFI... | Function: Seems to allow the organism to grow on cAMP.
Catalytic Activity: a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+)
Sequence Mass (Da): 36089
Sequence Length: 330
Subcellular Location: Periplasm
EC: 3.1.4.17
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Q8ZD92 | MKYLSIKSASDKIKSGLLKTGVILSFSLFSSLSTAAFEVVALGVDGGVSDGNLTSYLIRNDSQPLYLGLDAGSVLPGIARALEKGHFAAITDAMAAPLTRQGYIFRQSINSYFISHAHLDHVSGLIIGSPDDSKKTIYASADTIDVLRNYYFNWRVWPNFTDSGSGARLGTYRMQVVRPAQSLSLGLTRLTGEMYPLSHDKSPSSMLLISSNNEFFAYFGDTGPDDVEKSKNLDTVWRKLAEKVTQQQLKGMIIEVSYPNDVADNKLFGHMTPTWLLKELKKLEQYSGEGQPLKGLPVVISHIKPSFQQGQDVRKLILSE... | Catalytic Activity: a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+)
Sequence Mass (Da): 37874
Sequence Length: 343
Subcellular Location: Periplasm
EC: 3.1.4.17
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Q2YIF7 | MKRILLAEDDNDMRRFLVKALEKAGYHVTHFDNGASAYERLQEEPFSLLLTDIVMPEMDGIELARRATEIDPDLKIMFITGFAAVALNPDSDAPRDAKVLSKPFHLRDLVNEIEKMLIAA | Function: Component of a regulatory phosphorelay system that controls B.abortus cell growth, division, and intracellular survival inside mammalian host cells. This signaling pathway is composed of CckA, ChpT, CtrA and CpdR. CpdR is a response regulator substrate of ChpT. Unphosphorylated CpdR controls steady-state leve... |
O04147 | MEEVKKDVYSVWALPDEESEPRFKKLMEALRSEFTGPRFVPHVTVAVSAYLTADEAKKMFESACDGLKAYTATVDRVSTGTFFFQCVFLLLQTTPEVMEAGEHCKNHFNCSTTTPYMPHLSLLYAELTEEEKKNAQEKAYTLDSSLDGLSFRLNRLALCKTDTEDKTLETWETVAVCNLNP | Function: Hydrolyzes ADP-ribose 1'',2''-cyclic phosphate (Appr>1) that is produced during tRNA splicing into ADP-ribose 1''-phosphate (Appr-1''p) . Acts also on nucleoside 2',3'-cyclic phosphates .
Catalytic Activity: ADP-alpha-D-ribose 1'',2''-cyclic phosphate + H2O = ADP-alpha-D-ribose 1''-phosphate + H(+)
Sequence M... |
Q9BZB8 | MALSLEEEAGRIKDCWDNQEAPALSTCSNANIFRRINAILDNSLDFSRVCTTPINRGIHDHLPDFQDSEETVTSRMLFPTSAQESSRGLPDANDLCLGLQSLSLTGWDRPWSTQDSDSSAQSSTHSVLSMLHNPLGNVLGKPPLSFLPLDPLGSDLVDKFPAPSVRGSRLDTRPILDSRSSSPSDSDTSGFSSGSDHLSDLISSLRISPPLPFLSLSGGGPRDPLKMGVGSRMDQEQAALAAVTPSPTSASKRWPGASVWPSWDLLEAPKDPFSIEREARLHRQAAAVNEATCTWSGQLPPRNYKNPIYSCKVFLGGVPW... | Function: Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUU... |
P70166 | MAFSLEEAAGRIKDCWDNQEVPALSTCSNANIFRRINAILDDSLDFSKVCTTPINRGIHDQLPDFQDSEETVTSRMLFPTSAQESPRGLPDANGLCLGLQSLSLTGWDRPWSTQDSDSSAQSSTQSVLSMLQNPLGNVLGKAPLSFLSLDPLGSDLDKFPAPSVRGSRLDTRPILDSRSSSPSDSDTSGFSSGSDHLSDLISSLRISPPLPFLSMTGNGPRDPLKMGVGSRMDQEQAALAAVAPSPTSAPKRWPGASVWPSWDLLGAPKDPFSIEREARLHRQAAAVNEATCTWSGQLPPRNYKNPIYSCKVFLGGVPWD... | Function: Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUU... |
Q5R733 | MLFPTSAQESSRGLPDANDLCLGLQSLSLTGWDRPWSTQDSDSSAQSSTHSVLSMLHNPLGNVLGKPPLSFLPLDPLGSDLVDKFPAPSVRGSRLDTRPILDSRSSSPSDSDTSGFSSGSDHLSDLISSLRISPPLPFLSLTGGGPRDPLKMGVGSRMDQEQAALAAVTPSPTSASKRWPGASVWPSWDLLEAPKDPFSIEREARLHRQAAAVNEATCTWSGQLPPRNYKNPIYSCKVFLGGVPWDITEAGLVNTFRVFGSLSVEWPGKDGKHPRCPPKGYVYLVFELEKSVRSLLQACSHDPLSPDGLSEYYFKMSSRR... | Function: Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUU... |
Q7TN99 | MQDDLLMDKSKTQPQSQQQQRQQQQQQQQLQPEPGAAEAPSTPLSSEIPKPEDSSAVPALSPASAPPAPNGPDKMQMESPLLPGLSFHQPPQQPPPPQEPTAPGASLSPSFGSTWSTGTTNAVEDSFFQGITPVNGTMLFQNFPHHVNPVFGGTFSPQIGLAQTQHHQQPPPPAPQPPQPAQPPQAQPSQQRRSPASPSQAPYAQRSAAAYGHQPIMTSKPSSSSAVAAAAAAAAASSASSSWNTHQSVNAAWSAPSNPWGGLQAGRDPRRAVGVGVGVGVGVPSPLNPISPLKKPFSSNVIAPPKFPRAAPLTSKSWME... | Function: Sequence-specific RNA-binding protein which acts as a translational repressor in the basal unstimulated state but, following neuronal stimulation, acts as a translational activator . In contrast to CPEB1, does not bind to the cytoplasmic polyadenylation element (CPE), a uridine-rich sequence element within th... |
Q28CH2 | MQDDLLMDKSKAQQRQQPQQPPSSQTQQQQKEAASVAEPPSSRESSPPTHKDKMQMESPLLPGLSFQQEPPTTPSLSPSFGSTWSTGGSNSAVDDSFFPGITPVNGTMLFQNFPHHHHVNPVFGGTFSPQMGLAHQTQQQQRRSPASPNNHTAYTQRNAYSHQPILTNKPSSSPNSSSPSPSNWNNQQNAAWNTPSNPWGAMQPGRDPRRAVGVGVGVGVGVPSPLNPISPLKKTFSSNVIAPPKFSRASPLTPKSWVEDNAFRTDNGNTLLPLQDRNRPYDSFNLHTLENSLMDMIRTDHEPLKARMGLNFHHPGTDNI... | Function: Sequence-specific RNA-binding protein which acts as a translational repressor in the basal unstimulated state but, following neuronal stimulation, acts as a translational activator (By similarity). Does not bind to the cytoplasmic polyadenylation element (CPE), a uridine-rich sequence element within the mRNA ... |
