entry
stringlengths 6
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stringlengths 5
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stringlengths 3
2.44k
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stringlengths 2
35.2k
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stringlengths 7
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D4ADY9
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ELOV7_RAT
|
Elongation of very long chain fatty acids protein 7 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl7) (ELOVL fatty acid elongase 7) (ELOVL FA elongase 7) (Very long chain 3-ketoacyl-CoA synthase 7) (Very long chain 3-oxoacyl-CoA synthase 7)
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MAFSDLTSRTVRFYDNWIKDADPRVENWLLMSSPLPQTIILGLYVYFVTSLGPKLMENRKPFELKKAMITYNFFIVLFSVYMCYEFVMSGWGTGYSFRCDIVDYSQSPRAMRMVHTCWLYYFSKFIELFDTIFFVLRKKNSQVTFLHVFHHTIMPWTWWFGVKFAAGGLGTFHALLNTAVHVVMYFYYGLCAMGPAYQKYLWWKKHLTSLQLVQFVLVTVHIGQIFFMEDCNYQYPVFLYIIMSYGCIFLLLFLHFWYRAYTKGQRLPKTMENGNCKSKHH
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Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. May participate in the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000255|HAMAP-Rule:MF_03207}.
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D4AE59
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STK11_RAT
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Serine/threonine-protein kinase STK11 (EC 2.7.11.1) (Liver kinase B1 homolog) (LKB1)
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MDVADPQPLGLFPEGELMSVGMDTFIHRIDSTEVIYQPRRKRAKLIGKYLMGDLLGEGSYGKVKEVLDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLRHRNVIQLVDVLYNEEKQKMYMVMEYCVCGMQEMLDSVPEKRFPVCQAHGYFRQLIDGLEYLHSQGIVHKDIKPGNLLLTTNGTLKISDLGVAEALHPFAVDDTCRTSQGSPAFQPPEIANGLDTFSGFKVDIWSAGVTLYNITTGLYPFEGDNIYKLFENIGRGDFTIPCDCAPPLSDLLRGMLEYEPAKRFSIRQIRQHSWFRKKHPLAEALVPIPPSPDTKDRWRSMTVVPYLEDLHGRAEEEEDEDLFDIEDGIIYTQDFTVPGQVLEEEVGQNGQSHSLPKAVCVNGTEPQLSSKVKPEGRPGAANPARKVCSSNKIRRLSACKQQ
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Tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, thus promoting their activity: phosphorylates PRKAA1, PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2, SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non-AMPK family proteins such as STRADA, PTEN and possibly p53/TP53. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2 and thereby regulates processes including: inhibition of signaling pathways that promote cell growth and proliferation when energy levels are low, glucose homeostasis in liver, activation of autophagy when cells undergo nutrient deprivation, and B-cell differentiation in the germinal center in response to DNA damage. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton. Required for cortical neuron polarization by mediating phosphorylation and activation of BRSK1 and BRSK2, leading to axon initiation and specification. Involved in DNA damage response: interacts with p53/TP53 and recruited to the CDKN1A/WAF1 promoter to participate in transcription activation. Able to phosphorylate p53/TP53 the relevance of such result in vivo is however unclear and phosphorylation may be indirect and mediated by downstream STK11/LKB1 kinase NUAK1. Also acts as a mediator of p53/TP53-dependent apoptosis via interaction with p53/TP53: translocates to the mitochondrion during apoptosis and regulates p53/TP53-dependent apoptosis pathways. Regulates UV radiation-induced DNA damage response mediated by CDKN1A. In association with NUAK1, phosphorylates CDKN1A in response to UV radiation and contributes to its degradation which is necessary for optimal DNA repair (By similarity).
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D4AEC2
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CAMP2_RAT
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Calmodulin-regulated spectrin-associated protein 2
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MGDAADPREVRRTFIVPAIKPFDHYDFSRAKIACNLAWLVAKAFGTETVPEELREPFYTDQYDQEHIKPPVVNLLLSAELYCRAGSLILKSDAAKPLLGHDAVIQALAHKGLYVTDQEKLVTERDLHKKPIQMSAHLAMIDTLMMAYTVEMVSIEKVIACAQQYSAFFQATDLPYDIEDAVMYWINKVNEHLKDIMEQEQKSKEHHTAEAPGGQKSPSKWFWKLVPARYRKEQTLLKQLPCIPLVENLLKDGTDGCALAALIHFYCPAVVRLEDICLKETMSLADSLYNLQLIQEFCQEYLNHCCHFSLEDMLYAASSIKSNYLVFMAELFWWFEVVKPSFVQPRVVRPQGAEPAKDMPSVPVLNAAKRNVLDSSSSSDFTSRYTRPQTHSSVSGGIRRSSSMSYVDGFIGTWPKEKRTSVHGVSFDISFDKEDNAQSSTPNRGIIRSVSNEGLNNSRASKHIRKNLSFKPVNGGEEESIEEELHVDPHGDLKSYMPLSTNELNSNENTHHKLPNGALQNRVLLDEFGNQIETPSIEEALQIIHDTEKPPHTARPDQIANGFFLHGQDLSLLNSNIKLSQSSPDNITDPKGALSPITDTTEVDTGIHVPSEDIPETMDEDSSLRDYTVSLDSDMDDASKFLQDYDIRASNPREALSPCPSTISTKSQPGSSASSSSGVKMTSFAEQKFRKLNHTDGKSSGSSSQKTTPEGSELNIPHMVSWAQIPEESGVAQGRDTTQLLASEMVHLRMRLEEKRRAIEAQKKKMEAAFTKQRQKMGRTAFLTVVKKKGDGISPLREEAAGAEDEKVYTDRAKEKESQKMDGQRSKSLADIKESMENPQGKWLKSPSTPVDPEKQWNLTSPSEETLNEGELLEYTKSIEKLNSSLHFLQQEMQRLSLQQEMLMQMREQQSWVISPPQPSPQKQIRDFKPRQAGLSSAAAPFSADSPRPTHPSPQSSTRKSASFSVKNQRTPRPNELKITPLNRTLTPPRSVDSLPRLRRFSPSQVPIQTRSFVCFGDDGEPQKEPKPKEEIKKEPSECKGTLESCDHNPGEKEVKPLESTVSEVLSQPITETVCVTPNEDQLNQPTDPPPKPVFPPTAPKNVNLIEVSLSDLKPPEKADVSVEKFDGESDKEQFDDDQKVCCGFFFKDDQKAENDMAVKRAALLEKRLRREKETQLRKQQLEAEMEHRKEETRRKTEEERQKKEDERARREFIRQEYMRRKQLKLMEDMDTVIKPRPQVAKQKKQRPKSIHRDHIESPKTPIKGPPVSSLSLASLNTGDTESVHSGKRTPRSESVEGFLSPSRCGSRNGEKDWENASTTSSVASGTEYTGPKLYKEPSAKSNKHIIQNALAHCCLAGKVNEGQKKKILEEMEKSDANNFLILFRDSGCQFRSLYTYCPETEEINKLTGIGPKSITKKMIEGLYKYNSDRKQFSHIPAKTLSASVDAITIHSHLWQTKRPVTPKKLLPTKA
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Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization. Specifically recognizes growing microtubule minus-ends and autonomously decorates and stabilizes microtubule lattice formed by microtubule minus-end polymerization (By similarity). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (By similarity). In addition, it also reduces the velocity of microtubule polymerization (By similarity). Through the microtubule cytoskeleton, also regulates the organization of cellular organelles including the Golgi and the early endosomes (By similarity). Essential for the tethering, but not for nucleation of non-centrosomal microtubules at the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP, required to tether non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (By similarity). Also acts as a regulator of neuronal polarity and development: localizes to non-centrosomal microtubule minus-ends in neurons and stabilizes non-centrosomal microtubules, which is required for neuronal polarity, axon specification and dendritic branch formation. Through the microtubule cytoskeleton, regulates the autophagosome transport (By similarity).
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D4B387
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GGT1_ARTBC
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Glutathione hydrolase proenzyme (EC 3.4.19.13) (Gamma-glutamyltransferase ARB_02921) (EC 2.3.2.2) (Gamma-glutamyltranspeptidase) (Gamma-GT) (Leukotriene-C4 hydrolase) (EC 3.4.19.14) [Cleaved into: Glutathione hydrolase heavy chain; Glutathione hydrolase light chain]
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MAPAAMNLLCTVLYLLSSFAQVSDAAPWLFSRSIPASYHDGRLGAVASENSMCSEYGADMLKIGGNAADAVCIYRLSLFFAFLPYPALQEDRAMYHSGIGGGGFMLIRAPNGTYEFIDFRETAPAAAFQDMFKNNTSGSTSGGLASGVPGEVRGLEYLHKNYGKLPWKTVMEPAIRTARDGFRVTEDLSRIMLHSTKNGNFLAENAAWALDFAPQGTLLKVGDIITRRRYGDTLDKIAKYGADAFYTGPMAQAMVNALRAANGTMTLEDLKNYTVVSRPTAQIEYRGMTVTSTTAPSSGVVLLSILKLLNGYKNFFRMDPGPLSTHRMDEAIRFGYGQRTELGDPLFFSNLTDYQKKMISDEAANKNRMNISDEYTQDIAVYDPKGLESLNTPGTSHISTADRSGMAVSLTTTINLYFGSRVIVPETGIIMNNEMDDFSVPGRSNSFGYKPSPSNFIRPGKRPLSSICPTIITRPDGSLYFVSGAAGGSQIITGTLQSVINVMDRKMNVRQALKAPRLHDQLVPNVALMEDEFDKKTVDFMISRKHNVTREKSGSTVESIMRLKNGVFEASGEPRLANSGGVVV
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Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism.
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D4GP31
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XACC_HALVD
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Pentonolactonase XacC (EC 3.1.1.15) (EC 3.1.1.68) (L-arabinonolactonase) (Xylono-1,4-lactonase)
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MTVTRVVDTSCRLGEGPVWHPDEKRLYWVDIESGRLHRYDPETGAHDCPVETSVIAGVTIQRDGSLLAFMDRGRVGRVVDGDRRESARIVDSPTRFNDVIADPAGRVFCGTMPSDTAGGRLFRLDTDGTVTTVETGVGIPNGMGFTRDRERFYFTETEARTVYRYAYDEETGAVSARERFVESPETPGLPDGMTVDSAGHIWSARWEGGCVVEYDADGTELGRFDVPTEKVTSVAFGGPDLDSLYVTTAGGDGDGSAGEGDESTGDAAGALFRLDVAATGRPEFRSDVRLG
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Pentonolactonase involved in D-arabinose and D-xylose catabolism. Catalyzes the hydrolysis of both L-arabino-gamma-lactone and D-xylono-gamma-lactone to the corresponding acids. Can also hydrolyze D-galactono-gamma-lactone and D-glucono-delta-lactone.
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D4GP33
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ARADH_HALVD
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L-arabinose 1-dehydrogenase (NAD(P)(+)) (L-AraDH) (EC 1.1.1.376)
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MARIAVTGAAGNVGRVTVEALASDHDVTPITHREREGLDSVILDVRDEDALTEAFEGHDIVVHLAANPNPDAAWDSVYEVNIGGTYNVYEAALAADIDRLVFASTNHVHQMYNIADATRPETLAADAEAVGVSDPPRPDSYYGVSKVFGEALGNYYADRHGLEVLNLRIGWLLTADEVREKMDEEESVARYVRAMWLSPGDCEQGMRRAVEASLPDSPLAVNLISANDDRYLSLTETMRAIGYRPRDNSATVVE
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L-AraDH initiates the degradation of L-arabinose. Catalyzes the NAD(P)(+)-dependent conversion of L-arabinose to L-arabino-gamma-lactone. It is highly specific for L-arabinose as substrate and can use both NADP(+) and NAD(+) as electron acceptor, with a slight preference for NADP(+).
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D4GPK6
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LACC_HALVD
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Laccase (EC 1.10.3.2) (LccA multicopper oxidase)
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MTDWSRRRFLQTGAALGIAGTLPQTTTEVSAASPTLEKFVQPLPIPSVREPDGQRDGADAYEIAVTEFTQQLHPDLPETTVWGFDGSYPGPTIEADAGSPVHVRFDNSGLPSEHLFPVDDRLGGTTAENHPGYDGPVPEVRTVTHFHGLELDPANDGQSDMWTSPGGVEGPRFDSAWQELPMEQGRTTSTYHDHTLGITRLNAYAGLLGLYSITTDAERELGLPSGDYDIPLLLQDKEFNDDGSLHYPEEFVSAFLGDTAVVNGAVWPYVEVEPRRYRFRILNGANHRSFDLQLESESGSGVPTMYQFAPGHGFLESVVPIGPNGDLDSLLLTPFERGELVVDFSDHAGETLTLANGADMGPELTDLVEFRVSDPSTPPEDASADPTSLSLPTPASYDESDARVTREMTLGTEVRNGLITHTLNGHVFGDEDAPVYPQLGATEIWELQNESGGRHPIHLHLVTFRVIGRGPDGTQPPDPNELGPKDTVRVDPGERVRILVTFEGYTGQFPWHCHMLEHEDNKMMIPFVVENPVADYANEENVVDATGLTDAVGDWRNETLETEVLLEVIDQWRSGDEVA
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Catalyzes the oxidation of a wide variety of organic substrates, including bilirubin, syringaldazine (SGZ), 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) and dimethoxyphenol (DMP). No oxidation of Fe(2+) or guaiacol.
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D4GSE6
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KDGK1_HALVD
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2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase (2-dehydro-3-deoxyglucono/galactono-kinase) (EC 2.7.1.178) (2-keto-3-deoxygluconate/2-keto-3-deoxygalactonate kinase) (KDG kinase) (KDGK-1)
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MTALVTFGETMLRLSPPRGERLETARELEVQAGGAESNVAVAAARLGRDAAWFSKLPDSPLGRRIVSELRSHSVDTDGVVWTDDADARQGVYYLEHGASPRPTNVVYDRADAAVTTLETGEFDLDAVRDAEVCFTSGITPALSETLSETTADVLDEAQNAGTTTAFDLNYRTKLWSPDEAAEVYRDLLDSVDLLFAAERDAATVLGRDGDAESVARGLADDYDIETVVVTRGEEGSLAVSDGAVSEQGVYETETYDAIGTGDAFVGGFLAKHLDGGSVTESLEWASATASFKRTVEGDIAVVTPEDVERVVAEEGDGISR
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Involved in the degradation of glucose via the semi-phosphorylative Entner-Doudoroff pathway. Catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). Also catalyzes efficiently the phosphorylation of 2-keto-3-deoxygalactonate (KDGal) to 2-keto-3-deoxy-6-phosphogalactonate (KDPGal).
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D4GSF3
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UBAA_HALVD
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SAMP-activating enzyme E1 (EC 2.7.7.-) (Ubiquitin-like activating enzyme of archaea) (Ubl-activating enzyme)
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MTLSLDATQLDRYSRHIIMDEVGPEGQGRLLSSRVVVVGAGGLGAPAIQYLAAVGVGELVVVDDDVVERSNLQRQVVHCDDDVGTPKAESAAAFVRGLNPDVSVEPVEARVDKSNVHEVVAGSDVVVDASDNFPTRYLLNDVCRFEGIPLVHGAIYKFEGQATTLVPDGPCYRCLFPEAPEPGTVPDCATTGVLGVLPGTVGCIQATEAMKLLLDEGEALDGRLLFYDAMDMTFETVPYRTNPDCPVCGEGGVDSIEDIDYVESCAISLD
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Likely activates multiple ubiquitin-like SAMPs for protein conjugation as well as for sulfur transfer, via ATP-dependent adenylation at their C-terminus. In fact, it is required for the formation of all three SAMP1-, SAMP2- and SAMP3-protein conjugates, and for molybdenum cofactor (MoCo) biosynthesis and thiolation of tRNAs.
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D4GSH6
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NCSA_HALVD
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tRNA 2-thiolation protein NcsA (N-type ATP pyrophosphatase superfamily protein) (tRNA adenylyltransferase NcsA) (EC 2.7.7.-)
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MECDKCGRDAVMHAAYSGAHLCDDHFCASVEKRVRRRIREDNMLPRDASPENPQTWVIGLSGGKDSVVLTHILDDTFGRDPRIELVALTIHEGIEGYRDKSVDACVELAEDLDIHHELVTYEDEFGVQMDDVVEKDPENMAACAYCGVFRRDLLERFADELGADKLLTGHNLDDEAQTALMNFFEGDLKQVAKHFDASIGDFEKRRDAGEFIPRAKPLRDVPEKEVALYAHLKDLPAHITECPHSSEAYRGEIQQLLLKLEENHPGTRHSIMAGYEELAELTAREYRGEGRVDLNDCERCGSKTAGDVCRKCRLIESIEAV
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Required for thiolation of mcm(5)S(2)U at the wobble uridine position of tRNA specific for lysine (tRNA(Lys)). Probably acts by catalyzing adenylation of tRNA, an intermediate required for 2-thiolation. May also act as a sulfurtransferase that transfers sulfur from thiocarboxylated SAMP2 onto the uridine of tRNA at wobble position. Required for cell growth at elevated temperatures.
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D4GSH7
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FTSZ2_HALVD
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Cell division protein FtsZ 2
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MQDIVREAMERDEAERQTQSSLEDSDDQFGDPRIVIVGAGGAGNNTINRLYNIGVEGADTVAINTDKQHLKMIEADTKILVGKSLTQGLGAGGDPSMGERATEMAQGTIKDVLGDADLVFVTAGMGGGTGTGAAPVVAKIAKEQGAIVVGMVSTPFNVERARTVKAEEGLENLRNEADSIIVLDNNRLLDYVPNLPIGKAFSVMDQIIAETVKGISETITQPSLINLDYADMSTIMNQGGVAVMLVGETQDKNKTQEVVNDAMNHPLLDVDYRGASGGLVHITGGPDLTLKEAEGIASNITERLEAAANVIWGARIQDEYKGKVRVMAIMTGVQSAQVLGPSTQKQADKSRQSIQSRESQQQHSGSEFDSSERAQTAQSGTWSDGGRDEVEKNNGLDVIR
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Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity (By similarity). Required for division ring constriction. {ECO:0000255|HAMAP-Rule:MF_00909, ECO:0000269|PubMed:33903747}.
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D4GT97
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IPYR_HALVD
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Inorganic pyrophosphatase (PPA) (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase) (PPase)
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MVNLWEDMETGPNAPDEIYAVVECLKGERNKYEYDKDIPGVVLDRVLHSNVHYPSDYGFIPQTYYDDEDPFDVLVLVEDQTFPGCVIEARPVALMKMDDDGEQDDKVIAVPVEDPRYDHIEDLDDIPQQTLDEIDEFFATYKNLEAGKEVETLGWEDKQAAKDAIEHAMDLYEENFA
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Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions (By similarity). The hydrolysis of PPi by inorganic pyrophosphatase releases a considerable amount of energy that can drive unfavorable biochemical transformations to completion (Probable). Is not active on nucleoside triphosphates (ATP, TTP, GTP, or CTP) or nucleoside diphosphate (ADP). {ECO:0000255|HAMAP-Rule:MF_00209, ECO:0000269|PubMed:26546423, ECO:0000305|PubMed:26546423}.
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D4GTL2
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ACEB_HALVD
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Malate synthase (MSH) (EC 2.3.3.9)
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MTERRHDREFVRTFFTSPTAVEGEDDSAKMLRRAAGLRGMQAPDVWVPDNEDATAPSMRDEGAENIVEVISEQGAEFPGEIHPRMVWHRDSPETRYQGFQHMLDITDPERGAVEHIHGFVIPEVGGIDDWKKADEFFTIVEHEHGLDEGSLAMSVIIESGEAELAMGDLRDEMGKPTNNLERLFLLVDGEVDYTKDMRAMTPTGELPAWPELRHNTSRGASAAGCVAVDGPYDDIRDVEGYRERMTDNQAKGMLGIWSLTPGQVVEANTSPLPPKTGSWLLDADGEEVELASEDGVEAYDGDRLSLEATDGGYELRVGGDARELTADELREELLGLTSYVPSMDDIVDSMEEFEAAKEAGRGAIAMTQSATLRIGGTEIDIEKDRMWDEATYQAAMTPISLFQDVYENRPDQHEELEERYGAGVVERAMEVGL
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Involved in the glyoxylate cycle which synthesizes precursors for carbohydrates from C2 compounds such as acetate. Catalyzes the Claisen condensation between acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form the malyl-CoA intermediate that is subsequently hydrolyzed to produce malate and CoA.
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D4GTL3
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ACEA_HALVD
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Isocitrate lyase (ICL) (EC 4.1.3.1) (Isocitrase) (Isocitratase)
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MNPTELDSDVFAQDVDNQKARELREMLNTQDFVFAPGMYHALDARLAEMTGHDAAYMSGYSTVLGQFGFPDLEMVTMTEMVENAKRMVEATNLPVIADCDTGYGGIHNVRRAVREYEKAGVAAVHIEDQTTPKRCGHIAGKQIVSREKAKARFEAAVDAKQSEDTVVIARTDAYGSSNGDWDEHVERGRIYADAGVDIVWPEMPNPSREDAVAYAEEIHETHPDLKLAFNYSSSFAWSEEEDPLTFQELGDLGYKYIFITLFGLHSGAHAVYEDFKKLAEQDEEGQFDLEQRYLDHPTESHHELSFVSRYQDIETEFDPEARRRIEESEGFSEEQADPITSNDDD
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Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates.
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D4GTS4
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JAMM1_HALVD
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Desampylase (EC 3.4.19.15) (HvJAMM1)
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MTSSRLSLAADARDSILSHAREGAAGDPPAEVCGVLAGDSDARTVTAAHPVSNVAAEPRVAYELDPEETVSILEAIESAGDDAVGFYHSHPESDPVPSATDRERASWPGYVYLICSPDGRMTAHEWTGDEFRELSVAVE
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Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. Functions as a specific and not a general protease since it is unable to hydrolyze a variety of unmodified proteins otherwise hydrolyzed by proteinase K.
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D4GUA0
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AGLD_HALVD
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Glycosyltransferase AglD (EC 2.4.1.-) (Archaeal glycosylation protein D)
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MGRPTERRPAAATAAGVEVSVVLPAYNEARTIENTVRVTVETLESFLPADAFEVIVAEDGCDDETPEIADRLAAEDDRIRHYHSDDRLGRGGALERAFEAARGDTLVYFDTDLATDMRHLEELVERVRSGEYDAATGSRWMPDRVADRPRKRGVPSRAYNGLVRLFLRSDLRDHQCGFKAFSREAFEALRDDVEDNHWFWDTEMLVRAQRAGFRVAEFPVDWEPKGDTKVDLVRDILGMGSQILRTWWQLTVRPRITRRVTIVAGLLLTVLALALMTLYIDPSEVISVLGDADPALVAAAAVIYVVSWPLRGIRYREILRELGYREKAGFLTGAIFISQTGNLVFPARAGDAVRAYVVKARRNIPYPSGFASLAVERVFDLLTIAGLAGVVLVGLAATGGLDDIATVLATGVSGGSVDVSADDVRTAAYVATGVGVVAILGVLGIALSARADRNVVRAFVGRFSSDSYVELVAGVIEQFVSDLQAVAGNRAAFGRVGLTSLAIWTVDVVTAVVVLLALGVDIDPVVLVGVSFFAVSVGNLAKVLPLSPGGVGLYEIAFTVFMAALAPVTPAAALAAAVLDHAVKNAVTIVGGVGSMLSLNVSLTTAVEESAEVRDREHELADSK
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Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Catalyzes the addition of the mannose found at position 5 of the pentasaccharide to its own distinct dolichol phosphate carrier.
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D4GUJ7
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PAN1_HALVD
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Proteasome-activating nucleotidase 1 (PAN 1) (Proteasomal ATPase 1) (Proteasome regulatory ATPase 1) (Proteasome regulatory particle 1)
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MMTDTVDDVDLPYDKDSASQQEKITALQERLEVLETQNEEMRDKLLDTNAENNKYQQKLERLTHENKKLKQSPLFVATVQEITDEGVIIKQHGNNQEALTEVTDEMREELEPDARVAVNNSLSIVKRLDKETDVRARVMQVEHSPDVTYEDIGGLEEQMQEVRETVEMPLDRPEMFAEVGIDPPSGVLLYGPPGTGKTMLAKAVANQTNASFIKMAGSELVHKFIGEGAKLVRDLFEVARENEPAVIFIDEIDAIASKRTDSKTSGDAEVQRTMMQLLAEMDGFDERGNIRIIAATNRFDMLDPAILRPGRFDRLIEVPKPNEDGREIIFQIHTRKMNVSDDVDFVELAEMADNASGADIKAVCTEAGMFAIRDDRTEIFMQDFVDAWEKIQQEASDETEVSRAFA
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ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-terminus of the proteasomal ATPase functions like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates (Probable). Is also able to cleave other nucleoside triphosphates including GTP and TTP, but the rate of hydrolysis is 4- to 5-fold slower than for ATP.
