ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
B3PSB4 | MSDKAAAPKKQGRNNGAVVLMCLSFVFGMGAMSYAAVPLYRIFCQVTGYNGTTQRVEQMSSVVLDRKMRVTFDANVAPGLQWDFKPVEREVNPRIGETIQVKFTAENRSNETQRGQAVFNVTPGEAGVYFNKVQCFCFTETDLKPGEKLEMPVVFYIDPEIVNAVESKDIHTVTLSYTFYPKEGPKPLASNEGGAEKVEKKL | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 22465
Sequence Length: 202
Subcellular Location: Cell inner membrane
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Q92RG6 | MADNGQADRKERSNGVIVGTCLAFVAGMIGMAYAAVPLYDMFCRVTGYNGTTQRVEQASDLILDEKIKVTFDANVAAGLPWEFVPVQRDIDVRIGETVQIMYRAKNLASTPTTGQATFNVTPMAAGAYFNKVQCFCFTETTLEPGEEMEMPVVFFVDPEIVKPVETQGIKTLTLSYTFYPREPSKPVAQVKAKAENKL | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 21812
Sequence Length: 198
Subcellular Location: Cell inner membrane
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Q92IL2 | MSKKSNKNLAFSLLGLIISMVLLSFASVPIYNLFCKVTGYGGTTAKETVSVYSKVKGTKPIIIEFDANVDKDLPWRFIPRQQRVQIVPGQNTLVFYETENLSDNDIIGTSVYNVTPNKAGKYFVKIHCFCFEEQLLKAGERVLMPVTFYIDKDFELDPEMQDIKVLTLSYSFFKVREMSSLRGNYVSN | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 21399
Sequence Length: 188
Subcellular Location: Cell inner membrane
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Q92112 | MVLETLNPLHYNITSLVPDTMPVATVPILILMCFLFLIWNHEETSSIPGPGYCMGIGPLISHGRFLWMGVGNACNYYNKTYGDFVRVWISGEETFIISKSSSVSHVMKHWHYVSRFGSKLGLQCIGMYENGIIFNNNPAHWKEIRPFFTKALSGPGLVRMIAICVESTTEHLDRLQEVTTELGNINALNLMRRIMLDTSNKLFLGVPLDENAIVLKIQNYFDAWQALLLKPDIFFKISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLI... | Function: Catalyzes the formation of aromatic C18 estrogens from C19 androgens.
Catalytic Activity: 3 O2 + 3 reduced [NADPH--hemoprotein reductase] + testosterone = 17beta-estradiol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): ... |
Q38867 | MANPKVFFDILIGKMKAGRVVMELFADVTPRTANNFRALCTGENGIGKAGKALHYKGSAFHRIIPGFMCQGGDFTRGNGTGGESIYGSKFEDENFKLKHTGPGILSMANSGPNTNGSQFFICTEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSDMGNPSERVVIEDCGELKNPSS | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 18921
Sequence Length: 176
Subcellular Location: Cytoplasm
... |
Q8LDP4 | MAKASFILLGTLFLFGAIASIQAKEDLKEVTHKVYFDVEIDGKSAGRVVIGLFGKAVPKTAENFRALCTGEKGVGKSGKPLHYKGSKFHRIIPSFMIQGGDFTHGNGMGGESIYGQKFADENFKLKHTGPGVLSMANSGEDTNGSQFFITTVTTSWLDGRHVVFGKVVQGMDVVYKIEAEGKQSGTPKSKVVIADSGELPL | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved during embryogenesis and organ development by regulating the folding of EMB30/GNOM, and thus, by modulating its activity.
Catalytic Activity: [protein]-peptidy... |
P11372 | LGILFSNANTWKEMRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTNASPCDPTFILGCAPCNVICSIIFHNRFDYKDEHFLKLMEKFNENVRILSSPWLQICNNFPVLTDYLPGIHNTLVKNIEYTKNFIMEKVKEHQKSLDVNNPRDFIDCFLIKMDQENHLEFTLESLVTTVSDLFGAGTETTSTTLSISLLLLLKHPEVAAKVQEEIERVIGRHRSPCMQDRSRMPYTDAVIHEIQRYIDLIPINLPHAVTRDIKFRNYFIPKGMNIITSLTSVLHDEKEFPNPKVFDPGHFLDESGNFKKSDYFMPFSAGK... | 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... |
P33261 | MDPFVVLVLCLSCLLLLSIWRQSSGRGKLPPGPTPLPVIGNILQIDIKDVSKSLTNLSKIYGPVFTLYFGLERMVVLHGYEVVKEALIDLGEEFSGRGHFPLAERANRGFGIVFSNGKRWKEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICSIIFQKRFDYKDQQFLNLMEKLNENIRIVSTPWIQICNNFPTIIDYFPGTHNKLLKNLAFMESDILEKVKEHQESMDINNPRDFIDCFLIKMEKEKQNQQSEFTIENLVITAADLLGAGTETTSTTLRYALLLLLKHPEVT... | Function: A cytochrome P450 monooxygenase involved in the metabolism of polyunsaturated fatty acids (PUFA) . 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 (NADPH--hemopr... |
E9Q5K4 | MELLGLPTLALLVLVMSLSLLSVWTKMRTGGRLPPGPTPLPIIGNILQLDLKDIPASLSKLAKEYGPVYTLYFGSWPTVVLHGYDVVKEALLNQGDEFLGRGPLPIIEDSQKGHGIVFSEGERWKLLRRFSLMTLKNFGMGKRSLEERVQEEARCLVEELHKTEAQPFDPTFILACAPCNVICSILFNERFPYNDKTFLNLMDLLNKNFYQLNSIWIQMYNLWPTIMKYIPGKHREFSKRLGGVKNFILEKVKEHQESLDPANPRDYIDCFLSKIEEEKHNLKSDFNLENLAICGSNLFTAGTETTSTTLRFGLLLLVKH... | Function: A cytochrome P450 monooxygenase involved in polyunsaturated fatty acids (PUFAs) metabolism and signaling . Catalyzes preferentially the epoxidation of double bonds of PUFAs . Converts arachidonic acid (ARA, C20:4(n-6)) primarily to stereospecific products 8R,9S-epoxyeicosatrienoate (EET) and 11R,12S-EET . Pla... |
Q29510 | MDLFIVLVICLSCLLLVSLLKQSYARRKLPPGPTAFPLVGNVLQLDRKNISKSISMLAKEYGPVFTVYFGTKPSVVLHGYEAVKEALVDHGEEFSGRVTVPVFDRYAQGAGLFASQGELWKETRRFTLTVLRNMGMGKKTIEDRIQEEASCLVKALKETNASPCDPSSLLFCVPCNVICSIIFQNRFEYNDQTFQTLVKHFLDSIRLFNTPWMQLYNTFPILHYLPGSHHELFKVFNDQMKFFSEKIREHQESLDHNNPRDFIDYLLIKMEKEKHNKQSQFTMHHLLVTIWDVFDAGSQTTSSTMQFGLLLLMKHPEIAA... | 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... |
Q29478 | LVSTPWIELFNAFPSLLRHFPGSHNTIFKNMTEQRKFILEEIKKHQESLDLNNPQDFIDYFLIKMEKEKHNKHSEFTMDNLITTVWDVFSAGTETTSLTLRYGLLLLLKHPEVTAKVQEEIDRVVGRNRSPCMQDRSRMPYTDAVLHEIQRYIDLVPSNLPHVATQDVKFREYLIPKGTAILTSLTSVLHDGKEFPNPGQFDPAHFLDESGNFKKTDHFMAFSAGKRVCVGEGLARMELFLLLVSILQHFTLKPVVDPKHIDIAPSFKGMLSIPPFCEMCFIPV | 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... |
P10633 | MELLNGTGLWSMAIFTVIFILLVDLMHRRHRWTSRYPPGPVPWPVLGNLLQVDLSNMPYSLYKLQHRYGDVFSLQKGWKPMVIVNRLKAVQEVLVTHGEDTADRPPVPIFKCLGVKPRSQGVILASYGPEWREQRRFSVSTLRTFGMGKKSLEEWVTKEAGHLCDAFTAQAGQSINPKAMLNKALCNVIASLIFARRFEYEDPYLIRMVKLVEESLTEVSGFIPEVLNTFPALLRIPGLADKVFQGQKTFMALLDNLLAENRTTWDPAQPPRNLTDAFLAEVEKAKGNPESSFNDENLRMVVVDLFTAGMVTTATTLTWA... | 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... |
P12938 | MELLAGTGLWPMAIFTVIFILLVDLMHRRQRWTSRYPPGPVPWPVLGNLLQVDLCNMPYSMYKLQNRYGDVFSLQMGWKPVVVINGLKAVQELLVTCGEDTADRPEMPIFQHIGYGHKAKGVVLAPYGPEWREQRRFSVSTLRNFGVGKKSLEQWVTDEASHLCDALTAEAGRPLDPYTLLNKAVCNVIASLIYARRFDYGDPDFIKVLKILKESMGEQTGLFPEVLNMFPVLLRIPGLADKVFPGQKTFLTMVDNLVTEHKKTWDPDQPPRDLTDAFLAEIEKAKGNPESSFNDANLRLVVNDLFGAGMVTTSITLTWA... | 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... |
P79152 | RHEVELVAQTTIFIFGGYETTSTSLSFIIYELATHPDVQQKLQEEIDATFPNKAPPTYDALVQMEYLDMVVNETLRMFPIAGRLERLCKKDVEIHGVSIPKGTTVMVPLFVLHNNPEFWPEPEEFRPERFSKKNKDGINPYVYLPFGTGPRNCVGMRFALMNIKLALVRILQNFSFIPCKETQIPLKLYTQGLTQPEQPVILKVAPRGLGPQAEPDFL | 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... |
O42563 | MMSFLPYFSAETWTLLALLITLIVVYGYWPYGVFTKMGIPGPKPLPYFGTMLEYKKGFTNFDTECFQKYGRIWGIYDGRQPVLCIMDKSMIKTVLIKECYNIFTNRRNFHLNGELFDALSVAEDDTWRRIRSVLSPSFTSGRLKEMFGIMKQHSSTLLSGMKKQADKDQTIEVKEFFGPYSMDVVTSTAFSVDIDSLNNPSDPFVSNVKKMLKFDLFNPLFLLVALFPFTGPILEKMKFSFFPTAVTDFFYASLAKIKSGRDTGNSTNRVDFLQLMIDSQKGSDTKTGEEQTKGLTDHEILSQAMIFIFAGYETSSSTMS... | 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... |
P79102 | MELIPSFSMETWVLLATSLVLLYIYGTYSYGLFKKLGIPGPRPVPYFGSTMAYHKGIPEFDNQCFKKYGKMWGFYEGRQPMLAITDPDIIKTVLVKECYSVFTNRRIFGPMGIMKYAISLAWDEQWKRIRTLLSPAFTSGKLKEMFPIIGQYGDMLVRNLRKEAEKGNPVNMKDMFGAYSMDVITGTAFGVNIDSLNNPHDPFVEHSKNLLRFRPFDPFILSIILFPFLNPVFEILNITLFPKSTVDFFTKSVKKIKESRLTDKQMNRVDLLQLMINSQNSKEIDNHKALSDIELVAQSTIFIFGGYETTSSTLSFIIYE... | 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... |
