entry
stringlengths 6
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stringlengths 5
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| protein_name
stringlengths 3
2.44k
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stringlengths 2
35.2k
| function
stringlengths 7
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H2KZZ2
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HLH30_CAEEL
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Helix-loop-helix protein 30
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MIRQLNSPGGGGGLGLNNPRAQQPPGAQQQQQPQQAQQQFYDDEPYQANASQFRFGAGKSMEQRRETGNLIPIAQRSMGSTSTPFGSAPTQSYFGGGSSGAALSSPRKMQQTHQMLFGNIQPPRGSPPSDGSDKIHRFGESPTPGGVGGVFGTELDDLIIDELMGMEDDQRMRPGATRPMTIGGEKTMSMARPIPGASSRAGSGHSGSPITIPNAMSNNFRQVVSSSAPTSSIDIEKMIGAVSNGGGNSGGDNDPEDYYRDRRKKDIHNMIERRRRYNINDRIKELGQMLPKNTSEDMKLNKGTILKASCDYIRVLQKDREQAMKTQQQQKSLESTAHKYADRVKELEEMLARQGVQVPPSHLPPIPKVIERPIKQEIDESPPNHTPTGSFVSSSGFLSEVTNNTAAMQITSPNDSRPNNFMNNSAPSDSFFSVGSASPPDYRTSSGTASWKLPGSNAFSDLMMDDLNPMMNGDPLISSAGAHPSPHFHSSQMSPDIHWDASGFSPDPINTQQSNSGHYHMDFS
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Transcription factor which regulates the expression of genes involved in lipid metabolism and autophagy in response to nutrient availability, bacterial pore-forming toxins or heat shock. Binds to the E-box motif 5'-CACGTG-3'. Under fasting conditions, binds to the promoter and activates the expression of lipase genes lipl-2, lipl-3 and lipl-5, and to a lesser extent, lipl-1, thereby regulating lipolysis. Involved in modulating longevity in response to TOR signaling, dietary restriction, germline signaling, heat shock and the insulin-like signaling pathway. Involved in the immune response to infection by the S.aureus bacterium, probably acting downstream of the protein kinase dkf-1, leading to the transcriptional activation of host defense genes. May also play a role in lysosomal biogenesis in response to nutrient availability.
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H2L002
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GCY7_CAEEL
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Receptor-type guanylate cyclase gcy-7 (EC 4.6.1.2)
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MKPFYSMSLVLFLVITLLPKPMFPQVATGTTGNVIRVGFIHCRDFQSAPITVGYRTSAAAASIAVDRLKRENLMSGWEFNFTIEFDDCVESEAAGMTVDLIEKHNVDVIIGPTMNQPTLAAFIVSNYFNRPIIAWGLVNAAQLDDFERFPNAGILSAGQRSLGVAIRAVLKRYEWSQFVYAYFTEEDTEKCVTMRNDLQQVVSYFGDIILAYSIQVADISNDGMIEALKKIQSRGRIIVTCMKDGIGLRRKWLLAAEEAGMIGDEYVYVFSDIKSKGYVVPLLGGGERPSWILSTGSDENDTRALKAFKQSIFICDMMGQGSIATNYTIFGQEIIARMKEAPYFCTKDCEGENFTVAATYAGQLHDAVYAYGVALDKMLKAGQIAQYRNATAFMRYFPQSFIGMSGNVTINEKGTRNPTLFLLALDENNNNTRMATIYVENMSATFNALYSDEGVMWASRKNNARPVDVPLCGFTGNLCPKSFVDEYLIWVIVAIVVLFLAITAAACGIYFSIQARRQEIERLNRLWQIPFIHLHQINSKQKGKGEHSVRSLQSGTSTLSSRTTVSFKTESRNFLFFSLQRESDYEPVVAKKHAYRPRLDDDKCTFMRSLRNLDQDNLNRFIGLCLDGPQMLSVWRFCSRGSIADVILKATIQMDNFFIYSLIKDMVHGLVFLHGSMVGYHGMLTSKCCLIDDRWQVKISNYGLQDLRSPEMYEKKDLLWSAPELLRAEDIKGSKEGDVYSLGIICAELITRKGVFNMEDRKEDPEEIIYLLKKGGLKSPRPDLEYDHTIEINPALLHLVRDCFTERPSERPSIETVRSQLRGMNSSRNDNLMDHVFNMLESYASSLEEEVSERTKELVEEKKKSDVLLYRMLPKTVADKLKLGQTVEPETFEQVTIFFSDVVQFTTLASKCTPLQVVNLLNDLYTIFDGIIEKHDVYKVETIGDGYLCVSGLPHRNGNEHVRQIALMSLAFLSSLQFFRVPHLPSERINLRIGMNCGSVVAGVVGLTMPRFCLFGDAVNTASRMESNGKPGKIHVSAEANRMLHLVGGFDTESRGEVIIKGKGVMETFWLTGQGTGAVSGARHVSAKKVSKKMDEIHRQETLKSDEQLSD
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Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). Unlike other guanylate cyclases expressed in ASE neurons, may not play a role in chemotaxis responses toward salt ions in ASEL (ASE left) sensory neurons.
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H2L006
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TSP14_CAEEL
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Tetraspanin-14
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MPHRAPRRFMKTAPGACDWEQCLLMGSGEPTRARAVVSSSHKQRKPRQEISACLKWLVFLLNSIVFLVGVGILALGVYLFIKDFREVKLVDIILNPAILISIFGFSICVVSFFGFMGALRDNIFLLKCFAACVFLSYILVVAVTLVFFTLFYTDTTEGLSANWLLLYAVKNYHTNRNLAEIMDALQENLECCGVSSIAQGYRDWNMSYQFNCTNSNPQPEKCGVPFSCCRKSVISEAAGSSNPLLPAMRSLECWQNALTKRPGDLEHDIYTRGCLQPLRTLFESHAVHVGAFVALLIVPVCISVCLTNILAKQVDHQRYLLEREARRNDRRRKRDHNRRDQLNSLDLLEEGKFNNASANATRPRPPDIPPPLPPIEHVPRKKSRNASSSPTRKPKSAGVENAAARRKRTATTTRTPPAAAGPAPTPQATTTNRTHQWVLQQTDLVPQKSKS
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Functions redundantly with tsp-12 to regulate cell surface levels of the BMP type II receptor daf-4 (but not BMP type I receptor sma-6), probably by regulating endosomal sorting and recycling of receptors, preventing their targeting to degradative lysosomes. Together with tsp-12, regulates cell fate specification in the postembryonic mesodermal M lineage, body size, male development and vulva development, probably by positively modulating BMP-like Sma/Mab signaling. Together with tsp-12 involved in maintaining the structural and functional integrity of the endosomal network. Together with tsp-12, probably acts by modulating the activation of glp-1, Notch-like receptor, to regulate germline maturation. [Isoform a]: Functions redundantly with tsp-12 to regulate cell fate specification in the postembryonic mesodermal M lineage, body size, embryonic and vulva development. [Isoform b]: Functions redundantly with tsp-12 to regulate cell fate specification in the postembryonic mesodermal M lineage. Likely plays a complementary role in mesodermal development with tsp-14 isoform a, but may be more critical.
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H2L008
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ZTF16_CAEEL
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Zinc finger protein ztf-16
|
MDELNACTECGFTTTVFSEFQGHIEKHENEHSRSSSGEMSNSQTIEWGDGIQSSTPSPRSTPPSDPTPSPDSDEHLEHHISITEITNTLIKKEPGTKGQKTVHVCPHCNFTTCMSQHMKSHLEAHERHQGQMYQCDICKMQFSQKANMHRHRMRHSGVKPYECRFCKKRFFRKDQMQEHSMTHIKTGFGFDCPVSQCNMQFSQHNALRAHLEETHTISSTNPASCKRCNLMFANSRRLLLHFQTRHDDSESSPKKENTPKRKKLSNGNALPMDPANMSITEQLQRMVKSEFSPPNTDTSDNSTSSEFDKIPPSFPMANPDILLMCLNQMNQFNGFGENIPRPMLNIPNIPLPALHNIPAVAAIVKQDQVQLWSEQTSSSVSVSAPSPSEQSHSPPANESSLSLTEKEKSPTPEKEDEENVECCHCGMMFYDNTMYLLHKSLHSDGDPFKCALCGTQCGEKYMFTTHVIFADHSTQATTSA
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Positively regulates the expression of ver-1 in the amphid sheath glia of amphid sensory neurons. Together with ehn-3, plays a role in somatic gonad development and is required for proper gonadal primordium assembly and somatic gonad precursor cell morphology.
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H2L045
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TENSH_CAEEL
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Tensin homolog (EC 3.1.3.48) (C1 domain-containing phosphatase and tensin homolog) (Suppressor of vhp-1 deletion lethality protein svh-6)
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MAAAALCCASRKSNKYNNEAGYEVYTISEDQLRLKQKMKDRKEGVQVEYITSRLIVLSCTSETSERKFVESLLKASQQIQNAHNKHIRVWNVSQRRHDISSSLDAIPFGWPSETAPSLEKLCTICKNLDQWMLEHPLNIAVIFCKGGLERCAIVVNAFMRFNAISATDDSVDDRFSMQRFSERFLGPDGPPSYKRYLGYFSSLLSGRISVNSDPLYLHNIILTFFEPINVFLKIYERLVPVYQSKTVALNKSSKFEMDGSLKLRGDIFFKCIVAASSPGSSTRCLFTCQLNTCALELHPINSEGYSVVRLHKEELDLIFNDKKIDNRVTVELVVSHTSGPTTIATAAVQSVHSLLPRNNSYETFELAQDDETNRSRLEVEYSEIRKKSTKSSKSANPINNNQEEEMPVGPPVPPKPSTPIMNGERLGEYGVGGHIGNGDVVPERRGILPASLREKINQKKELEGRATPSIEPDLVGRDRYDKASRCFSYVPAKSMQEAFERPRRTSFSRAIEKRENSVENVSQEEVARTEIPQSYQQNDISTPAKWDEQVEDAKQSALLEELARAPSAMQHNYWGNGEVDNVQVVDQAQRAVITPTSTLQRRPKPPARSGSYRTLNDDAYCSDMDELCDPEYYLNYNSNTAPLPPPRRQEQHAGTRSVQLPRKKMNFDAVTDPLDDVLESTKRLGSAYSVGDVRGGQQQQQEQHNASNDFNFSNTLNNTPTDYRQHYRNRNCQSVTTPRNHHFSTPSREQEADAADTWLSGKLKKVRSKRDIDPDIVRRRTQEKMLLEELKDSAANNDENQHNLPNGHARGAGLQNIDPLAEFRREEERLRNTRSPYGEERWRGRMRGKPPTPPPRESSASPVNSLPRGTPAHHMDRQRHNQSVPLPMHHRQFDEDFDVNSLFNFSHDPRQQSTTLERGGRSLSRGARIQDAYYASQQDLSANNRFNSGQERVAAAIYRAETAHRDMYASGTINRAETPGRYFPENSAVLERSSTPSFPVSRATPLPFHPLLYNNGERGGSGHAAGGGGGGHNGYSTMNNRSASPRLFGGSSTLSRRSSVNSVDTSEIIHHHPLFVKDTSKYWYKPTISREQAINMLRDKPPGTFVVRDSNSFPGAFGLALKVSTPPPGVNPGDGSELVRHFLIEPSPKGVKLKGCNNEPVFGSLSALVYQHSITALALPTKLVLPDFDPAATPEHLSATQALLEQGAACNVVYVGSVDVESLTGNECVKRSIATCSQRAINGDSRAVSVHFKVSSQGVTLTDNTRKVFFRRHFNVQSVIFAGMDPIERRFENTRALGFHDGCIAQARLFAFVARIPSSSENACHVFAELEPEQPGSAVVNFINKVMLAQKNRS
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Probable phosphatase which regulates axon regeneration after injury by linking the svh-2 and integrin signaling pathways.
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H2L056
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UBXN3_CAEEL
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UBX domain-containing protein 3
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MDLTASLEDDQREKLRQYTEFTHQQDYEVAIGTLASLNWNLEQAIEAHLMQEDKNDDEDPEILETIPAAASGRNAGASSSSRFEPEVINIEDDEMPATRGRRRGRAVTPDETTTVDNQVKRLRIDDGSSSSSNGAATHHRGAAIPRQKRGQATEPTPSSSGSSSASFSSRRGTRANPVPPPNQEPAHPESARQNGGILASRHNNHNNQQNNHHHHHQRIPINPRRVDVFNVDSDEDDDSMAIAYEDDDDGVHEVHHSEVVARGSGPPNGRIPMIPDGFSSVSDALRNFVAIFSDRFCSTPQTQAFMPPFYTEPLPAAVKEAFDHPNSEHRRPLLFYINHDRSIAANIFASQVLCSETVSTLIRHQYVLFPWDITSDSNLMLFLEYLQAANMGDVRTIIQRLAMSKIESFPLMAIVVKERNSYRLVDYCRGTDTSDQVMEKLLSGVSEYSDIRMNEQSERREREEREAIRNQQEAEYKASLAADKARMEAKQQEIEEQRLEEERKLREEEEECVRRQTVASTVPEEPPASAPLAEIINVKFRLPEGGQDMRRFRRLESIQTLINYLSSKGYSPDKFKYFNSDFPKKEITRHFDLSHNFADTKWPAREQIFVEEI
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Ubiquitin-binding protein which acts as an adapter for ATPase cdc-48.1 and/or cdc-48.2, conferring substrate specificity. Together with ubxn-1 and ubxn-2, plays a role in hermaphrodite spermatogenesis probably by promoting the degradation of sex determination terminal factor tra-1. During mitosis, ensures the degradation of DNA licensing factor cdt-1 and the disassembly of the DNA replication CMG helicase complex by promoting the dissociation from chromatin of several of its components including cdc-45 and sld-5.
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H2L099
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GCK1_CAEEL
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Germinal center kinase 1 (EC 2.7.11.1)
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MTTTSSDELPRQADDDSMKWDRIYIQKLDPEVIFTKQERIGRGSFGEVYKGIDNRTGRVVAIKIIDLEQAEDEIEDIQQEIQVLSQCDSQYVTKYFGSFLKGSKLWIIMEYLGGGSALDLTKSGKLDESHIAVILREILKGLEYLHSERKIHRDIKAANVLVSEHGDVKVADFGVAGQLTETVKKRITFVGSPFWMAPELIKQSSYDYKADIWSLGITAIELANGEPPHSDLHPMRVLFLIPKNPPPVLQGSQWSKPFKEFVEMCLNKDPENRPSASTLLKHQFIKRAKKNSILVDLIERAAEYRLRTGVSSDSDLDEDSDGGGGTSKWDYPTVRGPRVSADDDGTVRQRTDRPRAQVDRRSPSGSPGGTIVRGSPQVAAVAEQLRNSSVGSSGYGSGGNSASSQYATSSLPQSHTASSGGATTITLGSPNGSPTSSLARTQSMVSPSGQRSGSAQSWELERGNRPMSERVSSQVSPSKYNQHRTSSSNGVQGGSGGRREYINGSGSGLNGNSSNQNHSEYSDAVRQRGPGGSGGRLDYRESHVPTSSQENLNHGRMYGYGAPPPSREANNVPMPRVKGALDCSLLPAIEHLSRTRHATAALDQLRHVFRDVEDSCPGICNELIEELMQRIAVPQVSQSDLDAAIRRLTTPPS
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Serine/threonine-protein kinase which is required for normal oogenesis and suppression of germline cell apoptosis. Inhibits phosphorylation and thus probably activation of mpk-1 during pachytene stage. Involved in excretory canal elongation during postembryonic development, probably acting downstream of ccm-3.
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H2L0G5
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PTC3_CAEEL
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Protein patched homolog 3
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MSFPDEETDLLSEAKHCIRNVIHRTHRKFLENRLIGNFDSEDFSDAWKKKFAHAPTWCDADMSLQQIKRGKAVGNTVALTARAFFQLWLFRIGCFVQRWAWSTIFISLFLYCLCLGGLRHVTIETDLVKLWVSEGGRLNEEMGYLGQVKFERESGHLVHKVKRAVEQTTEPPAPAVKAEVRRGPELPKENGLGGGFQVVIQTPSFDGQNILSKEALQQHTKLMEEISTYEVKMFNETWTLSDICFKPPGPSFNSGPLAGIMSKLLDKIIPCIWITPIDCYWDGAKPLGPNPPLNLGPEVASFVSSLPPGNVTWKNLNPTSVIKEVGTLFDLGPIGNFFERAGIDGAYLDRPCIDPLEEECPKSAPNYFDRCHALTKFNEWNMAKAMSEQVTLERKIIPKDDGKSDIAETILNDIFGKKRRKRQADTTTKKPATKKDEDYYEYEDDADYLAGIANSTIAKKNPEKEAKDLLCLEYGSSLLKWMQENPERLGEFLTKEEMPDYPNYGDVMTGGCKGFGKKIMEWPEDLIIGGIQRDNGKLVSAEALQSVFLVSGAYDVFARIKNDKTDSHPGLDRHHFQPWMAGEIISTWQRNFTKRLYSHELNRERRQFHPLASTSIADMLEEFSQFNYIIIVIGYILMVIYAAFTQGRFQGWWLAVQSNVALAICGVILVTISSICGLGFATHLGINFNAATTQVVPFLSLGLGIDDMFLLLHNYDEIINICNKNEIGVLLKETGMSVMLTSINNILAFISGYVLPIPALRSFCSQTAILLAFNLIFLMFIFPAMIGIDLRRQRKGKRDLAYCSRGNPQMATSQSVPSNVSNMSSRAELAGYEKQADEYKRHEPWYTVGGFLNKIYIPALKNNVVKACVLIGTTTAVVFGLYGMYTSTLGLELADVLPEHTPPAAFLRAREQYFSFYPMFAVLRGDKLDIPNQQQLIEEYRAQLGSSKFMIKAEGKLQPYWMSMLRVWLQSLDMALEKDLAAGKFDLTNGNPIKVNGEKPSPESMIAARLVCSFGTNYNCDGRLGKMKMVENEVINPEGFYNYLTGWFNVDNMMYYVSQASFYPTPPGWEYNEKLAKVVPAAEPLLYSQMPFYQNDLIDTPAIVKMIEEIRATCEEYSERGLSNHPSGIAFTFWEQYLTLRWNLFQAICIIALAVFCVISILMFNPWAATLIMCIVVITTIELGGFMGLMGIKMNPISAVTLICAVGIGVEFTAHVELAFLTALGTIDQRLESCLQHMFVPVYHGAISTFLGVVMLVFSEFDFVVTYFFYTMTLLVALGVFNGLCVLPVILTLVGPKPELTPTDGSSVLPPPPPLRQQYAEKSGGVEGGMRKRKEKRPAEVEMSARDSPSTSSASHSSDDESSPAHK
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Regulates osmosis during embryonic development. Required for larval development and in particular is involved in larval molting.
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H2L0N8
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ARL13_CAEEL
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ADP-ribosylation factor-like protein 13B (ADP-ribosylation factor-like protein 13)
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MTEKSWFETIFCCCCHRTPIIRREIKLGCFGIGSAGKTTFLKVLKGEDPRDLLRTNGFSTVKMEYDETFHLTIYDVGGDKGIRGIWSNYYAEVHGIIYVIDYSTDETFTESIEALHSLTSNPHVQKKPIFLLLNNQNNREFDDVEISNETKIQAGQHKIVLFSHFNKYNGYLDNIKSATLTVMARAKKDRNEYQEQFVRFIDSISEHYVELSEGVKTAELALRIRQEEAKEQRRLMQMKVEHDALKADVAGLELRNQPPVQPPIPPDPPSDPKSASVHIEESPPMSLASSTIPSDIIQSTPETGTPRDPVNFCRISQTSTKPVSPESNSVKEEPTIILKDNYFLPPKAPGRQYSRIQRIQNVLNNRVVPK
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Cilium-specific protein required to control the microtubule-based, ciliary axoneme structure. Required for normal sensory cilium function. May act by maintaining the association between IFT subcomplexes A and B.
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H2L0Q3
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GABR1_CAEEL
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Gamma-aminobutyric acid type B receptor subunit 1
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MFVRSSWLLLWGTIVWASAEPVTLHIGGTFPMESGSGGWAGGEACLPAVEMALKDVNSRLDILPGYVLNMTNHNSQCQPGLAMQQLYDFLYKPPTKLMLLTGCSPVTTVIAEAAPVWKLVVLSYGGSSPALSNRNRFPTLFRTHPSANMQNPTRIHIMEKFKWKRFTILMSVEEVFVTTAKDLEAIARKKGIKVDRQSFYGDPTDAMKTLQRQDARIIVGLFYVTEARKVLCQAYHHGLYGRRYVWFFIGWYADTWYIPPPEEHLNCTAEQMTEAAEYHFTTESVMLSRDNIPAISEMTGMQFQQRLTQYFQKDTANVGGFPEAPLAYDAVWALALAFNCTRNNLPSHIRLENFTYDNKVIADTLFQCVKNTSFRGVSGKVMFSDSGDRIARTQIEQMQGGKYKIMGYYDTTSGDLEWYNKEQWLNGKGPPPDSTVIKKHAMTVSNEFYYPTILFAVLGIAACVFIYLFTQKHHERLIIFQSQPECNNILLIGCSLCLFSLFLIGLPSDDISISESLFPLLCHARVTILLFGFTFAYGSMFAKVWIVHRMGATENQQLASRQKDEEENTPWEGIRTLISTMVGRQALMRKSSGQAYGALLEKRNTVLNQPISSSKFYVIVAALTAVDVFVCFVWVLIDPLHLTEQKFPLFTPADSEEDEMIMPVLQQCQSNQQEVWIGIIMGFKCLLLVFGTFLSYETRNLKLRFINDSRFVGLAIYNVAVMTLVTAPVVTLLIHGKVDANFAFISLTVLICTYISVGLIYGPKIRHIIKVPPSADEIQLNGNVGPGVMSKVDQKRYDMLKKENETLQIQIEEKERKIHECKERLEELTKNSETEDMNAQLLCENDKQIADENLTYSTATTLTTTIPLIDLQNGNHPGQIYENDNDDDGSSTSSDEILL
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Component of a heterodimeric G-protein coupled receptor for GABA, formed by gbb-1 and gbb-2 (By similarity). Within the heterodimeric GABA receptor, only gbb-1 seems to bind agonists, while gbb-2 mediates coupling to G proteins (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (By similarity). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (By similarity). Calcium is required for high affinity binding to GABA (By similarity). Plays a critical role in the fine-tuning of inhibitory synaptic transmission (By similarity). Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (By similarity). Along with gbb-2, may couple to the G(o)-alpha G-protein goa-1 to negatively regulate cholinergic receptor activity in the presence of high levels of acetylcholine in ventral cord motor neurons. As acetylcholine depolarizes body wall muscles, modulation of acetylcholine levels most likely results in the control of locomotory behavior. Acts in neurons to regulate lifespan, and this may be through G-protein-egl-8/PLC-beta signaling to the transcription factor daf-16/FOXO.
