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stringlengths 6
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stringlengths 11
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stringlengths 108
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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] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 13588
Sequence Length: 120
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
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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] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 27512
Sequence Length: 244
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
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P07098 | MWLLLTMASLISVLGTTHGLFGKLHPGSPEVTMNISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGNTGQRPVVFLQHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGTTIGFIAFSTNPSLAKRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFFDQFLATEVCSREMLNLLCSNALFIICGFDSKNFNTSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWGSPVQNRMHYDQSQPPYYNVTAMNVPIAVWNGGKDLLADPQDVGLLLPKLPNLIYHKEIPFYNHLDFIWAMDAPQEVYNDIVSMISEDKK | 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
Sequence Length: 398
Subcellular Location: Secreted
EC: 3.1.1.3
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Q7D5F9 | MSSYYARRPLQSSGCSNSDSCWDGAPIEITESGPSVAGRLAALASRMTIKPLMTVGSYLSPLPLPLGFVDFACRVWRPGQGTVRTTINLPNATAQLVRAPGVRAADGAGRVVLYLHGGAFVMCGPNSHSRIVNALSGFAESPVLIVDYRLIPKHSLGMALDDCHDAYQWLRARGYRPEQIVLAGDSAGGYLALALAQRLQCDDEKPAAIVAISPLLQLAKGPKQDHPNIGTDAMFPARAFDALAAWVRAAAAKNMVDGRPEDLYEPLDHIESSLPPTLIHVSGSEVLLHDAQLGAGKLAAAGVCAEVRVWPGQAHLFQLATPLVPEATRSLRQIGQFIRDATADSSLSPVHRSRYVAGSPRAASRGAFGQSPI | 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 | MWLLLITSVISTFGGAHGLFGKLGPGNPEANMNISQMITYWGYPCQEYEVVTEDGYILGVYRIPHGKNNSENIGKRPVVYLQHGLIASATNWIANLPNNSLAFMLADAGYDVWLGNSRGNTWSRKNVYYSPDSVEFWAFSFDEMAKYDLPATINFIVQKTGQEKIHYVGHSQGTTIGFIAFSTNPTLAKKIKTFYALAPVATVKYTQSPLKKISFIPTFLFKLMFGKKMFLPHTYFDDFLGTEVCSREVLDLLCSNTLFIFCGFDKKNLNVSRFDVYLGHNPAGTSVQDFLHWAQLVRSGKFQAFNWGSPSQNMLHYNQKTPPEYDVSAMTVPVAVWNGGNDILADPQDVAMLLPKLSNLLFHKEILAYNHLDFIWAMDAPQEVYNEMISMMAED | 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 (Da): 44588
Sequence Length: 395
Subcellular Location: Secreted
EC: 3.1.1.3
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Q1PDW3 | MIIMMNCFPCFTSQKSRNAPCTTNETNDDNVEHDEFRPPVVATTKRTEEREPAEQQPPVKTFNFRELATATKNFRQECLLGEGGFGRVYKGTLQSTGQLVAVKQLDKHGLHGNKEFLAEVLSLAKLEHPNLVKLIGYCADGDQRLLVFEYVSGGSLQDHLYEQKPGQKPMDWITRMKIAFGAAQGLDYLHDKVTPAVIYRDLKASNILLDAEFYPKLCDFGLHNLEPGTGDSLFLSSRVMDTYGYSAPEYTRGDDLTVKSDVYSFGVVLLELITGRRAIDTTKPNDEQNLVAWAQPIFKDPKRYPDMADPLLRKNFSERGLNQAVAITSMCLQEEPTARPLISDVMVALSFLSMSTEDGIPATVPMESFRDKSMSIALSRHGSCSVTPFCISRKDVGNKSSSSSDSEDEEEEKEQKAEKEEESTSKKRQEQEETATDSDDESDSNSEKDQEEEQSQLEKARESSSSSSDSGSERRSIDETNATAQSLKISYSNYSSEEEDNEKLSSKSSCKSNEESTFSRYDSGRDHDDSSRNTSMRINSLAHDDKEEDEEENHETRSYSDHDDSPRNTSMRINSLSHDDDEEEEEENHQTRLEHIHSSKSEDQSVYSDDDAGESGESSLHRIEAKEEEHISSDHD | 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 | MSNSVPLLCFWSLCYCFAAGSPVPFGPEGRLEDKLHKPKATQTEVKPSVRFNLRTSKDPEHEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHTREKDANVVVVDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGADIHKRLSPDDADFVDVLHTYTRSFGLSIGIQMPVGHIDIYPNGGDFQPGCGLNDVLGSIAYGTITEVVKCEHERAVHLFVDSLVNQDKPSFAFQCTDSNRFKKGICLSCRKNRCNSIGYNAKKMRNKRNSKMYLKTRAGMPFRVYHYQMKIHVFSYKNMGEIEPTFYVTLYGTNADSQTLPLEIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGASQSWYNLWKEFRSYLSQPRNPGRELNIRRIRVKSGETQRKLTFCTEDPENTSISPGRELWFRKCRDGWRMKNETSPTVELP | 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 . Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins .
Catalytic Activity: a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+)
Sequence Mass (Da): 56795
Sequence Length: 500
Subcellular Location: Secreted
EC: 3.1.1.3
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Q9WVG5 | MRNTVFLLGFWSVYCYFPAGSITTLRPQGSLRDEHHKPTGVPATARPSVAFNIRTSKDPEQEGCNLSLGDSKLLENCGFNMTAKTFFIIHGWTMSGMFESWLHKLVSALQMREKDANVVVVDWLPLAHQLYTDAVNNTRVVGQRVAGMLDWLQEKEEFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRLSPDDADFVDVLHTYTLSFGLSIGIRMPVGHIDIYPNGGDFQPGCGFNDVIGSFAYGTISEMVKCEHERAVHLFVDSLVNQDKPSFAFQCTDSSRFKRGICLSCRKNRCNNIGYNAKKMRKKRNSKMYLKTRAGMPFKVYHYQLKVHMFSYNNSGDTQPTLYITLYGSNADSQNLPLEIVEKIELNATNTFLVYTEEDLGDLLKMRLTWEGVAHSWYNLWNEFRNYLSQPSNPSRELYIRRIRVKSGETQRKVTFCTQDPTKSSISPGQELWFHKCQDGWKMKNKTSPFVNLA | 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 toward both types of substrates (By similarity). Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins (By similarity).
Catalytic Activity: a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+)
Sequence Mass (Da): 56629
Sequence Length: 500
Subcellular Location: Secreted
EC: 3.1.1.3
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Q6DBU8 | MIYRKIIWGILYVTLMLFDTHRAQECEEMTDLNFKDSLAGTSLKVRLLLYTRADPSCGQLLSHQEPFSNSQFNVSSVTTFLIHGYRPTGSPPVWMKQFVEFLLNRRDMNVIVVDWNRGATNMNYWQVVKNTRKVANNLTDLIQKMKDNGANLSSIHMIGVSLGAHISGFTGANFNGEIGRITALDPAGPEFNGRPPEDRLDPSDALFVEALHTDMDALGYRNLLGHIDYYANGGADQPGCPKTILSGSEYFKCDHQRSVFLYMSSVNGSCPIIAYPCESYTDFQDGTCMDCGKFKSAGCPIFGYDSVRWRDTLVQLEQTRTYFQTNKASPFCKVGYKVDIVSWNQKTHWGYLTIKLSNGTEETQVELNHKSLKFERFQETSVLAQFERDIQPVKKITLKFCPRKGLRPRKKLRLLHIRLTPLQNHLRPLCRYDLLLEESKDVTFKPIPCEDSNF | 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 (TG) (By similarity).
Catalytic Activity: 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + hexadecanoate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 51811
Sequence Length: 454
Subcellular Location: Secreted
EC: 3.1.1.-
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Q8WWY8 | MLRFYLFISLLCLSRSDAEETCPSFTRLSFHSAVVGTGLNVRLMLYTRKNLTCAQTINSSAFGNLNVTKKTTFIVHGFRPTGSPPVWMDDLVKGLLSVEDMNVVVVDWNRGATTLIYTHASSKTRKVAMVLKEFIDQMLAEGASLDDIYMIGVSLGAHISGFVGEMYDGWLGRITGLDPAGPLFNGKPHQDRLDPSDAQFVDVIHSDTDALGYKEPLGNIDFYPNGGLDQPGCPKTILGGFQYFKCDHQRSVYLYLSSLRESCTITAYPCDSYQDYRNGKCVSCGTSQKESCPLLGYYADNWKDHLRGKDPPMTKAFFDTAEESPFCMYHYFVDIITWNKNVRRGDITIKLRDKAGNTTESKINHEPTTFQKYHQVSLLARFNQDLDKVAAISLMFSTGSLIGPRYKLRILRMKLRSLAHPERPQLCRYDLVLMENVETVFQPILCPELQL | 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 Activity: 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + hexadecanoate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 50859
Sequence Length: 451
Subcellular Location: Secreted
EC: 3.1.1.-
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Q8CIV3 | MLRLCFFISFMCLVKSDTDETCPSFTRLSFHSAVVGTGLSVRLMLYTQRDQTCAQIINSTALGSLNVTKKTTFIIHGFRPTGSPPVWIEELVQSLISVQEMNVVVVDWNRGATTVIYPHASSKTRQVASILKEFIDQMLVKGASLDNIYMIGVSLGAHIAGFVGESYEGKLGRVTGLDPAGPLFNGRPPEERLDPSDALFVDVIHSDTDALGYKEALGHIDFYPNGGLDQPGCPKTIFGGIKYFKCDHQMSVYLYLASLQNNCSITAYPCDSYRDYRNGKCVSCGAGQIVPCPRVGYYADSWKEYLWDRDPPMTKAFFDTAETKPYCMYHYFVDIVSWNKSVRRGFITIKLRGEDGNITESKIDHEPSAFEKYHQVSLLARFNRDLDKVAEISLLFSTGSVVGPKYKLRVLQMKLRSLAHPDRPHLCRYDLVLMENVETSFQPILCSQQQM | 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 (TG) (By similarity).
Catalytic Activity: 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + hexadecanoate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 50675
Sequence Length: 451
Subcellular Location: Secreted
EC: 3.1.1.-
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Q6XZB0 | MRVYIFLCLMCWVRSDNKRPCLEFSQLSVKDSFRDLFIPRIETILMMYTRNNLNCAEPLFEQNNSLNVNFNTQKKTVWLIHGYRPVGSIPLWLQNFVRILLNEEDMNVIVVDWSRGATTFIYNRAVKNTRKVAVSLSVHIKNLLKHGASLDNFHFIGVSLGAHISGFVGKIFHGQLGRITGLDPAGPRFSRKPPYSRLDYTDAKFVDVIHSDSNGLGIQEPLGHIDFYPNGGNKQPGCPKSIFSGIQFIKCNHQRAVHLFMASLETNCNFISFPCRSYKDYKTSLCVDCDCFKEKSCPRLGYQAKLFKGVLKERMEGRPLRTTVFLDTSGTYPFCTYYFVLSIIVPDKTMMDGSFSFKLLNQLGMIEEPRLYEKNKPFYKLQEVKILAQFYNDFVNISSIGLTYFQSSNLQCSTCTYKIQSLMLKSLTYPERPPLCRYNIVLKDREEVFLNPNTCTPKNT | 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 Activity: 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + hexadecanoate
Sequence Mass (Da): 52922
Sequence Length: 460
Subcellular Location: Cell membrane
EC: 3.1.1.-
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Q4ICM0 | MSRTLTSRQAEELHKSIIAYLAANNLQDSANAMRTELGLGEDAFDTATAKKYETLLEKKWTSVVRLQKKIMDLEAQTQTLQTELNSATPTSNRRGDPSSWLPAGPPRHVLQSHRTPINCVAFHPIFSSIASGDEDATIKIWDWEFGELERTVKGHTKAVLDLDYGGPKGHTLLASCSSDLTIKLWDPANEYQNIRTLPGHDHSVSAVRFIPSGAPGAPLSGNLLASASRDVTVRIWDVTTGYCVKTIRGHADWIRDVSPSLDGKYLLSTGNDRTVRLWDISVPNPEAKLVMIGHEHFVECCTFAPPAAYSHLATLAGVKKPPPASSTAEFMATGGRDKTIRLWDGRGNCIKTLIGHDNWVRGLVFHPSGKFLLSVSDDKTIRCWDLSQEGKCVKTVEGSHEHFITSLRWAPPIIKDKGPGEETNGDVGTPKKAATAPQDVQIRCVIATGSVDMSLRIFSR | 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 (EE) transport from the hyphal tip. Required for localization of dynein to the mitotic spindle poles. Recruits additional proteins to the dynein complex at SPBs.
Sequence Mass (Da): 50451
Sequence Length: 460
Domain: Dimerization mediated by the LisH domain may be required to activate dynein.
Subcellular Location: Cytoplasm
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A9V790 | MVLTARQQEELQLAVHAYLVEAGHAEAAAAMAKSANLGDDAGDAKYTGLLEKKWTTITRLQKRNMELQAEVEELRSSARAPRSRTTTKMEEWVPRPPATVAVDGHRLPITAVAIHPSFAVMASASEDASIKLWDMESGNFERSLKGHTNAVNDIAYDREGNRLVSCSTDMTIKVWNMDNFTCTKTLSGHDHTVSSVRFDHTGDRVFSASRDKTIKIWELATGYCLQTLQGHSDWVRSIDVSADGAWICSASSDHTVRVWSVASGECKHVWSDHEHVVEHASFAPLVAHEALNLMIFGSKPSAEAASKGPFVASASRDKSICLFDVSTGQHLARLTGHDNWVRATAWSRGGRYLFSVADDKTMRVWDIATKRVSKTIPAHNHFVSCIAVHAKNTHVVTGSVDLKVKVWECN | 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: Dimerization mediated by the LisH domain may be required to activate dynein.
Subcellular Location: Cytoplasm
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P63005 | MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR | 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 dimer composition-dependent manner (By similarity). 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 such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet-activating factor (PAF) by removing the acetyl group at the SN-2 position. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos (By similarity). May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR .
Sequence Mass (Da): 46670
Sequence Length: 410
Domain: Dimerization mediated by the LisH domain may be required to activate dynein.
Subcellular Location: Cytoplasm
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Q0U1B1 | MSAILTDRQAEELHKAIIAYLGVINAPKTAAAFREEVNFSAAFDDATRKKYEGLLEKKWTSVVRLQKKVLELEQRNQSLQSELDSTTPTSLLRRNQDPSSWLPRAPARHTLQSHRSPITCVAFHPVFSSLASGSEDTTIKIWDWELGELERTVKGHTKGVLDVDFGGPRGGTLLASCSSDLTIKLWDPSDEYKNIRTLPGHDHSVSAIRFVPSGAAGSPSSGNLLVSASRDKTLRVWDVTTGYCVKTIRGHADWVRDVSPSFDGRWLLSAGNDQTARLWDASSGEAKCTFLGHEHVIECVTIAPPVSYANLASLAGLKKPPPLSSSAEFVATGSRDKTIKIWDGRGTLIKTLAGHDNWVRALIFHPGGKYLLSASDDKTIRCWDLTQEGRCVKVVTDAHSHFVSCMRWAPNVVKDAPTNGDAPNGTTANGASKKKDEESAKAGIRCVIATGCVDLNVRIFAS | 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 (EE) transport from the hyphal tip. Required for localization of dynein to the mitotic spindle poles. Recruits additional proteins to the dynein complex at SPBs.
Sequence Mass (Da): 50356
Sequence Length: 462
Domain: Dimerization mediated by the LisH domain may be required to activate dynein.