Q9Y6A2 | MSPGLLLLGSAVLLAFGLCCTFVHRARSRYEHIPGPPRPSFLLGHLPCFWKKDEVGGRVLQDVFLDWAKKYGPVVRVNVFHKTSVIVTSPESVKKFLMSTKYNKDSKMYRALQTVFGERLFGQGLVSECNYERWHKQRRVIDLAFSRSSLVSLMETFNEKAEQLVEILEAKADGQTPVSMQDMLTYTAMDILAKAAFGMETSMLLGAQKPLSQAVKLMLEGITASRNTLAKFLPGKRKQLREVRESIRFLRQVGRDWVQRRREALKRGEEVPADILTQILKAEEGAQDDEGLLDNFVTFFIAGHETSANHLAFTVMELSR... | Function: P450 monooxygenase that plays a major role in cholesterol homeostasis in the brain. Primarily catalyzes the hydroxylation (with S stereochemistry) at C-24 of cholesterol side chain, triggering cholesterol diffusion out of neurons and its further degradation . By promoting constant cholesterol elimination in n... |
Q9VCW1 | MFSLILLAVTLLTLAWFYLKRHYEYWERRGFPFEKHSGIPFGCLDSVWRQEKSMGLAIYDVYVKSKERVLGIYLLFRPAVLIRDADLARRVLAQDFASFHDRGVYVDEERDPLSANIFSLRGQSWRSMRHMLSPCFTSGKLKSMFSTSEDIGDKMVAHLQKELPEEGFKEVDIKKVMQNYAIDIIASTIFGLDVNSFENPDNKFRKLVSLARANNRFNAMFGMMIFLVPSIAQFLFRIGFKNPVGLAMLQIVKETVEYREKHGIVRKDLLQLLIQLRNTGKIDENDEKSFSIQKTPDGHIKTISLEAITAQAFIFYIAGQ... | 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): 59182
Sequence Length: 515
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9VFP1 | MIGIYLLIAAVTLLYVYLKWTFSYWDRKGFPSTGVSIPFGALESVTKGKRSFGMAIYDMYKSTKEPVIGLYLTLRPALLVRDAQLAHDVLVKDFASFHDRGVYVDEKNDPMSASLFQMEGASWRALRNKLTPSFTSGKLKAMFETSDSVGDKLVDSIRKQLPANGAKELELKKLMATYAIDIIATTIFGLDVDSFADPNNEFQIISKKVNRNNIEDIIRGTSSFLYPGLEKFFVKIGWKQEATERMRELSNRTVDLREQNNIVRKDLLQLLLQLRNQGKINTDDNIWSAESTKNGVKSMSKDLIAGQLFLFYVAGYETTA... | 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): 57384
Sequence Length: 508
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9V674 | MVLTEVLFVVVAALVALYTWFQRNHSYWQRKGIPYIPPTPIIGNTKVVFKMENSFGMHLSEIYNDPRLKDEAVVGIYSMNKPGLIIRDIELIKSILIKDFNRFHNRYARCDPHGDPLGYNNLFFVRDAHWKGIRTKLTPVFTSGKVKQMYTLMQEIGKDLELALQRRGEKNSGSFITEIKEICAQFSTDSIATIAFGIRANSLENPNAEFRNYGRKMFTFTVARAKDFFVAFFLPKLVSLMRIQFFTADFSHFMRSTIGHVMEERERSGLLRNDLIDVLVSLRKEAAAEPSKPHYAKNQDFLVAQAGVFFTAGFETSSST... | Function: Necessary and sufficient for resistance to insecticides DDT and imidacloprid. May be involved in the metabolism of insect hormones.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 59867
Sequence Length: 524
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9V675 | MELVLLILVASLIGIAFLALQQHYSYWRRMGVREIRPKWIVGNLMGLLNMRMSPAEFISQLYNHPDAENEPFVGIHVFHKPALLLRDPEMVRNILVKDFAGFSNRYSSSDPKGDPLGSQNIFFLKNPAWKEVRLKLSPFFTGNRLKQMFPLIEEVGASLDAHLRQQPLHNERMRCFDLEAKELCALYTTDVIATVAYGVSANSFTDPKCEFRRHGRSVFEFNLLRAAEFTLVFFLPHLVPFVRFKVVPAEATRFLRKTINYVMSEREKSGQKRNDLIDILIEFRRSTQLAKASGIKDQFVFEGDILVAQAVLFFTAGFES... | 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): 59608
Sequence Length: 519
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q964R1 | MFEFGSIIVTVIAVFITIPICLYLFLTRHFNFWKKRGVIYVRPLPFFGNLKDVLLQKKYIGYYLKDIYEENINKPYVGIFAFDQPALLVNDLEIVKNILVKDSRNFIDRMVKVDESLSPLNANAIFALRGQKWKHVRTSLTPTFTTGKMKNMFYLVDKCGQQLVLFIEKFAKAENPVAVKDAVERFTMDVTAMCAFGIECNSLQDPKAEFSNLLHRIFQLSFTSAVANLATFFAPWVQNFFRLKLMDSEIEDRIRDIVWRAVHLREKTGEKRNDLLDYLMELRTSETSKLDGDDFVAQAFGFLVAGFHTSSMTLTFALYE... | Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57918
Sequence Length: 501
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q964R0 | MVTITGCALCDALVILATLIVAAYLYYAVRFTYWKRKGVVNPKPLPVFGNFLPSVLQKRSPGQILWDIYKAAEAPFVGFYIFARPAILIKDPNIIKHVLVKDFNAFSDRHASAAESDTLGSQNLFTLNGAPWKYLRVKLSPTFTSGRMKKMYPLVESCAKQLQDYLKENCNTKAIEVKETTAKYATDVISTCAFGIESNSLKDPNAEFREFGRKIFEFTRYRTFEVMALFFSPGLVKFLNGNFFTKETTEFLRKVFWDTINFRESNKISRDDFMDLLIQLKNKGTIDNEDGEVTEKVDKIDKDSHLFEFTGDNLVSQPAL... | Location Topology: Peripheral membrane protein
Sequence Mass (Da): 59619
Sequence Length: 524
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9GQM9 | MTLVDWFLDTIALLLGLLHIWIARHFQHWEEKGVHHVAPQPLVGSMLRLLTFSVSPAVFIQGVHEAAGSHPYIGFYIFGRPALLVRDPSLLQHILVKDFSNFTDRLTSSNKHKDPVGAANLFCIKGNRWRQIRACITHTFSTARLKIMFSRVLNSASVTRDYILERGNQPINVKDLFVRTSLDSMCSTLFGIESSTLYNSEAQFLHYGHKMMRWTPYRALEALAHFFSPELLNVFDTRLFECESTEFLINAFSEAITEREKTGLYCSDLVDSLIQLKKQLIDVSEHEVLGQAMLFFAAGFETTSSAMAFAMYELALHPEI... | Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57163
Sequence Length: 503
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9VRI9 | MIAVFSLIAAALAVGSLVLLPVVLRGGCLLVVTIVWLWQILHFWHWRRLGVPFVPAAPFVGNVWNLLRGACCFGDQFRELYESKEAAGRAFVGIDVLHNHALLLRDPALIKRIMVEDFAQFSSRFETTDPTCDTMGSQNLFFSKYETWRETHKIFAPFFAAGKVRNMYGLLENIGQKLEEHMEQKLSGRDSMELEVKQLCALFTTDIIASLAFGIEAHSLQNPEAEFRRMCIEVNDPRPKRLLHLFTMFFFPRLSHRVGTHLYSEEYERFMRKSMDYVLSQRAESGENRHDLIDIFLQLKRTEPAESIIHRPDFFAAQAA... | 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): 60519
Sequence Length: 529
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9V676 | MLLIWLLLLTIVTLNFWLRHKYDYFRSRGIPHLPPSSWSPMGNLGQLLFLRISFGDLFRQLYADPRNGQAKIVGFFIFQTPALMVRDPELIRQVLIKNFNNFLNRFESADAGDPMGALTLPLAKYHHWKESRQCMSQLFTSGRMRDVMYSQMLDVASDLEQYLNRKLGDRLERVLPLGRMCQLYTTDVTGNLFYSLNVGGLRRGRSELITKTKELFNTNPRKVLDFMSVFFLPKWTGVLKPKVFTEDYARYMRHLVDDHHEPTKGDLINQLQHFQLSRSSNHYSQHPDFVASQAGIILLAGFETSSALMGFTLYELAKAP... | 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): 57845
Sequence Length: 501
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9V979 | MDLMHRTLLTALGALSVVYALVKFSLGYWKRRGILHEKPKFLWGNIKGVVSGKRHAQDALQDIYTAYKGRAPFVGFYACLKPFILALDLKLVHQIIFTDAGHFTSRGLYSNPSGEPLSHNLLQLDGHKWRSLHAKSAEVFTPANMQKLLVRLSQISSRIQRDLGEKSLQTINISELVGAYNTDVMASMAFGLVGQDNVEFAKWTRNYWADFRMWQAYLALEFPLIARLLQYKSYAEPATAYFQKVALSQLQLHRRRDRQPLQTFLQLYSNAEKPLTDIEIAGQAFGFVLAGLGPLNATLAFCLYELARQPEVQDRTRLEI... | 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): 55508
Sequence Length: 488
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9VRB3 | MVYSTNILLAIVTILTGVFIWSRRTYVYWQRRRVKFVQPTHLLGNLSRVLRLEESFALQLRRFYFDERFRNEPVVGIYLFHQPALLIRDLQLVRTVLVEDFVSFSNRFAKCDGRSDKMGALSLFLAKQPEWREIRTRLAPAFAGAKLKQMFSLMEEIGCDLEWYLKRLTRDLRRGDAERGAIVSIKDVCDLYNTDMIASIAFGLRSYSLRNTQSEIGSHCQDLFRPNVRRIIDLFVIFYLPKLVPLLRPKLFTEPHAEFLRRVIQLVIEERERGGDLRNDLIEMLLTLKKEADLQQDKSHFTHHRDFLAAQAASFEVAGI... | 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): 60763
Sequence Length: 520
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9V9L1 | MLLLLLLGSLTIVFYIWQRRTLSFWERHGVKYIRPFPVVGCTREFLTAKVPFFEQIQKFHEAPGFENEPFVGVYMTHRPALVIRDLELIKTVMIKKFQYFNNRVLQTDPHNDALGYKNLFFARSPGWRELRTKISPVFTSGKIKQMYPLMVKIGKNLQDSAERLGSGTEVQVKDLCSRFTTDLIATIAFGVEANALQDAKSEFFYHNRAIFSLTLSRGIDFAIIFMIPALASLARVKLFSRETTKFIRSSVNYVLKERERTGEKRNDLIDILLALKREAAANPGKMSKEVDLDYLVAQAAVFQTAGFETSASTMTMTLYE... | 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): 59321
Sequence Length: 514
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q96242 | MASISTPFPISLHPKTVRSKPLKFRVLTRPIKASGSETPDLTVATRTGSKDLPIRNIPGNYGLPIVGPIKDRWDYFYDQGAEEFFKSRIRKYNSTVYRVNMPPGAFIAENPQVVALLDGKSFPVLFDVDKVEKKDLFTGTYMPSTELTGGYRILSYLDPSEPKHEKLKNLLFFLLKSSRNRIFPEFQATYSELFDSLEKELSLKGKADFGGSSDGTAFNFLARAFYGTNPADTKLKADAPGLITKWVLFNLHPLLSIGLPRVIEEPLIHTFSLPPALVKSDYQRLYEFFLESAGEILVEADKLGISREEATHNLLFATCF... | Catalytic Activity: (13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate = (9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate + H2O
Sequence Mass (Da): 58197
Sequence Length: 518
Pathway: Lipid metabolism; oxylipin biosynthesis.