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H2LBU8
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YAP1_ORYLA
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Transcriptional coactivator YAP1 (Yes-associated protein 1) (Protein hirame) (Protein yorkie homolog) (Yes-associated protein YAP65 homolog)
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MDPSQHNPPVGHQIVHVRGDSETDLEALFNAVMNPKGAVVPQSVPMRMRKLPDSFFKPPEPKSHSRQASTDAGSGGVLTPHHVRAHSSPASLQLGAVSGGSLSGMASAGASPQHLRQSSYEIPDDVPLPPGWEMAKTSSGQRYFLNHIDQTTTWQDPRKALLQLNQATPPSTVPVQQQNLLSPASGPLPEGWEQAITPEGEIYYINHKNKTTSWLDPRLETRYALNQQRITQSAPVKQGGPLPPNPHGGVMGGNNQMRLQQMEKERIRLKQQELLRQSQRPQIDLQPSTANQDAEHCDELALRNQLPTSMDQDGSSNPVSSPMAQDARTMTANSNDPFLNSVSSGTYHSRDESTDSGLSMSSYSVPRTPDDFLNSVDEMDTGDPLAPSMATQPSRFPDYLDTIPGTDVDLGTLEGESMAVEGEELMPSLQEALSSDILNDMESVLAATKIDKESFLTWL
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Transcriptional regulator which can act both as a coactivator and a corepressor and is the critical downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis (By similarity). Plays a key role in tissue tension and 3D tissue shape by regulating cortical actomyosin network formation.
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H2LNR5
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ABCB7_ORYLA
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Iron-sulfur clusters transporter ABCB7, mitochondrial (ATP-binding cassette sub-family B member 7, mitochondrial)
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MAPMLVSLNCGIRVQRRTLTLLIRQTSSYHIWDKSCINNGTNYQRRRTYALNSLHPQRTASWSTNRTENRRQILEAAKHLQVTDKRTCWHGNAGGRLNADPKNVLKEVHSAKILSAMLSYVWPKDRPDLRARVAVSLGLLAGAKLTNVMVPFMFKYAVDELNQMSGHMLNLNDAPSTVATMTTAVLIGYGVSRAGSALFNELRNTVFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTVFEMFLVSAILYYKCGGEFAAVALGTLSAYTIFTILVTQWRTRFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGYLKLYESSSLKTTSTLAMLNFGQSAIFSVGLTAIMLLASKGIAAGNMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLNVDTKIKEKDLAPPLAVTPQDATIRFEDVYFEYMEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYISGQNIRDVSLESLRKALGVVPQDAVLFHNNIFYNLQYGNINATPEEVYQVARLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSITEENIMTSMKEMVKDRTSVFIAHRLSTIVDADEILVLSQGKVAERGTHQALLDTPGSLYAELWNAQNSKILNSRKSSSAPAAERLSQKEEERKKLQEEILNSVKGCGNCSC
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Exports glutathione-coordinated iron-sulfur clusters such as [2Fe-2S]-(GS)4 cluster from the mitochondria to the cytosol in an ATP-dependent manner allowing the assembly of the cytosolic iron-sulfur (Fe/S) cluster-containing proteins and participates in iron homeostasis (By similarity). May play a role in iron and lipid metabolism.
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H2LRU7
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PKD2_ORYLA
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Polycystin-2 (Polycystic kidney disease 2 protein homolog)
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MSATRVRPQSQAGTDKPPRTLDSSEGIEMENIQHQDPGLGGVAGSPSPPSRQAWSRDNPVFEPEEEIMQADWPQASPGRRSAFTASGGSSCSSGHGGYTRAGSSTQIPRGGLYPTQTLNGQQQDRHEHPGCMKRIFQNIRILWGTELMEDGDSNRERYLWNVLRELLTYIAFLITICILTYGMISTNMYYYTKAMSQLFLDAPLSSENPKTFRSLSTMEDFWKYTQGPFLGGMYWEVWYNNQSLPGNQSFIYYENILLGVPRLRQVRVHNETCSIHEDLRDEVQGCYGVYTPSNEDNSPFGPQNGTAWVHTTESKMNASTHWGQVSKYGGGGYYQDLSRTREESGLQLQFLKDHLWLDRGTRAIFLDFSVYNGNVNLVCIARLLVEFPATGGVLTSWQFQTLRLIKYVSSWDYFVGVCEVAFCLFVLYYVVEEVLEIHIHRLHYFKNLWNCLDVLIVTLSVVAIIMSITRAAMGGDLLKGLENYTSHTSFDSLANLQVQFNNMAAVIVFFCWVKLFKFINFNKTMSQLSTTMSRCAKDLVGFAIMFFIIFLAYAQLAYLVFGTQVNDFSTFQGSVFTQFRIILGDFDFFEIKEANPVLGPIYFITFVLFIFFILMNMFLAIINDTYSEVKADMAQHRSEMEMTDFIKKGCTKALVKLRLKKTTVDDISDSLRQAGGKLNYDELLQDLKEKGHTEAEIQAIFAKYDQDGDLELTEHDHQQMRDDLEKEREDLDLERNSLTRPSSGRSFPRTQDDSEEDDDEDSGHSSRRRGSSSGGVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEGMERAKLKRRDVLVRLLDGVMEDERLGRDADTHREQMERLVKEELERWETDDVASQVSHPQPATPIGPRPRPPSSLSTDGLDTSANGGTHV
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Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B. Can also form a functional, homotetrameric ion channel (By similarity). Functions as non-selective, voltage-gated cation channel. Required for normal oscillation of Ca(2+) levels within cilia these oscillations of the intraciliary Ca(2+) levels can trigger cytoplasmic Ca(2+) signaling cascades (By similarity). May contribute to the release of Ca(2+) stores from the endoplasmic reticulum (By similarity). Plays a role in fluid-flow mechanosensation: forms a complex with pkd1l1 in cilia to facilitate flow detection in left/right patterning. Required for normal specification of the body left-right axis during embryogenesis.
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H2N0D4
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AMY_ORYLA
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Alpha-amylase (EC 3.2.1.1)
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MKLFVLIALFGLGFAQHNPNTRDGRTAIVHLFEWRWADIAAECERFLGPKGFAGVQISPPNEHILVSSPWRPWWQRYQPISYNLCSRSGGENELRDMITRCNNVGVNVYVDAVINHMCGAGGGEGTHSSCGSWFNANNKDFPSVPYSNLDFNDGKCKTGSGNIENYGDPYQVRDCRLVGLLDLALEKDYVRGKVADFMNKLIDMGVAGFRVDACKHMWPGDLDNVYRRLNNLNTKWFPGGSRPFIFQEVIDLGGEPITTGEYVGLGRVTEFKYGARLGELFRKWNGQKLSYTKNWGEGWGFMADGNAVVFTDNHDNQRGHGAGGASILTFWDPRLYKMAVGYMLAHPYGFTRVMSSYSWDRNFVNGKDENDWIGPPSNGDGSTKPVPINPDQTCGDGWVCEHRWRQIMNMVQFRNVVNGQPHANWWDNGNNQVAFGRGNRGFIVFNNDDWALDVTLNTGLPGGTYCDVISGNKDGGSCTGKQITVGGDGRAHFYINNSEEDPFIAIHADSKL
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Catalyzes the hydrolysis of alpha-1,4 glycosidic linkages in starch, glycogen and similar oligosaccharides.
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H2Q5A1
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SCNNA_PANTR
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Amiloride-sensitive sodium channel subunit alpha (Alpha-NaCH) (Epithelial Na(+) channel subunit alpha) (Alpha-ENaC) (Nonvoltage-gated sodium channel 1 subunit alpha) (SCNEA)
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MSSIKGNKLEEQGPRPLQPTPGLMEGNKLEEQDSSPPQSTPGLMKGDKREEQGLGPEPAAPQQPTAEEEALIEFHRSYRELFEFFCNNTTIHGAIRLVCSQHNRMKTAFWAVLWLCTFGMMYWQFGLLFGEYFSYPVSLNINLNSDKLVFPAVTICTLNPYRYPEIKEELEELDRITEQTLFDLYKYSSFTTLVAGSRSRRDLRGTLPHPLQRLRVPPPPHGARRARSVASSVRDNNPQVDWKDWKIGFQLCNQNKSDCFYQTYSSGVDAVREWYRFHYINILSRLPETLPSLEKDTLGNFIFACRFNQVSCNQANYSHFHHPMYGNCYTFNDKNNSNLWMSSMPGINNGLSLMLRAEQNDFIPLLSTVTGARVMVHGQDEPAFMDDGGFNLRPGVETSISMRKETLDRLGGDYGDCTKNGSDVPVENLYPSKYTQQVCIHSCFQESMIKECGCAYIFYPRPQNVEYCDYRKHSSWGYCYYKLQVDFSSDHLGCFTKCRKPCSVTSYQLSAGYSRWPSVTSQEWVFQMLSRQNNYTVNNKRNGVAKVNIFFKELNYKTNSESPSVTMVTLLSNLGSQWSLWFGSSVLSVVEMAELIFDLLVITFLMLLRRFRSRYWSPGRGGRGAQEVASTLASSPPSHFCPHPTSLSLSQPGPAPSPALTAPPPAYATLGPRPSPGGSTGAGSSACPLGGP
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Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption of sodium in kidney, colon, lung and eccrine sweat glands. Also plays a role in taste perception.
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H2QII6
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RBP2_PANTR
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E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2)
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MRRSKADVERYIASVQGSTPSPRQKSIKGFYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDGRAKYWVERAAKLFPGSPAVYKLKEQLLDCEGEDGWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKRLKDAVAHCHEAERNIALRSSLEWNSCVVQTLKEYLESLQCLESDKSDWRATNTDLLLAYANLMLLTLSTRDVQESRELLESFDSALQSVKSLGGNDELSATFLEMKGHFYMHAGSLLLKMGQHSSNVQWRALSELAALCYLIAFQVPRPKIKLIKGEAGQNLLEMMACDRLSQSGHMLLNLSRGKQDFLREIVETFANKSGQSALYDALFSSQSPKDTSFLGSDDIGNIDVREPELEDLARYDVGAIRAHDGSLQHLTWLGLQWNSLPALPGIRKWLKQLFHHLPQETSRLETNAPESICILDLEVFLLGVVYTSHLQLKEKCNSHHSSYQPLCLPLPVCKQLCTERQKSWWDAVCTLIHRKAVPGNAAKLRLLVQHEINTLRAQEKHGLQPALLVHWAKCLQKTGSGLNSFYDQREYIGRSVHYWKKVLPLLKIIKKKNSIPEPIDPLFKHFHSVDIQASEIVEYEEDAHITFAILDVVNGNIEDAMTAFESIQSVVSYWNLALIFHRKAEDIENDALSPEEQEECKNYLRKTRDYLIKIIDDSDSNLSVVKKLPVPLESVKEMLKSVMQELEAYSEGGPLYTNGSLRNADSEIKHSTPSHTRYSLSPSKSYKYSPKTPPRWAEDQNSLLKMICQQVEAIKKEMQELKLNSSNSASPHRWPTENYGPDSVPDGYQGSQTFHGAPLTVATTGPSVYYSQSPAYNSQYLLRPAANVTPTKGPVYGMNRLPPQQHIYAYPQQMHTPPVQSSSACMFSQEMYGPPALRFESPATGILSPRGDDYFNYNVQQTSTNPPLPEPGYFTKPPIAAHASRSAESKTIEFGKTNFVQPMPGEGLRPSLPTQAHTTQPTPFKFNSNFKSNDGDFTFSSPQVVTQPPPAAYSNSESLLGLLTSDKPLQGDGYSGAKPIPGGQTIGPRNTFNFGSKNVSGISFTENMGSSQQKNSGFRRSDDMFTFHGPGKSVFGTPTLETANKNHETDGGSAHGDDDDDGPHFEPVVPLPDKIEVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQSILKAPGTNVATASNQAVRIVKEPTSHDNKDICKSDAGNLNFEFQFAKKEGSWWHCNSCSLKNASTAKKCVSCQNLNPSNKELVGPPLAETVFTPKTSPENVQDRFALVTPKKEGHWDCSICLVRNEPTVSRCIACQNTKSANKSGSSFVHQASFKFGQGDLPKPINSDFRSVFSTKEGQWDCSACLVQNEGSSTKCAACQNPRKQSLPATSIPTPASFKFGTSETSKTLKSGFEDMFAKKEGQWDCSSCLVRNEANATRCVACQNPDKPSPSTSVPAPASFKFGTSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCVACQNPGKQNQTTSAVSTPASSETSRAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCIACQSPGKQNQTTSAVSTPASSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCIACQCPSKQNQTTAISTPASSEISKAPKSGFEGMFIRKGQWDCSVCCVQNESSSLKCVACDASKPTHKPIAEAPSAFTLGSEMKLHDSPGSQVGTGFKSNFSEKASKFGNTEQGFKFGHVDQENSPSFMFQGSSNTEFKSTKEGFSIPVSADGFKFGISEPGNQEKKSEKPLENDTGFQAQDISGQKNGSGVIFGQTSSTFTFADLAKSTSGEGFQFGKKDPNFKGFSGAGEKLFSSQYGKMANKANTSGDFEKDDDAYKTEDSDDIHFEPVVQMPEKVELVTGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRLLLDIPLQTPHKLVDTGRAAKLIQRAEEMKSGLKDFKTFLTNDQTKVTEEENKGSGTGAAGASDTTIKPNPENTGPTLEWDNYDLREDALDDSVSSSSVHASPLASSPVRKNLFRFGESTTGFNFSFKSALSPSKSPGKLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLPDLVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWLWTAYDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTAQEKDSLITPHVSRSSTPRESPCGKIAVAVLEETTRERTDVTQGDDVADAASEVEVSSTSETTTKAVVSPPKFVFGSESVKSIFSSEKSKPFAFGNTSATGSLFGFSFNAPLKSNNSETSSVAQSGSESKVEPNKCELSKNSDIEQSSDSKVKNLSASFPTEESSINYTFKTPEKAKEKKKPEDSPSDDDVLIVYELTPTAEQKALATKLKLPPTFFCYKNRPDYVSEEEEDDEDFETAVKKLNGKLYLEGSEKCRPLEENTADNEKECIIVWEKKPTVEEKAKADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELQKVQEAQKSQTEEITSTTDSVYTGGTEVMVPSFCKSEEPDSITKSISSPSVSSETMDKPVDLSTRKEIDTDSTSQGESKIVSFGFGSSTGLSFADLASSNSGDFAFGSKDKNFQWANTGAAVFGTQSVGTQSAGKVGEDEDGSDEEVVHNEDIHFEPIVSLPEVEVKSGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQNLMKLQKGHVSLAAELSKETNPVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGEKGFGFKNSIFHRVIPDFVCQGGDITKHDGTGGQSIYGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFFITLKKAELLDFKHVVFGFVKDGMDTVKKIESFGSPKGSVCRRITITECGQI
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E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB. Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (By similarity). Binds single-stranded RNA (in vitro). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity.
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H2QL32
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PDE9A_PANTR
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High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A (EC 3.1.4.35)
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MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCCQEGQRIPPEREELIQSVLAQVAEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLFCVHDNYRNNPFHNFRHCFCVAQMMYSMVWLCSLQENFSQMDILILMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNIFSNIPPDGFKQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIMLQPLWESRDRYEELKRIDDAMKELQKKTDSLTSGATEKSRERSRDVKNSEGDCA
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Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart. Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein. In brain, involved in cognitive function, such as learning and long-term memory.
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H3BCW1
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ADPRS_LATCH
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ADP-ribosylhydrolase ARH3 (ADP-ribose glycohydrolase ARH3) (LchARH3) (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-)
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MSAVGRLAAVSLAQVRGALCGALLGDCMGAEFEGSDAVELPDVLEFVRLLEKEKKAGTLFYTDDTAMTRAVIQSLIAKPDFDEVDMAKRFAEEYKKEPTRGYGAGVVQVFKKLLSPKYSDVFQPAREQFDGKGSYGNGGAMRVASIALAYPNIQDVIKFARRSAQLTHASPLGYNGAILQALAVHFALQGELKRDTFLEQLIGEMERIEGGEMSASDAGEHDRPNEVKLPFCSRLKKIKEFLASSNVPKADIVDELGHGIAALESVPTAIYSFLHCMESDPDIPDLYNNLQRTIIYSISLGGDTDTIATMAGAIAGAYYGMDQVTPSWKRSCEAIVETEESAVKLYELYCKQLKTP
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ADP-ribosylhydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine and threonine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose. Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds (By similarity). Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos. Also hydrolyzes free poly(ADP-ribose) in mitochondria (By similarity). Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins (By similarity). Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers (By similarity).
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H3BV60
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TGR3L_HUMAN
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Transforming growth factor-beta receptor type 3-like protein (TGF-beta receptor type-3-like protein) (TGFR-3L) (Transforming growth factor-beta receptor type III-like protein) (TGF-beta receptor type III-like protein)
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MLGTVLLLALLPGITTLPSGPPAPPFPAAPGPWLRRPLFSLKLSDTEDVFPRRAGPLEVPADSRVFVQAALARPSPRWGLALHRCSVTPSSRPAPGPALALLREGCPADTSVAFPPPPPPSPGAARPARFSFRLRPVFNASVQFLHCQLSRCRRLRGVRRAPAPLTPPPPPPPSRCLPQDEACADTGSGSAEGLAADGPHLHTLTQPIVVTVPRPPPRPPKSVPGRAVRPEPPAPAPAALEPAPVVALVLAAFVLGAALAAGLGLVCAHSAPHAPGPPARASPSGPQPRRSQ
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Expressed in gonadotrope cells, acts as an inhibin B coreceptor and regulates follicle-stimulating hormone (FSH) levels and female fertility.
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H3JQW0
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OTEMO_PSEPU
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2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase (OTEMO) (EC 1.14.13.160) ((2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA 1,5-monooxygenase) (MO2)
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MSNRAKSPALDAVVIGAGVTGIYQAFLINQAGMKVLGIEAGEDVGGTWYWNRYPGCRLDTESYAYGYFALKGIIPEWEWSENFASQPEMLRYVNRAADAMDVRKHYRFNTRVTAARYVENDRLWEVTLDNEEVVTCRFLISATGPLSASRMPDIKGIDSFKGESFHSSRWPTDAEGAPKGVDFTGKRVGVIGTGATGVQIIPIAAETAKELYVFQRTPNWCTPLGNSPMSKEKMDSLRNRYPTILEYVKSTDTAFPYHRDPRKGTDVSESERDAFFEELYRQPGYGIWLSGFRDLLLNKESNKFLADFVAKKIRQRVKDPVVAEKLIPKDHPFGAKRVPMETNYYETYNRDNVHLVDIREAPIQEVTPEGIKTADAAYDLDVIIYATGFDAVTGSLDRIDIRGKDNVRLIDAWAEGPSTYLGLQARGFPNFFTLVGPHNGSTFCNVGVCGGLQAEWVLRMISYMKDNGFTYSEPTQAAENRWTEEVYADFSRTLLAEANAWWVKTTTKPDGSVVRRTLVHVSGGPEYRKRCEQVAYNNYNGFELA
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Involved in the degradation of (+)-camphor. Catalyzes the lactonization of 2-oxo-delta(3)-4,5, 5-trimethylcyclopentenylacetyl-CoA (OT-CoA), a key intermediate in the metabolism of camphor. 2-Oxocyclopentyl ethyl acetate is also a good substrate, as is 2-oxocyclohexyl ethyl acetate and methyl-substituted cyclohexanones, but free acid is a poor substrate.