Subcellular Location: Cytoplasm
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Q7ZUA6 | MEADEVSIREQNFHSQVREYTICFLLFAVLYIVSYFIITRYKRKADEQEDEDAIVNRISLFLSTFTLAVSAGAVLLLPFSIISNEILLSFPQNYYIQWLNGSLIHGLWNLASLFSNLCLFVLMPFAFFFLESEGFAGLKKGIRARILETLVMLILLALLILGIVWVASALIDNDAASMESLYDLWEFYLPYLYSCISLMGCLLLLLCTPVGLSRMFTVMGQLLVKPTILEDLDEQMYIITLEEEAIQRKLNGISSTLENQTVELERELEKVKCKKTNLERRKKASAWERNLVYPAVMILLLIETSISVLLVAFNILYLLVDETAMPKGSGGPGIGNASLSTFGFVGAALEIILIFYLMVSSVVGFYSLRFFENFIPRKDDTTMTKIIGNCVSILVLSSALPVMSRTLGITRFDLLGDFGRFNWLGNFYIVLSYNLLFAIMTTLCLVRKFTSAVREELLKALGLDKLHLSNNPRDSETKPSANGHQKTL | 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 | MEGQDEVSAREQHFHSQVRESTICFLLFAILYVVSYFIITRYKRKSDEQEDEDAIVNRISLFLSTFTLAVSAGAVLLLPFSIISNEILLSFPQNYYIQWLNGSLIHGLWNLASLFSNLCLFVLMPFAFFFLESEGFAGLKKGIRARILETLVMLLLLALLILGIVWVASALIDNDAASMESLYDLWEFYLPYLYSCISLMGCLLLLLCTPVGLSRMFTVMGQLLVKPTILEDLDEQIYIITLEEEALQRRLNGLSSSVEYNIMELEQELENVKTLKTKLERRKKASAWERNLVYPAVMVLLLIETSISVLLVACNILCLLVDETAMPKGTRGPGIGNASLSTFGFVGAALEIILIFYLMVSSVVGFYSLRFFGNFTPKKDDTTMTKIIGNCVSILVLSSALPVMSRTLGITRFDLLGDFGRFNWLGNFYIVLSYNLLFAIVTTLCLVRKFTSAVREELFKALGLHKLHLPNTSRDSETAKPSVNGHQKAL | 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 | MEEDEVTIREQNFYSQVRECIICFLLFAILYIVSYFIIKRYKRKGDEQEDEDATVNRVSLFLCTFTLAVSGGAVLLLPFSIISNEILLCFPKSYYIQWLNGSLIHGLWNLVSLFSNLCLFVLMPFAFFFLESEGFAGLKKGIKARILETIIMLILLALLIFGIVWVASALIDNSSASMESLYDLWDCYLPYLYSCISLMGCLLLLLCTPVGLSRMFTVMGQLLVKPTILEDIDEQMYIISLQEEALQRKLNGGNYTADYSRKKIEHDLLNARSMKSKLERRKNASAWQRNLVYPAVMILLLIATFSSVILVSLNILRLLVDETAMPKGSKGSGFGDASLFTFGFAGATLEIILIFYLMVSSVVGFYSLRFFSSFTPRKDDTTMTKVIGNCLSILVLSSALPVMSRTLGITRFDLLGDFGRFNWLGNFYIVVAYNLMFAVMTTLCLVRKFTSAVREELLKAIGLDRLQLSNKSSDSPSPNGHQKSL | 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 | METEDVTVREQIFHDRVRETIICVLLFICLYILSHFILTHFKKSAEFVTDDIEDATVNKIALWLCTFTLSVAVCAVLLLPISILSNEVLLTFPHSYYMQWLNGSLIRGLWNLVFLFSNLSLVFLMPFAYFFTESEGFAGSKKGVMARVYETAVMLLLLSLLVLGIVWVASALLHHNTARESLYDLWEYYLPYLYSGISLFGVLLLLLCTPFGLSRMFSVTGSLLVKPRLLENLEETMNCAVFEEASLSRKLKSTNTCWISAHLEALNKEFLSVQSKRITLELRKRASPWQRNLVYPVAMLLLLALTAVSVLMVCFHVLELLFDESAMPRGMEDPHLGLASFSMLGSLGAAVQVVIILYLMVSSVVGFYSSPLFTGLLPRAQDTTLTQIIGNCVSLLILSSALPVFSRTLGITKFDLLGDFGRHDWLGSFHIVFLYNMLFAGLTSACLINTVTWALQRELIRAFGLHRLPLTVSRSTIPLKLLLANGLSKIH | 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 | MEAPDYEVLSVREQLFHERIRECIISTLLFATLYILCHIFLTRFKKPAEFTTVDDEDATVNKIALELCTFTLAIALGAVLLLPFSIISNEVLLSLPRNYYIQWLNGSLIHGLWNLVFLFSNLSLIFLMPFAYFFTESEGFAGSRKGVLGRVYETVVMLMLLTLLVLGMVWVASAIVDKNKANRESLYDFWEYYLPYLYSCISFLGVLLLLVCTPLGLARMFSVTGKLLVKPRLLEDLEEQLYCSAFEEAALTRRICNPTSCWLPLDMELLHRQVLALQTQRVLLEKRRKASAWQRNLGYPLAMLCLLVLTGLSVLIVAIHILELLIDEAAMPRGMQGTSLGQVSFSKLGSFGAVIQVVLIFYLMVSSVVGFYSSPLFRSLRPRWHDTAMTQIIGNCVCLLVLSSALPVFSRTLGLTRFDLLGDFGRFNWLGNFYIVFLYNAAFAGLTTLCLVKTFTAAVRAELIRAFGLDRLPLPVSGFPQASRKTQHQ | 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 stabilizes the beta-catenin destruction complex that is required for regulating CTNNB1 levels (By similarity). Acts as a LCN1 receptor and can mediate its endocytosis .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55209
Sequence Length: 489
Subcellular Location: Cell membrane
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Q7ZX75 | MEVNQDVSVREQIFHDWVRECIICSLLFSTLYLLSYIVITKFKKHADFATVDVEDAAVNRIALWMCTFTLAVSVGAVLLLPFSIISNEVLLSVPHNYYIQWLNGSLIHGLWNLVFLFSNLSLVFLMPFAYLFTEAEGFAGSKKGVMSRVYETTVVLLLLTLLVFGIVWVASAIFDDDSAGRESLYDLWEYYLPYLYSGISLFGVLLLLLCTPFGLSRMFSVTGNLLVKPRLLENLEEHLSCTAFEEAAISRKISTKASCWLNLNMEALQKRLLAIQSHRITLEMRRRASPWQRNLVYPLAMLLLLALTGITVLIVCVNVLELLIDEAAMPKGIQGSQLGKVSFSVFGSFGAAVQVILIFYLMASSVVGFYSSPLFIQLLPQKQNTPMTKIIGNCVSLLILSSALPVFSRTLGITRFDLLGDFGRFNWLGNFYLILLYNMMFAGLATLCLVKKFTWAVQAELIRAFGLDRLPLSVKKIRSQGKA | 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 | MEIYRKSAAETFTQLEATEKGLTTSEVTKRQEKYGFNELKNKKKDPLWKLFLETFKDPMVIVLVIAALVQLVLGEVVESLIIFLVLIVNSIISVVQTRKAESSLDALREMSAPVAKVIRDGSKQSIHARELVPGDVVILDAGDFVPADGRLFESGSLKIDEGMLTGESEAVEKYIDTIPDEVGLGDRVNMVFSGSLVVYGRGMFVVTGTASETEIGKIAGLLETAEAKQTPLQRKLESFSKKLGLGILALCVLIFAVEAGRVLLGDNSADMATAILNAFMFAVAVAVAAIPEALSSIVTIVLAVGTNKMAKQHAIIRKLPAVETLGSTSVICTDKTGTLTQNKMTVVDYYLPDGTKENFPESPENWSEGERRLIHIAVLCNDSNINSEGKELGDPTEVALIAFSNKNNQDYNEIREKFIREGEIPFDSDRKLMSTLHTFNENKAMLTKGGPDVMFARCSYVFLDGEEKPMTEEILAKLKETNEEFSNQALRVLAYGYKRMPADTTELKLEDEQDIVLVGLTAMIDPPREAVYASIEESKKAGIRTVMITGDHKTTAQAIGRDIGLMDADDIALTGQELDAMPEEELDKKLEHIAVYARVSPENKIRIVKAWQKKGKITAMTGDGVNDAPALKQADIGVAMGSGTDVAKDSAAMILTDDNFVSIVDAVGVGRTVFDNIKKSIAYLFAGNLGAIIAILFALVLDWINPFTALQLLFINLVNDSLPAIALGMEKAEPDVMKRKPRDINEGIFAGGTMRAVISRGVLIGIAVIISQYIGMQISPEMSVAMAFTTLILARTLQTFAARSNVQTAFGAGFFSNKYVIGAVLLCFVLYGITVLPGAREIFSIPASFGLHEWSIAAGLALAAVVMMEIIKVVQNKFFK | 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 Activity: ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 95658
Sequence Length: 880
Subcellular Location: Cell membrane
EC: 7.2.2.10
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Q9NZU5 | MAKVAKDLNPGVKKMSLGQLQSARGVACLGCKGTCSGFEPHSWRKICKSCKCSQEDHCLTSDLEDDRKIGRLLMDSKYSTLTARVKGGDGIRIYKRNRMIMTNPIATGKDPTFDTITYEWAPPGVTQKLGLQYMELIPKEKQPVTGTEGAFYRRRQLMHQLPIYDQDPSRCRGLLENELKLMEEFVKQYKSEALGVGEVALPGQGGLPKEEGKQQEKPEGAETTAATTNGSLSDPSKEVEYVCELCKGAAPPDSPVVYSDRAGYNKQWHPTCFVCAKCSEPLVDLIYFWKDGAPWCGRHYCESLRPRCSGCDEIIFAEDYQRVEDLAWHRKHFVCEGCEQLLSGRAYIVTKGQLLCPTCSKSKRS | 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 cTNC promoter (By similarity). Plays a critical role in the development of cardiac hypertrophy via activation of calcineurin/nuclear factor of activated T-cells signaling pathway.
Sequence Mass (Da): 40833
Sequence Length: 365
Domain: The LIM zinc-binding domains and the Cys-rich region mediate interaction with GATA6.
Subcellular Location: Cytoplasm
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Q8VEE1 | MAKVAKDLNPGVQKMSLGQQQSARGVACLRCKGMCSGFEPHSWRKICKSCKCSQEEHCLSSDLDDDRKIGRLLMDSKYATLTARVKGGDGIRIYKRNRMIMTNPIATGKDPTFDTITYEWAPPGVTQKLGLQYMELIPKERQPVTGTEGALYRRRQLMHQLPIYDQDPSRCRGLVENELKAMEEFVKHYKSEALGVGEVALPGQGGLPKEENKTQEKPEGTETTAPTTNGSLGDPSKEVEYVCELCKGAAPVDSPVVYADRAGYSKQWHPTCFQCIKCSEPLVDLIYFWKDGAPWCGRHYCESVRPRCSGCDEIIFSEDYQRVEDLAWHRKHFICEGCEQLLSGRAYIVTKGQLLCPTCSKSKRS | 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 cTNC promoter. Plays a critical role in the development of cardiac hypertrophy via activation of calcineurin/nuclear factor of activated T-cells signaling pathway.
Sequence Mass (Da): 40996
Sequence Length: 365
Domain: The LIM zinc-binding domains and the Cys-rich region mediate interaction with GATA6.
Subcellular Location: Cytoplasm
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Q5PXT2 | MAKVAKDLNPGVQKMSLGQQQSARGVPCLRCKGTCSGFEPHSWRKICKSCKCSQEDHFLSSDLEDDRKIGRLLMDSKYSTLTARVKGGDGIRIYKRNRMIMTNPIATGKDPTFDTITYEWAPPGVTQKLGLQYMELIPKEKQPVTGTEGAYYRRRQLMHQLPIYDQDPSRCRGLLESELKVMEEFVKQYKSEALGVGEVALPGQGGLPKEEGKQQEKPEGAETAAPTANGSLGDPSKEYVCELCKGVAPADSPVVYSDRAGYSKQWHPACFVCAKCSEPLVDLIYFWKDGAPWCGRHYCESLRPRCSGCDEIIFSEDYQRVEDLAWHRKHFVCEGCEQQLGGRAYIITKGQLLCPTCSKSKRT | 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 cTNC promoter. Plays a critical role in the development of cardiac hypertrophy via activation of calcineurin/nuclear factor of activated T-cells signaling pathway (By similarity).
Sequence Mass (Da): 40660
Sequence Length: 363
Domain: The LIM zinc-binding domains and the Cys-rich region mediate interaction with GATA6.