Subcellular Location: Plastid
EC: 4.2.1.92
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P48417 | MASSALNNLVAVNPNTLSPSPKSTPLPNTFSNLRRVSAFRPIKASLFGDSPIKIPGITSQPPPSSDETTLPIRQIPGDYGLPGIGPIQDRLDYFYNQGREEFFKSRLQKYKSTVYRANMPPGPFIASNPRVIVLLDAKSFPVLFDMSKVEKKDLFTGTYMPSTELTGGYRILSYLDPSEPNHTKLKQLLFNLIKNRRDYVIPEFSSSFTDLCEVVEYDLATKGKAAFNDPAEQAAFNFLSRAFFGVKPIDTPLGKDAPSLISKWVLFNLAPILSVGLPKEVEEATLHSVRLPPLLVQNDYHRLYEFFTSAAGSVLDEAEQ... | Function: Involved in the biosynthesis of jasmonic acid, a growth regulator that is implicated also as a signaling molecule in plant defense. Acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides.
Catalytic Activity: (13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate = (9Z,13S... |
P22680 | MMTTSLIWGIAIAACCCLWLILGIRRRQTGEPPLENGLIPYLGCALQFGANPLEFLRANQRKHGHVFTCKLMGKYVHFITNPLSYHKVLCHGKYFDWKKFHFATSAKAFGHRSIDPMDGNTTENINDTFIKTLQGHALNSLTESMMENLQRIMRPPVSSNSKTAAWVTEGMYSFCYRVMFEAGYLTIFGRDLTRRDTQKAHILNNLDNFKQFDKVFPALVAGLPIHMFRTAHNAREKLAESLRHENLQKRESISELISLRMFLNDTLSTFDDLEKAKTHLVVLWASQANTIPATFWSLFQMIRNPEAMKAATEEVKRTLE... | Function: A cytochrome P450 monooxygenase involved in the metabolism of endogenous cholesterol and its oxygenated derivatives (oxysterols) . 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 cytochro... |
O46491 | MMSISLLGGIVTAVCCCLWLLLGMRRRQTGEPPLENGIIPYLGCALQFGANPLEFLRANQRKHGHIFTCQLMGNYVHFITNPLSYHKVLCHGKYLDWKKFHFTASAKAFGHRSIDPSDGNTTDNINKTIIKTLQGDALNLLAAAMMENLQLVLRPQVAPQPEKPAWVTEGMYSFCYRVMFEAGYVTLFGKDPIGHDAQKALILNNLDNFKQFDKIFPALVAGFPIHVFKTGHYAREKLAEGLRLQKLRKRDHISELVRFLNDTLSTLDDAEKAKSLLAVLWASQANTIPATFWCLFQTIRSPEAMKAASEEVNKTLEKAG... | Function: A cytochrome P450 monooxygenase involved in the metabolism of endogenous cholesterol and its oxygenated derivatives (oxysterols). 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 cytochrom... |
P51542 | MITIFWIWGICLSVCCCLWLILGLRRRRMGEPPLEKGWIPYLGCALQFGANPLDFLRANQRKYGHVFTCKLMGKYVHFITNSLSYHKVLCHGKYFDWKKFHFTTSAKAFGHRSIDPRDGNTTENINNTFNKTLQGDALISLTDAMMENLQLTLRRPEPKSRAWVTEGMYSFCYRVMFEAGYLTLFGRELTRQDAQRAFILNSLEDFKQFDKVFPALVAGLPIHIFMTAHNAREKLAEGLKHDNLRTRDHISELIRLRMFLNDTLSTFDAMEKAKTHLAILWASQANTIPATFWSLFHMMRSSEALKAATEEVNKALEDAD... | Function: A cytochrome P450 monooxygenase involved in the metabolism of endogenous cholesterol and its oxygenated derivatives (oxysterols) (By similarity). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NAD... |
B6YVF3 | MKLVLIDGEHYPDVISWAIKKLGDVCCAVFLGGSEKIGSIGEVERKIGVKVYHSPNYLDALRRALEENKVDEVVDLSDEPVLNYEDRFRIASLCMLYGVSYRGADFHFKPKPLKKTKKPSLAVIGTGKRVGKTAVSGFIARTLKEIAKPVIVTMGRGGPEEPELIEGDKFEITPEFLLKFAESGKHAASDHFEDALTSRVTTIGCRRCGGGMAGFPFFDVVDEGVKLAENLPNDLIILEGSGATFPPYRADRYVVVVGAKQKLDFVRGYFGTFRVSLADIVVVTMADSVGEERWKALRDAILEINPDVDLHFIAFRPRPL... | Function: Catalyzes the formation of cyclic 2,3-diphosphoglycerate (cDPG) by formation of an intramolecular phosphoanhydride bond at the expense of ATP.
Catalytic Activity: (2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-2,3-bisphosphoglycerate + phosphate
Sequence Mass (Da): 47469
Sequence Length: 432
Su... |
C6A0T3 | MRMVLIDGEHYPDVTAWAIKKIGDVSCAVFLGGTEKIGDMKSLEEKIGVKLYYGESYISNIKKAINENKIGEVIDLSDEPVLNYEDRFRIAAVLLKHGIKYKGADFEFSPKEMVQINKPSLTILGTGKRVGKTAISGFVARTLKEISKPIIVTMGRGGPEEPEIIEGNKLEITPDFLVRVAESGKHAASDHFEDALTSRVITIGCRRCGGGMVGFSFFDIVNKGIKLAEKLEGDIVILEGSGATFPAVKADKYITVVGATQRIEFIKSYFGPFRIGLADLIVITLADMVSKEKIEKIQKIIESINPDAEIHLTAFKPRPL... | Function: Catalyzes the formation of cyclic 2,3-diphosphoglycerate (cDPG) by formation of an intramolecular phosphoanhydride bond at the expense of ATP.
Catalytic Activity: (2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-2,3-bisphosphoglycerate + phosphate
Sequence Mass (Da): 47998
Sequence Length: 434
Su... |
P56947 | MKILKTQTLRGPNYWSIRRQKLIQMRLDLEDVAEKPSNLIPGFYEGLVKILPSLVEHFCSRDHRGGFLERVQEGTYMGHIVEHIALELQELAGMPVGFGRTRETSTPGIYNVVFEYVYEEAGRYAGRVAVRLCNSIITTGAYGLDELAQDLSDLKDLRANSALGPSTETIIKEAEARQIPWMLLSARAMVQLGYGANQQRIQATLSNKTGILGVELACDKEGTKTTLAEAGIPVPRGTVIYYADELADAIADVGGYPIVLKPLDGNHGRGITIDINSQQEAEEAYDLASAASKTRSVIVERYYKGNDHRVLVINGKLVAV... | Function: Catalyzes the ATP-dependent polymerization of arginine and aspartate to multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer).
Catalytic Activity: [L-4-(L-arginin-2-N-yl)aspartate](n) + ATP + L-aspartate = [L-4-(L-arginin-2-N-yl)aspartate](n)-L-aspartate + ADP + H(+) + phosphat... |
P58572 | MRILKIQTLRGPNYWSIRRHKLIVMRLDLETLAETPSNEIPGFYEGLVEALPSLEGHYCSPGCHGGFLMRVREGTMMGHIVEHVALELQELAGMHVGFGRTRETATPGIYQVVIEYLNEEAGRYAGRAAVRLCQSIVDRGRYPKAELEQDIQDLKDLWRDASLGPSTEAIVKEAEKRGIPWMQLSARFLIQLGYGVNHKRMQATMTDKTGILGVELACDKEATKRILAASGVPVPRGTVINFLDDLEEAIEYVGGYPIVIKPLDGNHGRGITIDIRSWEEAEAAYEAARQVSRSIIVERYYVGRDHRVLVVDGKVVAVAE... | Function: Catalyzes the ATP-dependent polymerization of arginine and aspartate to multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer).
Catalytic Activity: [L-4-(L-arginin-2-N-yl)aspartate](n) + ATP + L-aspartate = [L-4-(L-arginin-2-N-yl)aspartate](n)-L-aspartate + ADP + H(+) + phosphat... |
P73832 | MPLSSQPAILIIGGAEDKVHGREILQTFWSRSGGNDAIIGIIPSASREPLLIGERYQTIFSDMGVKELKVLDIRDRAQGDDSGYRLFVEQCTGIFMTGGDQLRLCGLLADTPLMDRIRQRVHNGEISLAGTSAGAAVMGHHMIAGGSSGEWPNRALVDMAVGLGIVPEIVVDQHFHNRNRMARLLSAISTHPELLGLGIDEDTCAMFERDGSVKVIGQGTVSFVDARDMSYTNAALVGANAPLSLHNLRLNILVHGEVYHQVKQRAFPRVT | Function: Exopeptidase that catalyzes the hydrolytic cleavage of multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer) into aspartate-arginine dipeptides.
Catalytic Activity: [L-4-(L-arginin-2-N-yl)aspartate](n) + H2O = [L-4-(L-arginin-2-N-yl)aspartate](n-1) + L-4-(L-arginin-2-N-yl)aspar... |
P0C8P3 | MLYRIPVSTVGYWHSPWQIHQFLLPIERFIHRNPMLQLDPISKTTHQHSGHKGLVMAIGGAEDKVRGRQILTTFCQRAGGLDAVIGVIPSASREPDAMGRLYHDIFRDIGVREVDILLVGDRADAEQEEMLARLSRCTGIFMSGGDQLRLSALLDETPLLYQLRHQVWEGKSILGGTSAGAAVLGECMIASGGSNEAPNRSLVDLATGLGILPDVLVDQHFHNRNRLARLISAISAHPDKLGVGIDEDTCAMFEADGTLRVLGRGSVTIVDPRDVSYTNYAHVDVNEPLSIYNLRLHILSDGDCYNLRTHQVQHKCILPP... | Function: Exopeptidase that catalyzes the hydrolytic cleavage of multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer) into aspartate-arginine dipeptides.