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D4GY98
|
DNLJ_HALVD
|
DNA ligase (EC 6.5.1.2) (Polydeoxyribonucleotide synthase [NAD(+)])
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MSDADVDAESNPYLRDPPTEFEPAESLSREAAEGQAALLREAVREHDHRYYVAADPLVSDAAYDALFSRLVALEDAFDLDTTNSPTNRVGGEPIDALETVEHVAPMLSIDQSTDADDLREFDERVRREVGAVDYVCEPKFDGLSVEVVYEDGEFVRAATRGDGRRGDDVSAQVKTIPTVPLSLRGDHPDRLAVRGEIYMPKSDFSDLNARRVEAGEDAFANPRNAAAGTLRNLDPSVVADRPLAVFFYDILDASARPDSQWAALDRLREWGLRVTDRIERAEDVAEAIDYRDRMQAARDDLDYEIDGTVIKVDSRDARERLGEKSRSVRWAFAYKFPARHEVTTVRDIVVQVGRTGRLTPVAILDPVDVGGVTVSRATLHNPDERAALGVAVGDRVRVKRAGDVIPQVVEVTEDGGGCYEFPDECPVCGSAVDRDGPLAFCSGGLSCPAQREASIGHFAVKGAMDIDGLGEERVAQLVDAGLVETVADLYDLTADDLAELEGWGETSAENLVAAVENAKHPSLDSFLVGLSIPEVGEATARGLAREFGSIEAFPIEADAEEDEFDAFEERLTTVPDVGETVARRVRDFFENADNRAVIRALLDRGVDPEPVESGGDELDGLTFVVTGTLAASRSDVTELVESHGGNVTGSVSGNTDYLVVGENPGRSKRDDAEANDVPTLAETEFEALLAERGVAYPPE
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DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. {ECO:0000255|HAMAP-Rule:MF_01588, ECO:0000269|PubMed:17132163}.
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D4GYE0
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ALF_HALVD
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Fructose-bisphosphate aldolase class 2 (FBP aldolase) (FBPA) (EC 4.1.2.13) (Fructose-1,6-bisphosphate aldolase) (Fructose-bisphosphate aldolase class II)
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MPFYGGEELATVYDEALDEGFGLIASNIAEPNIMMGLMEGADRMDSDLLLQMSGGACRFAGDGDAVAGLKAMGNYIETIAERYDIGVFLNMDHQTDLEFIEQQIELDIPSSIMIDASHEPFDENVATSREVVEMVEAAGSDVLIEAELGQIKGVEDEIEAEEAFYTDPEQAVEFVDKTGADLLAISVGTQHGVAKGKDLELRPDLANDIRQALRDHGLDTPLVLHGSSGVQPDQLQEMLKHGICKVNKDTRYQYEYTRTAYDRYNEEPNAIVPPEGVADARDTFFNETDWSPNKDVFDPRVAGRDIRERIADVHADLTEVSGSAGQSLFK
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Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. Is required for the utilization of fructose as a sole carbon and energy source. Plays a role in gluconeogenesis during growth on acetate, D-xylose, and casamino acids.
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D4GYG6
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AGLQ_HALVD
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Archaeal glycosylation protein Q
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MTSLSDILASSAEAGLSLQRSDGSMPAGHNGPYHDPETPVRNTSHWLVTFLKAHELTDENRFRQAASDAVSYLLSEEARPHGHTFEHRQNDTKDRCNGLMGQAWSLEALALAARALDNERAAAVAADVFLSHPFCDKLKLWQRVDTDGTILGFDRTFNHQLWFAASGGLVAHTAPQEVSQRVRDFLDSLPSTIDLYENGLIRHPLRPSMDLSELAESVTHDVHRSMVRNHLLHYLRPPRSKRRLRNKAEGYHSFNLYALAILAREFPSHSVWSTDLLSDILEYTLSEEFREATTDNKFSHPYNPPGFEVPAAMETFSVGSYKEREMWVNEQIQHSFDPNTSLLTRGTDDKQTHAARLYEATRLDDYEIYLD
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Putative isomerase involved in the N-glycosylation pathway. Required for the appearance of the methyl ester of hexuronic acid found at position four of the pentasaccharide N-linked to the S-layer glycoprotein. Either involved in preparing the third sugar for attachment of the fourth pentasaccharide subunit or processing the fourth sugar prior to its addition to the lipid-linked trisaccharide.
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D4GYH4
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AGLB_HALVD
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Dolichyl-monophosphooligosaccharide--protein glycotransferase AglB (EC 2.4.99.21) (Archaeal glycosylation protein B) (Dolichyl-phosphooligosaccharide-protein glycotransferase) (Oligosaccharyl transferase) (OST) (OTase) (Oligosaccharyl transferase AglB)
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MSDEQTKYSPSIAELARDWYHIPVLSTIILVMLWIRLRSYDAFIREGTVFFSGNDAWYHLRQVEYTVRNWPATMPFDPWTEFPFGRTAGQFGTIYDQLVATAALVVGLGSPSSDLVAKSLLVAPAVFGALTVIPTYLIGKRLGGRLGGLFGAVILMLLPGTFLQRGLVGFADHNIVEPFFMGFAVLAIMIALTVADREKPVWELVAARDLDALREPLKWSVLAGVATAIYMWSWPPGILLVGIFGLFLVLKMASDYVRGRSPEHTAFVGAISMTVTGLLMFIPIEEPGFGVTDFGFLQPLFSLGVALGAVFLAALARWWESNDVDERYYPAVVGGTMLVGIVLFSLVLPSVFDSIARNFLRTVGFSAGAATRTISEAQPFLAANVLQSNGQTAVGRIMSEYGFTFFTGALAAVWLVAKPLVKGGNSRKIGYAVGSLALIGVLFLIPALPAGIGSALGVEPSLVSLTIVTALIVGAVMQADYESERLFVLVWAAIITSAAFTQVRFNYYLAVVVAVMNAYLLREALGIDFVGLANVERFDDISYGQVAAVVIAVLLILTPVLIIPIQLGNGGVSQTAMQASQTGPGTVTQWDGSLTWMQNNTPAEGEFGGESNRMEYYGTYEYTDDFDYPDGAYGVMSWWDYGHWITVLGERIPNANPFQGGATEAANYLLAEDEQQAESVLTSMGDDGEGDQTRYVMVDWQMASTDAKFSAPTVFYDESNISRSDFYNPMFRLQEQGEQTTVAAASSLKDQRYYESLMVRLYAYHGSAREASPIVVDWEERTSADGSTTFRVTPSDGQAVRTFDNMSAAEEYVANDPTSQIGGIGTFPEERVSALEHYRLVKSSNSSALRSGSYQRSLISEGNTYGLQPQALVPNNPAWVKTFERVPGATVDGSGAPANTTVTARVQMRDLTTGTNFTYTQQAQTDADGEFTMTLPYSTTGYDEYGPDNGYTNVSVRAAGGYAFTGPTSVTGNSTIVSYQAENVAVDEGLVNGAEDGTVQVTLERNEQELDLPGDSSSEDSSSEDGTSDGSQTNESASTSTSASVDASAVSAAA
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Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (a hexose-linked tetrasaccharide composed of a hexose, 2 hexuronic acids and a methyl ester of hexuronic acid in H.volcanii) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (Probable). Involved in the assembly of an N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins (Probable).
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D4GYI2
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GLPA1_HALVD
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Anaerobic glycerol-3-phosphate dehydrogenase subunit A1 (G-3-P dehydrogenase A1) (G3PDH A1) (EC 1.1.5.3)
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MKKSPSVLVIGGGSTGTGIARDLAMRGLDVTLVEKGNLTHGTTGRMHGLLHSGGRYAVSDQPSAKECIEENRVLRRIAGHCVEMTGGLFVQRPEDSDEYFEKKLEGCRECGIPAEVLSAEEAREIEPYLAKDIKRAIKVPDGAVDPFRLCVANAASAVEHGARIETHSEVTDVLVEGGEVVGVEVTHQTGTGPYVHGEPGEVEEIRADYVVNATGAWAGQIGDFAGVNVEVRPSKGVMTIMNTRQVDTVVNRCRPKGDADIIVPHETTCILGTTDEEVEDPEDYPEEGWEVDLMIETLSELVPMLADARTIRSFWGVRPLYEPPGTGTEDPTDITREFFLLDHADRDDLPGMTSIVGGKLTTYRMMAEQISDHVCEKLGVDAECRTADEPLPGSEDFTVLRDYMDDFGLRSPIGRRSAQRLGSRADEVLNSVDPNPVVCECEAVTRAEIQDALDTAGTDLNSVRIQTRASMGNCQGAICCHRMANELAPEYDEKTVRASLDDLYQERWKGERHAMWGTQLSQTALKHMLHAATMNRDEDPAAADADIDFAAFDDGVASGGAVADGGRERAADRADDDALGGADGDN
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Conversion of glycerol 3-phosphate to dihydroxyacetone phosphate. Required for growth on glycerol and for glycerol metabolism.
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D4GYV5
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SUFS_HALVD
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Cysteine desulfurase (EC 2.8.1.7) (Selenocysteine lyase) (EC 4.4.1.16)
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MRVQESYPVDVDAIRADFPILERKVGGDISTPGEHDDDTTPLVYLDNAATSHTPEQVVDAIVDYYHGYNSNVHRGIHHLSQEASVAYEDAHDRVAEFIGASGGREEVVFTKNTTESMNLVAYAWGLDELGPGDSVVMTEMEHHASLVTWQQIAKKTGAEVRYIRVDDDGRLDMEHAKELIDDSTKMVSVVHVSNTLGTVNPVSELADMAHEVGSYIFVDGAQSVPTRPVDVEDIDADFFAFSGHKMCGPTGIGALYGKRDILDEMGPYLYGGEMIRSVTYEDSTWEDLPWKFEAGTPPIAQGVGFAAAVDYLDDIGMENVQAHEELLAEYAYDRLTEFDDIEIYGPPGDDRGGLVSFNLDSVHAHDLSSILNEQGVAIRAGDHCTQPLHDKLGVAASTRASFYIYNAREEVDKLVDAIDAARELFA
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Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Able to reassemble a removed [2Fe-2S] cluster of an apo-ferredoxin. Shows a selenocysteine lyase activity approximately 280-fold higher than its cysteine desulfurase activity.
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D4GYZ1
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PSB_HALVD
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Proteasome subunit beta (EC 3.4.25.1) (20S proteasome beta subunit) (Proteasome core protein PsmB)
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MRTPTHDEFSGRLDSLNGDRSNVFGPELGEFSNADRRADELGDKETKTGTTTVGIKTEEGVVLATDMRASMGYMVSSKDVQKVEEIHPTGALTIAGSVSAAQSLISSLRAEVRLYEARRGEDMSMQALSTLVGNFLRSGGFYVVQPILGGVDETGPHIYSIDPAGSILEEEYTVTGSGSQYALGVLEQEFEDGLSIEEAKGVATKAIRSAVERDLASGNGINIAVVTEDGVDIQRHQNFEGLE
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Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The H.volcanii alpha1-beta proteasome is able to cleave oligopeptides after Phe, Tyr and Trp, poorly after Glu but not after Arg. Thus, displays chymotrypsin-like activity, low caspase-like activity but no trypsin-like activity. {ECO:0000255|HAMAP-Rule:MF_02113, ECO:0000269|PubMed:10482525}.
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D4GZE7
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SAMP2_HALVD
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Small archaeal modifier protein 2 (SAMP2) (Ubiquitin-like small archaeal modifier protein 2)
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MNVTVEVVGEETSEVAVDDDGTYADLVRAVDLSPHEVTVLVDGRPVPEDQSVEVDRVKVLRLIKGG
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Functions as a protein modifier covalently attached to lysine residues of substrate proteins, as well as a sulfur carrier in tRNA thiolation. The protein modification process is termed sampylation and involves the formation of an isopeptide bond between the SAMP2 C-terminal glycine carboxylate and the epsilon-amino group of lysine residues on target proteins. Is able to form polymeric chains with itself at Lys-58, similar to ubiquitin and other ubiquitin-like proteins. May serve as a proteolytic signal in the cell to target proteins for degradation by proteasomes.
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D4HRL0
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GH7B_LIMQU
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Exoglucanase GH7B (EC 3.2.1.91) (1,4-beta-cellobiohydrolase) (Cellobiohydrolase 7B) (LqCel7B) (Glycosyl hydrolase family 7 protein B)
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MSLAVVFLLGFLAVSHGQQAGTETEEYHLPLTWERDGSSVSASVVIDSNWRWTHSTEDTTNCYDGNEWDSTLCPDADTCTENCAIDGVDQGTWGDTYGITASGSKLTLSFVTEGEYSTDIGSRVFLMADDDNYEIFNLLDKEFSFDVDASNLPCGLNGALYFVSMDEDGGTSKYSTNTAGAKYGTGYCDAQCPHDMKFIAGKANSDGWTPSDNDQNAGTGEMGACCHEMDIWEANSQAQSYTAHVCSVDGYTPCTGTDCGDNGDDRYKGVCDKDGCDYAAYRLGQHDFYGEGGTVDSGSTLTVITQFITGGGGLNEIRRIYQQGGQTIQNAAVNFPGDVDPYDSITEDFCVDIKRYFGDTNDFDAKGGMSGMSNALKKGMVLVMSLWDDHYANMLWLDATYPVDSTEPGALRGPCSTDSGDPADVEANFPGSTVTFSNIKIGPIQSYD
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Exocellobiohydrolase (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose. The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds in cellulose to reduce the polymerization degree of the substrate and create new chain ends for exocellobiohydrolases (CBHs). The CBHs release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units (Probable).
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D4N500
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DIOX1_PAPSO
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Thebaine 6-O-demethylase (EC 1.14.11.31) (Canadine demethylase) (EC 2.1.1.-)
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MEKAKLMKLGNGMEIPSVQELAKLTLAEIPSRYVCANENLLLPMGASVINDHETIPVIDIENLLSPEPIIGKLELDRLHFACKEWGFFQVVNHGVDASLVDSVKSEIQGFFNLSMDEKTKYEQEDGDVEGFGQGFIESEDQTLDWADIFMMFTLPLHLRKPHLFSKLPVPLRETIESYSSEMKKLSMVLFNKMEKALQVQAAEIKGMSEVFIDGTQAMRMNYYPPCPQPNLAIGLTSHSDFGGLTILLQINEVEGLQIKREGTWIAVKPLPNAFVVNVGDILEIMTNGIYHSVDHRAVVNSTNERLSIATFHDPSLESVIGPISSLITPETPALFKSGSTYGDLVEECKTRKLDGKSFLDSMRI
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Non-heme dioxygenase involved in biosynthesis of morphinan-type benzylisoquinoline and opiate alkaloids natural products. Mediates the conversion of thebaine to neopinone. Catalyzes also, with lower efficiency, the 6-O-demethylation of oripavine to neomorphinone, which is converted spontaneously to morphinone. Supports dealkylation reactions such as O,O-demethylenation in the metabolism of protopine, benzo[c]phenanthridine, and rhoeadine alkaloids cleaves a methylenedioxy bridge leaving two hydroxyl groups. Catalyzes the O-demethylation of methylenedioxy bridges on protopine alkaloids such as allocryptopine. No activity with (S)-reticuline, salutaridine, papaverine, (S)-corytuberine, (S)-scoulerine, pavine, noscapine or codeine.
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D4N502
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DIOX3_PAPSO
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Codeine O-demethylase (EC 1.14.11.32) (Thebaine 6-O-demethylase) (EC 1.14.11.31)
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METPILIKLGNGLSIPSVQELAKLTLAEIPSRYTCTGESPLNNIGASVTDDETVPVIDLQNLLSPEPVVGKLELDKLHSACKEWGFFQLVNHGVDALLMDNIKSEIKGFFNLPMNEKTKYGQQDGDFEGFGQPYIESEDQRLDWTEVFSMLSLPLHLRKPHLFPELPLPFRETLESYLSKMKKLSTVVFEMLEKSLQLVEIKGMTDLFEDGLQTMRMNYYPPCPRPELVLGLTSHSDFSGLTILLQLNEVEGLQIRKEERWISIKPLPDAFIVNVGDILEIMTNGIYRSVEHRAVVNSTKERLSIATFHDSKLESEIGPISSLVTPETPALFKRGRYEDILKENLSRKLDGKSFLDYMRM
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Non-heme dioxygenase involved in biosynthesis of morphinan-type benzylisoquinoline and opiate alkaloids natural products. Mediates the conversion of codeine to morphine. Catalyzes also, with lower efficiency, the 3-O-demethylation of thebaine to oripavine and of (S)-scoulerine to 3-O-demethylscoulerine. Supports, with a lower turnover, the conversion of codeinone to morphinone, of thebaine to neopinone, and of neopine to neomorphine. Supports dealkylation reactions such as O,O-demethylenation in the metabolism of protopine, benzo[c]phenanthridine, and rhoeadine alkaloids cleaves a methylenedioxy bridge leaving two hydroxyl groups. Catalyzes the O,O-demethylenation of methylenedioxy bridges on protopine alkaloids such as allocryptopine, cryptopine and protopine. No activity with (S)-reticuline, salutaridine, papaverine, (S)-corytuberine, oripavine, pavine or noscapine.
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D4NUX0
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HCT1_ACTRA
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Hydroxycinnamoyl-CoA:piscidic acid hydroxycinnamoyltransferase (EC 2.3.1.-) (ArHCT1) (ArHPT1) (BAHD acyltransferase/hydroxycinnamoyltransferase) (BAHD-type hydroxycinnamoyltransferase) (Cimicifugic acid synthase)
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MVCIKSSCVVKPSEPTPNVKLFLPESDQVKPWTHAPVFFVYQPEVDNSVSTSLENLKFSLSRALVPYYPLAGRLNGIGGGRFELHCNTMGAVIIEAESDARLEDFGDFRPTSETTKLAPYVDYAKDVSELPLLLVQLTRFKCGGIGIGIAMSHIVSDGKGAFGFITTWAKINRGEKGIIEPFHDRTAFYKGDPTAKPRCDHVELKGYPVLLGNKSAKEERAKETTTRMLNLSKNQVDKLKEKSNLGKPKDYVGREYSRFEAMSGHIWRCASKARRHENEQLTSLRITIDCRNRLRPPLPPRYSGNATMVTTSIAESGELLSNPLGLGFVCSVIRKCIDKVDDDYIKSATDFLISQDDLTPYRSGFHNVGSTEGVFLGNPNLAITSWVGLPINDVDFGWGKPIYMGPTALGYDGKLLIIPGKDDGSVIVPIRLQVAHIDDFEKFFYEDI
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Catalyzes the formation of cimicifugic acids. Uses hydroxycinnamoyl-CoA thioesters as hydroxycinnamoyl donor substrates. Has a strict specificity for piscidic acid as an acceptor substrate as none of the various other acceptors tested including 4-hydroxyphenyllactic acid, malate, spermidine or tetrahydroxyhexanedioic acid are substrates. Donor substrates include 4-coumaroyl-CoA, caffeoyl-CoA, sinapoyl-CoA and feruloyl-CoA. No activity with cinnamoyl-CoA, isoferuloyl-CoA, 3,4-dimethoxycinnamoyl-CoA or 3,4-dihydroxybenzoyl-CoA as donors. In the reverse reaction with fukinolic acid and CoA as substrates, a formation of fukiic acid is evident. Hence, fukiic acid may also serve as an acceptor substrate. Involved in the biosynthesis of cimicifugic and possibly fukinolic acids.
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D4P095
|
CNPD3_PSEAI
|
3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA (3',5'-cyclic AMP phosphodiesterase) (cAMP phosphodiesterase) (EC 3.1.4.53)
|
MSRHSNTPATDASVLLVQLSDSHLFAEDGARLLGMDTAHSLEKVVERVAREQPRIDLILATGDVSQDGSLDSYTRFRRLSAPLAAPLRWFAGNHDEREPMQRATEGSDLLEQIVDVGNWRVVLLDSSIPGAVPGYLEDDQLDLLRRAIDSAGERFLLVSFHHHPVPIGSDWMDPIGLRNPQALFDLLAPYPQLRCLLWGHIHQEFDRQRGPLRLLASPSTCVQFAPGSSDFTLDRLAPGYRWLRLHDDGRLETGISRVDDVVFEVDYDTAGY
|
Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes. Specifically required for regulation of virulence factors. Can also hydrolyze cGMP, but cGMP is unlikely to be synthesized by P.aeruginosa and cAMP is probably the biologically relevant substrate for CpdA in vivo.
|
D4YWD1
|
TPF_PELSA
|
Temporin-SHf (Temp-SHf) (Phe-rich antimicrobial peptide)
|
FLGTINLSLCEEERDADEEERRDEPDESNVEVKKRFFFLSRIFGK
|
Non-amphipathic alpha-helical antimicrobial peptide with potent activity against some Gram-positive bacteria (including methicillin-resistant Staphylococcus aureus (MRSA)), weak activity against Gram-negative bacteria and no activity against fungi. Permeabilizates membranes through a detergent-like effect probably via the carpet mechanism. More precisely, it strongly and selectively perturbs anionic bilayers membranes by interacting with the polar headgroups and the glycerol backbone region of the phospholipids, hence disrupting the acyl chain packing of the bilayer. Is not active against Leishmania (promastigote and axenic amastigote forms). Does not show hemolytic activity. Does not show toxicity for human THP-1-derived macrophages.
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D4Z2G1
|
LINB_SPHIU
|
Haloalkane dehalogenase (EC 3.8.1.5) (1,3,4,6-tetrachloro-1,4-cyclohexadiene halidohydrolase) (1,4-TCDN halidohydrolase)
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MSLGAKPFGEKKFIEIKGRRMAYIDEGTGDPILFQHGNPTSSYLWRNIMPHCAGLGRLIACDLIGMGDSDKLDPSGPERYAYAEHRDYLDALWEALDLGDRVVLVVHDWGSALGFDWARRHRERVQGIAYMEAIAMPIEWADFPEQDRDLFQAFRSQAGEELVLQDNVFVEQVLPGLILRPLSEAEMAAYREPFLAAGEARRPTLSWPRQIPIAGTPADVVAIARDYAGWLSESPIPKLFINAEPGALTTGRMRDFCRTWPNQTEITVAGAHFIQEDSPDEIGAAIAAFVRRLRPA
|
Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Has a broad substrate specificity since not only monochloroalkanes (C3 to C10) but also dichloroalkanes (> C3), bromoalkanes, and chlorinated aliphatic alcohols are good substrates. Shows almost no activity with 1,2-dichloroethane, but very high activity with the brominated analog. Is involved in the degradation of the important environmental pollutant gamma-hexachlorocyclohexane (gamma-HCH or lindane) as it also catalyzes conversion of 1,3,4,6-tetrachloro-1,4-cyclohexadiene (1,4-TCDN) to 2,5-dichloro-2,5-cyclohexadiene-1,4-diol (2,5-DDOL) via the intermediate 2,4,5-trichloro-2,5-cyclohexadiene-1-ol (2,4,5-DNOL). This degradation pathway allows S.japonicum UT26 to grow on gamma-HCH as the sole source of carbon and energy.
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D5ARP7
|
CCOP_RHOCB
|
Cbb3-type cytochrome c oxidase subunit CcoP (Cbb3-Cox subunit CcoP) (C-type cytochrome CcoP) (Cyt c(P)) (Cytochrome c oxidase subunit III)
|
MSKKPTTKKEVQTTGHSWDGIEELNTPLPRWWLWTFYATIVWGVAYSIAMPAWPIFASGATPGILGSSTRADVEKDIAKFAEMNKAVEDKLVATDLTAIAADPELVTYTRNAGAAVFRTWCAQCHGAGAGGNTGFPSLLDGDWLHGGSIETIYTNIKHGIRDPLDPDTLPVANMPAHLTDELLEPAQIDDVVQYVLKISGQPADEARATAGQQVFADNCVSCHGEDAKGMVEMGAPNLTDGIWLYGGDANTITTTIQLGRGGVMPSWSWAADGAKPRLSEAQIRAVASYVHSLGGGQ
|
C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. CcoP subunit is required for transferring electrons from donor cytochrome c via its heme groups to CcoO subunit. From there, electrons are shuttled to the catalytic binuclear center of CcoN subunit where oxygen reduction takes place. The complex also functions as a proton pump.
