ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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P21203 | MKVGYLGPAATFTHLAVSSCFQNGAEHVAYRTIPECIDAAVAGEVDFAFVPLENALEGSVNLTIDYLIHEQPLPIVGEMTLPIHQHLLVHPSRENAWKELDKIYSHSHAIAQCHKFLHRHFPSVPYEYANSTGAAAKFVSDHPELNIGVIANDMAASTYELKIVKRDIQDYRDNHTRFVILSPDENISFEVNSKLSSRPKTTLMVMLPQDDQSGALHRVLSAFSWRNLNLSKIESRPTKTGLGHYFFIIDIEKAFDDVLIPGAMQELEALGCKVRLLGAYQSYQL | Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Mass (Da): 31901
Sequence Length: 285
Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
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P10341 | MSDAPTVVAYLGPAGTFTEEALYKFADAGVFGDGEIEQLPAKSPQEAVDAVRHGTAQFAVVAIENFVDGPVTPTFDALDQGSNVQIIAEEELDIAFSIMVRPGTSLADVKTLATHPVGYQQVKNWMATTIPDAMYLSASSNGAGAQMVAEGTADAAAAPSRAAELFGLERLVDDVADVRGARTRFVAVQAQAAVSEPTGHDRTSVIFSLPNVPGSLVRALNEFAIRGVDLTRIESRPTRKVFGTYRFHLDISGHIRDIPVAEALRALHLQAEELVFVGSWPSNRAEDSTPQTDQLAKLHKADEWVRAASEGRKLN | Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Mass (Da): 33740
Sequence Length: 315
Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
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O36005 | MKSVITTTISAADAAGRFPSSSDLESIQGNIQRAAARLEAAQKLSGNHEAVVKEAGDACFAKYSYLKNAGEAGDSPEKINKCYRDIDHYMRLINYSLVVGGTGPVDEWGIAGSREVYRALNLPGSAYIAAFTFTRDRLCVPRDMSSQAGVEFTSALDYVINSLC | Function: Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex.
PTM: Contains two covalently linked phycoerythrobilin chromophores.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17669
Sequence Length: 164
Subcellular Location: Plastid
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Q9CEU2 | MKIAYLGPRGSFCSVVAETAFVSEELFAYDSILDVIEAYDEGKCDFALVPIENSTEGTVNMSIDKIFHDSKATVVAEFVLPISQNLLALSKEGKIEHIYSHPQALAQTRNYLREHYPQAKVEITDSTSAAAEFVKNHPDLPIAAVANSYAAKMYDLEIVAKNIQDLAGNSTRFWLLGKEKKSFDLLKTGEKVSLALTLPDNLPGALHKAISVFAWRDIDMTKIESRPLRTRLGQYFFNIDLVNNEKNNLKIPYALEELSGLGVKVRLLGNYAVYSLGEG | Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Mass (Da): 30966
Sequence Length: 279
Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
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Q58054 | MNKAVIYTLPKGTYSEKATKKFLDYIDGDYKIDYCNSIYDVFERVDNNGLGVVPIENSIEGSVSLTQDLLLQFKDIKILGELALDIHHNLIGYDKNKIKTVISHPQALAQCRNYIKKHGWDVKAVESTAKAVKIVAESKDETLGAIGSKESAEHYNLKILDENIEDYKNNKTRFILIGKKVKFKYHPKNYKVSIVFELKEDKPGALYHILKEFAERNINLTRIESRPSKKRLGTYIFYIDFENNKEKLEEILKSLERHTTFINLLGKYPVFD | Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Mass (Da): 31415
Sequence Length: 272
Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
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Q7TVJ6 | MVRIAYLGPEGTFTEAALVRMVAAGLVPETGPDALQRMPVESAPAALAAVRDGGADYACVPIENSIDGSVLPTLDSLAIGVRLQVFAETTLDVTFSIVVKPGRNAADVRTLAAFPVAAAQVRQWLAAHLPAADLRPAYSNADAARQVADGLVDAAVTSPLAAARWGLAALADGVVDESNARTRFVLVGRPGPPPARTGADRTSAVLRIDNQPGALVAALAEFGIRGIDLTRIESRPTRTELGTYLFFVDCVGHIDDEAVAEALKAVHRRCADVRYLGSWPTGPAAGAQPPLVDEASRWLARLRAGKPEQTLVRPDDQGAQA | Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Mass (Da): 33633
Sequence Length: 321
Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
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P07598 | MSRTVMERIEYEMHTPDPKADPDKLHFVQIDEAKCIGCDTCSQYCPTAAIFGEMGEPHSIPHIEACINCGQCLTHCPENAIYEAQSWVPEVEKKLKDGKVKCIAMPAPAVRYALGDAFGMPVGSVTTGKMLAALQKLGFAHCWDTEFTADVTIWEEGSEFVERLTKKSDMPLPQFTSCCPGWQKYAETYYPELLPHFSTCKSPIGMNGALAKTYGAERMKYDPKQVYTVSIMPCIAKKYEGLRPELKSSGMRDIDATLTTRELAYMIKKAGIDFAKLPDGKRDSLMGESTGGATIFGVTGGVMEAALRFAYEAVTGKKPDSWDFKAVRGLDGIKEATVNVGGTDVKVAVVHGAKRFKQVCDDVKAGKSPYHFIEYMACPGGCVCGGGQPVMPGVLEAMDRTTTRLYAGLKKRLAMASANKA | Cofactor: Binds 3 [4Fe-4S] clusters per subunit.
Function: May be involved in hydrogen uptake for the reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is likely to be the physiological electron carrier for the enzyme.
Catalytic Activity: H2 + 2 oxidized [2Fe-2S]-[ferredoxin] = 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 45951
Sequence Length: 421
Subcellular Location: Periplasm
EC: 1.12.7.2
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P07603 | MQIASITRRGFLKVACVTTGAALIGIRMTGKAVAAVKQIKDYMLDRINGVYGADAKFPVRASQDNTQVKALYKSYLEKPLGHKSHDLLHTHWFDKSKGVKELTTAGKLPNPRASEFEGPYPYE | Function: May be involved in hydrogen uptake for the reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is likely to be the physiological electron carrier for the enzyme.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Catalytic Activity: H2 + 2 oxidized [2Fe-2S]-[ferredoxin] = 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 13624
Sequence Length: 123
Subcellular Location: Periplasm
EC: 1.12.7.2
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Q55FP0 | MKINKKQIVFFILFSIFLNHVNGIFYLPGMIPHDFAQGEEGAIKVNKITSVHTQIPYKYYQLPGVCQPKEGIIDDTENLGEILLGDRIENSDYTFNFLTDGGKCKVINSESCSPIIKKEDLKVLEDRIQNQYRVHWLLDGLPVRQTGRLASDPGFDLGFMTLAEGQTVATAEKYLNNHLEITIFYHSNPTDNTSRIVGFEIFPTSRQYKKVENWKGDTGDDCPQYGENFEQLSVSVKEGEDQERFVLWTYEVKYTPSPVLWNKRWDIYFESNDNSVHWFSILNSLMIVFILTVMVAMIIIRTLKKDIRRYTSIDTSEDRDSQEETGWKMIHGDVFRPPSHPMLLSVCIGSGVQIFSMTLITMIFAVLGFLSPANIGGLATALIVLFVLSAMFAGYFSTRVFTIFKGRNWKKNTIYTALSMPGIIFGIFFFVNMFLRGAKSSAAVPFGTFASIIAMWFGISVPLVFLGSYFASKKPVPEDPVRTNQIPRQVPDQIWYMNPYLSILMGGILPFGAVFIELHFILTSLWDNQFYYIFGFLFIVLMILIVTSAEISIVMCYFQLCAEDHHWWWRSFLTAGSSSLYMFIYSVSFFRYLGITKFISSLLDFSYSFIMSLAFAALTGTIGFYSCYFLVRKIYSSIHIN | Function: Involved in adhesion, phagocytosis of hydrophilic particles and intracellular killing of bacteria . Associates with proteins harboring glycine-rich transmembrane domains and ensures their efficient localization to the cell surface .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73365
Sequence Length: 641
Subcellular Location: Membrane
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Q54ZW0 | MRLQILLIYLICIIVSSIVLVESSNKHHFKENDEVPFYVNNVGPYSNPTETYEFYTLPFCKPSSISYKKTKLGEILQGDSAVLSDYQFPFKSSFENKQLCEYTLKKEDIEKFKKAIGEYYYAEMIYDDLPIFSFVGTVDDSDLTNIRYYLYNHIPFEFDYNGDQVIRVNIDTEHIKVIELSDQDEITLKLTYSAKWQPTEHEFSKRMDLYEEFFTKELEIHWLSVMNSFFLVVLLTAFLAIMIMKILKNDYSRYSKTDEEEDSDYQEDYGWKLVHGDVFRFPPYKNVFSAFYGIGWQFISIVCGILALSLFGMFYPNNGGNMYTAGIVLYALTSGISGYQSAKMYKNMGGNKWAWNIVLTATLFVAPLFIVVILSNTVAITWHSTVALPILTMIEVITIWLFVGFPLTVVGGIAGRRLSENFEAPCRTKNFPREVPPIQWYRRLPCQILIAGFLPFSAIYIELFYIFNSVWGHSTYTLYGILCLVFLILINVTVCITVALTYFQLSMEDHKWWWNSFINGGSTVVFIYMYSIYYYYYISHMYGLLQATFYFTYMLIVCFFFFILLGTVGFYSSLIFVKRIYRNLKSD | Function: Involved in adhesion and phagocytosis of hydrophilic particles.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68547
Sequence Length: 587
Subcellular Location: Membrane
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P57793 | XVPCNKEFVXNXF | Function: Functions in the pathway of anaerobic degradation of trihydroxybenzenes by catalyzing reduction of the aromatic nucleus prior to ring fission.
Catalytic Activity: dihydrophloroglucinol + NADP(+) = 1,3,5-trihydroxybenzene + NADPH
Sequence Mass (Da): 1530
Sequence Length: 13
EC: 1.3.1.57
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A2QGH7 | MAPSQQEKYDIVIVGAGPVGIVLSLCMSRWGYKVKHIDNRPVPTATGRADGIQPRSTEILRNLGLKRQIMAFKPAKVYDVAFWDPLPGGQGIHRTGSWPSCPRFIDTRYPFTTLVHQGKIERVFLDEIQKAGTTVERPWTIVGFKNDGLDETYPVEVQLKSIDTNVIETVRTKYLFSGEGARSFIRQQLGIQIQYKDPISYVWGVMDGVVRTNFPDIETKCTIHSDAGSIMVIPREDNMVRLYVQIASSDDPDFDPRKTATAEDVQATARKILQPYWVEWDRVEWYSVYPIGQGISEKYTLDERVFMGGDACHTHSPKAGQGMNTAFHDALNMAWKLHAVESGLAKRSILSTYETERKDIAETLLSFDNKYAALFSKRRPTAGEVGEASHTTAAAGGEEDEFVKTFKSSCEFTSGYGVAYKPNVFTWDATHPAQSPLFDVPGVRLTPGRAFTPTTVTRLADSNHVHLEQEIPANGAFRIFIFAGKQDKTSKAITDLAANLEKERSFLSVYRRADIADVSFFENHLPHSKLFSICLVYAGEKNQIDVDSIPKILRDYHHHLYADNIPDVRVPQATYAAHEKLGFDVEKGGVVVTRPDSHVACTVQLSEGSGTVDALNAFFGSFATKPLGQDSQQSRL | Cofactor: Binds 1 FAD per subunit.
Function: FAD-dependent monooxygenase; part of the benzoic acid degradation pathway also known as the protocatechuic acid pathway (Ref.2). Benzoic acid debradation begins with the conversion of benzoic acid into 4-hydroxybenzoic acid through hydroxylation by the benzoate-4-monooxygenase bphA, and its partner NADPH-cytochrome P450 reductase cprA which act as a mediator in electron donation from NADPH (By similarity). 4-Hydroxybenzoic acid is then converted into 3,4-dihydroxybenzoic acid (also called protocatechuic acid) by the p-hydroxybenzoate-m-hydroxylase phhA (Ref.2). Protocatechuic acid is converted into 3-carboxy-cis,cis-muconic acid by the intradiol ring-cleavage dioxygenase prcA, which is further metabolized through the 3-oxoadipate pathway to finally enter the tricarboxylic acid cycle (TCA) (Ref.2).
Catalytic Activity: 4-hydroxybenzoate + H(+) + NADH + O2 = 3,4-dihydroxybenzoate + H2O + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 70898
Sequence Length: 636
Subcellular Location: Membrane
EC: 1.14.13.33
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P43336 | MSHFAKVARVPGDPILGLLDAYRNDPRADKLDLGVGVYKDAQGLTPILRSVKLAEQRLVEQETTKSYVGGHGDALFAARLAELALGAASPLLLEQRADATQTPGGTGALRLAGDFIAHCLPGRGIWLSDPTWPIHETLFAAAGLKVSHYPYVSADNRLDVEAMLAGLERIPQGDVVLLHACCHNPTGFDLSHDDWRRVLDVVRRRELLPLIDFAYQGFGDGLEEDAWAVRLFAGELPEVLVTSSCSKNFGLYRDRVGALIVCAQNAEKLTDLRSQLAFLARNLWSTPPAHGAEVVAAILGDSELKGLWQEEVEGMRSRIASLRIGLVEALAPHGLAERFAHVGAQRGMFSYTGLSPQQVARLRDEHAVYLVSSGRANVAGLDARRLDRLAQAIAQVCAD | Catalytic Activity: 2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic oxo-acid + L-glutamate
Sequence Mass (Da): 43273
Sequence Length: 399
Subcellular Location: Cytoplasm
EC: 2.6.1.57
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Q03298 | MQTMKTKVAIIGSGPAGLLLGQLLYKAGIEHVIVEQRSADYVASRIRAGILEQVSVDLLEQAGVDQNLKEKGLPHSGIEILTNGQKFRVDLSALTQGKQVTVYGQTEVTKDLMQAREQAGLCSFYESNDVQIHDFYNAPKVTFESNGTHYQIECDFIAGCDGYHGVCRASVPQDKIKTFEKVYPFGWLGVLADVPPVADELIYVQSERGFALCSMRSETRSRYYIQVPLTDHVENWSDDQFWEELKNRLDPESCEKLVTGPSIEKSIAPLRSFVTEPMRFGKLFLAGDAAHIVPPTGAKGLNLAASDIAYLSSALIEFYTQGSEQGIDQYSEKCLQRVWKAERFSWWMTHLLHRFETESEFDHKIKQAELSYILGSTAGQTTLAENYVGLPYEIKSLDYLKHAS | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the incorporation of an atom of dioxygen into p-hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). The reaction occurs in two parts: reduction of the flavin adenine dinucleotide (FAD) in the enzyme by reduced nicotinamide adenine dinucleotide phosphate (NADPH) in response to binding p-hydroxybenzoate to the enzyme and oxidation of reduced FAD with oxygen to form a hydroperoxide, which then oxygenates p-hydroxybenzoate.
Catalytic Activity: 4-hydroxybenzoate + H(+) + NADPH + O2 = 3,4-dihydroxybenzoate + H2O + NADP(+)
Sequence Mass (Da): 45271
Sequence Length: 404
Pathway: Aromatic compound metabolism; benzoate degradation via hydroxylation; 3,4-dihydroxybenzoate from benzoate: step 2/2.
EC: 1.14.13.2
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P15245 | MTKYSESYCDVLIVGAGPAGLMAARVLSEYVRQKPDLKVRIIDKRSTKVYNGQADGLQCRTLESLKNLGLADKILSEANDMSTIALYNPDENGHIRRTDRIPDTLPGISRYHQVVLHQGRIERHILDSIAEISDTRIKVERPLIPEKMEIDSSKAEDPEAYPVTMTLRYMSDHESTPLQFGHKTENSLFHSNLQTQEEEDANYRLPEGKEAGEIETVHCKYVIGCDGGHSWVRRTLGFEMIGEQTDYIWGVLDAVPASNFPDIRSPCAIHSAESGSIMIIPRENNLVRFYVQLQARAEKGGRVDRTKFTPEVVIANAKKIFHPYTFDVQQLDWFTAYHIGQRVTEKFSKDERVFIAGDACHTHSPKAGQGMNTSMMDTYNLGWKLGLVLTGRAKRDILKTYEEERHAFAQALIDFDHQFSRLFSGRPAKDVADEMGVSMDVFKEAFVKGNEFASGTAINYDENLVTDKKSSKQELAKNCVVGTRFKSQPVVRHSEGLWMHFGDRLVTDGRFRIIVFAGKATDATQMSRIKKFSAYLDSENSVISLYTPKVSDRNSRIDVITIHSCHRDDIEMHDFPAPALHPKWQYDFIYADCDSWHHPHPKSYQAWGVDETKGAVVVVRPDGYTSLVTDLEGTAEIDRYFSGILVEPKEKSGAQTEADWTKSTA | Function: Hydroxylates phenol to catechol . Phenol is the best substrate, but the enzyme also accepts isomeric diphenols, hydroxyl-, amino-, halogen- or methyl-substituted phenols and, to a lesser degree, cresols .
Catalytic Activity: H(+) + NADPH + O2 + phenol = catechol + H2O + NADP(+)
Sequence Mass (Da): 75162
Sequence Length: 665
Pathway: Aromatic compound metabolism; phenol degradation.