Catalytic Activity: [L-4-(L-arginin-2-N-yl)aspartate](n) + H2O = [L-4-(L-arginin-2-N-yl)aspartate](n-1) + L-4-(L-arginin-2-N-yl)aspar... |
Q8KQN8 | MIRSFIRSSALLLALLPVTGYSAGPLILVGGGLKDDNTAIYQRLIQLAGGNGQARIGVITAASIPESDDPDAGTADAANSKANGEFYAQLLETYGAADAQWIPIDLDQISNNSNPQVVAQINSMTGFFFGGGDQSRLTQTLQTATRADSPALAAIRARHNAGAVLAGTSAGTAIMVQGPMVTGGESYDGLRYGVYTTPSGDDLSYDMQGGFGFFNYGLLDTHFSERGRQGRIVRLADHTQVPFAFGVDENTALLVQNNATLGQVEMEVIGENGVFIFDLRNKERGTGSTYALYDVLGSYLTAGDRYRPVTGQFVIASGKT... | Function: Exopeptidase that catalyzes the hydrolytic cleavage of multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer) into aspartate-arginine dipeptides.
Catalytic Activity: [L-4-(L-arginin-2-N-yl)aspartate](n) + H2O = [L-4-(L-arginin-2-N-yl)aspartate](n-1) + L-4-(L-arginin-2-N-yl)aspar... |
A0A3G9JYJ6 | MAPISSTWSRLIRFVAIETSLVHIGEPIDATMDVGLARREGKTIQAYEIIGSGSALDLSAQVSKNVLTVRELLMPLSREEIKTVRCLGLNYPVHATEANVAVPKFPNLFYKPVTSLIGPDGLITIPSVVQPPKEHQSDYEAELVIVIGKAAKNVSEDEALDYVLGYTAANDISFRKHQLAVSQWSFSKGFGSLLLTIRMAQTHSGNINRFSRDQIFNVKKTISFLSQGTTLEPGSIILTGTPDGVGFVRNPPLYLKDGDEVMTWIGSGIGTLANTVQEEKTCFASGGHE | Function: Caffeoylpyruvate hydrolase; part of the gene cluster that mediates the fungal bioluminescence cycle . Involved in the recycling of oxyluciferin, a pyruvic acid adduct of caffeic acid, to caffeic acid . The fungal bioluminescence cycle begins with the hispidin synthetase that catalyzes the formation of hispidi... |
A0A1D6LAG9 | MAAAVVVRRAAGLIPLLSSRFGARMPLHRALSQIPPPRFCRLLSQQTKPFSASASNGAATDRTRELRLYNTKSRKKEQFRPRIPGREVGMYVCGVTPYDDSHIGHARAYVAFDVLYRYLRYLDYEVRYVRNFTDIDDKIIARANQLGEDPFSLSKRFSDDFLSDMANLQCLPPSVEPRVSDHVDEIINMIKQILDNRCAYVVGGDVYFSVDNFPEYGELSGRKLDDNRAGERVAVDERKRNPADFALWKAAKDGEPWWDSPWGPGRPGWHIECSAMSAHYLGHSFDIHGGGEDLIFPHHENEIAQSRAACCDSTINYWIH... | Cofactor: Binds 1 zinc ion per subunit.
Function: Nuclear genome-encoded factor required for normal assembly of chloroplast polysomes.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 64090
Sequence Length: 564
Subcellular Location: Plastid
EC: 6.1.1.16
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A0A1X9IRP7 | MGIRLLKMHGYDVDPNALKHFKQEDGKFSCYGGQMIESASPIYNLYRASQLRFPGEEILEEATKFAYNFLQEKIANNQIQEKWVISEHLIDEIKLGLKMPWYATLPRVEAAYYLQYYAGTGDVWIGKTFYRMPEISNDTYKELAVLDFNRCQAQHQFEWIYMQEWYQSSSVKAFGISKKELLLAYFLAAATIFEPERTQERIMWAKTQIVSRMIKSFLSKENTLSLEQKTTLLIDFGHDINGLNKINSVEKGNGLAGTLLTTFQQLLEEFDRYTTHQLKNAWSQWFVKLQQGEGDGGADAELLANTLNICAGHIAFNEDI... | 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 (+)-copalyl diphosphate... |
A0A075F9Z3 | MSMTLFASVTRPGLPGPTALRFPETRHLFHSVTAFAASFSPSKSSVGSSQCNATTPPAEYKEYTGNDLAKTTVDGIEKDIHSNKGLSDKTRELVMSIRSILRTMEEGEISMSPYDTAWVAMVEDIDGGGGPHFPSTLDWISSNQLADGSWGDPIFLVYDRLINTFACVIALTSWKMHPDKCDKAISFIRENMYKLDDEKEERMPIGFEMTFPPLVEKAKRLNINFPDDSPGLRKIYAQRDLKFKRIPWDKMHTVPTTLLYSLEGMALEADVLDWQKLLKLQSPDGSLFYSPASTAFALQQTGDHNCLQYLLKLVQTFNGG... | Function: Involved in the biosynthesis of labdane-type diterpenoid including marrubiin and other labdane-related furanoid diterpenoids with potential applications as anti-diabetics, analgesics or vasorelaxants (Probable). May be involved in the conversion of geranylgeranyl diphosphate (GGPP) to ent-copalyl diphosphate ... |
Q8GUU3 | MAIDCLVLGAGQEIGKSCVVVTINGKKIMFDCGMHMGCDDHNRYPNFSLISKSGDFDNAISCIIITHFHMDHVGALPYFTEVCGYNGPIYMSYPTKALSPLMLEDYRRVMVDRRGEEELFTTTHIANCMKKVIAIDLKQTIQVDEDLQIRAYYAGHVLGAVMVYAKMGDAAIVYTGDYNMTTDRHLGAAKIDRLQLDLLISESTYATTIRGSKYPREREFLQAVHKCVAGGGKALIPSFALGRAQELCMLLDDYWERMNIKVPIYFSSGLTIQANMYYKMLISWTSQNVKEKHNTHNPFDFKNVKDFDRSLIHAPGPCVL... | Function: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. May function as mRNA 3'-end-processi... |
Q8BTV2 | MSEGVDLIDIYADEEFNQDSEFNNTDQIDLYDDVLTAASQPSDDRSSSTEPPPPVRQEPAPKPNNKTPAILYTYSGLRSRRAAVYVGSFSWWTTDQQLIQVIRSIGVYDVVELKFAENRANGQSKGYAEVVVASENSVHKLLELLPGKVLNGEKVDVRPATRQNLSQFEAQARKRECVRVPRGGIPPRAHSRDSSDSADGRATPSENLVPSSARVDKPPSVLPYFNRPPSALPLMGLPPPPIPPPPPLSSSFGVPPPPPGIHYQHLMPPPPRLPPHLAVPPPGAIPPALHLNPAFFPPPNATVGPPPDTYMKASTPYNHH... | Function: Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'... |
A9LNK9 | MEDADGLSFDFEGGLDSGPVQNTASVPVAPPENSSSAAVNVAPTYDHSSATVAGAGRGRSFRQTVCRHWLRGLCMKGDACGFLHQFDKARMPICRFFRLYGECREQDCVYKHTNEDIKECNMYKLGFCPNGPDCRYRHAKLPGPPPPVEEVLQKIQQLTTYNYGTNRLYQARNVAPQLQDRPQGQVPMQGQPQESGNLQQQQQQQPQQSQHQVSQTLIPNPADQTNRTSHPLPQGVNRYFVVKSNNRENFELSVQQGVWATQRSNEAKLNEAFDSVENVILIFSVNRTRHFQGCAKMTSRIGGYIGGGNWKHEHGTAQYG... | Function: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation. May interact with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition (By similarity). Mediates poly(A) site selection . Binds RNA in a calcium-depen... |
O13284 | MFAKFDMLEEEARALVRKVGNAVDPIYGFSTTSCQIYDTAWAAMISKEEHGDKVWLFPESFKYLLEKQGEDGSWERHPRSKTVGVLNTAAACLALLRHVKNPLQLQDIAAQDIELRIQRGLRSLEEQLIAWDDVLDTNHIGVEMIVPALLDYLQAEDENVDFEFESHSLLMQMYKEKMARFSPESLYRARPSSALHNLEALIGKLDFDKVGHHLYNGSMMASPSSTAAFLMHASPWSHEAEAYLRHVFEAGTGKGSGGFPGTYPTTYFELNWVLSTLMKSGFTLSDLECDELSSIANTIAEGFECDHGVIGFAPRAVDVD... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Catalyzes the conversion of geranylgeranyl diphosphate to the gibberellin precursor ent-kaurene diphosphate in a two step process.
Catalytic Activity: ent-copalyl diphosphate = diphosphate + ent-kaur-16-ene
Sequence Mass (Da): 105724
Sequence Length: 946
Domain: The ... |
Q02929 | MRYNTAKLLVYDAEQVSKGIEKIQEHVENTEKYLSLYESTVINETDRIQLQELKALWEKYKSLVDKEVELVKSGKTEEARQLLLSDIDDIGDTLRDYFEAFVEYNTTAAKEKVDENKQVASTASTVMIVVIFVGILIAIALGVFISRIISKPIGQMVEAADRLALGDVEVDVKAETRDEIGKLAESFKRMIENIREQAYVVERIAAGDMTVDVRVKSDKDLLGKKLKEMVDTNNEVLSNINEVAAQVAAGAKQVSDSSMQLSQGATEQASSIEELTASLEQVANQTQLSAKNANQANELAEVAKNNAEQGNKQMAEMLNA... | Function: May bind attractants or detect changes in the extracellular concentration of soluble sugars.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 61043
Sequence Length: 557
Subcellular Location: Cell membrane
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A5UK38 | MKILFIGSRLYDDIDYYVRENGIESIITESNEDAINLDLPDQVFIVPRGMDSPKQIAISQNVDAVVPLIGIDPPLIEVAKMKEELEAETDIPVIAANVRAVRLTSDKIKTKEFYNEIGVPTPQYQILAKDDFESKLKMEFPVVLKQGQGQGGKDIKVAESLDDVKEYFEEFDHALCEKFIEGSEISIEVLGYNGEYVPLSPIYKGETTLEGIHPLNKIKTAPCLVEGLDNNLVQRTAYKVAKNLGSDGIFEMDFMFSKDEQQLYAIEVNTRPNGTRYLTTATCGVNSLCELVNMAAGKFSIKDIQDKLEYYYATEIPIGR... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Catalyzes the synthesis of carbamoyl phosphate from ATP, ammonium and bicarbonate. Proceeds via a three-step mechanism, i.e. the phosphorylation of hydrogencarbonate to carboxyphosphate, a nucleophilic attack of ammonia on carboxyphosphate yielding ca... |
Q68Y62 | MAEAHQAVAFQFTVTPDGIDLRLSHEALKQICLSGLHSWKKKFIRFKNGVITGVYPASPSSWLIVVVGVMSTMYAKIDPSLGIIAKINRTLDTTGYMSSQTKNIVSGVLFGTGLWVALIITMRYSLKVLLSYHGWMFAEHGKMSRATRIWMCMVKIFSGRKPMLYSFQTSLPRLPVPAVKDTVNRYLESVRPLMKDEDFKRMTALAQDFAVNLGPRLQWYLKLKSWWATNYVSDWWEEYVYLRGRGPLMVNSNYYAMDLLYVIPTHLQAATAGNGIHAILLYRHKLDREEIKPILFLGSTVPLCSAQWERMFNTCRIPGE... | Function: Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion (By similarity). Plays an important role in hepatic triglyceride metabolism (By sim... |
O60519 | MDDSKVVGGKVKKPGKRGRKPAKIDLKAKLERSRQSARECRARKKLRYQYLEELVSSRERAICALREELEMYKQWCMAMDQGKIPSEIKALLTGEEQNKSQQNSSRHTKAGKTDANSNSW | Function: Probable regulator of CREB1 transcriptional activity which is involved in adipose cells differentiation. May also play a regulatory role in the cell cycle. Identification in a chromosomal region frequently deleted in various cancers suggests that it might act as a tumor suppressor.