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D5AUZ9
|
CBIM_RHOCB
|
Cobalt transport protein CbiM (Energy-coupling factor transporter probable substrate-capture protein CbiM) (ECF transporter S component CbiM)
|
MHIMEGYLPVTHAIGWSLAAGPFVVAGAVKIRKIVAERPEARMTLAASGAFAFVLSALKIPSVTGSCSHPTGTGLGAVVFGPSVMAVLGVIVLLFQALLLAHGGLTTLGANAFSMAIVGPWVAWGVYKLAGKAGASMAVAVFLAAFLGDLATYVTTSLQLALAYPDPVSGFLGAALKFGSVFALTQIPLAIAEGFLTVIVVDALAGKVDDKDKLRILAGEAR
|
Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. The complex confers cobalt uptake upon expression in E.coli can also transport nickel with a very low affinity. A Cbi(MN) fusion protein has about 70% import capacity, but the holo-Cbi(MN)QO complex cannot be isolated, suggesting CbiN may destabilize it.
|
D5CBA0
|
CDIA_ENTCC
|
16S rRNA endonuclease CdiA (rRNase CdiA) (EC 3.1.-.-) (CdiA-ECL) (Toxin CdiA)
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MMKQDQVRFSQRALSALLSVLLATQPLLPAVAASITPSGNTQMDKAANGVPVVNIATPNQSGISHNKYNDYNVGKEGLILNNATGQLNQTQLGGLIQNNPNLKAGQEAKGIINEVTGANRSNLQGYTEVAGKAANVIVANPYGITCNGCGFINTPNVTLTTGKPVLDASGKLQSLDVTQGAVTIEGAGLNGSQSDAVSIISRATEINVQLHAKDLRVVAGANRVAADGSVSALKGEGTAPKVAVDTGALGGMYANRIRLVSSETGVGVNLGNLNARQGDIALSSAGKVVLKNTLASGSTTVSAADVTLRGDHKAGGNVTVSGQTALTLDQAHVAADNNLQLTTRGTLTQNGGAFTAANDATLAATTLIQSVDAQASAGRHLAVNAEKNAALNGSVVAGQQLSVKGGELVQQGNLSASEIALNAQTLTQESRSTTNASGNITLTTSGHSQLKGSTTAGQSLAVSAGSLANHGALAAVADTRINTGIFSNTGTVQGNSLTVSGTDITSSGALKSASTLDIRADNATLSGETGAKGKTTVTASGNLNNSGTLISDDTLTLNAAQIVNSGTLSGVRGLTTSGKTFTASATSVTQSDGDVALNNTDTTLAGETSAGGAVTVQGRSLNTTATAQTQGNSVGVAVQNAKLEGTQAAKGNMTLKADSSLNHTGKSSASGLKVETGHLSNSGTLTASALVIDSPEVINGGLIHAGQTLSLVTRLLDNRSSGVLYSPSALSLSLSELNNAGIITSDAALSLSGSNLTNSGELSGTSLAIDYETLKNSAEGMLLAQGANRITAQSVSSAGSMVGNTLTLNADRLESAGLLQGDSALSLTAGILNLLTGSRTLTGGALGLSGTTLTTAGQLQGQDVSIRSHDWTNRGSSLATGSLDVTTAGTLSNTGELMSQGNGTLNAVTTVNSGNMLSAGDLSLNGKTLRNSGTLQGNRVTAHQDTITNSGTLTGIAALMLAARLEMAAPLLTLVNDASGSLLTAGELSVTGGDLRNAGQWQGKRVLIHAQALTNGGAIQAENLLDAQIDSTLTGTAGSKITSNGELALSALTLANSGQWIAKHLTLGASTLNNSGEITGVVALSVALTQLNNQAGGKLLSAGALTLDVENATNAGQIQGKATTVTAGQLINSGRLQGEALTLNASGALNNTASGVLLSENALTVSTATLNNQGTLQGGGESSVKATTRVQNDGKMLSGGKLTLTAPELANSSSGLVQAVRLLLDVVKAVNGGNVLATTRAELRGSSLDNSGTLQGADLQANYQSVTNSGTVLGTTSLTINGDALDNTESGKLYSGDKLLLDVRNYSGRGDVVSLGDTTLKLVNALVNTGTLAASKTLSVSSQNAMTNSGVMQGNAIALSAGGAFTNNGTLTTGNGSSTFNAQSLLLNASGSLQAGGDVQLTSRENITVNGFTGTAGSLTMTAAGTLLNTALIYAGNNISLFAARIHNIYGDILADNSLWMQKNAVGEANAEVVNRSGTIETTRGDITVNTGHLLNEADGLTVSQSEREYPDAIPAADEHYFSYDLNGRRSDFVLLLEDWKNDGSKVVYDWYEQCLGSGANGSGQCRDRVDYRLTGEDIRQFLLSESVVSVSATGSSARIAAGRDITINAGTLDNRASHILAGRNAVLAGGTLNNLSAEGGRRVTYVQAEYRCEWFYRDCSDSKWEPLTQYPDGSWGWFDEDYGWYGWVPYILGERTTEFVADGGVYRSVISAGGNVSANFTSDISNTNVTANSGEFSNTIDAPTLNTLSPEAIGKGLNSESLAQGGSADIRFPEQLGNITDALKDISGGSSLSDQNGSSGNYPLPSGNNGYFVPSTDPDSPYLITVNPKLDELGNMDDSLFNGLYDLLGITPGATPRETNSAYTDRNQFLGSSYFLDRLGLNPDRDYRFLGDAAFDTRYVSNAILNQTGSRYINGIGSDLDQMRYLMDSAAEQQKTLGLKFGVALTAEQVAALDKSMLWWESATINGQTVMIPKVYLSPKDVTVHSGSVISGNNVQLAGGNVINSGSTIAAQNGLSIDSSNSLSNLNAGLLSAGGGLNLSALGDINNIGSTISGKTVGLESVAGSINNITRAQQWNVDAGNVHFSGTDVGKTASITATDGLTMRAGQDINVTGANVSAGGSLGMAAGNDINITANEIVTSEGRAGRNRATTETASVTHQGSTLSAGDDLTLQAGNDVNARAAAIAAEGDVGIQAGRDVDLLAEASMERSSSQAKKKTAIDESVRQQGTEIASGGNTVILAGRDVTAQAADVTAQGDIGVAAGRDVNLTTATESDYRYREQTKTSSGFLSKKTTHTIEEESATREKGSLLSGDNVTVSAGNNLRVLGSAVAGDGDVALSAGNNVDIVAATNTDTAWRFKETKKSGLMGTGGIGFTIGSSKSTHDLREQGTTQSESFSTVGSTGGNVSIAAGKQAHIGGADIIAQKDISLTGDSVVIEPGHDKRTRDEKFEQKSSGLTVALSGAAGSAVNNAVTTAQSAKQSSDSRLAALQGTQAALSGVQAGQAVALDQVKGDSDKRNNNTIGVSASIGSQSSKSSSHMESETTTGSTLSAGNNVTIKATGSDITVAGSQIKAGKDVTLDAARDVNLIASQDTQQTTGKNSSSGGSLGVGVGVGSGGAGISISANANSSKGHEKGNGVWQNETTVDAGNRVTINTGRDATIAGAQVSGETVVADIGRDLTIASTQDSDHYNSKQNSVSGGAGYTFGAGGFSGSINVSRDKMTSDYDSVQEQSGLFAGNGGFDVTVGNHTQLDSGVIASTATADKNRLDTGTLGFSDIHNQADFKTEHQGAGISSGGSIGKQFAGNMANALLAGGGNSGHAEGTTQAAVSEGTLIIRDKENQKQDVADLSRDAEHANGSISPIFDKEKEQQRLQEVQLIGEIGSQVVDIANTQGEINGLNAGRKELADKGITEPGADASDEVKAAYQNALRETDAYKTTTAKYGTGSDLQRGIQAATAALQGLAGSDLTAALAGASAPELAYRIGHGMGIDNNTAAKTIAHAILGGAVAALQGNSAAAGAAGAATGELAAKAIAGMLYPDVKDLSTLSEEQKQTVSALATISAGMAGGLAGDSTGSAVAGGQAGKNAAENNSLALVARGCAVAAPCRTKVAEQLLEIGAKAGIAGLAGAAVKDMADKMTSDELEHLVTLEMMGNDEIIAKYVSLLHDKYAPSHTGGNLLPETLPGHTGNNTGSVDTGPNHTGNTNRQNDSGSNNTGNTEGAPNTGGNTTITPIPNGPSKDDIAYLALKGKEAQEAASNLGFDRRIPPQKAPFNSHGQPVFYDGKNYITPDIDSHNVTNGWKMFNSKGKRIGTYDSGLNRIKD
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Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion upon forced induction decreases E.cloacae target cell counts about 20-fold, about 100-fold in E.coli. Intracellular expression of CdiA-CT (residues 3087-3321) inhibits E.coli cell growth when induced, but coexpression with its cognate immunity protein CdiI allows cell growth. Cleaves 16S rRNA in vivo and in vitro between adenine 1493 and guanosine 1494 of E.coli 16S rRNA. Inhibition of 16S rRNA cleavage is specific to the cognate immunity protein, non-cognate CdiI from E.chrysanthemi strain EC16 does not inhibit this protein. Purified CdiA-CT inhibits E.coli cell growth when added to cultures but not when added as a complex with cognate CdiI, suggesting cognate CdiI prevents import into the target cell. CdiA-CT (without CdiI) is probably imported in an F-pilus-mediated fashion, although it is not clear if this is physiologically significant. Gains access to the cytoplasm of target cells by using integral inner membrane protein FtsH. The CdiA protein is thought to be exported from the cell through the central lumen of CdiB, the other half of its two-partner system (TPS). The TPS domain probably remains associated with CdiB while the FHA-1 domain forms an extended filament with the receptor-binding domain (RBD) at its extremity in the secretion arrested state the C-terminus of the RBD and YP domains form a hairpin-like structure as the FHA-2, PT and CT domains are periplasmic. The YP domain is probably responsible for this arrest at the point where it re-enters the host cell periplasm. Upon binding to a target cell outer membrane receptor a signal is transmitted to activate secretion. The filament elongates slightly, the rest of CdiA is secreted and the FHA-2 domain becomes stably associated with the target cell's outer membrane where it facilitates entry of the toxic CT domain into the target cell periplasm. From there the toxic CT domain is cleaved and gains access to the target cell cytoplasm via an inner membrane protein (FtsH for this CDI).
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D5EY13
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XYFA_PRER2
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Endo-1,4-beta-xylanase/feruloyl esterase [Includes: Endo-1,4-beta-xylanase (EC 3.2.1.8); Feruloyl esterase (EC 3.1.1.73) (Ferulic acid esterase)]
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MKKLLVALSLIAGSLTASAQWGRPVDYAAGPGLKDAYKDYFTVGVAVNKFNISDPAQTAIVKKQFNSVTAENAWKPGEIHPKEGVWNFGLADSIANFCRENGIKMRGHCLCWHSQFADWMFTDKKGKPVKKEVFYQRLREHIHTVVNRYKDVVYAWDVVNEAMADDGRPFEFVDGKMVPASPYRQSRHFKLCGDEFIAKAFEFAREADPTGVLMYNDYSCVDEGKRERIYNMVKKMKEAGVPIDGIGMQGHYNIYFPDEEKLEKAINRFSEIVNTIHITELDLRTNTESGGQLMFSRGEAKPQPGYMQTLQEDQYARLFKIFRKHKDVIKNVTFWNLSDKDSWLGVNNHPLPFDENFKAKRSLQIIRDFDAAMDNRKPKEDFVPNPMNQPGQEYPMVNSEGYARFRVEAPDAKSVIVSLGLGGRGGTVLRKDKNGVWTGTTEGPMDPGFHYYHLTIDGGVFNDPGTHNYFGSCRWESGIEIPAKDQDFYAYRKDINHGNIQQVTFWSESTGKMQTANVYLPYGYGKVVKGKQERYPVLYLQHGWGENETSWPVQGKAGLIMDNLIADGKIKPFIVVMAYGLTNDFKFGSIGKFTAEEFEKVLIDELIPTIDKNFLTKADKWNRAMAGLSMGGMETKLITLRRPEMFGYWGLLSGGTYMPEEIKDPKAVKYIFVGCGDKENPEGINKSVEALKAAGFKAEGLVSEGTAHEFLTWRRCLEKMAQSLFK
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Involved in degradation of plant cell wall polysaccharides. Has endo-xylanase activity towards substrates such as oat spelt xylan (OSX), acetylated xylo-oligosaccharides and acetylated xylan, producing primarily xylobiose cannot hydrolyze xylobiose to xylose. Also has feruloyl esterase activity, releasing ferulic acid from methylferulate, and from the more natural substrates wheat bran, corn fiber, and XOS(FA,Ac), a corn fiber-derived substrate enriched in O-acetyl and ferulic acid esters. Exhibits negligible acetyl esterase activity on sugar acetates. Acts synergistically with Xyl3A to increase the release of xylose from xylan. Does not possess endoglucanase or mannanase activities since it is not able to hydrolyze carboxymethyl cellulose and locust bean gum.
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D5EY15
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XYL3A_PRER2
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Xylan 1,4-beta-xylosidase (EC 3.2.1.37) (1,4-beta-D-xylan xylohydrolase) (Alpha-L-arabinofuranosidase) (Arabinosidase) (EC 3.2.1.55) (Beta-D-xylosidase) (Exo-1,4-beta-xylosidase)
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MKYQLFLSLALCVGLGASAQTLPYQNPNLSAKERAVDLCSRLTLEEKAMLMLDESPAIPRLGIKKFFWWSEALHGAANMGNVTNFPEPVGMAASFNPHLLFKVFDIASTEFRAQYNHRMYDLNGEDMKMRSLSVWTPNVNIFRDPRWGRGQETYGEDPYLTSVMGVQVVKGLQGPEDARYRKLWACAKHYAVHSGPEYTRHTANLTDVSARDFWETYMPAFKTLVKDAKVREVMCAYQRLDDDPCCGSTRLLQQILRDEWGFEYLVVSDCGAVSDFYENHKSSSDAVHGTSKAVLAGTDVECGFNYAYKSLPEAVRKGLLSEKEVDKHVIRLLEGRFDLGEMDDPSLVEWSKIPYSAMSTKASANVALDMARQTIVLLQNKNNILPLKKNAEKIAIIGPNAHNEPMMWGNYNGTPNHTVTILDGVKAKQKKLVYIPGCDLTNDKVMECHLATDCVTPDGKKGLKGTFWNNTEMAGKPFTTEYYTKPVNVTTAGMHVFAPNLPIEDFSAKYETTFTAKEAGEYVVNVESTGHFELYVNGKQQFVNHIWRATPTRTVLKAEKGQKFDIEVRFQTVKTWGASMKIDVARELNIDYQETIAQLKGINKVIFCGGIAPSLEGEEMPVNIEGFKGGDRTSIELPKVQREFLKALKAAGKQVIYVNCSGSAIALQPETESCDAIVQAWYPGQEGGTAVADVLFGDYNPGGKLSVTFYKNDQQLPDYEDYSMKGRTYRYFDDALFPFGYGLSYTTFEVGEAKVEAATDGALYNVQIPVTNTGTKNGSETIQLYIRNLQDPDGPLKSLRGFERLDIKAGKTATANLKLTKESLEFWDAETNTMRTKPGKYEILYGTSSLDKDLKKLTITL
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Involved in degradation of plant cell wall polysaccharides. Has beta-xylosidase activity via its capacity to hydrolyze glycosidic linkages of beta-1,4-xylo-oligosaccharides of various lengths (X2 to X6), releasing xylose monomers. To a much lesser extent, also has alpha-L-arabinofuranosidase activity. Does not possess beta-D-glucosidase activity. Acts synergistically with Xyn10D-Fae1A to increase the release of xylose from xylan.
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D5JWB3
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SARED_ESCCA
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Sanguinarine reductase (EC 1.3.1.107)
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MADSSKKLTVLLSGASGLTGSLAFKKLKERSDKFEVRGLVRSEASKQKLGGGDEIFIGDISDPKTLEPAMEGIDALIILTSAIPRMKPTEEFTAEMISGGRSEDVIDASFSGPMPEFYYDEGQYPEQVDWIGQKNQIDTAKKMGVKHIVLVGSMGGCDPDHFLNHMGNGNILIWKRKAEQYLADSGVPYTIIRAGGLDNKAGGVRELLVAKDDVLLPTENGFIARADVAEACVQALEIEEVKNKAFDLGSKPEGVGEATKDFKALFSQVTTPF
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Catalyzes the reduction of benzophenanthridines, preferentially sanguinarine, to the corresponding dihydroalkaloids. Involved in detoxifying the phytoalexins produced by plant itself. The sanguinarine produced by intact cells upon elicitation, after excretion and binding to cell wall elements, is rapidly reabsorbed and reduced to the less toxic dihydrosanguinarine. Can work with both NAD(P) or NAD as a hydrogen donor, but at low concentrations, the reaction velocity with NAD(P)H is threefold higher than with NADH. However, chelerythrine shows maximum conversion rates with NADH. The substrate preference is sanguinarine > chelerythrine > chelirubine, macarpine or 10-OH-chelerythrine. No activity with berberine or phenanthridine cations.
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D5KXD2
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TPS12_SOLLC
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Sesquiterpene synthase 12 (SlTPS12) (Terpene synthase 12) ((E)-beta-ocimene synthase TPS12) (EC 4.2.3.106) ((Z)-gamma-bisabolene synthase TPS12) (EC 4.2.3.-) (Alpha-humulene synthase TPS12) (EC 4.2.3.104) (Beta bisabolene synthase TPS12) (EC 4.2.3.-) (Beta caryophyllene synthase TPS12) (EC 4.2.3.57) (Beta-myrcene synthase TPS12) (EC 4.2.3.15) (Gamma-curcumene synthase TPS12) (EC 4.2.3.-) (Limonene synthase TPS12) (EC 4.2.3.-) (Terpinolene synthase TPS12) (EC 4.2.3.113)
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MASSSANKCRPLANFHPTVWGYHFLSYTHEITNQEKVEVDEYKETIRKMLVEAPEGSEQKLVLIDAMQRLGVAYHFDNEIETSIQNIFDASSKQNDNDNNLYVVSLRFRLVRQQGHYMSSDVFKQFINQDGKFKETLTNDVQGLLSLYEASHLRVRDEEILEEALTFTTTHLESTVSNLSNNNSLKAEVTEAFSQPIRMTLPRVGARKYISIYENNDAHNHLLLKFAKLDFNMLQKLHQRELSDLTRWWKDLDFANKYPYARDRLVECYFWILGVYFEPKYSRARKMMTKVIQMASFFDDTFDAYATFDELEPFNNAIQRWDINAIDSVPPYLRHAYQALLDIYSEMEQALAKEFKSDRVYYAKYEMKKLVRAYFKEAQWLNNDNHIPKYEEHMENAMVSAGYMMGATTCLVGVEEFISKETFEWMINEPLIVRASSLIARAMDDIVGHEVEQQREHGASLIECYMKDYGVSKQEAYVKFQKEVTNGWMDINREFFCPDVEVPKFVLERVLNFTRVINTLYKEKDEYTNSKGKFKNMIISLLVESVEI
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Sesquiterpene synthase involved in the biosynthesis of volatile compounds. Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (1E,4E,8E)-alpha-humulene and (-)-(E)-beta-caryophyllene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into beta-bisabolene, gamma-curcumene and (Z)-gamma-bisabolene. Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene, (E)-beta-ocimene, limonene and terpinolene.
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D5LGE0
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AIP_HYAAS
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Immunoregulatory peptides (Anti-inflammatory peptides) [Cleaved into: Hyalomin-A1; Hyalomin-B1; Hyalomin-B2; Hyalomin-B3]
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MNYLCLVVTLVAVAGAISGEKFSDDNTGYQSTPSLRIRTTPGRRRQTPRTIGPPYTRRTLRTTTDYSTTVENGNLTTPAANSTEKGNGLYGLRRQTPRTIGPPYTRRTLRTTTGYWTTVEKGNGTTPAANSTEKGNRPYGRRRQTPRTIGPPYTRRTTTDYWAAVEKGYLTTPAANSTEKESRPNATQRREISWTFGPLYTWRTTKGYGTTLETTNATSTS
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[Hyalomin-A1]: Suppress host inflammatory response. Exerts significant anti-inflammatory functions, either by directly inhibiting host secretion of inflammatory factors such as tumor necrosis factor-alpha (TNF), monocyte chemotactic protein-1 (CCL2), and interferon-gamma (IFNG) or by indirectly increasing the secretion of immunosuppressant cytokine of interleukin-10 (IL10). Also potently scavenges free radical in vitro in a rapid manner. All tested concentrations of this peptide have little effect on the cell viability. In vivo, inhibits hind paw adjuvant-induced inflammation in mouse in a dose-dependent manner. [Hyalomin-B1]: Suppress host inflammatory response. Exerts significant anti-inflammatory functions, either by directly inhibiting host secretion of inflammatory factors such as tumor necrosis factor-alpha (TNF), monocyte chemotactic protein-1 (CCL2), and interferon-gamma (IFNG) or by indirectly increasing the secretion of immunosuppressant cytokine of interleukin-10 (IL10). Also potently scavenges free radical in vitro in a rapid manner. Low concentrations of this peptide have little effect on the cell viability, whereas high concentrations increase the cell viability by 10-20%. In vivo, inhibits hind paw adjuvant-induced inflammation in mouse in a dose-dependent manner.
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D5MP61
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3XYN1_VIBSX
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Beta-1,3-xylanase XYL4 (EC 3.2.1.32) (Beta-1,3-xylanase)
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MKRTYLSLIAAGVMSLSVSAWSLDGVLVPESGILVSVGQDVDSVNDYASALGTIPAGVTNYVGIVNLDGLNSDADAGAGRNNIAELANAYPTSALVVGVSMNGEVDAVASGRYNANIDTLLNTLAGYDRPVYLRWAYEVDGPWNGHSPSGIVTSFQYVHDRIIALGHQAKISLVWQVASYCPTPGGQLDQWWPGSEYVDWVGLSYFAPQDCNWDRVNEAAQFARSKGKPLFLNESTPQRYQVADLTYSADPAKGTNRQSKTSQQLWDEWFAPYFQFMSDNSDIVKGFTYINADWDSQWRWAAPYNEGYWGDSRVQANALIKSNWQQEIAKGQYINHSETLFETLGYGSTGGGDNGGGDNGGTNPPEPCNEEFGYRYVSDSTIEVFHKNNGWSAEWNYVCLNGLCLQGEIKNGEYVKQFDAQLGSTYGIEFKVADGESQFITDKSVTFENKQCGSTGTPGGGDNGSGGDNGGDNGSGGDNGSGGGTDPSQCSADFGYNYRSDTEIEVFHKDLGWSASWNYICLDDYCVPGDKSGDSYNRSFNATLGSDYKITFKVEDSASQFITEKNITFVNTSCAQ
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Catalyzes the hydrolysis of beta-1,3-xylan into oligosaccharides, mainly xylobiose, xylotriose and xylotetraose. Converts beta-1,3-xylotriose into xylose and xylobiose, converts beta-1,3-xylotetraose mainly into xylotriose and xylose, converts beta-1,3-xylopentaose into xylobiose and xylotriose. Does not hydrolyze beta-1,4-xylan, beta-1,4-mannan, beta-1,4-glucan, beta-1,3-xylobiose or p-nitrophenyl-beta-xyloside.
