ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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O34705 | MWTWKADRPVAVIVIIHGASEYHGRYKWLIEMWRSSGYHVVMGDLPGQGTTTRARGHIRSFQEYIDEVDAWIDKARTFDLPVFLLGHSMGGLVAIEWVKQQRNPRITGIILSSPCLGLQIKVNKALDLASKGLNVIAPSLKVDSGLSIDMATRNEDVIEADQNDSLYVRKVSVRWYRELLKTIESAMVPTEAFLKVPLLVMQAGDDKLVDKTMVIKWFNGVASHNKAYREWEGLYHEIFNEPEREDVFKAARAFTDQYI | Function: Phospholipase involved in the biosynthesis of the antibiotic bacilysocin. It probably catalyzes the hydrolysis of the 2-sn-acyl moiety of phosphatidylglycerol to produce bacilysocin (lysophosphatidylglycerol). Is also able to catalyze the hydrolysis reaction of one acyl bond in phosphatidylcholine in vitro (actual cleavage point is unknown), resulting in lysophosphatidylcholine.
Sequence Mass (Da): 29566
Sequence Length: 259
Pathway: Antibiotic biosynthesis; bacilysocin biosynthesis.
EC: 3.1.1.-
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Q9XWV2 | MNWIFIFLAAAVAIGCEARQERTYTVCQKPEGDLHYFKEGRKTDEELCAKRLATAYFHDEVNQTGWAFLEVDVISPKIPHYLQGYAAGFAEGRATRHLIDLHIINTVNGYCDGAKHFCDELGEFMVDNLKWMEQEIRENPEDEYWQQVNLTVNQLFGLIHGYENQLGAEIDFKQIAVHPIFMIQIAGDLEDLAMKFKKPENPKKVFSGPGHCSALVKLLPKNEDILFSHVTWSSYGTMLRINKKYSFKTGDPGQIYSFSSYPASITSTDDFVLTSAKLAILETTIGNYNEKSLDLITPNTVLTWIRAEIAHRTASSGLQWAEAFGRHNSGTYNNEWVVVDYKQFHRGKEVQPETGIIHVVEQMPGHIVHSDKTAHLFRETYWPGYNQPYYKQIIRFSDTDKMVEKFGDWYSYDKTPRALIFKRDHNTVTDMSSMIALMRSNNYTKDPLSKCDCNPPYSAENAIACRSDLNPLNGTYPFKSLGFRDHGAIDVKVTNSKLINSLQFTAVSGPPGGVTKDVPIFDWKTSPLREKVPHFGQPDRWNFAPVTYKWRKDAHRHYHLYQKLHKELSSL | Function: Putative phospholipase.
Sequence Mass (Da): 65439
Sequence Length: 571
Subcellular Location: Lysosome
EC: 3.1.1.-
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Q6P4A8 | MTRGGPGGRPGLPQPPPLLLLLLLLPLLLVTAEPPKPAGVYYATAYWMPAEKTVQVKNVMDKNGDAYGFYNNSVKTTGWGILEIRAGYGSQTLSNEIIMFVAGFLEGYLTAPHMNDHYTNLYPQLITKPSIMDKVQDFMEKQDKWTRKNIKEYKTDSFWRHTGYVMAQIDGLYVGAKKRAILEGTKPMTLFQIQFLNSVGDLLDLIPSLSPTKNGSLKVFKRWDMGHCSALIKVLPGFENILFAHSSWYTYAAMLRIYKHWDFNVIDKDTSSSRLSFSSYPGFLESLDDFYILSSGLILLQTTNSVFNKTLLKQVIPETLLSWQRVRVANMMADSGKRWADIFSKYNSGTYNNQYMVLDLKKVKLNHSLDKGTLYIVEQIPTYVEYSEQTDVLRKGYWPSYNVPFHEKIYNWSGYPLLVQKLGLDYSYDLAPRAKIFRRDQGKVTDTASMKYIMRYNNYKKDPYSRGDPCNTICCREDLNSPNPSPGGCYDTKVADIYLASQYTSYAISGPTVQGGLPVFRWDRFNKTLHQGMPEVYNFDFITMKPILKLDIK | Function: In view of the small size of the putative binding pocket, it has been proposed that it may act as an amidase or a peptidase (By similarity). Exhibits a weak phospholipase activity, acting on various phospholipids, including phosphatidylcholine, phosphatidylinositol, phosphatidylethanolamine and lysophospholipids.
PTM: The maturation cleavages that produces chains A and B are required to open the putative substrate binding pocket. Both chains A and B remain associated in the mature protein.
Sequence Mass (Da): 63255
Sequence Length: 553
Subcellular Location: Lysosome
EC: 3.1.1.-
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O62146 | MTRLIRSKKQFLIRSLHSVFYYLGSLLHSTFEMNVFIGLLLATVVASQSSEGRDESYTYKQLCIVDDKPQVLDGFDCRNQVAVARWQNAVNTTGWTFLEVETKENYCPQLQAYSAGYLEGLLSKTVLTYHLKNAQEDYCKNFTGYCSRLSDFLTENQKWIQSSLETVAPDDLYWGAVNRTYHQVSGLIDAYEGREFKPRITYELHPILYLNLNGDFYDLEKKLNKTRDPAFEQTGGKCSGLIKVAPGNADLFISQVTMSGFQNMLRVIKLYKFGYDRQFYPGYASSFSSYPGLLYSSDDFALQTSGLAVIETTISVFNTSLFENTKPVGQLPTWIRAIVSNQLARDAREWCKLYSLYNSGTYNNQWAVLDYKKFKPNQPLPKNGLFYVLEQMPGKIVYSDLTWFVEKYSYFPSYNIPFFKEITEISGFIGQAAKMGDWFKWGASPRAKIFERDHGNVHDLDSLTALMRYNDYKNDEFSKCKCNPPYSAEAGISARGDLNPANGTYEFPGQGHVNHGALDYKGTNVELMKKLQFVAQGGPTWGKVPSFKWSEFDFKDKVNHVGHPDEWKFNTLVHKWETEINA | Function: Putative phospholipase.
Sequence Mass (Da): 66638
Sequence Length: 582
Subcellular Location: Secreted
EC: 3.1.1.-
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Q8NHP8 | MVGQMYCYPGSHLARALTRALALALVLALLVGPFLSGLAGAIPAPGGRWARDGQVPPASRSRSVLLDVSAGQLLMVDGRHPDAVAWANLTNAIRETGWAFLELGTSGQYNDSLQAYAAGVVEAAVSEELIYMHWMNTVVNYCGPFEYEVGYCERLKSFLEANLEWMQEEMESNPDSPYWHQVRLTLLQLKGLEDSYEGRVSFPAGKFTIKPLGFLLLQLSGDLEDLELALNKTKIKPSLGSGSCSALIKLLPGQSDLLVAHNTWNNYQHMLRVIKKYWLQFREGPWGDYPLVPGNKLVFSSYPGTIFSCDDFYILGSGLVTLETTIGNKNPALWKYVRPRGCVLEWVRNIVANRLASDGATWADIFKRFNSGTYNNQWMIVDYKAFIPGGPSPGSRVLTILEQIPGMVVVADKTSELYQKTYWASYNIPSFETVFNASGLQALVAQYGDWFSYDGSPRAQIFRRNQSLVQDMDSMVRLMRYNDFLHDPLSLCKACNPQPNGENAISARSDLNPANGSYPFQALRQRSHGGIDVKVTSMSLARILSLLAASGPTWDQVPPFQWSTSPFSGLLHMGQPDLWKFAPVKVSWD | Function: Putative phospholipase.
PTM: The p76 protein is synthesized as a 80 kDa precursor which is then processed into a N-terminal 32 kDa form and a C-terminal 45 kDa form.
Sequence Mass (Da): 65472
Sequence Length: 589
Subcellular Location: Lysosome lumen
EC: 3.1.1.-
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P59588 | MFQQQKDWETRENAFAAFTMGPLTDFWRQRDEAEFTGVDDIPVRFVRFRAQHHDRVVVICPGRIESYVKYAELAYDLFHLGFDVLIIDHRGQGRSGRLLADPHLGHVNRFNDYVDDLAAFWQQEVQPGPWRKRYILAHSMGGAISTLFLQRHPGVCDAIALTAPMFGIVIRMPSFMARQILNWAEAHPRFRDGYAIGTGRWRALPFAINVLTHSRQRYRRNLRFYADDPTIRVGGPTYHWVRESILAGEQVLAGAGDDATPTLLLQAEEERVVDNRMHDRFCELRTAAGHPVEGGRPLVIKGAYHEILFEKDAMRSVALHAIVDFFNRHNSPSGNRSTEV | Catalytic Activity: a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine
Sequence Mass (Da): 38978
Sequence Length: 340
Subcellular Location: Cell inner membrane
EC: 3.1.1.5
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P44800 | MIREPYFHQFALAELLPFFEQFPTQYLSGKRNIKLAYRHLIQPESAVRKLMILVNGRAENMLKWSELAYDFYHQGYDVLLFDHRGQGYSQRIIPQKGHLDEFRFYVDDMAKIIEKVTALFSYSTQHLLAHSMGALIATYYLANYDHHINKAVLSSPFYGILLKHPIRDELIITLMNILGQGERYVFGKGAYQQAHLEYNELTFCKTRMKWMNRINRKNPAINLGGPTFRWVHLCLNAIKRLPKVIPKIEIPILILQAEKEKIVDNKNLEKLTALFPNARCEVILNAKHEVLFEKDNVRRNVLKSVNHFLNVQS | Catalytic Activity: a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine
Sequence Mass (Da): 36658
Sequence Length: 313
Subcellular Location: Cell inner membrane
EC: 3.1.1.5
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Q9C5Y0 | MAEKVSEDVMLLHGDLDLKIVKARRLPNMDMFSEHLRRLFTACNACARPTDTDDVDPRDKGEFGDKNIRSHRKVITSDPYVTVVVPQATLARTRVLKNSQEPLWDEKFNISIAHPFAYLEFQVKDDDVFGAQIIGTAKIPVRDIASGERISGWFPVLGASGKPPKAETAIFIDMKFTPFDQIHSYRCGIAGDPERRGVRRTYFPVRKGSQVRLYQDAHVMDGTLPAIGLDNGKVYEHGKCWEDICYAISEAHHMIYIVGWSIFHKIKLVRETKVPRDKDMTLGELLKYKSQEGVRVLLLVWDDKTSHDKFGIKTPGVMGTHDEETRKFFKHSSVICVLSPRYASSKLGLFKQQASPSSSIYIMTVVGTLFTHHQKCVLVDTQAVGNNRKVTAFIGGLDLCDGRYDTPEHRILHDLDTVFKDDFHNPTFPAGTKAPRQPWHDLHCRIDGPAAYDVLINFEQRWRKATRWKEFSLRLKGKTHWQDDALIRIGRISWILSPVFKFLKDGTSIIPEDDPCVWVSKEDDPENWHVQIFRSIDSGSVKGFPKYEDEAEAQHLECAKRLVVDKSIQTAYIQTIRSAQHFIYIENQYFLGSSYAWPSYRDAGADNLIPMELALKIVSKIRAKERFAVYVVIPLWPEGDPKSGPVQEILYWQSQTMQMMYDVIAKELKAVQSDAHPLDYLNFYCLGKREQLPDDMPATNGSVVSDSYNFQRFMIYVHAKGMIVDDEYVLMGSANINQRSMAGTKDTEIAMGAYQPNHTWAHKGRHPRGQVYGYRMSLWAEHLGKTGDEFVEPSDLECLKKVNTISEENWKRFIDPKFSELQGHLIKYPLQVDVDGKVSPLPDYETFPDVGGKIIGAHSMALPDTLTT | Cofactor: Ca(2+). Requires millimolar level (PIP2-dependent).
Function: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond to generate phosphatidic acids (PA). May be involved in PA accumulation in the dehydration stress response and in the transduction of hormonal and environmental signals to the microtubules cytoskeleton . Prefers phosphatidylethanolamine to phosphatidylcholine as substrate . Involved in H(2)O(2) and abscisic acid (ABA)-induced stomatal closure . Involved in nitric oxide (NO) signaling during stomatal closure . Plays a positive role in ABA-promoted senescence . Involved in basal defense and nonhost resistance .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + choline + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 98917
Sequence Length: 868
Domain: C2 domain is a calcium-binding fold, and the binding promotes the protein association with membranes. In PLD delta, all the calcium-coordinating acidic amino acids are conserved.
Subcellular Location: Cell membrane
EC: 3.1.4.4
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Q9T053 | MAYHPAYTETMSMGGGSSHGGGQQYVPFATSSGSLRVELLHGNLDIWVKEAKHLPNMDGFHNRLGGMLSGLGRKKVEGEKSSKITSDPYVTVSISGAVIGRTFVISNSENPVWMQHFDVPVAHSAAEVHFVVKDSDIIGSQIMGAVGIPTEQLCSGNRIEGLFPILNSSGKPCKQGAVLGLSIQYTPMERMRLYQMGVGSGNECVGVPGTYFPLRKGGRVTLYQDAHVDDGTLPSVHLDGGIQYRHGKCWEDMADAIRQARRLIYITGWSVFHPVRLVRRTNDPTEGTLGELLKVKSQEGVRVLVLVWDDPTSRSLLGFKTQGVMNTSDEETRRFFKHSSVQVLLCPRSGGKGHSFIKKSEVGTIYTHHQKTVIVDAEAAQNRRKIVAFVGGLDLCNGRFDTPKHPLFRTLKTLHKDDFHNPNFVTTADDGPREPWHDLHSKIDGPAAYDVLANFEERWMKASKPRGIGKLKSSSDDSLLRIDRIPDIVGLSEASSANDNDPESWHVQVFRSIDSSSVKGFPKDPKEATGRNLLCGKNILIDMSIHAAYVKAIRSAQHFIYIENQYFLGSSFNWDSNKDLGANNLIPMEIALKIANKIRAREKFAAYIVIPMWPEGAPTSNPIQRILYWQHKTMQMMYQTIYKALVEVGLDSQFEPQDFLNFFCLGTREVPVGTVSVYNSPRKPPQPNANANAAQVQALKSRRFMIYVHSKGMVVDDEFVLIGSANINQRSLEGTRDTEIAMGGYQPHYSWAMKGSRPHGQIFGYRMSLWAEHLGFLEQGFEEPENMECVRRVRQLSELNWRQYAAEEVTEMSGHLLKYPVQVDRTGKVSSLPGCETFPDLGGKIIGSFLALQENLTI | Cofactor: Ca(2+). Requires micromolar level (PIP2-dependent).
Function: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond to generate phosphatidic acids (PA). Plays an important role in various cellular processes, including phytohormone action, vesicular trafficking, secretion, cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis, membrane deterioration and senescence . Can use phosphatidylserine (PS) and phosphatidylethanolamine (PE) as substrates only in the presence of PIP2. Can use phosphatidylcholine (PC), phosphatidylglycerol (PG) or N-acylphosphatidylethanolamine (NAPE) as substrates in the presence of PE and PIP2 . Involved in membrane lipid modulation under aluminum (Al) stress and negatively modulate plant tolerance to Al .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + choline + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 95588
Sequence Length: 858
Domain: C2 domain is a calcium-binding fold, and the binding promotes the protein association with membranes. In PLD gamma, all the calcium-coordinating acidic amino acids are conserved.
Subcellular Location: Cytoplasm
EC: 3.1.4.4
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Q9T051 | MSMGGGSNHEFGQWLDQQLVPLATSSGSLMVELLHGNLDIWVKEAKHLPNMICYRNKLVGGISFSELGRRIRKVDGEKSSKFTSDPYVTVSISGAVIGRTFVISNSENPVWMQHFDVPVAHSAAEVHFVVKDNDPIGSKIIGVVGIPTKQLCSGNRIEGLFPILNSSGKPCRKGAMLSLSIQYTPMERMRLYQKGVGSGVECVGVPGTYFPLRKGGRVTLYQDAHVDDGTLPSVHLDGGIQYRHGKCWEDMADAIRRARRLIYITGWSVFHPVRLVRRNNDPTEGTLGELLKVKSQEGVRVLVLVWDDPTSMSFPGFSTKGLMNTSDEETRRFFKHSSVQVLLCPRYGGKGHSFIKKSEVETIYTHHQKTMIVDAEAAQNRRKIVAFVGGLDLCNGRFDTPKHSLFGTLKTLHKDDFHNPNFVTTEDVGPREPWHDLHSKIDGPAAYDVLANFEERWMASKPRGIGKGRTSFDDSLLRINRIPDIMGLSEASSANDNDPESWHVQVFRSIDSTSVKGFPKDPEEATGRNLLCGKNILIDMSIHAAYVKAIRSAQHFIYIENQYFLGSSFNWDSNKDLGANNLIPMEIALKIANKIRARENFAAYIVIPMWPEGAPTSKPIQRILYWQHKTMQMMYQTIYKALLEVGLDGQLEPQDFLNFFCLGNREVGTREVPDGTVNVYNCPRKPPQPNAAQVQALKSRRFMIYVHSKGMVVDDEFVLIGSANINQRSLEGTRDTEIAMGGYQPHHSWAKKGSRPRGQIFGYRMSLWAEHLGFLEQEFEEPENMECVRRVRQLSELNWGQYAAEEVTEMSGHLLKYPVQVDKTGKVSSLPGCETFPDLGGKIIGSFLTLQENLTI | Cofactor: Ca(2+). Requires micromolar level (PIP2-dependent).
Function: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond to generate phosphatidic acids (PA). Plays an important role in various cellular processes, including phytohormone action, vesicular trafficking, secretion, cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis, membrane deterioration and senescence. Can use phosphatidylserine but prefers ethanolamine-containing lipids as substrates. Can use phosphatidylcholine (PC) as substrates in the presence of phosphatidylethanolamine (PE) and PIP2 . Involved in membrane lipid modulation under aluminum (Al) stress and negatively modulate plant tolerance to Al .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + choline + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 96024
Sequence Length: 856
Domain: C2 domain is a calcium-binding fold, and the binding promotes the protein association with membranes. In PLD gamma, all the calcium-coordinating acidic amino acids are conserved.