PTM: Phosphorylated by AMPK... |
Q32M00 | MDDSKVVGGKVKKPGKRGRKPAKIDLKAKLERSRQSARECRARKKLRYQYLEELVSSRERAICALREELEMYKQWCMAMDQGKIPSEIRALLTGEEQSKPQQNSSRHPKAGKTDANTNSLVGN | Function: Probable regulator of CREB1 transcriptional activity which is involved in adipose cells differentiation. May also play a regulatory role in the cell cycle.
PTM: Phosphorylated by AMPK.
Sequence Mass (Da): 14002
Sequence Length: 123
Subcellular Location: Nucleus
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Q19267 | MSRILLLLAVLIGATSQKEVTIKNEKCRTCNFLVSTFDEGLKKTARHHFAGGDTAWEEKNLGKYKTSETRLIEVLEGVCKKSSLPNMDNFMGIAEIEFKCSTQLEKHEETIEEFYYNQQHNNMSNWLCVEQLKLCCPDGHFGKNCEQCPGLSEKADVCFGKGSCHGDGSREGSGKCKCETGYTGNLCRYCDIEYFEESRTVQGVVCKKCHEGCLGVCSSESSKGCSKCKNGWKLTEEGCADVNECQNESACTKEHEICVNTVGSFKCECKEGYKKDDEQNCQFDVEASPDRPFMPIDQQLKLIAFSSLIIIITFVVWHGS... | Function: Protein disulfide isomerase which associates with the unc-29 subunit of levamisole-sensitive nicotinic acetylcholine receptors (L-nAChR) to promote L-nAChR assembly in the endoplasmic reticulum at neuromuscular junctions.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Location Top... |
Q96HD1 | MAPWPPKGLVPAMLWGLSLFLNLPGPIWLQPSPPPQSSPPPQPHPCHTCRGLVDSFNKGLERTIRDNFGGGNTAWEEENLSKYKDSETRLVEVLEGVCSKSDFECHRLLELSEELVESWWFHKQQEAPDLFQWLCSDSLKLCCPAGTFGPSCLPCPGGTERPCGGYGQCEGEGTRGGSGHCDCQAGYGGEACGQCGLGYFEAERNASHLVCSACFGPCARCSGPEESNCLQCKKGWALHHLKCVDIDECGTEGANCGADQFCVNTEGSYECRDCAKACLGCMGAGPGRCKKCSPGYQQVGSKCLDVDECETEVCPGENKQ... | Function: Protein disulfide isomerase (By similarity). Promotes the localization of acetylcholine receptors (AChRs) to the plasma membrane (By similarity).
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45440
Sequence Length... |
Q6UXH1 | MRLPRRAALGLLPLLLLLPPAPEAAKKPTPCHRCRGLVDKFNQGMVDTAKKNFGGGNTAWEEKTLSKYESSEIRLLEILEGLCESSDFECNQMLEAQEEHLEAWWLQLKSEYPDLFEWFCVKTLKVCCSPGTYGPDCLACQGGSQRPCSGNGHCSGDGSRQGDGSCRCHMGYQGPLCTDCMDGYFSSLRNETHSICTACDESCKTCSGLTNRDCGECEVGWVLDEGACVDVDECAAEPPPCSAAQFCKNANGSYTCEECDSSCVGCTGEGPGNCKECISGYAREHGQCADVDECSLAEKTCVRKNENCYNTPGSYVCVCP... | Function: Protein disulfide isomerase (By similarity). Might play a role in the unfolded protein response (By similarity). May regulate transport of alpha4-beta2 neuronal acetylcholine receptor .
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 38192
Sequence Length: 353
S... |
P79145 | MSKCSRKKYIKTNLRQMTMDTMESQQDGSVTDSVAENESAHMQNQTGQNSIPTLTQVSVAGSGTGRGSPAVTLVQLPSGQTVHVQGIIQTPQPSVIQSPQIQTVQVATIAETDESAESEGVIDSHKRREILSRRPSYRKILNELSSDVPGVPKIEEEKSEEEGTPPNIATMAVPTSIYQTSTGQYIAIAQGGTIQISNPGSDGVQGLQALTMTNSGAPPPGATIVQYAAQSADGTQQFFVPGSQVVVQDEETELAPSHMAAATGDMPTYQIRAPTTALPQGVVMAASPGSLHSPQQLAEEATRKRELRLMKNREAARECR... | Function: Transcriptional regulator that binds the cAMP response element (CRE), a sequence present in many viral and cellular promoters. Isoforms are either transcriptional activators or repressors. Isoform Tau is a transcriptional activator. Plays a role in spermatogenesis and is involved in spermatid maturation (By s... |
Q03060 | MTMETVESQHDGSITASLTESKSAHVQTQTGQNSIPALAQVSVAGSGTRRGSPAVTLVQLPSGQTIHVQGVIQTPQPWVIQSSEIHTVQVAAIAETDESAESEGVIDSHKRREILSRRPSYRKILNELSSDVPGVPKIEEERSEEEGTPPSIATMAVPTSIYQTSTGQYIAIAQGGTIQISNPGSDGVQGLQALTMTNSGAPPPGATIVQYAAQSADGTQQFFVPGSQVVVQDEETELAPSHMAAATGDMPTYQIRAPTAALPQGVVMAASPGSLHSPQQLAEEATRKRELRLMKNREAAKECRRRKKEYVKCLESRVAV... | Function: Transcriptional regulator that binds the cAMP response element (CRE), a sequence present in many viral and cellular promoters. Isoforms are either transcriptional activators or repressors. Plays a role in spermatogenesis and is involved in spermatid maturation .
PTM: Isoform 9 is ubiquitinated by CDC34 and RA... |
P27699 | MSKCGRKKYMRTNVRQMTMETVESQQDRSVTRSVAEHSSAHMQTGQISVPTLAQVSVAGSGTGRGSPAVTLVQLPSGQTVQVQGVIQTPHPSVIQSPQIQTVQVATIAETDDSADSEVIDSHKRREILSRRPSYRKILNELSSDVPGIPKIEEEKSEEEGTPPNIATMAVPTSIYQTSTGQYIAIAQGGTIQISNPGSDGVQGLQALTMTNSGAPPPGATIVQYAAQSADGTQQFFVPGSQVVVQDEETDLAPSHMAAATGDMPTYQIRAPTTALPQGVVMAASPGSLHSPQQLAEEATRKRELRLMKNREAAKECRRRK... | Function: Transcriptional regulator that binds the cAMP response element (CRE), a sequence present in many viral and cellular promoters. Isoforms are either transcriptional activators or repressors. Isoform 2, isoform 3 and isoform 4 are repressors, while isoform 1 is an activator. Plays a role in spermatogenesis and i... |
A0A0K2JLU1 | MHALLRRVTRGNGFYIGDLFHAAAGHDATTPVTLDQPLQYAPELGTRFTVGQLAEQTDELAARLWAAGVRPTERVALYKKDNFDIALHACAAARIGAVPALLSPALEAPVVRTLLDRLDGPWLLTDATTLAGPLGTVLAPASVRAVLLTTGTPAEGALPAAGATGPAREGDAPPPAPVVRLADHRGAPKRPPVFLHPRQPSLITHSSGTTGVPKLAVHCPEAGWHRLVPQKVVSWPIRGKEKAALCMTFVHSRFYQGLAMFLSHGNPMLIAVDPDPSRIGPLFARERPGYIETHPNTYVDWEALADAPGEPLAGVRVFGA... | Function: Part of a gene cluster involved in the biosynthesis of cremeomycin, a light-sensitive o-diazoquinone with antibacterial and antiproliferative effects . Catalyzes the last step of cremeomycin biosynthesis, the diazotization of 3-amino-2-hydroxy-4-methoxybenzoate (3,2,4-AHMBA) with nitrite to generate cremeomyc... |
Q9T0J1 | MLSLLLPLISLLFQIQCFTVKSQPVPLNQICSNVTGNFTVNTPYAVNLDRLISSLSSLRRNVNGFYNISVGDSDEKVNSISQCRGDVKLEVCINCIAMAGKRLVTLCPVQKEAIIWYDKCTFRYSNRTIFNRLEISPHTSITGTRNFTGDRDSWEKSLRGLLEGLKNRASVIGRSKKNFVVGETSGPSFQTLFGLVQCTPDISEEDCSYCLSQGIAKIPSCCDMKMGSYVMSPSCMLAYAPWRFYDPVDTDDPSSVPATPSRPPKNETRSVTQGDKNRGVPKALIFASASVAIVVLFIVLLVVFLKLRRKENIRNSENKH... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 74355
Sequence Length: 665
Subcellular Location: Membrane
EC: 2.7.11.-
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O49564 | MASTSIMLSSFFSFFFLTFFVTYAQQNVTVHTICYYDGGNFTSNTSYSLNLNRLISSLPDLTPTINGFYNISINGEVNAIALCRGDVKPNQDCISCITTAAKQLVESCPNIIEANIWLEKCMFRYTSRIILGQMEPVPFSYTSSNVSVTDKEGFSKGLGDLLDSLGAKIDAANETKEVKFAAGVKGTIYALAQCTPDLSESDCRICLAQIFAGVPTCCDGKTGGWWTNPSCYFRFEVYPFFDLSVTSEQKQPLSSHNNNTRRSDQGKSKDRSKTLIFAVVPIVAIILGLVFLFIYLKRRRKKKTLKENAENEFESTDSLH... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 71935
Sequence Length: 642
Subcellular Location: Membrane
EC: 2.7.11.-