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D5MTF8
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HGL1D_WHEAT
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4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1d, chloroplastic (EC 3.2.1.182) (Beta-glucosidase 1d) (TaGlu1d) (EC 3.2.1.21)
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MALLAAATLNPTTHLSLRSRAGRNSENLWLRSAASSQKSKGRFCNLTVRAGTPSKPAEPIGPVFTKLKPWQIPKRDWFDKDFLFGASTSAYQIEGAWNEDGKGPSTWDHFCHKYPERISDGTNGDVAADSYHLYEEDVKALKDMGMKVYRFSISWSRILPNGTGEVNQAGIDYYNKLINSLISHDIVPYVTIWHWDTPQALEDKYGGFLDPQIVDDYKQFAKLCFESFGDRVKNWFTFNEPHTYCCFSYGEGIHAPGRCSPGMDCAVPEGDSLREPYTAGHHILLAHAEAVEMFRTHYNMHGDSKIGMAFDVMGYEPYQDSFLDDQARERSIDYNLGWFLEPVVRGDYPFSMRSLIGDRLPVFTKEEQEKLASSCDIMGLNYYTSRFSKHVDISPDVTPKLNTDDAYASSETTGSDGNDIGPITGTYWIYMYPKGLTDLLLIMKEKYGNPPIFITENGIADVDGDETMPDPLDDWKRLDYLQRHISAVKDAIDQGADVRGHFTWGLIDNFEWGSGYSSRFGLVYIDKNDGFKRKLKKSAKWFSKFNAVPKHLLGTTKPTGQAPV
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Acts in defense of young plant parts against pests via the production of hydroxamic acids from hydroxamic acid glucosides. Enzymatic activity is highly correlated with plant growth. The preferred substrate is DIMBOA-beta-D-glucoside.
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D5TM67
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CDAS_BACT1
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Diadenylate cyclase CdaS (DAC) (EC 2.7.7.85) (Cyclic-di-AMP synthase) (c-di-AMP synthase)
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MHEWGLSEELKIQTKQMIEIAEKELSIMRNAIDKEDECILCKMEDIHHMLANVQTLAATYYIQAYLSPYTESSSFITTAIQHLSARKHGALIVVERNETLEALIQTGTTLNAHLTAPLLESIFYPGNPLHDGAVLVKNNHIVSAANILPLTKSTEVDPELGTRHRAAIGLSEKSDALILVVSEETGRTSFALNGILYTISL
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One of 3 paralogous diadenylate cyclases (DAC) in this bacteria catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). It has slow DAC activity with ADP as a substrate and may have weak ADPase activity. Required for efficient spore formation, whereas in B.subtilis, it is required for efficient spore germination. It is produced under the control of different sigma factors in the two bacteria. It is also required for parasporal crystal formation.
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D5VRB9
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ELP3_METIM
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tRNA uridine(34) acetyltransferase (EC 2.3.1.-) (Elongator complex protein 3 homolog) (MinElp3)
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MKEKLMRCIIERILKEYKEGKTLDKKRIEQIKSECLRIYRIGIGHPSNSEILKYATEEEKKILIPILRKKPVRTISGVAVVAVMTSPAKCPHGKCIFCPGGLDSVFGDVPQSYTGREPATMRGLMFNFDPYLQTRARIEQLEKVGHPTDKIELIIMGGTFPAREIEYQDWFIKRCLDAMNERESKSLEEAQKINETAKHRCVALCIETRPDYCSEKEINQMLKLGATRVELGVQSIYNEILKLCKRGHSVEDTIKATQLLKDSGLKVSYHLMPGMPGSSIEMDKKMFKEIFTNPDFMPDMVKIYPCLVIEGTELYEMWKRGEFKPYREEEAIEVISYAKSIMPKWVRTSRIQRDIPATVIVDGVKKSNLGELVYKYMEKKGLRCRCIRCREVGHVYYKKGILPDPEHIKLVREDYEASGGTEIFLSFEDVKNDILIAFLRLRDPYKPFRKEIDDKTMLVRQLHVFGWEKALTRDIKEVSWQHMGYGRMLMKEAERIAKEEFGKKKILVTSGIGVREYYRKLGYKRVGAYMGKEL
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tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L-methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'-dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not show protein lysine acetyltransferase activity.
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D6MZJ6
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NSMA5_MOUSE
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Sphingomyelin phosphodiesterase 5 (EC 3.1.4.12) (Mitochondrial neutral sphingomyelinase) (mtnSMase)
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MSLPDISRRRSPVPQEDWPLTPNALRPSPFPNPVLQALYSLSRVLLFPTYWSLDQLLGCWAPSVRSKSLGWFKVLAGSGVLLPLVVVGLPLALVGLALWLPLQVWRRPFCYQPPPACWVWPQPWHPPAERRRCFVFLTANLCLLPHGLAHFNNLSHSLQRAEAVGAALLDSLQSSQYRVSECSQPPPRVPGGELKATLPMGLDFVCLQEVFDLRAARRLVRVLVPNLGPVIYDVGTFGLMAGPYIKVLGSGLLLASRYPLLRATFRCFPNARREDAMASKGLLSVQAQLGIVDGHPIVGYLHCTHLHAPVEDGHIRCKQLTLLLEWVEEFEAENRQSDEAVAFSVLLGDLNFDNCSQDHAKEQGHKLFSCFQDPCRLGVCQEQPWALGTILNSSMLRHSIACSPEMLRRALRQEKGRRLYLSGPLHGSYPAQSWKGRRLDYITYRRVPGSRLSPEAEQVTFSTAFAGLTDHLAMGLKLQVVCS
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Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide.
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D6PXE8
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VM3B_NAJAT
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Zinc metalloproteinase-disintegrin-like atrase-B (EC 3.4.24.-) (Snake venom metalloproteinase) (SVMP)
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MIQALLVIICLAVFPHQGSSIILESGNVNDYEVVYPQKVPALLKGGVQNPQPETKYEDTMRYEFQVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSPPVQDHCYYHGYIQNEADSSAVISACDGLKGHFEHQGETYFIEPLKISNSEAHAIYKDENVENEDETPEICGVTETTWESDESIEKTSQLTNTPEQDRYLQDKKYIEFYVIVDNRMYRYYNNDKPAIKIRVYEMINAVNTKFRPLKIHIALIGLEIWSNKDKFEVKPAASVTLKSFGEWRETVLLPRKRNDNAQLLTGIDFNGNTVGRAYIGSLCKTNESVAIVQDYNRRISLVASTMTHELGHNLGIHHDKASCICIPGPCIMLKKRTAPAFQFSSCSIREYREYLLRDRPQCILNKPLSTDIVSPPICGNYFVEVGEECDCGSPQACQSACCNAATCQFKGAETECRVAKDDCDLPELCTGQSAECPTDSLQRNGHPCQNNQGYCYNRTCPTLTNQCITLLGPHFTVSPKGCFDLNMRGDDGSFCGMEDGTKIPCAAKDVKCGRLYCTEKNTMSCLIPPNPDGIMAEPGTKCGDGMVCSKGQCVDVQTAY
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Snake venom zinc protease that inhibits the classical and alternative pathways of complement by cleaving factor B, C6, C7, and C8. Also slowly and selectively degrades alpha-chain of fibrinogen (FGA), and shows edema-inducing activity.
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D6R8X8
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HYUP_MICLQ
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Hydantoin permease (MHP) (Hydantoin transport protein) (NCS1 benzyl-hydantoin transporter) (Nucleobase cation symporter 1) (NCS1) (Sodium-coupled secondary active transport protein) (Sodium-hydantoin transporter Mhp1)
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MNSTPIEEARSLLNPSNAPTRYAERSVGPFSLAAIWFAMAIQVAIFIAAGQMTSSFQVWQVIVAIAAGCTIAVILLFFTQSAAIRWGINFTVAARMPFGIRGSLIPITLKALLSLFWFGFQTWLGALALDEITRLLTGFTNLPLWIVIFGAIQVVTTFYGITFIRWMNVFASPVLLAMGVYMVYLMLDGADVSLGEVMSMGGENPGMPFSTAIMIFVGGWIAVVVSIHDIVKECKVDPNASREGQTKADARYATAQWLGMVPASIIFGFIGAASMVLVGEWNPVIAITEVVGGVSIPMAILFQVFVLLATWSTNPAANLLSPAYTLCSTFPRVFTFKTGVIVSAVVGLLMMPWQFAGVLNTFLNLLASALGPLAGIMISDYFLVRRRRISLHDLYRTKGIYTYWRGVNWVALAVYAVALAVSFLTPDLMFVTGLIAALLLHIPAMRWVAKTFPLFSEAESRNEDYLRPIGPVAPADESATANTKEQNQR
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Nucleobase-proton symporter that mediates the sodium-dependent binding and uptake of 5-aryl-substituted hydantoin compounds. 5-indolyl methyl hydantoin and 5-benzyl hydantoin are the preferred substrates, with selectivity for a hydrophobic substituent in position 5 of hydantoin and for the L isomer over the D isomer.
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D6RGH6
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MCIN_HUMAN
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Multicilin (Multiciliate differentiation and DNA synthesis-associated cell cycle protein) (McIdas protein) (Protein Idas)
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MQACGGGAAGRRAFDSICPNRMLALPGRALLCKPGKPERKFAPPRKFFPGCTGGSPVSVYEDPPDAEPTALPALTTIDLQDLADCSSLLGSDAPPGGDLAASQNHSHQTEADFNLQDFRDTVDDLISDSSSMMSPTLASGDFPFSPCDISPFGPCLSPPLDPRALQSPPLRPPDVPPPEQYWKEVADQNQRALGDALVENNQLHVTLTQKQEEIASLKERNVQLKELASRTRHLASVLDKLMITQSRDCGAAAEPFLLKAKAKRSLEELVSAAGQDCAEVDAILREISERCDEALQSRDPKRPRLLPEPANTDTRPGNLHGAFRGLRTDCSRSALNLSHSELEEGGSFSTRIRSHSTIRTLAFPQGNAFTIRTANGGYKFRWVPS
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Transcription regulator specifically required for multiciliate cell differentiation. Acts in a multiprotein complex containing E2F4 and E2F5 that binds and activates genes required for centriole biogenesis. Required for the deuterosome-mediated acentriolar pathway. Plays a role in mitotic cell cycle progression by promoting cell cycle exit. Modulates GMNN activity by reducing its affinity for CDT1.
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D6VTK4
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STE2_YEAST
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Pheromone alpha factor receptor
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MSDAAPSLSNLFYDPTYNPGQSTINYTSIYGNGSTITFDELQGLVNSTVTQAIMFGVRCGAAALTLIVMWMTSRSRKTPIFIINQVSLFLIILHSALYFKYLLSNYSSVTYALTGFPQFISRGDVHVYGATNIIQVLLVASIETSLVFQIKVIFTGDNFKRIGLMLTSISFTLGIATVTMYFVSAVKGMIVTYNDVSATQDKYFNASTILLASSINFMSFVLVVKLILAIRSRRFLGLKQFDSFHILLIMSCQSLLVPSIIFILAYSLKPNQGTDVLTTVATLLAVLSLPLSSMWATAANNASKTNTITSDFTTSTDRFYPGTLSSFQTDSINNDAKSSLRSRLYDLYPRRKETTSDKHSERTFVSETADDIEKNQFYQLPTPTSSKNTRIGPFADASYKEGEVEPVDMYTPDTAADEEARKFWTEDNNNL
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Fungal class D1 G-protein-coupled receptor that acts as an alpha-factor pheromone receptor performing pheromone-dependent signal transduction involved in cellular conjugation, mating projection assembly, and in cell fusion. Following alpha-factor-binding, the signal is transmitted via a tripartite G protein consisting of alpha-, beta- and gamma-subunits (GAP1, STE4 and STE8 respectively) that prepares the cell for conjugation. In the inactive state, the cytoplasmic end of transmembrane domain 7 (TMD7) is unstructured and packs between TMD1-6, blocking the G protein coupling site. Agonist binding results in the outward movement of the extracellular ends of TMD6 and TMD7 by 6 Angstroms. On the intracellular surface, the G protein coupling site is formed by a 20 Angstroms outward movement of the unstructured region in TMD7 that unblocks the site, and a 12 Angstroms inward movement of TMD6.
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D6WMX4
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PINK1_TRICA
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Serine/threonine-protein kinase Pink1, mitochondrial (EC 2.7.11.1) (PTEN-induced putative kinase 1)
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MSVRAVGSRLFKHGRSLIQQFCKRDLNTTIGDKINAVSQATAAPSSLPKTQIPKNFALRNVGVQLGLQARRILIDNVLNRVTNSLSAELRKKATRRILFGDSAPFFALVGVSIASGTGILTKEEELEGVCWEIREAISKIKWQYYDIDESRFESNPITLNDLSLGKPIAKGTNGVVYSAKVKDDETDDNKYPFALKMMFNYDIQSNSMEILKAMYRETVPARMYYSNHDLNNWEIELANRRKHLPPHPNIVAIFSVFTDLIQELEGSKDLYPAALPPRLHPEGEGRNMSLFLLMKRYDCNLQSFLSTAPSTRTSLLLLAQLLEGVAHMTAHGIAHRDLKSDNLLLDTSEPESPILVISDFGCCLADKTNGLSLPYTSYEMDKGGNTALMAPEIICQKPGTFSVLNYSKADLWAVGAIAYEIFNCHNPFYGPSRLKNFNYKEGDLPKLPDEVPTVIQALVANLLKRNPNKRLDPEVAANVCQLFLWAPSTWLKPGLKVPTSGEILQWLLSLTTKVLCEGKINNKSFGEKFTRNWRRTYPEYLLISSFLCRAKLANVRNALHWIQENLPELD
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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.
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D6XZ22
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GGP_BACIE
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1,2-alpha-glucosylglycerol phosphorylase (EC 2.4.1.332) (2-O-alpha-glucosylglycerol phosphorylase) (GGP)
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MHEIGEHLTTNTGWDIIKNRYEAAQAITEGSNFMIGNGFMGYRGTFAEDGKDAYAACIVTDTWDKADGKWEELSTVPNALLTLLHVDGEPFIMSEEAASFERTLDLSQGVTSRKVSQRMKNGATITIHEEKFASYRKKHAVLMKYTVESDQDTDAVLDTGIDYDVWSINGDHLQGHHYFSHPTGDGVTAKTVSYEDTVTVVETCSLDADASEEDYQNPDGSGRTFSLSLEAGKPVTLEKAMIIYSSNDVDNPQDEALLEAKHMQSYEEEKAANRLEWDNLWSHYDVTIQNNIIDQVALRFNIYHAIIATPVHKSLPIGARGLSCQAYQGAAFWDQEIYNMPMYLYSNPEIARNILKYRHRTLDGARRKAKRLGYEGAYYAWISGKTGDELCPDFFFKDVLSGRDIRNHFNDWQIHISPDIAYAVKKYHQVTGDDAFIRDYGAEMIFEIARFLASHAVYKPMRGRYEFMRVQGPDEYHENVDNNAFTNHQAMFTLQAADELLQTLDEKTLSAVKEKIGLSDDEISLWRDMLANTYVPKPDKHGIIEQFDGYYDLETIIPAKKVTERLIKEDEYYGYPNGVTVRTQCIKQADVIQLFVLHPHLYDRKTVELNYEFYEPRTLHFSSLSPSSYAIVAAQIDKVEEAYRNFRKSVMIDLLNTNEAVSGGTFIGGIHTAANGASWQMVVNGFGGLSVHGDDIHLSPRLPDAWDGYTFKAIVKGQTLEVDVTKEQITITNKSEDRKPLTLHIFGEKSVLDSERITKSR
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Catalyzes both the (1) reversible phosphorolysis of 2-O-alpha-D-glucopyranosyl-sn-glycerol (GG) from beta-D-glucose 1-phosphate (betaGlc1P) and glycerol and (2) the hydrolysis of betaGlc1P. the betaGlc1P hydrolysis is a glucosyl-transfer reaction to an acceptor water molecule that produces an anomer-inverted alpha-glucose, not a phosphatase-type reaction. In the absence of glycerol produces alpha-D-glucopyranose and phosphate from beta-D-glucopyranose 1-phosphate.
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D7A5Q8
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YDDG_STAND
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Aromatic amino acid exporter YddG
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MSRSSATLIGFTAILLWSTLALATSSTGAVPPFLLTALTFTIGGAVGIAAGLARGVGLSVLRQPWPVWVHGIGGLFGYHFFYFSALKLAPPAEAGLVAYLWPLLIVLFSAFLPGERLRPAHVAGALMGLAGTVVLLGARAGGFGFAPEYVPGYLAAAACAVIWSVYSVASRRFARVPTEVVAGFCLATAALSALCHILFEPSVWPVGSEWLAVVALGIGPVGIAFYTWDIGMKRGDVRLLGVLSYAAPVLSTLLLVVAGFAAPSGALAIACALIVGGAAVATLLARR
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Amino acid transporter with broad substrate specificity. Can transport various amino acids, including L-threonine, L-methionine, L-lysine and L-glutamate.
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D7A6E5
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SOXA_STAND
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L-cysteine S-thiosulfotransferase subunit SoxA (EC 2.8.5.2) (Cytochrome c551 subunit monoheme) (Protein SoxA) (SoxAX cytochrome complex subunit A) (Sulfur oxidizing protein A) (Thiosulfate-oxidizing multienzyme system protein SoxA) (TOMES protein SoxA)
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MRRFAAGCLALALLVLPFVLTGARAAEDESEKEIERYRQMIEDPMANPGFLNVDRGEVLWSEPRGTRNVSLETCDLGEGPGKLEGAYAHLPRYFADTGKVMDLEQRLLWCMETIQGRDTKPLVAKPFSGPGRTSDMEDLVAFIANKSDGVKIKVALATPQEKEMYAIGEALFFRRSSINDFSCSTCHGAAGKRIRLQALPQLDVPGKDAQLTMATWPTYRVSQSALRTMQHRMWDCYRQMRMPAPDYASEAVTALTLYLTKQAEGGELKVPSIKR
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C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.
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D7EZN2
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LIPR2_PIG
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Pancreatic lipase-related protein 2 (PL-RP2) (Cytotoxic T lymphocyte lipase) (Galactolipase) (EC 3.1.1.26) (Triacylglycerol lipase) (EC 3.1.1.3)
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MLPSWTIGLLLLATVRGKEICYQPFGCFSDETPWARTCHWPFKLFPWAPKDIDTHFLLYTNENPNNFQLINITNLDTIEASNFQLDRKTRFIIHGFIDKGEDSWPSEMCKKMFKVEKVNCICVDWRRGALTRYTQAVHNTRVVGAEIAFLIQGLSTKFDYNPENVHLIGHSLGAHTAAEAGRRLGGHVGRLTGLDPAQPCFQNTPEEVRLDPSDAMFVDVIHTDSAPFIPFLGFGMSQKVGHLDFYPNGGKEMPGCQKNTLSTIVDVDGIWEGIEDFAACNHLRSYKYYSSSIFSPDGFLGYPCASYDEFQEEENKCFPCPAEGCPKMGHYADQFQGKTSAVGQTFFLNTGDSGNFTRWRYRVSVTLAGKRNVHGYIRIALYGSNANSKQYNIFKGSLQPNARYTHDIDVDLNVGKVQKVKFLWYNHIIDLFHPELGASQVMVQSGEDKTEHKFCGSDTVRENILQTLNPC
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Lipase that primarily hydrolyzes triglycerides and galactosylglycerides. In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides. Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional specificity. Can completely deacylate triacylglycerols (By similarity). When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase (By similarity). Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based diet, releasing long-chain polyunsaturated fatty acids (By similarity). Hydrolyzes medium- and long-chain fatty acyls in galactolipids. May act together with LIPF to hydrolyze partially digested triglycerides (By similarity). Hydrolyzes long-chain monoglycerides with high efficiency (By similarity). In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity (By similarity). Also has low phospholipase activity. In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids (By similarity). The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity).
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D7PC76
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S26A5_TURTR
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Prestin (Solute carrier family 26 member 5)
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MDHVEETEILAATQRYYVERPIFSHPVLQERLHKKDKISESIGDKLKQAFTCTPKKIRNIIYMFLPITKWLPAYRFKEYVLGDIVSGISTGVLQLPQGLAFAMLAAVPPVFGLYSSFYPVIMYCFFGTSRHISIGPFAVISLMIGGVAVRLVPDDIVIPGGVNATNSTEARDALRVKVAMSVTLLTGIIQFCLGVCRFGFVAIYLTEPLVRGFTTAAAVHVFTSMLKYLFGVKTKRYSGIFSVVYSTVAVLQNVKNLNVCSLGVGLMVFGLLLGGKEFNERFKEKLPAPIPLEFFAVVMGTGISAGFSLHESYNVDVVGTLPLGLLPPANPDTSLFHLVYVDAIAIAIVGFSVTISMAKTLANKHGYQVDGNQELIALGLCNSTGSLFQTFAISCSLSRSLVQEGTGGKTQLAGCLASLMILLVILATGFLFESLPQAVLSAIVIVNLKGMFMQFSDLPFFWRTSKIELTIWLTTFVSSLFLGLDYGLITAVIIALMTVIYRTQSPSYIVLGQLPDTDVYIDIDAYEEVKEVPGIKIFQINAPIYYANSDLYSSALKRKTGVNPAFILGARRKAMKKYAKEVGNANMANATVVKVDAEVDAEDGTKPEEEEDEIKYPPIVTKSTLPEELQRFMPPGDNVHTIILDFTQVNFMDSVGVKTLAGIVKEYGDVGIYVYLAGCSAQVVSDLTQNQFFENPALLDLLFHSIHDAVLGSQVREALAEQEATAAPPQEDSEPNATPEA
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Voltage-sensitive motor protein that drives outer hair cell (OHC) electromotility (eM) and participates in sound amplification in the hearing organ. Converts changes in the transmembrane electric potential into mechanical displacements resulting in the coupling of its expansion to movement of a charged voltage sensor across the lipid membrane. The nature of the voltage sensor is not completely clear, and two models compete (By similarity). In the first model, acts as an incomplete transporter where intracellular chloride anion acts as extrinsic voltage sensor that drives conformational change in the protein which is sufficient to produce a length change in the plane of the membrane and hence in the length of the OHC (By similarity). The second model in which multiple charged amino acid residues are distributed at the intracellular and extracellular membrane interfaces that form an intrinsic voltage sensor, whose movement produces the non-linear capacitance (NLC) (By similarity). However, the effective voltage sensor may be the result of a hybrid voltage sensor assembled from intrinsic charge (charged residues) and extrinsic charge (bound anion). Notably, binding of anions to the anion-binding pocket partially neutralizes the intrinsic positive charge rather than to form an electrically negative sensor, therefore remaining charge may serve as voltage sensor that, after depolarization, moves from down (expanded state) to up (contracted) conformation, which is accompanied by an eccentric contraction of the intermembrane cross-sectional area of the protein as well as a major increase in the hydrophobic thickness of the protein having as consequences the plasma membrane thickening and the cell contraction after membrane depolarization. The anion-binding pocket transits from the inward-open (Down) state, where it is exposed toward the intracellular solvent in the absence of anion, to the occluded (Up) state upon anion binding (By similarity). Salicylate competes for the anion-binding site and inhibits the voltage-sensor movement, and therefore inhibits the charge transfer and electromotility by displacing Cl(-) from the anion-binding site and by preventing the structural transitions to the contracted state. In addition, can act as a weak Cl(-)/HCO3 (-) antiporter across the cell membrane and so regulate the intracellular pH of the outer hair cells (OHCs), while firstly found as being unable to mediate electrogenic anion transport (By similarity). Moreover, supports a role in cardiac mechanical amplification serving as an elastic element to enhance the actomyosin- based sarcomere contraction system (By similarity).
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D7PDD4
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G6B_MOUSE
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Megakaryocyte and platelet inhibitory receptor G6b (ITIM-receptor G6b-B) (Immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing platelet receptor)
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MALVLPLLPLLLSKVQGNPEVSLEGSPGDRVNLSCIGVSDPTRWAWAPSFPACKGLSKGRRPILWASTRGTPTVLQHFSGRLRSLDNGIKRLELLLSAGDSGTFFCKGRHENESRTVLQVLGDKAGCRPAGSTHGYEYPKVLIPLLGVGLVLGLGVAGVVWRRRRLSPPPPPPPPPGPLPTFAPVINAEPQRPLEQESKISGHLDQEPSLHYADLDHSVLGRHRRMSTVVSGDASTVYAVVV
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Inhibitory receptor that acts as a critical regulator of hematopoietic lineage differentiation, megakaryocyte function and platelet production. Inhibits platelet aggregation and activation by agonists such as ADP and collagen-related peptide (By similarity). This regulation of megakaryocate function as well as platelet production ann activation is done through the inhibition (via the 2 ITIM motifs) of the receptors CLEC1B and GP6:FcRgamma signaling. Appears to operate in a calcium-independent manner (By similarity).