Subcellular Location: Cytoplasm
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O51253 | MKTRCFCLAAFSGILTTLAIPNEIKETGYSILGFVAYVPLFIALNKLEDKKALMGLTVFYFIIANSLQNFWLGFFHAFGWITFIGVIIGYIPYSLTLGYFLYYSLKSFKNKTMSITMLFTFYDYSRSIGFLAYPWGLAAFTVNNFNNLIQIADIFGVFFVSFAVYFLNSGIADFLIHKNKTNLLNIAFPTLLITASFTYGMIKKIELKNLLAKEIDSLNIAAIQLNTDPWLPGNDKKGIRDSIEITEQALKENPKIEFVIWSEGVLTYPFSKEDQHFKSSDLHNELKNFIKEHKIPFAIGAPSNLDKAIGIQQNSIYMVEPNLNITNIYSKIFLVPFAEKIPFYEYKFVRNFFLKNFRILGQIEGNKIEILKLKKFKFAPLICYDDAFPELSRFYKTQGANILVNFSNDSWSKTNSAEWQHFVVAKFRSIENGIKTIRATNSGITATINEYGETIKKLETFKKGYLLSTVKLSPTFTTIYEKIGDSFIHILVMMFLITTLRFQFMEDKNQLLSSSVVKIKV | 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-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59737
Sequence Length: 521
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
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P61034 | MSPAGKGPAWRQPAILAAAGAAHALSFAPDPLPAWSLAPVQVIALAVAAHASLQAPSARRALARGWLFAMFSFSLGLYWMYVSMHDYGGLAAPLAAAGVLALSAFLALFPGLACAAARWLCPPHWDASPPARARRTLYTAATWAACWAALEWLRAVVLTGFPWLNISYAHVDSPLAGWAPLLGVHGMALLAAFAAAALAGLWQSASGRIDSRQALAAGVALLLAGAGWLLGQFSWSRPEGKPLHLRLVQGNVEQSQKFDPALLETGLRRHLELASLPPRPGEPKPDMIILPETVLPVFQDQLPASVWDAWIEVARRADTRIAMGVPLHTQPDGATGHRYTNSVIGFDASTPVEQLRTGTTAMRYDKQHLVPWGEYVPPGFRWFVDMLDIPLGDFDRGAARQPSFDIAGQRIAFNICYEDLFGPELLPALQDGPDGRPGATIMANVSNLGWFGNTWALRQHLQIGRLRTMETARPMVAATNTGITAAIDARGRVAAALPADRAGVLPVAVQGMTGLTPYARFGDKPALALIGLLLIAAAARGRRPRQP | 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-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58475
Sequence Length: 547
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
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Q89WA1 | MSAFQRLRQIALAIILTWGWKRALVAITAGALSVLALAPFNLFPVLFITFPVLVWLIDGAGAGRYRGIPAAALTGYWFGLGYFVPGLYWIGYAFFVDADVFAWLTPFAVLGLPAYLSIFTAIGFALARLLWTKNATRVLALAASLTIAEWLRGHALTGFPWNAFGYALSEPLPLAQTASLIGLWGMTFLTVAIFASPATLIDRTPDRRVAWRAPAAAVALLIAMSIFGAIRLSLHPTTMVAGAKLRLMQPNLQQDAKFNYAAKTEVMKKYLALSDRASGPQSTGVRDATILIWPESAFPFFLTREADAMAEIAELLPKGTVLITGSVRAPDLPRGTPITRAYNSIYVIDHDGSVLAVYDKLHLVPFGEFLPYQDLMEKLGFEQLTRVRGGFIAGTVRHALPMPGAPSALPLICYEAIFPGEVAGRNERPGWIVNLTNDGWFGISTGPYQHLEQARMRAIELGLPLVRSANTGISAVIDPVGRTVASLGLGVEGILDASLPAAIPPTIYARVGDVPAAVLVALAVLLAVRRRVAKRHP | 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-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57997
Sequence Length: 537
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
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Q8YEA6 | MIARLAGRIILLNGWRRALAAFLSGAFATLTQPPFDIFVAGFVSFPVLVWLIDGAIARTDAGPLRRLLLAAKVGWWFGFGYFVSGLWWIGTALLVDADQFAWALPLAVLGLPAFLALFYAFAAMIARLLWSDGLGRILAFAFGFALAEWLRTFIFTGFPWNLIGYAAMPVPLLMQSVAVIGLVGMSALAVFVFAAPALLTGGHFARTGIGLAIFLALAHVGFGAWTLSRAPAIVDENGPLAVRIVQPSIAQAMKWDNAERRAIFDKLVGLTEEAPAEGKPRPDVIVWPETAIPYILESTPQALAHIGDALQEGQVLLAGAVREEKGADGGEPRYYNSIYTIDDRGRIVSTADKVHLVPFGEYLPFESFLRGLGLQEVVEMPGGFTAGTTRHALAVKDGRSFLPLICYEAIFPDELGYEGAGASAIINVTNDAWYGDTPGPYQHFRQAQVRAVEQGLPLIRAANNGLSAIVDTYGRITGSLALDAVGVVDSYLPSPRDPFWGRPPGWIQTVLILLTLLAASVGLILYSRRRFH | 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-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57539
Sequence Length: 532
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
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Q9PNJ9 | MKLKLNFLPYFSFIPKKLNTNSIIFKIIKVFFIAILLSNSIYLSFFENIFTQTISPFLAIWGLVLLLKSKTSKQYFWIGFFVGILWFWWIGLSSIYFNLNYLVPIIPIIIGFIYGLLFRLCYLLKFDFLRLCGIFCISFIHPLGFDWFNWGIFTVYGFFDPSYRGIICIFLIAYFIYEGYISRYYKIAIVLILFFSGFQYNEKQAQTLNLNYKLINTNISQDQKFLQENLKSNSDILIQDILQAINEKKELVILPETAFAFDLKNTKYELMLKELSYKITIITGAFHVEKEHTYNSTYIFKKGNVYILNKHFLVPFGEEIPFFKDLTKKYFLKNIEEFSKGPIQSKYKLDNQIITNAICYEATKEQNYQNSQIIIALSNNAWFNNSSEYKLQQLLMKFYASKYGVSVYHATNGKENIVILPKKLLSKDWKNLSKEIFNDKK | 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-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52109
Sequence Length: 441
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
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Q9AC16 | MIAWTRFRERPWSGPALALIAGLAAALAHPPFGVLPGLLGYAGLLHLLDNADVQRPLRSVFWRGWLAGVGYFGLGTWWVGEAFLVDAATHGWMAPFAVTGMAAGLALFWGLAALLYRALRPASAWRVLTFAGAFAALEWMRGHVLTGFPWNLPGETWKAGSAPSQLAALVGAYGLTWITLAIAGAPAVWRQGRGGRAATGLAVASLIGLYGYGAIALSRPLSPSGPTTVRIVQADIKQDLKWDAERFAQIVQAYVSLTATPYAAKPADIVIWPEGALPAAVNDYLAPGTWVRQAIVDSLAPGQLLLIGGYRYEGAGPHPTYYNSLVALRRTETDLELVGIYDKHRLVPFGEYLPADRFLTVIGFKSLARLSDNFTTGPTPAPLRISPELLVQPLICYESLFPGLAKPDPNVRALINVSNDAWFGVTSGPPQHLNLASYRAIESAKPILRATPTGISAVVDARGRIVPGASLGLGESGVIDAQIPGMGQVTPYDNFGDVAFLALILISGVVSARVRIGKISSSIAPKRKLS | 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-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56423
Sequence Length: 530
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
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Q8KCC4 | MNGAYRGALSRLLSKPFFLPLLSGLLLGISFPTWPAVHLEPLAWIALVPLLLSLEHEERFGPFFRKSWMSMLLFCLIALWWVCLATFVGGILTVFVQSLFSVVPLVVFYYFKKRAGFRSALLALPFIWTGWEWAYMQQDFSLGWLTFGNSQANLLWMVQYADVTGVWGVSFWLLTFNVLVLLLFMEKESFQVKVGIVMVMLVMIATPLLYARQVFRNTALDNTSPKVRVALVQPDIDPHEKWDGLGPEETLSRLYSLTGQSVRGERLELIIWPETAIPFYIRLPENKPYMDSVRRMVMRWNTPLLTGFPDEVPVFPNSARGEAVAASGAEYAAYNASMLLHPAGGPVQIYRKMRLVPFGERVPYSEYFPWLERLSFSMSGISSWAKGREATVMHFTSRDGQPVRMANIICYESIFPGQVSTFVRRGAQFLTLVTNDGWYGTSYGPWQHAAIDRLRCIENRRAMARCANTGVTLFYDICGRSYAETPWWQQSVLTADVPLESRITFYTAHPDLVPHVCLGIAGVLALVAAVRKR | 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-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60528
Sequence Length: 533
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
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O84539 | MFKLVSYIILSWVLVCLAQPDVSVVASVVSCICGYSLLWAGLFALVEQLSWKKVWCIAFIWTWTVEGAHFSWMLEDLYVGTSIYFVWGILLSYLATLFASFSCLVVWCCRKQYRGALVWLPGVWVAIEAIRYYGLLSGVSFDFIGWPLTATAYGRQFGSFFGWAGQSFLVIAANICCFAVCLLKHSFSKGLWLTLCAFPYLLGGAHYEYLKKHFSDSEVLRVAIVQPGYSPHMHAGRTASAIWRGLVSLCQTIQTPVDVIVFPEVSVPFGLHRQAYTLHENQPVLESLLPNKSWGEFFTNLDWIQAIAERYQCTVIMGMERWENKGGILHLYNAAECVSREGEITSYDKRILVPGGEYIPGGKIGFSLCQTFFPEFALPFQRLPGEFSGVVNITERIKAGISICYEETFGYAIRPYKRQQADILVNLTNDGWYPRSRLPLVHFYHGMLRNQELGIPCIRACRTGVSAAVDSLGRIVGILPWESRTCPVSTGVLQVSVPLYSYHTVYARLGDAPLLLIAVCSVIGAIAYFYRKKKETPPQTFF | 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-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60992
Sequence Length: 542
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
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Q7NQI3 | MLNAAGGAGCDPSSPTATSPMRILILLLAAALAGAFTLFAFAPYRLFWLMPLCLAALVELLQREPRRAFWLGYAWGLGAYVSNFRWIYDSLHDVAGLPAWIAAPLVLLLPAYLALYPGLASWLACRIDPRPGVRWLLAFPAAWELGEWLRGWVMTGFPWGAAGYSQITESPLAGYAPLGGIHLVNYLVALSAAALAMLARAGMRQRIGILIAAALAWGSGVWLRDIEWTTPAGKPITVALAQGNIAQELKWSPENLENSLLTYYRQVAMTRADLMILPETALPLFLDDLPSGYLSMMRGEASRAGMALASGIPRRTDDGRGYLNSVVALSDPKMPYYAKDHLVPFGEFVPLPGLIGWIYQHMDMPLSGFTRGGADQPPLTLAGQKVAFNVCYEDSFGEELIGPASRAGMLANVSNLAWFGKSEAMSQHLQLSQARSLETGRYMLRATNNGMTAIIRPDGEISAVAAPFTAQVLTGFAQSRQGLTPYMRFGNLPVVLGCGALLLLALLLGWRRRGQH | 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-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55968
Sequence Length: 516
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
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Q820B4 | MNSVLALIAGAILPLAFAPFNWFPIAFVSPAILLAVWLRSRPLVAWWRGWLFGFGFFGAGASWVYVSIHHFGNANVPLAVLITVLFVFVLALFIAFQGLSFSLFFRKRKAALTALFAFPAWWVVWEWLRSILFTGFPWLFLGYSQINSPLKGFGPLFGIYGISLIVAFISGCIYLLVTSKKLNKKIMCLILIILPFIVGWVLTFIPWTRPGSESVRVGLVQGNIGQRLKWDPDTLYSTLHTYYSETQKNWDHGIIVWPEAAIPIYPQQVSVFLQALDKEAKQHNTALMTGIPIYHEKTNKVFNGLMVLGDGHGLYLKRHLVPFGESFTSSKICNLLMKYFDIPMSDLSPGPEDQEPTVVKGIPFAPFICYEIAYPTEVLNHLSNKQFIVVVNDDSWFAGTIAPAQQLQIAQMRALETERYLLYSTNTGITAIISPEGKIVKSAPQNQRLLLTGQIKPVTGKTPLMRWNYYPVVGIIIIFLLLTFL | 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-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54620
Sequence Length: 485
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
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P23930 | MAFASLIERQRIRLLLALLFGACGTLAFSPYDVWPAAIISLMGLQALTFNRRPLQSAAIGFCWGFGLFGSGINWVYVSIATFGGMPGPVNIFLVVLLAAYLSLYTGLFAGVLSRLWPKTTWLRVAIAAPALWQVTEFLRGWVLTGFPWLQFGYSQIDGPLKGLAPIMGVEAINFLLMMVSGLLALALVKRNWRPLVVAVVLFALPFPLRYIQWFTPQPEKTIQVSMVQGDIPQSLKWDEGQLLNTLKIYYNATAPLMGKSSLIIWPESAITDLEINQQPFLKALDGELRDKGSSLVTGIVDARLNKQNRYDTYNTIITLGKGAPYSYESADRYNKNHLVPFGEFVPLESILRPLAPFFDLPMSSFSRGPYIQPPLSANGIELTAAICYEIILGEQVRDNFRPDTDYLLTISNDAWFGKSIGPWQHFQMARMRALELARPLLRSTNNGITAVIGPQGEIQAMIPQFTREVLTTNVTPTTGLTPYARTGNWPLWVLTALFGFAAVLMSLRQRRK | 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 intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein . In vitro, can utilize the phospholipids phosphatidylethanolamine (PE), phosphatidylglycerol (PG), phosphatidic acid (PA) or cardiolipin (CL) . PE is the most efficient acyl donor .
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-glyceryl-L-cysteinyl-[lipoprotein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57066
Sequence Length: 512
Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Subcellular Location: Cell inner membrane
EC: 2.3.1.269
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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 triphosphate.
Catalytic Activity: H2O + N(6)-(dimethylallyl)adenosine 5'-phosphate = D-ribose 5-phosphate + N(6)-dimethylallyladenine
Sequence Mass (Da): 25846
Sequence Length: 242
Subcellular Location: Cytoplasm
EC: 3.2.2.n1
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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); mostly active with t18:0 and saturated very long saturated fatty acids (C24:0 and C26:0), such as long-chain base (LCB) phytosphingosine (t18:0), lignoceroyl- and hexacosanoyl-CoAs . Mediates resistance to sphinganine-analog mycotoxins (SAMs, e.g. fumonisin B(1)) by restoring the sphingolipid biosynthesis (By similarity). Could salvage the transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi apparatus in ceramides-depleted cells after SAM exposure (By similarity). May prevent precocious cell death by delaying PR1 accumulation during aging . Contributes to hypoxic conditions tolerance (e.g. submergences), especially in the dark, by promoting the formation of very-long-chain (VLC) ceramide species (22:1, 24:1 and 26:1) and of VLC unsaturated ceramides, which are modulating CTR1-mediated ethylene signaling leading to endoplasmic reticulum (ER)-to-nucleus translocation of EIN2 and EIN3 .
Catalytic Activity: (4R)-hydroxysphinganine + a fatty acyl-CoA = an N-acyl-(4R)-4-hydroxysphinganine + CoA + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36498
Sequence Length: 310
Pathway: Sphingolipid metabolism.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.-
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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 auxin transport related proteins); accepts only C16:0 fatty acids, but with a wide range of d18 sphingoid bases, such as sphinganine (d18:0) and palmitoyl-CoA . Mediates resistance to sphinganine-analog mycotoxins (SAMs, e.g. fumonisin B(1)) by restoring the sphingolipid biosynthesis . Could salvage the transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi apparatus in ceramides-depleted cells after SAM exposure (By similarity). Contributes to hypoxic conditions tolerance (e.g. submergences), especially in the dark, by promoting the formation of very-long-chain (VLC) ceramide species (22:1, 24:1 and 26:1) and of VLC unsaturated ceramides, which are modulating CTR1-mediated ethylene signaling leading to endoplasmic reticulum (ER)-to-nucleus translocation of EIN2 and EIN3 .
Catalytic Activity: a sphingoid base + hexadecanoyl-CoA = an N-hexadecanoyl-sphingoid base + CoA + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34699
Sequence Length: 296
Pathway: Sphingolipid metabolism.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.291
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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); active on a broad substrate spectrum, both regarding chain lengths of fatty acids and the sphingoid base, such as long-chain base (LCB) phytosphingosine (t18:0) . Mediates resistance to sphinganine-analog mycotoxins (SAMs, e.g. fumonisin B(1)) by restoring the sphingolipid biosynthesis . Could salvage the transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi apparatus in ceramides-depleted cells after SAM exposure (By similarity). Contributes to hypoxic conditions tolerance (e.g. submergences), especially in the dark, by promoting the formation of very-long-chain (VLC) ceramide species (22:1, 24:1 and 26:1) and of VLC unsaturated ceramides, which are modulating CTR1-mediated ethylene signaling leading to endoplasmic reticulum (ER)-to-nucleus translocation of EIN2 and EIN3 .
Catalytic Activity: (4R)-hydroxysphinganine + a fatty acyl-CoA = an N-acyl-(4R)-4-hydroxysphinganine + CoA + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36549
Sequence Length: 308
Pathway: Sphingolipid metabolism.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.-
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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 forms even in the absence of the oxido-reductase DsbA .
