ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q51854 | MADRQRDPDLADTLLLLEHPPVYTLGRGSSLDFIKFTPPASFTAGVTPSSRAEPTPPQPGPELHRTERGGEVTYHCPGQLVGYPILNLRRLSADLHWYLRQLEEYLIRVLDHYGLRGERI | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity).
Catalytic Activity: L-lysyl-[protein]... |
A2C0K7 | MDKKLHSVSPESGPNSNLDLTPQLAQSSSAFLFEPKNIVPFETALGWQKNFLKNLIEEPFSPQAVWLLEHFSCFTMGRGSDKKNLLFEENNSPLPVFSIERGGEVTHHMPGQIVGYLVLNLSLHKKDLAWYLRELEQVLIDVLDLLGIEGKRVDGLTGVWCEDKKVGSIGIGCKRWVTQHGFSLNVDCDLIGFEKIIPCGLDKVKVGKLSDWIPGIKVCDVTPLLRESVKRRFKLNWEKINQSL | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
P07098 | MWLLLTMASLISVLGTTHGLFGKLHPGSPEVTMNISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGNTGQRPVVFLQHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGTTIGFIAFSTNPSLAKRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFFDQFLATEVCSREMLNLLCSNALFIICGFDSKNFNTSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWGSPVQNRMHYDQ... | Function: Catalyzes the hydrolysis of triacylglycerols to yield free fatty acids, diacylglycerol, monoacylglycerol, and glycerol . Shows a preferential hydrolysis at the sn-3 position of triacylglycerol .
Catalytic Activity: a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+)
Sequence Mass (Da): 45238
Sequ... |
Q7D5F9 | MSSYYARRPLQSSGCSNSDSCWDGAPIEITESGPSVAGRLAALASRMTIKPLMTVGSYLSPLPLPLGFVDFACRVWRPGQGTVRTTINLPNATAQLVRAPGVRAADGAGRVVLYLHGGAFVMCGPNSHSRIVNALSGFAESPVLIVDYRLIPKHSLGMALDDCHDAYQWLRARGYRPEQIVLAGDSAGGYLALALAQRLQCDDEKPAAIVAISPLLQLAKGPKQDHPNIGTDAMFPARAFDALAAWVRAAAAKNMVDGRPEDLYEPLDHIESSLPPTLIHVSGSEVLLHDAQLGAGKLAAAGVCAEVRVWPGQAHLFQLA... | Function: A short-chain esterase and phospholipase.
Catalytic Activity: a carboxylic ester + H2O = a carboxylate + an alcohol + H(+)
Sequence Mass (Da): 39611
Sequence Length: 373
EC: 3.1.1.1
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P04634 | MWLLLITSVISTFGGAHGLFGKLGPGNPEANMNISQMITYWGYPCQEYEVVTEDGYILGVYRIPHGKNNSENIGKRPVVYLQHGLIASATNWIANLPNNSLAFMLADAGYDVWLGNSRGNTWSRKNVYYSPDSVEFWAFSFDEMAKYDLPATINFIVQKTGQEKIHYVGHSQGTTIGFIAFSTNPTLAKKIKTFYALAPVATVKYTQSPLKKISFIPTFLFKLMFGKKMFLPHTYFDDFLGTEVCSREVLDLLCSNTLFIFCGFDKKNLNVSRFDVYLGHNPAGTSVQDFLHWAQLVRSGKFQAFNWGSPSQNMLHYNQK... | Function: Catalyzes the hydrolysis of triacylglycerols to yield free fatty acids, diacylglycerol, monoacylglycerol, and glycerol . Shows a preferential hydrolysis at the sn-3 position of triacylglycerol (By similarity).
Catalytic Activity: a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+)
Sequence Mass (... |
Q1PDW3 | MIIMMNCFPCFTSQKSRNAPCTTNETNDDNVEHDEFRPPVVATTKRTEEREPAEQQPPVKTFNFRELATATKNFRQECLLGEGGFGRVYKGTLQSTGQLVAVKQLDKHGLHGNKEFLAEVLSLAKLEHPNLVKLIGYCADGDQRLLVFEYVSGGSLQDHLYEQKPGQKPMDWITRMKIAFGAAQGLDYLHDKVTPAVIYRDLKASNILLDAEFYPKLCDFGLHNLEPGTGDSLFLSSRVMDTYGYSAPEYTRGDDLTVKSDVYSFGVVLLELITGRRAIDTTKPNDEQNLVAWAQPIFKDPKRYPDMADPLLRKNFSERG... | Function: Involved in pollen tube guidance into micropyle. Participates in perception of the ovule-secreted peptide signal LURE1.
PTM: Palmitoylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 71552
Sequence Length: 636
Subcellular Location: Cell membrane
EC: 2.7.11.-
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Q9Y5X9 | MSNSVPLLCFWSLCYCFAAGSPVPFGPEGRLEDKLHKPKATQTEVKPSVRFNLRTSKDPEHEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHTREKDANVVVVDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGADIHKRLSPDDADFVDVLHTYTRSFGLSIGIQMPVGHIDIYPNGGDFQPGCGLNDVLGSIAYGTITEVVKCEHERAVHLFVDSLVNQDKPSFAFQCTDSNRFKKGICLSCRKNRCNSIG... | Function: Exerts both phospholipase and triglyceride lipase activities . More active as a phospholipase than a triglyceride lipase . Hydrolyzes triglycerides, both with short-chain fatty acyl groups (tributyrin) and long-chain fatty acyl groups (triolein) with similar levels of activity toward both types of substrates ... |
Q9WVG5 | MRNTVFLLGFWSVYCYFPAGSITTLRPQGSLRDEHHKPTGVPATARPSVAFNIRTSKDPEQEGCNLSLGDSKLLENCGFNMTAKTFFIIHGWTMSGMFESWLHKLVSALQMREKDANVVVVDWLPLAHQLYTDAVNNTRVVGQRVAGMLDWLQEKEEFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRLSPDDADFVDVLHTYTLSFGLSIGIRMPVGHIDIYPNGGDFQPGCGFNDVIGSFAYGTISEMVKCEHERAVHLFVDSLVNQDKPSFAFQCTDSSRFKRGICLSCRKNRCNNIG... | Function: Exerts both phospholipase and triglyceride lipase activities (By similarity). More active as a phospholipase than a triglyceride lipase (By similarity). Hydrolyzes triglycerides, both with short-chain fatty acyl groups (tributyrin) and long-chain fatty acyl groups (triolein) with similar levels of activity to... |
Q6DBU8 | MIYRKIIWGILYVTLMLFDTHRAQECEEMTDLNFKDSLAGTSLKVRLLLYTRADPSCGQLLSHQEPFSNSQFNVSSVTTFLIHGYRPTGSPPVWMKQFVEFLLNRRDMNVIVVDWNRGATNMNYWQVVKNTRKVANNLTDLIQKMKDNGANLSSIHMIGVSLGAHISGFTGANFNGEIGRITALDPAGPEFNGRPPEDRLDPSDALFVEALHTDMDALGYRNLLGHIDYYANGGADQPGCPKTILSGSEYFKCDHQRSVFLYMSSVNGSCPIIAYPCESYTDFQDGTCMDCGKFKSAGCPIFGYDSVRWRDTLVQLEQTR... | Function: Hydrolyzes specifically phosphatidic acid (PA) to produce 2-acyl lysophosphatidic acid (LPA; a potent bioactive lipid mediator) and fatty acid (By similarity). Does not hydrolyze other phospholipids, like phosphatidylserine (PS), phosphatidylcholine (PC) and phosphatidylethanolamine (PE) or triacylglycerol (T... |
Q8WWY8 | MLRFYLFISLLCLSRSDAEETCPSFTRLSFHSAVVGTGLNVRLMLYTRKNLTCAQTINSSAFGNLNVTKKTTFIVHGFRPTGSPPVWMDDLVKGLLSVEDMNVVVVDWNRGATTLIYTHASSKTRKVAMVLKEFIDQMLAEGASLDDIYMIGVSLGAHISGFVGEMYDGWLGRITGLDPAGPLFNGKPHQDRLDPSDAQFVDVIHSDTDALGYKEPLGNIDFYPNGGLDQPGCPKTILGGFQYFKCDHQRSVYLYLSSLRESCTITAYPCDSYQDYRNGKCVSCGTSQKESCPLLGYYADNWKDHLRGKDPPMTKAFFDT... | Function: Hydrolyzes specifically phosphatidic acid (PA) to produce 2-acyl lysophosphatidic acid (LPA; a potent bioactive lipid mediator) and fatty acid. Does not hydrolyze other phospholipids, like phosphatidylserine (PS), phosphatidylcholine (PC) and phosphatidylethanolamine (PE) or triacylglycerol (TG).
Catalytic Ac... |
Q8CIV3 | MLRLCFFISFMCLVKSDTDETCPSFTRLSFHSAVVGTGLSVRLMLYTQRDQTCAQIINSTALGSLNVTKKTTFIIHGFRPTGSPPVWIEELVQSLISVQEMNVVVVDWNRGATTVIYPHASSKTRQVASILKEFIDQMLVKGASLDNIYMIGVSLGAHIAGFVGESYEGKLGRVTGLDPAGPLFNGRPPEERLDPSDALFVDVIHSDTDALGYKEALGHIDFYPNGGLDQPGCPKTIFGGIKYFKCDHQMSVYLYLASLQNNCSITAYPCDSYRDYRNGKCVSCGAGQIVPCPRVGYYADSWKEYLWDRDPPMTKAFFDT... | Function: Hydrolyzes specifically phosphatidic acid (PA) to produce 2-acyl lysophosphatidic acid (LPA; a potent bioactive lipid mediator) and fatty acid (By similarity). Does not hydrolyze other phospholipids, like phosphatidylserine (PS), phosphatidylcholine (PC) and phosphatidylethanolamine (PE) or triacylglycerol (T... |
Q6XZB0 | MRVYIFLCLMCWVRSDNKRPCLEFSQLSVKDSFRDLFIPRIETILMMYTRNNLNCAEPLFEQNNSLNVNFNTQKKTVWLIHGYRPVGSIPLWLQNFVRILLNEEDMNVIVVDWSRGATTFIYNRAVKNTRKVAVSLSVHIKNLLKHGASLDNFHFIGVSLGAHISGFVGKIFHGQLGRITGLDPAGPRFSRKPPYSRLDYTDAKFVDVIHSDSNGLGIQEPLGHIDFYPNGGNKQPGCPKSIFSGIQFIKCNHQRAVHLFMASLETNCNFISFPCRSYKDYKTSLCVDCDCFKEKSCPRLGYQAKLFKGVLKERMEGRPL... | Function: Hydrolyzes specifically phosphatidic acid (PA) to produce 2-acyl lysophosphatidic acid (LPA; a potent bioactive lipid mediator) and fatty acid. Does not hydrolyze other phospholipids, like phosphatidylserine (PS), phosphatidylcholine (PC) and phosphatidylethanolamine (PE) or triacylglycerol (TG).