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H3K2Y6
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MED12_ARATH
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Mediator of RNA polymerase II transcription subunit 12 (Protein CENTER CITY) (Protein CRYPTIC PRECOCIOUS)
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MQRYHAANCTSAVNNSAIGGASARDSGRADSSSIGNYSLNSRRPPPLTPYKLKCEKDGLNSRLGPPDFHPPTSNSPEENLTKEYVQFGYKETVDGLKESEEIILSQVHTFSKPVVHKCKEAVRKCLRAINESRALKRKAGQVYGVPLSGSLLCKPGFPEQRSCGEETKKRWIESLSQQHKRLRSLADNIPGYRRKTLFEVLIRNNVPLLRATWFIKVTYLNQVRPSPAAISSGTPDKTQASRCEQWTKDVIEYLQYLLDELLSRNSSFPAQQTRDRSPQMLYTGSMQKNSPASTSLYGEETSLHFKWWYMVRLLQWHHAEGLLFPNLIVDWVLKLLQEKEIFEILQLLLPIVYGVLESIVLSQTYVQSLVAIAVRFIQEPAPGGSDLVDNSRRAYTLSALIEMVRYLVLAAPDTFVASDFFPLPPSVAACGPNDVSYTSKAYENLEKLRSNSAEISAQFQGRGVLSRFEFLSFDYTISTIQRSADDLAKIASAGYPQHNVAKAVQALDKALSDGDIRAAYSYLFEDLCNGAVDEAWITDVSPCLRSSLRWIGAISTSFVCSVFFLIEWATCDFRDFRAGVPKDIKFSGRKDCSQVYLVIQLLKQKILGGEFTARKGKNCRNNFLGVSKPSGSMDAFESPGPLHDIIVCWIDQHEVHKGGAKRLQLLVFELIRSGIFNPIAYVRQLIVSGMIDVIQPAVDPERRMRHHRILKQLPGCFVHETLEEAQLFGGDKLSEAVRTYSNERRLLLRELLVEKGKYWNNLVLSDQKSKKISTSLSSVIFPRACNAKSNSKGPRKHTKSSVDIRELKERISALLQFPGMSCGVETPVRDEFQNSVKRSSGSVYSKMDQPEATPGCEDCRRAKRPKMNDEKSSCYQGNSPIASDEEDNWWIKKGSKTVESSLKVDPQIEITKQVPRGRQKMARKTQSLAQLQAARIEGSQGASTSHVCDNKVSCPHHGPGVEGENQKVVDVFRTSTPVDMVSVGNSLKQLQFVDKRSIAVWLTTAVRQLVEEPQKSSVRVGQFNRGAPVEEKNTIRWKLGADELYSILFLLDISLDLVSAVKFLLWLLPKANSTPSFAVQGGRNLVTVPRNVENNMCEIGEAILVSSLRRYENILLSADLVPEAMTALMNRAASLMSSNGKISGSAALVYTRYILKRYGSLPSVVEWHNNFKATSEKKLLSELDHTRSGNGEYGNPLGVPAGVDNPDDYLRKKISIGGARPSRVGLSMRDVLQRHVEEATHYLKKLIGTGTMKASLAEKNDDGYQVAQQIVVGLMDCIRQTGGAAQEGDPSLVSSAVSAIINSVGLSVARITDFSLGNIYQNHPSGVDSSNIARYILRIHITCLCLLKEALGERQSRVFEIALATESSTALTGVFAPVKGSRGQHQLSPESYDSNANNSTIDMSNGTGKMALSRATKITAAVSALVIGSITHGVITLERIVGLLRLKDYLDFVQFVRRTKSSSNGSARSMGASKVESPIEVYVHWFRLLVGNCKTVSEGLVLELVGESSVVAISRMQRMLPLKLVFPPAYSIIAFVLWRPFVSNSNSNSSVHEDTHRLYQSLTMAFHDVIKHLPFRDVCFRDTQGLYELIVADSTDAEFASVFESHGLDMHLKSVAFAPLRARLFLNSLIDCKVPSSGYSHEGVSEAKNRHQGNGTKLVDKLVSVLDCLQPAKFHWQWVELRLLLNEQALAEKLENHDMPLTDAIRSSCPTSEKPDASENEKNFIQILLTRLLVRPDAVPLFSEVVHLFGRSVEDSMLKQAEWFLAGQDVLFGRKTIRQKLIIVGESKGLPTKPQFWKPWGWCNSSSSDHITANKAGKKRKFEITSIEEGEVIEEGSGSRKVLLPRVLDENSPSVGYGITTERAFVQLVLPCIDQSSDESRSTFVNELVRQFSNIEQQLSSVTNRSTTSNKQMGTASSGSEISSNKGSTRKGLRGGSPSLARRSSANTTDTSPPPSPAALRASMSLRLQFLLRLLPVICGEPSFKNTRHALASTIVRLLGSRVVYEDYAVCSPRSELSKAETESTIDPSSMADLSSEVLFDRLLFVLHGLLSNHQPKWLKPRPSSNESSKDFTLFDRDAAESLQNELSRMQLPDTIRWRIQAAMPILLPSLRCSLSCQPHSVPPTALTLVQPSGSTAAAGTNQRNSPAISKSGTAAAQGKLKPTMLAPHQQQEADNTDVVDPWTLLEDGTSSGLSSSNASNSSDMANLRATCWLKGAVRVRRTDLTYVGSVDDDS
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Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Flowering regulator which suppresses FLC expression, promotes FT and TSF expression and up-regulates SOC1 and FUL mainly in an FT-dependent manner under long-day conditions. Involved in diverse developmental aspects through gene regulation and modulation of the auxin response. Acts closely together with MAB13. Involved in the regulation of embryo patterning and cotyledon organogenesis by transiently repressing a transcriptional program that interferes with this process.
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H6U1I8
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GLIP_TANCI
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GDSL lipase (TcGLIP) (EC 3.1.1.-) (Pyrethrin type I synthase)
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MAVASRKLGALVLVAVLCLSLPTGCLSSQQAAALFIFGDSVFDPGNNNHINTHVNFKANFWPYGQSYFSSPTGRFSDGRIIPDFIAEYASLPIIPAYLEPNNDFTHGANFASAGAGALIASHAGLAVGLQTQLRYFGDLVDHYRQNLGDIKSRQLLSDAVYLFSCGGNDYQSPYYPYTQEQYVDIVIGNMTNVIKGIYEKGGRKFGVVNVPLIGCWPGMRAKQPGNTCNTEVDELTRLHNQAFAKRLEQLEKQLEGFVYAKFDLSTAILNRMKNPSKYGFKEGESACCGSGPFGGNYDCGRIKEFGLCDNATEYFFFDPFHPNELASRQFAEMFWDGDSMVTQPYNLKALFEGKPSTKYLPNDEL
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Component of the monoterpenoid pyrethrins biosynthesis pyrethrins are widely used plant-derived pesticide. Acyltransferase that catalyzes the esterification of terpene acids and lipid alcohol substrates into pyrethrins mediates the transfer of a chrysanthemoyl moiety from the coenzyme A (CoA) thio-ester chrysanthemoyl CoA to pyrethrolone, and, to a lower extent, to jasmololone and cinerolone thus producing pyrethrins (e.g. pyrethrin type I). Can also use pyrethroyl CoA as substrate. Has also esterase activity, being able to cleave the ester bond of pyrethrin I, p-nitrophenyl butanoate and p-nitrophenyl octanoate to produce pyrethrolone and p-nitrophenol, respectively.
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H6WZF2
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TER_NICAL
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Terpineol synthase, chloroplastic (EC 4.2.3.111) (1,8-cineol synthase, chloroplastic) (EC 4.2.3.108) (Beta-myrcene synthase) (EC 4.2.3.15) (Limonene synthase) (EC 4.2.3.-) (Sabinene synthase) (EC 4.2.3.-)
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MNTEPSPNHYSAISSSDQNLTRRSGNYQPTMWDFEYIQSIHNDYAGDKYMKRFNELKEEMKKMIMAEGSQELEKLELIDNLQRLGVSYHFKHEIMQILSSIKQHSTPADSLYATALKFRLLREHGFHISQEIFDGLSETHTKDTKGMLYLYEASFLATEGESELEQAWTEKHLREYLKNKNIDQNVAKLVHRALELPLHWRMLRLEARWFISFYKKRQDMIPLLLELAILDFNIVQAAHIQDLKYVARWWKETGLAENLPFARDRLVENFFWTIGVNFLPQYGYFRRIETKVNALVTTIDDVYDVFGTLDELQCFTDAIQRWNTDELDNLPDNMKMCYFALDDFINEVACDALIVPYLRNAWTDLCKSYLIEAKWYFSKYIPTMEEYMDNAWISISAPVILVHAYFLIANPVNKEALHYLRNYHDIIRWSALILRLANDLGTSSDELKRGDVPKSIQCYMNEKKVSEEEARQHIRLLISETWKKLNEAHNVAAHPFPKMFVKSAMNLARMAQCMYQHGDGHGGQNSETQNRIMALLFESIPPA
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Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products of the 'cineole cassette', volatile compounds present in floral scent. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into alpha-terpineol and, as minor products, sabinene, beta-myrcene, limonene and 1,8-cineole.
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H7FWB6
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IBP_FLAFP
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Ice-binding protein (Antifreeze protein) (AFP) (FfIBP)
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MKILKRIPVLAVLLVGLMTNCSNDSDSSSLSVANSTYETTALNSQKSSTDQPNSGSKSGQTLDLVNLGVAANFAILSKTGITDVYKSAITGDVGASPITGAAILLKCDEVTGTIFSVDAAGPACKITDASRLTTAVGDMQIAYDNAAGRLNPDFLNLGAGTIGGKTLTPGLYKWTSTLNIPTDITISGSSTDVWIFQVAGNLNMSSAVRITLAGGAQAKNIFWQTAGAVTLGSTSHFEGNILSQTGINMKTAASINGRMMAQTAVTLQMNTVTIPQ
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Has antifreeze activity for survival in a subzero environment. Binds to the surface of ice crystals and inhibits their growth. Has high thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point, and thus the freezing of the cell fluid can be prevented protecting the organism from ice damage. The TH activity of this protein is 2.2 degrees Celsius at 5 uM and 2.5 degrees Celsius at 50 uM.
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H8F0D7
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PRPC_MYCTE
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2-methylcitrate synthase (2-MCS) (MCS) (EC 2.3.3.5) (Citrate synthase) (CS) (EC 2.3.3.16)
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MTGPLAAARSVAATKSMTAPTVDERPDIKKGLAGVVVDTTAISKVVPQTNSLTYRGYPVQDLAARCSFEQVAFLLWRGELPTDAELALFSQRERASRRVDRSMLSLLAKLPDNCHPMDVVRTAISYLGAEDPDEDDAAANRAKAMRMMAVLPTIVAIDMRRRRGLPPIAPHSGLGYAQNFLHMCFGEVPETAVVSAFEQSMILYAEHGFNASTFAARVVTSTQSDIYSAVTGAIGALKGRLHGGANEAVMHDMIEIGDPANAREWLRAKLARKEKIMGFGHRVYRHGDSRVPTMKRALERVGTVRDGQRWLDIYQVLAAEMASATGILPNLDFPTGPAYYLMGFDIASFTPIFVMSRITGWTAHIMEQATANALIRPLSAYCGHEQRVLPGTF
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Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA.
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H8WR05
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BFAT_VARPD
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Beta-phenylalanine transaminase (EC 2.6.1.-) (Aromatic beta-amino acid aminotransferase) (Beta-phenylalanine aminotransferase) (VpAT)
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MTHAAIDQALADAYRRFTDANPASQRQFEAQARYMPGANSRSVLFYAPFPLTIARGEGAALWDADGHRYADFIAEYTAGVYGHSAPEIRDAVIEAMQGGINLTGHNLLEGRLARLICERFPQIEQLRFTNSGTEANLMALTAALHFTGRRKIVVFSGGYHGGVLGFGARPSPTTVPFDFLVLPYNDAQTARAQIERHGPEIAVVLVEPMQGASGCIPGQPDFLQALRESATQVGALLVFDEVMTSRLAPHGLANKLGIRSDLTTLGKYIGGGMSFGAFGGRADVMALFDPRTGPLAHSGTFNNNVMTMAAGYAGLTKLFTPEAAGALAERGEALRARLNALCANEGVAMQFTGIGSLMNAHFVQGDVRSSEDLAAVDGRLRQLLFFHLLNEDIYSSPRGFVVLSLPLTDADIDRYVAAIGSFIGGHGALLPRAN
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Aminotransferase that acts exclusively on beta-amino acids and exhibits a broad substrate range in vitro, accepting meta-, para- and, to a lesser extent, ortho-substituted beta-phenylalanine derivatives as amino donors, and 2-oxoglutarate or pyruvate as amino acceptors. Is highly enantioselective toward (S)-beta-phenylalanine (is not active with (R)-beta-phenylalanine) and derivatives with different substituents on the phenyl ring, allowing the kinetic resolution of various racemic beta-amino acids to yield (R)-beta-amino acids with >95% enantiomeric excess (ee). Highly prefers aromatic beta-amino acids over aliphatic beta-amino acids cannot use beta-alanine or beta-glutamate as substrate. Is likely involved in the beta-phenylalanine degradation pathway that allows V.paradoxus strain CBF3 to use beta-phenylalanine as a sole nitrogen source.
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H8ZM70
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LAS_ABIBA
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Bifunctional abietadiene synthase, chloroplastic (Abietadiene cyclase) (Diterpene synthase TPS1) (AbdiTPS1) (Levopimaradiene/abietadiene synthase) (AbLAS) [Includes: Abietadiene synthase (EC 4.2.3.18) (Levopimaradiene synthase) (EC 4.2.3.32) (Neoabietadiene synthase) (EC 4.2.3.132); Copalyl diphosphate synthase (EC 5.5.1.12)]
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QSIPHFSTTLNAGSSARKRRSLYLRWGKGSNKIIACVGEGATSVPYQSAEKNDSLYSSTLVKREFPPGFWKDDLIDSLTSSHKVAASDEKRIETLISEIKNMFRCMGYGETNPSAYDTAWVARIPALDGSDNPHFPETVEWILQNQLKDGSWGEGFYFLAYDRILATLACIITLTLWRTGETQVHKGIEFFRTQAGKMEDEADSHRPSGFEIVFPAMLKEAKILGLDLPYDLPFLKQIIEKREAKLKRIPTDVLYALPTTLLYSLEGLQEIVDWQKIMKLQSKDGSFLSSPASTAAVFMRTGNKKCLDFLNFVLKKFGNHVPCHYPLDLFERLWAVDTVERLGIDRHFKEEIKEALDYVYSHWDERGIGWARENPVPDIDDTAMGLRILRLHGYNVSSDVLKTFRDENGEFFCFLGQTQRGVTDMLNVNRCSHVSFPGETIMEEAKLCTERYLRNALENVDAFDKWAFKKNIRGEVEYALKYPWHKSMPRLEARSYIENYGPDDVWLGKTVYMMPYISNEKYLELAKLDFNKVQSIHQTELQDLRRWWKSSGFTDLNFTRERVTEIYFSPASFIFEPEFSKCREVYTKTSNFTVILDDLYDAHGSLDDLKLFTESVKRWDLSLVDQMPQQMKICFVGFYNTFNEIAKEGRESQGRDVLGYIQNVWKVQLEAYTKEAEWSEAKYVPSFNEYIENASVSIALGTVVLISALFTGEVLTDEVLSKIDRGSRFLQLMGLTGRLVNDTKTYQAERGQGEVASAIQCYMKDHPKISEEEALKHVYTVMENSLEELNREFVNNKIPDIYRRLVFETARIMQLFYMQGDGLTLSHDMEIKEHVKNCLFQPVA
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Involved in defensive oleoresin formation in conifers in response to insect attack or other injury. Involved in diterpene (C20) olefins biosynthesis. Bifunctional enzyme that catalyzes two sequential cyclizations of geranylgeranyl diphosphate (GGPP) to abietadiene. The copalyl diphosphate (CPP) intermediate diffuses freely between the 2 active sites in the enzyme.
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H9A1V3
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AAE1_CANSA
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Hexanoyl-CoA synthase (EC 6.2.1.-) (Acyl-activating enzyme 1) (CsAAE1)
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MGKNYKSLDSVVASDFIALGITSEVAETLHGRLAEIVCNYGAATPQTWINIANHILSPDLPFSLHQMLFYGCYKDFGPAPPAWIPDPEKVKSTNLGALLEKRGKEFLGVKYKDPISSFSHFQEFSVRNPEVYWRTVLMDEMKISFSKDPECILRRDDINNPGGSEWLPGGYLNSAKNCLNVNSNKKLNDTMIVWRDEGNDDLPLNKLTLDQLRKRVWLVGYALEEMGLEKGCAIAIDMPMHVDAVVIYLAIVLAGYVVVSIADSFSAPEISTRLRLSKAKAIFTQDHIIRGKKRIPLYSRVVEAKSPMAIVIPCSGSNIGAELRDGDISWDYFLERAKEFKNCEFTAREQPVDAYTNILFSSGTTGEPKAIPWTQATPLKAAADGWSHLDIRKGDVIVWPTNLGWMMGPWLVYASLLNGASIALYNGSPLVSGFAKFVQDAKVTMLGVVPSIVRSWKSTNCVSGYDWSTIRCFSSSGEASNVDEYLWLMGRANYKPVIEMCGGTEIGGAFSAGSFLQAQSLSSFSSQCMGCTLYILDKNGYPMPKNKPGIGELALGPVMFGASKTLLNGNHHDVYFKGMPTLNGEVLRRHGDIFELTSNGYYHAHGRADDTMNIGGIKISSIEIERVCNEVDDRVFETTAIGVPPLGGGPEQLVIFFVLKDSNDTTIDLNQLRLSFNLGLQKKLNPLFKVTRVVPLSSLPRTATNKIMRRVLRQQFSHFE
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Involved in the biosynthesis of cannabinoids-related terpenophenolic natural products, which have pharmacological activity. Acyl-activating enzyme that catalyzes the conversion of hexanoic acid to hexanoyl-CoA, precursor of the cannabinoid pathway. Can also activate other fatty acids including heptanoate, octanoate and nonanoate.
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H9BZ66
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ABCG1_PETHY
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ABC transporter G family member 1 (ABC transporter ABCG.1) (PhABCG1)
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MTNQLPNKVELAEVVPQNGGVFLTWEDLWVTASSVKDGSKAILKGLTGYAMPGELLAIMGPSGSGKSTLLDTIAGRLGSSTRQSGDILINGRRQTLAYGSSAYVTQDDTLLATLTIKEAVYYSAELQLPNSMSKSEKKEIADVTLKGMGLQDAMETRIGGWSGKGISGGQKRRVSICLEILTRPKLLFLDEPTSGLDSAASYYVMKAIASQCQGRTIIASIHQPSVDVFSLFHSLCLLSSGRTVYFGPASAANEFFALSGFPCPTLQNPSDHFLKTINSDFDQDIEEGSTRRKSTEEVIDILIKSYKASDKYNAVQSQVAEICQQEGEMLDKRSHASFITQSLVLTRRSFINMSRDLGYYWLRLAVYVVIAVGLGSLYYDVGFSAASVQARGSMLMFVASFITFMAIGGFPSFVEDMKVFQREKLNGHYGSGSFVIANTLSAMPYLLLVSLIPGAIAYFMTGLQNGFEHFIYFALVLFTCMMIVESLMMIVASMVPNFLMGLIAGAGIQALMLLSGGFFRLPNDLPKPFWKYPLHYVAFHKYAYEGMFKNEFEGLKIHDVNGEDILRNTWQMNMDYSKWIDLVILLGMLVLYRVLFLLVVKAGEIVKPAIRAFMSHSPNQINSAERPLDVFDS
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ABC transporter controlling the release of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26). This scent, mostly produced in the evening and night by the petals, attracts the pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta).
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H9J9M0
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CDA1_BOMMO
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Chitin deacetylase 1 (BmCDA1) (EC 3.5.1.41)
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MARYARVATLAACLLFACALADGHRWRRQADETAKKDESLEQELCKDKDAGEWFRLVAGEGDNCRDVIQCTASGIQAIRCPAGLFFDIEKQTCDWKDAVKNCKLKNKERKIKPLLYTEEPLCQDGFLACGDSTCIERGLFCNGEKDCGDGSDENSCDIDNDPNRAPPCDSSQCVLPDCFCSEDGTVIPGDLPARDVPQMITITFDDAINNNNIELYKEIFNGKRKNPNGCDIKATYFVSHKYTNYSAVQETHRKGHEIAVHSITHNDDERFWSNATVDDWGKEMAGMRVIIEKFSNITDNSVVGVRAPYLRVGGNNQFTMMEEQAFLYDSTITAPLSNPRLCPYTMYFRMPHRCHGNLQSCPTRSHAVWEMVMNELDRREDPSNDEYLPGCAMVDSCSNILTGDQFYNFLNHNFDRHYEQNRAPLGLYFHAAWLKNNPEFLEAFLYWIDEILQSHNDVYFVTMTQVIQWVQNPRTVTEAKNFEPWREKCSVEGNPACWVPHSCKLTSKEVPGETINLQTCLRCPVNYPWLNDPTGDGHY
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Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin.
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H9JW43
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CDA8_BOMMO
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Chitin deacetylase 8 (BmCDA8) (EC 3.5.1.41) (Chitin deacetylase 17)
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MKRLSVLCSLLLVAAALGTELPLATPCDEEACKLPDCRCSSTNIPGGLRARDTPQFVTVTFDDGINVINIETYREVLYGRSNSNRCPAGATFYVSHEYTNYQLVNELYNRGFEIALHSISHRTPQAFWADATYQNLVQEIGDQKRQMAHFASIPASAIKGVRIPFLQMSGNTSFQVMADFDLLYDCTWPTTALTNPGLWPYTLHHESIQDCIIPPCPTASIPGPWVLPMISWRDLNNFPCSMVDGCFFTPDRTDEEGWFKFILTNFERHYLGNRAPFGFFVHEWFISSNPAIKRAFVRFMDIINNLNDVFMVNSAEVIDWVKNPVPIDRYRQQQCKFTMPSICRPSFCGPLTGTHNQLSYYMTICNTCPRNYPWVGNPLGQ
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Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine (GlcNAc) residues in chitin. Shows activity towards the chitinous oligomers GlcNAc(3), GlcNAc(4), GlcNAc(5) and GlcNAc(6), but not GlcNAc or GlcNAc(2). Requires the substrate to occupy subsites 0, +1, and +2 for optimum catalysis.