Location Topology: Lipid-anchor
Sequence Mass (Da): 26842
Sequence Length: 252
Subcellular Location: Cell outer membrane
EC: 3.4.24.-
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O61267 | MARDTQGTQGTQSQASNIWTQVESQPMEKIVWGRLYGKNIKIKSLGTSSKYRIIYTHSSFSVDLNNDEFTAGRGEANDLILTLNDLPEKILTRISKVHFIIKRANCELTNPVYIQDLSRNGTFVNNEKIGTNRMRILKNDDVISLSHPTYKAFVFKDLSPNESIGLPEEINKTYYVNRKLGSGAYGLVRLVYDTRTCQQFAMKIVKKNMLSGARPSTNFSDPDRVLNEAKIMKNLSHPCVVRMHDIVDKPDSVYMVLEFMRGGDLLNRIISNKLLSEDISKLYFYQMCHAVKYLHDRGITHRDLKPDNVLLETNDEETLLKVSDFGLSKFVQKDSVMRTLCGTPLYVAPEVLITGGREAYTKKVDIWSLGVVLFTCLSGTLPFSDEYGTPAAQQIKKGRFAYGHPSWKSVSQRAKLLINQMLIVDPERRPSIDDVLQSSWLRDAPMLQKAKRLMKLDGMEIEEENFLEPPTKRSRR | 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 | MAVSSALCIFSLLVLAQAQSELQQPKIELRLAGDKRKHYEGRLEVFYNNEWGTVCDDDFSIEAAHVACRQLGFLGAVAWSPSAKFGQGEGRIWLDNVHCTGRENSLAACPSNGFGVSDCRHSEDVGVICNQKRIPGHRFINIMNNNVETLEERVEEIRIRPISSHLKRIPITEGYVEVKERGKWRQICDEEWTPLNSRVACGMYGFPGEKNYNNKVYRSLSMRKKKNYWGFSVNCTGNEAHVSSCRLGKALEPKRNGTCGRGLPVVVSCVPGRAFAPSSSIGFRKAYRPEQPLVRLRGGANVGEGRVEVLKNGVWGTVCDDNWNLKAATVVCRELGFGSAKEALTGAKLGQGMGPVHMNEVECSGFEKSLTDCYFNNDALGCSHEEDAAVRCNVPAMGFQKRIRLSGGRNPFEGRVEVLAEKNGSLVWGTVCSENWGIIEAMVVCRQLGLGFASHAFQETWYWAGDANADNVVMSGVRCSGTEMSLPQCLHHGKHINCPKGGGRFAAGVSCSDTAPDLVLNAQLVEQTTYLEDRPMYALQCALEENCLSSTARKNDHSSYRRLLRFSSQIHNVGQSDFRPKLGYHAWTWHECHRHYHSMEVFTHYDLLSLNGTKVAEGHKASFCLEDTHCDEGISKRYHCANFGEQGITVGCWDTYRHDIDCQWIDVTDVKPGDYIFQVVINPNYDVAESDYTNNVMKCKCRYDGYRIWTYSCHIGGSRSSDMDEYSGMSNQLNHLR | 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' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation (By similarity). Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2) (By similarity). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription (By similarity). LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency (By similarity). Involved in epithelial to mesenchymal transition (EMT) and participates in repression of E-cadherin, probably by mediating deamination of histone H3 (By similarity). When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (By similarity). Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding . Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation (By similarity). Required with loxl2b for correct expression of Sox2 and for neural differentiation .
PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.
Catalytic Activity: H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+)
Sequence Mass (Da): 82334
Sequence Length: 737
Subcellular Location: Secreted
EC: 1.4.3.13
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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 protein
Sequence Mass (Da): 24789
Sequence Length: 226
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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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 protein
Sequence Mass (Da): 24282
Sequence Length: 226
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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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 protein
Sequence Mass (Da): 26920
Sequence Length: 247
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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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 protein
Sequence Mass (Da): 28302
Sequence Length: 255
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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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 protein
Sequence Mass (Da): 25322
Sequence Length: 228
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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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 protein
Sequence Mass (Da): 24559
Sequence Length: 227
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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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 protein
Sequence Mass (Da): 25835
Sequence Length: 232
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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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 include norloline, loline, N-methylloline, N-acetylloline, N-acetylnorloline, and N-formylloline . The first committed step is the condensation of O-acetyl-L-homoserine (derived from L-aspartic acid) and L-proline, probably catalyzed by the gamma-type pyridoxal 5'-phosphate(PLP)-dependent enzyme lolC, to give the diamino diacid, NACPP . Ensuing cyclization, decarboxylation, and acetylation steps yield 1-exo-acetamidopyrrolizidine (AcAP). LolO is required for installation of the ether bridge upon the pathway intermediate, 1-exo-acetamidopyrrolizidine (AcAP) . In sequential 2-oxoglutarate- and O(2)-consuming steps, lolO removes hydrogens from C2 and C7 of AcAP to form both carbon-oxygen bonds in N-acetylnorloline (NANL), the precursor to all other lolines . The enzymes lolD, lolE, lolF and lolT have also been proposed to be involved in the ether-bridge installation . Further processing of the exocyclic moiety of NANL by fungal N-acetamidase (LolN), methyltransferase (LolM), and cytochrome P450 (LolP) enzymes, with occasional involvement of a plant acetyltransferase, generates the other known lolines . LolN transforms NANL to norlonine which is monomethylated and dimethylated to respectively lonine and N-methyllonine (NML) by lolM . LolP catalyzes hydroxylation of the methyl group in N-methylloline (NML) and further oxygenation to N-formylloline (NFL) . A plant acetyltransferase is responsible for the acetylation of loline to form N-acetylloline (NAL) . LolA might interact with aspartate kinase to prevent feedback inhibition of its activity by these end products and thereby promote production of L-homoserine from L-aspartate .
Sequence Mass (Da): 28752
Sequence Length: 256
Pathway: Alkaloid biosynthesis.
EC: 1.14.11.-
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P75958 | MAMPLSLLIGLRFSRGRRRGGMVSLISVISTIGIALGVAVLIVGLSAMNGFERELNNRILAVVPHGEIEAVDQPWTNWQEALDHVQKVPGIAAAAPYINFTGLVESGANLRAIQVKGVNPQQEQRLSALPSFVQGDAWRNFKAGEQQIIIGKGVADALKVKQGDWVSIMIPNSNPEHKLMQPKRVRLHVAGILQLSGQLDHSFAMIPLADAQQYLDMGSSVSGIALKMTDVFNANKLVRDAGEVTNSYVYIKSWIGTYGYMYRDIQMIRAIMYLAMVLVIGVACFNIVSTLVMAVKDKSGDIAVLRTLGAKDGLIRAIFVWYGLLAGLFGSLCGVIIGVVVSLQLTPIIEWIEKLIGHQFLSSDIYFIDFLPSELHWLDVFYVLVTALLLSLLASWYPARRASNIDPARVLSGQ | 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 protein
Sequence Mass (Da): 45344
Sequence Length: 414
Subcellular Location: Cell inner membrane
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P44250 | MNTPFFISWRYQRGKQKNPLVALIAKFSAIGIALGVAVLIVGLSAMNGFERELNQRILAVVPHAEILSAPNATEPTIHHWQNLEKRLQQNPQIKGISPFVSFTALVENGSKLKVVQVKGVEKQAEDKVSSIGNFVQEQGWNKFEKEGGLVLGSGIAKELDVKVGDWITLLISQQNGDEQFAQPTREPVQVTSILRLDGQLDYSYALLPLAQAQTFLTYQPDQITGVELKLDDPFSARNLDLSMLNDYPQMLYMQNWISKFGYMYRDIQLIRTVMYIAMVLVIGVACFNIVSTLIMAVKDKQGDIAIMRTLGANNAFIKRIFIWYGLQAGMKGCLIGIVLGIILALNLTTFIQGIEWVIGKKLLSGDVYFVDFLPSELHWLDVLMVLVAALALSLMASLYPASRAAKLQPAQVLSSH | 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: Multi-pass membrane protein
Sequence Mass (Da): 46229
Sequence Length: 416
Subcellular Location: Cell inner membrane
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Q5MNH1 | MTLTNLDAIVVGAGFSGILAVYRLRKLGFRVQGFERQERLGGVWRENAYPGAAVDSLFPFYQFYDAELLQDWEWGEQFPTRAEMLRYFDHVDKRWEISASFEFGVSVSAARYSETTQRWTVTLEDGRRAEARWFIPAVGFSSVLNIPRIPGMSRFRGAIYHTAKWPHDAVSMRGKRVAVIGTGPSGVQIIQSVGKIAKAMTIFQQSPCLTLRKYGSPNQTATALCMRPDDHREALRLGLQTSNGFGYVPRDQDTLDVPIEERNHFYQQRYLAGGWAFWMAGFRDLCQNIQANRDAYDFWARRTRARIGDVTKRELLVPQIPSFAFGIKRPCLEEDLYEIMDQPHVKIIDISNQQIELITETSIRVHGQTVECEAIIFATGFGDEASGLRSLHIRGRNGIRLEDAWSDGVESHLGMAIHSFPNMFFLYGPQCPTLLVNSPAVITVQVEWLCEIISKCQQAGICQLEATSKSHCQWEKKMSLLWDKTLYHTHARKSKKTAEANKEEKTWVGGLILYRRELENCLANNLEGFQAWYVEETALL | 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 various modifications of the L-amino group and include norloline, loline, N-methylloline, N-acetylloline, N-acetylnorloline, and N-formylloline . The first committed step is the condensation of O-acetyl-L-homoserine (derived from L-aspartic acid) and L-proline, probably catalyzed by the gamma-type pyridoxal 5'-phosphate(PLP)-dependent enzyme lolC, to give the diamino diacid, NACPP . Ensuing cyclization, decarboxylation, and acetylation steps yield 1-exo-acetamidopyrrolizidine (AcAP). LolO is required for installation of the ether bridge upon the pathway intermediate, 1-exo-acetamidopyrrolizidine (AcAP) . In sequential 2-oxoglutarate- and O(2)-consuming steps, lolO removes hydrogens from C2 and C7 of AcAP to form both carbon-oxygen bonds in N-acetylnorloline (NANL), the precursor to all other lolines . The enzymes lolD, lolE, lolF and lolT have also been proposed to be involved in the ether-bridge installation . Further processing of the exocyclic moiety of NANL by fungal N-acetamidase (LolN), methyltransferase (LolM), and cytochrome P450 (LolP) enzymes, with occasional involvement of a plant acetyltransferase, generates the other known lolines . LolN transforms NANL to norlonine which is monomethylated and dimethylated to respectively lonine and N-methyllonine (NML) by lolM . LolP catalyzes hydroxylation of the methyl group in N-methylloline (NML) and further oxygenation to N-formylloline (NFL) . A plant acetyltransferase is responsible for the acetylation of loline to form N-acetylloline (NAL) . LolA might interact with aspartate kinase to prevent feedback inhibition of its activity by these end products and thereby promote production of l-homoserine from l-aspartate .
Sequence Mass (Da): 61573
Sequence Length: 540
Pathway: Alkaloid biosynthesis.
EC: 1.14.13.-
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Q5MNH6 | MTVTNKPVEPANVPVMDFEAIHASVGNERKEYLRQLDEAWSHHGAVYVINHSIGTETLEEAFVWCKKFFDLPLAVKNSVHIPPDVSKHFQGWTGTGEAISSQGVWDPDEIERLRKEMPTELKEAMELQDPCGTYPPGNPDLNLVEQHLPGYLDFLKKWFAACYKQSLQNMRLVCEILGMEDLDYIGKKFEPRHMSTHSTWNYFLGQPVSQLASGSSNRLNAHTDYCQFTMLFQDMVGGLELHDYEEDIYRPVPPIKGAMIVQVGDLLEKQTNGRWRSALHRVTAPSRYMYGGSPGGDDELVQRYSLVFFGHLNLDEMIKPLPGCEKPGKWSTLEWKDLMTAGQWLARRVALEYERKTAATVM | 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 differentiated by the various modifications of the L-amino group and include norloline, loline, N-methylloline, N-acetylloline, N-acetylnorloline, and N-formylloline . The first committed step is the condensation of O-acetyl-L-homoserine (derived from L-aspartic acid) and L-proline, probably catalyzed by the gamma-type pyridoxal 5'-phosphate(PLP)-dependent enzyme lolC, to give the diamino diacid, NACPP . Ensuing cyclization, decarboxylation, and acetylation steps yield 1-exo-acetamidopyrrolizidine (AcAP). LolO is required for installation of the ether bridge upon the pathway intermediate, 1-exo-acetamidopyrrolizidine (AcAP) . In sequential 2-oxoglutarate- and O(2)-consuming steps, lolO removes hydrogens from C2 and C7 of AcAP to form both carbon-oxygen bonds in N-acetylnorloline (NANL), the precursor to all other lolines . The enzymes lolD, lolE, lolF and lolT have also been proposed to be involved in the ether-bridge installation . Further processing of the exocyclic moiety of NANL by fungal N-acetamidase (LolN), methyltransferase (LolM), and cytochrome P450 (LolP) enzymes, with occasional involvement of a plant acetyltransferase, generates the other known lolines . LolN transforms NANL to norlonine which is monomethylated and dimethylated to respectively lonine and N-methyllonine (NML) by lolM . LolP catalyzes hydroxylation of the methyl group in N-methylloline (NML) and further oxygenation to N-formylloline (NFL) . A plant acetyltransferase is responsible for the acetylation of loline to form N-acetylloline (NAL) . LolA might interact with aspartate kinase to prevent feedback inhibition of its activity by these end products and thereby promote production of L-homoserine from L-aspartate .
Sequence Mass (Da): 41269
Sequence Length: 362
Pathway: Alkaloid biosynthesis.