Catalytic Ac... |
Q4ICM0 | MSRTLTSRQAEELHKSIIAYLAANNLQDSANAMRTELGLGEDAFDTATAKKYETLLEKKWTSVVRLQKKIMDLEAQTQTLQTELNSATPTSNRRGDPSSWLPAGPPRHVLQSHRTPINCVAFHPIFSSIASGDEDATIKIWDWEFGELERTVKGHTKAVLDLDYGGPKGHTLLASCSSDLTIKLWDPANEYQNIRTLPGHDHSVSAVRFIPSGAPGAPLSGNLLASASRDVTVRIWDVTTGYCVKTIRGHADWIRDVSPSLDGKYLLSTGNDRTVRLWDISVPNPEAKLVMIGHEHFVECCTFAPPAAYSHLATLAGVKK... | Function: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for nuclear migration during vegetative growth as well as development. Required for retrograde early endosome ... |
A9V790 | MVLTARQQEELQLAVHAYLVEAGHAEAAAAMAKSANLGDDAGDAKYTGLLEKKWTTITRLQKRNMELQAEVEELRSSARAPRSRTTTKMEEWVPRPPATVAVDGHRLPITAVAIHPSFAVMASASEDASIKLWDMESGNFERSLKGHTNAVNDIAYDREGNRLVSCSTDMTIKVWNMDNFTCTKTLSGHDHTVSSVRFDHTGDRVFSASRDKTIKIWELATGYCLQTLQGHSDWVRSIDVSADGAWICSASSDHTVRVWSVASGECKHVWSDHEHVVEHASFAPLVAHEALNLMIFGSKPSAEAASKGPFVASASRDKSI... | Function: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes.
Sequence Mass (Da): 45189
Sequence Length: 410
Domain... |
P63005 | MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTI... | Function: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic... |
Q0U1B1 | MSAILTDRQAEELHKAIIAYLGVINAPKTAAAFREEVNFSAAFDDATRKKYEGLLEKKWTSVVRLQKKVLELEQRNQSLQSELDSTTPTSLLRRNQDPSSWLPRAPARHTLQSHRSPITCVAFHPVFSSLASGSEDTTIKIWDWELGELERTVKGHTKGVLDVDFGGPRGGTLLASCSSDLTIKLWDPSDEYKNIRTLPGHDHSVSAIRFVPSGAAGSPSSGNLLVSASRDKTLRVWDVTTGYCVKTIRGHADWVRDVSPSFDGRWLLSAGNDQTARLWDASSGEAKCTFLGHEHVIECVTIAPPVSYANLASLAGLKKP... | Function: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for nuclear migration during vegetative growth as well as development. Required for retrograde early endosome ... |
Q7ZUA6 | MEADEVSIREQNFHSQVREYTICFLLFAVLYIVSYFIITRYKRKADEQEDEDAIVNRISLFLSTFTLAVSAGAVLLLPFSIISNEILLSFPQNYYIQWLNGSLIHGLWNLASLFSNLCLFVLMPFAFFFLESEGFAGLKKGIRARILETLVMLILLALLILGIVWVASALIDNDAASMESLYDLWEFYLPYLYSCISLMGCLLLLLCTPVGLSRMFTVMGQLLVKPTILEDLDEQMYIITLEEEAIQRKLNGISSTLENQTVELERELEKVKCKKTNLERRKKASAWERNLVYPAVMILLLIETSISVLLVAFNILYLLV... | Function: Putative membrane receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55084
Sequence Length: 488
Subcellular Location: Membrane
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Q8WVP7 | MEGQDEVSAREQHFHSQVRESTICFLLFAILYVVSYFIITRYKRKSDEQEDEDAIVNRISLFLSTFTLAVSAGAVLLLPFSIISNEILLSFPQNYYIQWLNGSLIHGLWNLASLFSNLCLFVLMPFAFFFLESEGFAGLKKGIRARILETLVMLLLLALLILGIVWVASALIDNDAASMESLYDLWEFYLPYLYSCISLMGCLLLLLCTPVGLSRMFTVMGQLLVKPTILEDLDEQIYIITLEEEALQRRLNGLSSSVEYNIMELEQELENVKTLKTKLERRKKASAWERNLVYPAVMVLLLIETSISVLLVACNILCLL... | Function: Putative membrane receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55098
Sequence Length: 490
Subcellular Location: Membrane
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Q5U4X7 | MEEDEVTIREQNFYSQVRECIICFLLFAILYIVSYFIIKRYKRKGDEQEDEDATVNRVSLFLCTFTLAVSGGAVLLLPFSIISNEILLCFPKSYYIQWLNGSLIHGLWNLVSLFSNLCLFVLMPFAFFFLESEGFAGLKKGIKARILETIIMLILLALLIFGIVWVASALIDNSSASMESLYDLWDCYLPYLYSCISLMGCLLLLLCTPVGLSRMFTVMGQLLVKPTILEDIDEQMYIISLQEEALQRKLNGGNYTADYSRKKIEHDLLNARSMKSKLERRKNASAWQRNLVYPAVMILLLIATFSSVILVSLNILRLLV... | Function: Putative membrane receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54690
Sequence Length: 485
Subcellular Location: Membrane
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Q803C7 | METEDVTVREQIFHDRVRETIICVLLFICLYILSHFILTHFKKSAEFVTDDIEDATVNKIALWLCTFTLSVAVCAVLLLPISILSNEVLLTFPHSYYMQWLNGSLIRGLWNLVFLFSNLSLVFLMPFAYFFTESEGFAGSKKGVMARVYETAVMLLLLSLLVLGIVWVASALLHHNTARESLYDLWEYYLPYLYSGISLFGVLLLLLCTPFGLSRMFSVTGSLLVKPRLLENLEETMNCAVFEEASLSRKLKSTNTCWISAHLEALNKEFLSVQSKRITLELRKRASPWQRNLVYPVAMLLLLALTAVSVLMVCFHVLEL... | Function: May play a role in lymphocyte development by negatively regulating the canonical Wnt signaling pathway (By similarity). May act as a LCN1 receptor (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55147
Sequence Length: 491
Subcellular Location: Cell membrane
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Q6UX01 | MEAPDYEVLSVREQLFHERIRECIISTLLFATLYILCHIFLTRFKKPAEFTTVDDEDATVNKIALELCTFTLAIALGAVLLLPFSIISNEVLLSLPRNYYIQWLNGSLIHGLWNLVFLFSNLSLIFLMPFAYFFTESEGFAGSRKGVLGRVYETVVMLMLLTLLVLGMVWVASAIVDKNKANRESLYDFWEYYLPYLYSCISFLGVLLLLVCTPLGLARMFSVTGKLLVKPRLLEDLEEQLYCSAFEEAALTRRICNPTSCWLPLDMELLHRQVLALQTQRVLLEKRRKASAWQRNLGYPLAMLCLLVLTGLSVLIVAIH... | Function: Plays an essential role in lymphocyte development by negatively regulating the canonical Wnt signaling pathway (By similarity). In association with UBAC2 and E3 ubiquitin-protein ligase AMFR, promotes the ubiquitin-mediated degradation of CTNNB1 and Wnt receptors FZD6 and LRP6 (By similarity). LMBR1L stabiliz... |
Q7ZX75 | MEVNQDVSVREQIFHDWVRECIICSLLFSTLYLLSYIVITKFKKHADFATVDVEDAAVNRIALWMCTFTLAVSVGAVLLLPFSIISNEVLLSVPHNYYIQWLNGSLIHGLWNLVFLFSNLSLVFLMPFAYLFTEAEGFAGSKKGVMSRVYETTVVLLLLTLLVFGIVWVASAIFDDDSAGRESLYDLWEYYLPYLYSGISLFGVLLLLLCTPFGLSRMFSVTGNLLVKPRLLENLEEHLSCTAFEEAAISRKISTKASCWLNLNMEALQKRLLAIQSHRITLEMRRRASPWQRNLVYPLAMLLLLALTGITVLIVCVNVL... | Function: May play a role in lymphocyte development by negatively regulating the canonical Wnt signaling pathway (By similarity). May act as a LCN1 receptor (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54229
Sequence Length: 483
Subcellular Location: Cell membrane
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Q8Y8Q5 | MEIYRKSAAETFTQLEATEKGLTTSEVTKRQEKYGFNELKNKKKDPLWKLFLETFKDPMVIVLVIAALVQLVLGEVVESLIIFLVLIVNSIISVVQTRKAESSLDALREMSAPVAKVIRDGSKQSIHARELVPGDVVILDAGDFVPADGRLFESGSLKIDEGMLTGESEAVEKYIDTIPDEVGLGDRVNMVFSGSLVVYGRGMFVVTGTASETEIGKIAGLLETAEAKQTPLQRKLESFSKKLGLGILALCVLIFAVEAGRVLLGDNSADMATAILNAFMFAVAVAVAAIPEALSSIVTIVLAVGTNKMAKQHAIIRKLP... | Function: Catalyzes the hydrolysis of ATP coupled with the transport of calcium. The transport is electrogenic with a probable ATP:Ca(2+):H(+) stoichiometry of 1:1:1. May have an important role in survival of the bacterium when stressed by a combination of a high calcium concentration and alkaline pH.