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H9L427
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BIPA_SALTY
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Large ribosomal subunit assembly factor BipA (EC 3.6.5.-) (50S ribosomal subunit assembly factor BipA) (GTP-binding protein BipA) (Ribosome-dependent GTPase BipA)
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MIENLRNIAIIAHVDHGKTTLVDKLLQQSGTFDARAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAHGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIIYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPLQMQISQLDYNNYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRNAKVGKVLTHLGLERIDSNIAEAGDIIAITGLGELNISDTICDPQNVEALPALSVDEPTVSMFFCVNTSPFCGKEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGRKQEPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDIRPGEVGQRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVILVPPIKMSLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRRANRGQKEE
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A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA (By similarity). A ribosome-stimulated GTPase, GTPase activity increases 4 fold in the presence of 70S ribosomes. Binds 70S ribosomes in the presence of GTP or its non-hydrolyzable analog GMPPNP in the presence of ppGpp or under stress conditions it binds to 30S ribosomal subunits. {ECO:0000255|HAMAP-Rule:MF_00849, ECO:0000269|PubMed:18621905, ECO:0000269|PubMed:19803466}.
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H9L478
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PDUJ_SALTY
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Bacterial microcompartment shell protein PduJ (Bacterial microcompartment protein homohexamer) (BMC-H) (Propanediol utilization protein PduJ)
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MNNALGLVETKGLVGAIEAADAMVKSANVQLVGYEKIGSGLVTVMVRGDVGAVKAAVDAGSAAASVVGEVKSCHVIPRPHSDVEAILPKSA
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One of the major shell proteins of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. The isolated BMC shell component protein ratio for J:A:B':B:K:T:U is approximately 15:10:7:6:1:1:2. At least one of PduA or PduJ is required for BMC assembly it must be encoded as the first gene in the pdu operon. Required for structural integrity of BMCs and to mitigate propionaldehyde toxicity, probably joins facets responsible for BMC closure. Edge residues (particularly Lys-25) are important for function and assembly of the BMC. 80% identical to PduA although their pore regions appear structurally identical, unlike PduA plays no role in 1,2-PD diffusion into or out of the BMC shell. If pduJ is cloned in the chromosomal position of pduA it is able to complement a pduA deletion it then has a functional pore as it assumes the transport functions of PduA. Overexpression of this protein leads to aberrant filaments that extend the length of the cell, cross the cleavage furrow and impair division. The filaments form nanotubes with a hollow center. Modeling suggests PduJ is probably the hub for binding multiple enzymes to the interior of the BMC modeling suggests PduC, PduD, PduG and PduM are targeted to PduJ (Probable). The 1,2-propanediol (1,2-PD) degradation bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low.
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H9N289
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NDMA_PSEPU
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Methylxanthine N1-demethylase NdmA (EC 1.14.13.178) (1-methylxanthine demethylase)
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MEQAIINDEREYLRHFWHPVCTVTELEKAHPSSLGPLAVKLLNEQLVVAKLGDEYVAMRDRCAHRSAKLSLGTVSGNRLQCPYHGWQYDTHGACQLVPACPNSPIPNKAKVDRFDCEERYGLIWIRLDSSFDCTEIPYFSAANDPRLRIVIQEPYWWDATAERRWENFTDFSHFAFIHPGTLFDPNNAEPPIVPMDRFNGQFRFVYDTPEDMAVPNQAPIGSFSYTCSMPFAINLEVSKYSSSSLHVLFNVSCPVDSHTTKNFLIFAREQSDDSDYLHIAFNDLVFAEDKPVIESQWPKDAPADEVSVVADKVSIQYRKWLRELKEAHKEGSQAFRSALLDPVIESDRSYI
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Involved in the caffeine degradation, which is the essential first step for assimilating the carbon and nitrogen in caffeine. Catalyzes the N1-demethylation of caffeine to produce theobromine and formaldehyde. Also catalyzes the N1-demethylation of theophylline, paraxanthine, and 1-methylxanthine to 3-methylxanthine, 7-methylxanthine, and xanthine, respectively. NADH is the preferred substrate.
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H9T8G6
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CDIA9_BURPE
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tRNA nuclease CdiA (EC 3.1.-.-) (CdiA-E479) (Toxin CdiA)
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SLDTTGNVDLTSANVKAGSLDLNAGNKLILDTATQTTHQVSRDGATSDKTTLGPAANLNVAGDASIKTGGDFQQNAGNLNVGGNLNANIGGNWNLGVQQTGEHKVVQRANGVSDTDLNSATGSTVNVGGKSAIGVGGDLTAQGARLDFGQGGTVAAKGNVTFGAASTTSTINANSSGDQGNRSYAETRHGADQALTGTTVKGGDTLNVVSGKDINVIGSTIDLKKGDANLLAAGDVNVGAATETHVYNSRETHSRSGVVSGTKIASSQDATSTVANGSLISADGVSIGSGKDINVQGSTVVGTHDVALNAAHDVNITTSQDTSQSSTTYQEQHSGLMSGGGLSFSVGNSKLAQQNQSSSVTNNASTVGSVDGNLTVNAGNTLHVKGSDLVAGKDVTGTAANIVVDSATDTTHQAQQQQTSKSGLTVGLSGSVGDAINNAISETQAARESAKDSNGRASALHSIAAAGDVAFGGLGAKALLDGAKGPQAPSIGVQVSVGSSHSSMQSSEDQTIQRGSSINAGGNAKLIATGNGTPKDGNITIAGSNVNAANVALVANNQVNLVNTTDTDKTQSSNSSSGSSVGVSIGTNGIGVSASMQRAHGDGNSDAAIQNNTHINASQTATIVSGGDTNVIGANVNANKVVADVGGNLNVASVQDTTVSAAHQSSAGGGFTISQTGGGASFSAQNGHADGNYAGVKEQAGIQAGSGGFDVTVKGNTDLKGAYIGSTADASKNSLTTGTLTTSDIENHSHYSANSAGFSAGASVGVSTKAVGPSSVSGSGGVTPMVFQNDSGDQSATTKSAVSVGAINITKPGEQTQDVANLNRDATNLNGTVSKTPDVQKMLSQQADTMNAAQAAGQTVSQGIGLYADGKRKDAIDAAKAAYERGDLVAMQSYIDQAKSWDEGGASRAGLQATGGALIGGLGGGSVLTAIGGAAGAGTSSLLAGQAEKISKSVGDMTGSSLVGNIAANVAATVGGALVGGSAGAAMASNVELYNAGNDPQKTDDRATIAGLQGLLSRTAAMASDAKAGVWNGMVNVAGVIVNIPNGGPFASPGDPGYVSLDGLKKPYKSGTSIGPDTEFLTPILATLGLGGKAAVGTDAGITSADVATVGNGALKNASGDLSAAANSARNQPYGQGASASQSPGTQGASSGSNISASNGSSSPTTIVASNPVDLNAFDRLNVVDPAVGKFRPGEAGAAAELENYLGGTLQRAPQGSSVDFVFSSGPNNGKTVDFMLTPDTVAQAAKINQFFDKNLNNFMNTLSDHAAAADFVPLDSRFLSEANKTLLVKAIGNLPQKLQAKIILIK
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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. The C-terminal 160 residues (CT domain) acts as a general tRNA nuclease, and inhibits growth in E.coli upon overexpression. Cleaves specifically within the T-loop of E.coli tRNA2(Arg) (between the post-transcriptionally modified thymidine-T55 and pseudouridine-Y56) also degrades most other tRNAs. Cleaves unmodified tRNA(Gln) and tRNA(Asp), showing the universal post-translational tRNA modifications present in the T-loop are not required for CT activity. Inactive CT domain binds tRNA, probably in a complex with 4 CT domains and 4 tRNAs. Toxic activity is neutralized by coexpression of the cognate immunity protein CdiI in E.coli, but not by non-cognate immunity proteins from other strains of B.pseudomallei. 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 domain form a hairpin-like structure as the FHA-2, PT and CT domains are periplasmic. 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.
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H9TB17
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AOXA_CAVPO
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Aldehyde oxidase 1 (EC 1.2.3.1) (Azaheterocycle hydroxylase 1) (EC 1.17.3.-)
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MEPSTLYFYVNGRRVTEKNVDPETMLLPYLGRNLRLTGTKYGCGGGGCGACTVMVSRYDRGTGQIRHYPACACLTPLCSLHGAAVTTVEGVGSTRTRLHPVQERIAKSHGTQCGFCTPGMVMSLYALLRSHPQPSEEQLLEALAGNLCRCTGYRPILDAGKTFCKTSGCCQSKENGVCCLDQGVNGVQEAEGEQTSQELCSEEEFVPLDPTQELIFPPELMILAQKQPQKSRVFTGDRVTWISPVTLKDLLEAKAKNPRAPVVMGNTSVGPEMKFKGVFHPVIISPDGIEELSVIKQGNEGLTLGAGLSLAQVQDVLADVVQQLPEEKTQTLCALLKQLRTLAGSQIRNMASLGGHIMSRHLDSDLNPVLAAASCTLHVPSQEGDRQIPLDEHFLSRSPSADLRPQEVLLSVTIPYSRKWEFVSAFRQAQRKRSARAIVNVGMRVFFGAGDGVISELCILYGGVGPAIVCATDACRKLVGRHWTEEMLDEACRLVLGEVAIPGAAPGGRVEFRRTLLVSFLFRFYLQVSQSLSRMDPGRYPSLVGKYESALEDLCLGHHQRTFELQSADAKQLPQDPIGRPIMHLSGIKHTTGEAIYCDDMPLVDRELSLAFVTSSRAHAAILSMDLSEALSLPGVVDIVTAEHLGDANSFAKETLLATDKVLCVGHLVCAVIADSEVQAKRAAEKVKIVYQDLEPLILTIEEAIQHDSFFETERKLESGDVAEAFRTAEQVLEGSIHMGGQEHFYMETQSMLAVPKGEDQEIDLYVSTQFPTYIQEIVASTLKLPVNKVMCHVRRVGGAFGGKVGKTAILAAITAFAALKHCRAVRCILERGEDMLITGGRHPYLGKYKVGFRNNGQVVALDMEHYSNAGSTLDESLMVVEMGLLKMENAYKFPNLRCRGHACKTNLPSNTALRGFGFPQSGLITEACIVEVAARCGLSPEEVREVNMYRGTEQTHYGQEIHTQRLAQCWSECKAKATFSLRRAAVDRFNAGSPWKKRGLAMVPLKFPVGLGSVAMGQAAALVHVYLDGSVLLTHGGIEMGQGVHTKMIQVVSRELKMPMANVHLRGTSTETVPNANVSGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKEWAQAAFDQSISLSAIGYFRGYDADMDWEKGKGHPFEYFVYGAACSEVEIDCLTGNHKNIRTDIVMDVGRSINPALDLGQVEGAFIQGMGLYTSEELKYGPQGALYTRGPDQYKIPAVCDVPAELHVFFLPPSKNSNTLYSSKGLGESGVFLGCSVLFAIWDAVSAARRERGLPGTLALSCPLTPEKIRMACEDRFTKMIPRDTPGSYVPWDVVV
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Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. May also catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis.
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H9XP47
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MBDH_SERMA
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Meso-2,3-butanediol dehydrogenase (BDH) (meso-2,3-BDH) (EC 1.1.1.-) ((R,S)-butane-2,3-diol dehydrogenase) (NAD(H)-dependent meso-2,3-BDH) (SmBdh)
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MRFDNKVVVITGAGNGMGEAAARRFSAEGAIVVLADWAKEAVDKVAASLPKGRAMAVHIDVSDHVAVEKMMNEVAEKLGRIDVLLNNAGVHVAGSVLETSIDDWRRIAGVDIDGVVFCSKFALPHLLKTKGCIVNTASVSGLGGDWGAAYYCAAKGAVVNLTRAMALDHGGDGVRINSVCPSLVKTNMTNGWPQEIRDKFNERIALGRAAEPEEVAAVMAFLASDDASFINGANIPVDGGATASDGQPKIV
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Catalyzes the NAD-dependent oxidation of meso-2,3-butanediol to (3R)-acetoin, and of (2S,3S)-2,3-butanediol to (3S)-acetoin, with much lower efficiency. Can also oxidize several primary alcohols such as glycerol, 1-2-pentanediol and 1,2-propanediol, with lower activity. Cannot use (2R,3R)-2,3-butanediol. In the presence of NADH, catalyzes the reduction of (3R)-acetoin to meso-2,3-butanediol, of (3S)-acetoin to (2S,3S)-2,3-butanediol and of diacetyl to (3S)-acetoin. No activity is detected with NADPH/NADP(+).
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I0DEB3
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NDB4D_VAEMS
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Amphipathic peptide VmCT1 (CT1) (Non-disulfide-bridged peptide 4.13) (NDBP-4.13) (Non-disulfide-bridged peptide 5.13) (NDBP-5.13)
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MKTQFVILIVAVVLLQLISHSEAFLGALWNVAKSVFGKRGLRNFDDLDDTFEPEMSEADLKYLQDLLR
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Cationic amphipathic peptide with antibacterial activities against both Gram-positive and Gram-negative bacteria. Also shows antifungal activities. Is mildly hemolytic against human erythrocytes. In addition, when tested in vitro on the parasite Trypanosoma cruzi (responsible of the Chagas disease), is able to reduce the number of the three forms (epimastigote, trypomastigote and amastigote). Also shows antiplasmodial and cytotoxic activity (tested on Plasmodium gallinaceum, and MCF-7 breast cancer cell line).
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I0DF35
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L_SFTS
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RNA-directed RNA polymerase L (Protein L) (EC 2.7.7.48) (Large structural protein) (Replicase) (Transcriptase) [Includes: cap-snatching endonuclease (EC 3.1.-.-)]
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MNLEVLCGRINVENGLSLGEPGLYDQIYDRPGLPDLDVTVDATGVTVDIGAVPDSASQLGSSINAGLITIQLSEAYKINHDFTFSGLSKTTDRRLSEVFPITHDGSDGMTPDVIHTRLDGTIVVVEFTTTRSHNIGGLEAAYRTKIEKYRDPISRRVDIMENPRVFFGVIVVSSGGVLSNMPLTQDEAEELMYRFCIANEIYTKARSMDADIELQKSEEELEAISRALSFFSLFEPNIERVEGTFPNSEIEMLEQFLSTPADVDFITKTLKAKEVEAYADLCDSHYLKPEKTIQERLEINRCEAIDKTQDLLAGLHARSNKQTSLNRGTVKLPPWLPKPSSESIDIKTDSGFGSLMDHGAYGELWAKCLLDVSLGNVEGVVSDPAKELDIAISDDPEKDTPKEAKITYRRFKPALSSSARQEFSLQGVEGKKWKRMAANQKKEKESHDALSPFLDVEDIGDFLTFNNLLADSRYGDESVQRAVSILLEKASAMQDTELTHALNDSFKRNLSSNVVQWSLWVSCLAQELASALKQHCRAGEFIIKKLKFWPIYVIIKPTKSSSHIFYSLGIRKADVTRRLTGRVFSETIDAGEWELTEFKSLKTCKLTNLVNLPCTMLNSIAFWREKLGVAPWLVRKPCSELREQVGLTFLISLEDKSKTEEIITLTRYTQMEGFVSPPMLPKPQKMLGKLDGPLRTKLQVYLLRKHLDCMVRIASQPFSLIPREGRVEWGGTFHAISGRSTNLENMVNSWYIGYYKNKEESTELNALGEMYKKIVEMEEDKPSSPEFLGWGDTDSPKKHEFSRSFLRAACSSLEREIAQRHGRQWKQNLEERVLREIGTKNILDLASMKATSNFSKDWELYSEVQTKEYHRSKLLEKMATLIEKGVMWYIDAVGQAWKAVLDDGCMRICLFKKNQHGGLREIYVMDANARLVQFGVETMARCVCELSPHETVANPRLKNSIIENHGLKSARSLGPGSININSSNDAKKWNQGHYTTKLALVLCWFMPAKFHRFIWAAISMFRRKKMMVDLRFLAHLSSKSESRSSDPFREAMTDAFHGNREVSWMDKGRTYIKTETGMMQGILHFTSSLLHSCVQSFYKSYFVSKLKEGYMGESISGVVDVIEGSDDSAIMISIRPKSDMDEVRSRFFVANLLHSVKFLNPLFGIYSSEKSTVNTVYCVEYNSEFHFHRHLVRPTLRWIAASHQISETEALASRQEDYSNLLTQCLEGGASFSLTYLIQCAQLLHHYMLLGLCLHPLFGTFMGMLISDPDPALGFFLMDNPAFAGGAGFRFNLWRACKTTDLGRKYAYYFNEIQGKTKGDEDYRALDATSGGTLSHSVMVYWGDRKKYQALLNRMGLPEDWVEQIDENPGVLYRRAANKKELLLKLAEKVHSPGVTSSLSKGHVVPRVVAAGVYLLSRHCFRFSSSIHGRGSTQKASLIKLLMMSSISAMKHGGSLNPNQERMLFPQAQEYDRVCTLLEEVEHLTGKFVVRERNIVRSRIDLFQEPVDLRCKAEDLVSEVWFGLKRTKLGPRLLKEEWDKLRASFAWLSTDPSETLRDGPFLSHVQFRNFIAHVDAKSRSVRLLGAPVKKSGGVTTISQVVRMNFFPGFSLEAEKSLDNQERLESISILKHVLFMVLNGPYTEEYKLEMIIEAFSTLVIPQPSEVIRKSRTMTLCLLSNYLSSRGGSILDQIERAQSGTLGGFSKPQKTFIRPGGGVGYKGKGVWTGVMEDTHVQILIDGDGTSNWLEEIRLSSDARLYDVIESIRRLCDDLGINNRVASAYRGHCMVRLSGFKIKPASRTDGCPVRIMERGFRIRELQNPDEVKMRVRGDILNLSVTIQEGRVMNILSYRPRDTDISESAAAYLWSNRDLFSFGKKEPSCSWICLKTLDNWAWSHASVLLANDRKTQGIDNRAMGNIFRDCLEGSLRKQGLMRSKLTEMVEKNVVPLTTQELVDILEEDIDFSDVIAVELSEGSLDIESIFDGAPILWSAEVEEFGEGVVAVSYSSKYYHLTLMDQAAITMCAIMGKEGCRGLLTEKRCMAAIREQVRPFLIFLQIPEDSISWVSDQFCDSRGLDEESTIMWG
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RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (By similarity). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are not polyadenylated. During replication, the polymerase binds the 5' and 3' vRNA extremities at distinct sites. In turn, significant conformational changes occur in the polymerase and in vRNA to initiate active RNA synthesis (By similarity). As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated (By similarity).
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I0IUP3
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MCM8_CHICK
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DNA helicase MCM8 (EC 3.6.4.12) (Minichromosome maintenance 8)
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MSRDLRGRGCPRGRGFQGWRGGWRGGWRGGWRGGWRGRTQKVEWKRAPEPASSRLVQSTLDQFIPYKGWKLYFSEAYADKSPFVQKTQAFEKFFMQRIELYDKDEIERKGSILVDYKELIEDRELTKSIPNISTELRDMPQKILQCMGLAIHQVLTKDLERHAAELQVQEGLPLDGEPIINVPLIHARLYNYEPLTQLKNVRANCYGKYIALRGTVVRVSNIKPLCTKLAFVCGTCGDVQSVPLPDGKYTLPTKCLVPECRGRSFTPDRSSPLTATVDWQSVKVQELMSDDQREAGRIPRTIECELVQDLVDSCVPGDVVTITGVVKVSSTEEGASKNKNDKCVFLLYIEANSVSNSKGQKTKNFEEETFQRSFMEFSLKDLYAVQEIQAEENLFRIIVNSLCPAIYGHEIVKAGLALALFGGCQKFVDDKNRIPVRGDPHVLIVGDPGLGKSQMLQAVCNVAPRGVYVCGNTSTSSGLTVTLSRDGASGDFALEAGALVLGDQGICGIDEFDKMGSQHQALLEAMEQQSISLAKAGIVCSLPARTSIVAAANPVGGHYNKAKTVSENLKMGSALLSRFDLVFILLDTPNEDHDHLLSEHVMAIRAGKQAVCSSAVVSRTNVQDRSVLEVVSDRPLLERLKISPGENFDAIPHQLLRKYVGYARQYVHPHLSPEAAQVLQEFYLELRKQNQGASSTPITTRQLESLIRLTEARSRLELREKCTKEDAEDVIEIMKYSMLGTYSDEFGKLDFERSQHGSGMSNRSQAKRFVSALSSIAERTYSNLFDLQQLRQVAKELQIRVFDFESFIESLNDQGYLLKKGSRLYQLQTM
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Component of the MCM8-MCM9 complex, a complex involved in homologous recombination repair following DNA interstrand cross-links and plays a key role during gametogenesis. The MCM8-MCM9 complex probably acts as a hexameric helicase required to process aberrant forks into homologous recombination substrates and to orchestrate homologous recombination with resection, fork stabilization and fork restart.