EC: 1.14.-.-
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Q5MNI1 | MDLTQFNTAGIVWPTVAAIAISYILLSSFLSWYRLRHIPGPFLASISSLWNVLNIVTGRTSPVLEKLPGKYGPLVRTGPNYVLTDDAEILRHVNGARSTYPRNGWYEGFKVDEHDHMGSHIDTSVHDAIKSKVIGGYNGKDGIDLEGAIGSQVKTLVSEIRRRHLGQPVDFSRLMRQMALDAITAVAFGEALGFLTAEDGDVFGYVSAVDKMLTYLTLASDLPVVRSVVRSRRMAPAVRCVLAYTGIGRMLNHTRRVVAERYAADDPGKGDMTASFIRKGLTQIECEGESHLQLIAGADTAVTVLRSTLLYIMTTPRVYTRLKAEIKAAVDAGEVVEVITMAQAQRLPYLQAVVLEGFRMRPAVVYGHFKSVPAGGDTLPNGVRLPAGTAIAPNYIALTRRADVYGADVDLFRPERFLDAEPAKRHEMERAMDLNFGLGRWQCAGRNIALMEMNKVFFELLRHFDLQILYPGKAWDEYTGVVYSQHNMWVQITESS | 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-amino group and include norloline, loline, N-methylloline, N-acetylloline, N-acetylnorloline, and N-formylloline . The first committed step is the condensation of O-acetyl-L-homoserine (derived from L-aspartic acid) and L-proline, probably catalyzed by the gamma-type pyridoxal 5'-phosphate(PLP)-dependent enzyme lolC, to give the diamino diacid, NACPP . Ensuing cyclization, decarboxylation, and acetylation steps yield 1-exo-acetamidopyrrolizidine (AcAP). LolO is required for installation of the ether bridge upon the pathway intermediate, 1-exo-acetamidopyrrolizidine (AcAP) . In sequential 2-oxoglutarate- and O(2)-consuming steps, lolO removes hydrogens from C2 and C7 of AcAP to form both carbon-oxygen bonds in N-acetylnorloline (NANL), the precursor to all other lolines . The enzymes lolD, lolE, lolF and lolT have also been proposed to be involved in the ether-bridge installation . Further processing of the exocyclic moiety of NANL by fungal N-acetamidase (LolN), methyltransferase (LolM), and cytochrome P450 (LolP) enzymes, with occasional involvement of a plant acetyltransferase, generates the other known lolines . LolN transforms NANL to norlonine which is monomethylated and dimethylated to respectively lonine and N-methyllonine (NML) by lolM . LolP catalyzes hydroxylation of the methyl group in N-methylloline (NML) and further oxygenation to N-formylloline (NFL) . A plant acetyltransferase is responsible for the acetylation of loline to form N-acetylloline (NAL) . LolA might interact with aspartate kinase to prevent feedback inhibition of its activity by these end products and thereby promote production of L-homoserine from L-aspartate .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 54981
Sequence Length: 496
Pathway: Alkaloid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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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-amino group and include norloline, loline, N-methylloline, N-acetylloline, N-acetylnorloline, and N-formylloline . The first committed step is the condensation of O-acetyl-L-homoserine (derived from L-aspartic acid) and L-proline, probably catalyzed by the gamma-type pyridoxal 5'-phosphate(PLP)-dependent enzyme lolC, to give the diamino diacid, NACPP . Ensuing cyclization, decarboxylation, and acetylation steps yield 1-exo-acetamidopyrrolizidine (AcAP). LolO is required for installation of the ether bridge upon the pathway intermediate, 1-exo-acetamidopyrrolizidine (AcAP) . In sequential 2-oxoglutarate- and O(2)-consuming steps, lolO removes hydrogens from C2 and C7 of AcAP to form both carbon-oxygen bonds in N-acetylnorloline (NANL), the precursor to all other lolines . The enzymes lolD, lolE, lolF and lolT have also been proposed to be involved in the ether-bridge installation . Further processing of the exocyclic moiety of NANL by fungal N-acetamidase (LolN), methyltransferase (LolM), and cytochrome P450 (LolP) enzymes, with occasional involvement of a plant acetyltransferase, generates the other known lolines . LolN transforms NANL to norlonine which is monomethylated and dimethylated to respectively lonine and N-methyllonine (NML) by lolM . LolP catalyzes hydroxylation of the methyl group in N-methylloline (NML) and further oxygenation to N-formylloline (NFL) . A plant acetyltransferase is responsible for the acetylation of loline to form N-acetylloline (NAL) . LolA might interact with aspartate kinase to prevent feedback inhibition of its activity by these end products and thereby promote production of L-homoserine from L-aspartate .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20669
Sequence Length: 184
Subcellular Location: Membrane
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Q5MNH3 | MTVNSKRIPFGKPMLEAFCMDPEYTNLNSSSCGSWPKVVSKQIRDYWSLLEAQPDLFSEFYQGLVLQEARLGLARLVHAAVSECVLVSNVTTGIFTVLYNQEFEERDVVVTLSTTYGAIDHGITSLAETRSFKTRRVEFELPTTGEKIVSQFETTIAQIRAKGLRPRLAILETIVSIPAVRMPFEDLLRVCQKECIMTLVDGAHSVGQFEVNLQELHPDFFVSDCHKWLFVPRPCAFLYVAERNQHMMRSAIPTSFGFIPKNGNSQLPLWSQMVSANGTASSFETLFAYTATSDNMPHLCIPTALRFRRDVCGGEAAIYEYIKWLAKEGGDKVAEILQTEVLEEPGLGAGADGQMRDCGIVTVRLPLAIATGPSTAPAHVPGGALTEKEVGPAVRYLTKALADRYKTWIPIADCRGWIWARLCAQVYLEVSDFEMAGNALKVICEEILSREMGQEISDSYRWHD | 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 the L-amino group and include norloline, loline, N-methylloline, N-acetylloline, N-acetylnorloline, and N-formylloline . The first committed step is the condensation of O-acetyl-L-homoserine (derived from L-aspartic acid) and L-proline, probably catalyzed by the gamma-type pyridoxal 5'-phosphate(PLP)-dependent enzyme lolC, to give the diamino diacid, NACPP . Ensuing cyclization, decarboxylation, and acetylation steps yield 1-exo-acetamidopyrrolizidine (AcAP). LolO is required for installation of the ether bridge upon the pathway intermediate, 1-exo-acetamidopyrrolizidine (AcAP) . In sequential 2-oxoglutarate- and O(2)-consuming steps, lolO removes hydrogens from C2 and C7 of AcAP to form both carbon-oxygen bonds in N-acetylnorloline (NANL), the precursor to all other lolines . The enzymes lolD, lolE, lolF and lolT have also been proposed to be involved in the ether-bridge installation . Further processing of the exocyclic moiety of NANL by fungal N-acetamidase (LolN), methyltransferase (LolM), and cytochrome P450 (LolP) enzymes, with occasional involvement of a plant acetyltransferase, generates the other known lolines . LolN transforms NANL to norlonine which is monomethylated and dimethylated to respectively lonine and N-methyllonine (NML) by lolM . LolP catalyzes hydroxylation of the methyl group in N-methylloline (NML) and further oxygenation to N-formylloline (NFL) . A plant acetyltransferase is responsible for the acetylation of loline to form N-acetylloline (NAL) . LolA might interact with aspartate kinase to prevent feedback inhibition of its activity by these end products and thereby promote production of L-homoserine from L-aspartate .
Sequence Mass (Da): 51741
Sequence Length: 464
Pathway: Alkaloid biosynthesis.
EC: 4.4.1.-
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P37945 | MAEELKRSIPLLPLRGLLVYPTMVLHLDVGRDKSVQALEQAMMHDHMIFLATQQDISIDEPGEDEIFTVGTYTKIKQMLKLPNGTIRVLVEGLKRAHIVKYNEHEDYTSVDIQLIHEDDSKDTEDEALMRTLLDHFDQYIKISKKISAETYAAVTDIEEPGRMADIVASHLPLKLKDKQDILETADVKDRLNKVIDFINNEKEVLEIEKKIGQRVKRSMERTQKEYYLREQMKAIQKELGDKEGKTGEVQTLTEKIEEAGMPDHVKETALKELNRYEKIPSSSAESSVIRNYIDWLVALPWTDETDDKLDLKEAGRLLDEEHHGLEKVKERILEYLAVQKLTKSLKGPILCLAGPPGVGKTSLAKSIAKSLGRKFVRISLGGVRDESEIRGHRRTYVGAMPGRIIQGMKKAGKLNPVFLLDEIDKMSSDFRGDPSSAMLEVLDPEQNSSFSDHYIEETFDLSKVLFIATANNLATIPGPLRDRMEIINIAGYTEIEKLEIVKDHLLPKQIKEHGLKKSNLQLRDQAILDIIRYYTREAGVRSLERQLAAICRKAAKAIVAEERKRITVTEKNLQDFIGKRIFRYGQAETEDQVGVVTGLAYTTVGGDTLSIEVSLSPGKGKLILTGKLGDVMRESAQAAFSYVRSKTEELGIEPDFHEKYDIHIHVPEGAVPKDGPSAGITMATALVSALTGRAVSREVGMTGEITLRGRVLPIGGLKEKALGAHRAGLTTIIAPKDNEKDIEDIPESVREGLTFILASHLDEVLEHALVGEKK | 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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (By similarity). Has been implicated in preventing sigma(G) activity under non-sporulation conditions.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 86607
Sequence Length: 774
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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Q6ML73 | MSYVSGYVPVIPLKNSVLFPDISMPLRIGREKSIAALQKALRDNHWVILLTQKNPNASVDKIEDLYQVGTLAKVESFRMEEDGSYNIFVKAHQRVRLIHSRDSEGHIEAQTEALEDSGRLDKKTEEALLSSLRQLSDDLLDLLPGNTRQIREMIAEIEDLQTLVNMCAAYADINISDKQEILEIPLLKDRALKLLDRLQELKERLKIQRGIRDKLQESFQQNQKESILREQMRVIREELGDHEGEDLFAKFKDKIDKAGMPPEALELAKNQLRRLETSNSASPEYQMIRTHLELMTSLPWNQSSAQQDIDLEAAERVLNEDHYGLEKIKKRILQHLAVMKLRKSQQGSILMFIGPPGVGKTSLGKSIARALGKKYVRVALGGVRDDAEIRGHRRTYIGALPGRIIAGIKKAGENDPVFILDEIDKLTRGFGGDPASAMLEVLDPEQNNTFQDHYLDTPFDLSKVFFIATANSLEGIPLPLLDRMEVIDLSGYTVDEKRQIARSHLWPKQLKEHGLEENQLQITDQALTKLLTHYTREAGVRDLQRKIASICKHMSLKIIKSEGLPLLVEEQDLEDIFGAERFSADMIGSLLPPGVVTGLAWTPVGGDILFIESAQMPGKGNLLLTGQLGEVMQESAKIALTLLKSRLPLLDPLLDFAKKDIHVHVPAGAIPKDGPSAGITMLTSMASMLLNKPVDPKVAMTGEISLRGSVMPVGGIKEKVIAAHRAGVQEILLCKRNEKDLREIPEDIRKDLRFHFVEDVNEVLKITLGVNVPKWDQVQLPPPSPLSSTDAGT | 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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 88636
Sequence Length: 793
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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P47481 | MPVTKKSQILVVRGQVIFPFVPFSLDVGRPRSRKIIKALKTLKTKRLVLVTQKFTGEQNPEFNDIYHVGTLCEIDEIVDVPGVDSKTVDYRIKGRGLQRVLIEKFSDADINEVSYQLLNSTVKDEANVDRFLQRIFPEKEEIEQLMEGAEKFLELENISKTVNVPKGLKQLDIITFKLANLVPNTESIKQAILEENEIANRLEKIIQAGIEDLQKIQDYGRSKNKETEFDKLDSKITRKINEQLSRQQRDFYLREKLRIIREEIGISSKKEDEVASIRKKLDENPYPEAIKKRILSELEHYENSSSSSQESTLTKTYIDTLLNLPWWQKSKDNSDVKNLIKTLDKNHTGLDKVKERIVEYLAVQLRTQKNKGPIMCLVGPPGVGKSSLAKSIAEALDKKFVKISLGGVHDESEIRGHRKTYLGSMPGRILKGMTRAKVINPLFLLDEIDKMTSSNQGYPSGALLEVLDPELNNKFSDNYVEEDYDLSKVMFIATANYIEDIPEALLDRMEIIELTSYTEQEKIEIAKNHLIKRCLEDADLNSEELKFTDEAISYIIKFYTREAGVRQLERLIQQVVRKYIVAMQKDGIKQETIDVNAVKKYLKKEIFDHTMRDEVSLPGIVNGMAYTPTGGDLLPIEVTHVAGKGELILTGNLKQTMRESANVALGYVKANAERFNINPSLFKKIDINIHVPGGGIPKDGPSAGAALVTAIISSLTGKKVDPTVAMTGEITLRGKVLVIGGVKEKTISAYRGGVTTIFMPEKNERYLDEVPKEIVDKLNIIFVKEYSDIYNKLFS | 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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 89988
Sequence Length: 795
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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Q6MTF4 | MLQYLKKIKGVSFMKTIKLPVVVTRGIFILPSTSKTIEFGRVKSKNALDASADLYNNQIVVVSQESPLEEEPNLEHLFYLGTVADLSVKKVWKDGTISVELNYNQKIKIDEFVEEDNIIYAIGSVFEDKLPKTDAQKTKIKEALEELQEKHSFNTSELLLVFNENDFNKLNSLIYQIIDKMPLVSLNTKLLLIQSTSILEKLELLKELIINRPKSTIKLNNNLNNNSTVDSEINKKLKDKMDKQQKEYYLREKMRIIKEELDDENSDASQLDKYKKRLEEEPFPESVKEKILSSIKRIETMQPGSAEVNVERNYVDWMMSIPWWEQSEDIDDLKYAQEILEKHHFGLKKVKERIIEYLAVKQKTKSLKGPIITFVGPPGVGKTSLARSIAEALGKKFVKVSLGGVKDESEIRGHRKTYVGSMPGRIIQALKRAKVKNPLFLLDEIDKMASDNRGDPASAMLEVLDPEQNKEFSDHYIEEPYDLSTVMFIATANYIENIPEALYDRMEIINLSSYTEIEKMHIAKDYLTKKILEEDQLTEDELRFTDEAYDEIIKYYTREAGVRQLERHLATIARKFIVKLLNGEITNLVVTREVVVQYLGKHIFEHTSKEEESQVGVVTGLAYTQFGGDILPIEVSTYNGKGNLTLTGKLGEVMKESATIALTYVKANHEKFGISKDKFDDIDIHIHVPEGAVPKDGPSAGITLTTALISALSKQPVSKDFGMTGEITLRGNVLPIGGLREKSISAARSGLKHILIPSKNVKDIEDVPQEVQDVLKITPVSKYEDVYEIIFKNNNQ | 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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 90443
Sequence Length: 796
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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Q4A696 | MQKKQTLNYVIVKTDEISFPFGYSEVLILEQDSIELLETTKFKFKNEDRLVIVYAEDVYTEEVKFLQRGLYIKPLDAKEVMYQGEKALILTFKALHFFDIQNFSYEMNQDEIMSANFLVDGNAKGTVGYEMVLSGHINNVEDVKENLMNEFRQDQNKMNFFSIFETLVNNSNSFGISTNNQAGTAMLFKQNYGAKDEVKPYDIEEIKALIDSKITQDNDPSEFLLNNFESLMTYFGFLDLNKFPHKWHLYNSFDYGNFTRLINEVGNFIQTALKLEENITSEISKKLNNQQKEFMLREKRKVIDDELAKLGKDTLQDDKDEYVKKLKNKTLKKMYPDSIKEIIRDETKRYSEMMQASPEANLVKNYVEYLKKLPWRKVSKDRLDIKYAREVLEKYHYGIKEVKERILEHLGVLINAQTYNKNYKNEVVSIDENYEIDLNLFKDKPSEKTVFNNVPILALVGPPGTGKTTLAKAISEALNKKYVKISLGGVKDESEIRGHRRTYVGAMPGKIVKGVAKAGVSNAVFLLDEIDKMASDHKGDPASAMLEVLDPEQNAQFQDHYLEQEYDLSKIIFIATANYFQNIPEALIDRVEVIELDPYTLNEKVQIAQKHLIPKVINEVYLDEKLFNIPEETLRFIINRYTREAGVRGLKRILDKIARKIVIKRVLEPDLKSFDISLNNLEELLGVAPYKTDEDKHDEIPGIATGLAYSTHGGSDLEIEVNVFKSEKGGIQLTGSLKDVMKESAQIALTYVRSNAKYFGIHSFDFDKHTIHIHVPEGATPKDGPSAGVTFTTAIISALTRLPVPNNYAMTGEITLQGKVLPIGGLKEKSFAAYWKKIKYVFIPHANIDNLQKIPDEIKREITYIPVKRYDEIFQILFRDQKPENTITFN | 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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (By similarity).