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D7PF45
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SHIP2_PIG
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Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (Protein 51C) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2)
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MASACGAPGPGAGPGAALGSPAPAWYHRDLSRAAAEELLARAGRDGSFLVRDSESVAGAFALCVLYQKHVHTYRILPDGEDFLAVQTSQGVPVRRFQTLGELIGLYAQPNQGLVCALLLPVERERELDPPDERDASDGEDEKPPLPPRSGTSVSAPLGPSSPPAAPEPPTPAVESAPNGLSTVSHEYLKGSYGLDLEAVRGGASNLPHLTRTLAASCRRLHSEVDKVLSGLEILSKVFDQQSSPMVTRLLQQQNPPQTGEQELESLVLKLSVLKDFLSGIQKKALKALQDMSSTAPPAPVQPSTRKAKTIPVQAFEVKLDVTLGDLTKIGKSQKFTLSVDVEGGRLVLLRRQRDSQEDWTTFTHDRIRQLIKSQRVQNKLGVVFEKEKERTQRKDFIFVSARKREAFCQLLQLMKNKHSKQDEPDMISVFIGTWNMGSVPPPRNVTSWFTSKGLGKTLDEVTVTIPHDIYVFGTQENSVGDREWLDLLRGGLKELTDLDYRPIAMQSLWNIKVAVLVKPEHENRISHVSTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLTSGNEKTARRNQNYLDILRLLSLGDRQLGAFDISLRFTHLFWFGDLNYRLDMDIQEILNYISRKEFEPLLRVDQLNLEREKHKVFLRFSEEEISFPPTYRYERGSRDTYAWHKQKPTGVRTNVPSWCDRILWKSHPETHIICNSYGCTDDIVTSDHSPVFGTFEVGVTSQFISKKGLSKTADQAYIEFESIEAIVKTASRTKFFIEFYSTCLEEYKKSFENDAQSSDNVNFLKVQWSSRQLPTLKPILDIEYLQDQHLLLTVKSMDGYESYGECVVALKSMIGSTAQQFLTFLSHRGEETGNIRGSMKVRVPTERLGTRERLYEWISIDKDEAGAKSKAPSVSRGSQEPRSGSRKPAPAEASCPLSKLFEEPEKPPPTGRPPAPPRAAPREEPLTPRLKPEGAPEPEGVAAPPPKNSFNNPAYYVLEGVPHQLLPPEPPSPARAPVPPATKNKVAITVPAPQLGRHRPPRVGEGSSSDEESGGTLPPPDFPPPPLPDSAIFLPPSREPLPGPGVRGRSGGEARALPPPKAHPRPPLPPGPLPPGTFLGEAAGGDDRSCSVLQVAKKLSEVDSAPPGPGRCLLLPGPLELQPARALPSDYGRPLSFPPPRIRESVQEDLAEEAPCPQAGRTGGLGEAGMGAWLRAIGLERYEEGLVHNGWDDLEFLSDITEEDLEEAGVQDPAHKRLLLDTLQLSK
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Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Required for correct mitotic spindle orientation and therefore progression of mitosis (By similarity). Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear (By similarity). While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking (By similarity). Confers resistance to dietary obesity (By similarity). May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane (By similarity). Part of a signaling pathway that regulates actin cytoskeleton remodeling (By similarity). Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation (By similarity). Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling (By similarity). Regulates cell adhesion and cell spreading (By similarity). Required for HGF-mediated lamellipodium formation, cell scattering and spreading (By similarity). Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation (By similarity). Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth (By similarity). Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A) (By similarity). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems (By similarity). Involved in EGF signaling pathway (By similarity). Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3 (By similarity). Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity (By similarity). Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1 (By similarity). In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling (By similarity). Plays a role in the localization of AURKA and NEDD9/HEF1 to the basolateral membrane at interphase in polarized cysts, thereby mediates cell cycle homeostasis, cell polarization and cilia assembly (By similarity). Additionally promotion of cilia growth is also facilitated by hydrolysis of (PtdIns(3,4,5)P3) to PtdIns(3,4)P2 (By similarity). Promotes formation of apical membrane-initiation sites during the initial stages of lumen formation via Rho family-induced actin filament organization and CTNNB1 localization to cell-cell contacts (By similarity). May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification (By similarity).
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D7RF80
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POLG_KFDV
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Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
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MAKGAVLKGKGGGPPRRVPKETAKKTRQGPGRLPNGLVLMRMMGVLWHMVAGTARNPILKRFWATVPVRQAIAALRKIRKTVGLLLDSLNKRRGKRRSTTGLLTPILLACLATLVFSATVRRERTGNMVIRAEGKDAATQVEVMNGTCTILATDMGSWCDDSIMYECVTIDSGEEPVDVDCFCKGVERVSLEYGRCGKPAGGRNRRSVSIPVHAHSDLTGRGHKWLKGDSVKTHLTRVEGWVWKNKFLTAAFCAVVWMVTDSLPTRFIVITVALCLAPTYATRCTHLQNRDFVSGTQGTTRVSLVLELGGCVTLTAEGKPSVDVWLDDIHQENPAKTREYCLHAKLANSKVAARCPAMGPATLPEEHQASTVCRRDQSDRGWGNHCGLFGKGSIVACAKFSCEAKKKATGYVYDVNKITYVVKVEPHTGDYLAANESHSNRKTASFTTQSEKTILTLGDYGDISLTCRVTSGVDPAQTVVLELDKTAEHLPKAWQVHRDWFEDLSLPWRHGGAQEWNHADRLVEFGEPHAVKMDIFNLGDQTGILLKSLAGVPVANIEGSKYHLQSGHVTCDVGLEKLKMKGMTYTVCEGSKFAWKRPPTDSGHDTVVMEVTYTGSKPCRIPVRAVAHGEPNVNVASLITPNPSMETTGGGFVELQLPPGDNIIYVGELSHQWFQKGSTIGRVLEKTRRGIERLTVVGEHAWDFGSVGGMLSSVGKALHTAFGAAFNTIFGGVGFLPRILLGVALAWLGLNSRNPTLSVGFLITGGLVLTMTLGVGADMGCAIDANRMELRCGEGLVVWREVTDWYDGYAFHPESPSVLAASLKEAYEEGICGIVPQNRLEMAMWRRVEAVLNLALAESDANLTVVVDKRDPSDYRGGKVGTLRRSGKEMKTSWKGWSQSFVWSVPEAPRRFMVGVEGAGECPLDKRRTGVFTVAEFGMGMRTKVFLDLRETASSDCDTGVMGAAVKSGHAVHTDQSLWMRSHRNATGVFISELIVTDLRNCTWPASHTLDNAGVVDSKLFLPAGLAGPRSHYNHIPGYAEQVKGPWSQTPLRVVREPCPGTAVKIDQSCDKRGASLRSTTESGKAIPEWCCRTCELPPVTFRSGTDCWYAMEIRPVHQQGGLVRSMVLADNGAMLSEGGVPGIVAVFVVLELVIRRRPTTGSSVVWCGMVVLGLVVTGLVTIEGLCRYVVAVGILMSMELGPEIVALVLLQAVFDMRTGLLVAFAVKRAYTTREAVATYFLLLVLELGFPEASLSNIWKWADSLAMGALILQACGQEGRTRVGYLLAAMMTQKDMVIIHTGLTIFLSAATAMAVWSMIKGQRDQKGLSWATPLAGLLGGEGVGLRLLAFRKLAERRNRRSFSEPLTVVGVMLTVASGMVRHTSQEALCALVAGAFLLLMMVLGTRKMQLTAEWCGEVEWNPDLVNEGGEVNLKVRQDAMGNLHLTEVEKEERAMALWLLAGLVASAFHWAGILIVLAVWTLFEMLGSGRRSELVFSGQETRTERNRPFEIKDGAYRIYSPGLLWGHRQIGVGYGAKGVLHTMWHVTRGAALVVDEAISGPYWADVREDVVCYGGAWSLESRWRGETVQVHAFPPGRPQETHQCQPGELILENGRKLGAVPIDLSKGTSGSPIINAQGEVVGLYGNGLKTNEAYVSSIAQGEAEKSRPEIPLSVQGTGWMSKGQITVLDMHPGSGKTHRVLPELVRQCADRGMRTLVLAPTRVVLKEMERALAGKKVRFHSPAVEGQTTAGAIVDVMCHATYVHRRLLPQGRQNWEVAIMDEAHWTDPHSIAARGHLYSLAKENRCALVLMTATPPGRGDPFPESNGAIMSEERAIPDGEWREGFDWITEYEGRTAWFVPSISKGGAVARTLRQRGKSVICLNSKTFEKDYLRVREEKPDFVVTTDISEMGANLDVSRVIDGRTNIKPEEVDGKVELTGTRKVTTASAAQRRGRVGRTSGRTDEYIYSGQCDDDDTSLVQWKEAQILLDNITTLRGPVATFYGPEQVKMPEVAGHYRLNEEKRKHFRHLMTQCDFTPWLAWHVATNTSNVLDRSWTWQGPEENAIDGADGDLVRFKTPGGSERVLQPVWKDCRMFREGRDVKDFILYASGRRSVGDVLGGLAGVPGLLRHRCASALDVVYTLLNENPGSRAMRMAERDAPEAFLTIVEVAVLGVATLGILWCFVARASVSRMFLGTVVLFAALFLLWIGGVDYGHMAGIALIFYTLLTVLQPEPGKQRSSDDNRLAYFLLGLFSLAGLVTANEMGMLDKTKADLAGLVWRGEQRHPAWEEWTNVDIQPARSWGTYVLIVSLFTPYMLHQLQTKIQQLVNSSVASGAQAMRDLGGGTPFFGVAGHVIALGVTSLVGATPMSLGLGVALAAFHLAIVASGLEAELTQRAHRVFFSAMVKNPMVDGDVINPFPDGETKPALYERRMSLILAIALCMGSVVLNRTAASMTEAGAVGLAALGQLVHPETETLWTMPMACGMAGLVRGSFWGLLPMGHRLWLRTTGTRRGGAEGETLGDIWKRRLNGCSREEFFQYRRSGVMETERDKARELLKRGETNMGLAVSRGTAKLAWLEERGYATLKGEVVDLGCGRGGWSYYAASRPAVMGVKAYTIGGKGHEVPRLITSLGWNLIKFRTGMDVYSLEAHRADTILCDIGESSPDPLAEGERSRRVILLMEKWKLRNPDASCVFKVLAPYRPEVLEALHRFQLQWGGGLVRVPFSRNSTHEMYFSTAISGNIINSVNTQSRKLLARFGDQRGPTKVPEVDLGTGTRCVVLAEDKVREADVAERIAALKTQYGDSWHVDKEHPYRTWQYWGSYKTEATGSAASLINGVVKLLSWPWNAREDVVRMAMTDTTAFGQQRVFKEKVDTKAQEPQVGTKIIMRAVNDWIFERLAGKKTPRLCTREEFIAKVRSNAALGAWSDEQNRWPNAREAVEDPEFWRLVDEERERHLGGRCAQCVYNMMGKREKKLGEFGVAKGSRAIWYMWLGSRYLEFEALGFLNEDHWASRDLSGAGVEGTSLNYLGWHLKKLSELEGGLFYADDTAGWDTRITNADLEDEEQILRYLEGEHRTLAKTILEKAYHAKVVKVARPSSSGGCVMDIITRRDQRGSGQVVTYALNTLTNIKVQLIRMMEGEGVIGPSDSQDPRLLRVEAWLKEHGEERLTRMLVSGDDCVVRPIDDRFGKALYFLNDMAKVRKDIGEWEPSEGYSSWEEVPFCSHHFHELTMKDGRVIIVPCRDQDELVGRARVSPGCGWSVRETACLSKAYGQMWLLSYFHRRDLRTLGLAICSAVPIDWVPQGRTTWSIHASGAWMTTEDMLEVWNRVWILDNPFMGDKGKVREWRDIPYLPKSQDGLCSSLVGRRERAEWAKNIWGSVEKVRRMIGPERYADYLSCMDRHELHWDLKLESNII
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[Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway.
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D7SFH9
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LRL26_ARATH
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Protein SUPPRESSOR OF NPR1-1 CONSTITUTIVE 4 [Includes: Glycerophosphodiester phosphodiesterase protein kinase domain-containing GDPDL2 (EC 3.1.4.46) (Glycerophosphodiester phosphodiesterase-like 2) (ATGDPDL2); LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-like 2.6 (EC 2.7.11.1) (Probable receptor-like serine/threonine-protein kinase LRK10L-2.6)]
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MNSQQSTRTKQMLQQSSTHLLCGVVLLQLFAAQVDAQRSTSPWQTLSGDAPLVIARGGFSGLFPDSSLAAYQFAMVVSVADVVLWCDVQLTKDGHGICFPDLNLANASNSEEVYPNRQKSYPVNGVTTKGWFPIDFSLTELQKVLFSLIRGILSRSGKFDENGYSISTVQNVATQMKPALFWLNVQHDEFYEQHNLSMSSFLLSTSRTVSIDFISSPEVNFFRKIAGGFGNNGPSFVFQFMGKEDFEPTTNRTYGSILSNLSFVKTFASGILVPKSYILPLDDKQYLLPHTSLVQDAHKAGLKLYASGFANDVDIAYNYSWDPVSEYLSFVDNGNFSVDGMLSDFPLTASASVDCFSHIGRNATKQVDFLVISKNGASGEYPGCTKLAYEKAIKDGSDVIDCPVQMSSDGIPFCSSSIDLVNSTTVGQTHLRNRSIIVPEISSVAGIFTFSLTWHEIQSLTPAISNPFRENGMSRNPNERNSGNLISLYEFLNLAKNSTSLSGILISLENVVYLREKKGLDVVKVVLNRLTETGYIVGTLKVMIQSTTRLVLVDFKNQSTYKTVYKIKETIGNITDSAIEDIKKFANAVVINKASVFPNSDSFLTGQTTNVLERLQKFQLPVYVELFQNEFVSQPFDFFADETVEINAYIFGAGINGTITEFPYTAARYKRNRCLGREEVPPYMLPVNPGGVLTLISTSSLPPAQDPNPIFTHDDVTEPPLPPVIAKSPTSTLGTPSTIAKPLRNFLKVIRIVSWSVAGVVLFLVLLTLVFCFHRKRETRLRQQKLKALIPLEHYTYAQVKRITKSFAEVVGRGGFGIVYKGTLSDGRVVAVKVLKDTKGNGEDFINEVATMSRTSHLNIVSLLGFCSEGSKRAIIYEFLENGSLDKFILGKTSVNMDWTALYRIALGVAHGLEYLHHSCKTRIVHFDIKPQNVLLDDSFCPKVSDFGLAKLCEKKESILSMLDTRGTIGYIAPEMISRVYGNVSHKSDVYSYGMLVLEIIGARNKEKANQACASNTSSMYFPEWVYRDLESCKSGRHIEDGINSEEDELAKKMTLVGLWCIQPSPVDRPAMNRVVEMMEGSLEALEVPPRPVLQQIPISNLHESSILSEDVSVYTEG
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Atypical receptor-like kinase involved in disease resistance.
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D7SSD8
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MJE1_VITVI
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Methyl jasmonate esterase 1 (VvMJE1) (EC 3.1.1.-) (Methyl esterase 5) (VvMES5) (Salicylic acid-binding protein 2-4)
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MEKRERHFVLVHGACHGAWCWYKVTTFLRSAGHKVTALDLAAAGANGKRLDELNSISDYHEPLMKFMTSLVAGEKVILVAHSLGGVSVSVAMERFPQKISVAVFVSAYMPGPDFNLSTVYQELHQRRQGASKDTQYTFDRGSNNPPTSIIFSPEDLAAKLYQLSPPEDLTLATTLMRPTKLFRGENLLKETTVTREKYGTVRRVYIVCDKDNILKEDFQRWMIKNNPSDEVKVIMGSDHMPMFSKPLDLCAYLQEIVESYS
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Methylesterase that catalyzes the hydrolysis of methyl jasmonate (MeJA) into jasmonate (JA). Can also use methyl salicylate (MeSA) as substrate with a lower efficiency.
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D7UQM5
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AURK_PATPE
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Aurora kinase (EC 2.7.11.1) (ApAurora)
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MTPTGPSHHSMAPKRVLPAASQSNMYGNIRSASTTSTTASTSSQALRLLQNAKTSKNADNRIAHAERQGPPSAHPAAMQKPAARVAPSNENRPDPAARQHQHQQQLQQQKATGHDRVLKESQAGNSTTTTMTSTQSKEANKWSLANFDIGRPLGKGKFGNVYLAREKKSKFIVALKVLFKSQLQKAKVEHQLRREIEIQSHLRHDHILRLYGYFYDDTRVYLILEYAARGELYKEMQAQKAGHFDEDRSAVYIYQLAKALLYCHEKKVIHRDIKPENLLLDLKGDLKIADFGWSVHAPSSRRATLCGTLDYLPPEMIEGKTHDEKVDLWSLGVLCYEFLVGKPPFESQGNTETYRKITKVEFTFPKHVSEGARDLICKLLKHNPSHRLSLEGVIAHAWIQEKISQRS
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Serine/threonine protein kinase that contributes to the regulation of cell cycle progression. Involved in meiotic apparatus formation and polar body extrusion. Contributes to Plk1 activation and phosphorylation of histone H3 at 'Ser-10' during meiosis I. Required for accurate progression of early embryonic M phase. Involved in chromosome alignment and cleavage furrow formation during early embryonic cycles. May be involved in mitotic spindle formation and cytokinesis.
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D7URM0
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LCDH_PSESP
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L-carnitine dehydrogenase (CDH) (L-CDH) (EC 1.1.1.108)
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MPFITHIKTFAALGSGVIGSGWVARALAHGLDVIAWDPAPGAEQALRQRVANAWPALEKQGLAAGAAQHRLSFVSSIEECVRDADFIQESAPERLDLKLDLHAKISAAAKPDAIIASSTSGLLPSEFYESSSHPERCVVGHPFNPVYLLPLVEIVGGRHTAPEAIEAAKGIYTELGMRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMGTFLTYTLAGGDAGMRHFMQQFGPALKLPWTYLPAPELTERLIDEVVDGTAAQVGERSIAELERYRDDTLLAVLEAIGTSKAKHGMTFSE
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Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3-dehydrocarnitine. Is specific for L-carnitine and NAD(+) as substrates since D-carnitine, other carnitine analogs such as choline and betaine, and NADP(+) are not substrates. Despite a high similarity to 3-hydroxyacyl-CoA dehydrogenases, cannot dehydrogenate 3-hydroxybutylate and 3-hydroxybutyl-CoA. Is probably involved in a L-carnitine degradation pathway that allows Xanthomonas translucens to grow on L-carnitine as the sole source of carbon and nitrogen.
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D7Y2H2
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CDNC_ECOM1
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Cyclic AMP-AMP-AMP synthase (EC 2.7.7.-) (CD-NTase018) (c-di-AMP synthase) (EC 2.7.7.85)
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MSTEHVDHKTIARFAEDKVNLPKVKADDFREQAKRLQNKLEGYLSDHPDFSLKRMIPSGSLAKGTALRSLNDIDVAVYISGSDAPQDLRGLLDYLADRLRKAFPNFSPDQVKPQTYSVTVSFRGSGLDVDIVPVLYSGLPDWRGHLISQEDGSFLETSIPLHLDFIKARKRAAPKHFAQVVRLAKYWARLMKQERPNFRFKSFMIELILAKLLDNGVDFSNYPEALQAFFSYLVSTELRERIVFEDNYPASKIGTLSDLVQIIDPVNPVNNVARLYTQSNVDAIIDAAMDAGDAIDAAFYAPTKQLTVTYWQKVFGSSFQG
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CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type III-C(AAA) CBASS system. Cyclic nucleotide synthase that upon activation catalyzes the synthesis of 3',3',3'-cyclic AMP-AMP-AMP (3',3',3'-c-tri-AMP or cAAA) as the major product, and 3',3'-c-di-AMP as a minor product. Cannot use GTP as a substrate. Protects E.coli strain JP313 against bacteriophage lambda cI- infection. When the cdnC-cap7-cap6-nucC operon is transformed into a susceptible strain it confers bacteriophage immunity. Mutations in the sensor (Cap7 also called HORMA) or effector proteins (CdnC, NucC) but not the disassembly protein (Cap6 also called Trip13) no longer confer immunity. The presence of the intact operon leads to culture collapse and cell death, which occurs before the phage has finished its replication cycle, thus protecting non-infected bacteria by aborting the phage infection and preventing its propagation.
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D7Y2H5
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NUCC_ECOM1
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Endodeoxyribonuclease NucC (EC 3.1.-.-) (NucC nuclease)
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MSDWSLSQLFASLHEDIQLRLGTARKAFQHPGAKGDASEGVWIEMLDTYLPKRYQAANAFVVDSLGNFSDQIDVVVFDRQYSPFIFKFNEQIIVPAESVYAVFEAKQSASADLVAYAQRKVASVRRLHRTSLPIPHAGGTYPAKPLIPILGGLLTFESDWSPALGMSFDKALNGDLSDGRLDMGCVASHGHFYFNNIDSKFNFEHGNKPATAFLFRLIAQLQFSGTVPMIDIDAYGKWLAN
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CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type III-C(AAA) CBASS system. A cyclic nucleotide-activated dsDNase. In the presence of 3',3',3'-cyclic AMP-AMP-AMP (cAAA), and to a lesser extent 3',3',3'-cyclic AMP-AMP-GMP (cAAG) and cyclic-di-AMP (c-di-AMP), endonucleolytically degrades dsDNA. Binds one cAAA in a pocket on one surface of the trimer cAAA binding promotes hexamerization, which is necessary for nuclease activation. Also binds c-diAMP or linear di-AMP with lower affinity. The nuclease digests dsDNA to about 50 bp lengths with a 2-base 3' overhang and a consensus recognition site of 5'-Axx|T-3'. DNA has been modeled to contact a pair of juxtaposed active sites (one from each layer of the hexamer), accounting for cleavage on both strands and the 2-base overhang. Protects E.coli strain JP313 against bacteriophage lambda cI- infection. When the cdnC-cap7-cap6-nucC operon is transformed into a susceptible strain it confers bacteriophage immunity. Mutations in the sensor (Cap7 also called HORMA) or effector proteins (CdnC, NucC) but not the disassembly protein (Cap6 also called Trip13) no longer confer immunity. The presence of the intact operon leads to culture collapse and cell death which occurs before the phage has finished its replication cycle, thus protecting non-infected bacteria by aborting the phage infection and preventing its propagation.
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D8QTR2
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MGH1_SELML
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Mannosylglycerate hydrolase MGH1 (EC 3.2.1.170)
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MAGPVRCLPPVVEATSIPHAPPVISKEVSEIVNNMLSVAIPAAAAASAQDQRFASQFRCGPEFTTMKAQALEACRKILAENDQGGYTIPAKGLYPYQWNWDSALVSLGLAEMEEERAWEELDRLMSAQWEDGMVPHIVFHKPSSTYFPGPEIWGSPDKPRNTTGITQPPVAAISVRRLLEEAKDKALALAMARKLFPKLLAWHRWFYRARDPEGTGLVATIHPWETGMDNSPAWDEALARVPIDDIPPYVRRDLGHVDAKMRPQKAEYDRYLTLLYRFRALDYDEAKLYYETPFRVTDLCTNCILHKANEDLLWLAGATGACTDESEIRGWTARANVAFDTLFDVEAGLYRCKDQLTGQFLPAATSAGFLPLFAGVASGEKASAVARTLGRWLDDVAYGIPSCDPRDPQFEALRYWRGPVWLIVNWMVSEGLKRYGYGELAQRVERDSYELVKNGGIFEYYCPLTGMGAGGGCFSWTAAMCLAWLFKT
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Catalyzes the hydrolysis of alpha-D-mannosyl-glycerate (MG) to D-glycerate and D-mannose. Can also hydrolyze alpha-D-glucopyranosyl-glycerate (GG)with lower efficiency.
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D8VPP5
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AL11A_OLEEU
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Pectinesterase 1 (EC 3.1.1.11) (Pollen allergen Ole e 11.0101) (Ole e 11-1) (allergen Ole e 11.0101)
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MSCIAVEAVLLGILLYIPIVLSDDRAPIPSNSAQLNSWFDGIIQPVAVRKATMDPALVTAEGQTKVIKLKSDGSGDFKSINEAIKSIPDDNTKRVILSLAPGNYSEKVKIGMYKHYITFYGEDPNNMPILVFGGTAAEYGTVDSATLIVESNYFSAVNLKIVNSAPRPDGKRVGAQAAALRISGDKASFYNVKIYGFQDTLCDDKGKHFYKDCYIEGTVDFIFGSGKSIFLNTELHAVPGDQPAIITAQARKTDSEDTGYYFVNCRVTGGGAFLGRSWMPAAKVVFAYTEMVDAIHPEGWILVKPEHESTVRFSEYNNKGPGANMEKRAKFVKRLSDAEAKQSISLGSIEASKWLLPPRVVGLP
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Catalyzes the demethylesterification of homogalacturonan components of pectin. May be involved in pollen tube development.