Subcellular Location: Cytoplasm
EC: 3.1.4.4
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Q86AV9 | MKNKIILLWLLLIVILCTISNVKGCGMTTHNTVARRAYNFSSFDGFEQYQKYVSENFDVFDAGAAFPDFGYDCGGLANESEAAHWPPFLRAATKYLLETYPQPWSLDGIRLAVFLLGVTSHQIADISWHSIGGIQQGLIRAMAGQDFNGTYELAHGNADEGGEFELAYNYDLSWLSDKWYVPITDIKNIFHSMNYPRVDDENLLRCNAILYAGAMGVKIGGRFFYPEIAKKSPFLVDHYQDYFIGGLDDMSIWTSYCWPVLMGWMDGEDIGDFCFIQPDPNNDDDNQHLRLHHKHSILKNGSKIKEALSKSILNEMKITNNGKGVTFSLPNSMEKAINQVLNKFNQNPIGTLLEKYLPNLFNNKNKFYQENENEQYNHDEEELNIIDIDIDIEEEEQEEEEDKPIRMLSKNNNFKNYEYLNDKKKSSSSKLKNKSKKNIIKLNSDSNDLGTNFTTIYGQNMYSYFGKDIRSKDLNGDGFDDLIISSPGFGVPGSMQTGCVYYIISNGSSVTIDGGSGFTSEFDIDQVATGKLCGNETHAKFGWNIDVLDFNLDGIFDIIIGAPSSSNANLQYLGMIYIYLGEKNNPAGEWSTESDLPSITIQGIEYADTIGTVLRVADCNADSNADLILGSPHSAGGGTQRGTVQIFYSSKKRISGIPISLNDADYYGHGEVDYEWFGYEIKVAGQGDSSTLLVGSPNYHDEETAIVNIGKITSFPYNVNLNSFDLNPKFVMVGVNKNDKLGYSYNMVNGSLFGLDNVNDIMVLSLPTRGFGDDFDQVGEVVLIDIDNLSGFVEIKNVNLLLSIKGTTKYSRFGESLLIGKLESTDEFARLFVGAPLWTDSIDTGPGCVFTFLPNQHLTNDPAVLKQNIINNTPVVIYDSTHSIKTFRIDDDSGSSGGRSFNNKRKDSRFGFRILLSDFNNDGKNDLIVSADRDSSKILEGGSINIFQ | Cofactor: Binds Ca(2+).
Function: Hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane. May also cleave GPI anchor intermediates intracellularly.
Catalytic Activity: an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol + a 1,2-diacyl-sn-glycero-3-phosphate + H(+)
Sequence Mass (Da): 105705
Sequence Length: 948
Subcellular Location: Secreted
EC: 3.1.4.50
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Q988B7 | MTERLAGKTALVTGAAQGIGKAIAARLAADGATVIVSDINAEGAKAAAASIGKKARAIAADISDPGSVKALFAEIQALTGGIDILVNNASIVPFVAWDDVDLDHWRKIIDVNLTGTFIVTRAGTDQMRAAGKAGRVISIASNTFFAGTPNMAAYVAAKGGVIGFTRALATELGKYNITANAVTPGLIESDGVKASPHNEAFGFVEMLQAMKGKGQPEHIADVVSFLASDDARWITGQTLNVDAGMVRH | Function: Involved in the degradation of pyridoxine or pyridoxamine (free, phosphate-unbound, forms of vitamin B6). Oxidizes pyridoxal to 4-pyridoxolactone, but does not have activity toward pyridoxal 5'-phosphate, pyridoxine, pyridoxamine, pyridoxamine 5'-phosphate, 4-phthalaldehyde, 2-nitrobenzaldehyde, pyridine, formaldehyde, 2-carboxybenzaldehyde or sugars.
Catalytic Activity: NAD(+) + pyridoxal = 4-pyridoxolactone + H(+) + NADH
Sequence Mass (Da): 25531
Sequence Length: 248
Pathway: Cofactor degradation; B6 vitamer degradation; 4-pyridoxate from pyridoxal: step 1/2.
EC: 1.1.1.107
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O17405 | MPLRLINFRQQRRCRQSPSVARLESIVLNRRELLLDHFQYSLFQNSSEIPMTTILINDRPMRHTHDGRADMTNFEMDLFDTRIEVPTSKNSGGDGMHSPYYDEESSKKRCCKCGNSRNRIIKPACVPISIVSLFIIALVFLPLFNEEDLASPIKLTTGCSVDCKTFLVESIPIGLPFKTNNHTAEAWINIIDNSKQYLDISVMYWNLNTSDYKSSVYGRRVYEAIIRAGKRGVKIRIAQDGASNLSDNKESAYLVQEGLAEVREINVTRLIGSGIIHTKFILSDIATLYIGSANMDWKSLSEVKEVGVVFQECPCVASDLYKIFAAYWKLGENDSVIPEKWPISYRTPFNFSSMAKLTMDGEPAEYFISSSPGPFNPKGREHDLAAIQKIMKDARKSVCISVMDYIPSTLYMKKSNRFWPEIDDSIRDAAYRGVNVRMLISHWDHSRKEMIPFLKSLQTITDGLPRYNRTEHGQVQVRIFTVPPNGKEKIPFTRVNHAKYMVTEDIAYIGTSNWSGDYFISTAGVAMVVRQPSATKRLQNVFDRDWNSEYSKDL | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + choline + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 63216
Sequence Length: 554
Subcellular Location: Membrane
EC: 3.1.4.4
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Q8IUK5 | MRGELWLLVLVLREAARALSPQPGAGHDEGPGSGWAAKGTVRGWNRRARESPGHVSEPDRTQLSQDLGGGTLAMDTLPDNRTRVVEDNHSYYVSRLYGPSEPHSRELWVDVAEANRSQVKIHTILSNTHRQASRVVLSFDFPFYGHPLRQITIATGGFIFMGDVIHRMLTATQYVAPLMANFNPGYSDNSTVVYFDNGTVFVVQWDHVYLQGWEDKGSFTFQAALHHDGRIVFAYKEIPMSVPEISSSQHPVKTGLSDAFMILNPSPDVPESRRRSIFEYHRIELDPSKVTSMSAVEFTPLPTCLQHRSCDACMSSDLTFNCSWCHVLQRCSSGFDRYRQEWMDYGCAQEAEGRMCEDFQDEDHDSASPDTSFSPYDGDLTTTSSSLFIDSLTTEDDTKLNPYAGGDGLQNNLSPKTKGTPVHLGTIVGIVLAVLLVAAIILAGIYINGHPTSNAALFFIERRPHHWPAMKFRSHPDHSTYAEVEPSGHEKEGFMEAEQC | Function: Plays a critical role in endothelial cell capillary morphogenesis.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 55760
Sequence Length: 500
Subcellular Location: Secreted
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Q91ZV7 | MRAQLWLLQLLLLRGAARALSPATPAGHNEGQDSAWTAKRTRQGWSRRPRESPAQVLKPGKTQLSQDLGGGSLAIDTLPDNRTRVVEDNHNYYVSRVYGPGEKQSQDLWVDLAVANRSHVKIHRILSSSHRQASRVVLSFDFPFYGHPLRQITIATGGFIFMGDMLHRMLTATQYVAPLMANFNPGYSDNSTVAYFDNGTVFVVQWDHVYLQDREDRGSFTFQAALHRDGRIVFGYKEIPMAVLDISSAQHPVKAGLSDAFMILNSSPEVPASQRRTIFEYHRVELDSSKITTTSAVEFTPLPTCLQHQSCDTCVSSNLTFNCSWCHVLQRCSSGFDRYRQEWLTYGCAQEAEGKTCEDFQDDSHYSASPDSSFSPFNGDSTTSSSLFIDSLTTEDDTKLNPYAEGDGLPDHSSPKSKGPPVHLGTIVGIVLAVLLVAAIILAGIYISGHPNSNAALFFIERRPHHWPAMKFHNHPNHSTYTEVEPSGHEKEGFVEAEQC | Function: Plays a critical role in endothelial cell capillary morphogenesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 55635
Sequence Length: 500
Subcellular Location: Cell membrane
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Q54K50 | MIINRLFIIIVLFFVNVNSKIISESTLNSCQGGTIQIAESIPLGLDISTNLSTHDAWMDLITNAQESIDLGFFYFTLLGGSDLDPVYGGQLGIDIFNAIVEAHSRGINVRIVQNEPSESFPDTETQTLAKLGIQVRSIDWVSLVGSGVLHTKLIIIDESSAYVGSANADWSSLAQVKELGIVLKNCPTMVADTEIAFQQYWNAADFTSLPINDWGSNYQALFNNTNMASLSLNNNNNNNNKNKNNDNDGSGTNQMYEMFLAVSPPQFQSTYRTGDIDALMDAINNADQSICITVMDYTPTTLYNDPNTYWPLIDNALRAAAFNRNVQVRMLISHWNYTSPIIPQWLHSLNQVDNIQVRWFVVPDFSTNPQIPYTRVNHAKFMVTEKQSYVGTSNWSQDYFTVTGGLSYNVFNNDFTNQLQSIFNRDWNSPYTQPIQNF | Function: Hydrolyzes membrane phospholipids, such as PtdCho (phosphatidylcholine), producing the free headgroup and PtdOH (phosphatidic acid; signaling molecule on its own).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + choline + H(+)
Sequence Mass (Da): 49186
Sequence Length: 438
EC: 3.1.4.4
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P20626 | MREKVVLFLSIIMAIMLPVGNAAAAPVVHNPASTANRPVYAIAHRVLTTQGVDDAVAIGANALEIDFTAWGRGWWADHDGIPTSAGATAEEIFKHIADKRKQGANITFTWLDIKNPDYCRDARSVCSINALRDLARKYLEPAGVRVLYGFYKTVGGPAWKTITADLRDGEAVALSGPAQDVLNDFARSENKILTKQKIADYGYYNINQGFGNCYGTWNRTCDQLRKSSEARDQGKLGKTFGWTIATGQDARVNDLLGKANVDGLIFGFKITHFYRHADTENSFKAIKRWVDKHSATHHLATVADNPW | Function: Virulence factor affecting bacterial dissemination and survival within the host . Has magnesium-dependent catalytic activity toward sphingomyelin (SM) and acyl- and alkyl-lysophosphatidylcholine (LPC), but not toward sphingosylphosphorylcholine (SPC) and phosphatidylcholine (PC) . Lysophosphatidic acid (LPA), assumed to result from LPC hydrolysis, evokes pathophysiological responses after LPA receptor internalization . Shows hemolytic activity .
Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine 1-phosphate + choline + H(+)
Sequence Mass (Da): 33884
Sequence Length: 307
EC: 3.1.4.-
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O00469 | MGGCTVKPQLLLLALVLHPWNPCLGADSEKPSSIPTDKLLVITVATKESDGFHRFMQSAKYFNYTVKVLGQGEEWRGGDGINSIGGGQKVRLMKEVMEHYADQDDLVVMFTECFDVIFAGGPEEVLKKFQKANHKVVFAADGILWPDKRLADKYPVVHIGKRYLNSGGFIGYAPYVNRIVQQWNLQDNDDDQLFYTKVYIDPLKREAINITLDHKCKIFQTLNGAVDEVVLKFENGKARAKNTFYETLPVAINGNGPTKILLNYFGNYVPNSWTQDNGCTLCEFDTVDLSAVDVHPNVSIGVFIEQPTPFLPRFLDILLTLDYPKEALKLFIHNKEVYHEKDIKVFFDKAKHEIKTIKIVGPEENLSQAEARNMGMDFCRQDEKCDYYFSVDADVVLTNPRTLKILIEQNRKIIAPLVTRHGKLWSNFWGALSPDGYYARSEDYVDIVQGNRVGVWNVPYMANVYLIKGKTLRSEMNERNYFVRDKLDPDMALCRNAREMGVFMYISNRHEFGRLLSTANYNTSHYNNDLWQIFENPVDWKEKYINRDYSKIFTENIVEQPCPDVFWFPIFSEKACDELVEEMEHYGKWSGGKHHDSRISGGYENVPTDDIHMKQVDLENVWLHFIREFIAPVTLKVFAGYYTKGFALLNFVVKYSPERQRSLRPHHDASTFTINIALNNVGEDFQGGGCKFLRYNCSIESPRKGWSFMHPGRLTHLHEGLPVKNGTRYIAVSFIDP | Function: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.
Catalytic Activity: 2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-lysyl-[collagen] + CO2 + succinate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 84686
Sequence Length: 737
Subcellular Location: Rough endoplasmic reticulum membrane
EC: 1.14.11.4
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O60568 | MTSSGPGPRFLLLLPLLLPPAASASDRPRGRDPVNPEKLLVITVATAETEGYLRFLRSAEFFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVRQWKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRTLPGGQPPPRVFLAVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVFHEPHIADSWPQLQDHFSAVKLVGPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLTNLQTLRILIEENRKVIAPMLSRHGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQRDVFSGSDTDPDMAFCKSFRDKGIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPVDWKEQYIHENYSRALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSGGRHEDSRLAGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESLFPGYHTKARAVMNFVVRYRPDEQPSLRPHHDSSTFTLNVALNHKGLDYEGGGCRFLRYDCVISSPRKGWALLHPGRLTHYHEGLPTTWGTRYIMVSFVDP | Function: Multifunctional enzyme that catalyzes a series of essential post-translational modifications on Lys residues in procollagen . Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens . Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine . Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues . Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues . Essential for normal biosynthesis and secretion of type IV collagens (Probable). Essential for normal formation of basement membranes (By similarity).
Catalytic Activity: 2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-lysyl-[collagen] + CO2 + succinate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 84785
Sequence Length: 738
Domain: The N-terminal domain mediates glycosyltransferase activity.
Subcellular Location: Rough endoplasmic reticulum
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Q9R0E1 | MAAAGPEPRLLLLLLLLLPPLPPVTSASDRPRGANAVNPDKLLVITVATAETEGYRRFLQSAEFFNYTVRTLGLGQEWRGGDVARTVGGGQKVRWLKKEMEKYADQKDMIIMFVDSYDVILASSPTELLKKFVQSGSHLLFSAESFCWPEWGLAEQYPEVGMGKRFLNSGGFIGFAPTIHQIVRQWNYKDDDDDQLFYTQLYLDPGLREKLKLSLDHKSRIFQNLNGALDEVILKFDQNRVRIRNVAYDTLPVVVHGNGPTKLQLNYLGNYVPNGWTPQGGCGFCNQTLRTLPGGQPPPRVLLAVFVEQPTPFLPRFLQRLLLLDYPPDRISLFLHNSEVYHEPHIADAWPQLQDHFSAVKLVGPEEALSAGEARDMAMDSCRQNPECEFYFSLDADAVLTNPETLRVLIEQNRKVIAPMLSRHGKLWSNFWGALSPNEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGETLRTELPQKEVFSSSDTDPDMAFCKSVRDKGIFLHLSNQHEFGRLLATSRYDTDHLHPDLWQIFDNPVDWREQYIHENYSRALDGEGLVEQPCPDVYWFPLLTEQMCDELVEEMEHYGQWSGGRHEDSRLAGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTEYLFPGYHTKTRAVMNFVVRYRPDEQPSLRPHHDSSTFTLNVALNHKGVDYEGGGCRFLRYDCRISSPRKGWALLHPGRLTHYHEGLPTTRGTRYIMVSFVDP | Function: Multifunctional enzyme that catalyzes a series of post-translational modifications on Lys residues in procollagen . Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens . Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine (By similarity). Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues . Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues . Catalyzes hydroxylation and glycosylation of Lys residues in the ADIPOQ collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues . Essential for normal biosynthesis and secretion of type IV collagens . Essential for normal formation of basement membranes .
PTM: N-glycosylated.
Location Topology: Peripheral membrane protein
Catalytic Activity: 2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-lysyl-[collagen] + CO2 + succinate
Sequence Mass (Da): 84922
Sequence Length: 741
Domain: The N-terminal domain mediates glycosyltransferase activity.
Subcellular Location: Rough endoplasmic reticulum
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Q20679 | MRVLPFLLPLIPVLLATTITDLPELVVVTVATENTDGLKRLLESAKAFDINIEVLGLGEKWNGGDTRIEQGGGQKIRILSDWIEKYKDASDTMIMFVDAYDVVFNADSTTILRKFFEHYSEKRLLFGAEPFCWPDQSLAPEYPIVEFGKRFLNSGLFMGYGPEMHKILKLKSVEDKDDDQLYYTMIYLDEKLRKELNMDLDSMSKIFQNLNGVIEDVELQFKEDGTPEAYNAAYNTKPLIVHGNGPSKSHLNYLGNYLGNRWNSQLGCRTCGLEVKESEEVPLIALNLFISKPIPFIEEVLQKIAEFDYPKEKIALYIYNNQPFSIKNIQDFLQKHGKSYYTKRVINGVTEIGDREARNEAIEWNKARNVEFAFLMDGDAYFSEPKVIKDLIQYSKTYDVGIIAPMIGQPGKLFTNFWGAIAANGYYARSEDYMAIVKGNRVGYWNVPFITSAVLFNKEKLEAMKDAYSYNKNLDPDMSMCKFARDNGHFLYIDNEKYYGFLIVSDEYAETVTEGKWHPEMWQIFENRELWEARYIHPGYHKIMEPEHVVDQACPDVYDFPLMSERFCEELIEEMEGFGRWSDGSNNDKRLAGGYENVPTRDIHMNQVGFERQWLYFMDTYVRPVQEKTFIGYYHQPVESNMMFVVRYKPEEQPSLRPHHDASTFSIDIALNKKGRDYEGGGVRYIRYNCTVPADEVGYAMMFPGRLTHLHEGLATTKGTRYIMVSFINP | Function: Multifunctional enzyme that catalyzes a series of post-translational modifications on Lys residues in procollagen . Catalyzes the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in type IV collagens (By similarity). Transfers galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine (By similarity). Catalyzes the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues . Essential for normal biosynthesis and secretion of type IV collagens . Essential for normal stability of the basement membrane .
Catalytic Activity: 2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-lysyl-[collagen] + CO2 + succinate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 84425
Sequence Length: 730
Domain: The N-terminal domain mediates glycosyltransferase activity.