A0A3G1QTU5 | FRSTAAGRCLPVTCCVFPRHFRVSSSSILPSNAKVVGGCKKNRQIAVEAAQSLEVDSQQPMNQEEVSEKMRQLREKIRWMLQNMDDGEISVSPYDTAWVAMVEDIGGGGGPQFPTSLEWISNNQLDDGSWGDLRFLIYDRILNTLACVAVLTQWKMHLHKCQKGLRFIRENIDNLENGNDEMMPVGFEVAFPSLIQTAKKVGIKIPTDSPFMKNIYAKRDLKLRKIPMDILHTKPTTLLHSLEGMEGLDWEKLLNLRTDDGSFLMSPSSTAYVFRHTKDELCHQYLLKSVNKFNGGVPNVYPVDMFEHLWCVDRLQRLGI... | Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities, and in the production of gibberellins phytohormones . Catalyzes the conversion of (2E,6E,10E)-geranyl... |
A0A1W6QDJ1 | MSSSSIVTSLLRPTTAADGVLPRQMAQVNSSCNIWRSKAKVGGINYFNPGNIKCVEEVHKSRQVVVAALKSLEYETEKPTNQDVVSEKMRVLSERIETMLQNMDEGEISISPYDTAWVALVEDTDGRPQFPTSLEWISNNQLADGSWGDRKFVIYDRILNTLACVVALTTWNMHPHKCNRGLRFIRDNMEKLENENEELMPIGFEVVFPSLIEAAQKLGIEIPHIDSPCIKKIQAMRDFKLKRIPMELLHKKPTSLLHSLEGMQGLVWEKLLDFRSDGSFLCSPSSTAYALQHTKDELCLQYLLKAVKKFNGGVPNVYPV... | Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities . Catalyzes the conversion of (2E,6E,10E)-geranylgeranyl diphosphate (GGPP) to ent-copalyl diphosphate... |
Q0JF02 | MPVFTASFQCVTLFGQPASAADAQPLLQGQRPFLHLHARRRRPCGPMLISKSPPYPASEETREWEADGQHEHTDELRETTTTMIDGIRTALRSIGEGEISISAYDTSLVALLKRLDGGDGPQFPSTIDWIVQNQLPDGSWGDASFFMMGDRIMSTLACVVALKSWNIHTDKCERGLLFIQENMWRLAHEEEDWMLVGFEIALPSLLDMAKDLDLDIPYDEPALKAIYAERERKLAKIPRDVLHSMPTTLLHSLEGMVDLDWEKLLKLRCLDGSFHCSPASTATAFQQTGDQKCFEYLDGIVKKFNGGVPCIYPLDVYERL... | Function: Catalyzes the conversion of geranylgeranyl diphosphate to the phytoalexin precursor syn-copalyl diphosphate . Required for the biosynthesis of momilactones that exude from roots and act as allelochemicals against lowland weeds in paddy soil .
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate = 9alpha... |
Q54518 | MIDIHSHIVFDVDDGPKSREESKALLAESYRQGVRTIVSTSHRRKGMFETPEEKIAENFLQVREIAKEVADDLVIAYGAEIYYTLDALEKLEKKEIPTLNDSRYALIEFSMHTSYRQIHTGLSNILMLGITPVIAHIERYDALENNEKRVRELIDMGCYTQINSYHVSKPKFFGEKYKFMKKRARYFLERDLVHVVASDMHNLDSRPPYMQQAYDIIAKKYGAKKAKELFVDNPRKIIMDQLI | Function: Dephosphorylates CpsD. Involved in the regulation of capsular polysaccharide biosynthesis.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 28354
Sequence Length: 243
Pathway: Capsule biogenesis; capsule polysaccharide biosynthesis.
EC: 3.1.3.48
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Q3K0S9 | MNKIANTEVEINIFNLLKKLWKKKFLITFVAIAFATAGLFYSLFIVTPQYTSSTRIYVINPNTPNNSITAQDLQAGSFLANDYKEIITSTDVLEKVISSEKLNYPSSQLLQKITVSILKDTRVISISVEDANPKMSQKLANSVREAAVSKIKAVTQVEDITTLEKGNLPKAPSSPNIKKNVLIGFIVGAGLSTIVLVIMGILDDRVNTEEDIEKALGLTSLGIVPDLNKL | Function: Required for CpsD phosphorylation (By similarity). Involved in the regulation of capsular polysaccharide biosynthesis. May be part of a complex that directs the coordinated polymerization and export to the cell surface of the capsular polysaccharide.
Location Topology: Multi-pass membrane protein
Sequence Mas... |
B1X536 | MSASLSQLVHQLSARFNNQQQAFDNPPLYAHIVVNCRPLVHLLPGSLLIEQSYAMDPLKPYRIRVLRAQTRDEKLIIFSYSLSDEQKYWGSVYEPERMLKIEEKDLQAIEGCNYIVRKKNSNFIGEVEPGCRCLVDRKGVTTYIVSKFELTNKGEMRTLDRGHNPVTHEQLWGSLGGVFEFNRTTDFSKEIPYDWIEEWKK | Function: Covalently attaches a chromophore to Cys residue(s) of phycobiliproteins.
Sequence Mass (Da): 23416
Sequence Length: 201
Subcellular Location: Plastid
EC: 4.-.-.-
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O65220 | MASSSILIPPILTRRNLLLSTTIATVTPPPPAKPPSPDITITDRVFLDFSLCPTYFRSDPSATLSSTTPCSDSTPLGRVVLGLYGRHVPITVSTFKRMCTSSSTSYKNTPVHKIFPGQYFLAGRQGGGRRDTAEVGYSLRDLPRNTDVVNSKAFLLPHARAGVVSLCLSENDDDDDIRLDPDYRNVEFLITTGPGPSPQLDGGNIVFGTVLEGLDVVTSISSIPTYKPSENIKQFNDFAEFLGDERAQNARSLWNRPLKTVFISGCGELKVTNPSLSPTLP | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
PTM: S-nytrosylated during the hypersensitive disease resistance response.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylprolin... |
Q6Q152 | MSTVYVLEPPTKGKVIVNTTHGPIDVELWPKEAPKSVRNFVQLCLEGYFDNTIFHRVIPGFLVQGGDPTGSGTGGDSIYGGVFADEFHSRLRFSHRGIVAMANASSPNSNGSQFFFTLDKCDWLDKKHTIFGKVTGDSIYNLLRLGEVDTSKDDRPLDPAPKILSVEVLWNPFEDIVPRVLAKTSEESAAEIKEPPTKPVKKLNLLSFGEEAEEEEKELAVVKQKIKSSHDVLNDPRLLKAEASDKERNASESKEVLSVREALNAKKEAAQKDKSFSVSDTVGNSDDDDDGEDETKFDAKMRNQVLSRRKEIGDTPSKPT... | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Involved in plant response to pathogen infection by increasing PAD4 expression in absence of EDS1 up-regulation.