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 102244
Sequence Length: 890
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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O31147 | MAEAKTVPVLFLNDSIVLPGMVVPIELDDAARAAVDAARASESGELLIAPRLEDRYPAYGVLASIVQIGRLPNGDAAAVVRGERRAHIGSGTSGPGAALWVQVEEVTDPEPTDETKKLAGEYKKLLLAMLQRRDAWQIVDMVNKITDPSALADTAGYASYLTGTQKRELLETTDVDRRLSLLIGWTGDHLAETEVNDKIAEDVRTGMEKQQKEFLLRQQLAAIRKELGELDDNGDGSSDDYRARIEQADLPEKVREAALREVGKLERASDQSPEGGWIRTWLDTVLDLPWNVRTEDSTDLARAREILDTDHHGLSDVKDRIVEYLAVRGAAPQRGMAVVGGRGSGAVMVLAGPPGVGKTSLGESVARALDRKFVRVALGGVRDEAEIRGHRRTYVGALPGRIVRAIGEAGSMNPVVLLDEIDKVGSDYRGDPAAALLEVLDPAQNHTFRDHYLDLDLDLSDVVFLVTANVIENIPSALLDRMELVEIDGYTADDKLAIAQGFLLPRQRERGGLTSDEVTVTEAALRKIAADYTREPGVRQFERLLAKAMRKAATKLADHPQAAPITIDEPDLVEYLGRPRFLPESAERTAVPGVATGLAVTGLGGDVLYIEANSTEGEPGLQLTGQLGDVMKESAQIAMSYVRAHAKQLGVDPEALNRRIHIHVPAGAVPKDGPSAGVTMVTALVSMATGRKVRGDVGMTGEVTLNGRVLPIGGVKQKLLAAQRAGLSTVFIPQRNQPDLDDVPADVLDALDVRPMTDVADIIAAALEPAHEASTAAAA | 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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 83676
Sequence Length: 779
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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Q2GE60 | MSEEELNNRDTESKQEHDENNSNFEAGSAHMNLPVLPLREVIFFPGDYLPIFIGRKGSIQAMDKALAETSENTGRMLLIAQKNPKKEIPEGKDLYEVGVIAKIAEPKINLQDGGVKLMVIVECRARAVNFRKSEGVLEADVLPIEEEESDNVDIEAYRRAVVQNFEKCVKLSETIPDEIIGLLSQIDSTSRIADLVTASINLKLSVKQEILETVDLLERIKKVHALLEKELGVLQVKQQIKEKTESQIKKSHKVYLLNEQLKAITKELYDKEGEEYDELVDLEKKIGNGKLSAEAKEKVSKELKKLKNMVPMSAEATVVRNYVDWIISLPWKKKGKMITDIAASERILKASHYGIEKVKERIIEYLAVQNRTKSFKGSILCLLGPPGVGKTSLASAIAEATGRPFVRMSLGGIKDESEIKGHRRTYIGAMPGKIIQHMKKAKLSNPVFLLDEIDKMSSDFRSDPAFALLEVLDPEQNAHFVDHYLEVEYDLSDVMFVATANSLNMIPALLDRLEIIRLEAYSEEEKLQIAEHYLIGKLQREHGLKKSEWSISKEALKLLIRRYTRESGVRNLKRELANLMRKAVKKLGVQSGLKSIEVSVKNLKKYAGVEKYTFGTAEPENLVGMTTGLAYTQTGGDLIMIEAVLLPGKGEIRSTGKLGEVMQESVQAAYSFVCSNCNKFGFTSKFFKSKDVHLHVPEGATSKDGPSAGVAICTSIVSVMTGIPVRSNVAMTGEVSLRGKVMEIGGLKEKLLAAVRGGIKIVLIPASNEKDLENIPKSVKNAVRIIPVSTVSEALTFTLAEQPTPLAVDVWPDIPLSSTQQSEQRV | 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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 91692
Sequence Length: 826
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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Q3JBB6 | MENNAYPTLPLKNTVLFPHLVLPLSVGRAGSIAAVEAALSSEDKLIAVFPQKDPRTDEPAADDLFRFGTVGIIKKMVRSEDTVQILVQGIERVEQLEMVQKQPYLSLKIATLSEPSDTGTEIEALHRTVIELAGKMIELVQPQIQVGIHHIISDVEKPLHQIYLLTSILSLDFDKEKELLAAATQVEALQLMHRYLNHEVQVLEVRQKITSTAQTEIDKKQREYVLRQQLEAIQEELGETNPEQAEIKELRQRMEETELPELVRKEVEKEITRLERMPSAAPDYQLTRGYVELALELPWNKTTEDRLDLKRAREILDEDHFDLEDVKERIIEHLAVMKLNPEAKSPILCFVGPPGVGKTSVGQSMARALGRKFERMSLGGLHDESELRGHRRTYIGAMPGRIIRAIRRTGYQNPLLMLDEIDKLGRDFRGDPAAALLEILDPAQNAEFHDNYLDLPFDLSKIFFVTTANTLDTIPRPLLDRMEILRLPGYSDEEKQHIARRYLIGRQIREAGLSEIQLSIPDETLSYLIRRYTREAGVRELERMLGRIARKVATQVATGQTQPVTVTPQDLVELLGPERFFAEEMRQQLAPGVAAGLAWTEAGGDVLYVEAALLPEGKGMTLTGQLGSIMQESAKAAQSYLWSRAEELNIDQKTIRESGVHIHVPAGAIPKDGPSAGVTMASALTSAYAHQPVRSDTAMTGEITLSGLVLPVGGIKEKVLAAHRSGIQRIILPKENEKDLREIPEHVRQSIQFILARRIEEVLAEAIPDLNR | 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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 86604
Sequence Length: 772
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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B3CUN9 | MAQVLNDISNRVLPLFPIRNTVLFPGLVLPILIGRDDSVKNLLRLGNDSENQHTILLTTQKNADDIKPSINSLYKIGVLAKITELVQLPNDNYKILIKVLDRVKLTIRRSHDLLVAEYVIVPDDEINNADEIKDKLANAIVLFNKYIRLSKKINPDLLVHVLSYTNQSYVVNALAANLICNVANKQSLLEITDVKQRIERLTDHVAKEIIIMETDELITSKAQKNLEKMQRDCFLNEKMKIIKNVLGVDDEKSDIAELQKKIDTLHLSKEAKAKAESELKKLKMMNPISAEAALTRNYLDILLGLPWKKEKESKININIDKALQDLNADHHGLEKVKERITEYLAVLQRTKKSIGTILCFIGPPGVGKTSLVKSIAEATKCKYAKFALGGVRDEAEIRGHRKTYIGAMPGKIISLIKRENSNNLVILLDEIDKISRDSRGDPAFALLEVLDPEQNSRFQDNYLEVEYDLSKVLFIATANSFNFPIPLRDRMEIIQIPGYVEGEKLEIAKHHLIPKQIKNNGLKNTEISFSDEAILELIRYYTREAGVRGLERKIGGICRKVLKKILSSKDIKSESVSKENIKDYLGSRKYKYGLAEDDNQVGITIGLAYTETGGDLIWVEAVMIPGKGKVKATGKLGDVMKESSQTAFSYFCSRAQKYNVKYEQYHKYDIHIHFPEGAIPKDGPSAGIAIFTTIVSLMTGIPVKLSVAMTGEITLRGRILPIGGLKEKLMAAKRGGIKTVIIPEGNTSDLEDIPNSIKNDLDIIPLSEADQVLDIALATTVTNSPAETAC | 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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 88221
Sequence Length: 790
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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A6LD45 | MNVYMKEKTRVFCQNSFDDLDDNIGIVMPILTECDVDEDFTEGIEKVGDTIPILPLRNMVLFPGVALPVIIGRPKSMRLIKEAVHKKSLIGVVCQKEMGTEDPILEDLYTTGVIADIVRVLEMPDGSTTVILQGKKRFELNELTETDPYLSGKITVLEDTKPDKTDREFEALISTIKDLTIKMLGAVAEPPRDLIFSIKNNKNVLYVVNFSCSNIPSGSAEKQQLLLIGDLKERAYRLLFILNREYQLVELKASIQMKTHEDINQQQKEYFLQQQIKTIQEELGGNINELEIKELREKASRKKWPAEVAQVFEKELRKLERLHPQSPDYSVQTQYVQNIVNLPWNEYSKDNFNLSHAQKVLDRDHYGLEKVKERIIEHLAVLKLKGDMKSPIICLYGPPGVGKTSLGRSIAEALRRKYVRVSLGGLHDEAEIRGHRRTYIGAMCGRIIQNIQKAGTSNPVFILDEIDKITNDFKGDPASALLEVLDPEQNNAFHDNYLDIDYDLSKVMFIATANNLNTISQPLLDRMELIEVSGYIMEEKVEIAAKHLVPKQMDVHGLKKGSVKFPKKTLQVIVEAYTRESGVRELDKKIAKIMRKLARKVASDEPIPTSIKPEDLYEYLGAVEYSRDKYQGNDYAGVVTGLAWTAVGGEILFVESSLSKGKGSKLTLTGNLGDVMKESAMLALEYIHAHAAQFNINEELFENWNVHVHVPEGAIPKDGPSAGITMVTSLVSAFTQRKVKKNLAMTGEITLRGKVLPVGGIKEKILAAKRAGIKELILCKENEKDINEIKPEYLKGLVFHYVSDIQQVVDLALLREKVDNPLF | 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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 92725
Sequence Length: 823
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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B2TFQ5 | MSADSENETSESSPAGEATASTSALPDEPLILLPVRNAVLFPGMVLPFTAGRGQVKEDVQAAVKRQQPLGVVLQRDPRVQDPTFDDLNTIGTVANVVRYVTSPEDGAHHLICQGVERFRLIAPVEGLGFRAARVEFLPETTARNPAVDARALVLRQRAGEMIGLLPNAGGELVRALDAIELPGLLADTIAGLLDIPPERKQEILETLDVCKRLDKVLDAVAGRIEVLRLSQEIGEQTRGRIDQRQREMMLREQLRTIQNELGENIESREEVRKLTEAIEAAHMPPEVESHARKELGRLERMPEASSEYSISVSYLEWLTELPWPLPAEAPIDIARARQILDEAHFGLDKVKRRILEYLGVRKLNPHGKAPILCFLGPPGVGKTSLGQSIARALERPFVRVSLGGVHDEAEIRGHRRTYIGAMPGNIIQAIRKAGARNCVMLLDELDKLGQGVHGDPAAAMLEVLDPEQNASFRDNYLGVPFDLSAIVFVATANQIEGIAGPLRDRMEILDLPGYTEAEKFQIAQRFLVPRQLEACGLTAAQCELPDETLRAIIRDYTREAGVRSLERQIGAVFRYVALRVAEDPSTHERIEPDRLSSILGHRRFESEVAMRTSLPGVVTGLAWTPVGGDLLFIEASSTPGGGRLVLTGQLGDVMKESVQAALTLVKSRCESLHIDCSNFDKRDIHVHVPAGAVPKDGPSAGVAMFIAIASLLMGRAVRSDCAVTGEISLRGIVLPVGGIKEKVLAALRGGIKTVLLPARNAPDLEDIPVDARNQMRFVLLETVDDAVREIIEDESVTSSRNVDI | 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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 87789
Sequence Length: 804
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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Q6ME13 | MLEEPIDALETEFENALNSLEDNQLSKINGQLPEQVHVFPLLRRPFFPGMAAPLVIEPGPFYEVLKVVAKSDHKCVGLVLTRSEQAEIYKVGFSDLYQIGVLARVLRIIPMEQGGAQVILNMERRIKIEKPTSETKTLKANVSYIEDDPILTTELKAYAISILSTIKELLKLNPLFKEELQIFLGHSDFTEPGKLADFAVALTTASREELQDVLETFDIRKRIDKALILLKKELDISILQHNINQKIEATINKSQKDFFLREQLKTIKKELGIERDDKSLDREKFEARLKERVVPSDVMKVITEELEKLSVLDMQSAEYSVVRGYLDWLTTIPWGIYSQENHNLEEAEKILAHDHYGLEDIKQRILEFIGVGKLAKGVRGSIICLVGPPGVGKTSIGKSIARALNRKFYRFSVGGMRDEAEIKGHRRTYVGAMPGKMIQALKYCQTMNPVIMLDEVDKMGKSFQGDPASALLEVLDPEQNAEFLDHYLDVRCNLSEVLFIVTANVLDTIPEPLKDRMDILRLSGYIMQEKLEIAKKYLIPRNRKEMGLKALEVSFTQEALRSIINGYARESGVRNLENLLKKILRKLAVNIVREQEEHDKEQAKKKKSSRSKKPIAFVPTKHSITPSNLKDFLGKPVFTSDRFYERTPVGVCMGLAWTAMGGATLYIESIKVAGEKTVMKLTGQAGDVMKESAEIAWSYVHSSIHKYAPGYTFFEKSQVHIHIPEGATPKDGPSAGITMVTSLLSLILDTPVLDNLGMTGELTLTGRVLPIGGVKEKLVAARRSGLKVLIFPKDNLRDYEELPEYIRKGITVHFVDHYDQVFKISFPNKHQMKLC | 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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 94306
Sequence Length: 835
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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B4RI01 | MNGEQSANGARTLPDDAVVVVPVSNVIFPGVVFPIVLDRPSAVAAAQQALREQHPLVLVLQQDVQAPDPGPQSLHRMGTLANVLRYVTGPDGAPHVACQGVERFEIDEWVEGFPFLVARGRRIPEPEAEGAAIEARFLHLRSQALEALQLLPQSPPGELVAAVEGASSPAALADLVAAYLDLQPPEKQQILETIDLEARLDKVSAFLAQRLEVLRLTSEIAQRTRQSLGERQRETLLREQMAAIQRELGEGEREELVELEAAIENAGMPEEVVQQARKELRRLARTPEAAAEYGMVRTYLEWLVELPWGVPEAAPIDLAEARRILDEDHFGLEKIKQRIIEHLAVRRLAPEGKAPILCFVGPPGVGKTSLGQSIARAMHRPFVRVSLGGVHDESEIRGHRRTYVGALPGNIIQAIRKAGRRDCVMMLDEIDKMSAGIHGDPSAALLEVLDPEQNVAFRDNYLAVPFDLSRVVFIATANMLDTIPGPLRDRMEVIQLSGYTAGEKRQIAERYLVRRQLEANGLTAEQVQIEPAALETLIARYTREAGVRSLEREIGRLLRHVAVRFAEGHTEPVRIGPTNLEPILGPPRVENEVAMRTSVPGVATGLAWTPVGGEILFIEATRTPGDGRLILTGQLGEVMRESAQTALSLVKSRAEALGVTPSLFKESDIHIHVPAGATPKDGPSAGVAMTMALISLLTDRTVRSDTAMTGEISLRGLVLPVGGIKEKVVAAATAGVRRVLLPARNRADERDIPEETRQTLELIWLERIEDAIEAGLDPRRGDVRQTQVRAAS | 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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 86499
Sequence Length: 792
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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B2RII6 | MIDRKYIRLGEDDEDDGFPVFFPVLSVCEEDEDFKVKEDHMQEEMPILALRNMILFPGVAMPIMVGREKSLKLIRYVEKKGVYFGAVSQRDMDVEEPDRADLYDVGVVAEIIRVLEMPDGTTTAIVQGRQRFALQEITATEPFMKGRVKLLPDILPGKNKDHEFEALVSTIQDMSLKMMELMVERPPRELILSMRRNKNPMYQINFASANISTSIAVKQELLEISKMKDRGYRLLYLLHKELQVMELKASIQMKTREEMDKQQKEYFLQQQIKTIQEELGGNINDIEVQELRTKATTMKWSSEVAETFEKELRKLERLHPQSPDYSVQMQYVQTIISLPWGVFSKDNFNLKRAQSVLDRDHFGLEKVKERIIEHLAVLKMKGDMKSPIICLYGPPGVGKTSLGKSIAESLGRKYVRISLGGLHDEAEIRGHRRTYIGAMCGRIIQSLQRAGTSNPVFVLDEIDKIDSDYKGDPSSALLEVLDPEQNNAFHDNYLDIDFDLSHVLFIATANSLSSISRPLLDRMELIDVSGYIIEEKVEIAARHLIPKQLVEHGFRKNDIKFSKKTIEKLIDDYTRESGVRTLEKQIAAVIRKITKEAAMNVVHTTKVEPSDLVTFLGAPRYTRDRYQGNGDAGVVIGLAWTSVGGEILFIETSLHRGREPKLTLTGNLGDVMKESAVIALDYIRAHSDELGISQEIFNNWQVHVHVPEGAIPKDGPSAGITMVTSLVSALTRRKVRAGIAMTGEITLRGKVLPVGGIKEKILAAKRSGITEIILCEENRKDIEEINDIYLKGLKFHYVSNINEVLKEALLEEKVIDTTDIYSFGKKTEEEKAEKVEKTEKKQRKK | 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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 95966
Sequence Length: 845