EC: 1.14.13.7
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Q0V6Q2 | MAEAFTTVPAKSSPARFRYTKANPVKDPTTSFAGKTILITGPNAGLGFEAATKFARLGASKLIFGVRSLERGQEAKTKIEQLTKCKRDAIQLVQLDMGSYASIEKFAKSVTDEFPVIHAAVLNAGVAPPSYKLSQEGWEMSLQVNVISTAYLAILLLPKLRESGRAIGEPAYLEFVSSTGHGDVTTESVRDGKSILKKVNDPANFKFTAQYQITKLLEIWAMEHIAAKTSPKEVIVNSACPGLCKSSIGRDFGIVLRGLDAVFKGIFAQTAEAGSRILVSAVTAGTDSHGGFWALDAVSVPGELVTSDEGKALSKQFWAEVLDVLRKQNADVEAILNG | Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the mycotoxins phomacins, leucine-derived cytochalasans with potent actin polymerization-inhibitory activities and monocot-specific antigerminative activities . The first step in the pathway is catalyzed by the hybrid PKS-NRPS phmA, assisted by the enoyl reductase phmE, that are responsible for fusion of the leucine precursor and the polyketide backbone to produce a 2-pyrrolidone intermediate . The polyketide synthase module (PKS) of phmA is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the leucine precursor . Because phmA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase phmE . Reduction by the hydrolyase phmG, followed by dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase phmD then yield the required isoindolone-fused macrocycle (Probable). A number of oxidative steps catalyzed by the tailoring cytochrome P450 monooxygenase phmB, the FAD-linked oxidoreductase phmC and the short-chain dehydrogenase/reductase phmF, are further required to afford the final products, phomacin D and phomacin E .
Sequence Mass (Da): 36227
Sequence Length: 338
Pathway: Mycotoxin biosynthesis.
EC: 1.1.1.-
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Q0V6Q0 | MVSGTDTTEVGATTKAPPSEGTEGILDDHSSNSQPQAEKPAKTHYPLSFWLAFLGLCCTGLVSALDGSIVATALPSIIESLDGGDDYPLYGQLADLWGRRYVMIGATIIFILGSGLCGGSSSMNMLIWSRAVQGIGAGGINMLIDMIICDLVPMRERGNFIGLLFLFVSLGATIGPFVGGILTDRASWRWLWLLILLQIFYINLPFGGVALLLLILFLHVKWKNDLSTMERLRRVDVIGNSILIGATFAILYALTYGGTRYTWSDPHIAAPLTIGLVGLVAAFFWEMSPWCKYPVMPPLHFQNRTSAAAFFISFMCMLLAFWINFFYPVYFQAVLIASPTRAGVYTLPRAIAFPLFAAVGGAIVSKTGRYRTVHLVSTGIMPLVMGLSSILDQGSSKAEWVIWQLLFGVSGGMMISTTLQAVQAALPESEVATSVGTWSFVRSLGTIWGLSIPAAIFNNRFDQLSTQFDPSIRALFTRGQAYEHGTAKFIQSFDPETRQIVIQAYIEALKRVWQIGIVFGGVTFLSVFFEKEIHLRTELKTDFGLDEKKKGEVAKEENDVENNGTTVQ | Function: MFS-type efflux transporter; part of the gene cluster that mediates the biosynthesis of thethe mycotoxins phomacins, leucine-derived cytochalasans with potent actin polymerization-inhibitory activities and monocot-specific antigerminative activities . PhmH might be involved in the excretion of phomacins (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62250
Sequence Length: 568
Subcellular Location: Cell membrane
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Q95XM2 | MPRFYLLSSCALLAFATSFCNAEKSQIRMPGVVPEADSYLCTSLELSDQENYLTGFKALTTKGTAHHILLFGCEEPGSDELVWDCGEMNKPDDEMPRAPTCGSKPAILYAWALDAPPLELPQDVGFRVGGDSNIRHLVMQVHYMHSKQEPDETGLEITHTEEPQPKLAATMLLVTGGTLPRNKTESFETACMIEEDVVMHPFAYRTHTHRHGKEVSGWLVKEDQKHEDHWKLIGRRDPQLAQMFVPVEDQAMTIQQGDMVTARCILQNNENRDISMGATEEDEMCNFYIMYWTDGEVMQDNTCYSPGAPDYKWAREADLNHIPK | Cofactor: Binds 2 copper ions per subunit.
Function: Monooxygenase that catalyzes an essential reaction in C-terminal alpha-amidation of peptides. Produces an unstable peptidyl(2-hydroxyglycine) intermediate. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
Catalytic Activity: a [peptide]-C-terminal glycine + 2 L-ascorbate + O2 = a [peptide]-C-terminal (2S)-2-hydroxyglycine + H2O + 2 monodehydro-L-ascorbate radical
Sequence Mass (Da): 36647
Sequence Length: 324
Subcellular Location: Secreted
EC: 1.14.17.3
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O01404 | MPRISEIAASVGLLLLIGVISVDGLVKEGDYQNSLYQQNLESNSATGATASFPFLMPNVSPQTPDLYLCTPIKVDPTTTYYIVGFNPNATMNTAHHMLLYGCGEPGTSKTTWNCGEMNRASQEESASPCGPHSNSQIVYAWARDAQKLNLPEGVGFKVGKNSPIKYLVLQVHYAHIDKFKDGSTDDSGVFLDYTEEPRKKLAGTLLLGTDGQIPAMKTEHLETACEVNEQKVLHPFAYRVHTHGLGKVVSGYRVRTNSDGEQEWLQLGKRDPLTPQMFYNTSNTDPIIEGDKIAVRCTMQSTRHRTTKIGPTNEDEMCNFYLMYYVDHGETLNMKFCFSQGAPYYFWSNPDSGLHNIPHIEASTL | Cofactor: Binds 2 copper ions per subunit.
Function: Monooxygenase that catalyzes an essential reaction in C-terminal alpha-amidation of peptides. Produces an unstable peptidyl(2-hydroxyglycine) intermediate. C-terminal amidation of peptides is required for normal developmental transitions and for biosynthesis of secretory peptides throughout the life.
Catalytic Activity: a [peptide]-C-terminal glycine + 2 L-ascorbate + O2 = a [peptide]-C-terminal (2S)-2-hydroxyglycine + H2O + 2 monodehydro-L-ascorbate radical
Sequence Mass (Da): 40564
Sequence Length: 365
Subcellular Location: Secreted
EC: 1.14.17.3
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P09785 | MGARRWLVSGVGYRLEESLEYRTLVPEALSIWRMAGANRMLFDCFDVDSKAARRSVAILSSCLRIECWGRDVVLRALNSNGRALLAPLSEDCPAQVTCLRDGDTLHWRFPQEESHADEWRRLHGLSSLEALRRVLGTLGDAEGPVLLGGLFSFDLAEQFEPLPAPAEPARHCPDYLFLVPELLLDIDHLARRTSLQAFVHDPAGHDRLAASLRQCADEFHGAVEEASESPVAGVRAGNYQVDLDDASFARQVERLQAHVRAGDVFQIVPSRSFSMPCADPWRAYRQLCLRNPSPYRFFLDAGDFCLFGASPESALKYDAESREVELYPIAGTRPRGRDARGAIDAELDNRLEAELRLDAKEIAEHMMLVDLARNDLARVCRSGTRQVRDMLKVDRYSHVMHLVSRVAGELHGELDALHAYRACLNMGTLVGAPKVRAMQLLRQYEDGYRGSYGGAIGILDSAGNLDTSIVIRSAEVREGIARVRAGAGVVLDSDPRLEAEETRNKALAVLTAVAAAERERGERDAHHAVG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, a precursor for Pseudomonas quinolone signal (2-heptyl-3-hydroxy-4-quinolone; PQS) production which is required to induce the genes for the biosynthesis of the virulence factor pyocyanine (PCN), a characteristic blue-green phenazine pigment produced by P.aeruginosa . In the first step, the glutamine-binding beta subunit (PhnB) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (PhnA) to produce anthranilate (By similarity).
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 58670
Sequence Length: 530
Pathway: Secondary metabolite biosynthesis; pyocyanine biosynthesis.
EC: 4.1.3.27
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A0A142C7A0 | MTSPQTHVIVIGAGITGLLTCQGLKKAGISYSCFERDTSLNSRSNEWTMAIHWSLPLLAEILPTEVRAKLATIACNPVAGIHSGLYPIIHGETGDLITGVPYKDGLRVPRSKMRALCAEGIDVQYGKTLADVAFNESGNGVVATFTDGTLVAGTMIVGADGPRSRVRETAMGDAKLAATTSFPIFHTNMTVCYNDAEKAKFVREKYPTSYLALSERSFHAFQSISSMPDGPDHPETWVFHMAMAWMGQSDNAMCYAERLALVKSKAEGLGEPARSAFMWMPEETEVHKADISYWISQPWNNRDGRLTLVGDAAHPMPPYRGQGLNHCICDVSKLLAGLAGVHSGSTTLSDAIQEFEAEMIPRGKEEVTCSVENGKMLHDWNKIQESPVFKRGFLPMDGHDTRKEIAQAS | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of phenalenones such as herqueinone, compounds that have been reported to treat tumors, bacterial infections and/or mycoses, and rheumatic diseases . The non-reducing polyketide synthase phnA synthesizes the heptaketide backbone and cyclizes it into the angular, hemiketal-containing naphtho-gamma-pyrone prephenalenone. The product template (PT) domain of phnA catalyzes only the C4-C9 aldol condensation, which is unprecedented among known PT domains . The transformation of prephenalenone to phenalenones requires an FAD-dependent monooxygenase phnB, which catalyzes the C2 aromatic hydroxylation of prephenalenone and ring opening of the gamma-pyrone ring simultaneously . Subsequent intramolecular deprotonation of C3 phenolic oxygen accelerates phenalenone ring closure to yield the tricyclic phenalenone core with a C2 hydroxylation . The prenyltransferase phnF further catalyzes reverse C-prenylation of phenalenone by direct electrophilic substitution at C6, or possibly via first a forward O-prenylation of a neighboring phenol in phenalenone, followed by a Claisen rearrangement . The hydroalkoxylation enzyme phnH catalyzes the 5-exo-trigcyclization via acid catalysis after the spontaneous deprotonation of 7-OH, which leads to the formation of the dihydrobenzofuran atrovenetin . Atrovenetin is further converted to deoxyherqueinone by the O-methyltransferase phnC which can methylate C2-OH to stabilize the northern portion of the phenalenone core . Finally, the oxidoreductase phnG converts deoxyherqueinone to herqueinone via C6 hydroxylation .
Catalytic Activity: 3,6,7,9-tetrahydroxy-3-methyl-2,3-dihydro-1H-naphtho[2,1-b]pyran-1-one + H(+) + NADPH + O2 = 2,3,4,7,9-pentahydroxy-6-methyl-1H-phenalen-1-one + 2 H2O + NADP(+)
Sequence Mass (Da): 44641
Sequence Length: 409
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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P09786 | MRITLLDNFDSFTYNLVEQFCLLGAEVRVMRNDTPLPTIQAALLADGCELLVLSPGPGRPEDAGCMLELLAWARGRLPVLGVCLGHQALALAAGGAVGEARKPLHGKSTSLRFDQRHPLFDGIADLRVARYHSLVVSRLPEGFDCLADADGEIMAMADPRNRQLGLQFHPESILTTHGQRLLENALLWCGALAVRERLRA | Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, a precursor for Pseudomonas quinolone signal (2-heptyl-3-hydroxy-4-quinolone; PQS) production which is required to induce the genes for the biosynthesis of the virulence factor pyocyanine (PCN), a characteristic blue-green phenazine pigment produced by P.aeruginosa . In the first step, the glutamine-binding beta subunit (PhnB) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (PhnA) to produce anthranilate (By similarity).
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 21845
Sequence Length: 200
Pathway: Secondary metabolite biosynthesis; pyocyanine biosynthesis.
EC: 4.1.3.27
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Q98GF5 | MSSSATLEIRGVSRRFGKNTAVSDINISIPQGQMVGVIGRSGAGKSTLLRMINRLVDPSQGSIFFDGAEVSRLRGSPLRRWQRDCAMIFQQFNLVPRLDVLTNVLLGKLNHRSTLSNLLGMFSRAECAEAVAALERLDIARTALQPAGTLSGGQQQRVAIARALMQQPKVILADEPIASLDPLNAKVVMDSLQDINLREGITVVTNLHTLDTARTYCNRIIGMAAGKVVFDGPPEELNREAVRLVYGADSSGAEISEAITSTSVAFKPKIAASAGPLEPAFPGY | Function: Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphonate(out) = ADP + H(+) + phosphate + phosphonate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30486
Sequence Length: 284
Subcellular Location: Cell inner membrane
EC: 7.3.2.2
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Q92V71 | MFQLKNVTRQFGKKTAVSTVTFDIPQGQMVGIIGRSGAGKSTLLRMINRLVDPSSGSIEFAGLQVSSLKGAALRNWQRDCAMIFQQFNLVPRLDVLTNVLLGRLNHRSTVLSVLNMFSREERIMAIGALERLGIEQTALQPAGTLSGGQQQRVAIARALMQQPKVLLADEPIASLDPLNAKIVMDALRDINERDGITVITNLHTLDTARNYCERVIGMAHGRVVFDGQPKDLTAAAVAAIYGAETAIEESMTSTSINIPAEAPRETASAGLKPLALAGP | Function: Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphonate(out) = ADP + H(+) + phosphate + phosphonate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30044
Sequence Length: 279
Subcellular Location: Cell inner membrane
EC: 7.3.2.2
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P96060 | MTSRNYLLLTPGPLTTSRTVKEAMLFDSCTWDDDYNIGVVEQIRQQLTALATASEGYTSVLLQGSGSYAVEAVLGSALGPQDKVLIVSNGAYGARMVEMAGLMGIAHHAYDCGEVARPDVQAIDAILNADPTISHIAMVHSETTTGMLNPIDEVGALAHRYGKTYIVDAMSSFGGIPMDIAALHIDYLISSANKCIQGVPGFAFVIAREQKLAACKGHSRSLSLDLYAQWRCMEDNHGKWRFTSPTHTVLAFAQALKELAKEGGVAARHQRYQQNQRSLVAGMRALGFNTLLDDELHSPIITAFYSPEDPQYRFSEFYRRLKEQGFVIYPGKVSQSDCFRIGNIGEVYAADITALLTAIRTAMYWTK | Cofactor: Thr-243 of one partner binds the pyridoxal phosphate moiety of the other.
Function: Involved in phosphonate degradation.
Catalytic Activity: (2-aminoethyl)phosphonate + pyruvate = L-alanine + phosphonoacetaldehyde
Sequence Mass (Da): 40249
Sequence Length: 367
EC: 2.6.1.37
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Q183T0 | MKKIYGEKIKAVVFDWAGTTVDYGCFAPLNVFIEIFKRRGIDVTMEEARKPMGKLKIDHIREMCEMDRIKNIWSDKFGKVPTEDDVNELYAEFEPMLFETLEEYTTPIPHVVETIEKLRKNGLKIGSTTGYTREMMNIVEPNAAKKGYSPDFLVTPSEVSQGRPYPWMCYKNAEALGVSPMSSMVKVGDTISDVKEGVNAGMWSVAVIKGSSELGLTQEEVENMDKEELKAKMSIVSKKFKEAGAHFVIETMAELEDILIKIENETIKSDFVPENDYILLTPGPLSTTKSVRASMLKDWCTWDVEYNNLVQDVRRRLVSLATQNTDKYTSVLMQGSGTFSVEAIIGSTISKDGKLLVIANGAYGKRMKDICNYLNIQFVDCTFKDIEAVDLNVVENLLKENKDITHISMVHCETTTGRLNPIQEVGKLAKEYNKIYIVDAMSSFGGIEIDVEDFNIDFLVSSSNKCIQGVPGFGFIIANKEELSKCKGIAKSLSLDVYAQWDTMEKNNGKWRFTSPTHVVRAFYQALLELEEEGSVEKRYARYKENQFTIASRLKSLGFDTLVNDNAQSPVITTFLYPKNAKFEFMEFYTYLKDNGFVIYPGKLTDIDTFRIGSIGEVYPTDMERLADVIEKFINR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in phosphonate degradation.
Catalytic Activity: (2-aminoethyl)phosphonate + pyruvate = L-alanine + phosphonoacetaldehyde
Sequence Mass (Da): 72044
Sequence Length: 636
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A0A8K1Y6D9 | MASVTITSVHEPTNPLAVAHTGEREVEGDQLIKTDTNNDNDIINTLLNNFLYPQELKHNVFVPRFQQRITIVKAWDILSLSTSPPNGTNGANGTNSAPHRPKDLHILDIGCGQGESAVTMAALLQPHMHGARLHITGIDTARPDYGTPYTVAETHAHLTASALGRHISFRREDAAAFFSPSRLSSPSPPGSWPSAANVDAVTLCHSLWYFPTPQSVADLFTTLAGARVPRVYLAEYSFRGSLPGGQQDAHILAARAQALLHASVLEKLSADSSQQNHQGREPRPRAPNVRAALDVGSIVEAAAAAGWAVRRQGTFVPAADMIEGHLEARLVVKDAFAEAVRAEGLSPEREHEVLGLVPGVKKAFARLAAAGVAKGRAMDVWWAELER | Function: Methyltransferase; part of the gene cluster that mediates the biosynthesis of the phomopsins, a group of hexapeptide mycotoxins which infects lupins and causes lupinosis disease in livestock . Within the pathway, phomM acts as an S-adenosylmethionine-dependent alpha-N-methyltransferase that catalyzes two successive N-methylation reactions, converting N-desmethyl-phomopsin A to phomopsin A and phomopsin A further to an N,N-dimethylated congener called phomopsin E . The pathway starts with the processing of the precursor phomA by several endopeptidases including kexin proteases as well as the cluster-specific S41 family peptidase phomP1 and the oligopeptidase phomG to produce 10 identical copies of the hexapeptide Tyr-Val-Ile-Pro-Ile-Asp. After being excised from the precursor peptide, the core peptides are cyclized and modified post-translationally by enzymes encoded within the gene cluster. The timing and order of proteolysis of the phomA precursor and PTMs are still unknown. Two tyrosinase-like enzymes, phomQ1 and phomQ2, catalyze the chlorination and hydroxylation of Tyr, respectively. PhomYb, is proposed to be involved in the construction of the macrocyclic structure. The other 4 ustYa family proteins may be involved in PTMs that generate the unique structure of phomopsin A. PhomYa is required for the hydroxylation of C-beta of Tyr. PhomYc, phomYd, and phomYe are responsible for the biosynthesis of 2,3-dehydroisoleucine (dIle), 2,3-dehydroaspartic acid (dAsp), and 3,4-dehydroproline (dPro), respectively. While dIle formation by phomYc is indispensable for the installation of dAsp by phomYd, the order of the other PTMs have not been elucidated yet. Most of the biosynthetic enzymes likely have broad substrate specificity, and thus, there might be a metabolic grid from a precursor to phomopsin A. The enzyme(s) responsible for the biosynthesis of 3,4-dehydrovaline (dVal) have also not been identified yet. Finally, phomM acts as an S-adenosylmethionine-dependent alpha-N-methyltransferase that catalyzes two successive N-methylation reactions, converting N-desmethyl-phomopsin A to phomopsin A and phomopsin A further to an N,N-dimethylated congener called phomopsin E (Probable).