Catalytic Activity: [protein]-peptidylproline ... |
Q8W4D0 | MEEESKNGGTTIPTEELAVVAVPPVVEEEEPMVGPGPAPRGKRKRPLQFEQAYLDSLPSANMYEKSYMHRDVVTHVAVSAAEFFISGSMDGHLKFWKKKGVGIEFAKHFRSHLGPIEGLAVSIDGLLCCTISNDHAVKIYDVVNYDMMAMIRLPYIPGAVEWVYKQGDVKAKLAVSDRDSLFVHIYDPRSGSNEPIASKEIHMNPIKVMKYNPVSDTMISGDTKGIIEYWSATTLQFPEDEVNFKLKSDTNLFEIIKCKTTISAIEVSPDGKQFSITAPDRRIRVFWFRTGKLRRVYDESLVVAQDLQRSDAPLYRLEAI... | Function: PPIases accelerate the folding of proteins (Probable). It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides . Histone proline isomerase that increases the rate of cis-trans isomerization of the synthetic histone H3 peptides H3P30 (RKSAP30F-p-nitroanilide) and H3P30K27me3 (... |
Q91WE4 | MVCIPCIVIPVLLWIFKKFLEPYIYPVVSRIWPKKAVQQSGDKNMSKVDCKGAGTNGLPTKGPTEVSDKKKD | Function: May activate the NF-kappa-B signaling pathway.
PTM: Undergoes ER-associated degradation (ERAD).
Sequence Mass (Da): 8036
Sequence Length: 72
Subcellular Location: Endoplasmic reticulum
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B1WC88 | MVCIPCIVIPVLLWIFKKFLEPYIYPVVSRIWPRKAVQQLDNKNTGKVDCKGADTNGFSTKGPTEVSDKKKD | Function: May activate the NF-kappa-B signaling pathway.
PTM: Undergoes ER-associated degradation (ERAD).
Sequence Mass (Da): 8169
Sequence Length: 72
Subcellular Location: Endoplasmic reticulum
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A0A0M5K865 | MVKLYCAVVGVAGSAFSVRVDESDTVDDLKDAIKAKKPNDFKDIDADKLELYVAKRDGVWLTEADVKSGVADITGLVRLEVVRAKLFSVGLSDEVVSEVDAQEEAAGRGPVNVLVVVPMKKRRVDAGVDEERRFFDTRDFPPLLAPPQRGATVESPEAQWEKLLNSLEWKEPKRLCASSGQNWPYQGESELAGHLVEPLALHYTAWYLQNEDKQNHAINLVLSGPGTGKSRMLDQMKGLMCAAAARSNNRKLKERMENAFVFSVTFENGTSATGSLLDRDNPEFDISYRMLYQLSKDRPNWKKFAKTLKSYRSLELDIEA... | Function: Secreted effector that suppresses plant basal defense and promotes plant susceptibility via targeting promoters of host HSP gene and thus inhibiting their expression. CRN108 binds directly to heat shock elements (HSEs) 5'-GAAnnTTC-3' and interferes with the association of the HSE with the plant heat shock tra... |
E9M7A1 | MVKLFCAIVGVAGSAFPVDIDGGQSVGDLKKAIKAESEDITIPAKDLKLFLAKTEGGAWLPDDDQAALDLEDGKVHEDIQALIDGEKMKATWTIEDVLTANNMTKRKGRAPKSRQIHVLVVVPEGAFGSASETSKMDQLVEKVDKMYEQTVLGKRKYVHSEVTSTQGRQLLNDLDIRVEFVRTVPFDAGEGSSVDPYEWKRVIIENGEEVVLTEEQQRKRYRRYVEHNIGTVLKETQLCVIGVERGTNILTVKVPGREIELAGRTDLLILSDLVAMRPTEVQYLPGVKMLIEVKRDVKASNDFQALSELIALDLLVDDPV... | Function: Secreted effector that, with CRN63, is critical to pathogenesis by modulating host defenses . Suppresses cell death elicited by the P.sojae necrosis-inducing protein or CRN63 . CRN115 and CRN63 may share the same molecular host targets that are involved in the cell death signal transduction pathway and that t... |
D0CCT2 | MYKLMKNIQTTALNRTTLMFPLALVLFEFAVYIGNDLIQPAMLAITEDFGVSATWAPSSMSFYLLGGASVAWLLGPLSDRLGRKKVLLSGVLFFALCCFLILLTRQIEHFLTLRFLQGIGLSVISAVGYAAIQENFAERDAIKVMALMANISLLAPLLGPVLGAFLIDYVSWHWGFVAIALLALLSWVGLKKQMPSHKVSVTKQPFSYLFDDFKKVFSNRQFLGLTLALPLVGMPLMLWIALSPIILVDELKLTSVQYGLAQFPVFLGLIVGNIVLIKIIDRLALGKTVLIGLPIMLTGTLILILGVVWQAYLIPCLLIG... | Function: Efflux pump that mediates resistance to chloramphenicol.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45882
Sequence Length: 413
Subcellular Location: Cell inner membrane
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Q96SW2 | MAGEGDQQDAAHNMGNHLPLLPAESEEEDEMEVEDQDSKEAKKPNIINFDTSLPTSHTYLGADMEEFHGRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQDFGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQKRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCELDIMNKCTS... | Function: Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2 or ILF2 . Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fib... |
Q12289 | MSSDTSLSESSLLKEESGSLTKSRPPIKSNPVRENIKSFVAGGVGGVCAVFTGHPFDLIKVRCQNGQANSTVHAITNIIKEAKTQVKGTLFTNSVKGFYKGVIPPLLGVTPIFAVSFWGYDVGKKLVTFNNKQGGSNELTMGQMAAAGFISAIPTTLVTAPTERVKVVLQTSSKGSFIQAAKTIVKEGGIASLFKGSLATLARDGPGSALYFASYEISKNYLNSRQPRQDAGKDEPVNILNVCLAGGIAGMSMWLAVFPIDTIKTKLQASSTRQNMLSATKEIYLQRGGIKGFFPGLGPALLRSFPANAATFLGVEMTHS... | Function: Transports carnitine, acetylcarnitine, propionylcarnitine and to a much lower extent medium- and long-chain acylcarnitines.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34754
Sequence Length: 327
Subcellular Location: Mitochondrion inner membrane
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Q9FIL7 | MPMRSKTPTPLRFSNGKHQRDDSEYSWTDVGTGEKARNVSVLGAIRRAAKKVFVIIFLGQRKLKPTECRSDPGESSTHDRESTLSGWTGYSSPSSFGRSTERKVSGQYRFSGSRFQSPGKDSSSSKSWHQGPVIFSFGELQRATANFSSVHQIGEGGFGTVFKGKLDDGTIVAIKRARKNNYGKSWLLEFKNEIYTLSKIEHMNLVKLYGFLEHGDEKVIVVEYVANGNLREHLDGLRGNRLEMAERLEIAIDVAHALTYLHTYTDSPIIHRDIKASNILITNKLRAKVADFGFARLVSEDLGATHISTQVKGSAGYVDP... | PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 52879