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I0IUP4
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MCM9_CHICK
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DNA helicase MCM9 (EC 3.6.4.12) (Minichromosome maintenance 9)
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MALRADQVSLIGQVFESYLLQHHRDDILGILRQGDDEAHYPVLVDALTLFETNMEIGEYFNAFPSQVLPIFDGALRRAAMAVLQAATPSPELRMKPNLHARISGLPICPELTREHIPKTRDVGHFLSVTGTVIRTSLVKVLEFERSYICNKCKHVFVAKADFEQYYAFCRPSACLNEEGCNSTKFTCLSGTSSSPSSCRDYQEIKIQEQVQRLSVGSIPRCMVVVLEDDLVDSCKSGDDITVYGVVMQRWKPFHQDARCDLELVLKANYVKVNNEQLAGVTIDEEVRKEFEDFWEKHRNNPLAGRNEILASLCPQVFGLYLVKLAVAMVLAGGVQRIDATGTRIRGESHLLLVGDPGTGKSQFLKYAVKITPRSVLTAGIGSTSAGLTVTAVKDFGEWNLEAGALVLADGGLCCIDEFNSIKEHDRTSIHEAMEQQTISVAKAGLVCKLNTRTTILAATNPKGHYDPAESVSVNIALGSPLLSRFDLVLVLLDTKNEEWDRIISSFILQNKGCPSKSEKLWSMEKMKTYFCLIKRIQPKLSDESNLILVRYYQMQRQSDCRNAARTTIRLLESLIRLAEAHARLMFRDTVTLEDAVTVVSVMESSMQGGALLGAINALHTSFPENPMTQYRMQCELILERLELHDLLHKELQRLDRLQKETYCQLQPEETSFSTITGCLNKNTFESKQKSQSEPSDQQKINSYPQPSLPKSNCEGDKHPEALRNPTPGNNISTKRLSRLNKRSDDGSLGWFDRLEDRNTDAEETFWKTSPLPKTSPDNMALKTMSKSSCSEEGNSSVPRKEDGMRGSLRTVTLCAPLEQDKVSEISSKRTEERKCFSSEANIQDPTSASASVQESVITQRVSKSLQRLHTEKSHRFFTSTQNSEANALPSVLPVSGLLDLSSDTDSVVGDENNSASAAVKHAVISMRKRSKGQAEKEAKAVSSHEPEITDGESPPAAKLAKFSFRPRTKLDDSSEKKNAEFPLFPSENTVKPGEQPQGEQLQKDCCPPEKRKMTLTCLGRKGLEKQSIGSKGNEEQLSQALGKEMGGNALIHSDVTLDVVSPPPTEKRREGEEKLGGPSTVRVCSSTLENLSKFCFASRPDSKSEAPPTIKTDTNNKESHSPLLKVHVSNPNKRKSFALGNASKDSVVTRKSLFSIAELDDATLDFDWD
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Component of the MCM8-MCM9 complex, a complex involved in homologous recombination repair following DNA interstrand cross-links and plays a key role during gametogenesis. The MCM8-MCM9 complex probably acts as a hexameric helicase required to process aberrant forks into homologous recombination substrates and to orchestrate homologous recombination with resection, fork stabilization and fork restart.
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I0J1I6
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BSR_PSETA
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Broad specificity amino-acid racemase (EC 5.1.1.10) (Arginine racemase) (Broad substrate specificity racemase)
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MPFSRTLLALSLGMALLQNPAFAAPPLSMTDGVAQVNTQDSNAWVEINKAAFEHNIRTLQTALAGKSQICAVLKADAYGHGIGLLMPSVIAMGVPCVGVASNEEARVVRESGFKGQLIRVRTAALSELEAALPYNMEELVGNLDFAVKASLIAEDHGRPLVVHLGLNSSGMSRNGVDMTTAQGRRDAVAITKVPNLEVRAIMTHFAVEDAADVRAGLKAFNQQAQWLMNVAQLDRSKITLHAANSFATLEVPESHLDMVRPGGALFGDTVPSHTEYKRVMQFKSHVASVNSYPKGNTVGYGRTYTLGRDSRLANITVGYSDGYRRAFTNKGIVLINGHRVPVVGKVSMNTLMVDVTDAPDVKSGDEVVLFGHQGKAEITQAEIEDINGALLADLYTVWGNSNPKILKDQ
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Amino-acid racemase able to utilize a broad range of substrates. Is mostly active with lysine and arginine and, to a lesser extent, with ornithine, whereas is about 10 times less active with alanine, methionine and ethionine. With phenylalanine as substrate only a trace activity is detectable, and is inactive with glutamate. Plays a key role in the catabolism of D-arginine and D-lysine, that allows P.taetrolens strain NBRC 3460 to grow on these basic D-amino acids as a sole carbon source.
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I1C083
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RLT1_RHIO9
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Mucoricin (EC 3.2.2.22) (Ricin-like toxin) (rRNA N-glycosidase)
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MYFEEGRLFFIKSQFNGRVLDVEDGSTEDDANIIVYTQKYEDCLNQLWRYENGYFINAKSAKVLDIRGGEMQPESQIIQYAQKMVEEAANQRWAIDEDGYIFCEARPDLVLDIQGAEDEDCVPVILYERREGEVSANQRWELVPFEG
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N-glycosylase that inhibits protein synthesis in the host by depurinating ribosomal rRNA, and thus acts as a ribosomal inactivating protein (RIP). Promotes vascular permeability in the host and induces necrosis and apoptosis of host alveolar epithelial cells.
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I1C4E4
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COTH2_RHIO9
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Invasin CotH2 (Spore coat protein homolog 2)
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MKLSLTIVSSSFLVAIAHAASVQFNLIAPSATDVKVSVNGQQVALTASDPNVPYFTGSAEVGGTEESFERSLAGITNSTFNDFYNRPVTYANLPQLPWPIENDPQWTRKGKKAEIFDDNYIPSVFFHGDDSQVQDLVKNVPKDKVTGTLTFIGSNYVHSFANVSFGIHGAGKKHNNAKQSWKWTLSGTDTMGNRNHFKLRHMEEDPTQIRERLYADILHAMGTYANETTMVRLFINGQGFGTFNMLDDITEFSYINAMFYGGNPPATLGPLFDGASGADFIYHPGNLDGYSSWKPNKDNANGEGYEAFDPLCKAWNETDYTDNTAIANFEKMFDTEHFLRFMVIEYLTAHWDGYWMGQTNDGAYRDPSDNNKWYFLDQDFDATFGVNLDVPENKDFISVSYKDFPSRYPAGVMANGLLQNADKKAKFEQYLTETVRVLFNNVTLTNRVLAIHNFLSPDLEWDRSIVQQSPGTNFGWTFEQTSQNLWQGVSAPNNNGGGAEWGLVEYIAAKSQAMAKEFNITIVSEPVGPPAANGTATSTNDGGNTHTAAGESKPASSSESSGSKIASQSVSGASRSAVSTVLLGVTALVATAIF
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Promotes invasion of host epithelial cells by adhering to receptors on the host cell surface to facilitate endocytosis of the pathogen into host cells. Binds HSPA5/BiP protein on the cell surface of host epithelial cells.
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I1CFE1
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COTH3_RHIO9
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Invasin CotH3 (Spore coat protein homolog 3)
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MKLSIISAAFLVAITHAASIKFNVIAPNATDVKVSVNGQQVTLTASDANVPYFTGSAEVGASKTYKYVAGGTEESFDRSLDGITNSTLNDFYNRPVTYANLPQLPWPIEKDPQWTRSGSKADIFDDNYIPSVFFHGDDSQVQNVVKNVPADRISGTLTFIGSNYVYSFQNVSFGIHGAGKKHNNAKQSWNWILSGSDTMGNRNFFKLRHMEEDPTQIRERLYSDILHAMGTYANDATMVRLFINNQGFGTFNMLDDITQFSYINAKFYNGKPPATLGPLYDGASGADFLYHPGNLDGYSSWVANTANPNGEAYEALDPLCKAWNETTYTDNTAIANFEKMFDLDRFMRFMVIEYLTADWDGYWMGQTNDGAYRDPTDNNKWYFLDQDFDGTFGVNLAAPEGNAFLDVSYKDFPSRYPGAVMINNLLQNADKKATFEKYLTETVRVLFNNVTLTNRVLALHNFLLPDLEWDRSIVQQSPGINFGWTFDQVTQNLWQGVTAPNNNGGGAAFGLVEYIAAKAQAVAKEFNISIVSQPVGPPSANGTTAAAPAPAAGNSTGKGGNQSISSSASSNKTSAQSTSGASRSKTAPIVLAISALALLVF
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Promotes invasion of host epithelial cells by adhering to receptors on the host cell surface to facilitate endocytosis of the pathogen into host cells. Binds HSPA5/BiP protein on the cell surface of host nasal epithelial cells.
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I1GQE7
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C85A1_BRADI
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Cytochrome P450 85A1 (BdCYP85A1) (3-dehydroteasterone synthase) (EC 1.14.14.-) (Castasterone synthase) (EC 1.14.14.-) (Teasterone synthase) (EC 1.14.14.-) (Typhasterol synthase) (EC 1.14.14.-)
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MVLAVLIGVLVGIVLVSSLLLRWNEVRYSRKQGLPPGTMGWPLFGETTEFLKQGPSFMKARRLRYGSLFRTHILGCPTVVCMDPELNRQMLQQGEGRGFVPGYPQSMLDILGRNNIAAVHGPLHRAMRGSMLALVRPASIRSSLLPKIDAFMRSHLHGWAGDLVDIQDKTKEMALLSALRQIAGITAGPLSDALKTELYTLVLGTISLPINLPGTSYYQGFQARKKLVSMLEKMIAERRSSGLVHNDMLDALLSGNDGTRERLSDEQIIDLIITLIYSGYETMSTTSMMAVKYLSDHPKALEELRKEHFDIRKGKSPEEAIDYNDFKSMTFTRAVIFETLRLATVVNGLLRKTTQDVEMNGYVIPKGWRIYVYTREINYDPCLYPDPMTFNPWRWLEKNMESHPHFMLFGGGGRMCPGKEVGTAEIATFLHYFVTRYRWEEEGTNTILKFPRVEAPNGLHIRVQNY
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Involved in reduction steps of the biosynthesis of plant campesterol-derivative steroids, ending to castasterone (CS) but missing brassinolide (BL). Catalyzes the C6-oxidation step in brassinosteroids biosynthesis the conversion of 6-deoxoteasterone (6-deoxoTE) to teasterone (TE), 3-dehydro-6-deoxoteasterone (6-deoxo3DT, 6-deoxo-3-DHT) to 3-dehydroteasterone (3DT, 3-DHT), 6-deoxotyphasterol (6-deoxoTY) to typhasterol (TY) and of 6-deoxocastasterone (6-deoxoCS) to castasterone (CS).
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I1GTC2
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BDTIR_BRADI
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Probable 2' cyclic ADP-D-ribose synthase BdTIR (Probable 2'cADPR synthase AbTIR) (EC 3.2.2.-) (NAD(+) hydrolase TIR) (EC 3.2.2.6) (NADP(+) hydrolase TIR) (EC 3.2.2.-) (TIR-only protein) (BdTIR)
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MASSGLSSRRSIMASRLTASAEAVNEPRRGAVVSRRVEYDEESLAGAGGESRYEVFINHRGVDTKRTVARLLYDRLAQAGLRGFLDNMSMRPGDRLEERIGSAIRECTVAVAIFSPSYCDSEYCLRELAMLVESRKAIIPIFYDIKPSDLLLPQAVADSEVYLPRDLERFKFALREAKHTVGITYDSATGDMAELVSAAADAVMYNMEKMETVQRRETMILSRL
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An NAD(+) hydrolase (NADase). Upon activation catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide NAD(+) cleavage triggers a defense system that promotes cell death. In addition to ADPR, also generates a cyclization variant of cyclic ADPR termed v-cADPR (2'cADPR). Also hydrolyzes NADP(+), but not other NAD(+)-related molecules. v-cADPR activates ThsA, an NAD(+) hydrolase in B.cereus (AC J8G6Z1). Probably makes 2'cADPR the cADPR made by this protein is bound by cmTad1 (AC P0DW61) and activates ThsA from B.cereus. Boiling cmTad1 bound to the cyclic nucleotide releases 2'cADPR, strongly suggesting it is the product of this protein (Probable).
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I1H7R8
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C90B1_BRADI
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Steroid (22S)-hydroxylase (EC 1.14.14.178) ((22S)-22-hydroxycampesterol synthase) (6-deoxycathasterone synthase) (Cytochrome P450 90B1) (BdCYP90B1)
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MAAMMASITSELLFFLPYILLALLTFYTTTVAKCHRWRRTEEKRRCPNLPPGAIGWPFIGETFGYLRAHPATSVGRFMEEHIARYGKIYRSSLFGDRTVVSADAGLNRYILQNEGKLFECSYPRSIGGILGKWSMLVLVGDPHREMRAISLNFLSSLRLRAVLLPEVERHTLLVLRHWPSASPAVFSAQHEAKKFTFNLMAKNIMSMDPGEEETERLRLEYITFMKGVVSAPLNFPGTAYWKALKSRATILGVIERKMEDRLQKMNKEDSSIEEDDLLGWAMKQSNLSKEQILDLLLSLLFAGHETSSMALALAIFFLEGCPKAVQELREEHLEIARRQRLRGECKLSWEDYKDMVFTQCVINETLRLGNVVRFLHRKVIRDVHYKGYDIPSGWKILPVLAAVHLDSSLYEDPSRFNPWRWKGNASGVAQSGNFMPYGGGTRLCAGSELAKLEMAIFLHHLVLNFRWELAEPDQAFVYPFVDFPKGLPIRVHRIAQEEEKSVLTVDI
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Involved in reduction steps of the biosynthesis of plant campesterol-derivative steroids, ending to castasterone (CS) but missing brassinolide (BL). Catalyzes the conversion of campesterol (CR) to (22S)-22-hydroxycampesterol (22-OHCR, 22-hydroxyCR) and of campestanol (CN) to 6-deoxycathasterone (6-deoxoCT).
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I1JNS6
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GIP1_SOYBN
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Probable aspartic proteinase GIP1 (EC 3.4.23.-) (Glucanase inhibitor protein 1) (GmGIP1)
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MPPPLPSLCNFNLAILFLFLTPTFQIPLIAPISKDDTTQLYTLSVFLKTPLQPTKLHLHLGSSLSWVLCDSTYTSSSSHHIPCNTPLCNSFPSNACSNNSSLCALFPENPVTRNTLLDTALIDSLALPTYDASSSLVLISDFIFSCATAHLLQGLAANALGLASLGRSNYSLPAQISTSLTSPRSFTLCLPASSANTGAAIFASTASSFLFSSKIDLTYTQLIVNPVADTVVTDNPQPSDEYFINLTSIKINGKPLYINSSILTVDQTGFGGTKISTAEPYTVLETSIYRLFVQRFVNESSAFNLTVTEAVEPFGVCYPAGDLTETRVGPAVPTVDLVMHSEDVFWRIFGGNSMVRVAKGGVDVWCLGFVDGGTRGRTPIVIGGHQLEDNLMQFDLDSNRFGFTSTLLLQDAKCSNLKVNNFANGIK
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Involved in plant defense against Phytophtora sojae. Contributes positively to soybean resistance against P.sojae. Binds the P.sojae xyloglucanase XEG1 and inhibits its cell wall degrading enzyme activity and its contribution as P.sojae virulence factor. XEG1 acts as an important virulence factor during P.sojae infection but also acts as a pathogen-associated molecular pattern (PAMP) in soybean and solanaceous species, where it can trigger defense responses including cell death. (Microbial infection) Possesses stronger binding affinity with XLP1, a truncated paralog of P.sojae XEG1 which has no enzyme activity. Is impaired in its inhibitor activity towards the P.sojae xyloglucanase XEG1 when hijacked by XLP1 binding.
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I1MRZ6
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DAT32_SOYBN
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Diacylglycerol O-acyltransferase 3-2 (GmDGAT3-2) (EC 2.3.1.20)
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MEISGTVLRQVSYVSGYGTHTRSRGLAPRFGVRMGMGSGFCDEGHLRYYQDTKKVLTPKKKLKLLKGFSKLGLASDPEKLAMFYDLQQNLTSDAGDVLLRELEAARAKEKEVKKKRKQEKKAKLKAAKMNCESSSSSSSESSDSDCGCDQVVDMNTFRAGVGVGVGVGVGVVAPAPVEESPLPKTAPIVEDANAHCVAMELCSKNDIYVSSASNGFKNESAVVTSAPQKRIEVCMGNKCKRSGAAALMQEFEKVVGVEGVAVVACKCMGKCKTAPNVKVQNSVDHNSLAQGLDDSVKIPANPLCIGVGLEDVDAIVARYFWESHTDIGMAGAGAATAT
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Involved in triacylglycerol (TAG) biosynthesis. Catalyzes the acylation of the sn-3 hydroxy group of sn-1,2-diacylglycerol using acyl-CoA. Incorporates preferentially monounsaturated fatty acids (MUFAs), especially oleic acid (C18:1) and to some extent palmitoleic acid (C16:1), into TAGs accumulating in seeds oil. Can also use, with low efficiency, hexadecanoic acid (C16:0), linoleic acid (C18:2) and linolenic acid (C18:3) as acyl-CoA substrates.
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I1RAQ3
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CFMN1_GIBZE
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Effector CFEMN1
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MKLSVFTSVLLAGLVAAQQEKLPKCAQPCVDQYTTGGGVAGCGQLDIKCICSNKNFLSGIACCLEKECDAQGKETAVKYAKQICATAGVTDLPDDVTCDKSAASSGTASGTATGATTPTSSDSTNTASATGGSSTVEPNAGAREGAAGFIGVGMAMLLAL
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Suppresses host programmed cell death during infection by binding to Z.mays WAK17 isoform 2 and Z.mays LRR5, to prevent activation of Z.mays WAK17 isoform 1 and the downstream hypersensitive response.
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I1RBR4
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CP51B_GIBZE
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Sterol 14-alpha demethylase CYP51A (EC 1.14.14.154) (Ergosterol biosynthetic protein CYP51A)
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MGLLQELAGHPLAQQFQELPLGQQVGIGFAVFLVLSVVLNVLNQLLFRNPNEPPMVFHWFPFVGSTITYGMDPPTFFRENRAKHGDVFTFILLGKKTTVAVGPAGNDFILNGKLKDVCAEEIYTVLTTPVFGKDVVYDCPNAKLMEQKKFMKIALTTEAFRSYVPIISSEVRDYFKRSPDFKGKSGIADIPKKMAEITIFTASHALQGSAIRSKFDESLAALYHDLDMGFTPINFMLHWAPLPWNRKRDHAQRTVAKIYMDTIKERRAKGNNESEHDMMKHLMNSTYKNGIRVPDHEVAHMMIALLMAGQHSSSSTSSWIMLRLAQYPHIMEELYQEQVKNLGADLPPLTYEDLAKLPLNQAIVKETLRLHAPIHSIMRAVKSPMPVPGTKYVIPTSHTLLAAPGVSATDSAFFPNPDEWDPHRWEADSPNFPRMASKGEDEEKIDYGYGLVSKGSASPYLPFGAGRHRCIGEHFANAQLQTIVAEVVREFKFRNVDGGHTLIDTDYASLFSRPLEPANIHWERRQ
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Together with cyp51A and cyp51C, encodes the sterol 14alpha-demethylase that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions. Essential for ascospore production. The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity). In filamentous fungi, during the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-ol) can be metabolized to eburicol (By similarity). Sterol 14alpha-demethylase catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of both these sterols in the form of formate, and converts eburicol and lanosterol to 14-demethyleburicol (4,4,24-trimethylergosta-8,14,24(28)-trienol) and 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, respectively, which are further metabolized by other enzymes in the pathway to ergosterol (Probable). Can also use susbtrates not intrinsic to fungi, such as 24,25-dihydrolanosterol (DHL), producing 4,4'-dimethyl-8,14-cholestadien-3-beta-ol, but at lower rates than the endogenous substrates (By similarity).
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I1RC73
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FGSR_GIBZE
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Zn(2)-C6 fungal-type transcription factor
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MPPRRSHKKSRAGCRRCKNRKIKCDEVHPRCGNCAKHGVPCDFSNPDVLEELAISTNTSTESVGAPTPSPAPTVNFNSAPRTPLTRPRAPSSPARAPRPNPSPPTSVYSQPSISSSTNTIDHGERMLELRLMHHYTNVTSKTLLTNSPAAEDIWQRAVPQMAFSGNGKTYLADAILSVAALHLRSMSPNDKALVRASHAYSASSLSAFGASLGAGITPENAEALFLTATLIAFQASASRIFVKDDGDAAPGDPTVRYVPPLSWFHAFQGVKTVVANSWQWIHHSDIVKVIIDSQPSFQLNLNPRSPDSFFGHMLEGLADELSNEDPRLVASTTQAYSHAVSVLNWAHKNYHAAAALTFTATVSKRYVDLVDARRPRALAILACFFALLKRMDNVWWLQDVARREVMGLVSLFEPGSKWWRHLEWPIRIAVLDGSSIPQDIWGTELEEQAPEQQNVLGSMTQHIEMFAEMLNQHTQPPIPIADEDLIVPDSPD
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Transcription factor that targets gene promoters containing 2 conserved CGAA repeat sequences. Positively regulates the expression of ergosterol biosynthesis genes including CYP51A and CYP51B encoding the sterol 14-alpha demethylase, and ERG6A and ERG6B encoding the sterol 24-C-methyltransferase.