Sequence Mass (Da): 41646
Sequence Length: 387
Pathway: Mycotoxin biosynthesis.
EC: 2.1.1.-
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P26976 | MKSRYLVFFLPLIVAKYTSAETVQPFHSPEESVNSQFYLPPPPGNDDPAYRYDKEAYFKGYAIKGSPRWKQAAEDADVSVENIARIFSPVVGAKINPKDTPETWNMLKNLLTMGGYYATASAKKYYMRTRPFVLFNHSTCRPEDENTLRKNGSYPSGHTAYGTLLALVLSEARPERAQELARRGWEFGQSRVICGAHWQSDVDAGRYVGAVEFARLQTIPAFQKSLAKVREELNDKNNLLSKEDHPKLNY | Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 28382
Sequence Length: 250
Subcellular Location: Periplasm
EC: 3.1.3.2
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O73884 | MKRCCEGVGLPCLFKGVGMASSRPPKYLLVFDFDGTIINESSDDSIVRAAPGQALPEHIRQSFREGFYNEYMQRVLAYMGDQGVKMGDFKAVYENIPLSPGMPDLFQFLSKNHELFEIILISDANMFGIECKLRAAGFYSLFRKIFSNPSSFDKRGYFTLGPYHSHKCLDCPANTCKRKILTEYLAERAQEEVEFERVFYVGDGANDFCPSVTLTSADVAFPRKGYPMHQMTQEMEKKQPGTFQATVVPWESATEVARYLQELLKKKC | Function: Phosphatase that has a high activity toward phosphoethanolamine (PEA) and phosphocholine (PCho) (By similarity). Involved in the generation of inorganic phosphate for bone mineralization .
Catalytic Activity: H2O + phosphoethanolamine = ethanolamine + phosphate
Sequence Mass (Da): 30443
Sequence Length: 268
Subcellular Location: Extracellular vesicle
EC: 3.1.3.75
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Q6DBV4 | MRDSVFNCCVSPPHPPGAAAAERRSRSPAPQNHSRFLMFFDFDETLVDECSDDSMVSAAPGGVLPGWLKDTYRPGRYNEYMQRVLAYLSEQGVTPAAIRATVEKLPPCPGIPALMHFLLSQPSRDFEVVCVSDANTVFIETWLQHMGFQPLFLRIFTNPAHFDDNGVLQLRPFHSHECLRCPANMCKAVVVRQYVAQRIRERGGRPYQKVLYMGDGANDFCPSLTLSPGDVAFPRRDFPMHKLIQEMGEAKPGEFKASVVPWKSGEDVVNTLRKILERT | Function: Phosphatase that has a high activity toward phosphoethanolamine (PEA) and phosphocholine (PCho). Involved in the generation of inorganic phosphate for bone mineralization.
Catalytic Activity: H2O + phosphoethanolamine = ethanolamine + phosphate
Sequence Mass (Da): 31403
Sequence Length: 279
Subcellular Location: Extracellular vesicle
EC: 3.1.3.75
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Q8TCT1 | MSGCFPVSGLRCLSRDGRMAAQGAPRFLLTFDFDETIVDENSDDSIVRAAPGQRLPESLRATYREGFYNEYMQRVFKYLGEQGVRPRDLSAIYEAIPLSPGMSDLLQFVAKQGACFEVILISDANTFGVESSLRAAGHHSLFRRILSNPSGPDARGLLALRPFHTHSCARCPANMCKHKVLSDYLRERAHDGVHFERLFYVGDGANDFCPMGLLAGGDVAFPRRGYPMHRLIQEAQKAEPSSFRASVVPWETAADVRLHLQQVLKSC | Function: Phosphatase that has a high activity toward phosphoethanolamine (PEA) and phosphocholine (PCho) . Involved in the generation of inorganic phosphate for bone mineralization (By similarity). Acts in a non-redundant manner with PHOSPHO1 in skeletal mineralization: while PHOSPHO1 mediates the initiation of hydroxyapatite crystallization in the matrix vesicles (MVs), ALPL/TNAP catalyzes the spread of hydroxyapatite crystallization in the extracellular matrix (By similarity).
Catalytic Activity: H2O + phosphoethanolamine = ethanolamine + phosphate
Sequence Mass (Da): 29713
Sequence Length: 267
Subcellular Location: Extracellular vesicle
EC: 3.1.3.75
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Q8R2H9 | MSGCFPAVGLRCLSRDGRMAAPGAPRFLLTFDFDETIVDENSDDSIVRAAPGQQLPESLRATYREGYYNEYMQRVFKYLGEQGVRPRDLRAVYETIPLSPGMGDLLQFIAKQGSCFEVILISDANTFGVESALRAAGHHSLFRRILSNPSGPDARGLLTLRPFHTHSCSRCPANMCKHKVLSEYLRERARDGVHFERLFYVGDGANDFCPMGLLAGGDVAFPRRGYPMHRLIQEAQKAEPSSFRAHVVPWETAADVRQHLQQVLKMC | Function: Phosphatase that has a high activity toward phosphoethanolamine (PEA) and phosphocholine (PCho) (By similarity). Involved in the generation of inorganic phosphate for bone mineralization . Acts in a non-redundant manner with PHOSPHO1 in skeletal mineralization: while PHOSPHO1 mediates the initiation of hydroxyapatite crystallization in the matrix vesicles (MVs), ALPL/TNAP catalyzes the spread of hydroxyapatite crystallization in the extracellular matrix .
Catalytic Activity: H2O + phosphoethanolamine = ethanolamine + phosphate
Sequence Mass (Da): 29911
Sequence Length: 267
Subcellular Location: Extracellular vesicle
EC: 3.1.3.75
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Q2KI06 | MKILLVFDFDNTIIDDNSDTWIVQCAPEKKLPLELKDSYKKGFWTEFMGRVFKYLGDEGVREDEMKRAMISMPFTPGMVELLNFIRKNKNKFDCIIISDSNSVFIDWVLEATNFHDVFDKVFTNPAAFDSNGHLTVEKHHTHSCTRCPQNLCKNVVLVEFVGEQLQQGVNYTRIVYIGDGGNDVCPVTFLKKNDIAMPRKGYALQKTLYRMCQNLEPMESSVVSWSSGVEIISYLQFLIKE | Function: Phosphatase that has high activity toward pyridoxal 5'-phosphate (PLP). Also active at much lower level toward pyrophosphate, phosphoethanolamine (PEA), phosphocholine (PCho), phospho-l-tyrosine, fructose-6-phosphate, p-nitrophenyl phosphate, and h-glycerophosphate.
Catalytic Activity: H2O + pyridoxal 5'-phosphate = phosphate + pyridoxal
Sequence Mass (Da): 27751
Sequence Length: 241
EC: 3.1.3.74
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Q8TCD6 | MKILLVFDFDNTIIDDNSDTWIVQCAPNKKLPIELRDSYRKGFWTEFMGRVFKYLGDKGVREHEMKRAVTSLPFTPGMVELFNFIRKNKDKFDCIIISDSNSVFIDWVLEAASFHDIFDKVFTNPAAFNSNGHLTVENYHTHSCNRCPKNLCKKVVLIEFVDKQLQQGVNYTQIVYIGDGGNDVCPVTFLKNDDVAMPRKGYTLQKTLSRMSQNLEPMEYSVVVWSSGVDIISHLQFLIKD | Function: Phosphatase that has high activity toward pyridoxal 5'-phosphate (PLP). Also active at much lower level toward pyrophosphate, phosphoethanolamine (PEA), phosphocholine (PCho), phospho-l-tyrosine, fructose-6-phosphate, p-nitrophenyl phosphate, and h-glycerophosphate.
Catalytic Activity: H2O + pyridoxal 5'-phosphate = phosphate + pyridoxal
Sequence Mass (Da): 27769
Sequence Length: 241
EC: 3.1.3.74
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P13792 | MNKKILVVDDEESIVTLLQYNLERSGYDVITASDGEEALKKAETEKPDLIVLDVMLPKLDGIEVCKQLRQQKLMFPILMLTAKDEEFDKVLGLELGADDYMTKPFSPREVNARVKAILRRSEIAAPSSEMKNDEMEGQIVIGDLKILPDHYEAYFKESQLELTPKEFELLLYLGRHKGRVLTRDLLLSAVWNYDFAGDTRIVDVHISHLRDKIENNTKKPIYIKTIRGLGYKLEEPKMNE | Function: Member of the two-component regulatory system PhoP/PhoR involved in the regulation of alkaline phosphatase genes phoA and phoB and of phosphodiesterase.
PTM: Phosphorylated by PhoR.
Sequence Mass (Da): 27598
Sequence Length: 240
Subcellular Location: Cytoplasm
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F4IRM4 | MGKPTGKKKNNNYTEMPPTESSTTGGGKTGKSFDRSATKSFDDDMTIFINRALELKEEGNKLFQKRDYEGAMFRYDKAVKLLPRDHGDVAYLRTSMASCYMQMGLGEYPNAINECNLALEASPRFSKALLKRARCYEALNKLDFAFRDSRVVLNMEPENVSANEIFERVKKVLVGKGIDVDEMEKNLVNVQPVGAARLRKIVKERLRKKKKKSMTMTNGGNDGERKSVEAVVEDAKVDNGEEVDSGRKGKAIEEKKLEDKVAVMDKEVIASEIKEDATVTRTVKLVHGDDIRWAQLPLDSSVVLVRDVIKDRFPALKGFLIKYRDSEGDLVTITTTDELRLAASTREKLGSFRLYIAEVSPNQEPTYDVIDNDESTDKFAKGSSSVADNGSVGDFVESEKASTSLEHWIFQFAQLFKNHVGFDSDSYLELHNLGMKLYTEAMEDIVTGEDAQELFDIAADKFQEMAALAMFNWGNVHMSKARRQIYFPEDGSRETILEKVEAGFEWAKNEYNKAAEKYEGAVKIKSDFYEALLALGQQQFEQAKLCWYHALSGEVDIESDASQDVLKLYNKAEESMEKGMQIWEEMEERRLNGISNFDKHKELLQKLGLDGIFSEASDEESAEQTANMSSQINLLWGSLLYERSIVEYKLGLPTWDECLEVAVEKFELAGASATDIAVMVKNHCSSDNALEGMGFKIDEIVQAWNEMYDAKRWQIGVPSFRLEPLFRRRSPKLHDILENVFSGPQ | Function: Carboxylate clamp type tetratricopeptide repeat protein that may act as a potential Hsp90/Hsp70 co-chaperone . Contributes to polar growth of root hairs .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 84222
Sequence Length: 745
Subcellular Location: Cytoplasmic vesicle membrane
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P13064 | MTQGAKKAPVIWVQGEGCTGCSVSLLNAVCPR | Cofactor: Binds 1 [3Fe-4S] cluster.
Catalytic Activity: A + H2 = AH2
Sequence Mass (Da): 3305
Sequence Length: 32
Subcellular Location: Periplasm
EC: 1.12.99.6
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B3FK34 | MPVKVCLIFAGGTGMNVATKLVDLGEAVHCFDTCDKNVVDVHRSVNVTLTKGTRGAGGNRKVILPLVRPQIPALMDTIPEADFYIVCYSLGGGSGSVLGPLITGQLADRKASFVSFVVGAMESTDNLGNDIDTMKTLEAIAVNKHLPIVVNYVPNTQGRSYESINDEIAEKIRKVVLLVNQNHGRLDVHDVANWVRFTDKHNYLIPQVCELHIETTRKDAENVPEAISQLSLYLDPSKEVAFGTPIYRKVGIMKVDDLDVTDDQIHFVINSVGVVEIMKTITDSKLEMTRQQSKFTQRNPIIDADDNVDEDGMVV | Function: A tubulin-like GTPase that forms filaments, which are required for positioning viral DNA and capsids in the middle of the host cell for optimal replication . The motor component of a partition system which pushes phage DNA (encased by protein gp105) to the center of the bacterial host cell . Also required for movement of phage capsids to the vicinity of the viral DNA and rotation of the encased viral DNA at midcell . Forms filaments during the lytic phase, which position phage DNA at the center of the bacterial host cell . Filaments have a three-stranded intertwined achitecture and form a spindle-like cytoskeleton within the infected cell . Has GTPase activity . Filaments grow at the plus end and depolymerize at the minus end, a process called treadmilling, and switch from growing in a polar manner to catastrophic depolymerization, i.e. they display dynamic instability, like tubulin. In infected host cells the filament ends close to the cell pole are relatively stable, while the other end near the phage DNA is highly dynamic . Both capsid movement and DNA rotation probably require treadmilling (Probable).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 34621
Sequence Length: 315
Domain: Consists of two domains: a nucleotide-binding N-terminus that hydrolyzes GTP and a C-terminus domain necessary for polymerization . The domains are bridged by a long, central helix . Interactions between the C-terminus and the following monomer drive polymerization .
Subcellular Location: Host cytoplasm
EC: 3.6.5.-
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Q8SDC3 | MMSKVKTRIYFCGGAGFRIGELFHGYHEDVCYIDTSVQNKHKHNTDDNTIIIEADTKLADQTARKRAIGMGKDRKAAAELISAHIPAIAHHFPAGDTNIVVYSMGGASGSTIGPSLVSHLQQQGEVVVSVVIGSYDSDISLRNSSGSLKTFEGVSSVSKVPMIINYHENVEGIPQSMVNQNILEVLNALVILFNQEHQSLDLMDITNWAHFHKHHDVPVQTVQLHVCFDRQEAQAILDPISIASLYTDPDRDVSISTVLTRTTGYADPEKYDFDQMHFVINGLSIEDIRKRLEERREMMNRAKANMRKRQSTLDVDDQATSSGLVFD | Function: A tubulin-like GTPase that forms filaments, which are required for positioning viral DNA and capsids in the middle of the host cell for optimal replication. The motor component of a partition system which pushes phage DNA (encased by protein gp105) to the center of the bacterial host cell . Also required for movement of phage capsids to the vicinity of the viral DNA and rotation of the encased viral DNA at midcell . Forms filaments during the lytic phase, which position phage DNA at the center of the bacterial host cell . Filaments have a three-stranded intertwined architecture and form a spindle-like cytoskeleton within the infected cell . Has GTPase activity (Probable). Filaments grow at the plus end and depolymerize at the minus end, a process called treadmilling, and switch from growing in a polar manner to catastrophic depolymerization, i.e. they display dynamic instability, like tubulin (By similarity). In infected host cells the filament ends close to the cell pole are relatively stable, while the other end near the phage DNA is highly dynamic. Both capsid movement and DNA rotation probably require treadmilling (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 36425
Sequence Length: 327
Domain: Consists of two domains: a nucleotide-binding N-terminus that hydrolyzes GTP and a C-terminus domain necessary for polymerization. The domains are bridged by a long, central helix. Interactions between the C-terminus and the following monomer drive polymerization.
Subcellular Location: Host cytoplasm
EC: 3.6.5.-
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F8SJR0 | MSKVKTRVYCCGGTGMDIGVNLQWHPDLVFIDTCDKNVTADHDLERVFLTEGTRGAGKNRRYMLPIIRPQVPGFLERYPAGDFNIVVFGLGGGSGSTIGPVIVSELAKAGESVAVVCMSGIEATEVLQNDIDTLKTLEGIAAATNTPVVINHIENVNGVPYTELDKEAIFNIHALINLTSQKHVRLDKLDIDNWINFTKKHNQIQPQLCQLHISNNRQEATSVPEPIAIASLFADASREVAFGTPFVRTVGISDVSDPDLLADQLHFVINSIGVASLFGSLTKQKQELEAAQVRYQQRNAIIDIDDNRTDDGFVV | Function: A tubulin-like GTPase that forms filaments, which are required for positioning viral DNA and capsids in the middle of the host cell for optimal replication . The motor component of a partition system which pushes phage DNA (encased by protein gp105) to the center of the bacterial host cell (By similarity). Also required for movement of phage capsids to the vicinity of the DNA and rotation of the encased viral DNA at midcell (By similarity). Forms filaments during the lytic phase, which position phage DNA at the center of the bacterial host cell . Filaments have a three-stranded intertwined architecture and form a spindle-like cytoskeleton within the infected cell (By similarity). Has GTPase activity (By similarity). Filaments grow at the plus end and depolymerize at the minus end, a process called treadmilling, and switch from growing in a polar manner to catastrophic depolymerization, i.e. they display dynamic instability, like tubulin (By similarity). In infected host cells the filament ends close to the cell pole are relatively stable, while the other end near the phage DNA is highly dynamic (By similarity). Both capsid movement and DNA rotation probably require treadmilling (Probable).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 34453
Sequence Length: 315
Domain: Consists of two domains: a nucleotide-binding N-terminus that hydrolyzes GTP and a C-terminus domain necessary for polymerization. The domains are bridged by a long, central helix. Interactions between the C-terminus and the following monomer drive polymerization.