Catalytic Activit... |
Q9NZU5 | MAKVAKDLNPGVKKMSLGQLQSARGVACLGCKGTCSGFEPHSWRKICKSCKCSQEDHCLTSDLEDDRKIGRLLMDSKYSTLTARVKGGDGIRIYKRNRMIMTNPIATGKDPTFDTITYEWAPPGVTQKLGLQYMELIPKEKQPVTGTEGAFYRRRQLMHQLPIYDQDPSRCRGLLENELKLMEEFVKQYKSEALGVGEVALPGQGGLPKEEGKQQEKPEGAETTAATTNGSLSDPSKEVEYVCELCKGAAPPDSPVVYSDRAGYNKQWHPTCFVCAKCSEPLVDLIYFWKDGAPWCGRHYCESLRPRCSGCDEIIFAEDY... | Function: Transcriptional cofactor that restricts GATA6 function by inhibiting DNA-binding, resulting in repression of GATA6 transcriptional activation of downstream target genes. Represses GATA6-mediated trans activation of lung- and cardiac tissue-specific promoters. Inhibits DNA-binding by GATA4 and GATA1 to the cTN... |
Q8VEE1 | MAKVAKDLNPGVQKMSLGQQQSARGVACLRCKGMCSGFEPHSWRKICKSCKCSQEEHCLSSDLDDDRKIGRLLMDSKYATLTARVKGGDGIRIYKRNRMIMTNPIATGKDPTFDTITYEWAPPGVTQKLGLQYMELIPKERQPVTGTEGALYRRRQLMHQLPIYDQDPSRCRGLVENELKAMEEFVKHYKSEALGVGEVALPGQGGLPKEENKTQEKPEGTETTAPTTNGSLGDPSKEVEYVCELCKGAAPVDSPVVYADRAGYSKQWHPTCFQCIKCSEPLVDLIYFWKDGAPWCGRHYCESVRPRCSGCDEIIFSEDY... | Function: Transcriptional cofactor that restricts GATA6 function by inhibiting DNA-binding, resulting in repression of GATA6 transcriptional activation of downstream target genes. Represses GATA6-mediated trans activation of lung- and cardiac tissue-specific promoters. Inhibits DNA-binding by GATA4 and GATA1 to the cTN... |
Q5PXT2 | MAKVAKDLNPGVQKMSLGQQQSARGVPCLRCKGTCSGFEPHSWRKICKSCKCSQEDHFLSSDLEDDRKIGRLLMDSKYSTLTARVKGGDGIRIYKRNRMIMTNPIATGKDPTFDTITYEWAPPGVTQKLGLQYMELIPKEKQPVTGTEGAYYRRRQLMHQLPIYDQDPSRCRGLLESELKVMEEFVKQYKSEALGVGEVALPGQGGLPKEEGKQQEKPEGAETAAPTANGSLGDPSKEYVCELCKGVAPADSPVVYSDRAGYSKQWHPACFVCAKCSEPLVDLIYFWKDGAPWCGRHYCESLRPRCSGCDEIIFSEDYQR... | Function: Transcriptional cofactor that restricts GATA6 function by inhibiting DNA-binding, resulting in repression of GATA6 transcriptional activation of downstream target genes. Represses GATA6-mediated trans activation of lung- and cardiac tissue-specific promoters. Inhibits DNA-binding by GATA4 and GATA1 to the cTN... |
O51253 | MKTRCFCLAAFSGILTTLAIPNEIKETGYSILGFVAYVPLFIALNKLEDKKALMGLTVFYFIIANSLQNFWLGFFHAFGWITFIGVIIGYIPYSLTLGYFLYYSLKSFKNKTMSITMLFTFYDYSRSIGFLAYPWGLAAFTVNNFNNLIQIADIFGVFFVSFAVYFLNSGIADFLIHKNKTNLLNIAFPTLLITASFTYGMIKKIELKNLLAKEIDSLNIAAIQLNTDPWLPGNDKKGIRDSIEITEQALKENPKIEFVIWSEGVLTYPFSKEDQHFKSSDLHNELKNFIKEHKIPFAIGAPSNLDKAIGIQQNSIYMVE... | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn... |
P61034 | MSPAGKGPAWRQPAILAAAGAAHALSFAPDPLPAWSLAPVQVIALAVAAHASLQAPSARRALARGWLFAMFSFSLGLYWMYVSMHDYGGLAAPLAAAGVLALSAFLALFPGLACAAARWLCPPHWDASPPARARRTLYTAATWAACWAALEWLRAVVLTGFPWLNISYAHVDSPLAGWAPLLGVHGMALLAAFAAAALAGLWQSASGRIDSRQALAAGVALLLAGAGWLLGQFSWSRPEGKPLHLRLVQGNVEQSQKFDPALLETGLRRHLELASLPPRPGEPKPDMIILPETVLPVFQDQLPASVWDAWIEVARRADTR... | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn... |
Q89WA1 | MSAFQRLRQIALAIILTWGWKRALVAITAGALSVLALAPFNLFPVLFITFPVLVWLIDGAGAGRYRGIPAAALTGYWFGLGYFVPGLYWIGYAFFVDADVFAWLTPFAVLGLPAYLSIFTAIGFALARLLWTKNATRVLALAASLTIAEWLRGHALTGFPWNAFGYALSEPLPLAQTASLIGLWGMTFLTVAIFASPATLIDRTPDRRVAWRAPAAAVALLIAMSIFGAIRLSLHPTTMVAGAKLRLMQPNLQQDAKFNYAAKTEVMKKYLALSDRASGPQSTGVRDATILIWPESAFPFFLTREADAMAEIAELLPKGT... | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn... |
Q8YEA6 | MIARLAGRIILLNGWRRALAAFLSGAFATLTQPPFDIFVAGFVSFPVLVWLIDGAIARTDAGPLRRLLLAAKVGWWFGFGYFVSGLWWIGTALLVDADQFAWALPLAVLGLPAFLALFYAFAAMIARLLWSDGLGRILAFAFGFALAEWLRTFIFTGFPWNLIGYAAMPVPLLMQSVAVIGLVGMSALAVFVFAAPALLTGGHFARTGIGLAIFLALAHVGFGAWTLSRAPAIVDENGPLAVRIVQPSIAQAMKWDNAERRAIFDKLVGLTEEAPAEGKPRPDVIVWPETAIPYILESTPQALAHIGDALQEGQVLLAGA... | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn... |
Q9PNJ9 | MKLKLNFLPYFSFIPKKLNTNSIIFKIIKVFFIAILLSNSIYLSFFENIFTQTISPFLAIWGLVLLLKSKTSKQYFWIGFFVGILWFWWIGLSSIYFNLNYLVPIIPIIIGFIYGLLFRLCYLLKFDFLRLCGIFCISFIHPLGFDWFNWGIFTVYGFFDPSYRGIICIFLIAYFIYEGYISRYYKIAIVLILFFSGFQYNEKQAQTLNLNYKLINTNISQDQKFLQENLKSNSDILIQDILQAINEKKELVILPETAFAFDLKNTKYELMLKELSYKITIITGAFHVEKEHTYNSTYIFKKGNVYILNKHFLVPFGEEI... | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn... |
Q9AC16 | MIAWTRFRERPWSGPALALIAGLAAALAHPPFGVLPGLLGYAGLLHLLDNADVQRPLRSVFWRGWLAGVGYFGLGTWWVGEAFLVDAATHGWMAPFAVTGMAAGLALFWGLAALLYRALRPASAWRVLTFAGAFAALEWMRGHVLTGFPWNLPGETWKAGSAPSQLAALVGAYGLTWITLAIAGAPAVWRQGRGGRAATGLAVASLIGLYGYGAIALSRPLSPSGPTTVRIVQADIKQDLKWDAERFAQIVQAYVSLTATPYAAKPADIVIWPEGALPAAVNDYLAPGTWVRQAIVDSLAPGQLLLIGGYRYEGAGPHPT... | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn... |
Q8KCC4 | MNGAYRGALSRLLSKPFFLPLLSGLLLGISFPTWPAVHLEPLAWIALVPLLLSLEHEERFGPFFRKSWMSMLLFCLIALWWVCLATFVGGILTVFVQSLFSVVPLVVFYYFKKRAGFRSALLALPFIWTGWEWAYMQQDFSLGWLTFGNSQANLLWMVQYADVTGVWGVSFWLLTFNVLVLLLFMEKESFQVKVGIVMVMLVMIATPLLYARQVFRNTALDNTSPKVRVALVQPDIDPHEKWDGLGPEETLSRLYSLTGQSVRGERLELIIWPETAIPFYIRLPENKPYMDSVRRMVMRWNTPLLTGFPDEVPVFPNSAR... | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn... |
O84539 | MFKLVSYIILSWVLVCLAQPDVSVVASVVSCICGYSLLWAGLFALVEQLSWKKVWCIAFIWTWTVEGAHFSWMLEDLYVGTSIYFVWGILLSYLATLFASFSCLVVWCCRKQYRGALVWLPGVWVAIEAIRYYGLLSGVSFDFIGWPLTATAYGRQFGSFFGWAGQSFLVIAANICCFAVCLLKHSFSKGLWLTLCAFPYLLGGAHYEYLKKHFSDSEVLRVAIVQPGYSPHMHAGRTASAIWRGLVSLCQTIQTPVDVIVFPEVSVPFGLHRQAYTLHENQPVLESLLPNKSWGEFFTNLDWIQAIAERYQCTVIMGME... | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn... |
Q7NQI3 | MLNAAGGAGCDPSSPTATSPMRILILLLAAALAGAFTLFAFAPYRLFWLMPLCLAALVELLQREPRRAFWLGYAWGLGAYVSNFRWIYDSLHDVAGLPAWIAAPLVLLLPAYLALYPGLASWLACRIDPRPGVRWLLAFPAAWELGEWLRGWVMTGFPWGAAGYSQITESPLAGYAPLGGIHLVNYLVALSAAALAMLARAGMRQRIGILIAAALAWGSGVWLRDIEWTTPAGKPITVALAQGNIAQELKWSPENLENSLLTYYRQVAMTRADLMILPETALPLFLDDLPSGYLSMMRGEASRAGMALASGIPRRTDDGR... | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn... |