Sequence Length: 470
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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P47866 | MDAALLLSLLEANCSLALAEELLLDGWGEPPDPEGPYSYCNTTLDQIGTCWPQSAPGALVERPCPEYFNGIKYNTTRNAYRECLENGTWASRVNYSHCEPILDDKQRKYDLHYRIALIINYLGHCVSVVALVAAFLLFLVLRSIRCLRNVIHWNLITTFILRNITWFLLQLIDHEVHEGNEVWCRCVTTIFNYFVVTNFFWMFVEGCYLHTAIVMTYSTEHLRKWLFLFIGWCIPCPIIVAWAVGKLYYENEQCWFGKEPGDLVDYIYQGPIILVLLINFVFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLG... | Function: G-protein coupled receptor for CRH (corticotropin-releasing factor), UCN (urocortin), UCN2 and UCN3. Has high affinity for UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promote... |
O42603 | MDSTIFEIIIDEFDANCSLLDAFQDSFLHSESSSFFGFEGPYCSATIDQIGTCWPRSLAGELVERPCPDSFNGIRYNTTRNVYRECFENGTWASWMNYSQCVPILDNKRKYALHYKIALIINYLGHCISILALVIAFLLFLCLRSIRCLRNIIHWNLITTFILRNIMWFLLQMIDHNIHESNEVWCRCITTIYNYFVVTNFFWMFVEGCYLHTAIVMTYSTDKLRKWVFLFIGWCIPSPIIVTWAICKLFYENEQCWIGKEPGKYIDYIYQGRVILVLLINFVFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPL... | Function: G-protein coupled receptor for CRH (corticotropin-releasing factor), UCN (urocortin), UCN2 and UCN3. Has high affinity for UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promote... |
P38892 | MPKTSYLNKNFESAHYNNVRPSYPLSLVNEIMKFHKGTRKSLVDIGCGTGKATFVVEPYFKEVIGIDPSSAMLSIAEKETNERRLDKKIRFINAPGEDLSSIRPESVDMVISAEAIHWCNLERLFQQVSSILRSDGTFAFWFYIQPEFVDFPEALNVYYKYGWSKDYMGKYLNDNQREILLNYGGEKLRSLLSDRFGDIEVTIYSPSDPNASTVTAENSQFLWRAAITLNQFKEFVKSWSIYTSWARDNPSKPDIADIFINELKEICHCEDLNVPLKIEWSTFYYLCRKRE | Function: Probable S-adenosylmethionine-dependent methyltransferase which mediates cantharidin resistance.
Sequence Mass (Da): 33785
Sequence Length: 291
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q8GY82 | MAVTSLLDTVFRRRKKKSTEFISFFEFDLDTIKAATNDFSELVGRGGFGFVYKGRLQNGQEIAVKILSTSSIRTERQFHNELIILSKLKHKNLINLLGFCTKRDQHGLVYEFMPNSSLDCFILDPHRAAQLNWEMCRNIIDGIARGLRYLHEESGLWVVHRDIKPGNILLDSDLKPKIVGFELARTMQQGENAAETTEIVGTVGYLDPEYIRSGRVSVKSDVYAFGVTILTIISRRKAWSVDGDSLIKYVRRCWNRGEAIDVIHEVMREEEREYSISEILRYIHIALLCVDENAERRPNIDKVLHWFSCFSTPLPDPTFG... | Function: Forms a complex with CRK36 that may negatively control abscisic acid (ABA) and osmotic stress signal transduction . Involved in plant response to ABA during seed germination, early seedling growth and responses to abiotic stresses by inducing the expression of ABA-responsive genes and stress-inducible genes .... |
Q9M0G5 | MASTLISSLAVVLPLTLLAPSMSMKISRIDVLGYICNNGTVSNEEAYRRSYQINLDAIRGDMRHVKFGTHEHGDPPERMYVLSQCVSDLSSDECSLCWSRATDLLSQCFPATGGWFHLDGCFVRADNYSFYQEPVSHQDTKICASDKEKSAEFKGLVKEVTKSIVEAAPYSRGFSVAKMGIRDLTVYGLGVCWRTLNDELCKLCLADGALSVTSCLPSKEGFALNAGCYLRYSNYTFYNERGLLAMSFTKENLTYIFVISMVGVLAIAAGFWCGKCFYMRTSPKKKIKGTKTKKFHLFGHLRIEKESESICTESHLMSFE... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 70182
Sequence Length: 625
Subcellular Location: Membrane
EC: 2.7.11.1
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Q9C5S8 | MSAYTSLNFLFLLTFFIGSLRVSAQLQDPTYVGHVCTNRISRNSIYFSNLQTLLTSLSSNNAYFSLGSHSLTKGQNSDMVFGLYLCKGDLSPESCRECVIFAAKDTRSRCPGGKEFLIQYDECMLGYSDRNIFMDTVTTTTIITWNTQKVTADQSDRFNDAVLSLMKKSAEEAANSTSKKFAVKKSDFSSSQSLYASVQCIPDLTSEDCVMCLQQSIKELYFNKVGGRFLVPSCNSRYEVYPFYKETIEGTVLPPPVSAPPLPLVSTPSFPPGKGKNSTVIIIAIVVPVAISVLICVAVFSFHASKRAKKTYDTPEEDDI... | Function: Involved in multiple distinct defense responses. May function as a disease resistance (R) protein.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 73402
Sequence Length: 659
Subcellular Location: Membran... |
Q9C5S9 | MSSLISFNFLFLFSFLTSSFTASAQDPFYLNHYCPNTTTYSSNSTYSTNLRTLLSSLSSRNASYSTGFQNATAGKAPDRVTGLFLCRGDVSPEVCRNCVAFSVNQTLNLCPKVREAVFYYEQCILRYSHKNILSTAITNEGEFILSNTNTISPNQKQIDGFTSFVSSTMSEAAGKAANSSRKLYTVNTELTAYQNLYGLLQCTPDLTRADCLSCLQSSINGMALSRIGARLYWPSCTARYELYPFYNESAIETPPLPPPPPPPPPRESLVSTPPISSSSLPGKSGNSTVLVVAVVVLAVLLFIALVGYCFLAKKKKKTFD... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 74501
Sequence Length: 674
Subcellular Location: Membrane
EC: 2.7.11.-
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Q0D5R3 | MRRHRPYLDGVAAAAATFLLAVLLHAPLAAGEDEPPPWVLCGPYPPSGNYSKNGTYQVNLDLLSTTLPKNTSSSPAMYATGTVGDVPDKVYGLALCRGDANASACERCVAAALRDAPRRCPLVKDVLVFYDLCQLRYSNRDFFLDDDYFVTTYTLQRSRRVGAAAAAAFDAAVAVLVNATADYAAADSSRRYGTGEEEGVDGDSDRPKIYALAQCTPDKTPEVCRTCLSTVIGQLPKEFSGRTGGGMFGVWCNFRYEVFPFFSGRPLLQLPAFVETPPPPPSPSATSGEKTKNRIGTVLAIVMPAIAAILLMVVACFCCW... | Function: Involved in disease resistance. Required for NPR1/NH1-mediated immunity to the bacterial blight pathogen Xanthomomas oryzae pv. oryzae (Xoo). Required for the benzothiadiazole (BTH)-induced immune response. Possesses kinase activity in vitro.