Subcellular Location: Rough endoplasmic reticulum
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Q9VTH0 | MRIQQSALLLLLLAVTSQGDAESNWNDKIKVFTVATEPTDGYTRYIRSARVYDIEVTTLGLGEEWKGGDMQKPGGGFKLNLLREAIAPYKNEPETIILFTDSYDVIITTTLDEIFEKFKESGAKILFSAEKYCWPDKSLANDYPEVEGKASRFLNSGAFIGYAPQVFALLVDPIEDTADDQLYFTKIFLDETKRAKLGLKLDVQSRLFQNLHGAKNDVKLKVDLESNQGVLQNVDFMTTPSIIHGNGLSKVDLNAYGNYLARTFNGVCLLCQENLLDLEETNLPVISLALMVTQPVPFFDQFLEGIESLNYPKEKLHLLIYSNVAFHDDDIKSFVNKHAKEYATAKFALSTDELDERQGRQLALDKARLHQSDYIFFVDADAHIDDGEVLRELLRLNKQFVAPIFSKHKELWSNFWGALSEGGYYARSHDYVDIVKRELIGMFNVPHVTSIYLVKKTAFDAISFKHKEFDPDMAMCESLRNAGIFMYASNLRIFGHLVNADDFNTTVTRPDFYTLFSNEIDWTEKYIHPNYSLQLNESNKIQQPCPDVYWFQIVSDAFCDDLVAIMEAHNGWSDGSNNDNRLEGGYEAVPTRDIHMKQVGLERLYLKFLQMFVRPLQERAFTGYFHNPPRALMNFMVRYRPDEQPSLRPHHDSSTYTINIAMNRAGIDYQGGGCRFIRYNCSVTDTKKGWMLMHPGRLTHYHEGLLVTNGTRYIMISFIDP | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Forms hydroxylysine residues in collagen type IV (By similarity). Required for the secretion of collagen type IV (vkg) from haemocytes, fat body and follicle cells .
Catalytic Activity: 2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-lysyl-[collagen] + CO2 + succinate
Sequence Mass (Da): 82510
Sequence Length: 721
Subcellular Location: Endoplasmic reticulum
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Q5UQC3 | MISRTYVINLARRPDKKDRILAEFLKLKEKGVELNCVIFEAVDGNNPEHLSRFNFKIPNWTDLNSGKPMTNGEVGCALSHWSVWKDVVDCVENGTLDKDCRILVLEDDVVFLDNFMERYQTYTSEITYNCDLLYLHRKPLNPYTETKISTHIVKPNKSYWACAYVITYQCAKKFMNANYLENLIPSDEFIPIMHGCNVYGFEKLFSNCEKIDCYAVQPSLVKLTSNAFNDSETFHSGSYVPSNKFNFDTDKQFRIVYIGPTKGNSFHRFTEYCKLYLLPYKVIDEKETNDFVSLRSELQSLSEQDLNTTLMLVVSVNHNDFCNTIPCAPTNEFIDKYKQLTTDTNSIVSAVQNGTNKTMFIGWANKISEFINHYHQKLTESNAETDINLANLLLISSISSDFNCVVEDVEGNLFQLINEESDIVFSTTTSRVNNKLGKTPSVLYANSDSSVIVLNKVENYTGYGWNEYYGYHVYPVKFDVLPKIYLSIRIVKNANVTKIAETLDYPKELITVSISRSEHDSFYQADIQKFLLSGADYYFYISGDCIITRPTILKELLELNKDFVGPLMRKGTESWTNYWGDIDPSNGYYKRSFDYFDIIGRDRVGCWNVPYLASVYLIKKSVIEQVPNLFTENSHMWNGSNIDMRLCHNLRKNNVFMYLSNLRPYGHIDDSINLEVLSGVPTEVTLYDLPTRKEEWEKKYLHPEFLSHLQNFKDFDYTEICNDVYSFPLFTPAFCKEVIEVMDKANLWSKGGDSYFDPRIGGVESYPTQDTQLYEVGLDKQWHYVVFNYVAPFVRHLYNNYKTKDINLAFVVKYDMERQSELAPHHDSSTYTLNIALNEYGKEYTAGGCEFIRHKFIWQGQKVGYATIHAGKLLAYHRALPITSGKRYILVSFVN | Function: Displays two enzymatic activities involved in procollagen processing. Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines are subsequentially glucosylated by a glucosyltransferase activity. Collagen post-translationally modified is detected in mimivirus virion.
Catalytic Activity: 2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-lysyl-[collagen] + CO2 + succinate
Sequence Mass (Da): 103501
Sequence Length: 895
EC: 1.14.11.4
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Q10022 | MRDHVEFCYYVIIYSLEKFQQRSKQFGISLFIFFLATAAVTVIVPTLLGVSQRGFFCDDDSIRYEYRKDTITAVQLMLYNLVLNAATVLFVEYYRMQKVESNINNPRYRWRNNHLHVLFVRLLTYFGYSQIGFVMNIALNIVTKHVVGRLRPHFLDVCKLANDTCVTGDSHRYITDYTCTGPPELVLEARKSFYSGHSAVSLYCATWSALYIQARLGPVLNNRIVVPISQTLMFMIGLGISFSRITDNKHHWSDVLVGIFIGIFLAVYTCTFWTDLFSNNSTESETQPLLLPRPPRTPRNSEDEERHRLDAVLPSTDSSIVFEATGPQDSDTILLPVPQSA | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39028
Sequence Length: 341
Subcellular Location: Membrane
EC: 3.1.3.-
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O23179 | MENKSPSKKNKPPSCGSLVTILSLDGGGVRGIIAGVILAFLEKQLQELDGEEARLADYFDVIAGTSTGGLVTAMLTVPDETGRPHFAAKDIVPFYLEHCPKIFPQPTGVLALLPKLPKLLSGPKYSGKYLRNLLSKLLGETRLHQTLTNIVIPTFDIKKLQPTIFSSYQLLVDPSLDVKVSDICIGTSAAPTFFPPHYFSNEDSQGNKTEFNLVDGAVTANNPTLVAMTAVSKQIVKNNPDMGKLKPLGFDRFLVISIGTGSTKREEKYSAKKAAKWGIISWLYDDGSTPILDITMESSRDMIHYHSSVVFKALQSEDKYLRIDDDTLEGDVSTMDLATKSNLENLQKIGEKMLTNRVMQMNIDTGVYEPVAENITNDEQLKRYAKILSDERKLRRLRSDTMIKDSSNESQEIK | Function: Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Catalyzes the hydrolysis of the neutral lipids monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and phosphatidylglycerol (PG), and less efficiently the polar lipids phosphatidylcholine (PC) and phosphatidylinositol (PI), but not the storage lipid triacylglycerol (TAG). May play a role in root development.
PTM: Phosphorylated at Ser-399 by CPK3. Phosphorylation enhances PLP1 activity towards phosphatidylcholine.
Sequence Mass (Da): 45824
Sequence Length: 414
Domain: The nitrogen atoms of the two glycine residues in the GGXR motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Subcellular Location: Cytoplasm
EC: 3.1.1.-
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Q84QY3 | MAASYSCRRTCEACSTRAMAGCVVGEPASAPGQRVTLLAIDGGGIRGLIPGTILAFLEARLQELDGPDARLADYFDCIAGTSTGGLITAMLAAPGDHGRPLFAASDINRFYLDNGPLIFPQKRCGMAAAMAALTRPRYNGKYLQGKIRKMLGETRVRDTLTNVVIPTFDVRLLQPTIFSTYDAKSMPLKNALLSDICISTSAAPTYLPAHCFQTTDDATGKVREFDLIDGGVAANNPTMVAMTQITKKIMVKDKEELYPVKPSDCGKFLVLSVGTGSTSDQGMYTARQCSRWGIVRWLRNKGMAPIIDIFMAASSDLVDIHAAVMFQSLHSDGDYLRIQDNTLHGDAATVDAATRDNMRALVGIGERMLAQRVSRVNVETGRYVEVPGAGSNADALRGFARQLSEERRARLGRRNACGGGGEGEPSGVACKR | Function: Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Hydrolyzes phospholipids as well as galactolipids. May play a role in disease resistance (By similarity).
Sequence Mass (Da): 46400
Sequence Length: 432
Domain: The nitrogen atoms of the two glycine residues in the GGXR motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
EC: 3.1.1.-
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W7K139 | MSDDDDKIYIYSDLFSKNFSDDEKDDSYEREKQVYSGSETQNAENEYSKLRAQNSTILNNYFDNDNIKNVENLKSNDPDQIDLILFPVNKNYYMNLFDGQLIENIHSIKLRKAGFYAIYVENNNNSKWDGIYFGLSRMQVELDYKLITKKNKDGGEYEKRNTSSYDNTESVQNTVGSEKEETENKNEETSNYNSNLNNEINKICKYNLDQTDILLDDSNSERRRNSKFKIKNTNYYDNLMLQNKYTNSILYDDDDDKNNTETYTCTFKTEDQIRVPSQKKKYIYLYNKYDNATLDLNVHTYMSLGMSILCKYSLLYCGKYNHIPRDPYTPFKKPVSILSLDGGGILTISTLLVLNRLEAELRKEIGSDDIKLIDCFDMVCGTSAGGLISLALLREIDLQDVSNMWPSTIKKVFEGNRNIISGIFFEGYDVNNVKDVFLERMGNKFMSSYKKFYCFVTATDVKHKPYKLFLIRNYTHKYNSINAESYDGINKVPLWLAAWATASAPTYLKGPSAEDIKKLGINIKPEIHLVDGALKASNPALIALEECARLNNKNLSTFIKEDLDTLVSIGTGQVPTKLTQSGASSKSASTFEILINSTHLLTRANDTHREVLQRLADRENTYFRFNVPHIGDIEIDSQDVRDFDLISKATQDYLFDEKFYEIKRLAHKLANNYIRSKYL | Function: Hydrolyzes the ester bond of the fatty acyl group attached at the sn-2 position of phospholipids such as phosphatidylcholine . Involved in gametogenesis; however, it is not clear whether it is involved in gametocytes development in host erythrocytes or in gametocyte activation in the mosquito midgut . Involved in gametocyte development in host erythrocytes; however, not involved in gametocytes activation including male gamete exflagellation . Involved in the rounding up of gametocytes following activation in the mosquito midgut; however, not required for gametocyte development in host erythrocytes . Required for exflagellation of activated male gametocytes . Involved in gametocytes egress from host erythrocytes by promoting the relocalization of perforin-like protein PLP2-containing vesicles to the periphery of gametocytes; PLP2 secretion is required for permeabilization of the erythrocyte membrane and thus, promotes gametocyte egress . Dispensable for asexual blood stage development .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Sequence Mass (Da): 78305
Sequence Length: 679
Subcellular Location: Cytoplasm
EC: 3.1.1.4
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Q9LJ64 | MTRRTMEKPFGCFLLLFCFTISIFFYSAAALTDEEASFLTRRQLLALSENGDLPDDIEYEVDLDLKFANNRLKRAYIALQAWKKAFYSDPFNTAANWVGPDVCSYKGVFCAPALDDPSVLVVAGIDLNHADIAGYLPPELGLLTDVALFHVNSNRFCGVIPKSLSKLTLMYEFDVSNNRFVGPFPTVALSWPSLKFLDIRYNDFEGKLPPEIFDKDLDAIFLNNNRFESTIPETIGKSTASVVTFAHNKFSGCIPKTIGQMKNLNEIVFIGNNLSGCLPNEIGSLNNVTVFDASSNGFVGSLPSTLSGLANVEQMDFSYNKFTGFVTDNICKLPKLSNFTFSYNFFNGEAQSCVPGSSQEKQFDDTSNCLQNRPNQKSAKECLPVVSRPVDCSKDKCAGGGGGGSNPSPKPTPTPKAPEPKKEINPPNLEEPSKPKPEESPKPQQPSPKPETPSHEPSNPKEPKPESPKQESPKTEQPKPKPESPKQESPKQEAPKPEQPKPKPESPKQESSKQEPPKPEESPKPEPPKPEESPKPQPPKQETPKPEESPKPQPPKQETPKPEESPKPQPPKQETPKPEESPKPQPPKQEQPPKTEAPKMGSPPLESPVPNDPYDASPIKKRRPQPPSPSTEETKTTSPQSPPVHSPPPPPPVHSPPPPVFSPPPPMHSPPPPVYSPPPPVHSPPPPPVHSPPPPVHSPPPPVHSPPPPVHSPPPPVHSPPPPVHSPPPPVQSPPPPPVFSPPPPAPIYSPPPPPVHSPPPPVHSPPPPPVHSPPPPVHSPPPPVHSPPPPVHSPPPPVHSPPPPSPIYSPPPPVFSPPPKPVTPLPPATSPMANAPTPSSSESGEISTPVQAPTPDSEDIEAPSDSNHSPVFKSSPAPSPDSEPEVEAPVPSSEPEVEAPKQSEATPSSSPPSSNPSPDVTAPPSEDNDDGDNFILPPNIGHQYASPPPPMFPGY | Function: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 102823
Sequence Length: 956
Subcellular Location: Secreted
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Q9XIB6 | MERPFGCFFILLLISYTVVATFDDEPSFPENADLTKDLEQKCFSINKVDPNLKFENDRLKRAYIALQAWKKAIYSDPFKTTANWVGSDVCSYNGVYCAPALDDDSLTVVAGVDLNHADIAGHLPPELGLMTDLALFHINSNRFCGIIPKSLSKLALMYEFDVSNNRFVGQFPEVSLSWPSLKFLDLRYNEFEGSLPSEIFDKDLDAIFLNNNRFESVIPGTIGKSKASVVTFANNKFSGCIPKSIGNMKNLNEIVFTGNNLTGCFPNEIGLLNNVTVFDASKNGFVGSLPSTLSGLASVEQLDLSHNKLTGFVVDKFCKLPNLDSFKFSYNFFNGEAESCVPGRNNGKQFDDTNNCLQNRPSQKPAKQCLPVVSRPVDCSKDKCSGGSNGGSSPSPNPPRTSEPKPSKPEPVMPKPSDSSKPETPKTPEQPSPKPQPPKHESPKPEEPENKHELPKQKESPKPQPSKPEDSPKPEQPKPEESPKPEQPQIPEPTKPVSPPNEAQGPTPDDPYDASPVKNRRSPPPPKVEDTRVPPPQPPMPSPSPPSPIYSPPPPVHSPPPPVYSSPPPPHVYSPPPPVASPPPPSPPPPVHSPPPPPVFSPPPPVFSPPPPSPVYSPPPPSHSPPPPVYSPPPPTFSPPPTHNTNQPPMGAPTPTQAPTPSSETTQVPTPSSESDQSQILSPVQAPTPVQSSTPSSEPTQVPTPSSSESYQAPNLSPVQAPTPVQAPTTSSETSQVPTPSSESNQSPSQAPTPILEPVHAPTPNSKPVQSPTPSSEPVSSPEQSEEVEAPEPTPVNPSSVPSSSPSTDTSIPPPENNDDDDDGDFVLPPHIGFQYASPPPPMFQGY | Function: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 90990
Sequence Length: 847
Subcellular Location: Secreted
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Q9XIL9 | MPHIYKQPLGIFQGFVPTLTDAEVSFIAQRQLLTLPENGELPDDIEYEVDLKVTFANHRLKRAYIALQAWKKAVYSDPFNTTGNWHGPHVCGYTGVFCAPALDDPDVAVVAGVDLNGADIAGHLPAELGLMTDVAMFHLNSNRFCGIIPKSFEKLSLMHEFDVSNNRFVGPFPSVVLSWPAVKFIDVRYNDFEGQVPPELFKKDLDAIFLNNNRFTSTIPDSLGESSASVVTFAHNKFSGCIPRSIGNMKNLNEIIFKDNSLGGCFPSEIGKLANVNVFDASMNSFTGVLPPSFVGLTSMEEFDISGNKLTGFIPENICKLPKLVNLTYAYNYFNGQGDSCVPGSQKQIALDDTRNCLPDRPKQRSAKECAVVISRPVDCSKDKCAGGSSQATPSKSPSPVPTRPVHKPQPPKESPQPNDPYNQSPVKFRRSPPPPQQPHHHVVHSPPPASSPPTSPPVHSTPSPVHKPQPPKESPQPNDPYDQSPVKFRRSPPPPPVHSPPPPSPIHSPPPPPVYSPPPPPPVYSPPPPPPVYSPPPPPPVHSPPPPVHSPPPPVHSPPPPVHSPPPPVHSPPPPVHSPPPPVYSPPPPPVHSPPPPVHSPPPPVHSPPPPVYSPPPPPPVHSPPPPVFSPPPPVHSPPPPVYSPPPPVYSPPPPPVKSPPPPPVYSPPLLPPKMSSPPTQTPVNSPPPRTPSQTVEAPPPSEEFIIPPFIGHQYASPPPPMFQGY | Function: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 78370
Sequence Length: 727
Subcellular Location: Secreted
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O81765 | MPFYKQPWVFSKVFVLAMAKPPSFGCCFFLLFFSFLSSSFVSFALTDTEAAFIVQRQLLTLPDNGELPDDIEYEVDLKATFANTRLKRAYIALQAWKKAIFSDPFNTTGNWHGPHVCGYTGVVCAPALDDSDVTVVAGVDLNGADIAGHLPAELGLMTDVAMFHLNSNRFCGIIPKSFEKLKLMHEFDVSNNRFVGPFPNVVLSWPDVKYFDLRFNDFEGQVPPELFKKELDAIFLNDNRFTSVIPESLGESPASVVTFANNKFTGCIPKSIGNMKNLNEIVFMDNDLGGCFPSEIGKLSNVTVFDASKNSFIGRLPTSFVGLTSVEEIDISGNKLTGLVPHNICQLPNLVNLTYSYNYFSGQGGSCVPGGSRKEIALDDTRNCLASRPEQRSAQECAVVINRPVDCSKDKCAGGSSTPSKPSPVHKPTPVPTTPVHKPTPVPTTPVQKPSPVPTTPVQKPSPVPTTPVHEPSPVLATPVDKPSPVPSRPVQKPQPPKESPQPDDPYDQSPVTKRRSPPPAPVNSPPPPVYSPPPPPPPVHSPPPPVHSPPPPPVYSPPPPPPPVHSPPPPVFSPPPPVYSPPPPVHSPPPPVHSPPPPAPVHSPPPPVHSPPPPPPVYSPPPPVFSPPPSQSPPVVYSPPPRPPKINSPPVQSPPPAPVEKKETPPAHAPAPSDDEFIIPPFIGHQYASPPPPMFAGY | Function: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 75248
Sequence Length: 699
Subcellular Location: Secreted
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C0HLD6 | FLSLIPKIAGGIASLVKDL | Function: The amidated Phylloseptin-1.2TR has weak antimicrobial activity against Gram-negative bacterium E.coli ATCC 25922 (MIC=100 uM), Gram-positive bacterium S.epidermidis ATCC 12228 (MIC=100 uM) and against fungus C.albicans ATCC 24433 (MIC=100 uM) . Has an anti-inflammatory effect, since it inhibits the production of the pro-inflammatory cytokines TNF-alpha and IL-1 beta, and induces the production of the anti-inflammatory cytokine IL-10 . Has an activity of stimulation of insulin release, which may protect the species from being eaten by predators by causing fatal hypoglycemia . Is cytotoxic to cancer line cells . Shows moderate hemolysis on mouse erythrocytes (LC(50)=75 uM) .