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D9I2F9
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NL1A1_RAT
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NACHT, LRR and PYD domains-containing protein 1a allele 1 (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1a, C-terminus (Nlrp1a-CT); NACHT, LRR and PYD domains-containing protein 1a, N-terminus (Nlrp1a-NT)]
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MEESQSKQESNTRVAQHGSQQDVDPTFQTKRALEKERSKPRPRPLPRVQLQSLPGWSSTSNDVPLSQLIREMDHESRRCIHRSKKKLDRSEHISQGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWDEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVPTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLVPSLGQPHRVEVLGFSEFERKDYFYKYFAKERNTIIDFNLIGSIPVLLTLCEVPWVCWLLCTCLEKQMQQGEVLSLTSQTTTALCLKYLSLTIPGQHLSTQLRTLCSLAAEGICQRRTLFSKSDLCKQGLAEDAIATFLKIGVLQRQPSSLSYSFAHLCLQEFFAAMSYILEDSEEAHGDMGNDRTVETLVERYGRQNLFEAPTVRFLLGLLNTREMREMENIFACKFPWETKLKLLQSIIGEPFCQPCHLGLFHCLYENQEEELLTETMLCFPLTASGPNHMEATVFQTNVKRLVIQTDMELMVVTFCITFSHVRSLRLKGKGQQEYKLTAPAMVLYRWTPISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGDNGVRQLCEGLRNPACNLSILRLDQASLSEQVITELRALETKNPKLFISSTWMSHMTMPTENTDGEESLTSSKQQQQQSGDKHMEPLGTDDDFWGPSGPVSTEVVDRERNLYRVRLPMAGSYHCPSTGLHFVVTRAVTIEIGFCAWSQFLHETPLQHSHMVAGPLFDIKAEHGAVTAVCLPHFVSLQEGKVDSSLFHVAHFQDHGMVLETPARVEPHFAVLENPSFSPMGVLLRMIPAVGHFIPITSITLIYYRLYLEDITFHLYLVPNDCTIRKAIDEEELKFQFVRINKPPPVDALYVGSRYIVSSSKEVEILPKELELCYRSPRESQLFSEIYVGNIGSGINLQLTDKKYMNLIWEALLKPGDLRPALPRMASAPKDAPALLHFVDQHREQLVARVTSVDPLLDKLHGLVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIMDLLEKSGGVSVRL
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Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (By similarity). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as B.anthracis lethal toxin (LT) or Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (By similarity). In the absence of GSDMD expression, the Nlrp1a inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (By similarity). [NACHT, LRR and PYD domains-containing protein 1a allele 1]: Constitutes the precursor of the Nlrp1a inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals. [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]: Regulatory part that prevents formation of the Nlrp1a inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, this part is ubiquitinated by the N-end rule pathway and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the Nlrp1a inflammasome. [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Constitutes the active part of the Nlrp1a inflammasome. In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, N-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing this form, which polymerizes to form the Nlrp1a inflammasome complex: the Nlrp1a inflammasome complex then directly recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, leading to gasdermin-D (GSDMD) cleavage and subsequent pyroptosis.
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D9I2G1
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NL1A4_RAT
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NACHT, LRR and PYD domains-containing protein 1a allele 4 (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1a, C-terminus (Nlrp1a-CT); NACHT, LRR and PYD domains-containing protein 1a, N-terminus (Nlrp1a-NT)]
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MGESQSKQESNTRVAQHGSQQDVDPTFQTKRALERERSSPQVEQSFLGQLQSLLGWSSTSKDVPLSQLIREMDHESRRHSHQSKKKLDRSEHISEGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWDEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVPTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLVPSLGQPHRVEVLGFSEFERKDYFYKYFAKERNTIIDFNLIGSIPVLLTLCEVPWVCWLLCTCLEKQMQQGEVLSLTSQTTTALCLKYLSLTIPGQHLSTQLRTLCSLAAEGICQRRTLFSKSDLCKQGLAEDAIATFLKIGVLQRQPSSLSYSFAHLCLQEFFAAMSYILEDSEEAHGDMGNDRTVETLVERYGRQNLFEAPTVRFLLGLLNTREMREMENIFACKFPWETKLKLLRSIIGEPFCQPCHLGLFHCLYENQEEELLTETMLCFPLTASGPNHMEATVFQTNVKRLVIQTDMELMVVTFCITFSHVRSLRLKGKGQQEYKLTAPAMVLYRWTPISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGDNGVRQLCEGLRNPACNLSILRLDQASLSEQVITELRALETKNPKLFISSTWMSHMTMPTENTDGEESLTSSKQQQQQSGDKHMEPLGTDDDFWGPSGPVSTEVVDRERNLYRVRLPMAGSYHCPSTGLHFVVTRAVTIEIGFCAWSQFLHETPLQHSHMVAGPLFDIKAEHGAVTAVCLPHFVSLQEGKVDSSLFHVAHFQDHGMVLETPARVEPHFAVLENPSFSPMGVLLRMIPAVGHFIPITSITLIYYRLYLEDITFHLYLVPNDCTIRKAIDEEELKFQFVRINKPPPVDALYVGSRYIVSSSKEVEILPKELELCYRSPRESQLFSEIYVGNIGSGINLQLTDKKYMNLIWEALLKPGDLRPALPRMASAPKDAPALLHFVDQHREQLVARVTSVDPLLDKLHGLVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIMDLLEKSGGVSVRL
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Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (By similarity). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (By similarity). In the absence of GSDMD expression, the Nlrp1a inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (By similarity). [NACHT, LRR and PYD domains-containing protein 1a allele 4]: Constitutes the precursor of the Nlrp1a inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals. [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]: Regulatory part that prevents formation of the Nlrp1a inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, this part is ubiquitinated by the N-end rule pathway and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the Nlrp1a inflammasome. [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Constitutes the active part of the Nlrp1a inflammasome. In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, N-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing this form, which polymerizes to form the Nlrp1a inflammasome complex: the Nlrp1a inflammasome complex then directly recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, leading to gasdermin-D (GSDMD) cleavage and subsequent pyroptosis.
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D9I2G3
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NL1A2_RAT
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NACHT, LRR and PYD domains-containing protein 1 allele 2 (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1a, C-terminus (Nlrp1a-CT); NACHT, LRR and PYD domains-containing protein 1a, N-terminus (Nlrp1a-NT)]
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MEESQSKQESNTRVAQHGSQQDVDPTFQTKRALEKERSKPRPRPLPRVQLQSLPGWSSTSKDVPLSQLIREMDHESRRCIHRSKKKLDRSEHISQGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWDEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVPTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLVPSLGQPHRVEVLGFSEFERKDYFYKYFAKERNTIIDFNLIGSIPVLLTLCEVPWVCWLLCTCLEKQMQQGEVLSLTSQTTTALCLKYLSLTIPGQHLSTQLRTLCSLAAEGICQRRTLFSKSDLCKQGLAEDAIATFLKIGVLQRQPSSLSYSFAHLCLQEFFAAMSYILEDSEEAHGDMGNDRTVETLVERYGRQNLFEAPTVRFLLGLLNTREMREMENIFACKFPWETKLKLLQSIIGEPFCQPCHLGLFHCLYENQEEELLTETMLCFPLTASGPNHMEATVFQTNVKRLVIQTDMELMVVTFCITFSHVRSLRLKGKGQQEYKLTAPAMVLYRWTPISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGDNGVRQLCEGLRNPACNLSILRLDQASLSEQVITELRALETKNPKLFISSTWMSHMTMPTENTDGEESLTSSKQQQQQSGDKHMEPLGTDDDFWGPSGPVSTEVVDRERNLYRVRLPMAGSYHCPSTGLHFVVTRAVTIEIGFCAWSQFLHETPLQHSHMVAGPLFDIKAEHGAVTAVCLPHFVSLQEGKVDSSLFHVAHFQDHGMVLETPARVEPHFAVLENPSFSPMGVLLRMIPAVGHFIPITSITLIYYRLYLEDITFHLYLVPNDCTIRKAIDEEELKFQFVRINKPPPVDALYVGSRYIVSSSKEVEILPKELELCYRSPRESQLFSEIYVGNIGSGINLQLTDKKYMNLIWEALLKPGDLRPALPRMASAPKDAPALLHFVDQHREQLVARVTSVDPLLDKLHGLVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIMDLLEKSGGVSVRL
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Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (By similarity). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as B.anthracis lethal toxin (LT) or Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (By similarity). In the absence of GSDMD expression, the Nlrp1a inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (By similarity). [NACHT, LRR and PYD domains-containing protein 1 allele 2]: Constitutes the precursor of the Nlrp1a inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals. [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]: Regulatory part that prevents formation of the Nlrp1a inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, this part is ubiquitinated by the N-end rule pathway and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the Nlrp1a inflammasome. [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Constitutes the active part of the Nlrp1a inflammasome. In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, N-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing this form, which polymerizes to form the Nlrp1a inflammasome complex: the Nlrp1a inflammasome complex then directly recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, leading to gasdermin-D (GSDMD) cleavage and subsequent pyroptosis.
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D9I2G4
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NL1A5_RAT
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NACHT, LRR and PYD domains-containing protein 1a allele 5 (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1a, C-terminus (Nlrp1a-CT); NACHT, LRR and PYD domains-containing protein 1a, N-terminus (Nlrp1a-NT)]
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MGESQSKQESNTRVAQHGSQQDVDPTFQTKRALERERSSPQVEQSFLGQLQSLLGWSSTSKDVPLSQLIREMDHESRRHSHQSKKKLDRSEHISEGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWEEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVLTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLIPSLGQPHRVEVLGFSEFERKDYFYKYFAKERNTIIDFNLIGSIPVLLTLCEVPWVCWLLCTCLEKQMQQGEVLSLTSQTTTALCLKYLSLTIPGQHLSTQLRTLCSLAAEGICQRRTLFSKSDLCKQGLAEDAIATFLKIGVLQRQPSSLSYSFAHLCLQEFFAAMSYILEDSEEARGDMGNDRTVETLVERYGRQNLFEAPTVRFLLGLLNTREMREMENIFACKFPWKTKLKLLRSIVGEPFCQPCHLGLFHCLYENQEEELLTETMLCFPLTASGPNHMEATVFQTNVKRLVIQTDMELMVVTFCITFSHVRSLRLKGKGQQEYKLTAPAMVLYRWTPISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGDNGVRQLCEGLRNPACNLSILRLDQASLSEQVITELRALETKNPKLFISSTWMSHMTMPTENTDGEESLTSSKQQQQQSGDKHMEPLGTDDDFWGPSGPVSTEVVDRERNLYRVRLPMAGSYHCPSTGLHFVVTRAVTIEIGFCAWSQFLHETPLQHSHMVAGPLFDIKAEHGAVTAVCLPHFVSLQEGKVDSSLFHVAHFQDHGMVLETPARVEPHFAVLENPSFSPMGVLLRMIPAVGHFIPITSITLIYYRLYLEDITFHLYLVPNDCTIRKAIDEEELKFQFVRINKPPPVDALYVGSRYIVSSSKEVEILPKELELCYRSPRESQLFSEIYVGNIGSGINLQLTDKKYMNLIWEALLKPGDLRPALPRMASAPKDAPALLHFVDQHREQLVARVTSVDPLLDKLHGLVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIMDLLEKSGGVSVRL
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Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (By similarity). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (By similarity). In the absence of GSDMD expression, the Nlrp1a inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (By similarity). [NACHT, LRR and PYD domains-containing protein 1a allele 5]: Constitutes the precursor of the Nlrp1a inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals. [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]: Regulatory part that prevents formation of the Nlrp1a inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, this part is ubiquitinated by the N-end rule pathway and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the Nlrp1a inflammasome. [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Constitutes the active part of the Nlrp1a inflammasome. In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, N-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing this form, which polymerizes to form the Nlrp1a inflammasome complex: the Nlrp1a inflammasome complex then directly recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, leading to gasdermin-D (GSDMD) cleavage and subsequent pyroptosis.
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D9I2H0
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NL1A3_RAT
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NACHT, LRR and PYD domains-containing protein 1a allele 3 (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1a, C-terminus (Nlrp1a-CT); NACHT, LRR and PYD domains-containing protein 1a, N-terminus (Nlrp1a-NT)]
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MGESQSKQESNTRVAQHGSQQDVDPTFQTKRALERERSSPQVEQSFLGQLQSLLGWSSTSKDVPLSQLIREMDHESRRHSHQSKKKLDRSEHISEGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWDEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVPTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLVPSLGQPHRVEVLGFSEFERKDYFYKYFAKERNTIIDFNLIGSIPVLLTLCEVPWVCWLLCTCLEKQMQQGEVLSLTSQTTTALCLKYLSLTIPGQHLSTQLRTLCSLAAEGICQRRTLFSKSDLCKQGLAEDAIATFLKIGVLQRQPSSLSYSFAHLCLQEFFAAMSYILEDSEEAHGDMGNDRTVETLVERYGRQNLFEAPTVRFLLGLLNTREMREMENIFACKFPWETKLKLLQSIIGEPFCQPCHLGLFHCLYENQEEELLTETMLCFPLTASGPNHMEATVFQTNVKRLVIQTDMELMVVTFCITFSHVRSLRLKGKGQQEYKLTAPAMVLYRWTPISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGDNGVRQLCEGLRNPACNLSILRLDQASLSEQVITELRALETKNPKLFISSTWMSHMTMPTENTDGEESLTSSKQQQQQSGDKHMEPLGTDDDFWGPSGPVSTEVVDRERNLYRVRLPMAGSYHCPSTGLHFVVTRAVTIEIGFCAWSQFLHETPLQHSHMVAGPLFDIKAEHGAVTAVCLPHFVSLQEGKVDSSLFHVAHFQDHGMVLETPARVEPHFAVLENPSFSPMGVLLRMIPAVGHFIPITSITLIYYRLYLEDITFHLYLVPNDCTIRKAIDEEELKFQFVRINKPPPVDALYVGSRYIVSSSKEVEILPKELELCYRSPRESQLFSEIYVGNIGSGINLQLTDKKYMNLIWEALLKPGDLRPALPRMASAPKDAPALLHFVDQHREQLVARVTSVDPLLDKLHGLVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIMDLLEKSGGVSVRL
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Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (By similarity). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (By similarity). In the absence of GSDMD expression, the Nlrp1a inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (By similarity). [NACHT, LRR and PYD domains-containing protein 1a allele 3]: Constitutes the precursor of the Nlrp1a inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals. [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]: Regulatory part that prevents formation of the Nlrp1a inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, this part is ubiquitinated by the N-end rule pathway and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the Nlrp1a inflammasome. [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Constitutes the active part of the Nlrp1a inflammasome. In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, N-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing this form, which polymerizes to form the Nlrp1a inflammasome complex: the Nlrp1a inflammasome complex then directly recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, leading to gasdermin-D (GSDMD) cleavage and subsequent pyroptosis.
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D9IA43
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CCON1_STUST
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Cbb3-type cytochrome c oxidase subunit CcoN1 (EC 7.1.1.9) (Cytochrome CBB3 subunit CcoN1)
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MNTATSTAYSYKVVRQFAIMTVVWGIVGMGLGVFIAAQLAWPFLNFDLPWTSFGRLRPLHTNAVIFAFGGCALFATSYYSVQRTCQTTLFAPKLAAFTFWGWQLVILLAAISLPLGFTSSKEYAELEWPIDILITIVWVAYAVVFFGTLAKRKVKHIYVGNWFFGAFILTVAILHVVNNLEIPVTAMKSYSLYAGATDAMVQWWYGHNAVGFFLTAGFLGIMYYFVPKQAERPVYSYRLSIVHFWALITVYIWAGPHHLHYTALPDWAQSLGMVMSLILLAPSWGGMINGMMTLSGAWHKLRSDPILRFLVVSLAFYGMSTFEGPMMAIKTVNALSHYTDWTIGHVHAGALGWVAMVSIGALYHLVPKVFGREQMHSIGLINTHFWLATIGTVLYIASMWVNGIAQGLMWRAINDDGTLTYSFVESLEASHPGFVVRMIGGAIFFAGMLVMAYNTWRTVQAAKPAEYDAAAQIA
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Cbb3-type cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits CcoN and CcoO form the functional core of the enzyme complex. Subunits CcoP and CcoQ may optionally bind to the core. CcoN is the catalytic subunit of the enzyme. Electrons originating in cytochrome c or a quinol are transferred to the bimetallic center formed by a high-spin heme and copper B. The complex also functions as a proton pump.
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D9IVE5
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ANM2_XENLA
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Protein arginine N-methyltransferase 2 (EC 2.1.1.319) (Histone-arginine N-methyltransferase PRMT2)
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MESSSECSSISDFQDSTEGDDANTLPENLCMREYVVICDYVATDNTQLSLCSGDKVLLLNAVSQDWWWVNHNGTCGYVPASHLHDALNEQEDTEVNDPWQDEEYYGSYKTLKLHLEMLSDVPRTMTYQNVILKNSSSLCGKHILDLGCGTGIISFFCAKFAQPEAVYAVEASKIAEQTCRLVEQNGISSLVHVIRQQAEELDLPTKVDVLVSEWMGTCLLFEFMLESVLQARDRWLKEDGVMWPSTACIHLVPCSAYKEYSNKVLFWDNPYQLDFSLLKPPATKEFFAKPQPDYILQPEDCLSEPCTLFHLNLKTLQVAELERMNCDFTFLVHTNGLLHGFTAWFSVQFENLEEQGHLELNTGPFSPLTHWKHTLFMLDEPLQVQKRDKISGSVVFERNSVWRRHMSVTLSWVISRELKMQKVGCKVFPIWR
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Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as histones. Involved in growth regulation (By similarity). Involved in embryonic dorsal development. {ECO:0000250, ECO:0000269|PubMed:20708585}.
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D9N164
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IRK10_MAGMG
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Inward rectifier potassium channel Kirbac3.1
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MTGGMKPPARKPRILNSDGSSNITRLGLEKRGWLDDHYHDLLTVSWPVFITLITGLYLVTNALFALAYLACGDVIENARPGSFTDAFFFSVQTMATIGYGKLIPIGPLANTLVTLEALCGMLGLAVAASLIYARFTRPTAGVLFSSRMVISDFEGKPTLMMRLANLRIEQIIEADVHLVLVRSEISQEGMVFRRFHDLTLTRSRSPIFSLSWTVMHPIDHHSPIYGETDETLRNSHSEFLVLFTGHHEAFAQNVHARHAYSCDEIIWGGHFVDVFTTLPDGRRALDLGKFHEIAQ
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Inward rectifier potassium channel that mediates potassium uptake into the cell. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. The inward rectification may be achieved by the blockage of outward current by cytoplasmic divalent metal ions and polyamines. Complements an E.coli mutant that is defective in K(+) uptake.
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D9PTN5
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MYRF2_CAEEL
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Myelin regulatory factor homolog 2 (EC 3.4.-.-) [Cleaved into: Myelin regulatory factor homolog 2, N-terminal; Myelin regulatory factor homolog 2, C-terminal]
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MGDLNPAETPEPKKNPVAKIASNLYSTQIVKPVPSVSNSTNLSPCQNPNMTNLFYITLLQNKLNKYTQQLLKKNEEGLNDPLANVEQFNIIQFLQNDVDFNLPIEAFEQGNMDQNIRIDPILQRQQMANQPMLMPQHMLQQLHQQQIYEQQLASMPMTPAITDLTRHGSSSSPSTTNSDPPYSPEGLNNFGLGTQRPNHGVIPNDISNVPQHINRQFNPRMGPNTSPNPPSFPQFLNSNHPTPGSYVQSISPDSNGQGFAQSNLYNALNVSSDESINGSDDIPNRKRPRMDQNMDPSFIMHAPVSGKLGAEVTEEGGQPNIRFFKYQEEQWCPMYDANGEELGRLQVHVLADKGFNYSTNDNCFVNQKKNHFQVTVKIEAIDPSPPQCFKINGVCKPIENFQLSFVGAKSESQNSEIPIRQSTTERKPILHTPVLFKIVERRMTIVTVPRLHFSETTLNNQRKNLRPNPDQKYFNLVVRLYATATDGTTVLMQAFASERVIVRATNPGSFEPPEMVDASWNKNGGILSTNGPVVIGKSEPRAQLTVDGDIYSSGRVMYPSDIRLKDNITEKGAKDALENLQKLRIVDYFYKPEVASKWGLTEDQRKRTGVIAQELAAVLPDAVKDLGDYLTVNESRVFYETVLATQELCRLTGDLDQKIDDKVAEISQRLTQYAQKKKMLNSMASGLNSEGRSLNASRTSLDSSASALTLTNTKKNRRSSRKDKKDAPKSKMTHGTVIGLVGVMAFCLLAMSALYILDWHNRNFGYHHFTPSATTSGPKEGPGNVVIPLDHYVPLRQPDAPPLVPFCPMETCRGYCCMEYDKDHAELEITEYDPNTATDNDFGFKADTRSDFTLKGFGNNVKISLPELGMQIDERYCIEKSCVKKRKVYSLFIPMTRYLPNVPLEVQIDVPSSKVVNNCGYIQEFDNRKCDETGSSSTETDAPRSIQLFDNTFQVSAGQWTQSAYRFRVGYSTELCSIDDTHFGGFYEEYNLIFYRACNRTNSTAINVV
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[Myelin regulatory factor homolog 2]: Constitutes a precursor of the transcription factor. Mediates the autocatalytic cleavage that releases the Myelin regulatory factor homolog 2, N-terminal component that specifically activates transcription of genes involved in synaptic rewiring during nervous system maturation. [Myelin regulatory factor homolog 2, C-terminal]: Membrane-bound part that has no transcription factor activity and remains attached to the endoplasmic reticulum membrane following cleavage. [Myelin regulatory factor homolog 2, N-terminal]: Transcription factor that specifically activates expression of genes involved in synaptic rewiring during nervous system maturation. Specifically required for dorsal D (DD) GABAergic motor neurons synaptic rewiring. Acts in complex with myrf-1 paralog.
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D9PUX5
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TFRB_METTM
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Fumarate reductase (CoM/CoB) subunit B (EC 1.3.4.1) (Thiol:fumarate reductase subunit B)
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MINVKVLRFEPGVDEKPHLESYDIPSKEKMKVLDALQLINKMYNANIAFRSSCRAGQCGSCAVKMNGEVVLACRAEVEDGAVIEPVDLPVIKDLMVDRSEIEDKVRAMGLYLQSEARGIQRIKPEDYQDTKKLRGCIECFSCISSCPVIKESTEYAGPYFMRYISKFAFDPRDEAERAAGGVEEGLYCCTTCGKCAEVCPKELNVPGDAIEKLRAMACREGAGPLDAHRKIKKLISETGRSVDHIGKGFIESVGQNPGSRIGFFTGCLVDYRMPDVGMALLRVLREHGFEVDVPDGQVCCGSPMIRTGQLDIVEDLVERNRRALEGYDTIITVCAGCGATLKKDYPRYGVELNVLDISEFLADRIDDIKMKPVNMRVTYHDPCHLLRGQGVKLEPRKILNSIPGLEFVEMEKQGQCCGSGGGVKSGKPEIAESLGKKKAEMIRKLNVDAVITICPFCQLHIKDSLEKEGLGDVKVMNILELLDMAYSDD
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Catalyzes the reduction of fumarate with reduced coenzyme M (CoM-S-H) and coenzyme B (CoB-S-H). In vitro, is able to reduces fumarate with reduced benzyl viologen, oxidize CoM-S-H and CoB-S-H to CoM-S-S-CoB with methylene blue, and reduce CoM-S-S-CoB with reduced benzyl viologen. The enzyme has specificity for the two thiol compounds as the CoB--CoM heterodisulfide reductase. The enzyme is very sensitive to oxygen.
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D9PVP5
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FNO_METTM
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F420-dependent NADP reductase (EC 1.5.1.40) (F420H2:NADP oxidoreductase)
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MKIAVLGGTGDQGLGLALRLALAGEEVIIGSRDAEKAVSAAQKVLEIAERDDLKVKGATNAEAAEEAEVAILTVPLQAQMATLGSVKEAIKGKVLIDATVPIDSCLGGSAVRYIDLWDGSAAERAARFLEDQGTRVAAAFNNISASALLDITGPVDCDCLIASDHRDALDLASELAEKIDGVRAIDCGGLENARVIEKITPLLINLNIKNRIRNAGIRITNLPE
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Catalyzes the reduction of NADP(+) with F420H(2) via hydride transfer, and the reverse reaction, i.e. the reduction of F420 with NADPH. Probably functions in the regeneration of NADPH required in biosynthetic reactions.