Q820B4 | MNSVLALIAGAILPLAFAPFNWFPIAFVSPAILLAVWLRSRPLVAWWRGWLFGFGFFGAGASWVYVSIHHFGNANVPLAVLITVLFVFVLALFIAFQGLSFSLFFRKRKAALTALFAFPAWWVVWEWLRSILFTGFPWLFLGYSQINSPLKGFGPLFGIYGISLIVAFISGCIYLLVTSKKLNKKIMCLILIILPFIVGWVLTFIPWTRPGSESVRVGLVQGNIGQRLKWDPDTLYSTLHTYYSETQKNWDHGIIVWPEAAIPIYPQQVSVFLQALDKEAKQHNTALMTGIPIYHEKTNKVFNGLMVLGDGHGLYLKRHL... | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn... |
P23930 | MAFASLIERQRIRLLLALLFGACGTLAFSPYDVWPAAIISLMGLQALTFNRRPLQSAAIGFCWGFGLFGSGINWVYVSIATFGGMPGPVNIFLVVLLAAYLSLYTGLFAGVLSRLWPKTTWLRVAIAAPALWQVTEFLRGWVLTGFPWLQFGYSQIDGPLKGLAPIMGVEAINFLLMMVSGLLALALVKRNWRPLVVAVVLFALPFPLRYIQWFTPQPEKTIQVSMVQGDIPQSLKWDEGQLLNTLKIYYNATAPLMGKSSLIIWPESAITDLEINQQPFLKALDGELRDKGSSLVTGIVDARLNKQNRYDTYNTIITLG... | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation . Utilizes a two-step reaction via a ping-pong mechanism . Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermedi... |
Q5ZC82 | MAMEAAAERSAGAGAAATAAPESGGGGAGERRSRFRRICVYCGSAKGRKASYQDAAVELGKELVERGIDLVYGGGSIGLMGLVSHAVHDGGRHVIGVIPKSLMPREVTGEPVGEVRAVSGMHERKAEMARFADAFIALPGGYGTLEELLEVITWAQLGIHKKPVGLLNVDGFYDPFLSFIDMAVSEGFIAEDARRIIISAPTARELVLKLEEYVPEYEVGLVWDDQMPHSFAPDLETRITSS | Function: Cytokinin-activating enzyme working in the direct activation pathway. Controls the shoot meristem activity. Phosphoribohydrolase that converts inactive cytokinin nucleotides to the biologically active free-base forms. Reacts specifically with cytokinin nucleoside 5'-monophosphates, but not with di- or triphos... |
Q9LDF2 | MGLFESVKSIDWEQESFPTYQDLGFLPLFAVFFPTIRFLLDRFVFEKLASLVIYGRMSTNKSDNIKDRKKNSPKVRKFKESAWKCIYYLSAELLALSVTYNEPWFSNTLYFWIGPGDQIWPDQPMKMKLKFLYMFAAGFYTYSIFALVFWETRRSDFGVSMGHHITTLVLIVLSYICRLTRAGSVILALHDASDVFLEIGKMSKYCGAESLASISFVLFALSWVVLRLIYYPFWILWSTSYQIIMTVDKEKHPNGPILYYMFNTLLYFLLVLHIFWWVLIYRMLVKQVQDRGKLSEDVRSDSESDDEHED | Function: Essential for plant growth, promotes cell division in root meristems . Catalyzes the biosynthesis of ceramide sphingolipids with C(16) to C(28) fatty acids, structural membrane lipids involved in membrane trafficking (e.g. early endosomes) and cell polarity (e.g. polar auxin transport related proteins); mostl... |
P47055 | MRFQLFIYFYFTIVVIAGTNTIQQFSDAGDRLITSLRNLDNNGTYETLTAEKVPIIEGQIQNISAKYEQHTFILKGLEAVLNYKVKSLDNNERESLEIEYEKVEKALDAALNVSPFEYIKKFKEVSRGKVVNALENLSREQNRITINGGREDEKEKEAREKKKRLDRIKRILTVSLLELGLAQGVADLCAVAPFACLLGVTVGSIGFIFWLALIYNAIQ | Function: Involved in spore wall assembly . May be involved in maintaining genome integrity .
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24843
Sequence Length: 219
Subcellular Location: Membrane
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Q9LJK3 | MESVSSRGGDPVVKPSMEVWHFQIAVYFAFGFFFLRLVLDRYVFQRIALWLLSTGSAPIKLNDAATRAKIVKCKESLWKLLYYAACDFFVLQVIYHEPWARDIKLYFHGWPNQELKLSIKLYYMCQCGFYVYGVAALLAWETRRKDFAVMMSHHVITIILLSYSYLTSFFRIGAIILALHDASDVFMETAKIFKYSEKEFGASVCFALFAVSWLLLRLIYFPFWIIRATSIELLDYLDMTSAEGTLMYYSFNTMLLMLLVFHIYWWYLICAMIVRLLKNRGKVGEDIRSDSEDDDD | Function: Prevents cell division in root meristems and promotes salicylic acid (SA) production and hypersensitive response (HR) . Catalyzes the biosynthesis of ceramide sphingolipids with C(16) fatty acids, structural membrane lipids involved in membrane trafficking (e.g. early endosomes) and cell polarity (e.g. polar ... |
Q6NQI8 | MGLLESVKSINWEHESSPVYQDFRVLPLFAVFFPSIRFLLDRFVFEKLAKYLIYGKHRQDMGDDTTERKKKIRKFKESAWKCVYYLSAEILALSVTYNEPWFMNTKYFWVGPGDQTWPDQQTKLKLKLLYMFVAGFYTYSIFALVFWETRRSDFGVSMGHHIATLILIVLSYVCSFSRVGSVVLALHDASDVFLEVGKMSKYSGAERIASFSFILFVLSWIILRLIYYPFWILWSTSYEVVLELDKDKHPIEGPIYYYMFNTLLYCLLVLHIYWWVLMYRMLVKQIQDRGKLSEDVRSDSEGEDEHED | Function: Essential for plant growth, promotes cell division in root meristems . Catalyzes the biosynthesis of ceramide sphingolipids with C(16) to C(28) fatty acids, structural membrane lipids involved in membrane trafficking (e.g. early endosomes) and cell polarity (e.g. polar auxin transport related proteins); activ... |
P25894 | MKIRALLVAMSVATVLTGCQNMDSNGLLSSGAEAFQAYSLSDAQVKTLSDQACQEMDSKATIAPANSEYAKRLTTIANALGNNINGQPVNYKVYMAKDVNAFAMANGCIRVYSGLMDMMTDNEVEAVIGHEMGHVALGHVKKGMQVALGTNAVRVAAASAGGIVGSLSQSQLGNLGEKLVNSQFSQRQEAEADDYSYDLLRQRGISPAGLATSFEKLAKLEEGRQSSMFDDHPASAERAQHIRDRMSADGIK | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease that cleaves substrates preferentially between Phe-Phe residues. Plays a role in response to some stress conditions. Seems to regulate the expression of speB.
PTM: The intramolecular disulfide bond improves the stability and the activity of LoiP. It form... |
O61267 | MARDTQGTQGTQSQASNIWTQVESQPMEKIVWGRLYGKNIKIKSLGTSSKYRIIYTHSSFSVDLNNDEFTAGRGEANDLILTLNDLPEKILTRISKVHFIIKRANCELTNPVYIQDLSRNGTFVNNEKIGTNRMRILKNDDVISLSHPTYKAFVFKDLSPNESIGLPEEINKTYYVNRKLGSGAYGLVRLVYDTRTCQQFAMKIVKKNMLSGARPSTNFSDPDRVLNEAKIMKNLSHPCVVRMHDIVDKPDSVYMVLEFMRGGDLLNRIISNKLLSEDISKLYFYQMCHAVKYLHDRGITHRDLKPDNVLLETNDEETLL... | Function: May have a role in germline establishment.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 54261
Sequence Length: 476
Subcellular Location: Nucleus speckle
EC: 2.7.11.1
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F1QQC3 | MAVSSALCIFSLLVLAQAQSELQQPKIELRLAGDKRKHYEGRLEVFYNNEWGTVCDDDFSIEAAHVACRQLGFLGAVAWSPSAKFGQGEGRIWLDNVHCTGRENSLAACPSNGFGVSDCRHSEDVGVICNQKRIPGHRFINIMNNNVETLEERVEEIRIRPISSHLKRIPITEGYVEVKERGKWRQICDEEWTPLNSRVACGMYGFPGEKNYNNKVYRSLSMRKKKNYWGFSVNCTGNEAHVSSCRLGKALEPKRNGTCGRGLPVVVSCVPGRAFAPSSSIGFRKAYRPEQPLVRLRGGANVGEGRVEVLKNGVWGTVCD... | Cofactor: Contains 1 lysine tyrosylquinone.