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I1REI8
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CFM1_GIBZE
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Effector CFEM1
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MKYSVAFVALAAVAAQAQSLADVPKCAIPCLDKAIASETSCDKTDLACVCKGFSAVRSKATSCVIDECGTDVAINEVLPATENLCKNPPKESEAKSTAEEEKPTTTAAATSTLVVVTTSAEVVETTAAATTTVAPIIPTTAAEEPATSTPAAATPTKGPEQANGAAGLKGLGALAMAAFAALAL
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Suppresses host programmed cell death during infection by binding to Z.mays WAK17 isoform 2 and Z.mays LRR5, to prevent activation of Z.mays WAK17 isoform 1 and the downstream hypersensitive response.
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I1RII8
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XYNB_GIBZE
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Endo-1,4-beta-xylanase B (Xylanase B) (EC 3.2.1.8) (1,4-beta-D-xylan xylanohydrolase B) (Xylanase 2)
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MVSFTYLLAAVSAVTGAVAAPNPTKVDAQPPSGLLEKRTSPTTGVNNGFYFSFWTDTPSAVTYTNGNGGQFSMNWNGNRGNHVGGKGWNPGAARTIKYSGDYRPNGNSYLAVYGWTRNPLVEYYIVENFGTYNPSSGAQKKGEINIDGSIYDIAVSTRNCAPSIEGDCKTFQQYWSVRRNKRSSGSVNTGAHFNAWAQAGLRLGSHDYQILAVEGYQSSGQATMTVSG
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Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Plays an important role in causing fusarium head blight (FHB) on cereal crops. Induces cell death and hydrogen peroxide accumulation in infected wheat leaves.
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I1RJR2
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CP51A_GIBZE
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Sterol 14-alpha demethylase CYP51A (EC 1.14.14.154) (Cytochrome P450 sterol 14alpha-demethylase A) (CYP51A) (ERG11) (Ergosterol biosynthetic protein CYP51A)
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MFHLLIYPLWVLVALFAVIIANLLYQQLPRRPDEPPLVFHWFPFFGNAVAYGLDPCGFFEKCREKHGDVFTFILFGRKIVACLGVDGNDFVLNSRLQDANAEEVYGPLTIPVFGSDVVYDCPNSKLMEQKKFVKFGLTQKALESHVQLIEREVLDYVETDPSFSGRTSTIDVPKAMAEITIFTASRSLQGEEVRRKLTAEFAALYHDLDLGFRPVNFLFPWLPLPHNRKRDAAHIKMREVYMDIINDRRKGGIRTEDGTDMIANLMGCTYKNGQPVPDKEIAHMMITLLMAGQHSSSSASSWIVLHLASSPDITEELYQEQLVNLSVNGALPPLQYSDLDKLPLLQNVVKETLRVHSSIHSILRKVKRPMQVPNSPYTITTDKVIMASPTVTAMSEEYFENAKTWNPHRWDNRAKEEVDTEDVIDYGYGAVSKGTKSPYLPFGAGRHRCIGEKFAYVNLGVIVATLVRNFRLSTIDGRPGVPETDYTSLFSRPAQPAFIRWERRKKI
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Together with cyp51B and cyp51C, encodes the sterol 14alpha-demethylase that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions. CYP51A encodes the sterol 14-alpha-demethylase induced on ergosterol depletion and is responsible for the intrinsic variation in azole sensitivity. The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity). In filamentous fungi, during the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-ol) can be metabolized to eburicol (By similarity). Sterol 14alpha-demethylase catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of both these sterols in the form of formate, and converts eburicol and lanosterol to 14-demethyleburicol (4,4,24-trimethylergosta-8,14,24(28)-trienol) and 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, respectively, which are further metabolized by other enzymes in the pathway to ergosterol (Probable). Can also use susbtrates not intrinsic to fungi, such as 24,25-dihydrolanosterol (DHL), producing 4,4'-dimethyl-8,14-cholestadien-3-beta-ol, but at lower rates than the endogenous substrates (By similarity).
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I1RNG8
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ATG1_GIBZE
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Serine/threonine-protein kinase ATG1 (EC 2.7.11.1) (Autophagy-related protein 1)
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MAGPQESSTSSGSRKSGSRAVGQFNIGSEIGKGSFAQVYLGWHKETKAAVAIKSVELERLNKKLRENLYSEIQILKTLRHPHIVALHDCIESTSHINLIMEYCELGDLSLFIKKREKLATHPATHDMARKYPSMPNSGLHEVVIRHFLKQLTSALEFLRSKNYVHRDVKPQNLLLLPSQPFRDQRSRPVMQASQDSLIPISGLASLPMLKLADFGFARVLPSTSLADTLCGSPLYMAPEILRYERYDAKADLWSVGTVLYEMSTGRPPFRARNHVELLRKIEAAEDVIKFPREVSITPELKALIRSLLKRSPVERLSFENFFTHQVVTSEIPGLVEDDIPKSLRQESRDPRSAFQSGSPSLSSRSPRQTGHQSPTEALVSRSPRDQQPRSPQVGSPGGSRYARRSNESQRTTGNSPREGGEGLGIRRPVAQHAMTAPVQQVAYDSVTGRNRASPPTSLLDQVRRNRALSNPPITEEERAAQDVALEREYVVVERRHVEVNALADELAANEKLGDASQRSGPITRRYTQQGAPTSTTGAISTPYSRNALATQPRHDRKSSYEKSLSASPGSASSAISKAIQDASLRLFGFKVPPLRASPKGPSPPLYQAFPTYPTPQAPVGLLGDGRNVQGTDEDGKAAQTIEELATRSDCVYGFAEVKYKQLVPLAPSADHILGGLEPEQLVNEEDGLTVEAIVALSEEALVLYVKSLTLLARAMDIASLWWSKKSRGDTGTGLSAAAAQTVVQRINAVVQWVRQRFNEVLEKSEIVRLKLTEAQKQLPDDHPSHPSNHGTESIASSAGSPTKQVYLTPGISAEKLMYDRALEMSRAAAIDEVTNENLSGCEISYITAIRMLEAVLDNDEGSGSETRRLSTGKEAEREAVKEVSGGELDSDEEAHVRKRRLAAVRKKQQMIAEANSKTNLVYQQAVRRRSGDMTPRSVPSHASS
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Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes (By similarity). Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome (By similarity). Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (By similarity). Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates (By similarity). Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8 (By similarity). Autophagy is required for proper vegetative growth, asexual/sexual reproduction, and full virulence. Autophagy is particularly involved in the biosynthesis of deoxynivalenol (DON), an important virulence determinant.
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I1S489
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GRA7_GIBZE
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Fatty acid synthase subunit beta (EC 2.3.1.86) (S-acyl fatty acid synthase thioesterase) (EC 3.1.2.14) [Includes: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9); [Acyl-carrier-protein] acetyltransferase (EC 2.3.1.38) (Gramillins biosynthesis cluster protein FGSG_11656) ([Acyl-carrier-protein] malonyltransferase) (EC 2.3.1.39)]
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MFPGDMESKASSMNGDQPSSPTPSSSTSVTIPTYTPTSMYDQELQFSRSVAKHVYEAAATLRAAFLCGFQPYTDVASFAHDEIVSQLHYWSSFISFVNDPANNQAFTRMDILEVTRALVQCAEDTVLAGNDIHMIVAHLQIPQSEKGRIIKTFVTANSMLGDQPEVEVSNLVRSSLDGESTVYVIFGGQGNGDGYFAELAELYEVYQPLVGDLVRSASDLFRHLTDKMDVNDCFSEGMELMAWIDKDNDTPIPSRPYLLSSAISFPLITLLQLLHFKISFHYSGCSFKDVQRFLAGVTGHSQGIIAAAAIAAVDSPASFHELSLQAMTVSFSMGVRIHQYYGPQVLPQLITEACLAEGKPIPTPMLSVRGLSIETLATTIQDLNKSLPRTKVQLEVGLRNNDSNYVITGDPMSLRGLCTHFDHKKKALDIVYQFLPAAAPYHNSYLSIAASRAIEDCQEIILRGCDLKMPVFSTVDGSDLRNNEGANLVPDLIRMVCCQVVNWPAALNMPGATHILDFGPGGAQGVGVLANSMKAGQGVRVIHATVLNGLNTELGYKPDLFDRSRKASERVSKPQPWVNSFQPTLTRFTENKLVVSTRFTRLFLQPPIMVAAMTPTTTSWDFVAAVMKAGFHAELACGGFHDRDSLSAAITAIANQVEPGTGITCNVIYSSPTSLRWQIDELEKLVAAGYQIDGLSIGAGVPSVEVVQGYVERLQLQHIALKPGSTEAIERTLKIAKALQPLPVVLQWTGGRGGGHHSNQDFHAPLISMYGKIRAQDNVVLVVGSGFGGPSDTLPYITGKWASDMGLPPMPVDGILLGSRVMVAKEAHTSTEAKHLIVATEGAPDDEWSGTYSRPTGGVLSVISEMRQPIHKIATRAVRLWHELDQTIFHLGPKERVAEITRRRDEIIRRLNHDYHRVWFGCSGPTRDPVELDEMTYSEVLHRFVELAYVTAEHRWVHLSWKKLFSELLTRTMSRLHRTSDSRSETLVDDLDDPYSTLATLTDASAQLITYEDSIYFLQLFRRRGQKPVPFIPVLDADFETWFKKDSLWQSEDIAAVPNHDAQRVCILHGPVAAQYSTKVDEPVGEILGNIHTAWVTAILQTHYQGQSELVPVFDNSPFHASQVESSKTNTELSTPPLNHGLWTLEQWIVHIVQSRDKNLNWAKALLASPRVLCGRRLVPNPFITTLSGLRSMDIHVAETTKTGVGAGFTFFKIPLEETHQDLLDLTLQSNNEISIQISHYPTLQSAPITLTHHMSCQFSKLAMNKSLSDRSAMIRDFYRRIWLGTSHESSHKSIYDKFECEPYTVTADAIRKYNDCTRLPTSMPPTSWATSEVPLDFAVVIAWKALVKPLFSRELEADILKLLHVSNEITLHSDHSPPMVHDVLHTESQVTEVVLQPSGKMVQVEAHVFRGKSCILDLKTRFLLVGNDTHRDHLFRRSILPPSEILLEDEISAMQLVQSSWFQPLRDTSDLVGKRVVFQLEDLMQFHENGQIRCHQITGCAMLDGSIVGNCYLETPDDAYLSLMGNILSQQTGSSSQPAIFETPLLLFEEQEISFTAPTCEQTIAYSAASGDSNPIHVSPVFASLAGLSSPIVHGMHISAEVLQIVYTWLCASSMSRLKKSHVLFAGKVCTGDRLAVSMKHTAMHRGLRVVEVQIHKNMAEELVFVGTYEIEQPLTALVFTGQGSQKKGMGMDLRDKSAAARRIWDTADDHFQHEYGFRITDIVRHDPPSLTVHFGGVHGRRVRSNYMALTYERVASDGQIIEAKLFPTINENTTKYVFSSESGLLSSTQFTQPALGLMELAIMADLEARQLIPSNVTFAGHSLGEYSALMAVGHIMPLEVFISTVFYRGLVMQSTVTYDHHGRSKYAMCAVDPTRVSTDFDGQKLGWLVTQIASEGQWLLEVVNHNVIDSQYVCAGEAIALHCLGVVLDRIHYASKSFFDDGSFDLTDCIRESVKEIRKDRSKVVLSRSKASIPLKGLDVPFHSSHLRSGVDPFRRRLQRSIKLDNASPTKLIGRYIPNLTGKPFEVTRQYFNEVLRLTGSIPIQQALESWDRVASTI
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Fatty acid synthase subunit beta part of the gene cluster that mediates the biosynthesis of gramillins A and B, bicyclic lipopeptides that induce cell death in maize leaves but not in wheat leaves. The nonribosomal peptide synthetase GRA1 incorporates respectively a glutamic adic (Glu), a leucine (Leu), a serine (Ser), a hydroxyglutamine (HOGln), a 2-amino decanoic acid, and 2 cysteins (CysB and CysA) (Probable). The biosynthesis of 2-amino decanoic acid incorporated in gramillins could be initiated by a fatty acid synthase composed of the alpha and beta subunits FGSG_00036 and FGSG_11656 (Probable). The cytochrome P450 monooxygenase FGSG_15680 could hydroxylate the fatty acid chain (Probable). Subsequent oxidation to the ketone by the oxidoreductase FGSG_00048 and transamination by aminotransferase FGSG_00049 could form 2-amino-decanoic acid (Probable). On the other hand, FGSG_15680 could also be responsible for the HO-modified glutamine at the gamma-position (Probable). Whether hydroxylation occurs on the fully assembled product or on the Gln residue prior to assembly into the gramillins requires further proof (Probable). The thioredoxin FGSG_00043 could also be required for the disulfide-bond formation between CysA and CysB (Probable). The specific involvement of the remaining proteins from the cluster is more difficult to discern, but could have broader regulatory (FGSG_00040 and FGSG_11657) or enzymatic functions (FGSG_00044 and FGSG_00045) (Probable). The final C-domain of GRA1 does not possess the expected sequence of a termination CT domain, often implicated in macrocyclization and release of a cyclopeptidein fungal NRPs and the thioesterase FGSG_00047 may act in concert with the terminal C-domain of GRA1 to catalyze the formation of the macrocyclic anhydride and release of the products (Probable).
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I1S9X9
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ATG9_GIBZE
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Autophagy-related protein 9
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MASNIFSRIKSPSGGSQSFYQQLRSGEDPEYDPGLDEENLGHRFDDFQAEGMDIGDSSMTVESVAPGSKGKGKATFRPTAHARSSGITSPRWQQDDDGDNEVPASLLMEPKDLDPPASPPNKRATNPGSSRTPASVGPSSARTRAQWEAATAQQQLHQDHPYTTPMGPQPIPVARGTMSNNPREKALWRWVNTSNLDSFMRDVYDYFEGGGLWCILCANALWLFQCIDYSRVPDSRSLHEVIVPQCTRKMSGLWNFAIWLYTFFFIWKCVQYFVEIRRLTYIRDFYIYLLDIPEQDMQTISWQDVVARIMALREENPKTATNISPRLRQFMGSQSKERLDALDIANRLMRKENYLIAMINKDILDLSLPVPFLRGRQMFSKTMEWYLQYCILDMAFNELGQVQQDFLRPDRRRLLSQKLRQRFLFAGFLNLLFAPVVLAYVVIVYFFTYYYEYQKDPKQAAARKYTSLAEWKFRQFNELPHIFYERLHMSYPFATRYIDQFPKRITEAVARTIAFMSGAITAILAIGSVLDSELFLNFEITKDRPVIFYLGVFAAIWATTRGMVSEETLVFNPEYALRNVIEYTRYVPDHWKNKLHSSEVKQEFSELYKMKVVIFLEEMMGIVTTPMLLLFSLPRCSDQIVDFFREFTIHVDGLGYVCSFAVFDFQKGPGNTGPQGPRPDVREDYYSTKHGKMAASYYGFLDNYAANPKTGIPGHLPPGPKPSFHPPPSFPGIGSPTLAADMQGSHIGRTGTETGRARSRAPGGRGPRIGVMPQPSPMASMLLDQHHQPPGGNMVARSLHASRYPRGYRGESQIIEETEASSIRRNGEDDELYEPGGALGESVWETSPARGVTRENSAANTEDPEAGVLGLIYQLQQTQRPRRGGGMV
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Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Required for mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking (By similarity). Autophagy is required for proper vegetative growth, asexual/sexual reproduction, and full virulence. Autophagy is particularly involved in the biosynthesis of deoxynivalenol (DON), an important virulence determinant. Required for aerial hyphae development and lipid droplet degradation in response to starvation.
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I1SB12
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MNCO_MICNN
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Carbohydrate oxidase (EC 1.1.3.-) (EC 1.1.3.5) (Lactose oxidase) (LaO)
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MRSAFILALGLITASADALVTRGAIEACLSAAGVPIDIPGTADYERDVEPFNIRLPYIPTAIAQTQTTAHIQSAVQCAKKLNLKVSAKSGGHSYASFGFGGENGHLMVQLDRMIDVISYNDKTGIAHVEPGARLGHLATVLNDKYGRAISHGTCPGVGISGHFAHGGFGFSSHMHGLAVDSVVGVTVVLADGRIVEASATENADLFWGIKGAGSNFGIVAVWKLATFPAPKVLTRFGVTLNWKNKTSALKGIEAVEDYARWVAPREVNFRIGDYGAGNPGIEGLYYGTPEQWRAAFQPLLDTLPAGYVVNPTTSLNWIESVLSYSNFDHVDFITPQPVENFYAKSLTLKSIKGDAVKNFVDYYFDVSNKVKDRFWFYQLDVHGGKNSQVTKVTNAETAYPHRDKLWLIQFYDRYDNNQTYPETSFKFLDGWVNSVTKALPKSDWGMYINYADPRMDRDYATKVYYGENLARLQKLKAKFDPTDRFYYPQAVRPVK
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Catalyzes the selective oxidation of C1 hydroxyl moieties on mono-, oligo- and polysaccharides with concomitant reduction of molecular oxygen to hydrogen peroxide. This results in the formation of the corresponding lactones, which typically undergo spontaneous hydrolysis. Carbohydrate oxidase is able to oxidize a variety of substrates including D-glucose, D-galactose, D-xylose, D-maltose, D-cellobiose, and lactose. In addition, among various oligosaccharides, the enzyme preferred tetrameric dextrins, indicating a favorable interaction of four linked glucose units with the substrate binding pocket.
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I1TEM1
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T3O_CATRO
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Tabersonine 3-oxygenase (T3O) (EC 1.14.14.50) (16-methoxytabersonine 3-oxygenase) (Cytochrome P450 71D1) (Cytochrome P450 71D1V2)
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MEFHESSPFVFITRGFIFIAISIAVLRRIISKKTKTLPPGPWKLPLIGNLHQFLGSVPYQILRDLAQKNGPLMHLQLGEVSAIVAASPQMAKEITKTLDLQFADRPVIQALRIVTYDYLDISFNAYGKYWRQLRKIFVQELLTSKRVRSFCSIREDEFSNLVKTINSANGKSINLSKLMTSCTNSIINKVAFGKVRYEREVFIDLINQILALAGGFKLVDLFPSYKILHVLEGTERKLWEIRGKIDKILDKVIDEHRENSSRTGKGNGCNGQEDIVDILLRIEEGGDLDLDIPFGNNNIKALLFDIIAGGTETSSTAVDWAMSEMMRNPHVMSKAQKEIREAFNGKEKIEENDIQNLKYLKLVIQETLRLHPPAPLLMRQCREKCEIGGYHIPVGTKAFINVWAIGRDPAYWPNPESFIPERFDDNTYEFTKSEHHAFEYLPFGAGRRMCPGISFGLANVELPLALLLYHFNWQLPDGSTTLDMTEATGLAARRKYDLQLIATSYA
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Cytochrome P450 catalyzing the monooxygenation of 16-methoxytabersonine, 16-hydroxytabersonine and tabersonine, but not of 2,3-dihydrotabersonine. Converts the C2,C3 alkene of tabersonine and 16-methoxytabersonine to the epoxides, which then spontaneously open to form the corresponding imine alcohols. Inactive in converting amyrin to ursolic acid.