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D9TT09
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SUCPP_THETC
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Sucrose 6(F)-phosphate phosphorylase (EC 2.4.1.329) (Sucrose 6'-phosphate phosphorylase) (SPP)
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MALKNKVQLITYPDSLGGNLKTLNDVLEKYFSDVFGGVHILPPFPSSGDRGFAPITYSEIEPKFGTWYDIKKMAENFDILLDLMVNHVSRRSIYFQDFLKKGRKSEYADMFITLDKLWKDGKPVKGDIEKMFLRRTLPYSTFKIEETGEEEKVWTTFGKTDPSEQIDLDVNSHLVREFLLEVFKTFSNFGVKIVRLDAVGYVIKKIGTSCFFVEPEIYEFLDWAKGQAASYGIELLLEVHSQFEVQYKLAERGFLIYDFILPFTVLYTLINKSNEMLYHYLKNRPINQFTMLDCHDGIPVKPDLDGLIDTKKAKEVVDICVQRGANLSLIYGDKYKSEDGFDVHQINCTYYSALNCDDDAYLAARAIQFFTPGIPQVYYVGLLAGVNDFEAVKKTKEGREINRHNYGLKEIEESVQKNVVQRLLKLIRFRNEYEAFNGEFFIEDCRKDEIRLTWKKDDKRCSLFIDLKTYKTTIDYINENGEEVKYLV
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Catalyzes the reversible phosphorolysis of sucrose 6(F)-phosphate into alpha-D-glucose 1-phosphate (Glc1P) and D-fructose 6-phosphate. May be involved in a new pathway for the degradation of sucrose, which could become phosphorylated on its fructose moiety during uptake via a PTS system. To a lesser extent, can also reversibly act on sucrose in vitro. Is also able to catalyze transglycosylation reactions in vitro.
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E0CJS3
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EOBII_PETHY
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MYB-like transcription factor EOBII (MYB-like protein NON1) (PhNON1) (Protein EMISSION OF BENZENOIDS II) (PhEOBII)
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MDKKPCNSQDAEVRKGPWTMEEDLILINYIANHGEGVWNSLAKSAGLKRTGKSCRLRWLNYLRPDVRRGNITPEEQLLIMELHAKWGNRWSKIAKHLPGRTDNEIKNYWRTRIQKHIKQAETMNGQAASSEQNDHQEACTSQMSNGPNDNTIDQTYSPTSYSGNVDTFQAGPNFLTEANDNMWSMEDIWSMQLLNGD
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MYB-type transcription factor controlling the production of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) by regulating the expression of ODO1 and EOBI, key regulators of the shikimate pathway, and of several biosynthetic floral scent-related genes including IGS, PAL2 and CFAT. This scent, mostly produced in the evening and night by the petals, attracts the pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta). Binds to and activates the ODO1 and EOBI promoters via MYB binding sites (MBS) 5'-AAACCTAAT-3' and 5'-CTAACT-3'. Regulates the promoters of IGS1, CFAT and PAL2. Controls flowers petal opening by modulating a global transcriptomic switch.
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E0CX11
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STMP1_HUMAN
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Short transmembrane mitochondrial protein 1
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MLQFLLGFTLGNVVGMYLAQNYDIPNLAKKLEEIKKDLDAKKKPPSA
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Microprotein involved in mitochondrial respiratory chain complex III (ubiquinol-cytochrome c oxidoreductase) and complex IV (mitochondrial cytochrome c oxidase complex) assembly. Required for the formation of mitochondrial supercomplexes (SCs). Also required for the activation of the NLRP3 inflammasome (By similarity).
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E0CZ16
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KLHL3_MOUSE
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Kelch-like protein 3
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MEGESVKPSPQPTAQAEDEEKNRRTVTVNAAHMGKAFKVMNELRSKRLLCDVMIVAEDVEVEAHRVVLAACSPYFCAMFTGDMSESKAKKIEIKDVDGQTLSKLIDYIYTAEIEVTEENVQVLLPAASLLQLMDVRQNCCDFLQSQLHPTNCLGIRAFADVHTCTDLLQQANAYAEQHFPEVMLGEEFLSLSLDQVCSLISSDKLTVSSEEKVFEAVISWINYEKETRLDHMAKLMEHVRLPLLPRDYLVQTVEEEALIKNNNTCKDFLIEAMKYHLLPLDQRLLIKNPRTKPRTPVSLPKVMIVVGGQAPKAIRSVECYDFEEGRWDQIAELPSRRCRAGVVFMAGHVYAVGGFNGSLRVRTVDVYDGVKDQWTSIASMQERRSTLGAAVLNDLLYAVGGFDGSTGLASVEAYSYKTNEWFFVAPMNTRRSSVGVGVVEGKLYAVGGYDGASRQCLSTVEQYNPATNEWIYVADMSTRRSGAGVGVLSGQLYATGGHDGPLVRKSVEVYDPGTNTWKQVADMNMCRRNAGVCAVNGLLYVVGGDDGSCNLASVEYYNPVTDKWTLLPTNMSTGRSYAGVAVIHKSL
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Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of ion transport in the distal nephron. The BCR(KLHL3) complex acts by mediating ubiquitination and degradation of WNK1 and WNK4, two activators of Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney, thereby regulating NaCl reabsorption. The BCR(KLHL3) complex also mediates ubiquitination of CLDN8, a tight-junction protein required for paracellular chloride transport in the kidney, leading to its degradation.
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E0SRA9
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ILVC_IGNAA
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Ketol-acid reductoisomerase (NAD(P)(+)) (KARI) (EC 1.1.1.383) (Acetohydroxy-acid isomeroreductase) (AHIR) (Alpha-keto-beta-hydroxylacyl reductoisomerase) (Ketol-acid reductoisomerase type 1) (Ketol-acid reductoisomerase type I)
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MAKIYKDEDISLEPIKNKTIAILGYGSQGRAWALNLRDSGLNVVVGLERQGDSWRRAIDDGFKPMYTKDAVAIADIIVFLVPDMVQKSLWLNSVKDFMKKGADLVFAHGFNIHFKIIEPPKDSDVYMIAPKSPGPIVRRSYEMGGGVPALVAVYQNVSGEALQKALAIAKGIGCARAGVIESTFKEETETDLFGEQVILVGGIMELIKASFETLVEEGYQPEVAYFETVNELKLIVDLIYEKGLTGMLRAVSDTAKYGGITVGKFIIDKSVRDKMKIVLERIRSGEFAREWIKEYERGMPTVFKELSELEGSTIETVGRKLREMMFRGMKQISSH
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Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH or NADH to yield (R)-2,3-dihydroxy-isovalerate.
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E0VIU9
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PRKN_PEDHC
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E3 ubiquitin-protein ligase parkin (EC 2.3.2.31)
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MSILEWFWNILCGMAQYLTFSKNLTNDNLVNIYVKSNVGGTISVNLDPKSDIKNVKELVAPKLGLEPDDVKIIFAGKELLDSTVIEVLDFFSDILHAVKVNKKIKNVIPDKPLCETLEELHQLNDQKNVESIEESNLKNEGKNKAHFFIYCANPCKKINTGKLRVCCSECKHGAFTVDTDPQSWADVLDKNKITGVCNNVGCEGLYAKFYFKCASHPSQGENDTAVPLNLIKRNHKKIPCLACTDICDPVLVFSCDNRHVTCLECFKNYCGSRLKDRQFLSHPDFGYTLPCPAGCSNSFIEEVHHFRLLTDAQYEQYHRFATEEFILQAGGVLCPQPGCGQGILIDQNCNRVQCSCGYVFCGKCLEGFHLGECLNPTDVPFLSQNCDYPLDPEKLEKARWDEASSTVIKVLTKPCPKCRTSTERAGGCMHMICTRANCGFHWCWVCQGPWERDCMASHWFG
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E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as Marf, Opa1, Sep1, Tom20 and porin (By similarity). Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates, depending on the context. Protects against mitochondrial dysfunction during cellular stress, by acting downstream of Pink1, to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components (By similarity). 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). Activation and recruitment onto the outer membrane of damaged/dysfunctional mitochondria (OMM) requires Pink1-mediated phosphorylation of both park and ubiquitin (By similarity). In depolarized mitochondria, mediates the decision between mitophagy or preventing apoptosis by inducing either the poly- or monoubiquitination of porin/VDAC polyubiquitination of porin promotes mitophagy, while monoubiquitination of porin decreases mitochondrial calcium influx which ultimately inhibits apoptosis (By similarity). When cellular stress results in irreversible mitochondrial damage, promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by promoting the ubiquitination of mitochondrial proteins (By similarity). Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains following mitochondrial damage, leading to mitophagy (By similarity). In developing tissues, inhibits JNK-mediated apoptosis by negatively regulating bsk transcription (By similarity). The Pink1-park pathway also promotes fission and/or inhibits fusion of damaged mitochondria by mediating the ubiquitination and subsequent degradation of proteins involved in mitochondrial fusion/fission such as Marf and Opa1 (By similarity). This prevents the refusion of unhealthy mitochondria with the healthy mitochondrial network and/or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes (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 via the ubiquitination of transcriptional repressor Paris which leads to its subsequent proteasomal degradation and allows activation of the transcription factor srl (By similarity). Promotes 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).
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E0W1I1
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PINK1_PEDHC
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Serine/threonine-protein kinase Pink1, mitochondrial (EC 2.7.11.1) (PTEN-induced putative kinase 1)
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MSLLAYTNLLLQNGRIFRYYKKANIKKFIKKIIKLDLKSTPSEASVSRQTFLSTGLNSVKNAVQLQARKLLINNVLERVTPTLNSDLKKKAAKRLFYGDSAPFFALVGVSLASGSGLLTKDDELEGICWEIREAVSKGKWNDSESENVEQLQAANLDELDLGEPIAKGCNAVVYSAKLKNVQSNKLAHQLAVKMMFNYDVESNSTAILKAMYRETVPAMSYFFNQNLFNIENISDFKIRLPPHPNIVRMYSVFADRIPDLQCNKQLYPEALPPRINPEGSGRNMSLFLVMKRYDCTLKEYLRDKTPNMRSSILLLSQLLEAVAHMNIHNISHRDLKSDNILVDLSEGDAYPTIVITDFGCCLCDKQNGLVIPYRSEDQDKGGNRALMAPEIANAKPGTFSWLNYKKSDLWAVGAIAYEIFNIDNPFYDKTMKLLSKSYKEEDLPELPDTIPFIIRNLVSNMLSRSTNKRLDCDVAATVAQLYLWAPSSWLKENYTLPNSNEIIQWLLCLSSKVLCERDITARNKTNTMSESVSKAQYKGRRSLPEYELIASFLRRVRLHLVRKGLKWIQELHIYN
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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).
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E0W4V5
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PSR2_PHYSO
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RxLR effector protein PSR2 (Avirulence homolog protein 146) (Suppressor of RNA silencing protein 2)
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MRLQCVVLFAALTLVAATHAPPNVKTVLSAEQHDIPVKRLLRPGNPAGKEDEERGINFSSVPGFEKLANLLKPKPGLKKLLKWADAKKPPETVFTRLRLDKTGTQLFDNTDFPVWAAYTRSVAQTDSEASAVMLKTLVSRYSDEVLSGMIAAAKKSSKTESIATKLETEQMRTWLAAKKTPDDMFLVFKLNKAGDDILSSPLLSAWTNYMKLSNKENPKAQTTLIATMTKHYGDSGVSQILAAARKSPATQSTAKRLEAEQVQLWLKKGRTPDDTFTLLSLDRAGDDLLASPQFNTWMKYINYYNKENPDEKTTVLAKLMTHFDDEELTPILVVARKVPSTESTAAKLQAEQFKNWLSADKSPEEAFTLLQLDKAGDDLLTNPQLTNWLKYTENFNLNKEINEQVTAIQVFRAQYVDDSRIANMVIAAEKVPNTQAIAKRVEDELFKGWTVVLNKPDDVFINLKLETVGENVFESPLWSFYTKFLEKYNTANPGKEQTMISGLARGYNDVTLTNMLLKAKEAPSTKTLATKLEDELVQYWLADKKLPDKLFGYLELKESVDGILTNPVFNVWLKYLNAFNDKAPVKKALMIDTLKSAFGDVAVSNMLFAAKKDPGTAKVAATLQTALLSKWVLEKKTPGQVSAILKEGAGADVSAKLLATYSAKFKVRWG
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Secreted effector that possesses RNA silencing suppression activity by inhibiting the biogenesis of small RNAs in the host plant to promote enhanced susceptibility of host to the pathogen during infection. Interferes with secondary siRNA production by associating with host dsRNA-binding protein DRB4. Inhibits the host salicylic acid pathway during infection.
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E0W544
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AVH23_PHYSO
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RxLR effector protein Avh23 (Avirulence homolog protein 23)
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MRLTYFLTVIVVATLHAGGTALATAEAPNHAAIVNVASADNVHSLDTTAEIGGRMLRKVKEDTVSKKDHEERGPGAILERQTAFVKKLFSRQNAIVNRAQGAFQRQNAFVNRDQGAFQRQNAFVKRAIQRQNHFKLSDNA
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Effector that suppresses plant defense responses during the early stages of pathogen infection. Suppresses cell death induced by effectors and PAMPs in plant hosts. Acts as a modulator of histone acetyltransferase (HAT) in plants. Avh23 binds to the ADA2 subunit of the HAT complex SAGA and disrupts its assembly by interfering with the association of ADA2 with the catalytic subunit GCN5. As such, Avh23 suppresses H3K9 acetylation mediated by the ADA2/GCN5 module and increases plant susceptibility.
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E0WN94
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ODC_NICGL
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Ornithine decarboxylase, chloroplastic (EC 4.1.1.17)
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MAGQTIIVSGLNPAAILQSTIGGGASPTAAAAAENGTRKVIPLSRDALQDFMLSIITQKLQDEKQPFYVLDLGEVVSLMDQWKSALPNIRPFYAVKCNPEPSFLSILSAMGSNFDCASRAEIEYVLALGISPDRIVFANPCKPESDIIFAAKVGVNLTTYDSEDEVYKIRKHHPKSELLLRIKPMFDGNARCPMGPKYGALPEEVEPLLRAAQAARLTVSGVSFHIGSGDADSNAYLGAIAAAKEVFETAAKLGMSKMTVLDVGGGFTSGHQFTAAAVAVKSALKQRFDDEPELTIIAEPGRFFAETAFTLATTIIGKRVRGELREYWINDGLYGSMNCVLYDHATVNATPLAVQSNRSNVTCGGSKTFPTTVFGPTCDALDTVLRDYQLPELQVNDWLVFPNMGAYTKAAGSNFNGFNTSAIVTHLAYAYPS
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Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins) nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN). Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine (By similarity). Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis (By similarity).
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E0X9C7
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TODS_PSEPT
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Sensor histidine kinase TodS (EC 2.7.13.3)
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MSSLDRKKPQNRSKNNYYNICLKEKGSEELTCEEHARIIFDGLYEFVGLLDAHGNVLEVNQVALEGAGITLEEIRGKPFWKARWWQISKKTEATQKRLVETASSGEFVRCDVEILGKSGGREVIAVDFSLLPICNEEGSIVYLLAEGRNITDKKKAEAMLALKNQELEQSVERIRKLDNAKSDFFAKVSHELRTPLSLILGPLEAVMAAEAGRESPYWKQFEVIQRNAMTLLKQVNTLLDLAKMDARQMGLSYRRANLSQLTRTISSNFEGIAQQKSITFDTKLPVQMVAEVDCEKYERIILNLLSNAFKFTPDGGLIRCCLSLSRPNYALVTVSDSGPGIPPALRKEIFERFHQLSQEGQQATRGTGLGLSIVKEFVELHRGTISVSDAPGGGALFQVKLPLNAPEGAYVASNTAPRRDNPQVVDTDEYLLLAPNAENEAEVLPFQSDQPRVLIVEDNPDMRGFIKDCLSSDYQVYVAPDGAKALELMSNMPPDLLITDLMMPVMSGDMLVHQVRKKNELSHIPIMVLSAKSDAELRVKLLSESVQDFLLKPFSAHELRARVSNLVSMKVAGDALRKELSDQGDDIAILTHRLIKSRHRLQQSNIALSASEARWKAVYENSAAGIVLTDPENRILNANPAFQRITGYGEKDLEGLSMEQLTPSDESPQIKQRLANLLQGGGAEYSVERSYLCKNGSTIWANASVSLMPQRVGESPVILQIIDDITEKKQAQENLNQLQQQLVYVSRSATMGEFAAYIAHEINQPLSAIMTNANAGTRWLGNEPSNIPEAKEALARIIRDSDRAAEIIRMVRSFLKRQETVLKPIDLKALVTDTSLILKAPSQNNSVNLDVVADDELPEIWGDGVQIQQLIINLAMNAIEAISQADCETRQLTLSFSGNDTGDALVISVKDTGPGISERQMAQLFNAFYTTKKEGLGMGLAICLTITEVHNGKIWVECPPAGGACFLVSIPARQGSGT
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Member of the two-component regulatory system TodS/TodT involved in the regulation of toluene degradation. Phosphorylates TodT via a four-step phosphorelay in response to toluene. Can also be induced by benzene and ethylbenzene.
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E0Y3X1
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NOTF_ASPSM
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Deoxybrevianamide E synthase notF (EC 2.5.1.109) (Reverse prenyltransferase notF)
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MTAPELRVDTFRAPEDAPKEPSAQQPRLPSSPSPAQALASYHHFPTNDQERWWEETGSLFSRFLEAGQYGLPQQYQFMFFFMHHLIPALGPYPQKWRSTISRSGLPIEFSLNFQKGSHRLLRIGFEPVSFLSGSSQDPFNRIPITDLLNRLSKLQLSNFDTPFFQHLLSKFQLSLSEVRQLQKQGSGPDAHPLKSQAAFGFDFNPDGAILVKGYVFPYLKAKAADVPVGTLIAEAVRTIDVERNQFTHAFGLINDYMQESTGYNEYTFLSCDFVETSEQRLKIYGAHTEVTWAKIAEMWTLGGRLIEEPEIIAGLARLKQIWSLLQIGEGSRAFKGGFDYDKSSATDQIASPIIWNYEIHPGSRFPVPKFYLPVHGENDLHVARALAQFWDSLGWPEHACAYPDTLQQLYPDQDISQTTRLQSWISYSYTAKRGVYMSVYYHSQSTYLWEED
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Deoxybrevianamide E synthase part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core. The first step of notoamide biosynthesis involves coupling of L-proline and L-tryptophan by the bimodular NRPS notE, to produce cyclo-L-tryptophan-L-proline called brevianamide F. The reverse prenyltransferase notF then acts as a deoxybrevianamide E synthase and converts brevianamide F to deoxybrevianamide E via reverse prenylation at C-2 of the indole ring leading to the bicyclo[2.2.2]diazaoctane core. Deoxybrevianamide E is further hydroxylated at C-6 of the indole ring, likely catalyzed by the cytochrome P450 monooxygenase notG, to yield 6-hydroxy-deoxybrevianamide E (Probable). 6-hydroxy-deoxybrevianamide E is a specific substrate of the prenyltransferase notC for normal prenylation at C-7 to produce 6-hydroxy-7-prenyl-deoxybrevianamide, also called notoamide S. As the proposed pivotal branching point in notoamide biosynthesis, notoamide S can be diverted to notoamide E through an oxidative pyran ring closure putatively catalyzed by either notH cytochrome P450 monooxygenase or the notD FAD-linked oxidoreductase (Probable). This step would be followed by an indole 2,3-epoxidation-initiated pinacol-like rearrangement catalyzed by the notB FAD-dependent monooxygenase leading to the formation of notoamide C and notoamide D. On the other hand notoamide S is converted to notoamide T by notH (or notD), a bifunctional oxidase that also functions as the intramolecular Diels-Alderase responsible for generation of (+)-notoamide T (Probable). To generate antipodal (-)-notoaminide T, notH' (or notD') in Aspergillus versicolor is expected to catalyze a Diels-Alder reaction leading to the opposite stereochemistry (Probable). The remaining oxidoreductase notD (or notH) likely catalyzes the oxidative pyran ring formation to yield (+)-stephacidin A (Probable). The FAD-dependent monooxygenase notI is highly similar to notB and is predicted to catalyze a similar conversion from (+)-stephacidin A to (-)-notoamide B via the 2,3-epoxidation of (+)-stephacidin A followed by a pinacol-type rearrangement (Probable). Finally, it remains unclear which enzyme could be responsible for the final hydroxylation steps leading to notoamide A and sclerotiamide (Probable).
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E0Y419
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VSPBF_MACLB
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Beta-fibrinogenase (VLBF) (EC 3.4.21.-) (Snake venom serine protease) (SVSP)
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MVLIRVLANLLLLQLSHAQKSSELVVGGDECNINEHRSLVFLYNSSFGCGGTLINQEWVLSAAHCDMENMRIYLGWHNFSLPNMNQKRRVAKEKFFCLSSKNYTEWDKDIMLIKMNRPVTYSTHVAPLSLPSSPPSVGSVCRIMGWGAITSPNETYPDVPHCANINILNYTVCRAAHPWLPAQSRTLCAGILQGGIDTCKGDSGGPLICNGQIQGIVSWGDNPCAQPLKPGHYTNVFDYTDWIQSIIAGNTTATCPP
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Snake venom serine protease that has fibrinogenolytic activities by hydrolyzing the beta chain of fibrinogen (FGB). Typical arginine esterase which hydrolyzes esters and amides of arginine.
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E0Y421
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VSPY_MACLB
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Chymotrypsin-like protease VLCTLP (EC 3.4.21.-) (Snake venom serine protease) (SVSP) (Vipera Lebetina with chymotrypsin-like proteolytic activity)
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MVLIRVLANLLLLQLSYAQKSSELVVGGDECNINEHRSLVFLYNSSFGCGGTLINQQWVLSAAHCDMENVQIYLGLHNLRLRNQDEQIRVAEEKFFCLSNKSYTKWDKDIMLIRLNSSVTYNTHIAPLSLPSSPPRVGSVCRIMGWGAITSPNETFPNVPHCANINILRYSVCRAAYRGLPAQSRTLCAGILQGGIGSCMGDSGGPLICNGEIQGIVSWGDDICAQPHKPVHYTKVFDYSDWIQSIIAGNTTATCPL
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Snake venom serine protease with tyrosine-specific chymotrypsin-like activity. Hydrolyzes the N-acetyl-L-tyrosine ethyl ester (ATEE). Has weak fibrinogenolytic activity. Weakly hydrolyzes azocasein, Aalpha-chain (FGA) and more slowly Bbeta-chain (FGB) of fibrinogen. Optimal substrates are angiotensins I and II (AGT).