Function: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine) (By similarity). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' o... |
Q6N999 | MADVLKLDGIRKSYNVGTPVETEVLHGIDLTMQRGDFLALMGPSGSGKSTLLNIIGLLDRPTGGRLLINGEDTGQLSDSALTHLRGHAIGFVFQYHYLISAFTARENVMMPMLVDRGRPDAAMEKRADELLDRVGLSRWRNNSATNMSGGQQQRVAVARALAMDPDLVLADEPTGNLDTKSANDVFELMRQINRERGTTFLLVTHNDDLAERCDRIVRVVDGKIAG | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane ... |
Q2RU16 | MPQAALRLDKVTRSFSQGREVLNVLTGADLAVNPGEIVALVGPSGAGKSTLLQICGLLEKPTAGEVRIGGISCGQLSEDRRTLLRRDHLGFVYQYHHLLPEFSAAENIVVPQMIAGIGRKPALARAAELLAKMGLSERQDHRPGQLSGGEQQRVAICRALANRPKLLLADEPTGNLDPNTAERVFQALLDLVRGEGLAALIATHNPDLARRMDRIVTLREGKVVAA | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane ... |
Q8KCE8 | MQLQVARHRPGTGEDRLMLEARKLVKSYALPGQPPLKILDGIDLSVAPGEMVTVIGASGSGKTTLLNLLGTLDTPDEGELIFDGSPVFQGSRCLLSKKELAAFRNRKIGFVFQFHHLLSDFTALENVAMAEFIGTGKLKPAKERAAVLLEKLGLKARLDHLPSELSGGEQQRVAIARALMNKPKLVLADEPSGNLDSRNSRMLYELMASLSKERQTSFVIVTHNEEFAATADRCLHMQDGRLQACGG | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane ... |
Q7UPK3 | MHSSPELLLEARGIRKSYHKDKIELPILRGIDVGFVTGEMSALVGRSGSGKSTLMHLLATLDQPDSGEVWFDGTRIDNQSRARRDQYRNSQIGIIFQFYHLLPELSAIENVLAPAMIRRSVLGYLRDRKSLRLRAEAMLDRVGLLTRSHHQPSEMSGGEMQRVAIARSLMSNPKLLLADEPTGNLDTETGATILSLLRELNREDELTIVMITHDDSIAETADRCYRMCDGLLEDNASNLAGGDRSDSAKLETVAA | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane ... |
Q9EYM2 | MSKIVLEAKDVYKHFTDGKSTVEVIKGLSLKIAAGEFVSIVGASGSGKSTLLHILGGLDQPTQGQVFLNEQRFDNLGEAERGFKRNQYLGFVYQFHHLLPEFSALENVAMPLMLRADTNYKEVKQQAEHLLDRVGLSHRLTHKPGELSGGERQRVALARALVARPAVMLADEPTGNLDRKTAFGIFELLSDLKQEFNMAMLIVTHDEQLAQSADSILHMQDGLWVDHS | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane ... |
Q8UFV7 | MAKKTVLRLTGVERTYGQGETSLSILRKADFELKSGEMVALVAPSGTGKSTLLHLAGLLEHPDAGEVLINGAPCNGLPDEARTAIRRSDIGFVYQFHHLLPEFTAVENVMMPQLIAGLTQAEARKRASALLDYMRVGHRGEHRPAELSGGEQQRVAIARAVANAPLLLLADEPTGNLDPETAHYVFDALEALVRQSGLAALIATHNHDLANRMDRRVTLADGKIVDF | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane ... |
F8DT93 | MNSPLSYNNVIEVTDLQRAFKQGEHEIQILRGIDLIVRRGEILALLGPSGAGKSTFLQAIGLLENGFTGSINILGQEIGSLNDKERTAIRRDHLGFVYQFHHLLPDFSALENVMLPQLIQGKSSHQAKEHAHFLLNSLKLEERLKHYPSQLSGGEQQRVAVARALANRPALVLADEPTGNLDEATGDIVLHEFLRLVRRQGSAAIIATHNMAMARKMDRIVTLHDGRLIEEY | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane ... |
Q5MNH9 | MTAASSPHPGVSAEDIEFYQANGYLRLPQEAHGLFDDLAKLQAWVAEISQWGLETGKWRHYYETTNGKHLLWGTEKLMEYHAPMRDLIAGEAPLTLLKSLTGKDMVVFKDEIGWKLPGGKGAVPHLDRPAYSMFAPEFIEIMIAVDAHTVENGCLQFVPGSHKEAVPISADGRIASAWLEGKEFIPMVLDPGDVLIFNESMAHRLDPNKTDQRRAAVFGTYHFDRSQPDLRDKFYAHRLIHSPPENAWVETVEAQT | Function: Dioxygenase; part of the gene cluster that mediates the biosynthesis of loline alkaloids, potent insecticidal agents composed of a pyrrolizidine ring system and an uncommon ether bridge linking carbons 2 and 7 . Lolines are structurally differentiated by the various modifications of the L-amino group and incl... |
P75958 | MAMPLSLLIGLRFSRGRRRGGMVSLISVISTIGIALGVAVLIVGLSAMNGFERELNNRILAVVPHGEIEAVDQPWTNWQEALDHVQKVPGIAAAAPYINFTGLVESGANLRAIQVKGVNPQQEQRLSALPSFVQGDAWRNFKAGEQQIIIGKGVADALKVKQGDWVSIMIPNSNPEHKLMQPKRVRLHVAGILQLSGQLDHSFAMIPLADAQQYLDMGSSVSGIALKMTDVFNANKLVRDAGEVTNSYVYIKSWIGTYGYMYRDIQMIRAIMYLAMVLVIGVACFNIVSTLVMAVKDKSGDIAVLRTLGAKDGLIRAIFV... | Function: Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA.
Location Topology: Multi-pass membrane... |
P44250 | MNTPFFISWRYQRGKQKNPLVALIAKFSAIGIALGVAVLIVGLSAMNGFERELNQRILAVVPHAEILSAPNATEPTIHHWQNLEKRLQQNPQIKGISPFVSFTALVENGSKLKVVQVKGVEKQAEDKVSSIGNFVQEQGWNKFEKEGGLVLGSGIAKELDVKVGDWITLLISQQNGDEQFAQPTREPVQVTSILRLDGQLDYSYALLPLAQAQTFLTYQPDQITGVELKLDDPFSARNLDLSMLNDYPQMLYMQNWISKFGYMYRDIQLIRTVMYIAMVLVIGVACFNIVSTLIMAVKDKQGDIAIMRTLGANNAFIKRI... | Function: Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA (By similarity).
Location Topology: Mul... |
Q5MNH1 | MTLTNLDAIVVGAGFSGILAVYRLRKLGFRVQGFERQERLGGVWRENAYPGAAVDSLFPFYQFYDAELLQDWEWGEQFPTRAEMLRYFDHVDKRWEISASFEFGVSVSAARYSETTQRWTVTLEDGRRAEARWFIPAVGFSSVLNIPRIPGMSRFRGAIYHTAKWPHDAVSMRGKRVAVIGTGPSGVQIIQSVGKIAKAMTIFQQSPCLTLRKYGSPNQTATALCMRPDDHREALRLGLQTSNGFGYVPRDQDTLDVPIEERNHFYQQRYLAGGWAFWMAGFRDLCQNIQANRDAYDFWARRTRARIGDVTKRELLVPQI... | Cofactor: Binds 1 FAD per subunit.
Function: FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of loline alkaloids, potent insecticidal agents composed of a pyrrolizidine ring system and an uncommon ether bridge linking carbons 2 and 7 . Lolines are structurally differentiated by the va... |
Q5MNH6 | MTVTNKPVEPANVPVMDFEAIHASVGNERKEYLRQLDEAWSHHGAVYVINHSIGTETLEEAFVWCKKFFDLPLAVKNSVHIPPDVSKHFQGWTGTGEAISSQGVWDPDEIERLRKEMPTELKEAMELQDPCGTYPPGNPDLNLVEQHLPGYLDFLKKWFAACYKQSLQNMRLVCEILGMEDLDYIGKKFEPRHMSTHSTWNYFLGQPVSQLASGSSNRLNAHTDYCQFTMLFQDMVGGLELHDYEEDIYRPVPPIKGAMIVQVGDLLEKQTNGRWRSALHRVTAPSRYMYGGSPGGDDELVQRYSLVFFGHLNLDEMIKP... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of loline alkaloids, potent insecticidal agents composed of a pyrrolizidine ring system and an uncommon ether bridge linking carbons 2 and 7 . Lolines are structurally differ... |
Q5MNI1 | MDLTQFNTAGIVWPTVAAIAISYILLSSFLSWYRLRHIPGPFLASISSLWNVLNIVTGRTSPVLEKLPGKYGPLVRTGPNYVLTDDAEILRHVNGARSTYPRNGWYEGFKVDEHDHMGSHIDTSVHDAIKSKVIGGYNGKDGIDLEGAIGSQVKTLVSEIRRRHLGQPVDFSRLMRQMALDAITAVAFGEALGFLTAEDGDVFGYVSAVDKMLTYLTLASDLPVVRSVVRSRRMAPAVRCVLAYTGIGRMLNHTRRVVAERYAADDPGKGDMTASFIRKGLTQIECEGESHLQLIAGADTAVTVLRSTLLYIMTTPRVYT... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of loline alkaloids, potent insecticidal agents composed of a pyrrolizidine ring system and an uncommon ether bridge linking carbons 2 and 7 . Lolines are structurally differentiated by the various modifications of the L-am... |
Q4G3R0 | MDLTQFNTAGIVWLTVAAIAISYILQSSFLSWYRLRHIPGPFLASISSLWNVLNIVTGRTSPVLEKLPGRYGPLVRTGPNYVLTDDAEILRHVNGVRSTYPRNGWYEGFRVDEYDHMGSHIDTSVHDAIKSKVIGGYNGKDGIDLEGAIGSQVKTLVSEIRRTRGSRPRSRPRWMPARWSRSSP | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of loline alkaloids, potent insecticidal agents composed of a pyrrolizidine ring system and an uncommon ether bridge linking carbons 2 and 7 . Lolines are structurally differentiated by the various modifications of the L-am... |