PTM: Phylloseptin-1.2TR is amidated, whereas Phylloseptin-1.3TR is the name given to the non-amidated form.
Sequence Mass (Da): 1955
Sequence Length: 19
Subcellular Location: Secreted
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O15162 | MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAGFPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVLTGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLRCSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCCGDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLIDFMFFESTGSQEQKSGVW | Cofactor: Magnesium. Can also use zinc with lower efficiency.
Function: Catalyzes calcium-induced ATP-independent rapid bidirectional and non-specific movement of phospholipids (lipid scrambling or lipid flip-flop) between the inner and outer leaflet of the plasma membrane resulting in collapse of the phospholipid asymmetry which leads to phosphatidylserine externalization on the cell surface . Mediates calcium-dependent phosphatidylserine externalization and apoptosis in neurons via its association with TRPC5 (By similarity). Also exhibits magnesium-dependent nuclease activity against double-stranded DNA and RNA but not single-stranded DNA and can enhance DNA decatenation mediated by TOP2A . Negatively regulates FcR-mediated phagocytosis in differentiated macrophages . May contribute to cytokine-regulated cell proliferation and differentiation (By similarity). May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes . Inhibits the functions of viral transactivators, including human T-cell leukemia virus (HTLV)-1 protein Tax, human immunodeficiency virus (HIV)-1 Tat, human hepatitis B virus (HBV) HBx, Epstein-Barr virus (EBV) BZLF1 and human cytomegalovirus IE1 and IE2 proteins through direct interactions . Mediates also the inhibition of influenza virus infection by preventing nuclear import of the viral nucleoprotein/NP .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out)
PTM: Phosphorylation at Thr-161 by PKC/PKCD increases its phospholipid scramblase activity during both cell stimulation and apoptosis . Phosphorylated by OXSR1 in the presence of RELT.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 35049
Sequence Length: 318
Domain: The N-terminal proline-rich domain (PRD) is required for phospholipid scramblase activity.
Subcellular Location: Cell membrane
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Q9JJ00 | MENHSKQTEAPHPGTYMPAGYPPPYPPAAFQGPSDHAAYPIPQAGYQGPPGPYPGPQPGYPVPPGGYAGGGPSGFPVQNQPAYNHPGGPGGTPWMPAPPPPLNCPPGLEYLAQIDQLLVHQQIELLEVLTGFETNNKYEIKNSLGQRVYFAVEDTDCCTRNCCGASRPFTLRILDNLGREVMTLERPLRCSSCCFPCCLQEIEIQAPPGVPVGYVTQTWHPCLPKFTLQNEKKQDVLKVVGPCVVCSCCSDIDFELKSLDEESVVGKISKQWSGFVREAFTDADNFGIQFPLDLDVKMKAVMLGACFLIDFMFFERTGNEEQRSGAWQ | Cofactor: Magnesium. Can also use zinc with lower efficiency.
Function: Catalyzes calcium-induced ATP-independent rapid bidirectional and non-specific distribution of phospholipids (lipid scrambling or lipid flip-flop) between the inner and outer leaflet of the plasma membrane resulting in collapse of the phospholipid asymmetry which leads to phosphatidylserine externalization on the cell surface . Mediates calcium-dependent phosphatidylserine externalization and apoptosis in neurons via its association with TRPC5 . Also exhibits magnesium-dependent nuclease activity against double-stranded DNA and RNA but not single-stranded DNA and can enhance DNA decatenation mediated by TOP2A (By similarity). Negatively regulates FcR-mediated phagocytosis in differentiated macrophages . May contribute to cytokine-regulated cell proliferation and differentiation .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out)
PTM: Phosphorylation at Thr-170 by PKC/PKCD increases its phospholipid scramblase activity during both cell stimulation and apoptosis (By similarity). Phosphorylated by OXSR1 in the presence of RELT (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 35914
Sequence Length: 328
Domain: The N-terminal proline-rich domain (PRD) is required for phospholipid scramblase activity.
Subcellular Location: Cell membrane
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B3PEU9 | MSATIRIAVDAMSGDLGPRVAIDAAQNFLQCHSDLEITLVGDESQLQQAHSLTGKNSRLHYLHAPDVVTMADDPLSALRHKKNSSMWKSLELLCLDRADACVSAGNTGALLAMARHQIKTLPGIERPAICKSMPVRSGVTYLLDLGANIDVGPELLHQFALMGAALARAAGVANPRVSLLNIGTEEYKGTQVLQQAQVLLQSDNSFTYSGFVEANRIFNGDVDVIVCDGFHGNVALKASEGVAQFIADKIAVEFKRHVFSRVMAFLAWPTLRRLKLQLNPARYNGASFLGLQKPVIKSHGNANEQAFIHALEVALQQVQERVPQRILEQISLH | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 36260
Sequence Length: 333
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q9PLB1 | MKVRLGVDMMGGDHDPLVVWEALEEVLLSLDGQPVEFSVFATPDVHQQLTHSPLSRSVQMIASESFVSMEDSVLAAVRKKRSSMALGLDSLQRGELDGFISAGNTAALVTLARAKIPMIPAVPRPALLVSVPTLSGFAVILDVGATVAVNPEEMVGFARMGLAYRQSLSSSDQSFTLGLLNIGSEERKGTDSHKHTFRMLRDVFGSAFLGNVESGDVFSGKVDIVVTDGFTGNVFLKTAEGLFDFLRHILGDHLEKTIKTRFDYTIYPGSIISGLSRLVIKCHGKSRETALFGGISGAVDLARSNVCGRIAAKFGLEEA | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 34245
Sequence Length: 319
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q9Z6U6 | MEVQIGIDLMGGDHSPLVVWQVLVDVLKSQSSTIPFAFTLFASEEIRKQIQEEFISDLPQEKFPKIISAENFVAMEDSPLAAIRKKSSSMALGLDYLQEDKLDAFISTGNTGALVTLARAKIPLFPAVSRPALLVCVPTMRGHAVILDVGANISVKPEEMVGFARMGLAYRQCLGDSKIPTIGLLNIGSEERKGTEAHRQTFRMLRETFGEAFLGNIESGAVFDGAADIVVTDGFTGNIFLKTAEGVFEFLQRILGDKLEADIQRRLDYTFYPGSVVCGLSKLVIKCHGKACGSSLFHGILGSINLAQARLCKRILSNLI | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 34857
Sequence Length: 320
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q8KAP3 | MGGDNAPACVVEGVIDALRESGNRFEILLIGQEEKVAPLLQQYDTGALKLRFVHAPEVITMEDVPATAVKAKQESSLVRGLKLCKAKDADAFVSAGNTGAMMAASLFVLGRIPGVLRPTIYAYFPRLGEGLTNLVDVGANVDCKPENLVQFAEMLTIYQRYAAKIEQPVVGLLNIGEEEGKGPDYLKQAWKMLQKAHEEQKINFIGNIEGHDILAGKATIVVCDGLVGNTILKFGESIPHFLGAIFKPALEKLVKEGKLDQNSAVLAGQTFKGIFEPFDVEKFGGVPFLGVDGISIVGHGRSSARAIKNMIYMAEHMIEQRVNERIAKMLA | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 35880
Sequence Length: 331
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q1QX56 | MTVRIAIDAMGGDLGPRATVLGSLQALSMHPDLEIQMYGPREALEDELETLPKRLSGYRSRLVLHDAPRVISQAMRVASALREAEGSSMLGALSGVREGRAQACVSAGNTGALMALGRRELGTISGISRPAISTAVPTQDGGRCYLLDLGANVDVQTRHLVDFARMGAVMARVVDEVAVPRVALLNIGVEANKGVPSVRDADRCLREDASRRIGDGTFDYIGYLEGDGIFSGAADVVVCDGFVGNAVLKASEGLATMLLTRLQETFEAHLTTRMVRAMARPALLRLKRRLDPVRYNGASLLGLAGIAVKSHGGADAKGFAYAVSRAVREIDMDLPAHLARALSDEGAAKPSTHSAAAVGGRVDSGLASDARPDDSHPQR | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 39986
Sequence Length: 379
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q7NSK6 | MTITVAVDAMGGDVGLKVTVPASIQFLQDHPDTHLILVGDQPALEAELALHDGAVRERILIQHATQVVGMDEAPQLALKNKKDSSMRVAINLVKEGKAQAAVSAGNTGALMATARFVLKTIPGIDRPAIAKLLPNVKGTSCVLDLGANVDCTPEQLLQFGIMGSELMACLQGKANPSVGLLNIGSEDIKGNDNIKKTAELLRQSELHFYGNVEGDDICKGTTDVVVCDGFTGNVALKTAEGLAHMFAVFLREEFGRSWWTRLCALAALPVLALFKKRIDPRRYNGASLLGLRGIVVKSHGSADVTGFRYALAQACEEAGSDVIAHIADRVAKQLDNLKQSEAEAN | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 36730
Sequence Length: 345
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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B5E8U7 | MRVAVDVMGGDNAPHVEVEGAVAAAREFGVPVTLVGDAEKVRAELARYDCKGLDIEVWHASEVVGMHDSASDAVRKKKDSSIRIAFELVKGGEAVAVVSAGNSGATMAAGMFVLKRMKGIDRAAIAQLFPTVSGKTLVLDVGGNVDCKPIHLVQFAVMGEVYARFVMGVDNPKVGLLSNGEEASKGNELTRETSALLREKPINYIGYVEGRDIFNGSVDVVVCDGFVGNVALKLSEGLAEAVGKMLKAEIKSSFLSQIGYLLSRKAFNNFKKTVDYAEYGGAPLLGINGVGMICHGGSNPKAIKNAIRFAHEYALKGVNGRMAEKLNESFPGDAREREGAPAPDAGTERVAS | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 37233
Sequence Length: 352
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q31HR8 | MSIKIAIDAMGGDHGIKVTVPASLEALSKFSDISIVLVGNQPLIEAELANHKYDKNRLSVEHAEQIVEMDDLPSKALRNKRKSSMRIALNLVKDDVAQACVSAGNTGALMAVSKFVLKTLPGIDRPAICTQMPTMKGHVHVLDLGANVGADGQSLAQFAVMGSVLAQAVDSNSRPRVGLLNIGEEEIKGHQRIKDANEILKSSDAINYVGYVEGDEIFKGDVDVVSCDGFDGNVALKASEGVAKMISFYLRAAFNKNLLTKLAGLVVYPVLKAFKAKVDPRRYNGASFLGLRKIVIKSHGGADVFSFYHAIAEARLEVNKNVPELIATEVKAILETH | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 36262
Sequence Length: 337
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q5QZ38 | MPELNIAIDAMGGDNGPSIVIEALEKAVHRYPDVKFTVVGHEQQLTPLLDKFNLSSHPSINLVHAEQVIEMDDKPGQSLRSKPESSMRVALQSLTDGNCQAMVSGGNTGALMTNAYFTLKTLPGVLRPALMTALPNQTGGKSYLLDLGANASCDSETLFQFGVMGAVAAEYLSGVPAPKISLLNMGEEDIKGNDVVRNAAARLAQCEQLNYIGFIEGNHLFSGRADVVVCDGFVGNVALKSCEGLATFIIDQMRDTLNSHWLYRFFFRFLQKRTHKSWDRLKPDHYNGASLIGLRHVVIKSHGSASAGAFYSAIQQAVAEAHEQLPERIKHRVEAVLSEQL | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 37164
Sequence Length: 341
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q1IJ05 | MPITIAVDAMGSDKAPTPEIEGALQAIRHFDVRVILVGKQDVLREHLGAHAHPGRLPIEIVHASEVISMHDKAALAVRSKRDSSMRVGLRLVREGKADAFVTAGNTGAAMATAKMVLGALPGVDRPALAAVFPTEKRTAAILLDVGANVDCKPQNLQQFAIMGEVYFRTVFAGKSPHARSPRVGILSIGEEETKGNELTREAYKLVKTLPLNFVGNVEGRDLFNGNVDVLVCDGFVGNVALKISEGLVKTVREMLKESLQQTIARQVGFLLSRQAFVDFKKRLDYSEYGGAPLLGLKGAAFVGHGSSNANAIKNAIRVAAEYVEHRVNEAIAREIAAASEKLGNHHSSAKKEEGEEARA | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 38552
Sequence Length: 359
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q8DWL9 | MKKIAVDAMGGDNAPQAIVEGVNQALADFSDIEIQLYGDEAKIKTYLKANDRVSIIHTDEKINSDDEPVKAIRKKKQASMVLGAQAVKDGKADAVLSAGNTGALLAAGLLVVGRIKNIDRPGLMSSLPTIDGKGFNMLDLGANAENTAHHLHQYAILGSFYAKNVRGVAHPRIGLLNNGTETTKGDPLRKETFALLAADETLNFIGNVEARDLMNSVADVVVTDGFTGNAVLKSIEGTALGIMEQLKTSIKQAGLRAKLGALLLKNSLYDLKDSLDYSGAGGAVLFGLKAPVVKCHGSSDAKSVYYTIKQIRIMLETDVVGQLVEEFSNRGD | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 35294
Sequence Length: 332
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q39DI4 | MQILLAALVAYLIGSVSFAVVVSGAMGLADPRSYGSKNPGATNVLRSGNKKAAILTLVGDAFKGWIAVWLARHLGLPDVAVAWVAIAVFLGHLYPVFFRFQGGKGVATAAGVLLAVHPVLGLATALTWLIVAFFFRYSSLAALVAAVFAPVFDVFLFGTGHNPVAWAVLAMSVLLVWRHRGNISKLLAGQESRIGDKKKAAADGGAQDGGKA | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22111
Sequence Length: 212
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
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Q3JVC1 | MQILLATVAAYLIGSVSFAVVVSAAMGLADPRSYGSKNPGATNVLRSGNKKAAILTLVGDAFKGWLAVWLVKRFGIGGEIGVALAAIAVFLGHLYPVFFRFQGGKGVATAAGVLLAVHPVLGLATALTWLIVAFFFRYSSLAALVAAVFAPIFDVFLFGTHDNPVAWAVLAMSVLLIWRHRSNISKLLAGEESRIGQKKKTGA | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21385
Sequence Length: 203
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
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Q2T0L4 | MQILLATVAAYLIGSVSFAVVVSAAMGLADPRSYGSKNPGATNVLRGGNKKAAILTLVGDAFKGWLAVWLVKHFGIGGEIGVALAAIAVFLGHLYPVFFRFQGGKGVATAAGVLLAVHPALGLATALTWLIIAFFFRYSSLAALVAAVFAPVFDVFLFGTRNNPVAWAVIAMSALLIWRHRSNISKLLAGEESRIGQKKTDA | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21228
Sequence Length: 202
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
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Q4FLQ2 | MEYLIVALSSYLLGSIPFGFILTKIFLKKDIRDIGSGNIGATNALRTGNKTLGYATLLLDITKAVLPVLYVKFNYPDYIFIASLSAFLGHVFPIWLKFKGGKGVATYVGILFSINIFLGLVFIISWAVTFLISKYSSLSSLVGSLMVPMYLIVFENYNSIFFIIMFVLIFYTHRENVKRLKNKEETKTKIY | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21605
Sequence Length: 191
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
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A3PEG1 | MNILIIFASYLLGSLPTGFLIGKYLKNIDLRTIGSGSTGATNVLRNVGKWPALFVFIIDLGKGLIAVKIAQYYTDQGLIEVIAGISAISGHIWPIWLRGKGGKAVATGLGMFLALSWKVGLASLGFFLIVLTKTKYVSLSSISAAILLPIFMFFYLGKFMHSYFFISLIVALLVIWKHRTNITRLLKGEESKINQTQ | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21647
Sequence Length: 197
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
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A2BY34 | MTIIIIVLSYFLGSIPTGFLFGKFLKNIDLRLIGSGSTGATNVLRNVGKWPAFFVFIIDVGKGLLAVKLSQSYTNQHLFEVLAGISAVSGHIWPIWLKGKGGKAVATGLGMFIALSWKVGFASLGIFLIILSKSKIVSLSSILAAFFLPLFMFLDIGVTNHPYFLISLVVSILVILKHRTNIRRLIKGEESKINSLNK | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21624
Sequence Length: 198
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
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Q7V5Y3 | MFNSLFGNLLSLVMGYLLGSLPSGYLAAHWLAGIDLREKGSGSTGATNVLRQVGKGPALAVFLIDVGKGTTAVLVARALELDDGWQVAAGLAALAGHIWPVWLGWKGGKAVATGLGMLLGISWPVGLACFGIFLTVLSFSRIVSLSSIIAALSLPLLMILRFQGNSPPAYLAVAFAAMAMVVWRHRSNLQRLLAGTEPRLGQSS | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21370
Sequence Length: 204
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
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Q7V0D9 | MHILIISISYFLGSLPTGFLFGKFLKNIDLRLTGSGSTGATNVLRNVGKWPAFFVFIIDVGKGLIAVKIAQHYTNQNLFEVLAGIAAISGHIWPIWLKGKGGKAVATGLGMFIALSWKIGFASLGIFLIILAKSKIVSLSSISAAIFLPFLMFLDIGSTNHPYFFISLVVSILVIWKHRTNIRRLLKGEELKINDINK | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21732
Sequence Length: 198
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
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Q46JD9 | MNLLILFFGYLFGSFPSGYLAGRIAKGIDIRSLGSGSTGATNVLRHIGKRAAITVFLLDVFKGVLSILLAKYLLLNDSWQVAVGLSTLIGHIWPVWLNWKGGKAVATGLGIFLGLSWQVGLATLGVFIIMITLFRIVSLASVSASLALPLIMFLSFSGSNLSLPFLIVSLLAMILVIWRHRENIVRLIRGKEPRIGQP | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21504
Sequence Length: 198
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
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Q91VC4 | MGLSMDRSPYARTGDQQRGCWYYLRYFFLFVSLIQFLIILGLVLFMIYGNVHATTESSLRATEIRADSLYSQVVGLSASQANLSKQLNISLLVKETVMQQLLTTRREMERINASFRQCQGDLITYINYNRFIAAIILSEKQCQEQLKEVNKTCEALLFKLGEKVKTLEMEVAKEKAVCSKDKESLLAGKRQTEEQLEACGKARERQQQEQQVTEENLRKVQSLCIPLDQEKFQADVLSAWRDSLIYRTLETLPYHYQLMPEYASLRRTCESLPGIMTTKIEELARGLRAGIERVTRENAELRRQKLELERAAQAAQEARARAGTEAQARETQLRAECARQTQLALEEKAALRAQRDNLERELEARKRELEQLRTEVDVRISALDTCVKAKSLPAVPPRVSGPPPNPPPIDPASLEEFKKRILESQRLPVVNPAAQPSG | Function: Endothelial cell-specific membrane protein involved in the formation of the diaphragms that bridge endothelial fenestrae. It is also required for the formation of stomata of caveolae and transendothelial channels. Functions in microvascular permeability, endothelial fenestrae contributing to the passage of water and solutes and regulating transcellular versus paracellular flow in different organs. Plays a specific role in embryonic development.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 49933
Sequence Length: 438
Subcellular Location: Cell membrane
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O04499 | MATSSAWKLDDHPKLPKGKTIAVIVLDGWGESAPDQYNCIHNAPTPAMDSLKHGAPDTWTLIKAHGTAVGLPSEDDMGNSEVGHNALGAGRIFAQGAKLCDQALASGKIFEGEGFKYVSESFETNTLHLVGLLSDGGVHSRLDQLQLLIKGSAERGAKRIRVHILTDGRDVLDGSSVGFVETLEADLVALRENGVDAQIASGGGRMYVTLDRYENDWEVVKRGWDAQVLGEAPHKFKNAVEAVKTLRKEPGANDQYLPPFVIVDESGKAVGPIVDGDAVVTFNFRADRMVMHAKALEYEDFDKFDRVRYPKIRYAGMLQYDGELKLPSRYLVSPPEIDRTSGEYLTHNGVSTFACSETVKFGHVTFFWNGNRSGYFNEKLEEYVEIPSDSGISFNVQPKMKALEIGEKARDAILSGKFDQVRVNIPNGDMVGHTGDIEATVVACEAADLAVKMIFDAIEQVKGIYVVTADHGNAEDMVKRDKSGKPALDKEGKLQILTSHTLKPVPIAIGGPGLAQGVRFRKDLETPGLANVAATVMNLHGFVAPSDYEPTLIEVVE | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the interconversion of 2-phosphoglycerate (2-PGA) and 3-phosphoglycerate (3-PGA) . Required for guard cell function (e.g. blue light-, abscisic acid- (ABA), and low CO(2)-regulated stomatal movements) and fertility (e.g. pollen grains production) .