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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A8F811 | MSTKFEKLEKLARESFQSPEVPETLPLIHLRNGMIIFPQTVVPVHVAREKTLLALEQSIESYQQFVFVTSQKDPSVEEPSFDQLYEIGTVSKVLQVVQLPDGSFRVLLEGLERARAYEVVQDNPFLVKLEILKVNYRKTKKLEALIRSVRESFAKYAYYTQRYSQETLSAMSEISDANRLADFVASLLPLQLKQRQSLLEQLKPAKRLEMILEILSHENEILEIERELDTKVKKRIEENQKEFFLREKLKAITEELGEKDTEADQLKARLQKLKLPEHAKQKATLEIERLEKMSPYSAEATVIRTYLDWLFNLPWDNSTEDRQDISQAEKILQASHYGLKEAKERILEFLAVRKRSNSVKAPILCFVGPPGVGKTSLARAVSQALNRKFAHMSLGGLRDEAEIKGHRRTYVGAMPGRILQLIRTAQSKNPVLLLDEIDKMAVSFQGDPAAALLEVLDPEQNKEFVDHYLEIPFDLSNVLFITTANVTHTIPPALLDRMEIIELEGYTDYEKSIIARQYIIPKLMGENALNEATFKITQGAIKKIIHTYTREAGVRQLTRMLQRLMRKSALKIEQGAKSVVIKSKDLEHFLGPQPVQNDIMLSKPEIGAVHGLAWTEYGGVVMVVESLLMPGKGDLILTGRLGEVMRESARIALSVARSFCGQDCKEKFQQSDIHINLPEGAVPKDGPSAGITMTVAMISSVLGKPVRNDTAMTGEITLRGKILAVGGVKEKILAAHRHGIKRILLPKTNEKDLKRIPPQVKDKMEFIFVEDIEKAVEKSCS | 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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 88290
Sequence Length: 781
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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O69177 | MTNKTSPATESATYPVLPLRDIVVFPHMIVPLFVGREKSIRALEEVMGTDKQIMLVTQINATDDDPEPSAIYKVGTIANVLQLLKLPDGTVKVLVEGRSRAEIERYTPRDDFYEAMAHALPEPDEDPVEIEALSRSVVSEFESYVKLNKKISPEVVGVASQIEDYSKLADTVASHLSIKIVEKQEMLETTSVKMRLEKALGFMEGEISVLQVEKRIRSRVKRQMEKTQREYYLNEQMKAIQKELGDSEDGRDEMAELEERISKTKLSKEAREKADAELKKLRQMSPMSAEATVVRNYLDWLLGLPWGKKSKIKTDLNHAEKVLDTDHFGLDKVKERIVEYLAVQARSSKIKGPILCLVGPPGVGKTSLAKSIAKATGREYIRMALGGVRDEAEIRGHRRTYIGSMPGKVVQSMKKAKKSNPLFLLDEIDKMGQDFRGDPSSALLEVLDPEQNSTFMDHYLEVEYDLSNVMFITTANTLNIPPPLMDRMEVIRIAGYTEDEKREIAKRHLLPKAIRDHALQPNEFSVTDGALMAVIQNYTREAGVRNFERELMKLARKAVTEILKGKTKKVEVTAENIHDYLGVPRFRHGEAERDDQVGVVTGLAWTEVGGELLTIEGVMMPGKGRMTVTGNLRDVMKESISAAASYVRSRAIDFGIEPPLFDKRDIHVHVPEGATPKDGPSAGVAMATAIVSVMTGIPISKDVAMTGEITLRGRVLPIGGLKEKLLAALRGGIKKVLIPEENAKDLADIPDNVKNSLEIIPVSRMGEVIAHALLRLPEPIEWDPASQPAALPSVDSQDEAGTSIAH | 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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (By similarity). In R.meliloti it is important for controlling the turnover of a constitutively expressed protein(s) that, when unregulated, disrupts normal nodule formation and normal growth.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 89458
Sequence Length: 806
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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Q92HZ1 | MHKKSLPLMALRDMVVFPGVIAPIFVGRPKSLQALSHTTISEEDNSKYILVTLQKKFDQENPSTHELYNTAILAKIIQIVKLPNNTAKILIEAVARVKLSNIKGEEAFEANYEIIPDEEIFDVNNMRSLVDNAVQLFSKYAINDKKVNAEIIETINKEISNSTNFIDIINILASHLITSLEAKQHLLEETSPFKRITTVISMLNSNIVNSETEQALQKRVRKQIEKTQRDYYLHEQMKAIQKELDEDKSELADIENKIKSLKLSKEAKEKAEAELKKLRTMNQMSAESGVTRNYLETLLSLPWGKYDNSKIDINQAEKILNRDHFGLEKVKERIIEYLAVLQRSSKIRGPILCLIGPPGVGKTSLVKSIAEGMGRKYTKLALGGVRDEAEIRGHRKTYLGSMPGKILGQLKKVKTSNPVMLLDEIDKMSSDFRGDPASALLEVLDPEQNSHFVDHYLEVEYDLSNVIFIATANSHDLPRALSDRMEKIYISGYVEETKLQIARNYLVPKQFKMHKIKKDEITISETAILDLIRYYTKESGVRALEREIGALTRKALKQILADKSVKHIAIDSNHLEEFLGAKKYNFGLAEKEDQIGSTTGLAYTEVGGELLTIEALAFPGKGEIKTTGKLGDVMKESAMAAYSCFRSRATNFGLKYDNYKDFDIHIHVPAGAIPKDGPSAGCALFTTIVSLMTKIPVHRTVAMTGEITLRGNVLPIGGLKEKLLAASRGGIKTVLIPEENVKDLKDIPPNIKESLEIISVSNIDQVLKHALVGTPINK | 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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Catalytic Activity: Hydrolysis of proteins in presence of ATP.
Sequence Mass (Da): 87000
Sequence Length: 778
Subcellular Location: Cytoplasm
EC: 3.4.21.53
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Q06327 | MFGELRDLLTGGGNETTTKKVKGTVVLMKKNVLDFNDFNASFLDRLHEFLGNKITLRLVSSDVTDSENGSKGKLGKAAHLEDWITTITSLTAGESAFKVTFDYETDFGYPGAFLIRNSHFSEFLLKSLTLEDVPGHGRVHYICNSWIYPAKHYTTDRVFFSNKTYLPHETPATLLKYREEELVSLRGTGEGELKEWDRVYDYAYYNDLGVPPKNPRPVLGGTQEYPYPRRGRTGRKPTKEDPQTESRLPITSSLDIYVPRDERFGHLKMSDFLAYALKAIAQFIQPALEAVFDDTPKEFDSFEDVLKIYEEGIDLPNQALIDSIVKNIPLEMLKEIFRTDGQKFLKFPVPQVIKEDKTAWRTDEEFAREMLAGLNPVVIQLLKEFPPKSKLDSESYGNQNSTITKSHIEHNLDGLTVEEALEKERLFILDHHDTLMPYLGRVNTTTTKTYASRTLLFLKDDGTLKPLVIELSLPHPNGDKFGAVSEVYTPGEGVYDSLWQLAKAFVGVNDSGNHQLISHWMQTHASIEPFVIATNRQLSVLHPVFKLLEPHFRDTMNINALARQILINGGGIFEITVFPSKYAMEMSSFIYKNHWTFPDQALPAELKKRGMAVEDPEAPHGLRLRIKDYPYAVDGLEVWYAIESWVRDYIFLFYKIEEDIQTDTELQAWWKEVREEGHGDKKSEPWWPKMQTREELVESCTIIIWVASALHAAVNFGQYPVAGYLPNRPTISRQYMPKENTPEFEELEKNPDKVFLKTITAQLQTLLGISLIEILSTHSSDEVYLGQRDSKEWAAEKEALEAFEKFGEKVKEIEKNIDERNDDETLKNRTGLVKMPYTLLFPSSEGGVTGRGIPNSVSI | 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 wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Function as regulators of root development by controlling the emergence of lateral roots . 9S-lypoxygenase-derived oxylipins may play an antagonistic role to ethylene signaling in the control of responses involving oxidative stress, lipid peroxidation and plant defense . LOX1-derived oxylipins may be involved in stress signaling from roots to shoots in response to cadmium exposure . 9S-lypoxygenase-derived oxylipins are engaged during infection to control the balance between salicylic acid (SA) and jasmonate (JA) signaling to facilitate infection by the fungal pathogen Fusarium graminearum . 9S-lypoxygenase-derived oxylipins activate brassinosteroid signaling to promote cell wall-based defense and limit pathogen infection . The LOX1-derived compound (9S)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoate protects plant tissues against infection by the bacterial pathogen Pseudomonas syringae pv tomato DC3000 . The LOX1-derived oxylipins are required to trigger stomatal closure in response to both infection by the bacterial pathogen Pseudomonas syringae pv tomato DC3000, and the pathogen-associated molecular pattern (PAMP) flagellin peptide flg22 . Contributes to the oxidation of free fatty acids during seed aging .
Catalytic Activity: (9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-octadecadienoate
Sequence Mass (Da): 98045
Sequence Length: 859
Pathway: Lipid metabolism; oxylipin biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.13.11.58
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Q76I22 | MLGGLKDKLTGKNGNKIKGLAVLMSRKLLDPRDFTASLLDNVHEVFGNSITCQLVSATVADQNNEGRGIVGSEANLEQGLTDLPSVSQGESKLTVRFNWEMDKHGVPGAIIIKNHHSTKFFLKTITLHDVPGCDTIVFVANSWIYPVGKYHYNRIFFANNSYLPSQMPEALRPYREDELRYLRGEDRQGPYQEHDRIYRYDVYNDLGEPDRDNPRPVLGGSQKHPYPRRGRTGRIPTKKDPNSESRLSLLEQIYVPSDERFAHLKMSDFAGYSIKAIVQGILPAIRTYVDLTPGEFDSFEDILKLYRGGLKLPSIPALEELRKSFPVQLIKDLLPVGGSYLLKFPKPDIIKENEVAWRTDEEFAREILAGLNPMVIRRLTEFPPKSTLDPSKYGDQTSTITPAHIEKNLEGLSVQQALDSNRLYILDHHDHFMPFLIDINSLDGIFTYATRTLLFLRDDDTLKPLAIELSLPHIEGNLTSAKSKVHTPASSGIESWVWQLAKAYVAVNDSGWHQLISHWLNTHAVMEPFVIATNRQLSVTHPVYKLLQPHYRDTMTINALARQTLINGGGIFEQTVFPGKHALAMSSAVYKNWNFTEQGLPDDLIKRGIAIKDPSSPSKVKLLIKDYPYATDGLAIWQAIEQWVTEYCAIYYPNDGVLQGDVELQAWWKEVREVGHGDLKDADWWPKMQSLPELTKACTTIIWIASALHAAVNFGQYPYAGYLPNRPTISRRPMPEPGSKEYTELDENPEKFFIRTITSQFQTILGVSLIEILSKHSADEIYLGQRDTPEWTSDPKALEAFKRFSRQLVEIESKVLNMNKDPLLKNRVGPANFPYTLMFPNTSDNKGAAEGITARGIPNSISI | 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-9 position of linoleic and linolenic.
Catalytic Activity: (9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-octadecadienoate
Sequence Mass (Da): 97499
Sequence Length: 863
Pathway: Lipid metabolism; oxylipin biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.13.11.58
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P08170 | MFSAGHKIKGTVVLMPKNELEVNPDGSAVDNLNAFLGRSVSLQLISATKADAHGKGKVGKDTFLEGINTSLPTLGAGESAFNIHFEWDGSMGIPGAFYIKNYMQVEFFLKSLTLEAISNQGTIRFVCNSWVYNTKLYKSVRIFFANHTYVPSETPAPLVSYREEELKSLRGNGTGERKEYDRIYDYDVYNDLGNPDKSEKLARPVLGGSSTFPYPRRGRTGRGPTVTDPNTEKQGEVFYVPRDENLGHLKSKDALEIGTKSLSQIVQPAFESAFDLKSTPIEFHSFQDVHDLYEGGIKLPRDVISTIIPLPVIKELYRTDGQHILKFPQPHVVQVSQSAWMTDEEFAREMIAGVNPCVIRGLEEFPPKSNLDPAIYGDQSSKITADSLDLDGYTMDEALGSRRLFMLDYHDIFMPYVRQINQLNSAKTYATRTILFLREDGTLKPVAIELSLPHSAGDLSAAVSQVVLPAKEGVESTIWLLAKAYVIVNDSCYHQLMSHWLNTHAAMEPFVIATHRHLSVLHPIYKLLTPHYRNNMNINALARQSLINANGIIETTFLPSKYSVEMSSAVYKNWVFTDQALPADLIKRGVAIKDPSTPHGVRLLIEDYPYAADGLEIWAAIKTWVQEYVPLYYARDDDVKNDSELQHWWKEAVEKGHGDLKDKPWWPKLQTLEDLVEVCLIIIWIASALHAAVNFGQYPYGGLIMNRPTASRRLLPEKGTPEYEEMINNHEKAYLRTITSKLPTLISLSVIEILSTHASDEVYLGQRDNPHWTSDSKALQAFQKFGNKLKEIEEKLVRRNNDPSLQGNRLGPVQLPYTLLYPSSEEGLTFRGIPNSISI | 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 the site for hydroperoxidation (in contrast to L-2 and L-3, which utilize either carbon 9 or 13). At pH above 8.5, only (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate is produced, but as the pH decreases, the proportion of (9S)-hydroperoxide increases linearly until at pH 6.0 it represents about 25 % of the products.
Catalytic Activity: (9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-octadecadienoate
Sequence Mass (Da): 94369
Sequence Length: 839
Pathway: Lipid metabolism; oxylipin biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.13.11.12
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R9WTS6 | MALAKQIMGASLMDQKTSVFGSNLCLNHVLVNKHRLRLRKTRKNGSMVVAAISEDLVKLXRVEKEKPVTFKVRAVLTVRNKNKEDFFKDTIFRKIDAITDQIGWNVVIQLFSNDIDPRTRAAKKSNEAVLKDWSKKSNVKTERVNYTADIMVDSDFGIPGAITISNKHQKEFFLETITIEGFACGPVHFPCNSWVQSTKDLPNPRIFFTNQPYLPDETPVGLKSLRYQELKDLRGDGTGVRKLSDRIYDYDVYNDLGNPDRGNDFVRPTLGGEKIPYPRRCRTGRVPSDTDITAESRVEKPFPLYVPRDEQFEESKANAFSTGRLRAVLHNLLPSMVTSISKKNDFKGFSQIDSLYSEGVFLKLGLQDDLLKKLPLPNLVTRLHESSQGGGLLKYDTPKILSKDKFAWLRDDEFARQTIAGVNPVSIEKLKVFPPVSQLDPEKHGPQESALREEHIVGFLDGRTVKQAIEEDKLFIIDYHDIYLPFLDRINALDGRKAYATRTIFYLNPSGTLKPVAIELSLPQALPGSESKRVLTPPSDATSNWMWQLAKAHXCSNDAGAHQLVHHFLRTHAAIEPFILAAHRQLSAMHPIYKLLDPHMRYTLEINQLARQNLINADGVIEACFTPGRYGMEISASAYKNWRFDLEGLPADLIRRGMAVPDPSKPHGLKLVMEDYPYASDGLMIWEAIQNWVKTYVNHYYPDSAQVCNDRELQAWYAESINVGHADLRHKDWWPTLAGADDLTSVLTTIIWLASAQHAALNFGQYPYGGYIPNRPPLMRRLLPDVNDPEYLSFHDDPQKYFLSALPSLLQSTKYMAVVDTLSTHSPDEEYIGERQQTDTWSGDAEIVEAFYAFSAEIQRIEKEIEKRNSDTSLKNRCGAGVLPYELLAPSSGPGATCRGVPNSISI | 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 responses to wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure (By similarity). Mediates the peroxidation of linolenic acid leading to the production of 13-hydroperoxylinolenic acid .
Catalytic Activity: (9Z,12Z,15Z)-octadecatrienoate + O2 = 13-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate
Sequence Mass (Da): 102462
Sequence Length: 907
Pathway: Lipid metabolism; oxylipin biosynthesis.