Subcellular Location: Host cytoplasm
EC: 3.6.5.-
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Q7N8B1 | MEKIMPISPISGHMPLSQIQVPQHATTSPLLEQGNRLFEQSVRRGPLHFQSSSLKHLCAELRQLQNAPSSMQARRVQDAIQHWENHHPKEVMARSTRLAELKQALAEQGTVGRTLQSKVMATGPQVILKQPMPALPQSIAAQITKAQTGCTTTLVSSATAELIKHNQNNQQHIKDSDGRKPVNNMPPPPPPPMADKTQKVKKWVVNTDSKQLQALRYYSAQGYNLINTYLRGGEYVKHQAIETLLSRNYLHSNEPTPQEFDAGMRAYIQDVTEGLNELAITDHKKVYRGLKFDKSELKNLLDQYTTEGNIIAEKGFLSTSPDKAWVNDTILVINLESGHKGRILGDAAHFKGEAEMLFPPESKMLVEKVLNRDDKEFDSHFSNLRLTDDASADTTRIKRIINIKMLNE | Function: Mono-ADP-ribosylates chicken skeletal alpha-actin and human non-skeletal beta- and gamma-actin. Mono-ADP-ribosylates 'Arg-177' of yeast actin, blocking its ability to polymerize. Does not possess NAD(+)-glycohydrolase activity, unlike most mART enzymes. Upon expression in S.cerevisiae almost completely inhibits growth.
Catalytic Activity: L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide
Sequence Mass (Da): 45857
Sequence Length: 408
EC: 2.4.2.31
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Q9FNP4 | MLQEPSAAFSLRRNSFRRRSPRSNVDDRGWNPLHIKARKGDLKSVKQLLDQGMDVNALAWGPKSKGVSALHLAAEGGHIEVMDLLLERGANIDAKTWGSCGWTPLHAAAKERKREAVKFLVENGAFLADDITDTRFNPPVHYCHGLEWAYEEMKKLNSESSSSSGGDTSSSSDN | Function: Promotes anthocyanin accumulation through interaction with PHYA, especially in response to far-red light, high light and sucrose treatment, probably by triggering A3G2XYLT/UF3GT expression . Required for gametophytes development as well as male-female gamete recognition during fertilization, possibly by regulating mitochondrial gene expression . Represses PHYA-mediated PIF3 phosphorylation .
PTM: Phosphorylated by PHYA.
Sequence Mass (Da): 19207
Sequence Length: 174
Subcellular Location: Cytoplasm
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A0A0A7EPL0 | MVIPATSRFGFRAEFNTKEFQASCISLANEIDAAIGRNEVPGNIQELALILNNVCRRKCDDYQTRAVVMALMISVKSACQLGWFPERETQELLAIIDLMWNGFSCPENVTSCVNSPVTLISQVIERFYPCVKLGHILVSFEAKPESKMMMKDFHISKKMPHSPKQKVGLFVVRTEDISRSNCIVHPQGVSFLLNGKGIDKRVNISMESGPQLPTNVTALLNLGANLLQAIGCFGGSYLIAIAFMDVIPLPNKPLLKDYVHPEVVGSNSDCDIIEGPSRISLSCPISRTRIKLPVKGHVCKHLQCFDFWNYVNMNTRRPSWRCPHCNQSVCYTDIRVDQKLRKILEEVGRNAADVVISADGTWMVETENDEDVELVPETTHDHGDPNSFINLGPTVKNPARDENEMETSTQVEEHNPCLSEIQGPSNDTHRPASDYTMLNQSHTSTNTLPQLPRTLNAFDGQQFVNLPQVINTRDSPASQALPMTFSPTPSPQDILATNAANFGTSMPAAQSSQFQGSHVTSLGNCEGRTSDLMARWNHIYGRVQTQFPPAPLSHHHYSMQNQSPSPAQQRPVPSYIAHPQTFHVNYGENADQRWMPSSIAHPQTLPVNYGGNTNQRPIPSSIAHPQTLPVNYRGNTDHRSTPYSITHLQTLLNYGGNADQRPMPSSITNLQTLPATYGGYAHQRPMSSSITHPRTSPVNYGGTPDQRPMPSSITHPQTLPVSYGGTTDQILNPGGAMGQFSSREFMNLTPANTENWRPQSRMRGSVAPGTGYDHMIIHPTRPVHPQAQTPPAPLSTSYDGADEIQAFIGHPSYPVSNNETQAGTSSLPVAEGLGYSGSFWSMPPETW | Function: Together with MOM1 and PIAL2, regulates transcriptional gene silencing (TGS) independently of changes in DNA methylation . E4-type SUMO ligase that promotes SUMO chain formation in a SCE1-dependent manner and thus contributes to a pathway for proteolytic removal of sumoylation substrates . Involved in stress responses (e.g. osmotic, salt and abscisic acid ABA) and sulfur metabolism .
Sequence Mass (Da): 93475
Sequence Length: 847
Pathway: Protein modification; protein sumoylation.
Subcellular Location: Nucleus
EC: 2.3.2.-
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F4JYG0 | MSTAAAARPVAGTGLREKTAASLVNSFRLASVTQRLRYHIQDGAKVDPKEFQICCISFAKGIDFAIANNDIPKKVEEFPWLLKQLCRHGTDVYTKTALMVLMISVKHACHLGWFSDSESQELIALADEIRTCFGSSGSTSPGIKSPGSTFSQIMERFYPFVKLGHVLVSFEVKAGYTMLAHDFYISKNMPHSLQEKIRLFVAQTDNIDTSACISNPPEVSFLLNGKGVEKRVNIAMDTGPQLPTNVTAQLKYGTNLLQVMGNFKGNYIIIIAFTGLVVPPEKPVLKDYLQSGVIEASPDSDIIEGPSRVSLSCPISRKRIKLPVKGQLCKHLQCFDFSNYVHINMRNPTWRCPHCNQPVCYPDIRLDQNMAKILKDVEHNAADVIIDAGGTWKVTKNTGETPEPVREIIHDLEDPMSLLNSGPVVFDLTGDDDAELEVFGDNKVEDRKPCMSDAQGQSNNNNTNKHPSNDDYSSIFDISDVIALDPEILSALGNTAPQPHQASNTGTGQQYSNLSQIPMSIDPMPVPVPFSQTPSPRDRPATTSTVFTIPNPSPQYSQVHASPVTPTGTYLGRTTSPRWNQTYQSQAPPMTTPYTSRKVSVPVTSQSPANVSSFVQSQHVPRVLSQPNNYGVRGLTSSHASTSRQHPSGPTVQSVSRLSDLVDVDLTVPDTSNWRPRMRGSLVPGSHSTALDHMIIRPSQQSQTSTRLNSSQPVQTPSVQTSQAQSPFTTAAYRTETVLGNRNHPVPAPPGIVRPTGPTS | Function: Together with MOM1 and PIAL1, regulates transcriptional gene silencing (TGS) independently of changes in DNA methylation . E4-type SUMO ligase that promotes SUMO chain formation in a SCE1-dependent manner and thus contributes to a pathway for proteolytic removal of sumoylation substrates . Involved in stress responses and sulfur metabolism .
Sequence Mass (Da): 83109
Sequence Length: 760
Pathway: Protein modification; protein sumoylation.
Subcellular Location: Nucleus
EC: 2.3.2.-
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Q8IYJ0 | MESRMWPALLLSHLLPLWPLLLLPLPPPAQGSSSSPRTPPAPARPPCARGGPSAPRHVCVWERAPPPSRSPRVPRSRRQVLPGTAPPATPSGFEEGPPSSQYPWAIVWGPTVSREDGGDPNSANPGFLDYGFAAPHGLATPHPNSDSMRGDGDGLILGEAPATLRPFLFGGRGEGVDPQLYVTITISIIIVLVATGIIFKFCWDRSQKRRRPSGQQGALRQEESQQPLTDLSPAGVTVLGAFGDSPTPTPDHEEPRGGPRPGMPHPKGAPAFQLNRIPLVNL | Function: Acts as a ligand for PILRA in neural tissues, where it may be involved in immune regulation.
PTM: O-glycosylation at Thr-140 is essential for recognition by PILRA.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 30076
Sequence Length: 282
Subcellular Location: Membrane
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O75925 | MADSAELKQMVMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLLKAGCSPAVQMKIKELYRRRFPQKIMTPADLSIPNVHSSPMPATLSPSTIPQLTYDGHPASSPLLPVSLLGPKHELELPHLTSALHPVHPDIKLQKLPFYDLLDELIKPTSLASDNSQRFRETCFAFALTPQQVQQISSSMDISGTKCDFTVQVQLRFCLSETSCPQEDHFPPNLCVKVNTKPCSLPGYLPPTKNGVEPKRPSRPINITSLVRLSTTVPNTIVVSWTAEIGRNYSMAVYLVKQLSSTVLLQRLRAKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHLIIDGLFMEILKYCTDCDEIQFKEDGTWAPMRSKKEVQEVSASYNGVDGCLSSTLEHQVASHHQSSNKNKKVEVIDLTIDSSSDEEEEEPSAKRTCPSLSPTSPLNNKGILSLPHQASPVSRTPSLPAVDTSYINTSLIQDYRHPFHMTPMPYDLQGLDFFPFLSGDNQHYNTSLLAAAAAAVSDDQDLLHSSRFFPYTSSQMFLDQLSAGGSTSLPTTNGSSSGSNSSLVSSNSLRESHSHTVTNRSSTDTASIFGIIPDIISLD | Function: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation (By similarity). Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (By similarity).
PTM: Sumoylated.
Sequence Mass (Da): 71836
Sequence Length: 651
Domain: The LXXLL motif is a transcriptional coregulator signature.
Pathway: Protein modification; protein sumoylation.
Subcellular Location: Nucleus speckle
EC: 2.3.2.-
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O75928 | MADFEELRNMVSSFRVSELQVLLGFAGRNKSGRKHDLLMRALHLLKSGCSPAVQIKIRELYRRRYPRTLEGLSDLSTIKSSVFSLDGGSSPVEPDLAVAGIHSLPSTSVTPHSPSSPVGSVLLQDTKPTFEMQQPSPPIPPVHPDVQLKNLPFYDVLDVLIKPTSLVQSSIQRFQEKFFIFALTPQQVREICISRDFLPGGRRDYTVQVQLRLCLAETSCPQEDNYPNSLCIKVNGKLFPLPGYAPPPKNGIEQKRPGRPLNITSLVRLSSAVPNQISISWASEIGKNYSMSVYLVRQLTSAMLLQRLKMKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLMCPLGKMRLTIPCRAVTCTHLQCFDAALYLQMNEKKPTWICPVCDKKAAYESLILDGLFMEILNDCSDVDEIKFQEDGSWCPMRPKKEAMKVSSQPCTKIESSSVLSKPCSVTVASEASKKKVDVIDLTIESSSDEEEDPPAKRKCIFMSETQSSPTKGVLMYQPSSVRVPSVTSVDPAAIPPSLTDYSVPFHHTPISSMSSDLPGLDFLSLIPVDPQYCPPMFLDSLTSPLTASSTSVTTTSSHESSTHVSSSSSRSETGVITSSGSNIPDIISLD | Function: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulator in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and the PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity. Isoform PIAS2-beta, but not isoform PIAS2-alpha, promotes MDM2 sumoylation. Isoform PIAS2-alpha promotes PARK7 sumoylation. Isoform PIAS2-beta promotes NCOA2 sumoylation more efficiently than isoform PIAS2-alpha. Isoform PIAS2-alpha sumoylates PML at'Lys-65' and 'Lys-160'.
PTM: Sumoylated.
Sequence Mass (Da): 68240
Sequence Length: 621
Domain: The LXXLL motif is a transcriptional coregulator signature.
Pathway: Protein modification; protein sumoylation.
Subcellular Location: Nucleus speckle
EC: 2.3.2.-
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P04737 | MNAVLSVQGASAPVKKKSFFSKFTRLNMLRLARAVIPAAVLMMFFPQLAMAAGSSGQDLMASGNTTVKATFGKDSSVVKWVVLAEVLVGAVMYMMTKNVKFLAGFAIISVFIAVGMAVVGL | Function: Propilin is the precursor of the pilus subunit, pilin, that forms conjugative pili, the filamentous surface appendages required for cell-to-cell contact during the earlier stages of bacterial conjugation, and that retract after contact is established. Mature pilin is assembled with the help of TraQ and TraX . Functions as a receptor for CdiA-CT from E.cloacae and E.coli, although it is not clear if this is physiologically relevant .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12768
Sequence Length: 121
Subcellular Location: Cell inner membrane
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P12060 | MNLSFAKGGLPAPVKNRAWQYCQMAWRGVTSKKALSRLAALSPLLLLGVGQMASATDLLAGGKDDVKATFGADSFVMMCIIIAELIVGVAMYIRTKNLLILLGLVVVIVFTTVGLTFIK | Function: Propilin is the precursor of the pilus subunit, pilin, that forms conjugative pili, the filamentous surface appendages required for cell-to-cell contact during the earlier stages of bacterial conjugation, and that retract after contact is established. Mature pilin is assembled with the help of TraQ and TraX (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12688
Sequence Length: 119
Subcellular Location: Cell inner membrane
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P53252 | MHRTYSLRNSRAPTASQLQNPPPPPSTTKGRFFGKGGLAYSFRRSAAGAFGPELSRKLSQLVKIEKNVLRSMELTANERRDAAKQLSIWGLENDDDVSDITDKLGVLIYEVSELDDQFIDRYDQYRLTLKSIRDIEGSVQPSRDRKDKITDKIAYLKYKDPQSPKIEVLEQELVRAEAESLVAEAQLSNITRSKLRAAFNYQFDSIIEHSEKIALIAGYGKALLELLDDSPVTPGETRPAYDGYEASKQIIIDAESALNEWTLDSAQVKPTLSFKQDYEDFEPEEGEEEEEEDGQGRWSEDEQEDGQIEEPEQEEEGAVEEHEQVGHQQSESLPQQTTA | Function: Negative regulator of cell wall integrity (CWI) in unstressed cells, probably by inhibiting protein kinase PKH1/PHK2 activity and regulating their downstream CWI pathways PKC1-MAP kinase pathway and protein kinase YPK1 pathway. Activity may be regulated by the transient increase of sphingolipid long chain bases (LCBs) during heat stress.
PTM: Phosphorylated by PKH1 and PKH2. Phosphorylation is inhibited by sphingolipid long chain bases (LCBs).
Sequence Mass (Da): 38349
Sequence Length: 339
Subcellular Location: Lipid droplet
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B6JFP0 | MSASGRSAREKLNFQLGLRRRGISDQAVLRALEDVPREQFVEPHDKEVAYADTALGIACGQTISQPYVVAYMTEQLRTHPRHRALEIGTGSGYQAAVLSRLCRQVVTVERYRTLADTARARLAALGCRNVEVVVGDGYDVPDTLGTFDRIIVTAAMETIPDSLMERLEPDGIMLVPVGPPEGVQQLVRLRKGADGVEQEDLIPVRFVPALVGLAKEL | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 23777
Sequence Length: 217
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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Q2IIL9 | MSRELAEWLGHMGIRDRRVLDAIAELDRARFVPPHLVAEAYADRPLPIGFGQTISQPFVVAFMTEALGLDGGERVLEVGTGSGYQTALLARLAGEVWSVEIVPGLAARARALLLGDLGLANVHLREGDGALGWPEAAPFDRILVTAAAPQVPPPLRAQLAPGGRMVLPVGEAESEQVLRVLERAADGIEEIEDLLPVRFVPLTHLPPAV | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22361
Sequence Length: 209
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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A8I4G3 | MTDSEAERAERAAFILSLRRRGIRDLAVLRALELVPRGLFVDPTLRRHAYEDVALPIACGQTMSQPSLVALMTEALALNAEHTVLEIGTGSGYQAAVLSHLAAQVVTMDRYRALVGEAQTRFQVLGLRNVAAFVGDGTQGLPGRAPYDRIMITAATGEVPRALVDQLKPGGVLIAPIGAPREVQKLRRFIKDGGNLEASDLMDVRFVPLVAGVAALL | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 23290
Sequence Length: 217
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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A1K4F0 | MSGRQDASHAGRARARMVERLRAQGIQDEGALAAMMQVPRHLFVEEGLAYSAYDDTALPIGFQQTISQPYVVARMIELLRSGGRQLGRVLEIGAGCGYQAAVLSTLATEVYAVERIRPLLDKARANLRPLRLPNVRLKHADGTLGLPEAAPFESIIVAAAAGGVPNALKEQLAPGGRLIIPVGGGEQRLLLIERQGNVFRESGYEAVRFVPLLAGTE | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 23331
Sequence Length: 217
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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Q2L008 | MRKPVGSKDGSGVYSRQGLDGYTPANSNTRISTATLPRPEPLRPAASSANLGLNSDRLRLAMVQRLRQMGITDDRVLDAMAAVPRHTFVDEALASRAYEDAALPIGHSQTISQPWVVARMIAAVCEARAPSRVLEVGAGCGYQAAVLAQFVREVHSIERIRGLYELARANLRALRLSTRVRLIYGDGTQGVPGVAPFDAIVVAAAGLAIPQALLNQLAPGGRLIAPEGSTSQRLVLIERTGTASWKRMELEAVRFVPLKAGIQS | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28283
Sequence Length: 264
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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P15246 | MAWKSGGASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYAKCNPYMDSPQSIGFQATISAPHMHAYALELLFDQLNEGAKALDVGSGSGILTACFARMVGPSGKVIGIDHIKELVDDSINNVRKDDPMLLSSGRVQLVVGDGRMGYAAEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPAGGNQMLEQYDKLQDGSVKMKPLMGVIYVPLTDKEKQWSRWK | Function: Initiates the repair of damaged proteins by catalyzing methyl esterification of L-isoaspartyl and D-aspartyl residues produced by spontaneous isomerization and racemization of L-aspartyl and L-asparaginyl residues in aging peptides and proteins (By similarity). Acts on EIF4EBP2, microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin C-terminal hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-synuclein and alpha-synuclein (By similarity).