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Q8S9L6 | MEHVRVIFFFACFLTLAPFHAFAQVDSYEFDPDFNCVDRGNFTANSTFAGNLNRLVSSLSSLKSQAYGFYNLSSGDSSGERAYAIGLCRREVKRDDCVSCIQTAARNLTKQCPLTKQAVVWYTHCMFRYSNRTIYGRKETNPTKAFIAGEEISANRDDFERLQRGLLDRLKGIAAAGGPNRKYAQGNGSASAGYRRFYGTVQCTPDLSEQDCNDCLVFGFENIPSCCDAEIGLRWFSPSCNFRFETWRFYEFDADLEPDPPAIQPADSPQSAARTERTGKGKGGSKVIIAIVIPILLVALLAICLCLVLKWRKNKSGYKN... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 75720
Sequence Length: 679
Subcellular Location: Membrane
EC: 2.7.11.-
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Q9CAL3 | MKKEPVHILPLYLPCLLMFLLSSLRQITGDARARAVKVTCSPLLEHNETAYVPNFVATMEKISTQVQTSGFGVALTGTGPDANYGLAQCYGDLPLNDCVLCYAEARTMLPQCYPQNGGRIFLDGCFMRAENYSFYNEYKGPEDSIVCGNTTRKNKTFGDAVRQGLRNAVTEASGTGGYARASAKAGESESESAFVLANCWRTLSPDSCKQCLENASASVVKGCLPWSEGRALHTGCFLRYSDQDFLNKIPRNGRSRGSVVVIVVSVLSSVVVFMIGVAVSVYICKRRTIKRKRRGSKDVEKMAKTLKDSSLNFKYSTLEK... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 72000
Sequence Length: 649
Subcellular Location: Membrane
EC: 2.7.11.-
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Q9LDT0 | MRQNNLFSLIFWLVPVSLIIVVSAQLCSEKFGTFTPGGTFDKNRRIILSSLPSEVTAQDGFYNASIGTDPDQLYAMGMCIPGAKQKLCRDCIMDVTRQLIQTCPNQTAAIHWSGGGKTVCMARYYNQPSSRPLDLESVSIGYNVGNLSTNLTDFDRLWERLIAHMVTKASSASIKYLSFDNSRFYAADETNLTNSQMVYALMQCTPDVSPSNCNTCLKQSVDDYVGCCHGKQGGYVYRPSCIFRWDLYPFNGAFDLLTLAPPPSSQLQSPPPVTNKDEKTIHTGTIIGIVIVVAMVIIMALLALGVSVCRSRKKYQAFAS... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 77800
Sequence Length: 700
Subcellular Location: Membrane
EC: 2.7.11.-
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Q9LDN1 | MRKTKKISFLIFWVVLISIIGAISSQQCNETGYFEPWKTYDTNRRQILTSLASKVVDHYGFYNSSIGKVPDEVHVMGMCIDGTEPTVCSDCLKVAADQLQENCPNQTEAYTWTPHKTLCFARYSNSSFFKRVGLHPLYMEHSNVDIKSNLTYLNTIWEALTDRLMSDASSDYNASLSSRRYYAANVTNLTNFQNIYALMLCTPDLEKGACHNCLEKAVSEYGNLRMQRGIVAWPSCCFRWDLYPFIGAFNLTLSPPPGSKRNISVGFFVAIVVATGVVISVLSTLVVVLVCRKRKTDPPEESPKYSLQYDLKTIEAATCT... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 71693
Sequence Length: 636
Subcellular Location: Membrane
EC: 2.7.11.-
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Q9XEC6 | MERSNLFHIPCFLLLFLLFNINGVHTTFVCGDEDFSPNTSYVENLESLLPSLASNVIRERGFYNVSLDGVYALALCRKHYEVQACRRCVDRASRTLLTQCRGKTEAYHWDSENDANVSCLVRYSNIHRFGKLKLEPIGNVPHSSLDPSSNLTRISQEFAARANRTVEVASTADESSVLKYYGVSSAEFTDTPEVNMLMQCTPDLSSSDCNHCLRENVRYNQEHNWDRVGGTVARPSCYFRWDDYRFAGAFDNLERVPAPPRSPQTRQDYRVKKGRMFQPWSVVVVVFPTGINLAVFVAFVLAYRRMRRRIYTEINKNSDS... | Function: Forms a complex with CRK45 that may negatively control abscisic acid (ABA) and osmotic stress signal transduction. Can phosphorylate CRK45 in vitro .
PTM: Autophosphorylated.
Location Topology: Single-pass membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
... |
Q9XEC7 | MGKSCVVTSSFSLLLLFLQTLKYVHAGFICYGDFFNVNYGVSRTYLFSSLPSNVVSNGGFYNASFGRDSKNNRVHVVALCRRGYEKQACKTCLEHVIEDTKSKCPRQKESFSWVTDEFDDVSCSLRYTNHSTLGKLELLPNTINPNPNSIDSKFNNMAMFSQEWIAMVNRTLEAASTAENSSVLKYYSATRTEFTQISDVYALMQCVPDLSPGNCKRCLRECVNDFQKQFWGRQGGGVSRPSCYFRWDLYPYYRAFDNVVRVPAPPPQASSTIIDYGRDEKSFQGSNIAIIVVPSVINLIIFVVLIFSWKRKQSHTIIND... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 73440
Sequence Length: 646
Subcellular Location: Membrane
EC: 2.7.11.-
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Q9CAL2 | MPILTLLLLILGLFISPSVSDSRGDTVAQICNNRTTTPQQRSLFVTNFLAAMDAVSPLVEAKGYGQVVNGTGNLTVYAYGECIKDLDKKDCDLCFAQIKAKVPRCLPFQKGTRGGQVFSDGCYIRYDDYNFYNETLSLQDRTVCAPKEITGVNRTVFRDNAAELVKNMSVEAVRNGGFYAGFVDRHNVTVHGLAQCWETLNRSGCVECLSKASVRIGSCLVNEEGRVLSAGCYMRFSTQKFYNNSGNSTSDGNGGHNHLGVILAVTSSVVAFVLLVSAAGFLLKKRHAKKQREKKQLGSLFMLANKSNLCFSYENLERAT... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 71611
Sequence Length: 646
Subcellular Location: Membrane
EC: 2.7.11.-
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Q9SYS3 | MGKCSALMIFLSSSLLLVLQTLHVVNAVKCFGNSFNGNSSTFAQNRQKLFPTLADKVIINDGFYNASLGQDPDKVYALVSCARGYDQDACYNCVQSLTQNTLTDCRSRRDSFIWGGNDDVTCLVRSSNQSTFGSVQLKPPVVWPSPDTIESSKNITLFKQQWEEMVNRTLEAATKAEGSSVLKYYKAEKAGFTEFPDVYMLMQCTPDLSSRDCKQCLGDCVMYFRKDYMGRKGGMASLPSCYFRWDLYSFHNAFDNVTRVPAPPPRPHAQEKESCITVKKGKSIGYGGIIAIVVVFTFINLLVFIGFIKVYARRGKLNNV... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 73236
Sequence Length: 654
Subcellular Location: Membrane
EC: 2.7.11.-
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O23081 | MTSSCSLSRPQHLFFFFFLFVPFLSLGQQISVDINSAIWEFPSNPLCLSQQSNFAKSSQFSKNLDSLVSSIPSLKSNTYNFYSLSVGSISDQERVEAIGICNRVVNRVDCLNCIAQAAVNLTTMYCPQHRGAYVRATKCMFRYSDKPIFGKLETSPVLEAPNPSNATGDRNEFIRLQSELLNRLRSMAASGGSKRKYAQGTDPGSPPYTTFFGAVQCTPDLSEKDCNDCLSYGFSNATKGRVGIRWFCPSCNFQIESDLRFFLLDSEYEPDPKPGNDKVKIIIATVCSVIGFAIIAVFLYFFMTRNRRTAKQRHEGKDLE... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 74887
Sequence Length: 665
Subcellular Location: Membrane
EC: 2.7.11.-
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Q9FNE1 | MRCLTKTRSFHYVIIFYSFFFLPFLSSSSDDQRTTVSGLFCGGRSKSSADPNYIPTFVEDMHSLSLKLTTRRFATESLNSTTSIYALIQCHDDLSPSDCQLCYAIARTRIPRCLPSSSARIFLDGCFLRYETYEFYDESVSDASDSFSCSNDTVLDPRFGFQVSETAARVAVRKGGFGVAGENGVHALAQCWESLGKEDCRVCLEKAVKEVKRCVSRREGRAMNTGCYLRYSDHKFYNGDGHHKFHVLFNKGVIVAIVLTTSAFVMLILLATYVIMTKVSKTKQEKRNLGLVSRKFNNSKTKFKYETLEKATDYFSHKKM... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 72706
Sequence Length: 651
Subcellular Location: Membrane
EC: 2.7.11.-
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Q9ZVE7 | MAVLSTIYSITRASTPTMASLTNDSPSPLPSSSPSKLPSPTSPSKKPLKLRQVSKQMGSQNQQRRGNKPSIAQIERAFGSGSYRDSEGEMDMNTVFDELLLGHANKFESKIEKKLREIGEIFVARTEPKLRSSGKPVLMFTIQWILPIWIMSLLVACGVIKLPFSIPFLDDLIM | Function: Probable subunit of the chloroplast NAD(P)H dehydrogenase (NDH) complex of the photosynthetic electron transport chain. Required for both formation and activity of NDH. May function in assembly or stabilization of the NDH complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19283
Seque... |