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 60580
Sequence Length: 557
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
Subcellular Location: Cytoplasm
EC: 5.4.2.12
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P00950 | MPKLVLVRHGQSEWNEKNLFTGWVDVKLSAKGQQEAARAGELLKEKKVYPDVLYTSKLSRAIQTANIALEKADRLWIPVNRSWRLNERHYGDLQGKDKAETLKKFGEEKFNTYRRSFDVPPPPIDASSPFSQKGDERYKYVDPNVLPETESLALVIDRLLPYWQDVIAKDLLSGKTVMIAAHGNSLRGLVKHLEGISDADIAKLNIPTGIPLVFELDENLKPSKPSYYLDPEAAAAGAAAVANQGKK | Function: Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also Catalyzes the reaction of EC 5.4.2.4 (synthase), but with a reduced activity.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27609
Sequence Length: 247
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
Subcellular Location: Cytoplasm
EC: 5.4.2.11
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Q9M9K1 | MGSSGDVNWKLADHPKLPKGKTIGLIVLDGWGESDPDQYNCIHKAPTPAMDSLKDGKPDTWRLIKAHGTAVGLPSEDDMGNSEVGHNALGAGRIYAQGAKLVDLALASGKIYEDEGFKYISQSFEKGTVHLIGLLSDGGVHSRLDQVQLLLKGFAERGAKRIRVHILTDGRDVLDGSSVGFVETLEADLAALRAKGVDAQVASGGGRMYVTMDRYENDWSVVKRGWDAQVLGEAPHKFKSALEAVKTLRAEPGANDQYLPSFVIVDDNGKAVGPIVDGDAVVTFNFRADRMVMHAKALEYKDFDKFDRVRVPDIRYAGMLQYDGELKLPSRYLVSPPLIDRTSGEYLAHNGVRTFACSETVKFGHVTFFWNGNRSGYFNEKLEEYVEIPSDSGISFNVQPKMKALEIAEKARDAILSGKFDQVRVNLPNGDMVGHTGDIEATVVACEAADRAVRTILDAIEQVGGIYVVTADHGNAEDMVKRDKSGKPALDKEGNLQILTSHTLKPVPIAIGGPGLSAGVRFRQDIETPGLANVAATVMNLHGFVAPSDYETSLIEVVEK | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the interconversion of 2-phosphoglycerate (2-PGA) and 3-phosphoglycerate (3-PGA) . Required for guard cell function (e.g. blue light-, abscisic acid- (ABA), and low CO(2)-regulated stomatal movements) and fertility (e.g. pollen grains production) .
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 60764
Sequence Length: 560
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
Subcellular Location: Cytoplasm
EC: 5.4.2.12
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Q12008 | MTASTPSNVMTLFLLRHGQSELNHENIFCGWIDAKLTEKGKEQARHSAELIEQYCKANNLRLPQIGYTSRLIRTQQTIETMCEEFKLKPQLQVVYDFNKIKLGDEFGSDDKDNMKIPILQTWRLNERHYGSWQGQRKPNVLKEYGKDKYMFIRRDYEGKPPPVDLDREMIQQENEKGSSTGYEFKEPNRQIKYELECSNHDIVLPDSESLREVVYRLNPFLQNVILKLANQYDESSCLIVGHGSSVRSLLKILEGISDDDIKNVDIPNGIPLVVELDKNNGLKFIRKFYLDPESAKINAEKVRNEGFIKNP | Function: Could be non-functional.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 36073
Sequence Length: 311
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
Subcellular Location: Cytoplasm
EC: 5.4.2.11
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P07738 | MSKYKLIMLRHGEGAWNKENRFCSWVDQKLNSEGMEEARNCGKQLKALNFEFDLVFTSVLNRSIHTAWLILEELGQEWVPVESSWRLNERHYGALIGLNREQMALNHGEEQVRLWRRSYNVTPPPIEESHPYYQEIYNDRRYKVCDVPLDQLPRSESLKDVLERLLPYWNERIAPEVLRGKTILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHQFLGDQEAIQAAIKKVEDQGKVKQAKK | Function: Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.11) activity.
PTM: Glycation of Lys-159 in diabetic patients inactivates the enzyme.
Catalytic Activity: (2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-bisphosphoglycerate + H(+)
Sequence Mass (Da): 30005
Sequence Length: 259
EC: 5.4.2.4
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P30792 | MGSSGFSWTLPDHPKLPKGKSVAVVVLDGWGEANPDQYNCIHVAQTPVMDSLKNGAPEKWRLVKAHGTAVGLPSDDDMGNSEVGHNALGAGRIFAQGAKLVDQALASGKIYDGDGFNYIKESFESGTLHLIGLLSDGGVHSRLDQLQLLLKGVSERGAKKIRVHILTDGRDVLDGSSIGFVETLENDLLELRAKGVDAQIASGGGRMYVTMDRYENDWDVVKRGWDAQVLGEAPYKFKSALEAVKTLRAQPKANDQYLPPFVIVDDSGNAVGPVLDGDAVVTINFRADRMVMLAKALEYADFDNFDRVRVPKIRYAGMLQYDGELKLPSRYLVSPPEIDRTSGEYLVKNGIRTFACSETVKFGHVTFFWNGNRSGYFDATKEEYVEVPSDSGITFNVAPNMKALEIAEKARDALLSGKFDQVRVNLPNGDMVGHTGDIEATVVACKAADEAVKIILDAVEQVGGIYLVTADHGNAEDMVKRNKSGKPLLDKNDRIQILTSHTLQPVPVAIGGPGLHPGVKFRNDIQTPGLANVAATVMNLHGFEAPADYEQTLIEVADN | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
PTM: The N-terminus is blocked.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 60620
Sequence Length: 559
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
Subcellular Location: Cytoplasm
EC: 5.4.2.12
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O24246 | LPTEDDMGNSEVGHNALGAGRIFAQGAKLVDSALETGKLYEGEGFKYIKESFPTNTLHLIGLLSDGGVHSRLDQLLLLVKGASERGAKRIRVHILTDGRDVLDGSSVGFAETLENYLAQLREKGVDAQIASGGGRMYVTMDRYENDWGVVKRGWDAQVLGEAPHKFKNAVEAIKTLRQEPNTSDQYLPPFVIVDENGKPVGPIVDGDAVVTFNFRADRMVMIAKALEYADFDKFDRVRFPKIRYAGMLQYDGELKLPSKYLVEPPEIDRTSGEYLTYNGVRTFACSETVKFGHVTFFWNGNRSGYFNPQMEEYVEIPSDSGITFNVQPKMKAVEIAEKGRGAILSKKFEQVRVNLPNSDMVGHTSSIEATVVACKAADEAVKIIIDAIEQVGGIYVVTADHGNAEDMVKRNKKGQPLLDKNGNIQILTSHTLQPVPIAIGGPGLAPGVQFRKDVPNGGLANVAATVMNLHGFEAPADYETTLIEVVDN | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 53395
Sequence Length: 488
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
Subcellular Location: Cytoplasm
EC: 5.4.2.12
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P35494 | MGSSGDAWKLKDHPKLPKGKTVAVIVLDGWGEAKPNEFNAIHVAETPVMYSLKNGAPEKWRLIKAHGNAVGLPTEDDMGNSEVGHNALGAGRIFAQGAKLVDLALASGKIYEGEGFKYVKECFEKGTLHLIGLLSDGGVHSRLDQVQLLLKGAAKHGAKRIRVHALTDGRDVLDGSSVGFMETLENSLAQLREKGIDAQVASGGGRMYVTMDRYENDWDVVKRGWDAQVLGEAPHKFKDPVEAVKKLRQEPNANDQYLAPFVIVDDNGKPVAAILDGDAVVTFNFRADRMVMLAKALEYENFDKFDRVRVPKIRYAGMLQYHGELQLPSHYLVSPPEIARHSGEYLVRNGVRTFACSETVKFGHVTFFWNGNRSGYFNEKLEEYVEIPSDSGITFNVKPKMKALEIAERTRDAILSGKFDQVRVNLPNGDMVGHTGDIKATIEACKSADEAVKMILEAIEQVGGIYLVTADHGNAEDMVKRNKKGEPALDKNGNIQILTSHTCEPVPIAIGGPGLAPGVRFRQDLPTGGLANVAATFMNLHGSEAPSDYEPSLIEVVDN | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 61067
Sequence Length: 559
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
Subcellular Location: Cytoplasm
EC: 5.4.2.12
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F1NQJ3 | MEEAAPCSEPAKTIKRIDRESVHRICSGQVVLSLGTAVKELVENSLDAGATNIDVRLKDHGAELIEVSDNGGGVEEENFEGLTLKHYTSKIQDFSDLIHVETFGFRGEALSSLCALSDVTISTCHKSAKVGTRLVFDHNGKITQKAPYPRQQGTTVSIQQLFHTLPVRHKEFQRNIKKEYAKMVQILQAYCIISKGVRINCTNQVGQGKKSPVVSTTGGPNLKENIGAVFGKKQLQSLIPFVQLPPNEAVCEEYGLKSTDLPEKLYSITGFISRCDHGVGRSTTDRQFFFINQRPCDPAKVVKLVNEVYHLYNKHQYPFIVLNICVDSECVDINVTPDKRQILLQEEKLLLAILKTSLIEMFGSDVNKLNVNQNLLDIVGNVKAPPGDAEKPWVEMSHHSETENPSSEGKRVMTLSRLRESFSLHQTESYFQSPKKVKQRHSSSKQLSLDTILSTVRTQKAVLSEDSESCHEMKSKMPVPRKYLRKVDDIDSGFCSTSESDAGYNTPEAGSCVISESVNNPIEEEFCSSEEQHQNEYLKTVGHSEKSLECDIQVLGTEHKLNRVNDCNNQTNLPQEATNSLPRVRRFKNEADDFKAGIHPKVENTRNYMPCVDVLVEVKKKTVPLEFSMKALAERVRKIVQQQQKCTETQNYRRFRAKISPGENKVAEDELRKEISKEMFAKMEIIGQFNLGFIIAKLNSDLFIIDQHATDEKYNFEMLQQHTVLQGQKLIAPQNLNLTAVNETVLIENLEIFRKNGFDFVINENAPVTQRVKLISLPTSKNWTFGPQDIDELIFMLSDCPGVMCRPSRVRQMFASRACRKSVMIGTALNVQEMKKLVTHMGEIEHPWNCPHGRPTMRHIASLDLIASE | Function: Component of the post-replicative DNA mismatch repair system (MMR). Involved in B cell growth by positively regulating B cell proliferation and controlling replication efficiency. Controls cell cycle to prevent re-replication and defects in DNA damage-induced G2 checkpoint. Doesn't seem to counteract or control the immunoglobulin gene conversion (Ig GC) and to contribute to guanine/uracil mismatch repair. Possesses an ATPase activity, but in the absence of gross structural changes, ATP hydrolysis may not be necessary for proficient mismatch repair (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 97996
Sequence Length: 869
Subcellular Location: Nucleus
EC: 3.1.-.-
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P54278 | MERAESSSTEPAKAIKPIDRKSVHQICSGQVVLSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSDNGCGVEEENFEGLTLKHHTSKIQEFADLTQVETFGFRGEALSSLCALSDVTISTCHASAKVGTRLMFDHNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHKEFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNQLGQGKRQPVVCTGGSPSIKENIGSVFGQKQLQSLIPFVQLPPSDSVCEEYGLSCSDALHNLFYISGFISQCTHGVGRSSTDRQFFFINRRPCDPAKVCRLVNEVYHMYNRHQYPFVVLNISVDSECVDINVTPDKRQILLQEEKLLLAVLKTSLIGMFDSDVNKLNVSQQPLLDVEGNLIKMHAADLEKPMVEKQDQSPSLRTGEEKKDVSISRLREAFSLRHTTENKPHSPKTPEPRRSPLGQKRGMLSSSTSGAISDKGVLRPQKEAVSSSHGPSDPTDRAEVEKDSGHGSTSVDSEGFSIPDTGSHCSSEYAASSPGDRGSQEHVDSQEKAPKTDDSFSDVDCHSNQEDTGCKFRVLPQPTNLATPNTKRFKKEEILSSSDICQKLVNTQDMSASQVDVAVKINKKVVPLDFSMSSLAKRIKQLHHEAQQSEGEQNYRKFRAKICPGENQAAEDELRKEISKTMFAEMEIIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTVLQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFVIDENAPVTERAKLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCRPSRVKQMFASRACRKSVMIGTALNTSEMKKLITHMGEMDHPWNCPHGRPTMRHIANLGVISQN | Function: Component of the post-replicative DNA mismatch repair system (MMR) . Heterodimerizes with MLH1 to form MutL alpha. DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Possesses an ATPase activity, but in the absence of gross structural changes, ATP hydrolysis may not be necessary for proficient mismatch repair .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 95797
Sequence Length: 862
Subcellular Location: Nucleus
EC: 3.1.-.-
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Q8RWB7 | MAGFTMSLNLLLLVAMVATNILSLYHLSSTTNFFQSTVKSSQSSVPTVPDHLLRQLHTIRAAINHLTTHQPDKSTSTSTSRAAVSSSSSSTAPKELLIYSKLSPIASACHNYPDLLHEYMNYTPFSLCPSDTDLVEKLILRGCHPLPRRRCFSRTPRNPSDSKPESNVLWSYYSCKSFDCLITKFSDLGFDLSLEKSKSQFSAYKSELDLPISQLLQIAKSANSVLRLGIDVGGGTGSFAAAMKARNVTVLTTTMNFNAPYSEAVAMRGLVPLHVPLQQRLPVFDGVVDLVRCGRAVNRWIPVTVMEFFFFDLDRILRGGGYLWLDRFFSKKVDLENVYAPMIGKLGYKKVKWAVANKADSKHGEVFLTALLQKPVAR | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 41956
Sequence Length: 378
Subcellular Location: Golgi apparatus membrane
EC: 2.1.1.-
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P40999 | MLSTKRLRVLELYSGIGGMHYALNLANIPADIVCAIDINPQANEIYNLNHGKLAKHMDISTLTAKDFDAFDCKLWTMSPSCQPFTRIGNRKDILDPRSQAFLNILNVLPHVNNLPEYILIENVQGFEESKAAEECRKVLRNCGYNLIEGILSPNQFNIPNSRSRWYGLARLNFKGEWSIDDVFQFSEVAQKEGEVKRIRDYLEIERDWSSYMVLESVLNKWGHQFDIVKPDSSSCCCFTRGYTHLVQGAGSILQMSDHENTHEQFERNRMALQLRYFTAREVARLMGFPESLEWSKSNVTEKCMYRLLGNSINVKVVSYLISLLLEPLNF | Function: Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp). Can also methylate cytosine 38 in tRNA(Glu), albeit to a lower level, but not tRNA(Lys). Pmt1-dependent tRNA methylation is induced by nitrogen limitation and depends on the nutrient-sensing protein kinase sck2. Does not have DNA-methylation activity.