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24565
Sequence Length: 227
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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A6X6Y1 | MRNFEKARVQMVEQLVHRGIHDTRVLEAMGTLAREKFIDEGFIEFAYDDTPLPIKNGQTISQPYMTAFMIASAHLGGGEHVLEIGTGSGYAAAIIAQIAGQIFTVERYSTLAEAAQQRFEDLGCDNIHVRTGDGSNGWPEEAPFDAIIVAAGAPEIPSPLKEQLKPGGRLIIPVGSMAGTQRLLCITRKSTEEFDEEDLGGVMFVPLVGNKAWPDMN | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 23632
Sequence Length: 217
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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Q6M116 | MPLNEIIPVIENLISRGYIKKQSVIDAILSVPRHKFISKSMESYAYVDSPLEIGYGQTISAIHMVGIMCEELDLDEGQNVLEVGTGSGYHAAVVSKIVGESGKVTTIERIPELFENSKKTLSELGYNNVEVVLGDGTKGYLENAPYDRIYVTASGPDVPKALFKQLNDGGILLAPVGAHFQTLMRYTKINGSISEEKLLEVAFVPLIGENGF | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 23108
Sequence Length: 212
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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B1ZJW1 | MTDAARARMLETQLIARGIRDAALLDAMGRVAREAFVPAEFAAEAYADGPLPIGAGQTISQPYIVALMIEALALRPGERVLEVGAGCGYAAAVLATMGARIFAIERHAALAEAARARLAALGLAVRLRVGDGHAGWPEAAPFDAILVSAAGSAVPEALKRQLAQGGRLVIPVGPPGGQTLLRLTRRGPERFESRDFGPVSFVPLLRGVGAAG | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 21935
Sequence Length: 212
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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A2SF76 | MSAGQRPAPKFPLRLDQVKPAGRSGAAPLLRPQRPLHQAATERGRGTTPAGLGLDSHLVRERMLARLQAEGVRDARVLAAMRAVPRHSFVDTALANQAYEDTSLPIGLGQTISKPSVVARMIELMLALQPAGARPRLLEIGSGCGYQAAVLAQLARQVVSIERLRPLYDKARENLAPLNFGNLRLVYGDGRIGHAPNAPYDGIIAAAGGEDIPQPWIDQLGPGGRLVAPMLDARSGGQVLVVIDRHADGNLVRSLHEAVRFVPLKSGTD | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28738
Sequence Length: 269
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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O26915 | MMDERRRMVQDLMERGYIKSEAVRRAMERVPREEFVPEDEMHRAYMDMPLPIGEGQTISAPHMVAMIAEILDLEPGMKVLEIGTGCGYNAAVIAEIIGPEGHLYTVERIGILYERARKKLRSLGYDNITVIHGDGSQGFADEAPYSRIYVTAAAPYIPDPLMKQLEIGGKLLIPVGSDKFYQELVLIERTSADDYRSRNLGGVAFVPLIGKHGWKFH | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity).
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24424
Sequence Length: 217
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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P23506 | MAWKSGGASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYAKSNPYMDSPQSIGFQATISAPHMHAYALELLFDQLHEGAKALDVGSGSGILTACFARMVGNSGKVIGIDHIKELVDDSITNVKKDDPMLLSSGRVRLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPAGGNQMLEQYDKLQDGSVKMKPLMGVIYVPLTDKEKQWSRWK | Function: Initiates the repair of damaged proteins by catalyzing methyl esterification of L-isoaspartyl and D-aspartyl residues produced by spontaneous isomerization and racemization of L-aspartyl and L-asparaginyl residues in aging peptides and proteins . Acts on EIF4EBP2, microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin C-terminal hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-synuclein and alpha-synuclein .
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24634
Sequence Length: 227
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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Q1D6W9 | MGDWGRADYLSRHGIKDARVLEAIARLNRADFVPEDLREEASADSPLPIGHGQTISQPYVVALMTEALQLQGDERVLEIGTGSGYQTALLSLLCREVYSVEIVPELAQSAREVLGRQGFENVSFREGDGSLGWPDQAPFDAILAAAAPPDVPLQLLSQLKPGGRMIIPVGPRGGTQQLLRIQRALRPGEVPQVESLLSVRFVPMTGQPLSQG | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22929
Sequence Length: 212
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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B2A578 | MKDKFSAQREKMVQKQLAKRDIEDPKVLDAFRKVPREEFITESKQHQAYGDHPLPIGHGQTISQPYIVAMMTQALEPSSHDIVLEVGTGSGYQTAILAELTKKVFSLERIPELSEQAGRILSKLGYQNIVLKISDDDNDLTIHEQKEFDKIIVTAAASQIPPELTQQLKEGGTLVIPVGELMFQELLVVTKHNGELRKKSLGGCRFVPLK | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 23515
Sequence Length: 210
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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Q82VW0 | MSVRHSGIGMTSLRTRVRMVERLREQGIKDEVVLAAMGFIPRHLFVEAALASRAYEDVALPINYGQTISSPWIVGRMTELLRNGGSNSLRKILEIGTGCGYQTAVLAKIASEVYSIERIGPLLTRTRIRLRELGILNIHLKHADGMRGLPEAGLFDGIMMTAVIPEIPETLLEQLAMGGRMVFPKGNRKQYLCVIDHTTEGFVETILDEVMFVPILPGTINR | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24641
Sequence Length: 222
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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A1B5M0 | MSDDPETAERKMRFLFALRQRGVTDPRVLEAMERIDRGEFVRGHFEDRAYDDTPLPIPCGQTISQPSVVGLMTQALEVGPRDKVLEIGTGSGYQAAVLSLLCRRVYTIDRHRRLVAEAEALFRHLGLPNITALVGDGSRGLPEQAPFDRIMVTAAAEDPPGPLLAQLKIGGIMVVPVGQSDAVQTLIRVRRGENGFDYDELRQVRFVPLVEGLGQT | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 23832
Sequence Length: 216
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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B2JG67 | MTGERAKRFPLGLEDLVREPRRADARDAKTGKPAVPKPVTSKPAGSSTRAPVVVTPVVKPVVKSAVTKNASGIVNTKSASTIRNDGARNQLPRPATAAFERTGAPNVALTSAVTLTSERVRERMVERLRANGITDPRVLDAMAMVPRHMFVDPGLATQAYEDAALPIGHHQTISKPSVVARMIELAAQGRTLNNVLEIGTGCGYQAAVLSQVARDVYSIERIKPLYERAKTNLRPLRIPNIRLHYGDGRIGLPAAAPFDAIVIAAAGLDVPQALREQLAIGARLVAPVGSQDGQSQVLTLVERTGPAQWRESRLDRVFFVPLKSGVI | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35123
Sequence Length: 327
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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Q6MCW9 | MVEKQIAARGIQDPRVLEAMGKVPRERFVSEHIAPLAYEDRPLSIDEGQTISQPFIVAVMAQQAQITPQDKVLEIGTGSGYSAAILSQLASHVYSMERYPKLAELAKKRLQEFGYNNVTVSVGDGSLGWEEFAPYEVIIVTAGGPQIPPSLLKQLAISGRLVIPVGPSLESQQLMRVMREDADHYRYENLGSVQFVPLVGKEGWQTTSSS | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 23084
Sequence Length: 210
Subcellular Location: Cytoplasm
EC: 2.1.1.77
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Q9LFP6 | MISWLDIYHVVSATVPLYVSMTLGFLSARHLKLFSPEQCAGINKFVAKFSIPLLSFQIISENNPFKMSPKLILSDILQKFLVVVVLAMVLRFWHPTGGRGGKLGWVITGLSISVLPNTLILGMPILSAIYGDEAASILEQIVVLQSLIWYTILLFLFELNAARALPSSGASLEHTGNDQEEANIEDEPKEEEDEEEVAIVRTRSVGTMKILLKAWRKLIINPNTYATLIGIIWATLHFRLGWNLPEMIDKSIHLLSDGGLGMAMFSLGLFMASQSSIIACGTKMAIITMLLKFVLGPALMIASAYCIRLKSTLFKVAILQAALPQGVVPFVFAKEYNLHPEIISTGVIFGMLIALPTTLAYYFLLDL | Function: Component of the intracellular auxin-transport pathway in the male gametophyte . Involved in the regulation of auxin homeostasis in pollen . Involved in the efflux of auxin from the endoplasmic reticulum into the cytoplasm . PIN5 and PIN8 may have an antagonistic/compensatory activity . Involved in the control of vein patterning . Redundantly with PIN6, inhibits the vein-formation-promoting functions of PIN5 . PIN5, PIN6, and PIN8 control vein network geometry, but they are expressed in mutually exclusive domains of leaf vascular cells .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40502
Sequence Length: 367
Subcellular Location: Endoplasmic reticulum membrane
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Q0JJV0 | MVSWKDIYLVLEATVPLYVAMILAYLSIKWWKLFTPEQCSGINKFVAKFSIPLLSFQVISTTDPYDMNIKLIYSDILQKSLALLGFAAISKACCAEKFDWLITGFSLSTLPNTLIVGIPLLKGMYGEQAGKLLSQIVVLQSLIWYTLLLFLFELRAANGMATTTSSETTGLIWALVGFRWHIRLPLIVSNSIRMLSDGGLGMAMFSLGLFTALQTKIIACGAKRMLLALAIRFFLGPALMGMSSYAIGMRGVLLKIAIVQAALPQGIVPFVFAKEYNVQADILSTAIIVGMMVAVPVALAYYFAMIIPAIK | Function: May act as a component of the auxin efflux carrier.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34120
Sequence Length: 311
Subcellular Location: Membrane
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Q5VQY3 | MITGSEVYQVVEAMAPLYTAAALGYGSVRWLKAFSNEQCAGINHFVALYAVPVLIFDMVSTNNVYKMNGRLIAADTLQKAVLLLGLMAWALWERSRARGAGAKAKAAVSSPLQWVITCFSVASLPNTIIMGVPLLNGMYGPVSKDLMKQIVVMQFCIWYNVIIFLYEYMAARRSASAPPPASSEGSAKISPSSPVKAAAAAADTNGNAVAADRPQEVAVNIEITEMAASTARDGVSGETTAAAKEVSSGEVAPVEEEEASAPAPSMKHVIWMAVKKLLQIPNTYASFLGLIWSLIAFKCGFSMPKIVEDSLFTIRTTAVGLSMFSSGTFIARQSRFVPCGYKIASFSMVIKFLIGPVVMLFASLVIGMHGTLLHIAVVQAALPLAVTSFVYAEEYKVHADIMSTGVILGIFISLPVTIVYYILLGL | Function: May act as a component of the auxin efflux carrier.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45565
Sequence Length: 426
Subcellular Location: Membrane
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Q9C6B8 | MITAADFYHVMTAMVPLYVAMILAYGSVKWWKIFTPDQCSGINRFVALFAVPLLSFHFIAANNPYAMNLRFLAADSLQKVIVLSLLFLWCKLSRNGSLDWTITLFSLSTLPNTLVMGIPLLKGMYGNFSGDLMVQIVVLQCIIWYTLMLFLFEYRGAKLLISEQFPDTAGSIVSIHVDSDIMSLDGRQPLETEAEIKEDGKLHVTVRRSNASRSDIYSRRSQGLSATPRPSNLTNAEIYSLQSSRNPTPRGSSFNHTDFYSMMASGGGRNSNFGPGEAVFGSKGPTPRPSNYEEDGGPAKPTAAGTAAGAGRFHYQSGGSGGGGGAHYPAPNPGMFSPNTGGGGGTAAKGNAPVVGGKRQDGNGRDLHMFVWSSSASPVSDVFGGGGGNHHADYSTATNDHQKDVKISVPQGNSNDNQYVEREEFSFGNKDDDSKVLATDGGNNISNKTTQAKVMPPTSVMTRLILIMVWRKLIRNPNSYSSLFGITWSLISFKWNIEMPALIAKSISILSDAGLGMAMFSLGLFMALNPRIIACGNRRAAFAAAMRFVVGPAVMLVASYAVGLRGVLLHVAIIQAALPQGIVPFVFAKEYNVHPDILSTAVIFGMLIALPITLLYYILLGL | Function: Acts as a component of the auxin efflux carrier. Seems to be involved in the basipetal auxin transport. Mediates the formation of auxin gradient which is required to ensure correct organogenesis. Coordinated polar localization of PIN1 is directly regulated by the vesicle trafficking process and apical-basal PIN1 polarity also depends on the phosphorylation of conserved serine residues by PID kinase. The ARF-GEF protein GNOM is required for the correct recycling of PIN1 between the plasma membrane and endosomal compartments.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67019
Sequence Length: 622
Subcellular Location: Cell membrane
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Q09298 | MSMKRFGKAAYRIANELVAKGGRLPIFQRFLPRIFPATYNLGVHVVLKKAPFPRQNALRIARLVTRHGRVFRPFSSVIIERHRFQNQNDWRRKFQPIRKELPRNVDLVERIRQIFGNSLRYNEDLKSTEWPNRIDSYEFGEFLGQGCNAAVYSARLANSDAESSGNTHYGAGFNEVTNILAEIPPVSKVAQKKFPLAIKLMFNFEHDRDGDAHLLKSMGNELAPYPNAAKLLNGQMGTFRPLPAKHPNVVRIQTAFIDSLKVLPDAIERYPDALHTARWYESIASEPKTMYVVMRRYRQTLHEYVWTRHRNYWTGRVIIAQLLEACTYLHKHKVAQRDMKSDNILLEYDFDDEIPQLVVADFGCALACDNWQVDYESDEVSLGGNAKTKAPEIATAVPGKNVKVNFEMADTWAAGGLSYEVLTRSNPFYKLLDTATYQESELPALPSRVNFVARDVIFDLLKRDPNERVKPNIAANALNLSLFRMGEDVKQMMEKCGISQMTTLLAGSSKVLSQKINSRLDKVMNLITAETIMANLAPHLISRAERQLRATFLSRMNREDIWRSLQYFFPAGVQLDTPATSSDCLETISSLMSSFSNDSENYEKQQKPAKNGYNNVPLLLRNVIRTDADGINGIVHRVRSK | Function: Protects against mitochondrial dysfunction during cellular stress, potentially by phosphorylating mitochondrial proteins (By similarity). Plays a role in mitophagy .
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 73054
Sequence Length: 641
Subcellular Location: Mitochondrion
EC: 2.7.11.1
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Q0KHV6 | MSVRLLTVRLIKHGRYILRSYCKRDIHANILDQNQLKTRSKRGFPLPSTAANVLRTTPQQAAKSVVNVVPRTINSPSGSPFNGSGSSPTSSSGIFRVGQHARKLFIDNILSRVTTTYSEDLRQRATRKLFFGDSAPFFALIGVSLASGSGVLSKEDELEGVCWEIREAASRLQNAWNHDEISDTLDSKFTIDDLEIGPPIAKGCAAVVYAADFKKDVASDGASLHTDAQPQATPAFAPNSWSTHEMMSPLQNMSRFVHNFGGSVDNVFHYSQPSAASDFVGAQSREQDQRHHEQQQHQNQEQEQHQNQEPSSSAFNVTSPANSNINSSVDSYPLALKMMFNYDIQSNALSILRAMYKETVPARQRGMNEAADEWERLLQNQTVHLPRHPNIVCMFGFFCDEVRNFPDGHLLYPVAQPQRINPQGYGRNMSLYLLMKRYDHSLRGLLDSQDLSTRNRILLLAQMLEAVNHLSRHGVAHRDLKSDNVLIELQDDAAPVLVLSDFGCCLADKVHGLRLPYVSHDVDKGGNAALMAPEIFNTMPGPFAVLNYGKADLWACGALAYEIFGNRNPFYSSSGGMARERGEMTLSLRNSDYRQDQLPPMSDACPPLLQQLVYNILNPNPSKRVSPDIAANVVQLFLWAPSNWLKAGGMPNSPEILQWLLSLTTKIMCEGRPQMGAGLMPVASCGNRRAYVEYLLICSFLARARLRRIRGALNWIQNVVA | Function: Acts as a serine/threonine-protein kinase . Exhibits a substrate preference for proline at position P+1 and a general preference at several residues for basic residues such as arginine (By similarity). Also exhibits moderate preferences for a phosphotyrosine at position P-3 and a tryptophan at P-5 (By similarity). Critical to mitochondrial homeostasis it mediates several pathways that maintain mitochondrial health and function . Protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins such as park and likely Drp1, to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components . Depending on the severity of mitochondrial damage and/or dysfunction, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to regulating mitochondrial dynamics and eliminating severely damaged mitochondria via mitophagy . Appears to be particularly important in maintaining the physiology and function of cells with high energy demands that are undergoing stress or altered metabolic environment, including spermatids, muscle cells and neurons such as the dopaminergic (DA) neurons . Mediates the translocation and activation of park at the outer membrane (OMM) of dysfunctional/depolarized mitochondria . At the OMM of damaged mitochondria, phosphorylates pre-existing polyubiquitin chains, the Pink1-phosphorylated polyubiquitin then recruits park from the cytosol to the OMM where park is fully activated by phosphorylation at 'Ser-94' by Pink1 . When cellular stress results in irreversible mitochondrial damage, functions with park to promote the clearance of dysfunctional and/or depolarized mitochondria by selective autophagy (mitophagy) . The Pink1-park pathway also promotes fission and/or inhibits fusion of damaged mitochondria, by phosphorylating and thus promoting the park-dependent degradation of proteins involved in mitochondrial fusion/fission such as Marf, Opa1 and fzo . This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes . Also likely to promote mitochondrial fission independently of park and Atg7-mediated mitophagy, via the phosphorylation and activation of Drp1 . Regulates motility of damaged mitochondria by phosphorylating Miro which likely promotes its park-dependent degradation by the proteasome; in motor neurons, this inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria being eliminated in the soma . The Pink1-park pathway is also involved in mitochondrial regeneration processes such as promoting mitochondrial biogenesis, activating localized mitochondrial repair, promoting selective turnover of mitochondrial proteins and initiating the mitochondrial import of endogenous proteins . Involved in mitochondrial biogenesis by promoting the park-dependent ubiquitination of transcriptional repressor Paris which leads to its subsequent proteasomal degradation and allows activation of the transcription factor srl . Functions with park to promote localized mitochondrial repair by activating the translation of specific nuclear-encoded mitochondrial RNAs (nc-mtRNAs) on the mitochondrial surface, including several key electron transport chain component nc-mtRNAs . During oogenesis, phosphorylates and inactivates larp on the membrane of defective mitochondria, thus impairing local translation and mtDNA replication and consequently, reducing transmission of deleterious mtDNA mutations to the mature oocyte . Phosphorylates the mitochondrial acyl-CoA dehydrogenase Mcad, and appears to be important for maintaining fatty acid and amino acid metabolism via a mechanism that is independent of it's role in maintaining production of ATP .