Q5MNH3 | MTVNSKRIPFGKPMLEAFCMDPEYTNLNSSSCGSWPKVVSKQIRDYWSLLEAQPDLFSEFYQGLVLQEARLGLARLVHAAVSECVLVSNVTTGIFTVLYNQEFEERDVVVTLSTTYGAIDHGITSLAETRSFKTRRVEFELPTTGEKIVSQFETTIAQIRAKGLRPRLAILETIVSIPAVRMPFEDLLRVCQKECIMTLVDGAHSVGQFEVNLQELHPDFFVSDCHKWLFVPRPCAFLYVAERNQHMMRSAIPTSFGFIPKNGNSQLPLWSQMVSANGTASSFETLFAYTATSDNMPHLCIPTALRFRRDVCGGEAAIYE... | Function: L-cysteine desulfhydrase-like protein; part of the gene cluster that mediates the biosynthesis of loline alkaloids, potent insecticidal agents composed of a pyrrolizidine ring system and an uncommon ether bridge linking carbons 2 and 7 . Lolines are structurally differentiated by the various modifications of ... |
P37945 | MAEELKRSIPLLPLRGLLVYPTMVLHLDVGRDKSVQALEQAMMHDHMIFLATQQDISIDEPGEDEIFTVGTYTKIKQMLKLPNGTIRVLVEGLKRAHIVKYNEHEDYTSVDIQLIHEDDSKDTEDEALMRTLLDHFDQYIKISKKISAETYAAVTDIEEPGRMADIVASHLPLKLKDKQDILETADVKDRLNKVIDFINNEKEVLEIEKKIGQRVKRSMERTQKEYYLREQMKAIQKELGDKEGKTGEVQTLTEKIEEAGMPDHVKETALKELNRYEKIPSSSAESSVIRNYIDWLVALPWTDETDDKLDLKEAGRLLDE... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
Q6ML73 | MSYVSGYVPVIPLKNSVLFPDISMPLRIGREKSIAALQKALRDNHWVILLTQKNPNASVDKIEDLYQVGTLAKVESFRMEEDGSYNIFVKAHQRVRLIHSRDSEGHIEAQTEALEDSGRLDKKTEEALLSSLRQLSDDLLDLLPGNTRQIREMIAEIEDLQTLVNMCAAYADINISDKQEILEIPLLKDRALKLLDRLQELKERLKIQRGIRDKLQESFQQNQKESILREQMRVIREELGDHEGEDLFAKFKDKIDKAGMPPEALELAKNQLRRLETSNSASPEYQMIRTHLELMTSLPWNQSSAQQDIDLEAAERVLNE... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
P47481 | MPVTKKSQILVVRGQVIFPFVPFSLDVGRPRSRKIIKALKTLKTKRLVLVTQKFTGEQNPEFNDIYHVGTLCEIDEIVDVPGVDSKTVDYRIKGRGLQRVLIEKFSDADINEVSYQLLNSTVKDEANVDRFLQRIFPEKEEIEQLMEGAEKFLELENISKTVNVPKGLKQLDIITFKLANLVPNTESIKQAILEENEIANRLEKIIQAGIEDLQKIQDYGRSKNKETEFDKLDSKITRKINEQLSRQQRDFYLREKLRIIREEIGISSKKEDEVASIRKKLDENPYPEAIKKRILSELEHYENSSSSSQESTLTKTYIDT... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
Q6MTF4 | MLQYLKKIKGVSFMKTIKLPVVVTRGIFILPSTSKTIEFGRVKSKNALDASADLYNNQIVVVSQESPLEEEPNLEHLFYLGTVADLSVKKVWKDGTISVELNYNQKIKIDEFVEEDNIIYAIGSVFEDKLPKTDAQKTKIKEALEELQEKHSFNTSELLLVFNENDFNKLNSLIYQIIDKMPLVSLNTKLLLIQSTSILEKLELLKELIINRPKSTIKLNNNLNNNSTVDSEINKKLKDKMDKQQKEYYLREKMRIIKEELDDENSDASQLDKYKKRLEEEPFPESVKEKILSSIKRIETMQPGSAEVNVERNYVDWMMS... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
Q4A696 | MQKKQTLNYVIVKTDEISFPFGYSEVLILEQDSIELLETTKFKFKNEDRLVIVYAEDVYTEEVKFLQRGLYIKPLDAKEVMYQGEKALILTFKALHFFDIQNFSYEMNQDEIMSANFLVDGNAKGTVGYEMVLSGHINNVEDVKENLMNEFRQDQNKMNFFSIFETLVNNSNSFGISTNNQAGTAMLFKQNYGAKDEVKPYDIEEIKALIDSKITQDNDPSEFLLNNFESLMTYFGFLDLNKFPHKWHLYNSFDYGNFTRLINEVGNFIQTALKLEENITSEISKKLNNQQKEFMLREKRKVIDDELAKLGKDTLQDDKD... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
O31147 | MAEAKTVPVLFLNDSIVLPGMVVPIELDDAARAAVDAARASESGELLIAPRLEDRYPAYGVLASIVQIGRLPNGDAAAVVRGERRAHIGSGTSGPGAALWVQVEEVTDPEPTDETKKLAGEYKKLLLAMLQRRDAWQIVDMVNKITDPSALADTAGYASYLTGTQKRELLETTDVDRRLSLLIGWTGDHLAETEVNDKIAEDVRTGMEKQQKEFLLRQQLAAIRKELGELDDNGDGSSDDYRARIEQADLPEKVREAALREVGKLERASDQSPEGGWIRTWLDTVLDLPWNVRTEDSTDLARAREILDTDHHGLSDVKDR... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
Q2GE60 | MSEEELNNRDTESKQEHDENNSNFEAGSAHMNLPVLPLREVIFFPGDYLPIFIGRKGSIQAMDKALAETSENTGRMLLIAQKNPKKEIPEGKDLYEVGVIAKIAEPKINLQDGGVKLMVIVECRARAVNFRKSEGVLEADVLPIEEEESDNVDIEAYRRAVVQNFEKCVKLSETIPDEIIGLLSQIDSTSRIADLVTASINLKLSVKQEILETVDLLERIKKVHALLEKELGVLQVKQQIKEKTESQIKKSHKVYLLNEQLKAITKELYDKEGEEYDELVDLEKKIGNGKLSAEAKEKVSKELKKLKNMVPMSAEATVVR... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
Q3JBB6 | MENNAYPTLPLKNTVLFPHLVLPLSVGRAGSIAAVEAALSSEDKLIAVFPQKDPRTDEPAADDLFRFGTVGIIKKMVRSEDTVQILVQGIERVEQLEMVQKQPYLSLKIATLSEPSDTGTEIEALHRTVIELAGKMIELVQPQIQVGIHHIISDVEKPLHQIYLLTSILSLDFDKEKELLAAATQVEALQLMHRYLNHEVQVLEVRQKITSTAQTEIDKKQREYVLRQQLEAIQEELGETNPEQAEIKELRQRMEETELPELVRKEVEKEITRLERMPSAAPDYQLTRGYVELALELPWNKTTEDRLDLKRAREILDEDH... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
B3CUN9 | MAQVLNDISNRVLPLFPIRNTVLFPGLVLPILIGRDDSVKNLLRLGNDSENQHTILLTTQKNADDIKPSINSLYKIGVLAKITELVQLPNDNYKILIKVLDRVKLTIRRSHDLLVAEYVIVPDDEINNADEIKDKLANAIVLFNKYIRLSKKINPDLLVHVLSYTNQSYVVNALAANLICNVANKQSLLEITDVKQRIERLTDHVAKEIIIMETDELITSKAQKNLEKMQRDCFLNEKMKIIKNVLGVDDEKSDIAELQKKIDTLHLSKEAKAKAESELKKLKMMNPISAEAALTRNYLDILLGLPWKKEKESKININID... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
A6LD45 | MNVYMKEKTRVFCQNSFDDLDDNIGIVMPILTECDVDEDFTEGIEKVGDTIPILPLRNMVLFPGVALPVIIGRPKSMRLIKEAVHKKSLIGVVCQKEMGTEDPILEDLYTTGVIADIVRVLEMPDGSTTVILQGKKRFELNELTETDPYLSGKITVLEDTKPDKTDREFEALISTIKDLTIKMLGAVAEPPRDLIFSIKNNKNVLYVVNFSCSNIPSGSAEKQQLLLIGDLKERAYRLLFILNREYQLVELKASIQMKTHEDINQQQKEYFLQQQIKTIQEELGGNINELEIKELREKASRKKWPAEVAQVFEKELRKLE... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
B2TFQ5 | MSADSENETSESSPAGEATASTSALPDEPLILLPVRNAVLFPGMVLPFTAGRGQVKEDVQAAVKRQQPLGVVLQRDPRVQDPTFDDLNTIGTVANVVRYVTSPEDGAHHLICQGVERFRLIAPVEGLGFRAARVEFLPETTARNPAVDARALVLRQRAGEMIGLLPNAGGELVRALDAIELPGLLADTIAGLLDIPPERKQEILETLDVCKRLDKVLDAVAGRIEVLRLSQEIGEQTRGRIDQRQREMMLREQLRTIQNELGENIESREEVRKLTEAIEAAHMPPEVESHARKELGRLERMPEASSEYSISVSYLEWLTE... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
Q6ME13 | MLEEPIDALETEFENALNSLEDNQLSKINGQLPEQVHVFPLLRRPFFPGMAAPLVIEPGPFYEVLKVVAKSDHKCVGLVLTRSEQAEIYKVGFSDLYQIGVLARVLRIIPMEQGGAQVILNMERRIKIEKPTSETKTLKANVSYIEDDPILTTELKAYAISILSTIKELLKLNPLFKEELQIFLGHSDFTEPGKLADFAVALTTASREELQDVLETFDIRKRIDKALILLKKELDISILQHNINQKIEATINKSQKDFFLREQLKTIKKELGIERDDKSLDREKFEARLKERVVPSDVMKVITEELEKLSVLDMQSAEYS... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
B4RI01 | MNGEQSANGARTLPDDAVVVVPVSNVIFPGVVFPIVLDRPSAVAAAQQALREQHPLVLVLQQDVQAPDPGPQSLHRMGTLANVLRYVTGPDGAPHVACQGVERFEIDEWVEGFPFLVARGRRIPEPEAEGAAIEARFLHLRSQALEALQLLPQSPPGELVAAVEGASSPAALADLVAAYLDLQPPEKQQILETIDLEARLDKVSAFLAQRLEVLRLTSEIAQRTRQSLGERQRETLLREQMAAIQRELGEGEREELVELEAAIENAGMPEEVVQQARKELRRLARTPEAAAEYGMVRTYLEWLVELPWGVPEAAPIDLAE... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