Q99R74 | MKWLSRILTVIVTMSMACGALIFNRRHQLKTKTLNFNHKALTIIIPARNEEKRIGHLLHSIIQQQVPVDVIVMNDGSTDETARVARSYGATVVDVVDDTDGKWYGKSHACYQGVTHACTNRIAFVDADVTFLRKDAVETLINQYQLQGEKGLLSVQPYHITKRFYEGFSAIFNLMTVVGMNVFSTLDDGRTNQHAFGPVTLTNKEDYYATGGHKSANRHIIEGFALGSAYTSQSLPVTVYEGFPFVAFRMYQEGFQSLQEGWTKHLSTGAGGTKPKIMTAIVLWLFGSIASILGLCLSLKYRQMSVRKMVALYLSYTTQF... | Function: Catalyzes the glycosylation of 4,4'-diaponeurosporenoate, i.e. the esterification of glucose at the C1'' position with the carboxyl group of 4,4'-diaponeurosporenic acid, to form glycosyl-4,4'-diaponeurosporenoate. This is a step in the biosynthesis of staphyloxanthin, an orange pigment present in most staphy... |
Q4L977 | MTKLESLLHASTGLSLISGYLMYNRRYLLSFDKKREGETTQSISVIIPARNEEKRLPKLLKSLSQQSMRVECIVMDDDSNDRTAEIAREMGAKVYNVTYDNNGNTWIGKSYACYLGASYTVSDILIFMDADVELNNEHALEAIIQSYARQQYRGLMSIQPYHVVYKPYEHLSAMFNLMTVVGTNSFSTLSKSKGESLAFGPVTVMNKSDYILTQGHKNAASHIIEGFSLGKAFQRCQLPVTRFEGQGFVSFRMYEAGFKTMIEGWTKHLAVGASSTQPHIMMLIILWMVGCITSFSGLALSLFMKTLSFKRMALSYSLYT... | Function: Catalyzes the glycosylation of 4,4'-diaponeurosporenoate, i.e. the esterification of glucose at the C1'' position with the carboxyl group of 4,4'-diaponeurosporenic acid, to form glycosyl-4,4'-diaponeurosporenoate. This is a step in the biosynthesis of staphyloxanthin, an orange pigment present in most staphy... |
Q9M9Y8 | MDLCFQNPVKCGDRLFSALNTSTYYKLGTSNLGFNGPVLENRKKKKKLPRMVTVKSVSSSVVASTVQGTKRDGGESLYDAIVIGSGIGGLVAATQLAVKEARVLVLEKYLIPGGSSGFYERDGYTFDVGSSVMFGFSDKGNLNLITQALKAVGRKMEVIPDPTTVHFHLPNNLSVRIHREYDDFIAELTSKFPHEKEGILGFYGDCWKIFNSLNSLELKSLEEPIYLFGQFFQKPLECLTLAYYLPQNAGAIARKYIKDPQLLSFIDAECFIVSTVNALQTPMINASMVLCDRHYGGINYPVGGVGGIAKSLAEGLVDQG... | Function: Carotene cis-trans-isomerase that converts 7,9,9'-tri-cis-neurosporene to 9'-cis-neurosporene and 7,9,9',7'-tetra-cis-lycopene (also known as prolycopene) into all-trans-lycopene. Isomerization requires redox-active components, suggesting that isomerization is achieved by a reversible redox reaction acting at... |
Q8S4R4 | MCTLSFMYPNSLLDGTCKTVALGDSKPRYNKQRSSCFDPLIIGNCTDQQQLCGLSWGVDKAKGRRGGTVSNLKAVVDVDKRVESYGSSDVEGNESGSYDAIVIGSGIGGLVAATQLAVKGAKVLVLEKYVIPGGSSGFYERDGYKFDVGSSVMFGFSDKGNLNLITQALAAVGRKLEVIPDPTTVHFHLPNDLSVRIHREYDDFIEELVSKFPHEKEGIIKFYSECWKIFNSLNSLELKSLEEPIYLFGQFFKKPLECLTLAYYLPQNAGSIARKYIRDPGLLSFIDAECFIVSTVNALQTPMINASMVLCDRHFGGINY... | Function: Carotene cis-trans-isomerase that converts 7,9,9'-tri-cis-neurosporene to 9'-cis-neurosporene and 7,9,9',7'-tetra-cis-lycopene (also known as prolycopene) into all-trans-lycopene. Isomerization requires redox-active components, suggesting that isomerization is achieved by a reversible redox reaction acting at... |
Q8KFK3 | MQRREFFQHFLKRAGIGAGALGAATAGLVGYYQPRKEVFDTSGKNNDELAEKLTTPKKAVVIGGGLAGISSALELARRNFEVTLVEASPSLGGKLTGWSIEALGEQFPVEHGFHGFFDQYYNLNEMFASAGIGSDMFTASPGYPVIFSDRQVEVFGQTPKWFPFNILSVVQQSKRLDIMSFLKDYPGLWPVISMFRYQYDRTFRDWDSIDFMTYCRRGEVLPAFIDTVLHPFSDATMNRMEVLSAAEAMRYFHFYFMGSPEGLAFRIITKDCMSALIEPLERKMTSLGVRVLKGRKAQNLVMQDGRVTAVRLDGAGAANG... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Involved in the biosynthesis of chlorobactene, a carotenoid with aromatic end group . Catalyzes the introduction of two additional double bonds into the ionone ring of gamma-carotene to produce chlorobactene. The reaction includes an intramolecular methyl transf... |
P72449 | MFARDSGRGHRHGRDRQAAVVPAPAGRARFTGDAPAVAVVGGGIAGIAAATLLAERGVRVTLYEREPGLGGRLSGWPTELTDGTTVTMSRGFHAFFRQYYNLRGLLRRVDPDLGSLTRLPDYPLWHGSGLRDSFARVPRTPPLSAMGFVALSPTFGLRDLVRINPRAAVGLLDVRVPEVYERLDGISATDFLDRIRFPEAAHHLAFEVFSRSFFADPRELSAAELALMFHIYFLGSSEGLLFDVPGEPFPAALWEPLHHYLEVHRVDVRTRTPLRQVRPRPGGGLDLTTDDRTTRYDALVLALDSGALRRLVAASPELGD... | Function: Involved in the biosynthesis of isorenieratene, a carotenoid with aromatic end groups . Catalyzes the introduction of two additional double bonds into each ionone ring of beta-carotene to produce isorenieratene. The reaction includes an intramolecular methyl transfer from position C1 to position C2 of the rin... |
P81995 | PRNPEIQNEIIDLHNYLRRSVNPXASNMLRSQW | Function: Blocks contraction of smooth muscle elicited by high potassium-induced depolarization, but does not block caffeine-stimulated contraction. May target voltage-gated calcium channels on smooth muscle (By similarity).
PTM: Contains 8 disulfide bonds.
Sequence Mass (Da): 3974
Sequence Length: 33
Subcellular Locat... |
P81994 | GGGKDYRVEIVDKHNXLRRSVXXTARN | Function: Blocks contraction of smooth muscle elicited by high potassium-induced depolarization, but does not block caffeine-stimulated contraction. May target voltage-gated calcium channels on smooth muscle (By similarity).
PTM: Contains 8 disulfide bonds.
Sequence Mass (Da): 3075
Sequence Length: 27
Subcellular Locat... |
Q9FLH0 | MATSSRSERFPITPSTAATNRLTITPNSRVLKSPLTEEIMWKRLKDAGFDEQSIKNRDKAALIAYIAKLESEVYDYQHNMGLLLLEKNELSSQYEEIKASVDESDLTHMREKSAYVSALAEAKKREESLKKDVGIAKECISSLEKTLHEMRAECAETKVSAGSTMSEAHVMIEDALKKLADAEAKMRAAEALQAEANRYHRIAERKLKEVESREDDLTRRLASFKSECETKENEMVIERQTLNERRKSLQQEHERLLDAQVSLNQREDHIFARSQELAELEKGLDTAKTTFEEERKAFEDKKSNLEIALALCAKREEAVS... | Function: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments (By similarity). Required for nucleus structure organization (e.g. size and shape) . In... |
Q43125 | MSGSVSGCGSGGCSIVWFRRDLRVEDNPALAAAVRAGPVIALFVWAPEEEGHYHPGRVSRWWLKNSLAQLDSSLRSLGTCLITKRSTDSVASLLDVVKSTGASQIFFNHLYDPLSLVRDHRAKDVLTAQGIAVRSFNADLLYEPWEVTDELGRPFSMFAAFWERCLSMPYDPESPLLPPKKIISGDVSKCVADPLVFEDDSEKGSNALLARAWSPGWSNGDKALTTFINGPLLEYSKNRRKADSATTSFLSPHLHFGEVSVRKVFHLVRIKQVAWANEGNEAGEESVNLFLKSIGLREYSRYISFNHPYSHERPLLGHLK... | Cofactor: Binds 1 FAD per subunit.
Function: Photoreceptor that mediates primarily blue light inhibition of hypocotyl elongation and photoperiodic control of floral initiation, and regulates other light responses, including circadian rhythms, tropic growth, stomata opening, guard cell development, root development, bac... |
B0WRR9 | MTDKVRNRVQCWPALAQESSCVDFIPARQGATCGSTVVFIPCCGLTRGRRVLCQWFPCLSGGCCSQESSCVDFIPARQGATCGSTVVFIPCCGLTRGRRVLCQWFPCLSGGCCSQHTVNIIGEPPRPVGAPSFEFVEFGRLPSILSTELKLFQRAPVPEDFGIYYEGNADIARQRWTGGEAKALELLGRRLKQEEEAFREGYYLPTQARPDFLAPPSSMSAALRFGCLSVRMFYWCVHDLFARVQANNQLKHPGGHHITGQLIWREYFYTMSVHNPHYAVMELNPICLNIPWYEAKDDSLDRWKEGRTGFPLIDAAMRQL... | Cofactor: Binds 1 FAD per subunit.