PTM: Proteolytically cleaved . In healthy cells, the precursor is continuously imported into mitochondria where it is proteolytically cleaved into its short form by the mitochondrial rhomboid protease rho-7 . The short form is then released into the cytosol where it rapidly undergoes proteasome-dependent degradation (Probable). In unhealthy cells, when cellular stress conditions lead to the loss of mitochondrial membrane potential, mitochondrial import is impaired leading to the precursor accumulating on the outer mitochondrial membrane (OMM) .
Location Topology: Single-pass membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 80228
Sequence Length: 721
Subcellular Location: Mitochondrion outer membrane
EC: 2.7.11.1
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Q9BXM7 | MAVRQALGRGLQLGRALLLRFTGKPGRAYGLGRPGPAAGCVRGERPGWAAGPGAEPRRVGLGLPNRLRFFRQSVAGLAARLQRQFVVRAWGCAGPCGRAVFLAFGLGLGLIEEKQAESRRAVSACQEIQAIFTQKSKPGPDPLDTRRLQGFRLEEYLIGQSIGKGCSAAVYEATMPTLPQNLEVTKSTGLLPGRGPGTSAPGEGQERAPGAPAFPLAIKMMWNISAGSSSEAILNTMSQELVPASRVALAGEYGAVTYRKSKRGPKQLAPHPNIIRVLRAFTSSVPLLPGALVDYPDVLPSRLHPEGLGHGRTLFLVMKNYPCTLRQYLCVNTPSPRLAAMMLLQLLEGVDHLVQQGIAHRDLKSDNILVELDPDGCPWLVIADFGCCLADESIGLQLPFSSWYVDRGGNGCLMAPEVSTARPGPRAVIDYSKADAWAVGAIAYEIFGLVNPFYGQGKAHLESRSYQEAQLPALPESVPPDVRQLVRALLQREASKRPSARVAANVLHLSLWGEHILALKNLKLDKMVGWLLQQSAATLLANRLTEKCCVETKMKMLFLANLECETLCQAALLLCSWRAAL | Function: Serine/threonine-protein kinase which protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins such as PRKN and DNM1L, to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components . Depending on the severity of mitochondrial damage and/or dysfunction, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to regulating mitochondrial dynamics and eliminating severely damaged mitochondria via mitophagy . Mediates the translocation and activation of PRKN at the outer membrane (OMM) of dysfunctional/depolarized mitochondria . At the OMM of damaged mitochondria, phosphorylates pre-existing polyubiquitin chains at 'Ser-65', the PINK1-phosphorylated polyubiquitin then recruits PRKN from the cytosol to the OMM where PRKN is fully activated by phosphorylation at 'Ser-65' by PINK1 . In damaged mitochondria, mediates the decision between mitophagy or preventing apoptosis by promoting PRKN-dependent poly- or monoubiquitination of VDAC1; polyubiquitination of VDAC1 by PRKN promotes mitophagy, while monoubiquitination of VDAC1 by PRKN decreases mitochondrial calcium influx which ultimately inhibits apoptosis . When cellular stress results in irreversible mitochondrial damage, functions with PRKN to promote clearance of damaged mitochondria via selective autophagy (mitophagy) . The PINK1-PRKN pathway also promotes fission of damaged mitochondria by phosphorylating and thus promoting the PRKN-dependent degradation of mitochondrial proteins involved in fission such as MFN2 . This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes . Also promotes mitochondrial fission independently of PRKN and ATG7-mediated mitophagy, via the phosphorylation and activation of DNM1L . Regulates motility of damaged mitochondria by promoting the ubiquitination and subsequent degradation of MIRO1 and MIRO2; in motor neurons, this likely inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria undergoing mitophagy in the soma . Required for ubiquinone reduction by mitochondrial complex I by mediating phosphorylation of complex I subunit NDUFA10 (By similarity). Phosphorylates LETM1, positively regulating its mitochondrial calcium transport activity .
PTM: Proteolytically cleaved . In healthy cells, the precursor is continuously imported into the inner mitochondrial membrane (IMM), where it is proteolytically cleaved by mitochondrial-processing peptidase (MPP) and then undergoes further proteolytic cleavage by PARL or AFG3L2 to give rise to the 52 kDa short form . The 52 kDa short form is then released into the cytosol where it rapidly undergoes proteasome-dependent degradation . In unhealthy cells, when cellular stress conditions lead to the loss of mitochondrial membrane potential, mitochondrial import is impaired leading to the precursor accumulating on the outer mitochondrial membrane (OMM) . If accumulation at the OMM fails and it is imported into the depolarized mitochondria, it undergoes cleavage by the IMM protease OMA1, promoting its subsequent degradation by the proteasome .
Location Topology: Single-pass membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 62769
Sequence Length: 581
Subcellular Location: Mitochondrion outer membrane
EC: 2.7.11.1
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E0W1I1 | MSLLAYTNLLLQNGRIFRYYKKANIKKFIKKIIKLDLKSTPSEASVSRQTFLSTGLNSVKNAVQLQARKLLINNVLERVTPTLNSDLKKKAAKRLFYGDSAPFFALVGVSLASGSGLLTKDDELEGICWEIREAVSKGKWNDSESENVEQLQAANLDELDLGEPIAKGCNAVVYSAKLKNVQSNKLAHQLAVKMMFNYDVESNSTAILKAMYRETVPAMSYFFNQNLFNIENISDFKIRLPPHPNIVRMYSVFADRIPDLQCNKQLYPEALPPRINPEGSGRNMSLFLVMKRYDCTLKEYLRDKTPNMRSSILLLSQLLEAVAHMNIHNISHRDLKSDNILVDLSEGDAYPTIVITDFGCCLCDKQNGLVIPYRSEDQDKGGNRALMAPEIANAKPGTFSWLNYKKSDLWAVGAIAYEIFNIDNPFYDKTMKLLSKSYKEEDLPELPDTIPFIIRNLVSNMLSRSTNKRLDCDVAATVAQLYLWAPSSWLKENYTLPNSNEIIQWLLCLSSKVLCERDITARNKTNTMSESVSKAQYKGRRSLPEYELIASFLRRVRLHLVRKGLKWIQELHIYN | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Acts as a serine/threonine-protein kinase . Exhibits a substrate preference for proline at position P+1 and a general preference at several residues for basic residues such as arginine (By similarity). Also exhibits moderate preferences for a phosphotyrosine at position P-3 and a tryptophan at P-5 (By similarity). Critical to mitochondrial homeostasis it mediates several pathways that maintain mitochondrial health and function (By similarity) Protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins such as park and likely Drp1, to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components . Depending on the severity of mitochondrial damage and/or dysfunction, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to regulating mitochondrial dynamics and eliminating severely damaged mitochondria via mitophagy (By similarity). Appears to be particularly important in maintaining the physiology and function of cells with high energy demands that are undergoing stress or altered metabolic environment, including spermatids, muscle cells and neurons such as the dopaminergic (DA) neurons (By similarity). Mediates the translocation and activation of park at the outer membrane (OMM) of dysfunctional/depolarized mitochondria . At the OMM of damaged mitochondria, phosphorylates pre-existing polyubiquitin chains, the Pink1-phosphorylated polyubiquitin then recruits park from the cytosol to the OMM where park is fully activated by phosphorylation at 'Ser-94' by Pink1 (By similarity). When cellular stress results in irreversible mitochondrial damage, functions with park to promote the clearance of dysfunctional and/or depolarized mitochondria by selective autophagy (mitophagy) (By similarity). The Pink1-park pathway also promotes fission and/or inhibits fusion of damaged mitochondria, by phosphorylating and thus promoting the park-dependent degradation of proteins involved in mitochondrial fusion/fission such as Marf, Opa1 and fzo (By similarity). This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes (By similarity). Also likely to promote mitochondrial fission independently of park and Atg7-mediated mitophagy, via the phosphorylation and activation of Drp1 (By similarity). Regulates motility of damaged mitochondria by phosphorylating Miro which likely promotes its park-dependent degradation by the proteasome; in motor neurons, this inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria being eliminated in the soma (By similarity). The Pink1-park pathway is also involved in mitochondrial regeneration processes such as promoting mitochondrial biogenesis, activating localized mitochondrial repair, promoting selective turnover of mitochondrial proteins and initiating the mitochondrial import of endogenous proteins (By similarity). Involved in mitochondrial biogenesis by promoting the park-dependent ubiquitination of transcriptional repressor Paris which leads to its subsequent proteasomal degradation and allows activation of the transcription factor srl (By similarity). Functions with park to promote localized mitochondrial repair by activating the translation of specific nuclear-encoded mitochondrial RNAs (nc-mtRNAs) on the mitochondrial surface, including several key electron transport chain component nc-mtRNAs (By similarity). During oogenesis, phosphorylates and inactivates larp on the membrane of defective mitochondria, thus impairing local translation and mtDNA replication and consequently, reducing transmission of deleterious mtDNA mutations to the mature oocyte (By similarity). Phosphorylates the mitochondrial acyl-CoA dehydrogenase Mcad, and appears to be important for maintaining fatty acid and amino acid metabolism via a mechanism that is independent of it's role in maintaining production of ATP (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
PTM: Proteolytically cleaved. In healthy cells, the precursor is continuously imported into mitochondria where it is proteolytically cleaved into its short form by the mitochondrial rhomboid protease rho-7 (8231301). The short form is then released into the cytosol where it rapidly undergoes proteasome-dependent degradation. In unhealthy cells, when cellular stress conditions lead to the loss of mitochondrial membrane potential, mitochondrial import is impaired leading to the precursor accumulating on the outer mitochondrial membrane (OMM).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 65446
Sequence Length: 575
Subcellular Location: Mitochondrion outer membrane
EC: 2.7.11.1
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D6WMX4 | MSVRAVGSRLFKHGRSLIQQFCKRDLNTTIGDKINAVSQATAAPSSLPKTQIPKNFALRNVGVQLGLQARRILIDNVLNRVTNSLSAELRKKATRRILFGDSAPFFALVGVSIASGTGILTKEEELEGVCWEIREAISKIKWQYYDIDESRFESNPITLNDLSLGKPIAKGTNGVVYSAKVKDDETDDNKYPFALKMMFNYDIQSNSMEILKAMYRETVPARMYYSNHDLNNWEIELANRRKHLPPHPNIVAIFSVFTDLIQELEGSKDLYPAALPPRLHPEGEGRNMSLFLLMKRYDCNLQSFLSTAPSTRTSLLLLAQLLEGVAHMTAHGIAHRDLKSDNLLLDTSEPESPILVISDFGCCLADKTNGLSLPYTSYEMDKGGNTALMAPEIICQKPGTFSVLNYSKADLWAVGAIAYEIFNCHNPFYGPSRLKNFNYKEGDLPKLPDEVPTVIQALVANLLKRNPNKRLDPEVAANVCQLFLWAPSTWLKPGLKVPTSGEILQWLLSLTTKVLCEGKINNKSFGEKFTRNWRRTYPEYLLISSFLCRAKLANVRNALHWIQENLPELD | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Acts as a serine/threonine-protein kinase . Exhibits a substrate preference for proline at position P+1 and a general preference at several residues for basic residues such as arginine . Also exhibits moderate preferences for a phosphotyrosine at position P-3 and a tryptophan at P-5 . Critical to mitochondrial homeostasis it mediates several pathways that maintain mitochondrial health and function (By similarity). Protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins such as park and likely Drp1, to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components . Depending on the severity of mitochondrial damage and/or dysfunction, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to regulating mitochondrial dynamics and eliminating severely damaged mitochondria via mitophagy (By similarity). Appears to be particularly important in maintaining the physiology and function of cells with high energy demands that are undergoing stress or altered metabolic environment, including spermatids, muscle cells and neurons such as the dopaminergic (DA) neurons (By similarity). Mediates the translocation and activation of park at the outer membrane (OMM) of dysfunctional/depolarized mitochondria . At the OMM of damaged mitochondria, phosphorylates pre-existing polyubiquitin chains, the Pink1-phosphorylated polyubiquitin then recruits park from the cytosol to the OMM where park is fully activated by phosphorylation at 'Ser-80' by Pink1 . When cellular stress results in irreversible mitochondrial damage, functions with park to promote the clearance of dysfunctional and/or depolarized mitochondria by selective autophagy (mitophagy) (By similarity). The Pink1-park pathway also promotes fission and/or inhibits fusion of damaged mitochondria, by phosphorylating and thus promoting the park-dependent degradation of proteins involved in mitochondrial fusion/fission such as Marf, Opa1 and fzo (By similarity). This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes (By similarity). Also likely to promote mitochondrial fission independently of park and Atg7-mediated mitophagy, via the phosphorylation and activation of Drp1 . Regulates motility of damaged mitochondria by phosphorylating Miro which likely promotes its park-dependent degradation by the proteasome; in motor neurons, this inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria being eliminated in the soma (By similarity). The Pink1-park pathway is also involved in mitochondrial regeneration processes such as promoting mitochondrial biogenesis, activating localized mitochondrial repair, promoting selective turnover of mitochondrial proteins and initiating the mitochondrial import of endogenous proteins (By similarity). Involved in mitochondrial biogenesis by promoting the park-dependent ubiquitination of transcriptional repressor Paris which leads to its subsequent proteasomal degradation and allows activation of the transcription factor srl (By similarity). Functions with park to promote localized mitochondrial repair by activating the translation of specific nuclear-encoded mitochondrial RNAs (nc-mtRNAs) on the mitochondrial surface, including several key electron transport chain component nc-mtRNAs (By similarity). During oogenesis, phosphorylates and inactivates larp on the membrane of defective mitochondria, thus impairing local translation and mtDNA replication and consequently, reducing transmission of deleterious mtDNA mutations to the mature oocyte (By similarity). Phosphorylates the mitochondrial acyl-CoA dehydrogenase Mcad, and appears to be important for maintaining fatty acid and amino acid metabolism via a mechanism that is independent of it's role in maintaining production of ATP (By similarity). Exhibits a substrate preference for proline at position P+1 and a general preference at several residues for basic residues such as arginine . Also exhibits moderate preferences for a phosphotyrosine at position P-3 and a tryptophan at P-5 .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
PTM: Proteolytically cleaved. In healthy cells, the precursor is continuously imported into mitochondria where it is proteolytically cleaved into its short form by the mitochondrial rhomboid protease rho-7 (TcasGA2_TC013516). The short form is then released into the cytosol where it rapidly undergoes proteasome-dependent degradation. In unhealthy cells, when cellular stress conditions lead to the loss of mitochondrial membrane potential, mitochondrial import is impaired leading to the precursor accumulating on the outer mitochondrial membrane (OMM).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 64072
Sequence Length: 570
Subcellular Location: Mitochondrion outer membrane
EC: 2.7.11.1
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Q96JA3 | MEGVLYKWTNYLSGWQPRWFLLCGGILSYYDSPEDAWKGCKGSIQMAVCEIQVHSVDNTRMDLIIPGEQYFYLKARSVAERQRWLVALGSAKACLTDSRTQKEKEFAENTENLKTKMSELRLYCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAAFTSELLYRTPPGSPQLAMLKSSKMKHPIIPIHNSLERQMELSTCENGSLNMEINGEEEILMKNKNSLYLKSAEIDCSISSEENTDDNITVQGEIRKEDGMENLKNHDNNLTQSGSDSSCSPECLWEEGKEVIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCYAVVPVLDKLGPTVFAPVKMDLVGNIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLKGFLTEVKNGEKDIQTALNNAYGKTLRQHHGWVVRGVFALALRAAPSYEDFVAALTVKEGDHQKEAFSIGMQRDLSLYLPAMEKQLAILDTLYEVHGLESDEVV | Function: Cargo transport protein that is required for apical transport from the Golgi complex. Transports AQP2 from the trans-Golgi network (TGN) to sites of AQP2 phosphorylation. Mediates the non-vesicular transport of glucosylceramide (GlcCer) from the trans-Golgi network (TGN) to the plasma membrane and plays a pivotal role in the synthesis of complex glycosphingolipids. Binding of both phosphatidylinositol 4-phosphate (PIP) and ARF1 are essential for the GlcCer transfer ability. Also required for primary cilium formation, possibly by being involved in the transport of raft lipids to the apical membrane, and for membrane tubulation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 58261
Sequence Length: 519
Domain: The PH domain of FAPPS binds the small GTPase ARF1 and phosphatidylinositol-4-phosphate (PtdIns4P) with high selectivity, and is required for recruitment of FAPPs to the trans-Golgi network (TGN).