Location Topology: Single-pass membrane protein
Sequence Mass (Da):... |
Q8L7G3 | MSSLFPFIFLFLFSFLTSFRASAQDPRFLAYYCPNATTYSSNSTYLTNLKTLLSSLSSRNASYSTGFQNATVGQALDRVTGLFLCRGDVSPEVCRNCVTFAVNNTFSRCPNQREAVFYYEECILRYSHKNILSTAITNEGEFILRNPNHISPIQNQINQFTNLVLSNMNQIAIEAADNPRKFSTIKTELTALQTFYGLVQCTPDLSRQNCMNCLTSSINRMPFSRIGARQFWPSCNSRYELYDFYNETAIGTPPPPLPPLASPSLSDKSGNSNVVVVAVVVPIIVAVLIFIAGYCFFAKRAKKTYGTTPALDEDDKTTIE... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 73925
Sequence Length: 659
Subcellular Location: Membrane
EC: 2.7.11.-
|
O65468 | MYIVSMFGLAGLEALICFIFLFLFSFLTSFKASAQNPFYLNHDCPNRTTYSSNSTYSTNLKTLLSSFASRNASYSTGFQNIRAGQTPDRVTGLFLCRGDLSPEVCSNCVAFSVNESLTRCPNQREAVFYYEECILRYSHKNFLSTVTYEGELIMRNPNNISSIQNQRDQFIDLVQSNMNQAANEAANSSRKFSTIKTELTSLQTLYGLVQCTPDLARQDCFSCLTSSINRMMPLFRIGARQFWPSCNSRYELYAFYNETAIGTPSPPPLFPGSTPPLTSPSIPGKSGNSTVLVVAIVVLAVLLFIALVGYCFLAQRTKKT... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 75412
Sequence Length: 676
Subcellular Location: Membrane
EC: 2.7.11.-
|
Q04929 | MAGQFDSEDRGSWYWGRLSRGDAVSLLQGQRHGTFLVRDSGSIPGDFVLSVSESSRVSHYIVNSLGPAGGRRAGGEGPGAPGLNPTRFRIGDQEFDSLPSLLEFYKIHYLDTTTLIEPVSRSRQNSGVILRQEEVEYVRALFDFNGNDDEDLPFKKGDILKIRDKPEEQWWNAEDMDGKRGMIPVPYVEKCRPSSASVSTLTGGNQDSSHPQPLGGPEPGPYAQPSINTPLPNLQNGPFYARVIQKRVPNAYDKTALALEVGELVKVTKINMSGQWEGECNGKRGHFPFTHVRLLDQQNPDEDFS | Function: May mediate attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility (By similarity). Involved in cell branching and adhesion (By similarity). May regulate the EFNA5-EPHA3 signaling (By similarity).
PTM: P... |
P46108 | MAGNFDSEERSSWYWGRLSRQEAVALLQGQRHGVFLVRDSSTSPGDYVLSVSENSRVSHYIINSSGPRPPVPPSPAQPPPGVSPSRLRIGDQEFDSLPALLEFYKIHYLDTTTLIEPVSRSRQGSGVILRQEEAEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVPYVEKYRPASASVSALIGGNQEGSHPQPLGGPEPGPYAQPSVNTPLPNLQNGPIYARVIQKRVPNAYDKTALALEVGELVKVTKINVSGQWEGECNGKRGHFPFTHVRLLDQQNPDEDFS | Function: Involved in cell branching and adhesion mediated by BCAR1-CRK-RAPGEF1 signaling and activation of RAP1.
PTM: Phosphorylated on Tyr-221 upon cell adhesion. Results in the negative regulation of the association with SH2- and SH3-binding partners, possibly by the formation of an intramolecular interaction of pho... |
Q64010 | MAGNFDSEERSSWYWGRLSRQEAVALLQGQRHGVFLVRDSSTSPGDYVLSVSENSRVSHYIINSSGPRPPVPPSPAQPPPGVSPSRLRIGDQEFDSLPALLEFYKIHYLDTTTLIEPVARSRQGSGVILRQEEAEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVPYVEKYRPASASVSALIGGNQEGSHPQPLGGPEPGPYAQPSVNTPLPNLQNGPIYARVIQKRVPNAYDKTALALEVGELVKVTKINVSGQWEGECNGKRGHFPFTHVRLLDQQNPDEDFS | Function: Involved in cell branching and adhesion mediated by BCAR1-CRK-RAPGEF1 signaling and activation of RAP1.