Function: Blue light-dependent regulator that is the input of the circadian feedback loop. Has no photolyase activity for cyclobutane pyrimidine dimers or 6-4 photoproducts. Regulation of expression by light suggests a role in photoreception for locomotor activity rhythms. Functions, ... |
G1UB63 | MLPSIVISIVLASFVSAESSITEAPTTTAEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSICSVAGVWDPYWMVPANVQSSLSAAATAVASSSEQPVETSSEPAGSSQSVESSQPAETSSSEPAETSSSEPAETSSETSSEQPASSEPAETSSEESSTITSAPSTPEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSICSVAGVWDPYWMVP... | Function: Heme-binding protein involved in heme-iron utilization. The ability to acquire iron from host tissues is a major virulence factor of pathogenic microorganisms. Required for biofilm formation.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the ce... |
Q5A0X8 | MKFSTILAIPFAIAFANAAAAPAVTAAPAPAADNPYTIYPPVPKTASINGFADRIYDQIPKCAQECVKQSTSSTPCPYWDTGCLCVIPNFTGAVGNCVASKCRGADVTNFRKLAVGACAAAGVWDPYWIIPASVSSALDAAATATGN | Function: Secreted heme-binding protein involved in the utilization of iron from human hemoglobin during hyphal growth . May also play a role in non-hemoglobin iron utilization . Heme transfer occurs between PGA7, RBT5 and CSA2 supporting a model in which the 3 CFEM proteins cooperate in a heme-acquisition system and f... |
Q57476 | MIRFIFKHKKMHKPKELVFGQTIIQLNQVNGADKRKLIWLLIIKRSRQAFPYFQREDAVIYLDNAATTLKPQVLIDRTAEFYASAGSVHRSQYDAAQTVQYEQARTQVKEWVHAEDKHAVIWTSGTTHAINLVANGLMPQLNAEDEILISQADHHANFVTWHETAKKCGAKIQVLPILDNWLIDENALISALSEKTKLVALNFVSNVTGTEQPIKRLIQLIRKHSNALVLVDAAQAISHIKIDLQDLDADFLAFSAHKIYGPNGLGVLTGKLTALSQLQPLFFGGKMVDRVSNDRITFAELPYRLEAGTPNIAGVIGFNA... | Function: Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 49048
Sequence Length: 437
EC: 2.8.1.7
|
Q9K7A0 | MNAHEIKKLFPVLDQEVNGSPLVYLDSAATSQKPIAVIEALDDYYRRYNSNVHRGVHTLGTLATDGYEGAREKIRRFIHASSTEEIIFTRGTTTAINLVAASYGRANLGEGDEIVITPMEHHSNIIPWQQVAKATGATLTYLPLQKDGTIKIEDVEKTISEKTKIVAIMHVSNVLGTINPVKEIAEIAHRHGAIMLVDGAQSAPHMKIDVQELGCDFFAFSGHKMAGPTGIGVLYGKKAHLEKMEPVEFGGEMIDFVGLYDSTWKELPWKFEGGTPIIAGAIGLGAAIDFLEDIGLDEIEKHEHELAQYALDRLSELEGM... | Function: Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 44632
Sequence Length: 406
EC: 2.8.1.7
|
P63517 | MTASVNSLDLAAIRADFPILKRIMRGGNPLAYLDSGATSQRPLQVLDAEREFLTASNGAVHRGAHQLMEEATDAYEQGRADIALFVGADTDELVFTKNATEALNLVSYVLGDSRFERAVGPGDVIVTTELEHHANLIPWQELARRTGATLRWYGVTDDGRIDLDSLYLDDRVKVVAFTHHSNVTGVLTPVSELVSRAHQSGALTVLDACQSVPHQPVDLHELGVDFAAFSGHKMLGPNGIGVLYGRRELLAQMPPFLTGGSMIETVTMEGATYAPAPQRFEAGTPMTSQVVGLAAAARYLGAIGMAAVEAHERELVAAAI... | Function: Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 44596
Sequence Length: 417
EC: 2.8.1.7
|
Q49420 | MSAIKFNPSSFRKNFKWFENNKNWINFDNAATSIALDVVAEASKEYYQYFCVNPHNKNPEINQKLIAIIEETRDLLAKFFNAKKNEIIFTSSATESLNLFAFGLSSLVKSNDEIILKEDEHAANVFPWVNLAKENKAKLKIIKKTPNKSWTDAFLKACTPSTKLLVITATSNLFGNSIDYEKISKHLKKISPNSFIVVDAVQAVPHHKIDITSANIDFLTFSTHKFYGPTGLGIAFIKSELQSRLKPFKLGGDIFKSLDNNFKIIFKEGPSKFEAGTLNIMAIYALNKQLKFMQKEFNFSEMVFYSKQLKNLAYQLLSQN... | Function: Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 46618
Sequence Length: 408
EC: 2.8.1.7
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Q9HXX3 | MSLPSPWRADFPAFSAFAAEGLTYLDSAATAQKPQAVLDALNGYYLGGAANVHRAQHVPGERATRAFEAARSRVAHWLHAGNPAEVLFTRGTTEAINLVAYGLERHFRPGDELLVSALEHHANLLPWQQLALRRGLVLRVLPLDERGVIDLEQARHIIGERTRLLAISQLSNVLGTWQPVVELIQLARERGAWTLVDGAQGSVHGRHDLPGLGCDFYAFSGHKLYGPDGIGVLWGRPQALEQLAHWQFGGEMVRHTGFHEASFHAAPLGFEAGTPAVSAAIGLGATIDWLATLDEAEVAAHEGALHARLLAGLLARDGVS... | Function: Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 43274
Sequence Length: 401
EC: 2.8.1.7
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A8AI45 | MQRLLILVAVCLLSGCLTAPPKEAAKPTLMPRAQSYKDLTHLPMPTGKIFVSVYNIQDETGQFKPYPASNFSTAVPQSATAMLVTALKDSRWFIPLERQGLQNLLNERKIIRAAQENGTVAINNRIPLQSLTAANIMVEGSIIGYESNVKSGGVGARYFGIGADTQYQLDQIAVNLRVVNVSTGEILSSVNTSKTILSYEVQAGVFRFIDYQRLLEGEIGYTSNEPVMLCLMSAIETGVIFLINDGIDRGLWDLQNKAERQNDILVKYRHMSVPPES | Function: May be involved in the biogenesis of curli organelles.
Location Topology: Lipid-anchor
Sequence Mass (Da): 30541
Sequence Length: 277
Subcellular Location: Cell membrane
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P0AEA4 | MQRLFLLVAVMLLSGCLTAPPKEAARPTLMPRAQSYKDLTHLPAPTGKIFVSVYNIQDETGQFKPYPASNFSTAVPQSATAMLVTALKDSRWFIPLERQGLQNLLNERKIIRAAQENGTVAINNRIPLQSLTAANIMVEGSIIGYESNVKSGGVGARYFGIGADTQYQLDQIAVNLRVVNVSTGEILSSVNTSKTILSYEVQAGVFRFIDYQRLLEGEVGYTSNEPVMLCLMSAIETGVIFLINDGIDRGLWDLQNKAERQNDILVKYRHMSVPPES | Function: May be involved in the biogenesis of curli organelles.
Location Topology: Lipid-anchor
Sequence Mass (Da): 30557
Sequence Length: 277
Subcellular Location: Cell membrane
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A0A0K1IRS6 | MTANKQVRAVLLAALMVFSVFAGSIAFTGTAAAAATSATVSPDTVDKGPSASVDVTVNSGGANDVHVWLDLNDDGYYNASEPNSTDTAAATATLSLSIPESVSAGEYNVSAAESASLTAGTTQQEAYDTLDVVAANPADFNSATHFDDGTPKVEVAFDEAVTVNEMNVTDGETNLSQSVSVSSGQVNVTLSQVYTDDLEVTYNVTDTSGNTATATEDVTFAPIYVANESNNTAYQGSNVAVVASAVDTDVEVEGADDDNNYQFSGSTGPNSQVFVFDTDGKTLDTYQFTVGGAQKAQVDVRDLGLELTVDDLNITTKDGI... | Function: S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coats the surface of the cell.
PTM: Glycosylated.
Sequence Mass (Da): 89168
Sequence Length: 855
Subcellular Location: Secreted
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Q5V7F4 | MTNTKQKINAVFLSALMVMSVFAAAVAFSGAAAAANRGAGFTYSTGPTDSNGGGNGDSVGQVGPGAVVFQGEEDLEDGGNFGSNTDIGQLQKVSGDNSGILLGNPIPQDQPTGSYTFDGNSGTDGVTLQTPRVTSVEVQNGGSGDVTGSTLQTSSSGPDAFVRADYNFQEAEDLEITVEDENGLEVTNEIVVQKTGLPTADRNNDNGASGSNGDFDVGWELDTTDIDEGQYTITVEGTEDLTFGDASETVTVNITSDQQASLNLDNDEVVQGENLQFNVENSPEGNYHVVLVESSEFRDGITADQASRIFRNVGDVQEVG... | Function: S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.
PTM: Asn-455 is glycosylated by a pentasaccharide comprising a hexose, 2 hexuronic acids, a methyl ester of a hexuronic acid and a final hexose. The complete pentasaccharide is first assembl... |
B0R8E4 | MTDTTGKLRAVLLTALMVGSVIGAGVAFTGGAAAANASDLNDYQRFNENTNYTYSTASEDGKTEGSVASGATIFQGEEDVTFRKLDNEKEVSPATLSRTGGSDEGVPLQMPIPEDQSTGSYDSNGPDNDEADFGVTVQSPSVTMLEVRNNADNDVTGGVLNTQQDESSIAVDYNYYAAEDLELTVEDEDGLDVTDEILAADQSGGAYEDGTGNNGPNTLRFDIDPNNVDAGDYTVSVEGVEDLDFGDATESASVTISSSNKASLNLAEDEVVQGANLKYTIENSPEGNYHAVTIDSSDFRDSSSGADAAKVMRSVGDTVD... | Function: S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.
PTM: N-linked glycan at Asn-36 consists of a glycosaminoglycan chain, constructed by a repeating sulfated pentasaccharide block composed of GlcNAc, GalNAc, Gal, GalA, 3-O-methyl-GalA, and su... |
P25062 | MTKLKDQTRAILLATLMVTSVFAGAIAFTGSAAAERGNLDADSESFNKTIQSGDRVFLGEEISTDAGLGASNPLLTGTAGNSEGVSLDLSSPIPQTTENQPLGTYDVDGSGSATTPNVTLLAPRITDSEILTSSGGDVTGSAISSSDAGNLYVNADYNYESAEKVEVTVEDPSGTDITNEVLSGTDTFVDDGSIGSTSSTGGGVGIDMSDQDAGEYTIILEGAEDLDFGDATETMTLTISSQDEIGIELDSESVTQGTDVQYTVTNGIDGNEHVVAMDLSDLQNDATTEQAKEVFRNIGDTSEVGIANSSATNTSGSSTG... | Function: S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.
PTM: O-glycosylated on 4 to 6 threonine residues; glycans consist of Glc-Gal disaccharides.
Sequence Mass (Da): 85189
Sequence Length: 827
Domain: The glycoprotein is arranged on a p6 lattic... |
Q8TSG7 | MKRFAALSLAALMLLTVFASAASAVDVIEIRGPVYNGSDIDDIIDTYGDGTILTMDATDFAAFYYDIDDNVTTETLSIEDVPDTEGNVIGEGGLIYETTIQEVEYEYYNPDAGWDNYSLMGFFAEKYIPINPDKADKLSKLILDSDDKYTIRTGEMLDLGEGYAIEAKQVDVDGEKVWLEFTKDGEFVDDEIISVSTADDEANTWDVELDDIEDEDDVIVLKVHVNQVFQGAVDSIAQIEGLWLIDYANAMTIESDDEFGNLDDVSIDGDTLTITNEDTFTLTRDDEEEIGEGLYFATADTPSNVLRFYAMKEITDPGTY... | Function: S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.
PTM: Glycosylated.
Sequence Mass (Da): 74394
Sequence Length: 671
Subcellular Location: Secreted
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P27373 | MRKFTLLMLLLIVISMSGIAGAAEVKNLNTSKTFTKIQEAIDDPSTTDGNIIIVGPGNYTENILVNKSLTLKSNGSAIINAVSSEKSTITIKANNVWIEGFIIIGGKNGIYMENVTGCTITNNTIQNAFVSGWEYYGGNGICLVNSTNNTITNNIIRNNTWNGINVCESKGNIIKNNTIMYSGGIGIYVWGFNKFEGNNIIENNRIINATYGGIYLFRPSNNKICRNYIANVSSGGGGMSGAICIDVSDYNIVKDNIGINCDGGLFTDGMIGNEITNNIFKNCKVAVSESTYGPASRNNKIYGNYFINYETAISDPKGEL... | Function: The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.
PTM: N-glycosylated; contains glycans composed of methyl-Man, Man and GalNAc residues in a molar ratio of 2:3:1.
Sequence Mass (Da): 65481
Sequence Length: 593
Subcellular Location: Secreted
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