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I1WVY3
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CDIA2_BURP2
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tRNA nuclease CdiA-2 (tRNase CdiA-2) (EC 3.1.-.-) (CdiA-Bp1026b) (Toxin CdiA-2) (Toxin CdiA-II)
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MNKNRYRVVFNRARGALMVVQENGRASHGSGSRDARAGVVPAWLSLSPFALRHVALAVLVAAGVVPIWVNAQVVAGGAHAPSVIQTQNGLQQVNINRPGASGVSMNTYNQFDVPKPGIILNNSPINVQTQLGGIIGGNPNFQAGDAARLIVNQVNSNNPSFIRGKVEIGGAAAQLVIANQAGLVVDGGGFLNTSRATLTTGNPNFGPDGSLTGFNVNQGLISVVGAGLDTANVDQVDLLARAVQINAKAYAKTLNVVAGSNQVDYNTLNATPIAANGPAPTIAIDVSQLGGMYANRVFLVSSENGVGVANAGDIAAQAGDLTLQANGRLVLSGHTNAAGNMSLSASGGIQNSGVTYGKQSVTITTGADLTNSGALTAQQNLTANVGSLNSTGTLGAGINVDSTVGTSGDLNVTSSGQLTATGTNSAAGNATFTGSGVNLSNSATAANGNLALTATAGDVNLAGSTVSAKGAVNAQASGTVVNDRGNLSSGAGMTLGGGSLSNQGGRANSQGPLSVQMAGTVSNQNGMLSSQSTADVRGSAIQNNAGLIQSAGKQTIAGASIDNSAGRLISLNADGLSVTATGALTNAAGANVSGDPGGVIGGKGDVTVQGNTVTNSGSMSADATLHVIGQSVDNGNGALHAGQTTTVDAGNHLSNAGGRVEGQSAVLNGATLDNSQGTVNAATVSLNGTTLLNHGGTVTQTGTGPMTVAITDTLDNSNNGLIQTRSTDLSLTSTTLINDNGGTITHVGPGTLTVGNGSGTVSNKAGAIASNGRTVLQGKTIDNSAGSASGQTGLSVNAADSITNLGGKLTSNANVDVTAGGALVNDGGELGSKTAATTIHSASLSNLNGKIVSPTLTATVAGLLDNSQNGDFEANQLALTAANLKNQGGHISQWQSGPTTLAVSGTLDNSNGGVIQTNSTDLTLAPAVLDNSKGTITHGGTGTLTLTPGNGAGALQNTGGTIGTNGQAIVKAGSLDNGSGVIAAKLGLSATIAGAMNNTQGLMRSNAALSIISNGALSNHQGHIEAGTPGDTSTLSIQAASIDNTDGAVHDFGTGKMTVQGGSQIVNSHAGGVDGMGQMTGQGDVTIGAASISNTQGGQLMGANLLIQGATLDNSGGQVGNVANATGDVNVAMSGAVTNTNGSITSTRDLSVAASTLLGGGAYSAARDAAINLQGDFTTTPQTQFNIGRDLTFTLPGTFANSANLQSVHNLTVNAGNIVNTGAMTAGSLLSTHSGDLTNYGAMVGGSVAIQASGTVSNLGPVALIGASDTSGLLEIVAHDIENRDDTTLGDSMPTTTIFGLGKVALAGGKDANGNYTNAALINNSSAAIQSGASMELHADKVTNTRRVMQTSGNTSQVDPALLQQLGISMSGCAAYYIAACSGQDVHWINLFHDPNYPDYDPAPIIAALKLQPGGVFTVPPNGGQWNSGYQYTTYEGKATANTVTKLSPGAQIASGGDLDASTVKTFQNYWSSVTAAGNIKQPASLDMDGWGATGQQAPGVTVVYSGYYHYNNYDNSEHNWTLPFGDKPFVGGPGGYTQAAPADVRQYSLPDYRSTWGANGTISGNGVSVNNTAANATIPSLGLLPGQAVPGLTIGTVSGNASGTQSGAAAIKGGTPTWVDPVIASATAVNVLSNLTIPQGGLYRPNSAPNPTYLIETNPAFTRMNNFLSSDYYLNQIGVNPLTTEKRLGDGFYEQQLVRNQVTQLTGKAVLGPYTDLQGMYQSLMLAGAEWSKSLNLPLGMSLSAQQVAALTTNVIIMQTETVGGQQVLVPVVYLAKADQQNANGPLITAGNIDLKNTQVFTNSGTVKADTTLALQGKQIDNAFGALQSGGLTSLDTTGNVDLTSANVKAGSLDLNAGNKLILDTATQTTHQVSRDGATSDKTTLGPAANLNVAGDASIKTGGDFQQNAGNLNVGGNLNANIGGNWNLGVQQTGEHKVVQRANGVSDTDLNSATGSTVNVGGKSAIGVGGDLTAQGARLDFGQGGTVAAKGNVTFGAASTTSTINANSSGDQGNRSYAETRHGSDQALTGTTVKGGDTLNVVSGKDINVIGSTIDLKKGDANLLAAGDVNVGAVTERHVYNSRETHSRSGVVSGTKIASSQDATSTVANGSLISADGVSIGSGKDINVQGSTVVGTHDVALNAAHDVNITTSQDTSQSSTTYQEQHSGLMSGGGLSFSVGNSKLAQQNQSSSVTNNASTVGSVDGNLTVNAGNTLHVKGSDLVAGKDVTGTAANIVVDSATDTTRQAQQQQTSKSGLTVGLSGSVGDAINNAISETQAARESAKDSNGRASALHSIAAAGDVAFGGLGAKALLDGAKGPQAPSIGVQVSVGSSHSSMQSSEDQTIQRGSSINAGGNAKLIATGNGTPKDGNITIAGSNVNAANVALIANNQVNLVNTTDTDKTQSSNSSSGSSVGVSIGTNGIGVSASMQRAHGDGNSDAAIQNNTHINASQTATIVSGGDTNVIGANVNANKVVADVGGNLNVASVQDTTVSAAHQSSAGGGFTISQTGGGASFSAQNGHADGNYAGVNEQAGIQAGSGGFDVTVKGNTDLKGAYIASTADASKNSLTTGTLTTSDIENHSHYSANSAGFSAGASVGVSTKAVGPSSVSGSGGVTPMVFQNDSGDQSATTKSAVSAGAINITKPGEQTQDVANLNRDATNLNGTVSKTPDVQKMLSQQADTMNAAQAAGQTVSQGIGLYADGKRKDAIDAAKAAYERGDLVAMQSYIDQAKSWDEGGASRAGLQATGGALIGGLGGGSVLTAIGGAAGAGTSSLLAGQAEKISKSVGDMTGSSLVGNIAANVAATVGGALVGGSAGAAMASNVELYNAGNDPQKTDDRATIAGLQGLLNQAVAAGAKGLSTIANARNAIGNAISGALDSAADQFGTLMKRDAEGKMSQSPAELVSQGVANGINTVLGSKGGEPPLAGPSAVAVDSLTGQAANAALGATDRTPPSNAILSNSNSDNNSTQGSQSGTVTKTPNPEATGSLSGKPTQIPPLSDEVTTRSLIRENQSAVTLANKGYDVVQNPEVLGPKNPDYTINGQVFDNYAPATGNVRNIATTISNKVSSGQASNIVVNLADSSASPAAIEAQINSYPIPGLGKVIVIDKLGNITIIKPKGN
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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. The C-terminal 301 residues (the CT fragment) cleaves near the C-terminus of E.coli tRNA1B(Ala), probably preventing tRNA charging, and inhibits growth in E.coli. A truncated CT fragment (residues 2948-3122) has tRNA endonuclease activity on several B.thailandensis tRNAs as well as tRNA2(Arg) where it cleaves after A-70 and U-71. Inactive CT domain binds tRNA, probably in a 1:1 complex. Toxic activity is neutralized by coexpression of the cognate immunity protein CdiI in E.coli, but not by non-cognate immunity proteins from other strains of B.pseudomallei. May use lipopolysaccharide as its target cell receptor. Probably gains access to the cytoplasm of target cells (B.thailandensis strain E264) by using integral inner membrane protein BTH_II0599. Protein BTH_I0359 is also implicated in an unknown fashion in CDI in B.thailandensis strain E264. 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 domain form a hairpin-like structure as the FHA-2, PT and CT domains are periplasmic. Upon binding to a target cell outer membrane receptor (possibly a lipoprotein in this CDI) 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 (probably inner membrane protein BTH_II0599).
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I1Z695
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EREC2_ORYSJ
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LRR receptor-like serine/threonine-protein kinase ER2 (EC 2.7.11.1) (ERECTA homolog 2) (ER homolog 2) (OsER2) (Receptor-like cytoplasmic kinase 85) (OsRLCK85)
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MTTTTTTRLLLAAILLAVAAADDDGQTLLEIKKSFRNVDNVLYDWAGDGAPRRYCSWRGVLCDNVTFAVAALNLSGLNLGGEISPAIGNLKSVESIDLKSNELSGQIPDEIGDCTSLKTLDLSSNNLGGDIPFSISKLKHLENLILKNNQLVGMIPSTLSQLPNLKILDLAQNKLNGEIPRLIYWNEVLQYLGLRSNNLEGSLSPEMCQLTGLWYFDVKNNSLTGIIPDTIGNCTSFQVLDLSYNRLTGEIPFNIGFLQVATLSLQGNNFSGPIPSVIGLMQALAVLDLSFNQLSGPIPSILGNLTYTEKLYLQGNRLTGSIPPELGNMSTLHYLELNDNQLTGFIPPELGKLTGLFDLNLANNNLEGPIPDNISSCMNLISFNAYGNKLNGTVPRSLHKLESITYLNLSSNYLSGAIPIELAKMKNLDTLDLSCNMVAGPIPSAIGSLEHLLRLNFSNNNLVGYIPAEFGNLRSIMEIDLSSNHLGGLIPQEVGMLQNLILLKLESNNITGDVSSLINCFSLNVLNVSYNNLAGIVPTDNNFSRFSPDSFLGNPGLCGYWLGSSCYSTSHVQRSSVSRSAILGIAVAGLVILLMILAAACWPHWAQVPKDVSLCKPDIHALPSSNVPPKLVILHMNMAFLVYEDIMRMTENLSEKYIIGYGASSTVYKCVLKNCKPVAIKKLYAHYPQSLKEFETELETVGSIKHRNLVSLQGYSLSPAGNLLFYDYLENGSLWDVLHAGSSKKQKLDWEARLRIALGAAQGLAYLHHDCNPRIIHRDVKSKNILLDKDYEAHLADFGIAKSLCTSKTHTSTYVMGTIGYIDPEYACTSRLNEKSDVYSYGIVLLELLTGKKPVDNECNLHHLILSKAADNTVMEMVDPDIADTCKDLGEVKKVFQLALLCSKRQPSDRPTMHEVVRVLDCLVYPDPPSKPALPPALPQSSTVPSYVNEYVSLRGGSTLSCENSSSASDAELFLKFGEVISQNTE
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Receptor kinase that may be involved in the regulation of cell proliferation and cell growth.
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I2C090
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VCO3_OPHHA
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Ophiophagus venom factor (OVF) (CVF-like) (Complement C3 homolog) [Cleaved into: OVF alpha chain; OVF gamma chain; OVF beta chain]
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MEGMALYLVAALLIGFPGSSHGALYTLITPGVLRTDTEEQILVEAHGDNTPKQLDIFVHDFPRKQKILFQKRVDMNPAGDMLVTPTIKIPAEEVSKDSRQNQYVVVQVTGPQVRLEKVVLLSYQSGFVFIQTDKGIYTPGSPVLYRVFSMDHNMRQMDKTVVVEFQTPEGIVVSSNRIDLNFTRPYNLPELGSLGTWKIVAKYEHSPENYTAYFDVRKYVLPSFEVHLQPSEKSFYIDGNENFHVSITARYLYGEEVEGVAFVLFGVKIDGAKKSIPDSLTRIPILDGDGEATLKRDTLRSRFPNLNELVGHTLYASVTVITESGSDMVATEQSGIHIVTSPYQIYFTKTPKYFKPGMPYELTVYVTNPDGSPAAKVPVVSEAIHSEGTTLSDGTAKLILNTPLDTQSLLITVRTNHGDLPRERQATKSMTATAYQTQGGSGNYLHVAITSTEIKPGDNLPVNFNVRGNANSLNQVKYFTYLVGRQPKGAGQNLVAMNLRITPDLIPSFRFVAYYQVGNNEIVADSVWVDVKDTCMGTLVVKGASLTDNQIHMPGAAMKIKLEGDPGAQVGLVAVDKAVYVLNDKYKISQAKIWDTIEKSDFGCTAGGGQNNLGVFEDAGLALTTSTNLNTKQRSDTKCPQPANRRRRSSVLLLDSKASKAAQFQDQDLRKCCEDSMHENPMGYTCEKRAKYIQEGDACKAAFLECCRYIKGILDENQWESGLFLPRNDNEDGFIQDSDIIPRTDFPKSWLWHTVQLTEQPNSNGISSKTMSIYLKESITTWEVLAVSFTPTKGICVAEPYEIKVMKDFFIDLRVPYSVVRKEQVEIRAVLYNYAGRDIYVRVELLYNPAFCSASTEEQRYRQQFTIKALSSRAVPFVIVPLQQGLHDIEVRASVQGWESVSDGVKKKLKVVPEGVQKCIVTIIKLDPRAKGVDGTQREVVKARKLDDKVPDTEIETKITIQADPVAQIIENSIDGSKLNHLIITPSGCGEQNMIRMTAPVIATYYLDTTEQWETLGRNHRNEAVKQIMTGYAQQMVYKKANHSYAAFTNRASSTWLTAYVVKVFAMATKMVAGISHEIICGGVRWLILNRQQPDGAFKENAPVLSGTMQGGIQGDESEVTVTAFTLVALLESKTICNDSVNSLDSSIKKATDYLLKKYEKLQRPYTTALTAYALAAADRLNDDRVLMAASTGKNRWEEYNAHTHNVEGTSYALLALLKMKKFDQTGPIVRWLTDQNFYGGTYGQTQATVMLFQALAEYKIQMPTHKDLNLDIIIKLPERELPLHYRLDATNAILARTAETKLNQDFTVSASGDGTATMTILTVYNAQLQEKANVCNKFHLDVSVENIHLNFKHAKGAKGALMLKICMRYLGEVDSTMTIIDISMLTGFLPDAEDLTRLSEGVDRYISRYEVDNNMAQKVAVIIYLDKVSHSEDECLQFKILKHFEVGFIQPGSVKVYSYYNLDEQCTKFYHPDKGTGLLNKICVGNICRCAAETCSLLSQQEKIDLPLRIQKACASNVDYVYKTKLLRIEEKDGYDIYVMDVLEVIKPGTDENPQANARQYISQRKCQEALNLNVNDDYLIWGLRSDLWPMKDKFSYLITKNTWIERWPHEDECQDEEFQNLCLDFAHLSNILTIFGCPT
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Complement-activating protein in cobra venom. It is a structural and functional analog of complement component C3b, the activated form of C3. It binds factor B (CFB), which is subsequently cleaved by factor D (CFD) to form the bimolecular complex OVF/Bb. OVF/Bb is a C3/C5 convertase that cleaves both complement components C3 and C5. Structurally, it resembles the C3b degradation product C3c, which is not able to form a C3/C5 convertase. Unlike C3b/Bb, OVF/Bb is a stable complex and completely resistant to the actions of complement regulatory factors H (CFH) and I (CFI). Therefore, OVF continuously activates complement (By similarity). As a result, OVF exhibits complement-depleting activity. {ECO:0000250, ECO:0000269|PubMed:22561424}.
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I2CYZ4
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D4FAD_CHLRE
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Acyl-lipid (7-3)-desaturase, chloroplastic (EC 1.14.19.31) (Acyl-lipid 4-desaturase) (Fatty acyl delta4 desaturase)
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MNATMQRSAVAGRTSGKVATTARASSMARPRLPIAGRVARRSAVTVRAVAEPVVVDKAVEAPAKPVPSGGDPWEDEKWTKYKWTVYRGVAYDLTPYLDRHPGGRWLLNLAIGRDATALFESYHLRPEVAASMLKRLPVLADFPVDAVPPSPRPNDSELYNAIRERVRKEVFKGTEIKGAHRSGSEGAAFAVLGYAAAMYALYTYDANPLTGALLGLGGAWIGLTIQHCGNHGAMSTNPVVNNLMGLTNDLAGGSSLMWRYHHQVSHHIHCNDDALDEDVFSAFPMLRFDDRLPKAWYHQFQHVYMWALFPFLQLVFQIGDWQALLTNRTVGATLYGASNFERQTLIAGKLAHYFLLYGLPAFLHGPTAMLGGAAGYLFTQSIVLAATFAVSHNVPETKPLDPGPTRENLDESAVTRDWGVQQVLTSANWGGVIGNFFTGGLNLQIEHHLFPAISFMHYPAISKIVADECKQRGIPYSHYDTLPEILGRFVRYMKEVGAAPQKPVKRDGEMLMLSKF
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Fatty acid desaturase that introduces a cis double bond at the 4-position in 16-carbon polyunsaturated fatty acids that contain a Delta(7) double bond, resulting in the production of 16 carbon fatty acid (7Z,10Z,13Z)-hexadeca-7,10,13-trienoate.
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I2DBY1
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DYP_AURAJ
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Dye-decolorizing peroxidase AauDyP1 (EC 1.11.1.19) (EC 1.11.1.7) (AjP I) (Manganese-independent peroxidase I) [Cleaved into: Dye-decolorizing peroxidase AauDyP2 (EC 1.11.1.19) (EC 1.11.1.7) (AjP II) (Manganese-independent peroxidase II)]
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MRLSPVFVALLSGLLAADLGLARSVAPRVADSPAAVTGTRKTSLLKNVAGLPPVPSAAQVAATSLNTDDIQGDILVGMHKQKQLFYFFAINDPATFKTHLASDIAPVVASVTQLSNVATQPLVALNIAFSNTGLLALGVTDNLGDSLFANGQAKDATSFKESTSSWVPQFAGTGIHGVIILASDTTDLIDQQVASIESTFGSSISKLYSLSASIRPGNEAGHEMFGFLDGIAQPAINGFNTPLPGQNIVDAGVIITGATNDPITRPSWAVGGSFLAFRQLEQLVPEFNKYLLDNAPAGSGSLQARADLLGARMVGRWKSGAPIDLTPTADDPALGADAQRNNNFTYSHAGFDLGSDQSHCPFSAHIRKTRPRADLGGSLTPPNLSAGANSIMRSGIPYGPEVTSAESASNTTTQERGLAFVAYQAQLSQGFHFLQQTWADNANFPPGKTPATVGLDPIIGQNNGQPRVVNGLLPSNSSASLSIPQFVVSHGGEYFFSPPISAIGGRLSA
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Manganese-independent peroxidase that is able to convert a large number of compounds, but its physiological substrate is not known. In addition to classic peroxidase substrates (e.g. 2,6-dimethoxyphenol), oxidizes dyes such as Reactive Blue 5 and Reactive Black 5.
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I2G9B4
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VKT_MACLN
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Kunitz-type serine protease inhibitor PIVL
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MSSGGLLLLLGLLTLWAELTPVSSQDRPKFCYLPADPAECNAYMPRFYYDSASNKCKEFIYGGCRGNANNFKNRAECRHTCVASRKGIQPRIASN
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Serine protease inhibitor that inhibits trypsin. Exhibits an anti-tumor effect and displays integrin inhibitory activity without being cytotoxic. Is able to dose-dependently inhibit the adhesion, migration and invasion of human glioblastoma U87 cells. Also impairs the function of alpha-v/beta-3 (ITGAV/ITGB3) and to a lesser extent, the activity of alpha-v/beta-6 (ITGAV/ITGB6), alpha-v/beta-5 (ITGAV/ITGB5), alpha-1/beta-1 (ITGA1/ITGB1) and alpha-5/beta-1 (ITGA5/ITGB1) integrins.
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I2HAA0
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TBC8_CAEEL
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Rab GTPase-activating protein tbc-8 (TBC domain family member 8)
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MQMFRHSSADMWRAKKPTLERRSTDGRRSSIVDWINGLSDNNNYKSDHWVEKHDEGCERMTRNGSVCAVEESEPDVPTQHREVLLTKLKIEIKNIMAEHGAKKYLNLNSPYVTSLCIAVDACIMDGLRRRLLTLFNSPSSMSLLQIIAKSNGPAQQVLDQTREIEELRTSAIPVHLIWIREALYLKSLSTIINHFIDSKSVRRYYDNSALLLDPVKGRLVATLMMAPCMVTYRRMSNRIEQEATAEELVEGATRGSTSTVPSRPPLSITRQVSSIAASVERNGSVSRDYVFSLHHSCKSTLLYGKNNVCVAMNGSDFAKGYMSLQKFYDGNLSLKWVPNQLMHASSQPSSGHSNNGEFTNIWKNTINIEMQDIIYIHLHQKDEISPTCLTFVNCEGVQSAPFQLPAGQHSIAFLSSLETGLAPLLRLDPPLWVGTTKEKILPRLRKRSTAVANPAMLDYVFRLVRTSGVEPAPEDIEDPLAPTSHSPPIHDNCVSLPNSPYIVDNVDSIVNFQIGTACQSMRNQIMARAFYGWLTYVRHLRTIRTHLLHLVDTKTLICDDDCDPVDEKFWKQARAEPTEENEKEFLKRVYWRGIEGINTKEVRRMAWPYLLGLFEWNESPESRLEQFTSQYWQDIEEWRVLEAEVRRRDEEAFRAARARKAASPVREESCDVFEDPNEPTCSQHYDRENLITLFRANLHRIDKDVERCDRNLMFFSNKDNLESLRRVMYTYVRRNLEEGYTQGMCDLLAPLLVTFEDEALTLECFSLLMLRQRGKFPQRPGMSKCLLNLRSLIQVVDPQIYALISDIDYAQALSFAFRWFLLDFKRELSYECTYKVWEVIWAAQRLRITDDFAIFFGLATITNYHDVLITNNFDYTDMIKFFNEMAERHDCSRLLSSARTHVKCLQNLVQHLK
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Interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others. GTPase activator for rab-2. In association with ric-19 activates rab-2 during dense core vesicle maturation in cholinergic motoneurons.
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I3L5V6
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SARM1_PIG
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NAD(+) hydrolase SARM1 (NADase SARM1) (EC 3.2.2.6) (NADP(+) hydrolase SARM1) (EC 3.2.2.-) (Sterile alpha and TIR motif-containing protein 1)
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MVLTILFSAYKLCRFFAMSSPRPGAERLAVPGPDGGGGAGPWWTAGGRGPREVSPGVGAEVQGALERALPELQQALSALKQAGGGRAVGAGLAEVFQLVEEAWLLPAMGREVAQGLCDAIRLEGGLDLLLRLLQAPELETRVQAARLLEQILVAENRRDRVARIGLGVILNLAKEREPVELARSVAGILEHMFKHSEETCQRLVAAGGLDAVLYWCRRTDPALLRHCALALANCAMHGGQAAQRRMVEKRAAEWLFPLAFSKEDELLRLHACLAVAVLATNKEVEREVERSGTLALVEPLVASLDPGRFARCLVDASDTSQGRGPDDLQRLVPLLDSSRMEAQCIGAFYLCAEAVIMHIKNRNKVFSDIGAIQSLKRLVSYSTNGTTSALAKRALRLLGEEVPRPILPCVASWKEAEVQTWLQQIGFSQYCESFREQQVDGDLLLRLTEEELQTDLGMKSGITRKRFFRELTELKTFANYATCDRSNLADWLGSLDPRFRQYTYGLVSCGLDRSLLHRVSEQQLLEDCGIRLGVHRVRILTAAREMLHSPLPCTGSKPSGDVPDVFISYRRNSGSQLASLLKVHLQLHGFSVFIDVEKLEAGKFEDKLIQSIMSARNFVLVLSAGALDKCMQDHDCKDWVHKEIVTALSCGKNIVPVIDGFEWPEPHTLPEDMQAVLTFNGIKWSHEYQEATIEKIIRFLQGRSSRDSSAGSDTSLEGAAPMGPT
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NAD(+) hydrolase, which plays a key role in axonal degeneration following injury by regulating NAD(+) metabolism (By similarity). Acts as a negative regulator of MYD88- and TRIF-dependent toll-like receptor signaling pathway by promoting Wallerian degeneration, an injury-induced form of programmed subcellular death which involves degeneration of an axon distal to the injury site. Wallerian degeneration is triggered by NAD(+) depletion: in response to injury, SARM1 is activated and catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR), cyclic ADPR (cADPR) and nicotinamide NAD(+) cleavage promoting cytoskeletal degradation and axon destruction (By similarity). Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules (By similarity). Can activate neuronal cell death in response to stress (By similarity). Regulates dendritic arborization through the MAPK4-JNK pathway (By similarity). Involved in innate immune response: inhibits both TICAM1/TRIF- and MYD88-dependent activation of JUN/AP-1, TRIF-dependent activation of NF-kappa-B and IRF3, and the phosphorylation of MAPK14/p38 (By similarity).