Subcellular Location: Golgi apparatus
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Q5F3S2 | MAFVKSGWLLRQSTILRRWKKNWFDLWSDGRLIFYDDQNRHDIEDKIHMRIHCINLRVGNECRDFQPPEGKQRDCLLQIVCRDGKTVNLCAESADDCLAWKIALQDARTNTGYVGSDVMYDETAISSAPPPYTAYATPSPEVYGYGYGQYHGAYPTVGPQVFYASNGQAYDVPYQYPYHGPYGQPPANHVIIRERYRDNDGDLALGMLAGAATGMALGSLFWVF | Function: Involved in retrograde transport of recycling endosomes.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25410
Sequence Length: 224
Domain: The PH domain specifically binds phosphatidylserine, which is enriched in recycling endosome membranes, it doesn't recognize PIPs.
Subcellular Location: Recycling endosome membrane
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Q96CS7 | MAFVKSGWLLRQSTILKRWKKNWFDLWSDGHLIYYDDQTRQNIEDKVHMPMDCINIRTGQECRDTQPPDGKSKDCMLQIVCRDGKTISLCAESTDDCLAWKFTLQDSRTNTAYVGSAVMTDETSVVSSPPPYTAYAAPAPEQAYGYGPYGGAYPPGTQVVYAANGQAYAVPYQYPYAGLYGQQPANQVIIRERYRDNDSDLALGMLAGAATGMALGSLFWVF | Function: Involved in retrograde transport of recycling endosomes.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24736
Sequence Length: 222
Domain: The PH domain specifically binds phosphatidylserine, which is enriched in recycling endosome membranes, it doesn't recognize PIPs.
Subcellular Location: Recycling endosome membrane
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Q9QZC7 | MAFVKSGWLLRQSTILKRWKKNWFDLWSDGHLIYYDDQTRQSIEDKVHMPVDCINIRTGHECRDIQPPDGKPRDCLLQIVCRDGKTISLCAESTDDCLAWKFTLQDSRTNTAYVGSAILSEETAVAASPPPYAAYATPTPEVYGYGPYSGAYPAGTQVVYAANGQAYAVPYQYPYAGVYGQQPANQVIIRERYRDNDSDLALGMLAGAATGMALGSLFWVF | Function: Involved in retrograde transport of recycling endosomes.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24574
Sequence Length: 221
Domain: The PH domain specifically binds phosphatidylserine, which is enriched in recycling endosome membranes, it doesn't recognize PIPs.
Subcellular Location: Recycling endosome membrane
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P54734 | MEQLLDNRYRVIKTLGSGGFGETFLAEDSQMPSNRRCVVKQLRPIHNNPQIYQLVQERFQREAAILEDLGSYSGQIPTLYAYFQSNTQFYVVQEWVEGDTLTAKLKQQGVLSESAVRDILINLLPVLEYVHSKRIIHRDIKPDNIILRHRDGKPVLIDFGAVRESMGTVINSQGNPTSSIVIGTPGYMPSEQAAGRPVYSSDLYSLGLTAIYLLTGKQPQELETEPHSGEIIWHRYALNISPTLAAVIDRAIAYHPRERFTTAREMLEALQLGVVSYPPTVPYQQPQSSPTVPYQQPPVVTTPPFATQTNTVAVSPGTAPTPQPINHNNSNKGILMGSLIAGGLIGASVVIGFALTRPNQPVTQTTSLPSETTISNNDTPTVEPSPTDTPETPISQTVTQDPTPQASVRFPINSRPFTTPIDSKPRNTTEPTTSVPQPTTPSEPQITTPVEATDRPSPEQAVQNYYETINQGEYSTAWNLLASSFQNNRKLHPRGYDSYLDWWGGQVENVDVEQVSLLKANADTATVNARLRYFMKSGRQSSSSVRFSLVWDADNNRWVVSGAR | Function: Probably required for both normal cellular growth and differentiation. Inactivation of pknA leads to colonies that appear light green and rough in the absence of combined nitrogen.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 62385
Sequence Length: 564
EC: 2.7.11.1
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P54744 | MTTPPHLSDRYELGDILGFGGMSEVHLARDIRLHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHPSIVAVYDTGEAETSAGPLPYIVMEYVDGATLRDIVHTDGPMPPQQAIEIVADACQALNFSHQNGIIHRDVKPANIMISATNAVKVMDFGIARAIADSTSVTQTAAVIGTAQYLSPEQARGDSVDARSDVYSLGCVLYEILTGEPPFIGDSPVSVAYQHVREDPIPPSQRHEGISVDLDAVVLKALAKNPENRYQTAAEMRADLIRVHSGQPPEAPKVLTDADRSCLLSSGAGNFGVPRTDALSRQSLDETESDGSIGRWVAVVAVLAVLTIAIVAAFNTFGGNTRDVQVPDVRGQVSADAISALQNRGFKTRTLQKPDSTIPPDHVISTEPGANASVGAGDEITINVSTGPEQREVPDVSSLNYTDAVKKLTSSGFKSFKQANSPSTPELLGKVIGTNPSANQTSAITNVITIIVGSGPETKQIPDVTGQIVEIAQKNLNVYGFTKFSQASVDSPRPTGEVIGTNPPKDATVPVDSVIELQVSKGNQFVMPDLSGMFWADAEPRLRALGWTGVLDKGPDVDAGGSQHNRVAYQNPPAGAGVNRDGIITLKFGQ | Function: Protein kinase that regulates many aspects of mycobacterial physiology. Is a key component of a signal transduction pathway that regulates cell growth, cell shape and cell division via phosphorylation of target proteins.
PTM: Autophosphorylated. Dephosphorylated by PstP (By similarity).
Location Topology: Single-pass membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 66187
Sequence Length: 622
Subcellular Location: Cell membrane
EC: 2.7.11.1
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A0QNG1 | MTTPQHLSDRYELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETPNGPLPYIVMEYVDGVTLRDIVHTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALADTGNSVTQTAAVIGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRRHADVTPELDAVVLKALAKNPDNRYQTAAEMRADLIRVHEGQAPDAPKVLTDAERTSMLAAPPADRAGAATQDMPVPRPAGYSKQRSTSVARWLIAVAVLAVLTVVVTVAINMVGGNPRNVQVPDVAEQSADDAQAALQNRGFKTVIDRQPDNEVPPGLVIGTDPEAGSELGAGEQVTINVSTGPEQALVPDVAGLTPTQARQKLKDAGFEKFRESPSPSTPEQKGRVLATNPQANQTAAIINEITIVVGAGPEDAPVLSCAGQNAESCKAILAAGGFTNTVVVEVDNPAAAGQVVGTEPADGQSVPKDTVIQIRVSKGNQFVMPDLVGQFWSDAYPRLTALGWTGVLDKGPDVRDSGQRTNAVVTQSPSAGTPVNKDAKITLSFAA | Function: Protein kinase that regulates many aspects of mycobacterial physiology. Is a key component of a signal transduction pathway that regulates cell growth, cell shape and cell division via phosphorylation of target proteins (By similarity). Probably phosphorylates RseA .
PTM: Autophosphorylated. Dephosphorylated by PstP (By similarity).
Location Topology: Single-pass membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 66318
Sequence Length: 625
Domain: The PASTA domains interact with peptidoglycans and are required for PknB localization.
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9Z986 | MERYDIVRIIGKGGMGEVYLAYDPVCSRKVALKKIREDLAENPLLKRRFLREARIAADLIHPGVVPVYTIYSEKDPVYYTMPYIEGYTLKTLLKSVWQKESLSKELAEKTSVGAFLSIFHKICCTIEYVHSRGILHRDLKPDNILLGLFSEAVILDWGAAVACGEEEDLLDIDVSKEEVLSSRMTIPGRIVGTPDYMAPERLLGHPASKSTDIYALGVVLYQMLTLSFPYRRKKGKKIVLDGQRIPSPQEVAPYREIPPFLSAVVMRMLAVDPQERYSSVTELKEDIESHLKGSPKWTLTTALPPKKSSSWKLNEPILLSKYFPMLEVSPASWYSLAISNIESFSEMRLEYTLSKKGLNEGFGILLPTSENALGGDFYQGYGFWLHIKERTLSVSLVKNSLEIQRCSQDLESDKETFLIALEQHNHSLSLFVDGTTWLIHMNYLPSRSGRVAIIVRDMEDILEDIGIFESSGSLRVSCLAVPDAFLAEKLYDRALVLYRRIAESFPGRKEGYEARFRAGITVLEKASTDNNEQEFALAIEEFSKLHDGVAAPLEYLGKALVYQRLQEYNEEIKSLLLALKRYSQHPEIFRLKDHVVYRLHESFYKRDRLALVFMILVLEIAPQAITPGQEEKILVWLKDKSRATLFCLLDPTVLELRSSKMELFLSYWSGFIPHLNSLFHRAWDQSDVRALIEIFYVACDLHKWQFLSSCIDIFKESLEDQKATEEIVEFSFEDLGAFLFAIQSIFNKEDAEKIFVSNDQLSPILLVYIFDLFANRALLESQGEAIFQALDLIRSKVPENFYHDYLRNHEIRAHLWCRNEKALSTIFENYTEKQLKDEQHELFVLYGCYLALIQGAEAAKQHFDVCREDRIFPASLLARNYNRLGLPKDALSYQERRLLLRQKFLYFHCLGNHDERDLCQTMYHLLTEEFQL | Function: Together with the serine/threonine kinase Pkn1, may play a role in the specific interactions with host proteins during intracellular growth.
PTM: Autophosphorylated on serine and threonine residues.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 107410
Sequence Length: 932
EC: 2.7.11.1
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P0DPS9 | MQRYELIRLIGKGGMGEVYLAHDKACSRRVALKRIREDLSGNALLRKRFLREAKIAADLIHPGIVPVYSICSDGEAVYYTMPYIEGFSLKSLLKSVWQKEVLSKELEEKTSVKSFLPIFDKICATVEYIHSKGVLHRDLKPDNILLGLFGEVVIVDWGAAIFKHAKELKLEQDDEAAVSFDERNICYSSMTIPGKIVGTPDYMAPESLLGVEASEKTDIYALGLILYQMLTLAFPYRRKKGRKLSYRDVVLPPIEMSPYREIPPSLSQIAMKAIAINPADRFSSIQELRQALQPYLQGDPEWTVKATLMAKEKSCWKYYDPILLSRYFPVLASSPAQWYNFMLSEVEISASTRVEYTVTKSAVHEGMGILFLPSKEAERGEFYCGYGLWFSVQNHELTVSLIKNGIEIQKKSQEMISQQYRFAILIEKSDNRIAVFVEQALFILHIDYLPSLGNRLGVIIQDLQGMSNIAISESIGALRVSCLAVPDAFLSEKLYDQAAIFYRKIRDSFPGRKESYEAQFRLGVTLLTQIEEQGGDLTQALSSFDYLHGGAGAPLEYLGKALVYQRNGSFVEEIRCLLFALKRYSQHPEIPRLEDHLCFRLYDSLHKHRSEALVFMLLILWIAPEKISVREEKRFLRIIYHKQQATLFCQVDKAPLQFRSSKMELFLSFWTGFSLFLPELFRRAGELRDYQALADIFYVAGVSGNREAFMQFSTALANVSDEITFPESLHNQKVAELMFFVKGVEALRNKDYQKAKKLLWKTPFTLQLYALDIFHIQAFLDEEIESFIDLLQAIYDPASEEERDHILVYIIQTHLWNRDLERAYKLLNDRFPLDEELAEYSEAFILWGCYLALTGDRVAVKAHFSRCRYKYGKSALIGKCVDGDIFDYLDNLVWWEKKMTLFQSYFLLRCLNESPRRYEKYRQAYLSMENNFFD | Function: Together with the serine/threonine kinase Pkn1, may play a role in the specific interactions with host proteins during intracellular growth (Probable). Autophosphorylates and also phosphorylates Pkn1 .
PTM: Autophosphorylated on serine and threonine residues (By similarity) . Present in elementary bodies 40 hours post-infection as 2 bands of approximately 55 to 60 and 45 to 50 kDa, which may be due to differential phosphorylation as well as degradation; an enzymatically active full-length protein can also be detected .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 107754
Sequence Length: 934
EC: 2.7.11.1
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P9WI78 | MSDAVPQVGSQFGPYQLLRLLGRGGMGEVYEAEDTRKHRVVALKLISPQYSDNAVFRARMQREADTAGRLTEPHIVPIHDYGEINGQFFVEMRMIDGTSLRALLKQYGPLTPARAVAIVRQIAAALDAAHANGVTHRDVKPENILVTASDFAYLVDFGIARAASDPGLTQTGTAVGTYNYMAPERFTGDEVTYRADIYALACVLGECLTGAPPYRADSVERLIAAHLMDPAPQPSQLRPGRVPPALDQVIAKGMAKNPAERFMSAGDLAIAAHDALTTSEQHQATTILRRGDNATLLATPADTGLSQSESGIAGAGTGPPTPGAARWSPGDSATVAGPLAADSRGGNWPSQTGHSPAVPNALQASLGHAVPPAGNKRKVWAVVGAAAIVLVAIVAAAGYLVLRPSWSPTQASGQTVLPFTGIDFRLSPSGVAVDSAGNVYVTSEGMYGRVVKLATGSTGTTVLPFNGLYQPQGLAVDGAGTVYVTDFNNRVVTLAAGSNNQTVLPFDGLNYPEGLAVDTQGAVYVADRGNNRVVKLAAGSKTQTVLPFTGLNDPDGVAVDNSGNVYVTDTDNNRVVKLEAESNNQVVLPFTDITAPWGIAVDEAGTVYVTEHNTNQVVKLLAGSTTSTVLPFTGLNTPLAVAVDSDRTVYVADRGNDRVVKLTS | Function: Part of a signaling pathway that enables adaptation to osmotic stress through cell wall remodeling and virulence factor production.
PTM: Autophosphorylated. Dephosphorylated by PstP.
Location Topology: Single-pass membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 69545
Sequence Length: 664
Subcellular Location: Cell membrane
EC: 2.7.11.1
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P40804 | MTKCNLPEVVVTGVGVTASIGQGKEDFASSLLSGRHAFDVMKRSGRQKDSRFIGAEIASLSYPDRLSKKMLRKASFSSRAALVTLTEAWEEAELDDADSSRIGLVVGGSNFQQRENFEVYERYQDRSGFISPAYGLSFMDSDLCGICTDQFGITGLAYTVGGASASGQLAVIHAIQQVLSGEVDTCIALGALMDLSYMECEALRALGAMGTDKYADEPENACRPFDQNRDGFIYGESCGALVIERKETALRRGLKPYAALSGWSIKLDGNRNPDPSLEGEIHVIQKALERARLLPEDIDYINPHGTGSFIGDEIELKALRACRLSHAYINATKSITGHGLSAAGIVEIISVLLQMKKSALHPSRNLDHPIDDSFHWVNEKSISYRIKNALSLSMGFGGMNTAVCIQNIEKCGGES | Function: Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It decarboxylates selectively the malonyl group attached on the acyl-carrier-protein AcpK (Mal-AcpK).
Catalytic Activity: H(+) + malonyl-[ACP] = acetyl-[ACP] + CO2
Sequence Mass (Da): 45009
Sequence Length: 415
Pathway: Antibiotic biosynthesis; bacillaene biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.1.1.87
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P40830 | MVSAGIEAMNVFGGTAYLDVMELAKYRHLDTARFENLLMKEKAVALPYEDPVTFGVNAAKPIIDALSEAEKDRIELLITCSESGIDFGKSLSTYIHEYLGLNRNCRLFEVKQACYSGTAGFQMAVNFILSQTSPGAKALVIASDISRFLIAEGGDALSEDWSYAEPSAGAGAVAVLVGENPEVFQIDPGANGYYGYEVMDTCRPIPDSEAGDSDLSLMSYLDCCEQTFLEYQKRVPGANYQDTFQYLAYHTPFGGMVKGAHRTMMRKVAKVKTSGIETDFLTRVKPGLNYCQRVGNIMGAALFLALASTIDQGRFDTPKRIGCFSYGSGCCSEFYSGITTPQGQERQRTFGIEKHLDRRYQLSMEEYELLFKGSGMVRFGTRNVKLDFEMIPGIMQSTQEKPRLFLEEISEFHRKYRWIS | Function: Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the aldol condensation between the acetyl group attached to the acyl-carrier-protein AcpK (Ac-AcpK) and a beta-ketothioester polyketide intermediate linked to one of the consecutive thiolation domains of PksL.