PTM: Phosphorylated on Tyr-221 upon cell adhesion. Results in the negative regulation of the association with SH2- and SH3-binding partners, possibly by the formation of an intramolecular interaction of pho... |
Q8NSP8 | MMEKIRLILLSSRPISWINTAYPFGLAYLLNAGEIDWLFWLGIVFFLIPYNIAMYGINDVFDYESDMRNPRKGGVEGAVLPKSSHSTLLWASAISTIPFLVILFIFGTWMSSLWLTLSVLAVIAYSAPKLRFKERPFIDALTSSTHFTSPALIGATITGTSPSAAMWIALGSFFLWGMASQILGAVQDVNADREANLSSIATVIGARGAIRLSVVLYLLAAVLVTTLPNPAWIIGIAILTYVFNAARFWNITDASCEQANRSWKVFLWLNYFVGAVITILLIAIHQI | Function: Catalyzes the elongation of the C(40) carotenoid all-trans-lycopene to the acyclic C(50) carotenoid flavuxanthin during decaprenoxanthin biosynthesis . Acts as a bifunctional enzyme that catalyzes the elongation of lycopene by attaching a C(5) isoprene unit at C-2, as well as the hydroxylation of the new isop... |
P54976 | MAFEQRIEAAMAAAIARGQGSEAPSKLATALDYAVTPGGARIRPTLLLSVATACGDDRPALSDAAAVALELIHCASLVHDDLPCFDDAEIRRGKPTVHRAYSEPLAILTGDSLIVMGFEVLARAAADQPQRALQLVTALAVRTGMPMGICAGQGWESESQINLSAYHRAKTGALFIAATQMGAIAAGYEAEPWEELGARIGEAFQVADDLRDALCDAETLGKPAGQDEIHARPNAVREYGVEGAAKRLKDILGGAIASIPSCPGEAMLAEMVRRYAEKIVPAQVAARV | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the condensation of farnesyl diphosphate (FPP) and isopentenyl diphosphate (IPP) to yield geranylgeranyl diphosphate (GGPP) needed for biosynthesis of carotenoids and diterpenes.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (... |
P48368 | MKPLQTNFNLLTYLYERKEIVEDTLNKSIPRGNPTFIYDSIRYSLSAGGKRIRPILCLASCELAGGTMEMALPTACALEMIHTMSLIHDDLPAMDNDSYRRGKPTNHIIYGEDLAILAGDALLAYAFEFIATQTKNVPADLIVKVIAQVAHSVTTSGLVGGQIIDLSSEGKSDTTLETLNFIHIHKTGALLEAAVLSGALLAGAKEKDMNRFLRYAQNIGLAFQIIDDVLDIISTEEKLGKSIGKDLKTQKATYPSFWGVEESIKQAELLVEEAKEEILYFDNKAIPLIAIADFIVNRNN | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the condensation of farnesyl diphosphate (FPP) and isopentenyl diphosphate (IPP) to yield geranylgeranyl diphosphate (GGPP) needed for biosynthesis of carotenoids and diterpenes.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (... |
P22873 | MVSGSKAGVSPHREIEVMRQSIDDHLAGLLPETDSQDIVSLAMREGVMAPGKRIRPLLMLLAARDLRYQGSMPTLLDLACAVELTHTASLMLDDMPCMDNAELRRGQPTTHKKFGESVAILASVGLLSKAFGLIAATGDLPGERRAQAVNELSTAVGVQGLVLGQFRDLNDAALDRTPDAILSTNHLKTGILFSAMLQIVAIASASSPSTRETLHAFALDFGQAFQLLDDLRDDHPETGKDRNKDAGKSTLVNRLGADAARQKLREHIDSADKHLTFACPQGGAIRQFMHLWFGHHLADWSPVMKIA | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the condensation of farnesyl diphosphate (FPP) and isopentenyl diphosphate (IPP) to yield geranylgeranyl diphosphate (GGPP) needed for biosynthesis of carotenoids and diterpenes.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (... |
B1XJV9 | MVVADAHTQGFSLAQYLQEQKTIVETALDQSLVITEPVTIYEAMRYSLLAGGKRLRPILCLAACEMLGGTAAMAMNTACALEMIHTMSLIHDDLPAMDNDDLRRGKPTNHKVYGEDIAILAGDALLSYAFEYVARTPDVPAERLLQVIVRLGQAVGAEGLVGGQVVDLESEGKTDVAVETLNFIHTHKTGALLEVCVTAGAILAGAKPEEVQLLSRYAQNIGLAFQIVDDILDITATAEELGKTAGKDLEAQKVTYPSLWGIEKSQAEAQKLVAEAIASLEPYGEKANPLKALAEYIVNRKN | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the sequential condensation of three molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to yield geranylgeranyl diphosphate (GGPP). Thereby, is a key enzyme for the biosynthesis of terpenenoids.
Catalytic Activity: dimethylall... |
P54906 | MSALRPPARGGLGLSRLGVRLAGSRRFQLIAERVPFLRRIGRREGEELFDIVAGFVHSQVLYALVELRVLHLVAEGPQTVQALAAATGLAPERMQLLLQGGAALKLLTRRRDGQFDLAVRGAAFLAVPGLEAMVGHHHVLYRDLADPVAFLKGETEPELARFWPYVFGAGGATDPEVTAKYSRLMTESQGLVAEDALRLVDLMGVRRLMDVGGGTGAFLAAVGRAYPLMELMLFDLPVVAEAAPQRLTEAGLAGRFTVHGGSFRDDPLPLGADAISLVRVLFDHSDETVKLLLHRVREALPAGGRVIVAEAMSGGARPHR... | Function: Methyltransferase that mediates the O-methylation of 1-hydroxy carotenoids. Converts hydroxyneurosporene to methoxyneurosporene or demethylspheroidene to spheroidene. Also able to produce spirilloxanthin (By similarity).
Catalytic Activity: demethylspheroidene + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-h... |
D5AP78 | MPKDDHTGATADRTAQPTGTGKQPLVPGQPGAAPVQPGRVNFFTRIALSQRLHEIFERLPLMNRVTRREGEALFDIVSGFVQSQVLLAIVEFRVLHILAGASWPLPQLAERTGLAEDRLAVLMQAAAALKLVKFRRGLWQLAPRGAAFITVPGLEAMVRHHPVLYRDLADPVAFLKGDIEPELAGFWPYVFGPLAQEDAGLAERYSQLMADSQRVVADDTLRLVDLRDAKRVMDVGGGTGAFLRVVAKLYPELPLTLFDLPHVLSVADRFSPKLDFAPGSFRDDPIPQGADVITLVRVLYDHPDSVVEPLLAKVHAALPP... | Function: Methyltransferase that mediates the O-methylation of 1-hydroxy carotenoids. Converts hydroxyneurosporene to methoxyneurosporene or demethylspheroidene to spheroidene. Also able to produce spirilloxanthin.
Catalytic Activity: demethylspheroidene + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + sp... |
Q02861 | MASEGGSVRHVIVVGAGPGGLSAAINLAGQGFRVTVVEKDAVPGGRMKGLTLGASGEYAVDTGPSILQLPGVLEQIFRRAARRLEDYVKLLPLDVNTRVHFWDGTHLDTTRHLDRMEAELAKFGPRQASALRQWMEDGREKYGIAYQKFICTSADNLGYYAPWRLAPTLRFKPWQTLYRQLDGFFHDDRVTYALAYPSKYLGLHPTTCSSVFSVIPFLELAFGVWHVEGGFRELSRGMMRCARDLGATFRMGTPVEKVRVDAGRAVGVKLVGGEVLDADAVVVNADLAYAARSLIPAEAREGSRLTDAALERAKYSCSTF... | Function: Dehydrogenates carotenes in the trans conformation: converts all-trans-zeta-carotene into all-trans-lycopene, one of the last dehydrogenation steps of lycopene biosynthesis.