Catalytic Activity: cytidine(38) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(38) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 37976
Sequence Length: 330
Subcellular Location: Cytoplasm
EC: 2.1.1.204
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Q23552 | MSTDQQSSVEDQTVAMVNVRRANFKSFWDKYSDKPDTNSMMLNHSAEELESSDRADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAHLGNINYQVGDAVGLKMESNSVDLVFTNWLMMYLSDEETVEFIFNCMRWLRSHGIVHLRESCSEPSTGRSKAKSMHDTANANPTHYRFSSLYINLLRAIRYRDVDNKLWRFNVQWSCSVPTYIKRSNNWRQVHWLAEKVPAEDGAKGTSFNELVELIKNTWQNEQEAWDAKLDDEKYVWTDKVFSSALTSLPSNSTFFLYTPRTVSPYCHINAHTLAETFNANVWNTEIIPEYYRTSLTKSNNLKDQRVRFGWNQSLTDSVTYWQQKDALFDVFVATEFLSTVDDETIRQLPNVMSDGAKFITLEPVDEVNEAEMKQRIQELGYTLKSFTDVTDQCIEAQEQYFKDHEQLRDEKVIRKNWVLLELTH | Function: Catalyzes the first step in the synthesis of phosphocholine by converting phosphoethanolamine into phospho-monomethylethanolamine (N-methylethanolamine phosphate). Phosphocholine is a precursor for phosphatidylcholine, a major component in membranes and a precursor itself in the production of glycoconjugates secreted by parasitic nematodes to avoid host immune responses.
Catalytic Activity: phosphoethanolamine + S-adenosyl-L-methionine = H(+) + N-methylethanolamine phosphate + S-adenosyl-L-homocysteine
Sequence Mass (Da): 55148
Sequence Length: 475
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphocholine from phosphoethanolamine.
EC: 2.1.1.103
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O74189 | MAKKPVTPASKVAAKQAAVRSRHQEDVFTLDPLIDPIFQKGELRSYLVTEPSPSVLKKRSIHTKEYWMLSSLLLIAFYVRMYNLSNPNSVVFDEVHFGGFARKYILGTFFMDVHPPLAKMLFGAVGAIGGFKGDFEFKSIGDKFPDSTPYIFMRQFPALLGVGTVILCYLTLRQSGVRPIIAYITTFLLIIENSNVTISRYILLDSPLIFFIAAAIYAWKKFEIQIPFTFGWYRSLLATGIALGLALSSKWVGLFTVAWVGFLCIYQLWFLIGDLSVSTKKIWGHFFARGIILLGVPIALYLGFFAIHFQLLNKEGDGGAFMSSAFRAGLQGNKIPRDITEQVGLGSVVTIRHVDTQGGYLHSHEHFYQTGSKQQQITLYPHLDSNNKWLIEPYNGTIHNETFVPLINGMKIRLKHINTGRRLHSHDEKPPVSERDWQKECSCYGYDGFAGDANDDWVVEIVNYRSQKGEAQTFVKAINTIFRLRHAMTGHYLFSSEVKLPEWGFGQQEVTSASQGKRALTHWYIETNENSILPPSEAKIINYPKLSLWQKVVESHKRMWKINQGLTSHHHWQSSPSEWPLLLRGINYWNKEHKQVYLLGNAVTWWAATLSIITFGTYVLVTVFRWHLGTPLSTNKHVFNFNVQTFSYVLGWALHYLPFFIMGRQLFLHHYLPALYFGILALGHFFEIFTGYLTSRSKYFQQVAFVLVGLFSILSLVFYVNYSSLIYGTPWTKASCELTKPFSGWDYNCGTFFDTLGEYDIQEKSLASESEIPTETVVVEAKQTPKAEPKLAKQDDHIESPAAAEPVEEKEVKEEVEQLAPPLAVDFEEETPKVEDPQVADVDASSNDEKSVEEKQQQEQQQEQEQVEDESVHQVQQ | Function: Protein mannosyltransferase (PMT) involved in hyphal growth and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the protein-O-glycosylation activity, while PMT5 and PMT6 may specifically modulate a much narrower spectrum of target proteins. Accounts for the O-glycosylation of the cell wall proteins KRE9, PIR2, RHD3, and ALS1, as well as the SEC20 t-SNARE component. O-glycosylation of SEC20 is essential for its stability. Required for filamentation and early phases of biofilm formation.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 99935
Sequence Length: 877
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.109
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O13898 | MDKQSTFQDPKEKHRIQRDVKLSRPRKRFSFLDYVVVIFLTVVAFCVRAQRLMNPAKVVFEELRYYNYAVDYVNNKLLMDVYPPLGKLLFSLVAALTGNKYELNTLDEPGQQYPFTDVAYSMRLFTCLLGSLLVPLMYGTVYFPTKSKTAASLAALFVIFDNGLITMSRYIMIEIPALYFMSLTAFYWSVYEAQQKRPFSLRWHTSLLSTGVALGLALSTKLSAMFTFGWLLILAAFHLWNLLGDLSVPMYRIVKHLFSYIFYLIGVPITVYLAVFAVHSHIAYKASVADAFLPPEHRHALAGNRFDDQFADVAYGSLVTIRNAIPEHGYLHSSELLYPEGTEQQIISLVDEPNQNALWIIEHEHSQDNNRSNIELLKDGSVVRLRHVMTGRALHSHEHKPIVSNNDWQLEASAYGGFGFEGDANDLFRIQILEKKSKHATSNGTVETLNTKFRLIHVFANCELMSSHRRFPDWGDYQREVTCCRNCVERSTTWFIESNYHDGLPSDSRKITYRKPGFLESFVEHNKLMWLKDRKMGDGHVYESSALTWPLLLGPLRFFYEQHLQVFFMGNPFVWYSVISLVAFFVIVQIFCLARWNLGYNDFGPSAFHYNYNIGKFVVAWLLHWAPYILETDRVFLYHYLPALYFGIAALGVSWSFLGNAVFGNRTAYKALSVIIMALMFLVYRLYSPFTYMTTLTKSSCRALELKGSWNFHCNTYLDNLSDYKFSSDAGETYFEKAAPHPFVYSEDTAKKSEGDTPLNKNLNDYYPSWDQRVEAGYKLAAQQKAEQEAREAAEKAASEAAERSSSEAAASSSSESVAAASVEAERLAMEADEFNGASETVDGASVEAERSAMEAAALNNAAESTEVVGSSPESVASEQEENVAESAQARVE | Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. Required for normal cell growth and septum formation. Shown to actively O-mannosylate wsc1.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 101335
Sequence Length: 893
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.109
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Q42963 | MEVISTNTNGSTIFKNGAIPMNGHQNGTSEHLNGYQNGTSKHQNGHQNGTFEHRNGHQNGTSEQQNGTISHDNGNELLGSSDSIKPGWFSEFSALWPGEAFSLKVEKLLFQGKSDYQDVMLFESATYGKVLTLDGAIQHTENGGFPYTEMIVHLPLGSIPNPKKVLIIGGGIGFTLFEMLRYPSIEKIDIVEIDDVVVDVSRKFFPYLAANFNDPRVTLVLGDGAAFVKAAQAGYYDAIIVDSSDPIGPAKDLFERPFFEAVAKALRPGGVVCTQAESIWLHMHIIKQIIANCRQVFKGSVNYAWTTVPTYPTGVIGYMLCSTEGPEVDFKNPVNPIDKETTQVKSKLGPLKFYNSDIHKAAFILPSFARSMIES | Function: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) . Methyltransferase that mediates the conversion of putrescine to N-methylputrescine . Promotes leaves ripening .
Catalytic Activity: putrescine + S-adenosyl-L-methionine = H(+) + N-methylputrescine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 41142
Sequence Length: 375
Pathway: Alkaloid biosynthesis; nicotine biosynthesis.
EC: 2.1.1.53
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P33775 | MSEEKTYKRVEQDDPVPELDIKQGPVRPFIVTDPSAELASLRTMVTLKEKLLVACLAVFTAVIRLHGLAWPDSVVFDEVHFGGFASQYIRGTYFMDVHPPLAKMLYAGVASLGGFQGDFDFENIGDSFPSTTPYVLMRFFSASLGALTVILMYMTLRYSGVRMWVALMSAICFAVENSYVTISRYILLDAPLMFFIAAAVYSFKKYEMYPANSLNAYKSLLATGIALGMASSSKWVGLFTVTWVGLLCIWRLWFMIGDLTKSSKSIFKVAFAKLAFLLGVPFALYLVFFYIHFQSLTLDGDGASFFSPEFRSTLKNNKIPQNVVADVGIGSIISLRHLSTMGGYLHSHSHNYPAGSEQQQSTLYPHMDANNDWLLELYNAPGESLTTFQNLTDGTKVRLFHTVTRCRLHSHDHKPPVSESSDWQKEVSCYGYSGFDGDANDDWVVEIDKKNSAPGVAQERVIALDTKFRLRHAMTGCYLFSHEVKLPAWGFEQQEVTCASSGRHDLTLWYVENNSNPLLPEDTKRISYKPASFISKFIESHKKMWHINKNLVEPHVYESQPTSWPFLLRGISYWGENNRNVYLLGNAIVWWAVTAFIGIFGLIVITELFSWQLGKPILKDSKVVNFHVQVIHYLLGFAVHYAPSFLMQRQMFLHHYLPAYYFGILALGHALDIIVSYVFRSKRQMGYAVVITFLAASVYFFKSFSPIIYGTPWTQELCQKSQWLSGWDYNCNTYFSSLEEYKNQTLTKRESQPAATSTVEEITIEGDGPSYEDLMNEDGKKIFKDTEGNELDPEVVKKMLEEEGANILKVEKRAVLE | Function: Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT2 and more rarely with PMT3 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export. Required for incorporation of proteins in the cell wall.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 92675
Sequence Length: 817
Domain: The large luminal loop 5 is essential for mannosyltransferase activity but not for PMT1-PMT2 complex formation.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.109
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B9DFI7 | MALKSSSADGKTRSSVQIFIVFSLCCFFYILGAWQRSGFGKGDSIALEMTNSGADCNIVPSLNFETHHAGESSLVGASEAAKVKAFEPCDGRYTDYTPCQDQRRAMTFPRDSMIYRERHCAPENEKLHCLIPAPKGYVTPFSWPKSRDYVPYANAPYKALTVEKAIQNWIQYEGDVFRFPGGGTQFPQGADKYIDQLASVIPMENGTVRTALDTGCGVASWGAYLWSRNVRAMSFAPRDSHEAQVQFALERGVPAVIGVLGTIKLPYPTRAFDMAHCSRCLIPWGANDGMYLMEVDRVLRPGGYWILSGPPINWKVNYKAWQRPKEDLQEEQRKIEEAAKLLCWEKKYEHGEIAIWQKRVNDEACRSRQDDPRANFCKTDDTDDVWYKKMEACITPYPETSSSDEVAGGELQAFPDRLNAVPPRISSGSISGVTVDAYEDDNRQWKKHVKAYKRINSLLDTGRYRNIMDMNAGFGGFAAALESQKLWVMNVVPTIAEKNRLGVVYERGLIGIYHDWCEAFSTYPRTYDLIHANHLFSLYKNKCNADDILLEMDRILRPEGAVIIRDDVDTLIKVKRIIAGMRWDAKLVDHEDGPLVPEKVLIAVKQYWVTNSTSTH | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 69623
Sequence Length: 616
Subcellular Location: Golgi apparatus membrane
EC: 2.1.1.-
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Q22993 | MSSLSIPRQSLYYVNKVTEGRSVSNVQVVSPCQKQGQTYVTAFTPLTSNVQVHTSLEQLSTIRNADVLIFNNALSQIITNADLLTDFLKNATNATAIGGTVIIREDLKDCSDKRQVARLTDYFDVFRTTDSDGNNTGLDLYTVDQVEHSNYVEQNFLDFIFVFRKKVFAPTTDATITFRDFLDKTQYTNTGIDAYEWMFGVNFISPGGYDENLKIIKRFGDFKPGQTMLDIGVGIGGGARQVADEFGVHVHGIDLSSNMLAIALERLHEEKDSRVKYSITDALVYQFEDNSFDYVFSRDCIQHIPDTEKLFSRIYKALKPGGKVLITMYGKGYGEQSDKFKTYVAQRAYFLKNLKEIADIANKTGFVNVQTENMTPRFKEILLEERGHLEQNEAEFMSKFTQRERDSLISGWTDKLGYIEKDNHNWNFFLAQKPFPK | Function: Catalyzes the last two methylation reactions in the synthesis of phosphocholine, by converting phospho-monomethylethanolamine (N-methylethanolamine phosphate) into phospho-dimethylethanolamine (N,N-dimethylethanolamine phosphate) and the latter into phosphocholine. Phosphocholine is a precursor for phosphatidylcholine, a major component in membranes and a precursor itself in the production of glycoconjugates secreted by parasitic nematodes to avoid host immune responses.
Catalytic Activity: N-methylethanolamine phosphate + S-adenosyl-L-methionine = H(+) + N,N-dimethylethanolamine phosphate + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49769
Sequence Length: 437
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphocholine from phosphoethanolamine.
EC: 2.1.1.103
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Q9C100 | MSYEQLHAQSGQLRQRFPSKHSEIEDEVANEKEELKDATKSALGEVKTNKKYYILGYFLVPLLLTVIAGFVRVWKIADSNVVIWDEAHFGKFASYYLKHEFYFDVHPPLGKMLNAVAGKLVGYDGSFDFSSGATYPEDLNYKFMRLWNAAFGTLCIPLVYFTALNFNYSFLAATLCTLMVALDNHLATISRFILLDSMLLFFIISTFFCLSRYHVYHKAPFTFYWFKWLFLTGVCIGCVCSVKLVGLFITAVVGLYTVDELWCLLNDKRVTWKAYAGHWIARVCLLIFLPILIYAFTFWIQFAVLYRSGPGDAQMPSLFQARLEGSPLTKNPIDLMYGSKFTLKSRNPTGALLHSHVQTYPEGSEQQQVTGYHHKDGNNEWMFVPTHGVAYNYEENDPMNPILNGSVVRLIHPFTNRNLHTHKIPAPLNKRMYEVSGYGLGDVGDEKDYWIVNILYDTAHRDAYNVRSLSTVFQLYNPVVGCYLSSSSSSLPSWGFGQIEMYCDPDPDPSNTDTQWNVEEHINPRLPEGSINDYPSSFWSDFLHLNRAMLRANNGLIPDEDKLDALRSEAYQWPFLLATLRMCGWGDNQIKYLLVGNPVAYWFATSSLIVFALFVVGAVLAWRRRVLRWSQEACDTFHYAGIYPFLGWFFNYLPYYIMGRVLYVHHYEPSYALSTFTAAFVVDWFTKKMPKIVRVVVFISLYAIIAGVFIYFKDVTFGMHGPASDFHRLRWLNSWNVHD | Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85037
Sequence Length: 739
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.109
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Q59Q38 | MTPPIKSPSSSSVDYGKLSEQLMIAYTKDVLQRNLQKFHGEQHRQQFKQLLNQPVIKSIHSLSGIIVRYRHNNSELDKALDTIDLPKIFERLEIREKTNKDKNLDYDDLLVLELLNYFKNDFFKWVNSPDCPSCGSNEDVQGLGAINPSSSKTISQSQAIIDQVSVIEVHECKKCKQKIEFPRINNPVTLLTTRRGRCGEWVNCFMLILQALIGGGDDDSDRIRYVWNQEDHVWCEYYSLSSKRWIHLDPCEGVYDEPLLYCNNWGKRMSYVIGFNYNYMIDLSDKYIVPEKQIPKNSIVNVQNVNFVISYSNGINQLKHFKRIEQQQQQQEVDVNEQRNLAFLKLYHNFLVPYNKEINQLKPELTKTTPSTDLPSGRQSGSTEWTKSRGENGES | Cofactor: Binds 1 zinc ion per subunit.
Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (By similarity).
Catalytic Activity: Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.
Sequence Mass (Da): 45840
Sequence Length: 395
Subcellular Location: Cytoplasm
EC: 3.5.1.52
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Q6BNI6 | MSSQGNKYEYGELADKLILAYSKRRLFKAIGTKRDRQQQFSRLDNKDKRFISKLIDVSNSNEKHKIPSELDIALDCIDLAKIYEGVDKREYERESKAKDPNLIYEDFIVLELLHYFKHDFFKWVNKPECSRCKQSSNNIVPTGNSGPPSINPSEISIIENYKCTKCNIAVSFPRYNNPIKLLETKSGRCGEWVNCFIFILRALLGSQSQIRYVWNHEDHVWCEYYSLGLKRWIHLDPCEGVFDEPNLYCENWGKKMSWCFAFGETYIMDVSDKYITKSDKQINKLESVSSLKNIKEFIDTLNDDKLVRYYSNMALTASDENRNLMRLYQEVILIHNSEKFNKENKIEVSRTHNIPTGRQTGDAEWTKSRGEDGNE | Cofactor: Binds 1 zinc ion per subunit.
Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (By similarity).
Catalytic Activity: Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.
Sequence Mass (Da): 43898
Sequence Length: 375
Subcellular Location: Cytoplasm
EC: 3.5.1.52
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Q7F0R1 | MVARRFVVRQGGGGGGGGEAEEHEVEYDTEHGLDILRLQIFSLTSVPPELQKIVVEADGSVVDDGTDLEAISEGLRLVAITGEEEEAEAAAAAEAARAQEKSDEELARMIQAEEEALLLQQYSIRNDGGEEFRERVEPYMHQVLMYEDPMRQEAARKTVPMDELQEKALVSLAKEGNFSPSKDEEDHAFLLQLLFWFKQSFRWVNAPPCDSCGRETFNVGMGTALPSEIKFGANRVEIYRCNYCSSTTRFPRYNDPYKLLETRKGRCGEWANCFTFYCRSFGYEARLILDFTDHVWTECFSNLYGRWMHLDPCEGVYDNPLLYEKGWNKKLDYVIAISKDGVRDVTKRYTRKWHEVLSRRIITSEDTVSAILSSITGKYRSGLSIDGLTALENRDKKESEELSKAAYLEVDTSISLPGRQSGSVEWRKASQKCSTYILSITSGNGCG | Cofactor: Binds 1 zinc ion per subunit.
Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (By similarity).
Catalytic Activity: Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.