Catalytic Activity: 3-oxobutanoyl-[ACP] + acetyl-[ACP] + H2O = (3S)-hydroxy-3-methylglutaryl-[ACP] + H(+) + holo-[ACP]
Sequence Mass (Da): 46780
Sequence Length: 420
Pathway: Antibiotic biosynthesis; bacillaene biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.3.-
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P40805 | MDLVTYQTIKVRFQASVCYITFHRPEANNTINDTLIEECLQVLNQCETSTVTVVVLEGLPEVFCFGADFQEIYQEMKRGRKQASSQEPLYDLWMKLQTGPYVTISHVRGKVNAGGLGFVSATDIAIADQTASFSLSELLFGLYPACVLPFLIRRIGRQKAHYMTLMTKPISVQEASEWGLIDAFDAESDVLLRKHLLRLRRLNKKGIAHYKQFMSSLDHQVSRAKATALTANQDMFSDPQNQMGIIRYVETGQFPWEDQ | Function: Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. Probably catalyzes the dehydration of the (S)-3-hydroxy-3-methylglutaryl group attached to PksL.
Sequence Mass (Da): 29411
Sequence Length: 259
Pathway: Antibiotic biosynthesis; bacillaene biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.2.1.-
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P40802 | MTHSVVELIEIESAIIQVKMQDRTHKNAFSQELTDDLIQAFEYIRQNPKYKAVILTGYDNYFASGGTQEGLLRIQQGLTKFTDDNLYSLALDCEIPVIAAMQGHGIGGGFVMGLFADIVILSRESVYTANFMKYGFTPGMGATFIVPKKLGFSLAQEILLNAGSYRGADLEKRGVPFKVLPRAEVLDYAVELAQELAEKPRNSLVTLKDHLVAPLRDQLPRVIEQELMMHEKTFHHEEVKSRIKGLYGN | Function: Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. May have a role in the decarboxylation of the (S)-3-methylglutaryl group attached to PksL.
Sequence Mass (Da): 27896
Sequence Length: 249
Pathway: Antibiotic biosynthesis; bacillaene biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.-.-.-
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O31785 | MEKLMFHPHGKEFHHNPFSVLGRFREEEPIHRFELKRFGATYPAWLITRYDDCMAFLKDNRITRDVKNVMNQEQIKMLNVSEDIDFVSDHMLAKDTPDHTRLRSLVHQAFTPRTIENLRGSIEQIAEQLLDEMEKENKADIMKSFASPLPFIVISELMGIPKEDRSQFQIWTNAMVDTSEGNRELTNQALREFKDYIAKLIHDRRIKPKDDLISKLVHAEENGSKLSEKELYSMLFLLVVAGLETTVNLLGSGTLALLQHKKECEKLKQQPEMIATAVEELLRYTSPVVMMANRWAIEDFTYKGHSIKRGDMIFIGIGSANRDPNFFENPEILNINRSPNRHISFGFGIHFCLGAPLARLEGHIAFKALLKRFPDIELAVAPDDIQWRKNVFLRGLESLPVSLSK | Function: Involved in the metabolism of the antibiotic polyketide bacillaene which is involved in secondary metabolism. The substrate is dihydrobacillaene.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 46729
Sequence Length: 405
Pathway: Antibiotic biosynthesis; bacillaene biosynthesis.
Subcellular Location: Cell membrane
EC: 1.14.-.-
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P49695 | MIEPLQPGDPGRIGPYRLVSRLGAGGMGQVFLARSPGGRPVVVKVILPEYANDDEYRIRFAREVEAARRVGGFHTAQVIDADPTADPPWMATAYIPGPSLRKAVTERGPLYGNNLRTLAAGLVEGLAAIHACGLVHRDFKPSNIVLAADGPRVIDFGVARPLDSSVMTQSGAVIGTLAYMSPEQTDGSQVGPASDVFSLGTVLAFAATGRSPFMADSIGEIIARISGPPPELPELPDDLRELVYACWEQNPDLRPTTAELLAQLSTDHTGDDWPPPHLSDLIGSMLPLGATTSPNPSLAIEPPPPSHGPPRPSEPLPDPGDDADEPSAEKPSRTLPEPEPPELEEKPIQVIHEPERPAPTPPRPREPARGAIKPKNPRPAAPQPPWSPPRVQPPRWKQLITKKPVAGILTAVATAGLVVSFLVWQWTLPETPLRPDSSTAPSESADPHELNEPRILTTDREAVAVAFSPGGSLLAGGSGDKLIHVWDVASGDELHTLEGHTDWVRAVAFSPDGALLASGSDDATVRLWDVAAAEERAVFEGHTHYVLDIAFSPDGSMVASGSRDGTARLWNVATGTEHAVLKGHTDYVYAVAFSPDGSMVASGSRDGTIRLWDVATGKERDVLQAPAENVVSLAFSPDGSMLVHGSDSTVHLWDVASGEALHTFEGHTDWVRAVAFSPDGALLASGSDDRTIRLWDVAAQEEHTTLEGHTEPVHSVAFHPEGTTLASASEDGTIRIWPIATE | Function: May play a regulatory role during the complex growth cycle and in secondary metabolite production.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 78950
Sequence Length: 742
EC: 2.7.11.1
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Q8GVC7 | MLRLGRSAASEVSSIRNSLQLQLEQRGARPMQCAYQTQSHSNPEGAKRGRSPMSLAVMGAAALSVGLELQTDGIAQARAAMEPGTQLQRHKWQLFDQIGAGAFGVVRLGMHEESGEVAAVKIVPLENPNDQRSYPALEREIAALKLVKALGGHNSIVDLRDVYVEGRKLFLVTELARGGELFEQIVAYGSFPELKARDVAREMASALSFMHRHGLVHKDVKPENILMSARVVDHNSGVYRKSNRHESSSLVKLADFGSAGPASVNTNLEDIGTAAYLPPEVLNSGMCTSACDMWALGCVLYIMLSGSHPFDLDGMSADSVVEHRVKSEPVTFDFSAWDNVSPHAKDLISKLLVKDPTLRLTADQMLQHPWMNASAEAAAAGLRRPSPLLAGQPIPRGPA | Function: May regulate an early stage of the zoospore pathway.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 43173
Sequence Length: 399
EC: 2.7.11.1
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P00513 | MNITDIMNAIDAIKALPICELDKRQGMLIDLLVEMVNSETCDGELTELNQALEHQDWWTTLKCLTADAGFKMLGNGHFSAAYSHPLLPNRVIKVGFKKEDSGAAYTAFCRMYQGRPGIPNVYDVQRHAGCYTVVLDALKDCERFNNDAHYKYAEIASDIIDCNSDEHDELTGWDGEFVETCKLIRKFFEGIASFDMHSGNIMFSNGDVPYITDPVSFSQKKDGGAFSIDPEELIKEVEEVARQKEIDRAKARKERHEGRLEARRFKRRNRKARKAHKAKRERMLAAWRWAERQERRNHEVAVDVLGRTNNAMLWVNMFSGDFKALEERIALHWRNADRMAIANGLTLNIDKQLDAMLMG | Function: Serine/threonine kinase that modulates host metabolism to favor virus replication cycle. Participates together with gene 2 protein (gp2) in the host transcription shutoff. Phosphorylates host RNA polymerase subunit RpoC and to a lesser extent subunit RpoB. This modification seems to increase rho-dependent transcription termination, which may help to switch from host to viral RNA polymerase transcription during phage development. Phosphorylates host components of the RNA degradosome rne and RhlB, leading to stabilization of mRNAs synthesized by T7 RNA polymerase. Phosphorylates host dsRNA specific processing enzyme RNase III/rnc, leading to enhance activity of the ribonuclease that may increase maturation of T7 late transcripts possessing multiple Rnase III processing sites. Phosphorylates several components of the host translational machinery including initiation factors InfA, InfB, and InfC, ribosomal subunit RpsA and RpsF, as well as elongation factor G/FusA. These phosphorylations may enhance T7 late protein production.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 41124
Sequence Length: 359
EC: 2.7.11.1
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Q03674 | MQLRNILQASSLISGLSLAADSSSTTGDGYAPSIIPCPSDDTSLVRNASGLSTAETDWLKKRDAYTKEALHSFLSRATSNFSDTSLLSTLFSSNSSNVPKIGIACSGGGYRAMLGGAGMIAAMDNRTDGANEHGLGGLLQSSTYLSGLSGGNWLTGTLAWNNWTSVQEIVDHMSESDSIWNITKSIVNPGGSNLTYTIERWESIVQEVQAKSDAGFNISLSDLWARALSYNFFPSLPDAGSALTWSSLRDVDVFKNGEMPLPITVADGRYPGTTVINLNATLFEFTPFEMGSWDPSLNAFTDVKYLGTNVTNGKPVNKDQCVSGYDNAGFVIATSASLFNEFSLEASTSTYYKMINSFANKYVNNLSQDDDDIAIYAANPFKDTEFVDRNYTSSIVDADDLFLVDGGEDGQNLPLVPLIKKERDLDVVFALDISDNTDESWPSGVCMTNTYERQYSKQGKGMAFPYVPDVNTFLNLGLTNKPTFFGCDAKNLTDLEYIPPLVVYIPNTKHSFNGNQSTLKMNYNVTERLGMIRNGFEAATMGNFTDDSNFLGCIGCAIIRRKQESLNATLPPECTKCFADYCWNGTLSTSANPELSGNSTYQSGAIASAISEATDGIPITALLGSSTSGNTTSNSTTSTSSNVTSNSNSSSNTTLNSNSSSSSISSSTARSSSSTANKANAAAISYANTNTLMSLLGAITALFGLI | Function: Sequentially removes both fatty acyl groups from diacylglycerophospholipids and therefore has both phospholipase A and lysophospholipase activities. However, it does not display transacylase activity. Substrate preference is phosphatidylserine > phosphatidylinositol > phosphatidylcholine > phosphatidylethanolamine . The substrate specificity is pH- and ion-dependent. In contrast with activities observed at optimum pH 3.5, the order of substrate preference at pH 5.5 is phosphatidylserine = phosphatidylethanolamine > phosphatidylcholine > phosphatidylinositol .
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
Location Topology: Lipid-anchor
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine
Sequence Mass (Da): 75455
Sequence Length: 706
Subcellular Location: Secreted
EC: 3.1.1.5
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B0XZV8 | MKALLSLLTAVAVATATPLDLSLRALPNAPDGYTPAKVSCPATRPSIRGAGSLSPNETSWLEIRRKNTVQPMTDLLGRLNLGFDAAGYIDRVSSNASNLPNIAIAVSGGGYRALTNGAGAIKAFDSRTQGSTQSGHLGGLLQSATYVSGLSGGGWLVGSVYLNNFTTIADLQSGDHGNVWQFSTSILEGPKAKHLQFLSTADYWKDLLKAVDGKSDAGFNTSLTDYWGRALSYQFINDRTGNGGLSYTWSSIALTDPFRRGEMPLPILVADGRNPGELLIGSNSTVYEFNPWEFGSFDPSIFGFAPLEYLGSRFDNGQLPRGEPCVRGFDNAGFVMGTSSSLFNQFILRLNKTDLPDLAKDVFSKILTAIGRDGDDIAVYGPNPFYGYRNSTAAYSRSRELDVVDGGEDGQNIPLHPLIQPVRHVDVIFAVDSSADGPYSWPNGSALVATYERSLNSSGIGNGTVFPAVPDVNTFVNLGLNTRPTFFGCDPANLSAPAPLVVYLPNAPYSTHSNTSTFQLAYSDSERDEIITNGYNVVTRGNATVDKSWPSCVGCAILQRSMYRTNTSMPAVCNSCFKEYCWNGTVDSKTPRTYEPTLLLGSTSTNAAYTQGVTWLVGILAVGVAMGMTA | Function: Catalyzes the release of fatty acids from lysophospholipids.
PTM: The GPI-like anchor contains a phosphoceramide lipid group.
Location Topology: Lipid-anchor
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine
Sequence Mass (Da): 67417
Sequence Length: 630
Subcellular Location: Cell membrane
EC: 3.1.1.5
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Q9UVX1 | MKVNLKLIIGSILISQAQAIWPFDSSGSSSSSDSSPSETGSSGGTFPFDLFGSGSSLTQSSSAQASSTKSTSDSASSTDSSLFSSSNSGSSWYQTFLDGDSGDQKTDYAPFNLTCPSKKTFIRTASELSQQEKDYIHKRQETTNKNLIDFLSKRANLSDFDAKSFINDNAPNHNITIGLSFSGGGYRAMLAGAGQILGLDGRYEDANKHGLGGLLDSSTYVVGLSGGNWLVGSLALNDWLSVGDIVNGKSTIWQLQDSILNPSGMRIDKTIAYYYGLAQAVQAKEDAGFQTSVTDTWGRALSYQFFEEDDSGTGGANITWSSIRNLSSFQDHSMPYPIVVANGRTPGTYIINENSTIFEISPYELGSWDPSLKSFSNIQYLGSSVNNGNPNNTDICVNNFDNAGFIMGTSSSLFNQILLQLDNYSINSIIKMILEKVLTDVSDEEYDIAVYEPNPFFGADSAGIKSITTNDTLYLCDGGEDLQNVPFYPLIQNKRGVDVIFAFDNSADTNSSWPNGTSIQETYKRQFSKQGKGTPFPFAPDYKTFLDKNMGDKPVFFGCNSSDLEDLVAWHENDKINVTDVPLVVYTSNTRMSYNSNFSTFKLSYSDQEKFGAIRNGFETVTRNNLTDDENWSTCVGCAIIRRQQERLGEEQSDECKKCFQEYCWTGGFKDAASVSSVSGISGLAAKTHTSGGTSSTTQQTSTTTGSSANGGSSSTGSSSSSKKKNGGDLVNGGVPSSIFLVFNSLLGLIIAYL | Function: Catalyzes the release of fatty acids from lysophospholipids. Phospholipase B may well contribute to pathogenicity by abetting the fungus in damaging and traversing host cell membranes, processes which likely increase the rapidity of disseminated infection (By similarity).
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine
Sequence Mass (Da): 81412
Sequence Length: 754
Subcellular Location: Secreted
EC: 3.1.1.5
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Q08108 | MIRPLCSKIIISYIFAISQFLLAANAWSPTDSYVPGTVSCPDDINLVREATSISQNESAWLEKRNKVTSVALKDFLTRATANFSDSSEVLSKLFNDGNSENLPKIAVAVSGGGYRSMLTGAGVLAAMDNRTEGAYEHGLGGLLQSTTYLSGASGGNWLVGTLALNNWTSVQDILNNMQNDDSIWDLSDSIVTPGGINIFKTAKRWDHISNAVESKQNADYNTSLADIWGRALAYNFFPSLNRGGIGLTWSSIRDFPVFQNAEMPFPISVADGRYPGTKVINLNATVFEFNPFEMGSWDPSLNSFANVKYLGTNVSNGVPLERGKCTAGFDNAGFIMGTSSTLFNQFLLRINSTHLPSFITRLARHFLKDLSQDFNDIAVYSPNPFKDTKFLDSDYTTSIVDSDSLFLVDGGEDDENVPVLPLIQKERDVDIIFAVDNSADMRLAWPDGSSLVHTYERQFVKQGQGMSFPYVPDTNTFVNLGLNKKPTFFGCDANNLTDLQYIPPLVVYLPNAEYSFNSNQSAFKLSYSESQRRSMIQNGFEIATRNNFTDDPEFMGCVGCAIIRRKQQALNITLPPECETCFKNYCWNGTLDTTPLPDVEKDVHHSFINVNSFNSSIGQEESLYAGSSASQSSSSSSSSSSSSEIPSATATLEKKAATNSGSHLSGISVKFSAMIMLTLLMFTGAV | Function: Sequentially removes both fatty acyl groups from diacylglycerophospholipids and therefore has both phospholipase A and lysophospholipase activities. Substrate preference is phosphatidylserine > phosphatidylinositol. Does not cleave phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid and phosphatidylinositol-bisphosphate . Mainly responsible for the degradation of phosphatidylinositol in vivo .
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine
Location Topology: Lipid-anchor
Sequence Mass (Da): 75077
Sequence Length: 686
Subcellular Location: Cell membrane
EC: 3.1.1.5
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Q9UTH5 | MYFQSFYFLALLLATAVYGQVASPELHSLSRRNWKKPPPFPSTNASYAPVIRSCDSSEIMVNSLPRGELPDLENDFIEKRLSNANEALTTFLQSKNTTADLDLSSIVGDNGPRLGIAVSGGGWRSMLFGGGALAALDSRSNETTLGGLLQSAHYITGADGGSWLLSSLAVNEFRTIQNISKSIWYTRLGIFFIEETHFGDLKNYYTNVVDEVNQKAAAGFNVSLTDYWGRAIARHFVGQLRGGPNLTYSSVQNASWFQTAEYPYPLIVTQGLTGGLPDGSNGTATNSSIYEISPYYLTSFDNNVRSYTPTQYLGTNYSNGTAVDGKCVTQFDNVGFLVGTSSTRYNEALIDVSLRQSRMSRRLGFTLRHMRINGSSVSFYPNPYTDATDIAGNATAVSEDIVDTPYLDLFDGGYDGQNIPIWPLLQPERKLDVVFAFDSSGDTSNFWPNGSSLVATYERVTQRASDAVYDVEDFVHVPTPETFVNLGLNANPTFFGCDGRNTTRGDVPVDHNTPPLVVYMPNTPWTMKSNLVDHRYRIANSEIQALIQNGFVATTQDNSTDFASCLACAVVQRSLERRNQSTSAACQQCFSQYCWNGTVDNTPVDDDSKNPTYNPAVKTSSASGVHANILLSFFVLLATLLVTA | Function: Catalyzes the release of fatty acids from lysophospholipids.
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine
Sequence Mass (Da): 70570
Sequence Length: 644
Subcellular Location: Secreted
EC: 3.1.1.5
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