B2RII6 | MIDRKYIRLGEDDEDDGFPVFFPVLSVCEEDEDFKVKEDHMQEEMPILALRNMILFPGVAMPIMVGREKSLKLIRYVEKKGVYFGAVSQRDMDVEEPDRADLYDVGVVAEIIRVLEMPDGTTTAIVQGRQRFALQEITATEPFMKGRVKLLPDILPGKNKDHEFEALVSTIQDMSLKMMELMVERPPRELILSMRRNKNPMYQINFASANISTSIAVKQELLEISKMKDRGYRLLYLLHKELQVMELKASIQMKTREEMDKQQKEYFLQQQIKTIQEELGGNINDIEVQELRTKATTMKWSSEVAETFEKELRKLERLHP... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
A8F811 | MSTKFEKLEKLARESFQSPEVPETLPLIHLRNGMIIFPQTVVPVHVAREKTLLALEQSIESYQQFVFVTSQKDPSVEEPSFDQLYEIGTVSKVLQVVQLPDGSFRVLLEGLERARAYEVVQDNPFLVKLEILKVNYRKTKKLEALIRSVRESFAKYAYYTQRYSQETLSAMSEISDANRLADFVASLLPLQLKQRQSLLEQLKPAKRLEMILEILSHENEILEIERELDTKVKKRIEENQKEFFLREKLKAITEELGEKDTEADQLKARLQKLKLPEHAKQKATLEIERLEKMSPYSAEATVIRTYLDWLFNLPWDNSTE... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
O69177 | MTNKTSPATESATYPVLPLRDIVVFPHMIVPLFVGREKSIRALEEVMGTDKQIMLVTQINATDDDPEPSAIYKVGTIANVLQLLKLPDGTVKVLVEGRSRAEIERYTPRDDFYEAMAHALPEPDEDPVEIEALSRSVVSEFESYVKLNKKISPEVVGVASQIEDYSKLADTVASHLSIKIVEKQEMLETTSVKMRLEKALGFMEGEISVLQVEKRIRSRVKRQMEKTQREYYLNEQMKAIQKELGDSEDGRDEMAELEERISKTKLSKEAREKADAELKKLRQMSPMSAEATVVRNYLDWLLGLPWGKKSKIKTDLNHAE... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
Q92HZ1 | MHKKSLPLMALRDMVVFPGVIAPIFVGRPKSLQALSHTTISEEDNSKYILVTLQKKFDQENPSTHELYNTAILAKIIQIVKLPNNTAKILIEAVARVKLSNIKGEEAFEANYEIIPDEEIFDVNNMRSLVDNAVQLFSKYAINDKKVNAEIIETINKEISNSTNFIDIINILASHLITSLEAKQHLLEETSPFKRITTVISMLNSNIVNSETEQALQKRVRKQIEKTQRDYYLHEQMKAIQKELDEDKSELADIENKIKSLKLSKEAKEKAEAELKKLRTMNQMSAESGVTRNYLETLLSLPWGKYDNSKIDINQAEKIL... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
Q06327 | MFGELRDLLTGGGNETTTKKVKGTVVLMKKNVLDFNDFNASFLDRLHEFLGNKITLRLVSSDVTDSENGSKGKLGKAAHLEDWITTITSLTAGESAFKVTFDYETDFGYPGAFLIRNSHFSEFLLKSLTLEDVPGHGRVHYICNSWIYPAKHYTTDRVFFSNKTYLPHETPATLLKYREEELVSLRGTGEGELKEWDRVYDYAYYNDLGVPPKNPRPVLGGTQEYPYPRRGRTGRKPTKEDPQTESRLPITSSLDIYVPRDERFGHLKMSDFLAYALKAIAQFIQPALEAVFDDTPKEFDSFEDVLKIYEEGIDLPNQAL... | Cofactor: Binds 1 Fe cation per subunit. Iron is tightly bound.
Function: 9S-lipoxygenase that can use linoleic acid or linolenic acid as substrates. Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to w... |
Q76I22 | MLGGLKDKLTGKNGNKIKGLAVLMSRKLLDPRDFTASLLDNVHEVFGNSITCQLVSATVADQNNEGRGIVGSEANLEQGLTDLPSVSQGESKLTVRFNWEMDKHGVPGAIIIKNHHSTKFFLKTITLHDVPGCDTIVFVANSWIYPVGKYHYNRIFFANNSYLPSQMPEALRPYREDELRYLRGEDRQGPYQEHDRIYRYDVYNDLGEPDRDNPRPVLGGSQKHPYPRRGRTGRIPTKKDPNSESRLSLLEQIYVPSDERFAHLKMSDFAGYSIKAIVQGILPAIRTYVDLTPGEFDSFEDILKLYRGGLKLPSIPALEE... | Cofactor: Binds 1 Fe cation per subunit. Iron is tightly bound.
Function: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. This lipoxygenase introduces molecular oxygen exclusively into the C... |
P08170 | MFSAGHKIKGTVVLMPKNELEVNPDGSAVDNLNAFLGRSVSLQLISATKADAHGKGKVGKDTFLEGINTSLPTLGAGESAFNIHFEWDGSMGIPGAFYIKNYMQVEFFLKSLTLEAISNQGTIRFVCNSWVYNTKLYKSVRIFFANHTYVPSETPAPLVSYREEELKSLRGNGTGERKEYDRIYDYDVYNDLGNPDKSEKLARPVLGGSSTFPYPRRGRTGRGPTVTDPNTEKQGEVFYVPRDENLGHLKSKDALEIGTKSLSQIVQPAFESAFDLKSTPIEFHSFQDVHDLYEGGIKLPRDVISTIIPLPVIKELYRTD... | Cofactor: Binds 1 Fe cation per subunit. Iron is tightly bound.
Function: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. With linoleate as substrate, L-1 shows a preference for carbon 13 as... |
R9WTS6 | MALAKQIMGASLMDQKTSVFGSNLCLNHVLVNKHRLRLRKTRKNGSMVVAAISEDLVKLXRVEKEKPVTFKVRAVLTVRNKNKEDFFKDTIFRKIDAITDQIGWNVVIQLFSNDIDPRTRAAKKSNEAVLKDWSKKSNVKTERVNYTADIMVDSDFGIPGAITISNKHQKEFFLETITIEGFACGPVHFPCNSWVQSTKDLPNPRIFFTNQPYLPDETPVGLKSLRYQELKDLRGDGTGVRKLSDRIYDYDVYNDLGNPDRGNDFVRPTLGGEKIPYPRRCRTGRVPSDTDITAESRVEKPFPLYVPRDEQFEESKANAF... | Cofactor: Binds 1 Fe cation per subunit.
Function: Component of the monoterpenoid pyrethrins biosynthesis; pyrethrins are widely used plant-derived pesticide . Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or resp... |
P93184 | MLTATKPLVGGACAAPSSSARRRTFVVPEARRKPGNGRRTSVSKVGSTSTSTTTTTTTTLSADSNGAAVGTVTRPDVHVQDRTHATEMKATVTVHMSKAAGVRDFLYDLILKTWLHVDLVSSELDPQTGQEREPISGAVKHSGRVDDEWDMYEATFKVPASFGPIGAVQVTNYHHSEMLLGDIEVFPTGQEESAVTFHCKSWIDPSHCTPDKRVFFPAHSYLPSQTPKGVEGLRKRELEILRGTGCGERKEHDRIYDYDVYNDLGNPDDDNNPTTRPVLGGKEHPYPRRCRTGRPRSKKDPFSEERSHKEHIYVPRDEAF... | Cofactor: Binds 1 Fe cation per subunit. Iron is tightly bound.
Function: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. This enzyme is possibly involved in jasmonic acid synthesis. It exhi... |
O24370 | MLKPQLQQSSQSTKALIPSWNTNPLFLASFPINILNKNFRLKKKNNFRVHHNYNGASTTKAVLSSTEKATGVKAVVTVQKQVNLNLSRGLDDIGDLLGKSLLLWIVAAELDHKTGIEKPGIRAYAHRGRDVDGDTHYEADFVIPQDFGEVGAILIENEHHKEMYVKNIVIDGFVHGKVEITCNSWVHSKFDNPDKRIFFTNKSYLPSQTPSGVSRLREEELVTLRGDGIGERKVFERIYDYDVYNDLGEADSNNDDAKRPVLGGKELPYPRRCKTGRPRSKKDPLSETRSTFVYVPRDEAFSEVKSVAFSGNTVYSVLHA... | Cofactor: Binds 1 Fe cation per subunit.
Function: Plant lipoxygenase involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence. May not be involved in the bulk production of jasmonate upon wounding. Catalyzes the hydroperoxidation of lipids containing... |
P38418 | MYCRESLSSLQTLNVAKSLSSLFPKQSALINPISAGRRNNLPRPNLRRRCKVTASRANIEQEGNTVKEPIQNIKVKGYITAQEEFLEGITWSRGLDDIADIRGRSLLVELISAKTDQRITVEDYAQRVWAEAPDEKYECEFEMPEDFGPVGAIKIQNQYHRQLFLKGVELKLPGGSITFTCESWVAPKSVDPTKRIFFSDKSYLPSQTPEPLKKYRKEELETLQGKNREEVGEFTKFERIYDYDVYNDVGDPDNDPELARPVIGGLTHPYPRRCKTGRKPCETDPSSEQRYGGEFYVPRDEEFSTAKGTSFTGKAVLAAL... | Cofactor: Binds 1 Fe cation per subunit. Iron is tightly bound.
Function: 13S-lipoxygenase that can use linolenic acid as substrates. Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyz... |
P29250 | MLGGIIGGLTGNKNARLKGSLVLMRKNALDINDFGATVIDGISEFLGRGVTCQLVSSSLVDPNNGNRGRVGTEASLEQWLTSLPSLTTGESKFGVTFEWEVEKMGIPGAIIVKNNHAAEFFLKTITLDNVPGHGAVVFVANSWIYPASKYRYNRVFFSNDTSLPSKMPAALKPYRDDELRNLRGDDQQGPYQEHDRVYRYDVYNDLGEPDSGNPRPVLGGSPDRPYPRRGRTGRKPTKTDPTAESRLSLLENIYVPRDERFGHLKMADFLGYSIKALVDGIVPAIRTYVDLTPGEFDSFKDILKLYEGGLKLPSIPALEE... | Cofactor: Binds 1 Fe cation per subunit. Iron is tightly bound.