Sequence Mass (Da): 50513
Sequence Length: 447
Subcellular Location: Cytoplasm
EC: 3.5.1.52
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O74739 | MDFHAISQRFIDMMRSKNSQNASQPPETYPFYHEVRQMSQHPWMYEDPELQDYALSILPLDKLFQDASELEKEGDGSWGYQDYVIQALLKWFKREFFVWVNQPPCEKCGGETHMTGNGPPNEEEKWNGVRNVELYQCNVCGHNQRFPRYNRIRALLDSRKGRCGEWANCFTFLCRALGSRARWIWNAEDHVWTEVYSNKQQRWVHVDSGEESFDEPLIYEQGWGKKMSYCLGFGIDSVRDVSHRYIRHPENGLPRDRCPESVLQQALHEINIEFRSRLTDSERKALEEEDKREKDELDGYMRPVSQATPTNTDLPARQTGNVEWKEKRGEAGK | Cofactor: Binds 1 zinc ion per subunit.
Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (By similarity).
Catalytic Activity: Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.
Sequence Mass (Da): 39241
Sequence Length: 333
Subcellular Location: Cytoplasm
EC: 3.5.1.52
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Q6CAX5 | MSQATFAKELTAKFAQLWTEKTKRPLPPVNQAMMQRLRQGQRQSGPNEVFSRVSALFRDLSLIPQSFENAELQDMAMEILPLDRLYSVAEERAEEEGERDNWGLQDYLIMELLRWFKQDYFTWVNSPPCETCGENGNVQFVRRENSTPEEQKYDASGTEVHQCSNCNTEIRFPRYNDLSKLMETRRGRCGEWAKCFAFFCRALGLRTRYIWNAEDHVWSEVYSERRKEWIHTDSCEEAWNSPTIYSQGWGKKMSYVVGFSGDGVTDVTRRYVRKADQQLPRTMVPDEQFKTILNSITSDIRQNLSPSEKEELKREDEAEERELASYNADEPQEAQMPRQSGSVEWTKARGEGGSDD | Cofactor: Binds 1 zinc ion per subunit.
Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (By similarity).
Catalytic Activity: Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.
Sequence Mass (Da): 41494
Sequence Length: 356
Subcellular Location: Cytoplasm
EC: 3.5.1.52
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Q02890 | MGEVYEKNNIDFDSIAKMLLIKYKDFILSKFKKAAPVENIRFQNLVHTNQFAQGVLGQSQHLCTVYDNPSWHSIVLETLDLDLIYKNVDKEFAKDGHAEGENIYTDYLVKELLRYFKQDFFKWCNKPDCNHCGQNTSENMTPLGSQGPNGEESKFNCGTVEIYKCNRCGNITRFPRYNDPIKLLETRKGRCGEWCNLFTLILKSFGLDVRYVWNREDHVWCEYFSNFLNRWVHVDSCEQSFDQPYIYSINWNKKMSYCIAFGKDGVVDVSKRYILQNELPRDQIKEEDLKFLCQFITKRLRYSLNDDEIYQLACRDEQEQIELIRGKTQETKSESVSAASKSSNRGRESGSADWKAQRGEDGK | Cofactor: Binds 1 zinc ion per subunit.
Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins. Involved in the formation of free oligosaccharide in cytosol.
Catalytic Activity: Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.
Sequence Mass (Da): 42485
Sequence Length: 363
Subcellular Location: Cytoplasm
EC: 3.5.1.52
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Q0CBN5 | MNKKLKLFSMPGAQTSQIVIMLFQSLLHLLEAIASREPTRYIITYSIGNTHTPEIFSYSDLLQSARKAAGALRFKYHVVPGSVVLLHFNDHWNSMLWFWATLIADCIPAMSTPFSNNPETRLRHLKHLSTTLRSPKCLTTASLAAEFAGQEYITPICVQSLDYENLVHLPIKEGGDIAVLMFTSGSSGHCKVVPLTHEQILASLSGKAWTFPLPDNTAQLNWVGMNHVASLVEVHLFSIYTHSDQVHIPTVEVLSHVTLFLDLIHRHRVSRTFAPNFFLAKLRAALSADDTLAKYTGSLSNLRYIVSGGEANVTQTINDLAQMLKKCGAVSNVIVPAFGMTETCAGAIYNTSFPQYDVEHGLPFASVGSCMPGIQVRIVQLNGNGNSVPPGTVGNLEICGPVVLKGYFNDPAATKSTFTNDNWFKTGDLAFVDDNGMLVLAGREKDSIIVNGANYSPHDIESAIDEANIPGLISGFTCCFSTFPPSADTEEVIIVYLPNYTPADTVRRSETAAAIRKVAMMSVGVRATVLPLDRTMLEKSTLGKLARGKIKAAYERGDYKSYQEANEQMMALHHKVSHHQPRSGLEQSLLGVFTRTIPENLTEDFDVLTSIFDLGITSIELLKLKRGIEDLIGHGQIPLITLMTNPTIRTLSDALKQHAQQRDCSIYNPVVVLQSQGKKPPIWLVHPVGGEVMIFMNLAKFIIDRPVYGLRARGFNDGEDPFHTFEEIVSTYHASIKEKQPSGPYAIAGYSYGAKVAFDIAKALEHNGDEVRFLGLLDLPPSLNGTQMRAVAWKEMLLHICRMVGVIREEGIKKIYPRLEPENISPRHAIETVMGEADVTRLAELGLTASALERWANLTHALQRCIVDHKTNGSVAGADAFYCDPMASMAISNEQWACDYIGKWSDHTRSPPRFHHIAGTHYTILDAENIFSFQKTFLRALNDRGI | Function: Nonribosomal peptide synthetase that mediates the biosynthesis of phenguignardic acid . PngA alone is sufficient for phenguignardic acid synthesis . PngA first activates phenylpyruvic acid (PPA) through its A domain to AMP-PPA . The PPA unit is then loaded to the T domain and eventually transferred to the TE domain . Another PPA unit is then loaded onto the T domain . The TE domain likely promotes the enolate formation on the attached unit, followed by a nucleophilic attack on the carbonyl to yield an ether linkage between the two units . Finally, the TE domain probably catalyzes a similar reaction to give the cyclized dioxolanone core and releases phenguignardic acid .
Catalytic Activity: 2 3-phenylpyruvate + H(+) = H2O + phenguignardate
Sequence Mass (Da): 104487
Sequence Length: 946
Domain: AtrA has a A-T-TE domain architecture (Probable). The adenylation (A) domain recognizes and activates the aryl acid substrates, and loads them onto the thiolation (T) domain (Probable). The thioesterase (TE) domain shares the missing condensation (C) domain function, and is responsible for condensation and final product release (Probable).
EC: 6.3.2.-
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Q0A7A1 | MKSVKKSFQYGNHTVTLETGGVARQADGAVLVNMSDTVVLVTAVGRKEADPGKGFFPLTVNYQERTYAAGKIPGGFFKREGRPSEKETLTCRLIDRPIRPLFPEGFYNEVQVVATVLSMNPEVDADIPALIGASAALSISGIPFDGPIGAARVGYKDGEYLLNPTFEETAASDLDLVVAGTENAVLMVESEANQLPEEAMLGAVLYGHEQMQVAIQAINELTAEAGKPRWDWHPPQGDAALETAIKDLVGDDLAAAYQIPEKQERQNRIGELRQRAVEALGENREEEGGWPEKDVGDAFKGLEKDIVRGRILAGERRIDGRDTRTVRPIDIEVGSLPRTHGSAIFTRGETQAVVVTTLGTGRDAQIIDAIEGERKEQFMLHYNFPPYCVGETGFMGTPKRREIGHGKLAKRGIEAVMPAADDCPYVIRVVSEITESNGSSSMATVCGTSLSLMDAGVPVKAPVAGIAMGLIKEDEQFAVLSDILGDEDHLGDMDFKVAGTESGVTALQMDIKIQGITREIMEQALEQAREGRLHILGEMNNAISGPRSEMSEYAPRLLTIRIDPDKIRDVIGKGGATIRALTEETGTTIDISDDGKVTIASADKAAADEARRRIELLTADVEVGTVYEGKVSKLMDFGAFVNILPGRDGLVHISQISNERVERVGDYLKEGDTVRVKVLEVDRQGRIRLSMKAVQDGE | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 75642
Sequence Length: 698
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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B3EU51 | MLNKIISKTISLPEHREITIETGKLAKQADGSVVVRMGDTMLLATVVFKQELDPTVDFLPLHVEYQEKFAAAGKIPGGFLRREGKLGDHEVLISRLVDRAIRPLFPDNYKHETQINIFLISADPEILPESLAGLAASAALMISPIPFEGPISEVRVARIDGQFVVNPTQSALEKADIDLMVGGSEKNILMVEGEMDEVQEADIIAAIQFAHEAIKLQCQVQKELADAVATLKFEAEPLQETENFELKDRTFKALYDKVYATAKKGITNKHLRKSSFKQIKKEYLKELLQQDPETSTVHFDKYYYELEKQVVRDLALNEGLRLDGRKLDEIRAIESEIDYLPAAHGSSLFTRGETQSLTTVTLGTKLDEQLIDRALLNGYSRFMLHYNFPSFSTGEVKFNRGPGRREIGHGHLAMRALKKVLPLDTENPYTIRIVSDILESNGSSSMATVCAGSLALMDAGISIRSAVSGIAMGLLMDEQTGKHAILSDILGDEDALGDMDFKVAGTAKGITACQMDIKVSGLTPQLLQKALEQAKAGRLHILGEMNKTITEPKTTYKKHAPSFSTMTIPKNMIGAVIGPSGKIVQEMQRETGTTIIIEEVEGKGIIKFFGPNQEAVQSAEKRVKDIVAEPVVGDVYQGTVKSIVPFGAFVEFMPGKEGLLHISEVKWERIENLDQVLELGEVIPVKLLEIDPKSGKYKLSRKVLLPNPKATEA | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 78662
Sequence Length: 713
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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Q2IQ01 | MTPIQKTATVGGKEVLLETGKVAKQAHGSVWVRLGDSIVLVTAVSAAEKKEGIDFFPLTVDYQEKLFAAGRVPGSFFRREGRPTEKETLTSRLVDRSCRPLFAEGYSNETQVIATVISFDQENDTDVLALTGASAALHISDIPFGGPIAGVRVARVGGQLVANPTLAQRADADLDVVMAASRDAIVMVEGGAQEVSEAVMIEALLFGQAAVQPLLDAQDALRAATGNKPRRAFDPPKNDVELRAKVKALTWEKVKEAYGRDEKHDRYGRLSEIKKELLQALKEEAAGDAAKLATIALREKEIKGYYEDVKYDYMRKMITDERRRIGGRGMADIRKITCEVGLLPRVHGSSLFTRGETQALVATTLGTAEDEQRVEMLTGMVFKKFMLHYNFPPFSVGEVKFLRSPGRREIGHGALAERALRAVMPPEDQFPYTVRVVSDIMESNGSSSMASVCGGCLSLMDAGVPIKAPVAGIAMGLIKEGEKIAILSDILGDEDHLGDMDFKVCGTAAGITSIQMDIKIGGVTREILEQALSQAAEGRKHILGEMAKALSAPRGSISAYAPRITTIKIRPERIKDIIGPGGKTIKDITARTGTSINIEDDGSVSIASPNQDKVEEAIKMIRGLTQEAEVGRIYMGTVRKIAEFGAFVEIFPGTDGLIHISELSDKRVKSVSDVLSEGEEVMVKVISVDRSGKIRLSRKEALADSAKKSEGTEPPKGEPAK | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 77920
Sequence Length: 721
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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O66593 | MSVEEKARIGNSEEPIIIETGKYAKLTDGSVVVRQGGTAVLVTAVMSDEPITDVDFTPLAVDYRERASAYGRIPGGFTKREGKPTDREILVSRVIDRPIRPLFPEGFFHDVIITALTLSADDKYDPDVLAITGASAALHISRIPFEGPIAGVRVCRVNGEFVANPTYEQRKEADLDIVMAGTKDAIVMVEGGGKEIPEEVLADALFFGLDAIKEVIEAQERLREKVGKPKFEYQKVELPEDILKALEEECTPKILEAFNIKDKKERYSTLDKIVEEFIEAHQIPEELHFAVKYFYKKLESRLMREKVLKEGVRIDGRKPNEIRPIWIEVHPFERPHGNAIFTRGQTQAYVTVTLGTPDEALIIETIAEGEVFKRFMLHYSMPPFSVGEAKPWGPPRRREIGHGALAERAIEPLLPPEEEYPFIIRVVSDILESNGSTSMATVCGASLALFDAGVPMKDNKHVAGIAMGLILEKDRYVILSDILGDEDHLGDMDFKVAGTKDGITSVQMDIKVKGITKEIMLDALKQAREGRLYILEKMYEAIPEPRKEPHPYTPKVEVVDVPEEKAPLIIGPGGSTVKKIYDETGVKVWVGEQGKVYLFVFPGGDVEKAKQMIQDIVREVEVGAVYKGTITRVEPYGVFVELWPGKIGLLHVSKMAEPVRSATEKYKVGEEIIVKVLDLDELGRPRFTTIGIEDVGTEKKEVKPKVGDVYEGKVVRVEPYGAFIEYAPGKVGLLHVSKMKERVKDARQKYKVGDVVKVKVVEIDEQGRPKFTDDV | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 86489
Sequence Length: 775
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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A1BDY1 | MIINKAIDLGKGKILSIETGKMAKQADGAALVRLGDTMVLATVVSSKTPPPANQDYFPLQVEYREKYSAAGKFPGGFFKREGRPSEKEILTARLIDRALRPLFPDGYLFETQIIVTVFSSDQINDADVLGGVAASAAIMVSDIPFHNSMSEVRVGRINGEFIVNPNINELQGSDIDICIGGTANTICMLEGEMKEISEAEMLDAIKFGHEAIRKICALQDEMAAEIARPQRSFAPVKAPAKLKEVIAGLSETRLKELAYTPLCKEDRAEKTASVYKETLQSTLELFKALLTPEEIAAEPEKALCLNAHIIEEEIHAVEKKVMRHMILDDGKRLDGRTLDEIRPISIELGIIPRAHGSALFTRGETQALVTITLGTKKDAQSVDTLTDSADKRFMLHYNFPPFSVGETGRVGGTGRREIGHGNLAERSIKMVSPSETDFPYTIRIVSDILESNGSSSMASVCGGTLALMDGGVPIRKPVSGIAMGLIKEGDAYSVLSDILGNEDHLGDMDFKVAGTEDGITACQMDIKIDGLDYHILETALEQARKGRLHILDKMEVAIPISRGELAQYAPRLTSIQIPVDAIGLIIGKGGETIRSITEETGAEINIEDDGTVTIACSSPEGTNAAVETIKTLISKPEIGNTYLGKVRDIRDELGAFVEFLPKTDGLVHISEISKERVTKVSDHLKVGDRVKVKLVDIRKDPRTGKNRFALSIKAVESEPEKSDENKAGTEGN | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 79495
Sequence Length: 732
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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Q9Z6R0 | MNFQTISINLTEGKILVFETGKIARQANGAVLVRSGETCVFASACAVDLDDKVDFLPLRVDYQEKFSSTGKTLGGFIKREGRPSEKEILVSRLIDRSLRPSFPYRLMQDVQVLSYVWSYDGQVLPDPLAICAASAALAISDIPQSNIVAGVRIGCIDNQWVINPTKTELASSTLDLVLAGTENAILMIEGHCDFFTEEQVLDAIEFGHKHIVTICKRLQLWQEEVGKSKNLSAVYPLPAEVLTAVKECAQDKFTELFNIKDKKVHAATAHEIEENILEKLQREDDDLFSSFNIKAACKTLKSDTMRALIRDREIRADGRSLTTVRPITIETSYLPRTHGSCLFTRGETQTLAVCTLGSEAMAQRYEDLNGEGLSKFYLQYFFPPFSVGEVGRIGSPGRREIGHGKLAEKALSHALPDSATFPYTIRIESNITESNGSSSMASVCGGCLALMDAGVPISSPIAGIAMGLILDDQGAIILSDISGLEDHLGDMDFKIAGSGKGITAFQMDIKVEGITPAIMKKALSQAKQGCNDILNIMNEALSAPKADLSQYAPRIETMQIKPTKIASVIGPGGKQIRQIIEETGVQIDVNDLGVVSISASSASAINKAKEIIEGLVGEVEVGKTYRGRVTSVVAFGAFVEVLPGKEGLCHISECSRQRIENISDVVKEGDIIDVKLLSINEKGQLKLSHKATLE | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 75347
Sequence Length: 694
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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Q8KBY3 | MFIKKKIDLGHGKVITIETGKMAKQADGSAVVTMNDTMVLATVVSSKTPPSPNQDFFPLQVEYREKYSAAGKFPGGFFKREGRPSEKEILSARLIDRALRPLFPDGYYQETQIIISVISSDTINDADVLGGIAASAAIMVSDIPFANPMSEVRVGRINGLFIVNPDINELAQSDMDICIGGTEDTICMLEGEMKEISEAEMLDAIKFGHDAIKKICALQRELAAEVAKPKRPFSPTVAPDELVNFVEEHCSAELKALAYTPLAKEERAEKTKAIYTQTIRKTLTHFTDRVGPDQIEADPTSAFCLNEHMIEECIHAVEKKVMRHMILDDGKRLDGRTLEQVRPISIELGLIPRAHGSALFTRGETQALVTLTLGTKKDAQSVDTLTDDKDKRFMLHYNFPPFSVGEIGRVGGAGRREIGHGNLAERAIKMVMPSEQEFPYTVRLVSDILESNGSSSMASVCGGTLAAMDGGIPLKKPVSGIAMGLIKEGDRYAVLSDILGNEDHLGDMDFKVAGTRDGITACQMDIKIDGLDYHILETALEQARKGRLHILDVMAEAIPESRADIGKYAPRLTTIQIPVDAIGMVIGKGGETIRSITEETGAEINIDDDGTVTIACSSPEATKAAVETIKTLVSKPEVGTIYMGKVRDIRDELGAFVEFLPKTDGLVHISEIARERIAKVSDVLKVGDRIKVKLIDVRKDPRTGKTKFALSIKALLDTDQQAETNGEAKPARD | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 79938