Catalytic Activity: 2 A + all-trans-zeta-carotene = 2 AH2 + all-trans-lycopene
Sequence Mass (Da): 58421
Sequence Length: 529
Pathway: C... |
P21334 | MAETQRPRSAIIVGAGAGGIAVAARLAKAGVDVTVLEKNDFTGGRCSLIHTKAGYRFDQGPSLLLLPGLFRETFEDLGTTLEQEDVELLQCFPNYNIWFSDGKRFSPTTDNATMKVEIEKWEGPDGFRRYLSWLAEGHQHYETSLRHVLHRNFKSILELADPRLVVTLLMALHPFESIWHRAGRYFKTDRMQRVFTFATMYMGMSPFDAPATYSLLQYSELAEGIWYPRGGFHKVLDALVKIGERMGVKYRLNTGVSQVLTDGGKNGKKPKATGVQLENGEVLNADLVVVNADLVYTYNNLLPKEIGGIKKYANKLNNRK... | Function: Phytoene desaturase involved in the carotenoid biosynthesis pathway . Converts phytoene into 3,4-didehydrolycopene via the intermediates phytofluene, zeta-carotene, neurosporene and lycopene, by introducing up to five double bonds into phytoene . Is also able to desaturate 1-hydroxyneurosporene into 1-hydroxy... |
P21685 | MKPTTVIGAGFGGLALAIRLQAAGIPVLLLEQRDKPGGRAYVYEDQGFTFDAGPTVITDPSAIEELFALAGKQLKEYVELLPVTPFYRLCWESGKVFNYDNDQTRLEAQIQQFNPRDVEGYRQFLDYSRAVFKEGYLKLGTVPFLSFRDMLRAAPQLAKLQAWRSVYSKVASYIEDEHLRQAFSFHSLLVGGNPFATSSIYTLIHALEREWGVWFPRGGTGALVQGMIKLFQDLGGEVVLNARVSHMETTGNKIEAVHLEDGRRFLTQAVASNADVVHTYRDLLSQHPAAVKQSNKLQTKRMSNSLFVLYFGLNHHHDQL... | Function: Converts 15-cis-phytoene into all-trans-lycopene via the intermediary of all-trans-phytofluene, all-trans-zeta-carotene and all-trans-neurosporene, by the introduction of four double bonds.
Catalytic Activity: 15-cis-phytoene + 4 A = 4 AH2 + all-trans-lycopene
Sequence Mass (Da): 55008
Sequence Length: 492
Pa... |
P54982 | MAPPKHVIIIGAGAGGTATAARLAREGIKVTVVEKNNFGGGRCSLINHNGHRFDQGPSLYLMPKLFEEAFEALDEKIEDHVELLRCHNNYKVHFDDGDKIQLSSDLSRMKPEMERIEGPDGFLRFLDFMKESHTHYEGGVEMAIKQNFETIWKLIRLQYVPALFRLHIFDFVYSRAAKYFKTKKMRMAFTFQSMYMGMSPYDSPAVYNLLQYTEFAEGIWYPKGGFNTVIQKLENIATEKFGARFIYEAPVAKINTDDKGKKVTGVTLQSGEVIEADAVVCNADLVYAYHNLLPPCRWTTNTLAEKKLTSSSISFYWSLK... | Function: Phytoene desaturase involved in the carotenoid biosynthesis pathway. Converts phytoene into 3,4-didehydrolycopene via the intermediary of phytofluene, zeta-carotene, neurosporene and lycopene, by introducing up to five double bonds into phytoene (By similarity).
Catalytic Activity: 15-cis-phytoene + 5 A = 5 A... |
Q2XXQ9 | MILLKLYLTLAAILCQSRGTTSLDLDDLMTTNPEIQNEIINKHNDLRRTVDPPAKNMLKMSWDNIIAESAKRAALRCNQNEHTPVSGRTIGGVVCGENYFMSSNPRTWSFGIQSWFDERNYFKFGFGPTRAGVMVGHYTQKERCRPEV | Function: Blocks ryanodine receptors, and potassium channels.
PTM: Contains 8 disulfide bonds.
Sequence Mass (Da): 16858
Sequence Length: 148
Subcellular Location: Secreted
|
Q2XXQ7 | MILLKLYLTLAAILCQSRGTTSLDLDDLMTTNPEIQNEIINKHNDLRRTVDPPAKNMLKMSWDNTIAESAKRAALRCNQNEHTPVSGRTIGGVVCGENYFMSSNLRTWSFGIQSWFDERNYFKFGFGPTRAGVMVGHYTQVVWYKSYKMGCAINLCPNEPLKYFLVCQYCPGGNVVGRKYEPYAIGEPCAACPNNCDNGL | Function: Blocks ryanodine receptors, and potassium channels.
PTM: Contains 8 disulfide bonds.
Sequence Mass (Da): 22485
Sequence Length: 200
Subcellular Location: Secreted
|
Q2XXP3 | MILLKLYLTLAAILCQSRGMTSLDLDDLMTTNPEIQNEIINKHNDLRRTVDPPAKNMLKMSWDNIIAESAKRAALRCNYKEHTSIAERTIGGCGVWEKILSC | Function: Blocks ryanodine receptors, and potassium channels.
PTM: Contains 8 disulfide bonds.
Sequence Mass (Da): 11533
Sequence Length: 102
Subcellular Location: Secreted
|
Q2XXP2 | MILLKLYLTLAAILCQSRGMTSLDLDDLMTTNPEIQNEIINKHNDLRRTVDPPAKNMLKMSWDNIIAESAKRAALRCNYKEHTSIAERTIGGVVCGENYFMSSNPRTWSSSIQSWFDERNNFMFGFGPTIPGVMVGHYTQVVWYKSYKVGCAINLCPAQSLKYFQVCQYCPGGNVAGRKYEPYTIGEPCAARPKDCDNGLCTNPCAYNDDYTSCPDLTKQVGCHHPVTANC | Function: Blocks ryanodine receptors, and potassium channels.
PTM: Contains 8 disulfide bonds.
Sequence Mass (Da): 25880
Sequence Length: 231
Subcellular Location: Secreted
|
P02488 | MDVTIQHPWFKRTLGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKIQTGLDATHERAIPVAREEKPSSAPSS | Function: Contributes to the transparency and refractive index of the lens. Acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA.
PTM: Acetylation... |
P68405 | MDVTIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVLEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKVQSGLDAGHSERAIPVSREEKPSSAPSS | Function: Contributes to the transparency and refractive index of the lens. Acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA.
PTM: Acetylation... |
P24622 | MDVTIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISELMTHMWFVMHQPHAGNPKNNPVKVRSDRDKFVIFLDVKHFSPEDLTVKVLEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKVQSGLDAGHSERAIPVSREEKPSSAPSS | Function: Contributes to the transparency and refractive index of the lens. Acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA.
PTM: Acetylation... |
P02477 | MDIAIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRSVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKVTSGMDAGHSERAIPVSREEKPSSAPSS | Function: Contributes to the transparency and refractive index of the lens. Acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA.