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E1B328
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WR52N_ARATH
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Disease resistance protein RRS1 (Disease resistance protein RCH2) (Disease resistance protein SLH1) (Probable WRKY transcription factor 52) (Protein RPS4-homolog) (Protein SENSITIVE TO LOW HUMIDITY 1) (Resistance to Colletotrichum higginsianum 2 protein) (Resistance to Ralstonia solanacearum 1 protein) (WRKY DNA-binding protein 52)
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MTNCEKDEEFVCISCVEEVRYSFVSHLSEALRRKGINNVVVDVDIDDLLFKESQAKIEKAGVSVMVLPGNCDPSEVWLDKFAKVLECQRNNKDQAVVSVLYGDSLLRDQWLSELDFRGLSRIHQSRKECSDSILVEEIVRDVYETHFYVGRIGIYSKLLEIENMVNKQPIGIRCVGIWGMPGIGKTTLAKAVFDQMSSAFDASCFIEDYDKSIHEKGLYCLLEEQLLPGNDATIMKLSSLRDRLNSKRVLVVLDDVCNALVAESFLEGFDWLGPGSLIIITSRDKQVFRLCGINQIYEVQGLNEKEARQLFLLSASIMEDMGEQNLHELSVRVISYANGNPLAISVYGRELKGKKKLSEMETAFLKLKRRPPFKIVDAFKSSYDTLSDNEKNIFLDIACFFQGENVNYVIQLLEGCGFFPHVEIDVLVDKCLVTISENRVWLHKLTQDIGREIINGETVQIERRRRLWEPWSIKYLLEYNEHKANGEPKTTFKRAQGSEEIEGLFLDTSNLRFDLQPSAFKNMLNLRLLKIYCSNPEVHPVINFPTGSLHSLPNELRLLHWENYPLKSLPQNFDPRHLVEINMPYSQLQKLWGGTKNLEMLRTIRLCHSQHLVDIDDLLKAENLEVIDLQGCTRLQNFPAAGRLLRLRVVNLSGCIKIKSVLEIPPNIEKLHLQGTGILALPVSTVKPNHRELVNFLTEIPGLSEASKLERLTSLLESNSSCQDLGKLICLELKDCSCLQSLPNMANLDLNVLDLSGCSSLNSIQGFPRFLKQLYLGGTAIREVPQLPQSLEILNAHGSCLRSLPNMANLEFLKVLDLSGCSELETIQGFPRNLKELYFAGTTLREVPQLPLSLEVLNAHGSDSEKLPMHYKFNNFFDLSQQVVNDFFLKALTYVKHIPRGYTQELINKAPTFSFSAPSHTNQNATFDLQPGSSVMTRLNHSWRNTLVGFGMLVEVAFPEDYCDATDVGISCVCRWSNKEGRSCRIERNFHCWAPGKVVPKVRKDHTFVFSDVNMRPSTGEGNDPDIWAGLVVFEFFPINQQTKCLNDRFTVTRCGVRVINVATGNTSLENISLVLSLDPVEVSGYEVLRVSYDDLQEMDKVLFLYIASLFNDEDVDFVAPLIAGIDLDVSSGLKVLADVSLISVSSNGEIVMHSLQRQMGKEILHGQSMLLSDCESSMTENLSDVPKKEKKHRESKVKKVVSIPAIDEGDLWTWRKYGQKDILGSRFPRGYYRCAYKFTHGCKATKQVQRSETDSNMLAITYLSEHNHPRPTKRKALADSTRSTSSSICSAITTSASSRVFQNKDEPNQPHLPSSSTPPRNAAVLFKMTDMEEFQDNMEVDNDVVDTRTLALFPEFQHQPEEEDPWSTFFDDYNFYF
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Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Acts also as a disease resistance protein involved in resistance to fungal and bacterial pathogens, including R.solanacearum, P.syringae pv. tomato and C.higginsianum. RRS1 mediated resistance depends on salicylic acid and NDR1 (AC O48915).
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E1BB50
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CDK12_BOVIN
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Cyclin-dependent kinase 12 (EC 2.7.11.22) (EC 2.7.11.23) (Cell division protein kinase 12)
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MPNPERHGGKKDGSGGASGTLQPSSGGGSSNSRERHRLGSKHKRHKSKHSKDMGLVTPEAAPLGTVIKPLVEYDDISSDSDTFSDDLAFKVDRRENDERRGTDRSDRLHKHRHHQHRRTRDLLKTKQTEKEKNLEASSKSGSTKDRISGSSKRSNEENDDHGKAQISKSSNKESRSSKLHKEKTRKERELKSGHKDRSKSHRKRETPKSYKTVDSPKRRSRSPHRKWSDSPKQDDSPSGASYGQDYDLSPPRSHTSSNYDSYKKSPGSTSRRQSISPPYKEPSAYQSSTRSPSPYSRRQRSVSPYSRRRSSSYERSGSYSGRSPSPYGRRRSSSPFLSKRSLSRSPLPSRKSMKSRSRSPAYSRHSSSHSKKKRSGSRSRHSSISPVRLPLNSSLGAELSRKKKERAAAAAAAKMDGKESKGSPIFLPKKENSSVEAKDSGLEPKKLPRGVKLEKSAPDTELVNVTHLNTEVKNSLDTGKVKLDENSEKHPVLKDTKVQGTKDSKPVALKEEIVTPKETETSEKETLPPLPTVTSPPPLPTTTPPPQTPPLPPLPPLPAIPQQPPLPPPQPTFSQVLSSSTSTLPPSVHPRTSTLSSQANSQPSVQVSVKTQVSVTAAIPHLKTSTLPPLPLPPLLLGDDDMDSPKETLPSKPVKKEKEQRPRHLLTDLPLPPELPGGDPSPPDSPEPKAITPPQQPYKKRPKICCPRYGERRQTESDWGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLIHRSVVNMKEIVTDKQDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSGQIKLADFGLARLYNSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLPYFNTMKPKKQYRRRLREEFSFFFLPWGALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVELSKMDPPDLPHWQDCHELWSKKRRRQRQSGVLVEEPPPPKASRKETISGTSAEPVKNSSPAPPQPAPGKVEPGAGDAIGLGDITQQLNQSELAVLLNLLQSQTDLSIPQMAQLLNIHSNPEMQQQLEALNQSISALTAATSQQQDSEPTAPEESLKEIAPAPAVQPSAEQTTPEASSTPADMQNMLAVLLSQLMKTQEPAGNLEENNSDKNSGPQGPRRTPTMPQEEAAGKQTGHESH
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Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors (By similarity).
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E1BB52
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CDK13_BOVIN
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Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 2.7.11.23) (CDC2-related protein kinase 5) (Cell division cycle 2-like protein kinase 5) (Cell division protein kinase 13)
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MPSSSDTALGGGGGLSWAEKKLEERRKRRRFLSPQQPPLLLPLLQPQLLQPPPPPPPLLFLAAPGTAAAAAAAAAASSSCFSPGPPLEVKRLARGKRRAGGRQKRRRGPRAGQEAEKRRVFSLPQPQQDGGGGASSGGGVTPLVEYEDVSSQSEQGLLLGGASAATAATAAGGTGGSGGSPASSSGTQRRGEGSERRPRRDRRSSSGRSKDRHREHRRRDGQRGGGEASKSRSRHGHGGEERAEAGKSGSSSSSGGRRKSASATSSSSSSRKDRDPKAHRSRTKSSKEPPSAYKEPPKAYREDKTEPKAYRRRQRSLSPLGGRDDSPVSHRASQSLRNRKSPSPAGGGSSPYSRRLARSPSPYSRRRSPSYSRHSSYERGGDVSPSPYSSSSWRRSRSPYSPVIRRSAKSRSRSPYSSRHSRSRSRHRLSRSRSRHSSISPSTLTLKSSLAAELNKNKKARAAEAARAAEAAKAAEAAKAAEAAAKAAKAASTSTPTKGNTETGASASQTNHVKDVKKLKTEHAPSPSSGGTLKNDKAKTKPPLQVTKVDNNLIVDKATKKAVVVGKESKSAATKEEPVSLKEKTKPLTPSIGAKEKEQHVALVTSTLPPLPLPPMLPEDKDADSLRGNISVKAVKKEVEKKLRCLLADLPLPPELPGGDDLSKSPEEKKTATQLHNKRRPKICGPRFGEIKEKDIDWGKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIKLPYFNTMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVEPSKMPPPDLPLWQDCHELWSKKRRRQKQMGMTDDVSTVKAPRKDLSLGMDDSRTSTPQSVLPSSQLKPQGNSNAAPVKTGPGQQLNHSELAILLNLLQSKTSVNMADFVQVLNIKVNSETQQQLNKINLPAGILATGEKQTDPSTPQQESSKPLGGIQPSQNMQPKVEPDAAQAAVQSAFAVLLTQLIKAQQSKQKDVLLEERENGSGHEAPLQLRPPPEPATPASGQDDLIQHQDMRLLELTPEPDRPRILPPDQRPPEPPEPPPVTEEDLDYRTENQHVPTTSSSLTDPHAGVKAALLQLLAQHQPQDDPKRESGIDYQAGDTYVPSSDYKDNFGSSSFSSAPYVSNDGLGSASAPPLERRSFMGNSDIQSLDNYSTTSSHSGGPPQPSAFSESFPSSVAGYGDIYLNTGPMLFSGDKDHRFEYSHGPIAVLANSSDPSTGPESTHPLPAKMHNYNYGGSLQETPGGHGLMHGQTWTSPAQGPGYSQGYRGHISTSAGRGRGRGLPY
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Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis (By similarity).
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E1BD44
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BATF_BOVIN
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Basic leucine zipper transcriptional factor ATF-like (B-cell-activating transcription factor) (B-ATF)
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MPHSSDSSDSSFSRSPPPGKQDSSDDVRKVQRREKNRIAAQKSRQRQTQKADTLHLESEDLEKQNAALRKEIKQLTEEMKYFTSVLSSHEPLCSVLAPGAPSPPEVVYSTHAFHQPHVSSPRFQP
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AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells and class-switch recombination (CSR) in B-cells. Acts via the formation of a heterodimer with JUNB that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4 (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 (or IRF8) and activation of genes. Controls differentiation of T-helper cells producing interleukin-17 (Th17 cells) by binding to Th17-associated gene promoters: regulates expression of the transcription factor RORC itself and RORC target genes such as IL17 (IL17A or IL17B). Also involved in differentiation of follicular T-helper cells (TfH) by directing expression of BCL6 and MAF. In B-cells, involved in class-switch recombination (CSR) by controlling the expression of both AICDA and of germline transcripts of the intervening heavy-chain region and constant heavy-chain region (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic cell differentiation via interaction with IRF4 and IRF8 to mediate cooperative gene activation. Regulates effector CD8(+) T-cell differentiation by regulating expression of SIRT1. Following DNA damage, part of a differentiation checkpoint that limits self-renewal of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to differentiation of HSCs, thereby restricting self-renewal of HSCs (By similarity).
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E1BE10
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PLD6_BOVIN
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Mitochondrial cardiolipin hydrolase (EC 3.1.4.-) (Choline phosphatase 6) (Mitochondrial phospholipase) (MitoPLD) (Phosphatidylcholine-hydrolyzing phospholipase D6) (Phospholipase D6) (PLD 6)
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MRPLRWQVAVVAAAGLALALETLPAVLRWLWVRRRRPRREVLFFPSQVTCTEALLRSPGATPSGCPCSLPHGESSLSRLLSALLAARVSLELCLFAFSSPQLGRAVQLLHQRGVRVRVVTDCDYMALNGSQIGLLRKAGIQVRHDQDLGYMHHKFAIVDRKVLITGSLNWTTQAIQNNRENVLIVEDEEYVRLFLEEFERIWEEFNPTRFSFFPQKERAR
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Presents phospholipase and nuclease activities, depending on the different physiological conditions. Interaction with Mitoguardin (MIGA1 or MIGA2) affects the dimer conformation, facilitating the lipase activity over the nuclease activity. Plays a key role in mitochondrial fusion and fission via its phospholipase activity. In its phospholipase role, it uses the mitochondrial lipid cardiolipin as substrate to generate phosphatidate (PA or 1,2-diacyl-sn-glycero-3-phosphate), a second messenger signaling lipid. Production of PA facilitates Mitofusin-mediated fusion, whereas the cleavage of PA by the Lipin family of phosphatases produces diacylgycerol (DAG) which promotes mitochondrial fission. Both Lipin and DAG regulate mitochondrial dynamics and membrane fusion/fission, important processes for adapting mitochondrial metabolism to changes in cell physiology. Mitochondrial fusion enables cells to cope with the increased nucleotide demand during DNA synthesis (By similarity). Mitochondrial function and dynamics are closely associated with biological processes such as cell growth, proliferation, and differentiation. Mediator of MYC activity, promotes mitochondrial fusion and activates AMPK which in turn inhibits YAP/TAZ, thereby inducing cell growth and proliferation. The endonuclease activity plays a critical role in PIWI-interacting RNA (piRNA) biogenesis during spermatogenesis. Implicated in spermatogenesis and sperm fertility in testicular germ cells, its single strand-specific nuclease activity is critical for the biogenesis/maturation of PIWI-interacting RNA (piRNA). MOV10L1 selectively binds to piRNA precursors and funnels them to the endonuclease that catalyzes the first cleavage step of piRNA processing to generate piRNA intermediate fragments that are subsequently loaded to Piwi proteins. Cleaves either DNA or RNA substrates with similar affinity, producing a 5' phosphate end, in this way it participates in the processing of primary piRNA transcripts. piRNAs provide essential protection against the activity of mobile genetic elements. piRNA-mediated transposon silencing is thus critical for maintaining genome stability, in particular in germline cells when transposons are mobilized as a consequence of wide-spread genomic demethylation. PA may act as signaling molecule in the recognition/transport of the precursor RNAs of primary piRNAs. Interacts with tesmin in testes, suggesting a role in spermatogenesis via association with its interacting partner (By similarity).
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E1BFR5
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GWL_BOVIN
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Serine/threonine-protein kinase greatwall (GW) (GWL) (EC 2.7.11.1) (Microtubule-associated serine/threonine-protein kinase-like) (MAST-L)
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MEPTMGGEMESGGGAATGECVNRIPVPRPPSIEEFTIVKPISRGAFGKVYLGQKGNRLYAVKVVKKADMINKNMTHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNRDIDINMMDILTTPSMAKPRQDYSRTPGQVLSLISSLGFHTPVAEGNHDTANVLSTQVSETSPLSQGLTCPMSVDQKDTTPYSSKLLKSCPEMVASHPRMPVKCLTSHLLQSRKRLATSSTSSPSHTFISSMESECHSSPRWEKDCQESDDAAGSTMMSWNTVEKPLCTKSVDAMETKSFNERDLELALSPIHNSSVVPATGNSYVNLAKKCSSGEVSWEARELDVNNINMTADTSQYCFHESNQRAVDSGGMTEEHLGKRSCKRIFELVDSSPRQGIIPNKKSCFEYECSNEMRDCYATQRTGFAFEVQDLKLLVYRDQQNDCVNKENVGSSFTDKHQTPEKSPVPMIEKNLMCELDDDCDKNSKKDYLSSSFLCSDGDRTPKSIHMDSDSSFPGISIMESPLGGQSLDPDKNIKESSLEESNIEDLLPVSPSCQESTLPKGVECPTIQDSNQKMLAPSSEVLKPLTSKRNAVAFRSFNSHINASNSSEPSKMSITSLDMMDVSCAYSGSYPTAITPTQRERSDMPYQQTPNQVKSETPYRTPKSVRRGAAPVDDGRILGTPDYLAPELLLARAHGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILKRDIPWPEGEEKLSDNAQSAVDILLTIDDTKRAGMKELKHHPLFSGVDWENLQHQKMPFIPQPDDETDTSYFEARNNAQHLTVSGFSL
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Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and ENSA at 'Ser-62' and 'Ser-67', respectively. ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited (By similarity).
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E1BGN7
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CGAS_BOVIN
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Cyclic GMP-AMP synthase (cGAMP synthase) (cGAS) (EC 2.7.7.86) (2'3'-cGAMP synthase)
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MAPPRRKATRKASETASGVSAPCVEGGLSAEPSEPAAVPEAPRPGARRCGAAGASGSRREKSRLDPREKPQVRARAARAEDQAEGPAAPTADAEPPAAPGHSLPRASTRSRGTASSARARRPQSGPPEGPGLGPRAPSPHLGRREEAPGAWKPRAVLEKLKLSRQEISVAAEVVNRLGDHLLRRLNSRESEFKGVDLLRTGSYYERVKISAPNEFDLMFTLEVPRIQLEEYCNSSAHYFVKFKRNPKGSPLDQFLEGGILSASKMLFKFRKIIKEEIKHIEDTDVIMERKKRGSPAVTLLIRKPREISVDIILALESKSSWPASTQKGLPISNWLGTKVKDNLKRQPFYLVPKHAKEGSLFQEETWRLSFSHIEKAILTNHGQTKTCCETEGVKCCRKECLKLMKYLLEQLKKKFGKQRGLDKFCSYHVKTAFLHVCTQNPHDSWWLYKDLELCFDNCVTYFLQCLKTEHLEHYFIPDVLSKQIEYEQNNGFPVFDEF
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Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Catalysis involves both the formation of a 2',5' phosphodiester linkage at the GpA step and the formation of a 3',5' phosphodiester linkage at the ApG step, producing c[G(2',5')pA(3',5')p]. Acts as a key DNA sensor: directly binds double-stranded DNA (dsDNA), inducing the formation of liquid-like droplets in which CGAS is activated, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates STING1, thereby triggering type-I interferon production. Preferentially binds long dsDNA (around 45 bp) and forms ladder-like networks that function cooperatively to stabilize individual cGAS-dsDNA complexes. Acts as a key foreign DNA sensor, the presence of double-stranded DNA (dsDNA) in the cytoplasm being a danger signal that triggers the immune responses. Has antiviral activity by sensing the presence of dsDNA from DNA viruses in the cytoplasm. Also acts as an innate immune sensor of infection by retroviruses by detecting the presence of reverse-transcribed DNA in the cytosol (By similarity). Detection of retroviral reverse-transcribed DNA in the cytosol may be indirect and be mediated via interaction with PQBP1, which directly binds reverse-transcribed retroviral DNA. Also detects the presence of DNA from bacteria (By similarity). 2',3'-cGAMP can be transferred from producing cells to neighboring cells through gap junctions, leading to promote STING1 activation and convey immune response to connecting cells. 2',3'-cGAMP can also be transferred between cells by virtue of packaging within viral particles contributing to IFN-induction in newly infected cells in a cGAS-independent but STING1-dependent manner. Also senses the presence of neutrophil extracellular traps (NETs) that are translocated to the cytosol following phagocytosis, leading to synthesis of 2',3'-cGAMP (By similarity). In addition to foreign DNA, can also be activated by endogenous nuclear or mitochondrial DNA (By similarity). When self-DNA leaks into the cytosol during cellular stress (such as mitochondrial stress, DNA damage, mitotic arrest or senescence), or is present in form of cytosolic micronuclei, CGAS is activated leading to a state of sterile inflammation. Acts as a regulator of cellular senescence by binding to cytosolic chromatin fragments that are present in senescent cells, leading to trigger type-I interferon production via STING1 and promote cellular senescence. Also involved in the inflammatory response to genome instability and double-stranded DNA breaks: acts by localizing to micronuclei arising from genome instability. Micronuclei, which as frequently found in cancer cells, consist of chromatin surrounded by its own nuclear membrane: following breakdown of the micronuclear envelope, a process associated with chromothripsis, CGAS binds self-DNA exposed to the cytosol, leading to 2',3'-cGAMP synthesis and subsequent activation of STING1 and type-I interferon production (By similarity). In a healthy cell, CGAS is however kept inactive even in cellular events that directly expose it to self-DNA, such as mitosis, when cGAS associates with chromatin directly after nuclear envelope breakdown or remains in the form of postmitotic persistent nuclear cGAS pools bound to chromatin (By similarity). Nuclear CGAS is inactivated by chromatin via direct interaction with nucleosomes, which block CGAS from DNA binding and thus prevent CGAS-induced autoimmunity. Also acts as a suppressor of DNA repair in response to DNA damage: inhibits homologous recombination repair by interacting with PARP1, the CGAS-PARP1 interaction leading to impede the formation of the PARP1-TIMELESS complex (By similarity). In addition to DNA, also sense translation stress: in response to translation stress, translocates to the cytosol and associates with collided ribosomes, promoting its activation and triggering type-I interferon production (By similarity).
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E1BHJ4
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CP26B_BOVIN
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Cytochrome P450 26B1 (EC 1.14.13.-)
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MLFEGLELVSALATLAACLVSVTLLLAVSQQLWQLRWAATRDKSCKLPIPKGSMGFPLIGETGHWLLQGSGFQSSRREKYGNVFKTHLLGRPLIRVTGAENVRKILMGEHHLVSTEWPRSTRMLLGPNTVSNSIGDIHRNKRKVFSKIFSHEALESYLPKIQLVIQDTLRAWSSHPEAINVYQEAQKLTFRMAIRVLLGFSIPEEDLGHLFEVYQQFVENVFSLPVDLPFSGYRRGIQARQTLQKGLEKAIREKLQCTQGKDYSDALDILIESSKEHGKEMTMQELKDGTLELIFAAYATTASASTSLIMQLLKHPAVLEKLREELRAKGLLHSGGCPCEGTLRLDTLSGLHYLDCVIKEVMRLFTPVSGGYRTVLQTFELDGFQIPKGWSVMYSIRDTHDTAPVFKDVNVFDPDRFGQARSEDKDGRFHYLPFGGGVRTCLGKHLAKLFLKVLAVELASTSRFELATRTFPRITLVPVLHPVDGLSVKFFGLDSNQNKILPETEAMLSATV
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A cytochrome P450 monooxygenase involved in the metabolism of retinoates (RAs), the active metabolites of vitamin A, and critical signaling molecules in animals (By similarity). RAs exist as at least four different isomers: all-trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-dicis-RA, where atRA is considered to be the biologically active isomer, although 9-cis-RA and 13-cis-RA also have activity (By similarity). Catalyzes the hydroxylation of atRA primarily at C-4 and C-18, thereby contributing to the regulation of atRA homeostasis and signaling (By similarity). Hydroxylation of atRA limits its biological activity and initiates a degradative process leading to its eventual elimination (By similarity). Involved in the convertion of atRA to all-trans-4-oxo-RA. Can oxidize all-trans-13,14-dihydroretinoate (DRA) to metabolites which could include all-trans-4-oxo-DRA, all-trans-4-hydroxy-DRA, all-trans-5,8-epoxy-DRA, and all-trans-18-hydroxy-DRA (By similarity). Shows preference for the following substrates: atRA > 9-cis-RA > 13-cis-RA (By similarity). Plays a central role in germ cell development: acts by degrading RAs in the developing testis, preventing STRA8 expression, thereby leading to delay of meiosis. Required for the maintenance of the undifferentiated state of male germ cells during embryonic development in Sertoli cells, inducing arrest in G0 phase of the cell cycle and preventing meiotic entry. Plays a role in skeletal development, both at the level of patterning and in the ossification of bone and the establishment of some synovial joints. Essential for postnatal survival (By similarity).
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E1BJS7
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LIN41_BOVIN
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E3 ubiquitin-protein ligase TRIM71 (EC 2.3.2.27) (Protein lin-41 homolog) (RING-type E3 ubiquitin transferase TRIM71) (Tripartite motif-containing protein 71)
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MASFPETDFQICLLCKEMCGSPAPLSSNSSASSSSSQTSTSSGGGGGGPGAAARRLHVLPCLAFCRPCLEAHRGGAPGEPLKLRCPVCDQKVVLAEAAGMDARPSSAFLLSNLLDAVVATADEPPPKNGRAGAAAGAGGHGSNHRHHAHHAHPRAAASAPPPPLPPAPPPPAPPRSAPGGPAGSPSALLLRRPHGCSSCDEGNAASSRCLDCQEHLCDNCVRAHQRVRLTKDHYIERGPPGPAAAAAAAAAQQLGLGPPFPGAPFSLLSVFPERLGFCQHHDDEVLHLYCDTCSVPICRECTVGRHGGHSFVYLQEALQDSRALTIQLLADAQQGRQAIQLSIEQAQTVAEQVEMKAKVVQSEVKAVTARHKKALEERECELLWKVEKIRQVKAKSLYLQVEKLRQNLNKLESTISAVQQVLEEGRALDILLARDRMLAQVQELKTVRSLLQPQEDDRVMFTPPDQALYLAIKSFGFVSSGAFAPLTKATGDGLKRALQGKVASFTVIGYDHDGEPRLSGGDLMSAVVLGPDGNLFGAEVSDQQNGTYVVSYRPQLEGEHLVSVTLCNQHIENSPFKVVVKSGRSYVGIGLPGLSFGSEGDSDGKLCRPWGVSVDKEGYIVVADRSNNRIQVFKPCGAFHHKFGTLGSRPGQFDRPAGVACDASRRIVVADKDNHRIQIFTFEGQFLLKFGEKGTKNGQFNYPWDVAVNSEGKILVSDTRNHRIQLFGPDGVFLNKYGFEGALWKHFDSPRGVAFNHEGHLVVTDFNNHRLLVIHPDCQSARFLGSEGTGNGQFLRPQGVAVDQEGRIIVADSRNHRVQMFESNGSFLCKFGAQGSGFGQMDRPSGIAVTPDGMIVVVDFGNNRILIF
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E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance (By similarity). Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A (By similarity). In addition, participates in post-transcriptional mRNA repression in a miRNA independent mechanism (By similarity). Facilitates the G1-S transition to promote rapid embryonic stem cell self-renewal by repressing CDKN1A expression. Required to maintain proliferation and prevent premature differentiation of neural progenitor cells during early neural development: positively regulates FGF signaling by controlling the stability of SHCBP1 (By similarity). Specific regulator of miRNA biogenesis. Binds to miRNA MIR29A hairpin and postranscriptionally modulates MIR29A levels, which indirectly regulates TET proteins expression (By similarity).
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