Sequence Length: 733
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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O84849 | MAFETFSVALDKDKTLIFETGKIARQASGAVLVKMNETWVFSSACAASLSEAVDFLPFRVDYQEKFSSAGRTSGGFLKREGRPSEREILVSRLMDRSLRPSFPNRLMQDIQVLSYVWSYDGKTLPDPLAICGASAALAISEVPQNCIVAGVRVGLVGGKWVINPTRDELSASKLDLVMAGTASAVLMIEGHCDFLTEEQVLEAIAFGQTYIAKICDAIEAWQKAIGKQKNFSAVLDMPEDVQNVVSDFIREKFEKALSFRDKEALEQASKELEESVIANLVQEENSDFSLLNVKAAFKTAKSNQMRALIQDLGIRVDGRTTTEIRPISIETPFLPRTHGSCLFTRGETQSMAVCTLGGENMAQRFEDLNGDGAARFYLQYFFPPFSVGEVGRIGSPGRREIGHGKLAEKALSHVLPETSRFPYIIRLESNITESNGSSSMASVCGGCLALMDAGVPIKAPVAGIAMGLILDRDQAIILSDISGIEDHLGDMDFKVAGTAKGITAFQMDIKIEGITHKIMEQALAQAKQGRSHILNLMTQVLASPKGTVSKYAPRIETMQINTSKIATVIGPGGKQIRQIIERSGAQVDINDDGVINIAASTQESINKAKELIEGLTGEVEVGKVYNGRVTSIATFGVFVEVLPGKEGLCHISELSKQKVDNISDFVKEGDKLAVKLLSINEKGQLKLSHKATLED | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 75499
Sequence Length: 695
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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A5CSN9 | MEGPEIKFAEAVLDNGKYGTRTVRFEAGRLAQQAQGAVAAYLDEDTMLLSATSVGKHPKDNFDFFPLTIDVEERSYAAGKIPGSFFRREGRPSTEAILVCRLIDRPLRPSFITGLRNEVQVVITVLSIAPDEFYDSLAINAASASSMLSGIPFSGPIAGVRLALIGDQWVVFPKHSQLKEAVFDITVAGRVVTDSEGNEDVAIMMVEAEATEGAWDLIQGGATKPDEAIVAQGLEAAKPFIQQLVAAQASLAQQAAKPTVDYPVFLPYAQETYDAVSALALDELGTVYQTADKIERQDADDALKTRTKEAVAAKVEAGELPQSALTEFSAAYKSVTKTVVRGRILRDGVRMDGRGLADIRPLDAEVQVIPRVHGSAIFQRGETQILGVTTLNMLKMEQQIDSLSPITKKRYLHHYNFPPYSTGETGRVGSPKRREIGHGFLAERALVPVLPSREDFPYAIRQVSEALGSNGSTSMGSVCASTLSLLNAGVPLRAPVAGIAMGLVSDTVDGQVRYAALTDILGAEDALGDMDFKVAGTSEFVTAIQLDTKLDGIPTSVLDGALKQAKEARTAILGVLNQAIDGPDEMAPTAPRVISVNIPVDKIGELIGPKGKTINAIQDETGADISIEEDGTVYIGAVDGPSADAARAQVNAIANPTNPEVGESFLGTVVKIATFGAFVSLLPGKDGLLHISEVRKLAGGKRVENVEDVLGVGQKILVEITKIDDRGKLSLAPVLEETADQEGRDAASHGSEAPAEG | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 80380
Sequence Length: 757
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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Q73VX0 | MSVAEIEEGVFEATATIDNGSFGTRTIRFETGRLAQQAAGAVVAYLDDENMLLSATTASKSPKEHFDFFPLTVDVEERMYAAGRIPGSFFRREGRPSTDAILTCRLIDRPLRPSFVDGLRNEIQVVVTILSLDPNDLYDVLAINAASASTQLGGLPFSGPIGGVRVALIDGTWVAFPTVEQLERAVFDMVVAGRKVDGADGPDVAIMMVEAEATSNVIELIDGGAQAPTETVVAQGLEAAKPFIEVLCTAQQELADKAARPTSDYPTFPDYGDDVYYSVASVATDELSKALTIGGKAERDARTDELKAEVLARLAETYEGREKEVSAAFRSLTKKLVRQRILTDHFRIDGRGITDIRALSAEVAVVPRAHGSALFQRGETQILGVTTLDMVKMAQQIDSLGPETTKRYMHHYNFPPFSTGETGRVGSPKRREIGHGALAERALVPVLPSLEDFPYAIRQVSEALGSNGSTSMGSVCASTLALLNAGVPLKAPVAGIAMGLVSDDIEVEAGDGTKSLERRFVTLTDILGAEDAFGDMDFKVAGTKDFVTALQLDTKLDGIPSQVLAGALSQAKDARLTILEVMAEAIDEPDEMSPYAPRVTTIRVPVDKIGEVIGPKGKIINAITEETGAQISIEDDGTVFVGATDGPSAQAAIDRINAIANPQLPTVGERFLGTVVKTTDFGAFVSLLPGRDGLVHISKLGKGKRIAKVEDVVNVGDKLRVEIADIDKRGKISLVLVEEDNSAPADTPAAAPADATS | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 80542
Sequence Length: 757
Subcellular Location: Cytoplasm
EC: 2.7.7.8
|
A0QVQ5 | MSVVELEDGVYESTAVIDNGSFGTRTIRFETGRLAQQAAGSAVAYLDDETMLLSATTASKNPKDHFDFFPLTVDVEERMYAAGRIPGSFFRREGRPSTDAILTCRLIDRPLRPSFVDGLRNEIQVVVTVMSLDPKDLYDVLAINAASMSTQLAGLPFSGPVGGARIALIDGTWVAFPTVEQLERAVFDMVVAGRIVGDGDSADVAIMMVEAEATENVVELVAGGAQAPTEAVVAEGLEAAKPFIKALCAAQQELADRAAKPAGEYPVFPDYEADVYDAVASVATEALAEALTIAGKTERNDRTDEIKVEVLERLAEPYAGREKEIGAAFRSLTKKLVRQRILTDHFRIDGRGITDIRALSAEVAVIPRAHGSALFERGETQILGVTTLDMIKMAQQIDSLGPENTKRYMHHYNFPPYSTGETGRVGSPKRREIGHGALAERALVPVLPSIEEFPYAIRQVSEALGSNGSTSMGSVCASTLALLNAGVPLKAPVAGIAMGLVSDDVDVDGKVEKRYVALTDILGAEDAFGDMDFKVAGTKDFVTALQLDTKLDGIPSQVLAGALSQAKDARLTILDVMAEAIDRPDEMSPYAPRITTIKVPVDKIGEVIGPKGKMINSITEETGAQISIEDDGTVFVGAADGLSAQAAIDKINAIANPQLPKVGERFLGTVVKTTDFGAFVSLLPGRDGLVHISKLGKGKRIAKVEDVVKVGDKLRVEIADIDNRGKISLVLVAEESAESAESAGDKGAEKAEGAAADVTPAEA | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 81027
Sequence Length: 763
Subcellular Location: Cytoplasm
EC: 2.7.7.8
|
A3PY93 | MSVVEIEDGVYESTAVIDNGSFGTRTIRFETGRLAQQAAGAVVAYLDDETMLLSATSASKSPKDHFDFFPLTIDVEERMYAAGRIPGSFFRREGRPSTDAILTCRLIDRPLRPTFVSGLRNEIQVVVTVMSLDPKDLYDVVAINAASASTQIAGLPFSGPVGGVRVALIDGTWVAFPTVEQLERAVFDMVVAGRKTADDVAIMMVEAEATDKVVELVAGGAQAPTEAVVAEGLEAAKPFIKVLCEAQQELAGRAAKPTADYPLFPEYGEDVYYAVASVATDALSEALTIAGKEERNNRTDEIKVEVLGRLADQFAGREKEIGGAFRSLTKKLVRQRILTDHFRIDGRGVTDIRALSAEVAIVPRAHGSALFERGETQILGVTTLDMVKMAQQIDSLGPETSKRYMHHYNFPPYSTGETGRVGSPKRREIGHGALAERALMPVLPSVEEFPYAIRQVSEALSSNGSTSMGSVCASTLSLLNAGVPLKAPVAGIAMGLVSDDVEVDGKTERRFVTLTDILGAEDAFGDMDFKCAGTKDFVTALQLDTKLDGIPSQVLAGALAQAKDARITILEVMAEAIDAPDEMSPYAPRITTIKVPVDKIGEVIGPKGKMINSITEETGASISIEDDGTVFVGASNGEAAQAAIDKINAIANPQLPKIGERFLGTVVKTTDFGAFVSLLPGRDGLVHISKLGRGKRIAKVEDVAKVGDKLRVEIADIDNRGKISLVLVAEEEAAEASDNGSATPSDKAPATADATTAGN | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 80676
Sequence Length: 759
Subcellular Location: Cytoplasm
EC: 2.7.7.8
|
B2A3A3 | MPTTVSEEIAGYQLTLETGELAKQANGAVKVQYGNTVVLVTATASKEPKDDLNFFPLTVDYEERLYAVGKIPGGFIKREGKPTEKATLTARLTDRPIRPLFPDGFRNPVHIVSTVLSVDQNCPPEIASIIGASAALSISDIPFDGPIASVKVGKVNDEIVVTPDVDEHEESQLDLVVAGTKDAIMMVEAEANELPEDEMLEAIMKAHEEIKKIITMQEQLVEQVGQKKMEVELDLPSDELVSEVEELALEDIEKVLQIKDKLEREDAMDEAKQKVVDHLLEKYNSEENEDEEEELKEKHIKSAFDSILKREMRSRIIHENSRPDGRGQKEIRPVTCDVDLLPNTHGSGLFTRGQTQVLNVCTLGALGDVQILDGLDIEESKRYMHHYNFPPYSVGEAGFMKGPGRREIGHGALAERALKPMIPTEKDFPYTIRLVSEVLESNGSTSMGSVCASSLSLMDAGVPIEKAVSGIAMGLIKEGDQLAILSDIQGIEDFLGDMDFKVAGTEDGITALQMDIKISGTTREILKQALKQGKDGYLHILNIMKQTISEPREELSPLAPRVIKKQIDPDKIRNVIGPGGKMINKIIDETGVKIDIEPDGLIYISSSDAEQAEQAIKAIDELIKEPEVGEVYLGKVVRTEKYGAFVEILPGKEGLVHISELAEDRVGKTEDVAKVGDEILVKIINIDERGRINLSRKQALGEEDGKTNNDDKKSTKKT | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 79043
Sequence Length: 718
Subcellular Location: Cytoplasm
EC: 2.7.7.8
|
Q9ZD43 | MFNEITKSVMWNGQVLEISTGKIARQANAAVTVKMGNSILLCTCVVANKVKDGIGFFPLTINYREMAYSAGKIPGGFFKREGKASDREILVSRLIDRPIRPLFHQAFMHETHVTCSVLSYDPATPVDILAIIGASAALSISPAPYLEIVAASKVGLINGEFVLNPTLELLKTSQLDLVVAGTEDSVMMVESEAHLLSEDKMLEAVKFGFESFQTVIKLIKELAKEAKKPKFEMQDLYPSSLKKEIEKLFTKEVEQAFEIKSKQERSTDLALIYEKVLTHFVRDIENKKYNNYQIESALKAISADILRNKILEKNIRIDGRSTTDIRQIACEVGLLPSAHGSALFTRGETQSLVSTTFGTSLDEQIVDSLEGEYKERFMLNYIFPPYSVNEAMPMKAPSRREVGHGKLAWRAINPILPNKVQFPYSIRVVAETTESNGSSSMATVCGSSLALMHAGVPIKAPVAGIAMGLVKESNKFAVLSDIIGDEDYFGDMDFKVAGTSSGITALQMDIKISGIDFKIIQIALEQARLGRLHILEQMNKVISKPNSELSKNAPSSTTVKIDKDKIKDIIGPGGKIIKEICETSNAKIDISDDGTVSIYASDRDKIKIALDKIKAIAVEPEIGEIFNGTVMKVLDSGAFINYLGNKDGFVHISEISDARIDKVSSVLKQGDIVKVKLIGFDNKGKAKLTIKNAYKDHSSNNTKQKNNVKDDSESEQRRDTSKKRTWNEDNNTEMSEVITERKYFT | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 82340
Sequence Length: 745
Subcellular Location: Cytoplasm
EC: 2.7.7.8
|
B8I2R5 | MFKSFSMELAGRTLTVETGKLAQLANGSALIRYGDTVIMSSATASAAPRDGIDFFPLSVDYEERLYAVGKIPGGFIKREGKPSEKAILTSRVIDRPIRPLFPKDLRNDVAVVNTVMSVEQDNSPEIAAMIGASVAISISDIPFNGPIGGVVLGLVDGEVIINPNEEQRAKSKMYVTLAGTKEKITMIEAGADIVPDDVMFDAIKKGHEEIKKICDFINGIVKEVGKAKFTYESADVPADLFEVVKEFAYDKMRIAVLATDKQDRDAKVSQLTEETQAALAEQFPEMESKINDALYKLEKKVVREYILKEGKRIDGRRLDEIRTLSAEVGILPRTHGSGLFERGQTQVLTTVTLGAMGDVQMLDGIDTEETKRYMHHYNFPGYSVGEAKTSRGPGRREIGHGALAERSLVPVIPTETEFPYAFRLVSEVLMSNGSTSQGSVCGSTLALMDAGVPIKAPVAGISAGLVIDEENPDNFVTFMDIQGIEDFFGDMDFKVAGTTEGITAIQMDIKVDGLSYEIIRQAFELTRMGRLQIINDVILKAIPQPRKELSEYAPKIITTNIDPEKIRDVIGPGGKMINKIIAETGVKIDIEEDGRVYILTPDSAAAQKALKIIQGIAKDIEPGEVYLGKVVRITTFGAFVEILPGKDGLVHISKLDKKRVEKVEDVVSIGDEILVKVTEIDKQGRINLSRKDAMAEENTTEEK | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 76926
Sequence Length: 703
Subcellular Location: Cytoplasm
EC: 2.7.7.8
|
A1AWB1 | MGINTKSFVMGKHTITLETGRIARQAHGAVLVSMDDTQVLVTVVGSKKMHPGQDFFPLSVDYIEKTYAAGKIPGGFLKREARPSEKETLTSRLIDRPIRPLFPNGFMNEVQVLITVISANSEVDPDIISMLGVSAALSISGIPFNGPIGSARVGYSNGKYTLNPTYTELVDSDLDMVVAGTDKAILMVESEASELSEKIILDAIIYAHEQYQVAITNIAEFVTQVGVQKWDWEAPATNEVLLSNIKSQFGKQINEAYKIKEKLNRHVKVGEIKTAAIEALVNEDKNGNSIDEVSKYFNKVEKSTVRERILNNDPRIDGRDNETVRELKIETGVLENTHGSALFTRGETQALVVTTLGSKREAQLIEKLESSERQNDYFLLHYNFPPYCVGEIGRVGTTKRREIGHGRLVRRGIAACLPSIEEFPYTVRVVSEITESNGSSSMASICGASLSLMDAGVPIKAPVAGIAMGLVKEGDRFTILTDILGDEDHLGDMDFKVAGTSRGINALQMDIKIQGITREIMEIALKQAKEARLNILGQMNQVICEPNTSNKNTPKTAVIKIQTDKIRDLIGKGGETIKGIISTSSASVDVDDNGNVNIFSNDQKSFDTAMQMVKDVTTTPKIGKVYTGKVVKIVDFGAFINIKPNQDGLLHISEIAHERVDKVENHLKEGDEIDVKVLSLDRGRIKLSRKVLLEK | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 76315
Sequence Length: 695
Subcellular Location: Cytoplasm
EC: 2.7.7.8
|
Q9NPJ4 | MGGGERYNIPAPQSRNVSKNQQQLNRQKTKEQNSQMKIVHKKKERGHGYNSSAAAWQAMQNGGKNKNFPNNQSWNSSLSGPRLLFKSQANQNYAGAKFSEPPSPSVLPKPPSHWVPVSFNPSDKEIMTFQLKTLLKVQV | Function: Involved in nonsense-mediated mRNA decay (NMD) by acting as a bridge between the mRNA decapping complex and the NMD machinery . May act by targeting the NMD machinery to the P-body and recruiting the decapping machinery to aberrant mRNAs . Required for UPF1/RENT1 localization to the P-body . Plays a role in glucocorticoid receptor-mediated mRNA degradation by interacting with the glucocorticoid receptor NR3C1 in a ligand-dependent manner when it is bound to the 5' UTR of target mRNAs and recruiting the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay . Also acts as a nuclear receptor coactivator . May play a role in controlling the energy balance between energy storage and energy expenditure (By similarity).
Sequence Mass (Da): 15591
Sequence Length: 139
Domain: The interaction between PNRC2 and nuclear receptors is dependent on the SH3 binding motif.
Subcellular Location: Nucleus
|
Q75EG5 | MYGKSGPPPEGYVPQHPPAQGYAPHNPPPGYVHENPFQEPVPQGQEYSPQGQQYQFRKDQYYNLDHQGSGAPIGDASFEDKFPTEAGNRLKFNDWPFTIIFLLTVGAFIAVAVLTLRGWSLSPTSNGSGIYDGDNTHTLNTNAAILLLISCGVAVALSVFGLVLAGMYTKFFIYAAMILNTVVGLGTAITYLVLRHWSAGIVFMIFTILTAVCYWLMRSRIPFSVAVLRTVMSVMKKHPQTWLVSLLGTIVSAAFSVIFSVVLVATYIKYDPKSENGGCDVSGGSCSRGKLIGILVLVFFCGFYISEVIRNVIHCTIAGIYGCWYYFSKSDQGMPRWPAFGSLKRALTTSFGSICFGSLIVSLIQLLRQIIQLLRNGIISGISDSGWMQCLWLILDAVVGVFEWMAEYFNHYAYCFIALYGKPYLRAAKETWHMLREKGIDALINDNLINLALGFYTLFVGYTTALFSYLFLRFTKPDYNSGGGFNAVLMAFSFLIAIQLTHVATETIRSGTATFFVALGNDPEIFRVSYPQRFDEIFRAYPDVLNKLSHQHV | Function: Probably involved in transport through the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61473
Sequence Length: 553
Subcellular Location: Cell membrane
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