PTM: Acetylation... |
A0A1J4UAV9 | MNMSKTTISVKLKIIDLSSEKKEFLDNYFNEYAKATTFCQLRIRRLLRNTHWLGKKEKSSKKWIFESGICDLCGENKELVNEDRNSGEPAKICKRCYNGRYGNQMIRKLFVSTKKREVQENMDIRRVAKLNNTHYHRIPEEAFDMIKAADTAEKRRKKNVEYDKKRQMEFIEMFNDEKKRAARPKKPNERETRYVHISKLESPSKGYTLNGIKRKIDGMGKKIERAEKGLSRKKIFGYQGNRIKLDSNWVRFDLAESEITIPSLFKEMKLRITGPTNVHSKSGQIYFAEWFERINKQPNNYCYLIRKTSSNGKYEYYLQY... | Cofactor: Mg(2+) is required for dsDNA cleavage.
Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary t... |
A0A2U3D0N8 | MIKVYRYEIVKPLDLDWKEFGTILRQLQQETRFALNKATQLAWEWMGFSSDYKDNHGEYPKSKDILGYTNVHGYAYHTIKTKAYRLNSGNLSQTIKRATDRFKAYQKEILRGDMSIPSYKRDIPLDLIKENISVNRMNHGDYIASLSLLSNPAKQEMNVKRKISVIIIVRGAGKTIMDRILSGEYQVSASQIIHDDRKNKWYLNISYDFEPQTRVLDLNKIMGIDLGVAVAVYMAFQHTPARYKLEGGEIENFRRQVESRRISMLRQGKYAGGARGGHGRDKRIKPIEQLRDKIANFRDTTNHRYSRYIVDMAIKEGCGT... | Cofactor: Mg(2+) is required for dsDNA cleavage.
Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary t... |
P0DW62 | MGESVKAIKLKILDMFLDPECTKQDDNWRKDLSTMSRFCAEAGNMCLRDLYNYFSMPKEDRISSKDLYNAMYHKTKLLHPELPGKVANQIVNHAKDVWKRNAKLIYRNQISMPTYKITTAPIRLQNNIYKLIKNKNKYIIDVQLYSKEYSKDSGKGTHRYFLVAVRDSSTRMIFDRIMSKDHIDSSKSYTQGQLQIKKDHQGKWYCIIPYTFPTHETVLDPDKVMGVDLGVAKAVYWAFNSSYKRGCIDGGEIEHFRKMIRARRVSIQNQIKHSGDARKGHGRKRALKPIETLSEKEKNFRDTINHRYANRIVEAAIKQG... | Cofactor: Mg(2+) is required for dsDNA cleavage.
Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary t... |
A0A482D308 | MAKNTITKTLKLRIVRPYNSAEVEKIVADEKNNREKIALEKNKDKVKEACSKHLKVAAYCTTQVERNACLFCKARKLDDKFYQKLRGQFPDAVFWQEISEIFRQLQKQAAEIYNQSLIELYYEIFIKGKGIANASSVEHYLSDVCYTRAAELFKNAAIASGLRSKIKSNFRLKELKNMKSGLPTTKSDNFPIPLVKQKGGQYTGFEISNHNSDFIIKIPFGRWQVKKEIDKYRPWEKFDFEQVQKSPKPISLLLSTQRRKRNKGWSKDEGTEAEIKKVMNGDYQTSYIEVKRGSKIGEKSAWMLNLSIDVPKIDKGVDPS... | Cofactor: Mg(2+) is required for dsDNA cleavage . Mg(2+) and Mn(2+) support ssDNA cleavage equally .
Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids... |
P35833 | MKLMVLQLLLWHSALWTVHEATPLGPARSLPQSFLLKCLEQVRKIQADGAELQERLCAAHKLCHPEELMLLRHSLGIPQAPLSSCSSQSLQLTSCLNQLHGGLFLYQGLLQALAGISPELAPTLDTLQLDVTDFATNIWLQMEDLGAAPAVQPTQGAMPTFTSAFQRRAGGVLVASQLHRFLELAYRGLRYLAEP | Function: Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes.
PTM: O-glycosylated.
Sequence ... |
P09919 | MAGPATQSPMKLMALQLLLWHSALWTVQEATPLGPASSLPQSFLLKCLEQVRKIQGDGAALQEKLVSECATYKLCHPEELVLLGHSLGIPWAPLSSCPSQALQLAGCLSQLHSGLFLYQGLLQALEGISPELGPTLDTLQLDVADFATTIWQQMEELGMAPALQPTQGAMPAFASAFQRRAGGVLVASHLQSFLEVSYRVLRHLAQP | Function: Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes.
PTM: O-glycan consists of Gal-... |
G0HV86 | MTGNSDKVRSLFLTALMVFSVFAGTIAFSGGAAAAANVSVQQAAEYDSGTVELALNGSTGSPVTTGDINIYIDGNENPSNYGVSSVDTTDDGTTGRLQFSLDQDVQPNRNLTVEVSGLTGGDNTVVAEDIDVTSQTIDADDDSGDTNAFRGEVLAIRADGGEGDADDATSSTQIVVEDSNGAVVTQDTYTANSKVYTYETENLDTGEEYEVTVGGTADENITISNLDLNVNIDDDVGDGANIDDTDTLAVNVSTTRGGEPANATLFNEDDDKVATQIKSLKGNENVVFDFGNQSADDSPYYVKVTDNQTGVSAESDQINV... | Function: S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell. In H.hispanica, the S-layer contains two different glycoproteins, Slg1 and Slg2, which share highly similar amino acid sequences.
PTM: N-glycosylated on Asn-307; this N-linked glycan is a br... |
P35206 | MSTTLLWFSSVIGYVIQTKCLSNIQSKKEISVGPNGTIATPETNGDNGNSSSLTFYLTFMYFASWLLLVPASRLWEKMRPMFVSDSDSNRNSQFDNNNSGSVTNEDVDTFSHVLDDPQPRIPAQQQKQKIISVATFKYVAKLTVLALIMIVADLTYNMALSLSPAFDVALMQNTAIFEIVTLLYGVCGISRKNYVFRNFLIMMNAVIGILIISYTKATCDMLAGKLSVNPNTGELSDPFLFDRLKGALICGLGALIMGPFAVLWNRWFCSNISKNENSAVVLVKQSTHMALIGIIGMVILLPFIPKFPSRESVESISLFY... | Function: Required for calcium regulation. May regulate calcium accumulation by a non-vacuole organelle. Also regulates the activity of CSH1 and SUR1 during mannosyl phosphorylinositol ceramide synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45442
Sequence Length: 410
Subcellular Location:... |
P21158 | MRAFATNVCTGPVDVLINNAGVSGLWCALGDVDYADMARTFTINALGPLRVTSAMLPGLRQGALRRVAHVTSRMGSLAANTDGGAYAYRMSKAALNMAVRSMSTDLRPEGFVTVLLHPGWVQTDMGGPDATLPAPDSVRGMLRVIDGLNPEHSGRFFDYQGTEVPW | Function: Cell-cell signaling protein required for fruiting body formation, a multicellular developmental program that is induced in response to starvation . Necessary for rippling, cellular aggregation, spore differentiation and for gene expression that is initiated after 6 hours of starvation . In starving cells, the... |
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