Function: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-p... |
Q20800 | MRIPCLLRPLLGWFFGLCILFSALFGNYIITLFLGLPILGRHKQWRNLMDRAISYWMTIPMGLLEFLMGVRIRVSGDEIEFGSPAMIVMNHRTRLDWMYMWCALYQINPWLITSNKISLKAQLKKLPGAGFGMAAAQFVFLERNAEVDKRSFDDAIDYFKNIDKKYQILLFPEGTDKSEWTTLKSREFAKKNGLRHLDYVLYPRTTGFLHLLNKMREQEYVEYIYDITIAYPYNIVQSEIDLVLKGASPREVHFHIRKIPISQVPLNEQDASRWLTDRWTIKEQLLHDFYSEEQPINRQFPVERGDGVWRSWKEPRRHFY... | Function: Acyltransferase required for the fatty acid remodeling of phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or PI). Mediates the conversion of lysophosphatidylinositol (2-acylglycerophosphatidylinositol or LPI) into PI (LPIAT activity). Has preference for saturated and mono-unsaturated fatty acids... |
E0SHN8 | MKKYLGIVLMALVIAGCTSRVPQTEQPATIEPAVPTPSKPQLPPSESQPLPTPPKIQVPVLDWSAAVTPLVGQMVKTDGIARGSILLLNKLKNNTNGSLQTAQATTALYNALASSGQFTMVSREQLGVARQSLGLSEEDSLESRSKAVGLARYVGAQYVLYADASGDVKSPELSMQLMLVQTGEIVWSGNGTVRQQ | Function: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b).
Location Topology: Lipid-anchor
Sequence Mass (Da): 20804
Sequence Length: 196
Subcellular Location: Cell outer membrane
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D0Z8F8 | MIKRMSGIALAALLLSGCQGLLPRGETPSQPPAPTTPAKPSVVPTPTPPVVTPVPQPPKMTSVDWQGSFAPLIDQLLSAPGVEAGSILLVDGVQNKTNGQLSMANASEVLRSALAGNPRFQMVSTAQLAQAKQSLGLAANDSLGSRSKAIGLARQVSAQYVLYTTVSGNVQAPRLAMQLMLVQSGEIIWSGKGPVAL | Function: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b).
Location Topology: Lipid-anchor
Sequence Mass (Da): 20329
Sequence Length: 197
Subcellular Location: Cell outer membrane
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D4I110 | MSWIRIRRSGVLLLALVLSGCINQQQQPQPAAPVEPVTPPVNVPQPPKAEPGQNVPPPPKMQPLNWSATVSPLVGQMLKADGINAGNVLLVDNVKNSTNGSLQSAKATAALLNSLENNGQFSLVTPQQLAAARQTLGLSADDSLVSRSKAIGLARYVGAQYVLYSNAEGDIKSPSLQLQLMLVQTGEIIWSGSGAVVH | Function: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b).
Location Topology: Lipid-anchor
Sequence Mass (Da): 20829
Sequence Length: 198
Subcellular Location: Cell outer membrane
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C4K8P0 | MKKYLLSASIVFLLASCAQPPAKIGRPSKSEPSTVSTDSPEGISSESAEIGIVPLTPKIKSFDWSVPMKPLVENMSQTKDLPNGSVLLVDTVKNNTNGLLQIEKATESLLHILSSNNTFFLISANQLAKAKTALGISKQDNLSSRSKAIALGRYLKAEYVLYTDVSDDIQSPVINMELMLVKTGEIIWADKTAMTLAP | Function: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b).
Location Topology: Lipid-anchor
Sequence Mass (Da): 21397
Sequence Length: 198
Subcellular Location: Cell outer membrane
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Q7N395 | MRRILFVALSVMFLAGCPSLPPEQPEPPTPVVPVTPSEKPTPPSEKVPEPPKMSAIDWESTVQPLVEQLVKAHGLENAKLLLVDTVKNNTNGALQTMQATDALRQAISSEHVFELIPQNQVQNARQSLGLSEEDSLGLRSKAIGLARYLNAEYVLYSIVSGNSDKRDIVMQLMLVKTGEILWSGHGDVK | Function: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b).
Location Topology: Lipid-anchor
Sequence Mass (Da): 20675
Sequence Length: 189
Subcellular Location: Cell outer membrane
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A1JME2 | MKRYLSVALAALVLTGCITQPPVEPTTPPVTIEPVTPPVPETPPPVDNVPPPPKMEQSIDWAASVEPLVAQMVNSNDVANGSILLLDSVKNNTNGRLPTAKATSALHQVLSSNKKFVLISPQQLAVAKQTLGLSEEDSLGSRSKAIGLARYVSAQYVLYSDVSGDVKSPTIEMQLMQAQTGEIIWSGNGPVKR | Function: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b).
Location Topology: Lipid-anchor
Sequence Mass (Da): 20520
Sequence Length: 193
Subcellular Location: Cell outer membrane
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P65319 | MRWIGVLVTALVLSACAANPPANTTSPTAGQSLDCTKPATIVQQLVCHDRQLTSLDHRLSTAYQQALAHRRSAALEAAQSSWTMLRDACAQDTDPRTCVQEAYQTRLVQLAIADPATATPPVLTYRCPTQDGPLTAQFYNQFDPKTAVLNWKGDQVIVFVELSGSGARYGRQGIEYWEHQGEVRLDFHGATFVCRTS | Function: Strongly binds and inhibits lysozyme, may help bacteria survive in lysozyme-producing host cells such as monocyte-derived macrophages.
PTM: Glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 21624
Sequence Length: 197
Subcellular Location: Cell membrane
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O33192 | MTAHTHDGTRTWRTGRQATTLLALLAGVFGGAASCAAPIQADMMGNAFLTALTNAGIAYDQPATTVALGRSVCPMVVAPGGTFESITSRMAEINGMSRDMASTFTIVAIGTYCPAVIAPLMPNRLQA | Function: Overexpression induces expression of sensor protein kdpD gene at low K(+) concentrations (0 and 250 uM, tested in M.smegatis).
PTM: Modified by Lgt on Cys-35 with an S-linked diacylglycerol, signal peptide is removed by LspA, modified by Lnt with amide-linked fatty acid (By similarity).
Location Topology: Sin... |
Q9TLX4 | MTNIHSTAIVHPAASLGRNVVVGPYSIIGSDVSIGDYTRIGPHVVITGKTVIGCNNQILSGCILGSVPQDLRYIDSELTGLYIGNNNLIRENVTVHRASGNGVTYIGNNNLIMVNCHVAHDCQIRNNIIISNSVSLAGHVIIDSCVIIGGHAGLHQFVHVGALSMIAAMSKIEKNVLPFVVVSGMPAITRTINLVGLKRYGISKTDINYIRLMLENLKVQPLAFDTYSIFKKFKSDNLLKRNVAVQYFSDFLFNSFRARGFIPFKVPKK | Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. The target for the lipopolysaccharides produced in the chloroplast could either be the cell envelope of the eukaryote or the plastid membrane.
Catalytic Activ... |
Q8X8X8 | MIDKSAFVHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGEVNQDLKYAGEPTRVEIGDRNRIRESVTIHRGTVQGGGLTKVGSDNLLMINAHIAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMAAVHQFCIIGAHVMVGGCSGVAQDVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETYPEVKAFTDFFARSTRGLIR | Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo-[ACP]
Sequence Mass (... |
B4RVJ5 | MSKPIRIGMVAGEPSGDILAAGMVAELKRQYPDAIIEGIGGPNMIDAGFHSLFDMETLSVMGLVEVLAHLPAILKVKKQLLAHFEQNPPDIFVGVDAPDFNLRVEKALKARGIKTMHYVSPTVWAWREKRIHKIAKAANRVLGLFPFEQQVYDKYHVPYTFVGHTMADAIAIEPDQNAARQELGVESNAYVLAVLPGSRRGEVETLLPVFLETIEAIHVKRSDIQFLIPAANEHRLAQIKAFLQEANNAEERLPIQVTQGTSRDAMIASDVILLASGTATLEAMLCKRPMVAAYLLSPLTYKIMQRLYKAPFFTLPNLLA... | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D... |
O67420 | MKKIFLSLADRSASNYVYEILKEGFEEYEIYGLTDEKLEKIGVKSVARYSEISTVGLIEALPKVFKFLKIYRKILKNLKNTDTLIACDAPALNLRLIKDARKLGVKRIIYFISPQVWAWKPKRAEIIANYCDHVIVILPFEKKIYRKFPNLKVHYVGHPLVDLVKPQKTKEEFMKAFKKEPLPLLLGSREGEIRRHVKLLKGIIEELKKSFDVISPTFREFSKFIERELKVKTLTYEGASYDCFFYSKASLIASGTASLEAGIAGNPHVVYYKVNPITYFLGKRLVKVPYISLVNILLKEEVVPEFIQKSSDEILKGFEK... | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D... |
F4IF99 | MMFQITKSKLRFPLSTFTKRYSSFQAAKSVIDKAAIDGELRVFIVSGEVSGDNIGSRLMSSLKKLSPLPIRFNGVGGSLMCKKGLNSLFPMEDLAVMGVWELLPHLYKFRVKLKETIDAAVKFKPHVVVTVDSKGFSFRLLKELRARYKQQRLENCSVHFHYVAPSFWAWKGGESRLGGLSEFVDHLFCILPNEERVCREHGVEATFVGHPVLEDASEFDLVRRCKPQELKLEGLSFSEHSIPSDSTVISVLPGSRLQEVERMLPIFSKAMKLLKDPFPKLVTLIHVASNNQVDHYIGESFSEWPVPAILVPSGSTQLKY... | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. Lipid A-like molecules in plants may serve as structural componen... |
Q5NZG2 | MATRIAMVAGEASGDLLASHLIRAIRQQVPEAEFYGIGGPKMQAEGFDALWPCERLAVHGYVDALKRYRELSGIRKALLRRVQADRPDAFIGVDAPDFNLWLEGRIRSSGIPAIHFVSPSIWAWRGGRIKGIARSVSHMLCLFPFEPALYEKAGIPVSYVGHPLADVFPLVPDRAAARELLSLPTDCRIVALLPGSRQSEVRSLAATYIETARLLAERHPDIGFVVPLATRETRALFEQALHAADADELPIRLLFGHAVEAMTAADVVLVASGTASLEAALLKRPMVISYRIGKWQYRLMKRMAYLPWVGLPNILCNDSV... | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D... |
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