Subcellular Location: Plastid
EC: 1.13.11.-
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P93184 | MLTATKPLVGGACAAPSSSARRRTFVVPEARRKPGNGRRTSVSKVGSTSTSTTTTTTTTLSADSNGAAVGTVTRPDVHVQDRTHATEMKATVTVHMSKAAGVRDFLYDLILKTWLHVDLVSSELDPQTGQEREPISGAVKHSGRVDDEWDMYEATFKVPASFGPIGAVQVTNYHHSEMLLGDIEVFPTGQEESAVTFHCKSWIDPSHCTPDKRVFFPAHSYLPSQTPKGVEGLRKRELEILRGTGCGERKEHDRIYDYDVYNDLGNPDDDNNPTTRPVLGGKEHPYPRRCRTGRPRSKKDPFSEERSHKEHIYVPRDEAFTERKMGAFDTKKFMSQLHALTTGLKTAKHKSQSFPSLSAIDQLYDDNFRNQPVQPEGGKLRFVIDLLETELLHLFKLEGAAFLEGIRRVFKFETPEIHDRDKFAWFRDEEFARQTIAGMNPMSIQLVTEFPIKSNLDEATYGPADSLITKEVVEEQIRRVMTADEAVQNKKLFMLDYHDLLLPYVHKVRKLDGTTLYGSRALFFLTADGTLRPIAIELTRPKSKKKPQWRQVFTPGCDGSVTGSWLWQLAKAHILAHDAGVHQLVSHWLRTHACTEPYIIAANRQLSQMHPVYRLLHPHFRFTMEINAQARAMLINAGGIIEGSFVPGEYSLELSSVAYDQQWRFDMEALPEDLIRRGMAVRNPNGELELAIEDYPYANDGLLVWDAIKQWALTYVQHYYPCAADIVDDEELQAWWTEVRTKGHADKQDEPWWPELDSHENLAQTLATIMWVTSGHHAAVNFGQYPMAGYIPNRPTMARRNMPTEIGGDDMRDFVEAPEKVLLDTFPSQYQSAIVLAILDLLSTHSSDEEYMGTHEEPAWTKDGVINQAFEEFKESTRKIVEQVDEWNNDPDRKNRHGAGMVPYVLLRPSDGDPTDGDPTDEKMVMEMGIPNSISI | 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 exhibits linoleate 13-lipoxygenase and arachidonate 15-lipoxygenase activity.
PTM: The N-terminus is blocked.
Catalytic Activity: (9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-octadecadienoate
Sequence Mass (Da): 105864
Sequence Length: 936
Pathway: Lipid metabolism; oxylipin biosynthesis.
Subcellular Location: Plastid
EC: 1.13.11.12
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O24370 | MLKPQLQQSSQSTKALIPSWNTNPLFLASFPINILNKNFRLKKKNNFRVHHNYNGASTTKAVLSSTEKATGVKAVVTVQKQVNLNLSRGLDDIGDLLGKSLLLWIVAAELDHKTGIEKPGIRAYAHRGRDVDGDTHYEADFVIPQDFGEVGAILIENEHHKEMYVKNIVIDGFVHGKVEITCNSWVHSKFDNPDKRIFFTNKSYLPSQTPSGVSRLREEELVTLRGDGIGERKVFERIYDYDVYNDLGEADSNNDDAKRPVLGGKELPYPRRCKTGRPRSKKDPLSETRSTFVYVPRDEAFSEVKSVAFSGNTVYSVLHAVVPALESVVTDPNLGFPHFPAIDSLFNVGVDLPGLGDKKSGLFNVVPRLIKAISDTRKDVLLFESPQLVQRDKFSWFRDVEFARQTLAGLNPYSIRLVTEWPLRSKLDPKVYGPPESEITKELIEKEIGNYMTVEQAVQQKKLFILDYHDLLLPYVNKVNELKGSMLYGSRTIFFLTPQGTLKPLAIELTRPPVDDKPQWKEVYSPNDWNATGAWLWKLAKAHVLSHDSGYHQLVSHWLRTHCCTEPYIIASNRQLSAMHPIYRLLHPHFRYTMEINALAREALINANGVIESSFFPGKYAIELSSIAYGAEWRFDQEALPQNLISRGLAVEDPNEPHGLKLAIEDYPFANDGLVLWDILKQWVTNYVNHYYPQTNLIESDKELQAWWSEIKNVGHGDKRDEPWWPELKTPNDLIGIITTIVWVTSGHHAAVNFGQYSYAGYFPNRPTVARSKMPTEDPTAEEWEWFMNKPEEALLRCFPSQIQATKVMAILDVLSNHSPDEEYIGEKIEPYWAEDPVINAAFEVFSGKLKELEGIIDARNNDSKLSNRNGAGVMPYELLKPYSEPGVTGKGVPYSISI | 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 a cis,cis-1,4-pentadiene structure. Linolenic acid is the preferred substrate, before linoleic and arachidonic acids. Has also some activity with phosphatidylglycerol, but not with galactolipids.
Catalytic Activity: (9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-octadecadienoate
Sequence Mass (Da): 101937
Sequence Length: 899
Pathway: Lipid metabolism; oxylipin biosynthesis.
Subcellular Location: Plastid
EC: 1.13.11.12
|
P38418 | MYCRESLSSLQTLNVAKSLSSLFPKQSALINPISAGRRNNLPRPNLRRRCKVTASRANIEQEGNTVKEPIQNIKVKGYITAQEEFLEGITWSRGLDDIADIRGRSLLVELISAKTDQRITVEDYAQRVWAEAPDEKYECEFEMPEDFGPVGAIKIQNQYHRQLFLKGVELKLPGGSITFTCESWVAPKSVDPTKRIFFSDKSYLPSQTPEPLKKYRKEELETLQGKNREEVGEFTKFERIYDYDVYNDVGDPDNDPELARPVIGGLTHPYPRRCKTGRKPCETDPSSEQRYGGEFYVPRDEEFSTAKGTSFTGKAVLAALPSIFPQIESVLLSPQEPFPHFKAIQNLFEEGIQLPKDAGLLPLLPRIIKALGEAQDDILQFDAPVLINRDRFSWLRDDEFARQTLAGLNPYSIQLVEEWPLISKLDPAVYGDPTSLITWEIVEREVKGNMTVDEALKNKRLFVLDYHDLLLPYVNKVRELNNTTLYASRTLFFLSDDSTLRPVAIELTCPPNINKPQWKQVFTPGYDATSCWLWNLAKTHAISHDAGYHQLISHWLRTHACTEPYIIAANRQLSAMHPIYRLLHPHFRYTMEINARARQSLVNGGGIIETCFWPGKYALELSSAVYGKLWRFDQEGLPADLIKRGLAEEDKTAEHGVRLTIPDYPFANDGLILWDAIKEWVTDYVKHYYPDEELITSDEELQGWWSEVRNIGHGDKKDEPWWPVLKTQDDLIGVVTTIAWVTSGHHAAVNFGQYGYGGYFPNRPTTTRIRMPTEDPTDEALKEFYESPEKVLLKTYPSQKQATLVMVTLDLLSTHSPDEEYIGEQQEASWANEPVINAAFERFKGKLQYLEGVIDERNVNITLKNRAGAGVVKYELLKPTSEHGVTGMGVPYSISI | 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. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Required for the wound-induced synthesis of jasmonic acid (JA) in leaves.
Catalytic Activity: (9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-octadecadienoate
Sequence Mass (Da): 102046
Sequence Length: 896
Pathway: Lipid metabolism; oxylipin biosynthesis.
Subcellular Location: Plastid
EC: 1.13.11.12
|
P29250 | MLGGIIGGLTGNKNARLKGSLVLMRKNALDINDFGATVIDGISEFLGRGVTCQLVSSSLVDPNNGNRGRVGTEASLEQWLTSLPSLTTGESKFGVTFEWEVEKMGIPGAIIVKNNHAAEFFLKTITLDNVPGHGAVVFVANSWIYPASKYRYNRVFFSNDTSLPSKMPAALKPYRDDELRNLRGDDQQGPYQEHDRVYRYDVYNDLGEPDSGNPRPVLGGSPDRPYPRRGRTGRKPTKTDPTAESRLSLLENIYVPRDERFGHLKMADFLGYSIKALVDGIVPAIRTYVDLTPGEFDSFKDILKLYEGGLKLPSIPALEELRKRFPLQLVKDLIPAGGDYLLKLPMPHVIREDKKAWMTDDEFAREILAGVNPMVIARLTEFPPRSRLDPARYGDQTSTITAAHVERGLEGLTVQQAIDGNLLYVVDHHDHFMPYLLDINSLDDNFIYATRTLLFLRGDGTLAPLAIELSLPHLQDDGLITARSTVYTPAARGGTGAGAVEWWVWQLAKAYVNVNDYCWHQLISHWLNTHAVMEPFVIATNRQLSVAHPVHKLLLPHYRDTMTINALARQTLINGGGIFEMTVFPRKHALAMSSAFYKDWSFADQALPDDLVKRGVAVPDPASPYKVRLLIEDYPYANDGLAVWHAIEQWATEYLAIYYPNDGVLQGDAELQAWWKEVREVGHGDIKDATWWPEMKTVAELVKACATIIWIGSALHAAVNFGQYPYAGYLPNRPSVSRRPMPEPGTKEYDELARDPEKVFVRTITKQMQAIVGISLLEILSKHSSDEVYLGQRDTPEWTSDAKALEAFKRFGARLTEIESRVVAMNKDPHRKNRVGPTNFPYTLLYPNTSDLKGDAAGLSARGIPNSISI | 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-pentadiene structure.
Catalytic Activity: (9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-octadecadienoate
Sequence Mass (Da): 97184
Sequence Length: 870
Pathway: Lipid metabolism; oxylipin biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.13.11.58
|
Q20800 | MRIPCLLRPLLGWFFGLCILFSALFGNYIITLFLGLPILGRHKQWRNLMDRAISYWMTIPMGLLEFLMGVRIRVSGDEIEFGSPAMIVMNHRTRLDWMYMWCALYQINPWLITSNKISLKAQLKKLPGAGFGMAAAQFVFLERNAEVDKRSFDDAIDYFKNIDKKYQILLFPEGTDKSEWTTLKSREFAKKNGLRHLDYVLYPRTTGFLHLLNKMREQEYVEYIYDITIAYPYNIVQSEIDLVLKGASPREVHFHIRKIPISQVPLNEQDASRWLTDRWTIKEQLLHDFYSEEQPINRQFPVERGDGVWRSWKEPRRHFYVKLTSLMFWTLVISFCSYHIFFVRTLQLGFLYFFVISFYLSWRYGGIDKYIIFKWQESRKSLQKSPSSSSI | 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 as acyl donors and sn-2-acyl lysoPI (2-acyl-sn-glycero-3-phospho-D-myo-inositol) as acyl acceptor. Contributes to the asymmetric cell division of epithelial cells. Asymmetric cell division is the fundamental mechanism by which multicellular organisms generate cell diversity.
Catalytic Activity: a 2-acyl-sn-glycero-3-phospho-D-myo-inositol + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46520
Sequence Length: 391
Pathway: Phospholipid metabolism; phosphatidylinositol metabolism.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.-
|
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
|
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
|
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
|
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
|
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: Single-pass membrane protein
Sequence Mass (Da): 13106
Sequence Length: 127
Subcellular Location: Cell membrane
|
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 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 (Da): 29377
Sequence Length: 269
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6.
Subcellular Location: Plastid
EC: 2.3.1.129
|
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 (Da): 28050
Sequence Length: 262
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6.
Subcellular Location: Cytoplasm
EC: 2.3.1.129
|
B4RVJ5 | MSKPIRIGMVAGEPSGDILAAGMVAELKRQYPDAIIEGIGGPNMIDAGFHSLFDMETLSVMGLVEVLAHLPAILKVKKQLLAHFEQNPPDIFVGVDAPDFNLRVEKALKARGIKTMHYVSPTVWAWREKRIHKIAKAANRVLGLFPFEQQVYDKYHVPYTFVGHTMADAIAIEPDQNAARQELGVESNAYVLAVLPGSRRGEVETLLPVFLETIEAIHVKRSDIQFLIPAANEHRLAQIKAFLQEANNAEERLPIQVTQGTSRDAMIASDVILLASGTATLEAMLCKRPMVAAYLLSPLTYKIMQRLYKAPFFTLPNLLANEAIIPELLQEEVNAENMSNQLLNFFESDNSALIARFTDLHHTLKCNADKTAAKAVVEELFA | 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-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Mass (Da): 42334
Sequence Length: 382
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.4.1.182
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O67420 | MKKIFLSLADRSASNYVYEILKEGFEEYEIYGLTDEKLEKIGVKSVARYSEISTVGLIEALPKVFKFLKIYRKILKNLKNTDTLIACDAPALNLRLIKDARKLGVKRIIYFISPQVWAWKPKRAEIIANYCDHVIVILPFEKKIYRKFPNLKVHYVGHPLVDLVKPQKTKEEFMKAFKKEPLPLLLGSREGEIRRHVKLLKGIIEELKKSFDVISPTFREFSKFIERELKVKTLTYEGASYDCFFYSKASLIASGTASLEAGIAGNPHVVYYKVNPITYFLGKRLVKVPYISLVNILLKEEVVPEFIQKSSDEILKGFEKVYKNEEEIKEKLGTLKFILGERFVIRKLRELFLEIV | 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-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Mass (Da): 41300
Sequence Length: 356
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.4.1.182
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F4IF99 | MMFQITKSKLRFPLSTFTKRYSSFQAAKSVIDKAAIDGELRVFIVSGEVSGDNIGSRLMSSLKKLSPLPIRFNGVGGSLMCKKGLNSLFPMEDLAVMGVWELLPHLYKFRVKLKETIDAAVKFKPHVVVTVDSKGFSFRLLKELRARYKQQRLENCSVHFHYVAPSFWAWKGGESRLGGLSEFVDHLFCILPNEERVCREHGVEATFVGHPVLEDASEFDLVRRCKPQELKLEGLSFSEHSIPSDSTVISVLPGSRLQEVERMLPIFSKAMKLLKDPFPKLVTLIHVASNNQVDHYIGESFSEWPVPAILVPSGSTQLKYDAFGASQAALCTSGTVAVELQLAHLPSLVAYRAHFLTELLIRYKAKIPYISLPNILLDSPIIPEALFQACNPSNLASILERLLLDEKMRERQVVGAEKLIQLLHPSESRMGNSIHCTGLESHRYTPSILAASTILSYARR | 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 components of the outer membranes of mitochondria and/or chloroplasts, or may be involved in signal transduction or plant defense responses (Potential).
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Mass (Da): 51465
Sequence Length: 460
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 5/6.
Subcellular Location: Mitochondrion
EC: 2.4.1.182
|
Q5NZG2 | MATRIAMVAGEASGDLLASHLIRAIRQQVPEAEFYGIGGPKMQAEGFDALWPCERLAVHGYVDALKRYRELSGIRKALLRRVQADRPDAFIGVDAPDFNLWLEGRIRSSGIPAIHFVSPSIWAWRGGRIKGIARSVSHMLCLFPFEPALYEKAGIPVSYVGHPLADVFPLVPDRAAARELLSLPTDCRIVALLPGSRQSEVRSLAATYIETARLLAERHPDIGFVVPLATRETRALFEQALHAADADELPIRLLFGHAVEAMTAADVVLVASGTASLEAALLKRPMVISYRIGKWQYRLMKRMAYLPWVGLPNILCNDSVVPELLQDDATPQALADALDRWLNDADACAELALRFDALHRELRQDTAGRAAAAILPYLNRSPEWKPSRQSA | 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-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Mass (Da): 43120
Sequence Length: 391
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.4.1.182
|
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