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I3LGZ3
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GL15L_PIG
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Protein GPR15LG (Protein GPR15 ligand) (Protein GPR15L)
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MRFLALTSLLCILLLCLSFFSAEGRRHPRNPAKPGKIRICCPRLPGPDLMPQKGHHMRICRPCKFKQKPQLWVVPGALPQV
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Highly cationic protein that has multiple functions. Acts as a chemotactic factor that mediates lymphocytes recruitment to epithelia through binding and activation of the G-protein coupled receptor GPR15. May be a tumor suppressor together with SUSD2 has a growth inhibitory effect on colon cancer cells which includes G1 cell cycle arrest. May regulate keratinocyte proliferation. In addition, through activation of Mas-related G protein-coupled receptors (MRGPRs) contributes to pruritogenesis by activating itch-selective sensory neurons and mast cells degranulation (By similarity). Has antimicrobial activity against Gram-positive bacteria, including Staphylococcus aureus and Actinomyces spec., and Mycoplasma hominis and lentivirus.
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I3LM39
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CGAS_PIG
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Cyclic GMP-AMP synthase (cGAMP synthase) (cGAS) (EC 2.7.7.86) (2'3'-cGAMP synthase) (Mab-21 domain-containing protein 1)
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MAARRGKSTRTASEVGAAGPRASARSVNGAPTVPEAARPGARRNGPSRASGCRREKSGPDPREKPQVRTRTARAEDQAEGPSAPSERVEPPSAQGASLLRAGSCRAREARSARELRPQAGATELAAPARMEAPPGAWKLQTVLEKVRLSRHEISEAAEVVNWVVEHLLRRLQGGESEFKGVALLRTGSYYERVKISAPNEFDVMFKLEVPRIQLEEYCNSGAHYFVKFKRNPGGNPLEQFLEKEILSASKMLSKFRKIIKEEIKNIEGVTVERKRRGSPAVTLLISKPKEISVDIILALESKSSWPASTQKGLPISQWLGAKVKNNLKRQPFYLVPKHAKEGSGFQEETWRLSFSHIEKDILKNHGQSKTCCEIDGVKCCRKECLKLMKYLLEQLKKKFGNRRELAKFCSYHVKTAFFHVCTQDPHDNQWHLKNLECCFDNCVAYFLQCLKTEQLANYFIPGVNLFSRDLIDKPSKEFLSKQIEYERNNGFPVFW
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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 are frequently found in cancer cells, consist of chromatin surrounded by their 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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I3LMB3
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PLM_PIG
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Phospholemman (FXYD domain-containing ion transport regulator 1) (Sodium/potassium-transporting ATPase subunit FXYD1)
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MASLSHILVLWVGILTVVNAEAPQEHDPFTYDYQSLRIGGLIIAGILFILGILIVLSRRCRCKFNQQQSLGKMRSPHLAAQFSSESC
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Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell. Inhibits NKA activity in its unphosphorylated state and stimulates activity when phosphorylated. Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated inhibition of ATP1B1. Contributes to female sexual development by maintaining the excitability of neurons which secrete gonadotropin-releasing hormone.
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I3M072
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APOA1_ICTTR
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Apolipoprotein A-I (Apo-AI) (ApoA-I) [Cleaved into: Proapolipoprotein A-I (ProapoA-I); Truncated apolipoprotein A-I]
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MKAVVLTVAVLFLTGSQARHFWQQDEPQSSWDRIKDFATVYLDAVKDSGRDYVTQFETSALGKQLNLKLLDNWDSLSSTVSKVREQIGPVSQDFWDKLEKDTVSLRQEMNKDLEEVKRKVQPYLDEFQKRWQEDVERYRQQVEPLSKELREGARQKLLELHEKLSPLGQEMRDRARTHVDALRTHLAPYSDELRQRLAARLEALKEGSSFAEYQAKATEHLSALGEKAKPALEDLRQGLLPVLESLKLSFWSAVDEATKKLNTQ
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Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility.
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I3PB36
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CNL_PETHY
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Trans-cinnamate:CoA ligase, peroxisomal (Cinnamic acid:CoA ligase) (Ph-CNL) (PhCNL) (EC 6.2.1.-) ((E)-caffeate:CoA ligase CNL) (EC 6.2.1.-) (4-coumarate:CoA ligase CNL) (EC 6.2.1.12) (Protein ACYL-ACTIVATING ENZYME) (PhAAE)
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MDELPKCGANYVPLTPLTFLTRAFKSYANRTSIIYAGARFTWEQTYKRCCRLASSLQSLNIVKNDVVSVLAPNVPATYEMHFAVPMAGAVLNTINTRLDPMNIAIILKHSEAKLLFVDYEYLEKARKALELLMSTNFITAQNSKKISMPQVILIDDLYSPTRIQQQDQLEYEQLVHQGNPEYAPENIVDDEWDPIVLNYTSGTTSEPKGVVYSHRGAFLSTLNTIMGWEMGTEPVYLWSLPMFHINGWTLTWGIAARGGTNVCIRNTTAQEIYSNITLHKVTHMCCAPTVFNILLEAKPHERREITTPVQVMVGGAPPPTTLIGKIEELGFHVVHCYGITEAGGTTLVCEWQSEWNKLSREDQANLKARQGISVLALEDVDVKNSKTMQSVPHNGKTMGEICLRGSSIMKGYFKNDKANSQVFKNGWFLTGDVAVIHQDGYLEIKDRCKDIIISGGENISSIEVENAILKHPSVIEAAVVAMPHPRWGETPCAFVIKTKNPEIKEADIIVHCKKELPGFMVPKHVQFLEELPKTGTGKVKKLQLREMAKSFGIFDNANQTSQILDLPARL
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Involved in the biosynthesis of floral volatile benzenoid/phenylpropanoid (FVBP) scent (e.g. benzylbenzoate, phenylethylbenzoate, and methylbenzoate). Catalyzes the formation of CoA esters of cinnamic acid, and, with lower efficiency, of 4-coumaric acid and caffeic acid.
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I3PB37
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4CL1_PETHY
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4-coumarate:CoA ligase 1 (Ph-4CL1) (Ph4CL1) (EC 6.2.1.12) ((E)-caffeate:CoA ligase 4CL1) (EC 6.2.1.-) (Benzoate:CoA ligase 4CL1) (EC 6.2.1.25) (Trans-cinnamate:CoA ligase 4CL1) (EC 6.2.1.-) (Trans-ferulate:CoA ligase 4CL1) (EC 6.2.1.-)
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MPMETETNQGDLIFRSKLPDIYIPKHLPLHSYCFENISEFSSRPCLINGANNHIYTYADVELTSRKVAAGLNKLGIQQKDTIMILLPNSPEFVFAFMGASYLGAISTMANPLFTPAEVVKQAKASNAKLIITQACFVNKVKDYAFDNNLNVICIDSAPEGCIHFSELTQADEHDIPDVKIQSDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENANLYMHSEDVLMCVLPLFHIYSLNSVLLCGLRVGAAILIMQKFDIVQFCELIEKYKVTIGPFVPPIVLAIAKSPVVDNYDLSSVRTVMSGAAPLGKELEDAVRIKFPNAKLGQGYGMTEAGPVLAMCLAFAKEPFDIKSGACGTVVRNAEMKIVDPDTGCSLPRNQPGEICIRGDQIMKGYLNDPAATTRTIDKEGWLHTGDIGYIDNDDELFIVDRLKELIKYKGFQVAPAELEALLLNHPNISDAAVVPMKDEQAGEVPVAFVVRSNGSDITEDEVKDFVSKQVIFYKRIKRVFFVETVPKSPSGKILRKDLRARLAAGVPN
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Catalyzes the formation of CoA esters of trans-cinnamic acid, 4-coumaric acid, ferulic acid, benzoic acid and caffeic acid.
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I3PLQ6
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SOMT2_PAPSO
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Scoulerine-9-O-methyltransferase 2 (PsSOMT2) (EC 2.1.1.117) (3-O-acetyl-4'-O-demethylpapaveroxine 4'-O-methyltransferase OMT2) (EC 2.1.1.352) (O-methyltransferase 2)
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MEIHLESQEQEMKYQSQIWNQICGTVDTSVLRCAIQLGIFDAIHNSGKPMITLTELSSIVSSPSSSSIEPCNLYRLVRYLSQMDLISIGECLNEATVSLTGTSKLLLRNQEKSLIDWVLAISCEMMVVVWHELSSSVSTPADEPPIFQKVHGKNALELAGEFPEWNDLINNAMTSDTSVTKPALIQGCGKILNGVTSLIDVGGGHGATMAYIVEAFPHIKGAVIDLPHVVEAAPERPGVEFISGDIFKSISNADAVLLKYVLHNWEDTECVNLLKRCKEAVPADKGKVIIMDLVIDDDDNSILTQAKLSLDLTVMNHGGGRERTKEDWRNLIEMSGFSRHEIIPISAMPSIIVAYP
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Methyltransferase involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine. Catalyzes the conversion of (S)-scoulerine to (S)-tetrahydrocolumbamine. The heterodimers SOMT2-SOMT3 and SOMT2-6OMT convert 3-O-acetyl-4'-O-demethylpapaveroxine to 3-O-acetylpapaveroxine, where SOMT2 is the catalytic subunit.
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I3R634
|
NASA_HALMT
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Assimilatory nitrate reductase (EC 1.7.7.2)
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MPRNLRFLSVVNHVTKQVPTTCMRCAVGCGHVHLGSENAYGLETVRGDPSHPVNNGLACGRGIRESADPAGEWLTRPLVREDGELVQTSWSDAMARVGATIRTAVATDPDEVAVLGSGQQTNEAAYALGKLARAGIGTRNYDANTTLCMASAVTAYYRAFGSDAPPPTYDDIPNAETHLVWGANPAVAHPVMFRWIRQSATDGRLVVVDPVETKTAAVADDHVSVAPGGDLALARAILRHLVDTDQIDESFVRSNTEGFDDVVSALPSVTDAAARAGVSLDTVEELAALLDAPTLIYWGMGVNQSVRGTATAGALVNLCLASGNLGPGTGPFSLTGQANSMGTRVCSSKGTWSGHRPFEHPDHRRAVAEAWDVPVSRLPDDSGPGPVGILDSSPSVVWTVATNPLAGFPDATAAREVLRDSFLVVQDAFRSDTVELADVVLPAATWGESEGTAMNMERTVSRIRAATETPPGVRQDLDIIADVAARVAPGLLPRPPVSPSAIFDEFAALTEGTDADCSGISYTRLDGERAVRWPAPEPNSDAGYRYYDPSTSRWTFPTPSGKARFSTLDGEPLPEPVDGDYPLTLTTGREADGYNTGVRSRSDTPEEPVARVNPETVDTYHDAVADTDGELRTTVVSRRASVSVTLDRDDAVPPGLVWLSIHHPMTNQLTSPAVDPQSNEPNFKQCAVRFVHPDAPAKADFLAAEVSD
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Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation. Catalyzes the reduction of nitrate to nitrite, using ferredoxin as the electron donor. Can use reduced methyl viologen but neither NADPH nor NADH as electron donors.
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I3R637
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NASD_HALMT
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Assimilatory ferredoxin-dependent nitrite reductase (NiR) (EC 1.7.7.1) (Ferredoxin:nitrite reductase)
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MASKKEQWKSDLYGDAVRDELEAFAEEGFESIPEDERDKWFTRFKFWGVFQQRTGQESYFMMRLTNANGVLEPGQLRTIAEVARDYATGPVDNPEFGNGWVDLTTRQSIQLHWLELEDIPEIWEQLESVGVTSRSAGGDTMRNITGCPVAGKDTHELVESKPLLDRFQSELREDDALSNMPRKFNISVTGCREGCAQDSINDIGLEPARKEVDGEVITGFNVRVGGGLGSRKPRVARSLDVFVADEERAYEVVRGFVELYHDHGNRDVRARARSRFFVDDWGTEKIRDRLESEYLDFELQSAGEDIRDEYTYNAGRPQSAGKSDHVGVHEQSDGRYYVGLSVAVGRLTAADALELADLADKYGSGKIRLTRRQNPIVMDVPAGALDDLLAEPLLSKHTPEPNPFQRGTVACTGTEFCSLALTETKARTARMLRWLRDNVEVPDDVHQLKIHYSGCTADCGQANTADIGLFGMRAQKDGEMVEAMDIGVGGGIGDEPSFVEWIHQRVPADEVPGAIASLVEAFAAHRTAGQTFRQWVEAEGPDAVAEYCEPIETDFEAPYMHDAKQSWYPFADEDEPPKTEQPMTSD
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Catalyzes the reduction of nitrite to ammonium in the nitrate assimilation pathway, using ferredoxin as the electron donor. Can use reduced methyl viologen but neither NADPH nor NADH as electron donors.
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I3R9M8
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NARH_HALMT
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Respiratory nitrate reductase subunit beta (EC 1.7.5.1) (Nitrate reductase beta chain)
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MSTDSDAETVDLADGVDHQVAMVMDLNKCIGCQTCTVACKSLWTEGGGRDYMYWNNVETKPGKGYPRNWEESGGGWKSSEHKERKPGQIPDKEDYGDAWEFNHEEIMYNGSDRPLRPDSDPEWGPNWDEDQGTGEYPNSYYFYLPRICNHCTHPSCVEACPRKAIYKREEDGIVLIDQERCRGYRYCVEGCPYKKVYYNATQKTSEKCIFCYPRIEGEGPDGKTFAPACAEDCPPQLRLVGFLDDEQGPIHKLVEEYEVALPLHPEYQTQPNVYYIPPFAPPQHSEDGESVDVDRIPRNYLEELFGERVHDALDTIEREREKVNRGGGSELLDMLTDTNPARKFRLEVFDDD
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The respiratory membrane-bound nitrate reductase enzyme complex plays a role in generation of metabolic energy by using nitrate as a terminal electron acceptor during anaerobic conditions. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers.
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I3R9M9
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NARG_HALMT
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Respiratory nitrate reductase subunit alpha (EC 1.7.5.1) (Nitrate reductase alpha chain)
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MSRNDASQLDDGETTAESPPDDQANDAPEVGDPPGDPVDADSGVSRRTFLEGIGVASLLGIGTSAASDDSLFQMGGLKPVDDPIGNYPYRDWEDLYREKWDWDSVSRSTHSVNCTGSCSWNVYVKNGQVWREEQSGDYPRFDESLPDPNPRGCQKGACYTDYVNADQRIKHPLKRVGERGEGKWKRISWDEALTEIAEHVVDEVEAGRYDAISGFTPIPAMSPVSFASGSRLVNLLGGVSHSFYDWYSDLPPGQPITWGTQTDNAESADWYNADYIIAWGSNINVTRIPDAKYFLESGYNGTKRVGVFTDYSQTAIHTDEWLSPDSGTDTALALGMAQTIVDEGLYDEAHLKEQTDMPLLVRQDTGKFLRASDVPSVNTDADRPEWMLLMLDSNGRIREAPGSLGERDGQKDYSKSIELDFDPQLDGETTVQTQSGRVQVRTVWAELRDELANWDPEMVHEETTVGKETYQRIAREFAEADKAKIIQGKGVNDWYHNDLGNRALQLLVTLTGNLGEQGTGLDHYVGQEKIWTFHGWKTLSFPTGKVRGVPTTLWTYYHAGILDNTDPDTAAKIRESIDKGWMPVYPEERDNGSRPDPTTMFVWRGNYFNQAKGNVAVEEQLWPKLDLVVDINFRMDSTAMYSDIVLPTASHYEKHDLSMTDMHTYVHPFTPAVEPLGESKTDWQIFRELAQKIQEVATERGVEPISDRKFDREIDLQSVYDDYVRDWETGEEGALAEDRAACEYILEHSEESNPADSDEQITFADTVEQPQRLLEAGDHWTSDIEDGEAYAPWKDFVQDKNPWPTVTGRQQYYIDHDWFLELGEELPTHKEGPENTGGDYPMEYNTPHGRWAIHSTWRDSEKLLRLQRGEPLLYLHPEDAEERGIEDGDSVEVFNDLAEVELQAKIYPSSQRGTARMYFAWERFQFDSDSNFNSLVPMYMKPTQLVQYPEDSGEHLHFFPNYWGPTGVNSDVRVDVRKAGGGDE
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The respiratory membrane-bound nitrate reductase enzyme complex plays a role in generation of metabolic energy by using nitrate as a terminal electron acceptor during anaerobic conditions. The alpha chain is the actual site of nitrate reduction.
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I3V6A7
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SOMT1_PAPSO
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Scoulerine-9-O-methyltransferase 1 (PsSOMT1) (EC 2.1.1.117) (Norreticuline 3-O-methyltransferase SOMT1) (EC 2.1.1.-) (O-methyltransferase 1) (Reticuline 3-O-methyltransferase SOMT1) (EC 2.1.1.-) (Tetrahydrocolumbamine 2-O-methyltransferase SOMT1) (EC 2.1.1.89)
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MATNGEIFNTYGHNRQTATVTKITASNESSNGVCYLSETANLGKLICIPMALRAAMELNVFQLISKFGTDAKVSASEIASKMPNAKNNPEAAMYLDRILRLLGASSILSVSTTKKSINRGGDDVVVHEKLYGLTNSSCCLVPRQEDGVSLVEELLFTSDKVVVDSFFKLKCVVEEKDSVPFEVAHGAKIFEYAATEPRMNQVFNDGMAVFSIVVFEAVFRFYDGFLDMKELLDVGGGIGTSVSKIVAKYPLIRGVNFDLPHVISVAPQYPGVEHVAGDMFEEVPKGQNMLLKWVLHDWGDERCVKLLKNCWNSLPVGGKVLIIEFVLPNELGNNAESFNALIPDLLLMALNPGGKERTISEYDDLGKAAGFIKTIPIPISNGLHVIEFHK
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Methyltransferase involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine. Catalyzes the conversion of (S)-scoulerine to (S)-tetrahydrocolumbamine. Can convert (S)-tetrahydrocolumbamine to tetrahydropalmatine. Can convert (S)-norreticuline to (S)-norcodamine. Can convert (S)-reticuline to (S)-codamine. Substrate preference is (S)-scoulerine > (S)-tetrahydrocolumbamine > (S)-norreticuline > (S)-reticuline.
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I3VE74
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HCMB_AQUTE
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2-hydroxyisobutanoyl-CoA mutase small subunit (EC 5.4.99.64) (2-hydroxyisobutyryl-CoA mutase small subunit) (HCM small subunit)
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MDQTPIRVLLAKVGLDGHDRGVKVVARALRDAGMDVIYSGLHRTPEEVVNTAIQEDVDVLGVSLLSGVQLTVFPKIFKLLDERGAGDLIVIAGGVMPDEDAAAIRKLGVREVLLQDTPPQAIIDSIRSLVAARGAR
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Together with HcmA, catalyzes the isomerization of 2-hydroxyisobutyryl-CoA and 3-hydroxybutyryl-CoA. Is specific for 2-hydroxyisobutyryl-CoA and (S)-3-hydroxybutyryl-CoA, and shows only very low activity with (R)-3-hydroxybutyryl-CoA, isobutyryl-CoA and butyryl-CoA. In vitro, can isomerize pivalyl-CoA and isovaleryl-CoA, with much lower efficiency. Plays a central role in the degradation of substrates bearing a tert-butyl moiety, such as the fuel oxygenate methyl tert-butyl ether (MTBE) and its metabolites.
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I3VE77
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HCMA_AQUTE
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2-hydroxyisobutanoyl-CoA mutase large subunit (EC 5.4.99.64) (2-hydroxyisobutyryl-CoA mutase large subunit) (HCM large subunit)
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MTWLEPQIKSQLQSERKDWEANEVGAFLKKAPERKEQFHTIGDFPVQRTYTAADIADTPLEDIGLPGRYPFTRGPYPTMYRSRTWTMRQIAGFGTGEDTNKRFKYLIAQGQTGISTDFDMPTLMGYDSDHPMSDGEVGREGVAIDTLADMEALLADIDLEKISVSFTINPSAWILLAMYVALGEKRGYDLNKLSGTVQADILKEYMAQKEYIYPIAPSVRIVRDIITYSAKNLKRYNPINISGYHISEAGSSPLQEAAFTLANLITYVNEVTKTGMHVDEFAPRLAFFFVSQGDFFEEVAKFRALRRCYAKIMKERFGARNPESMRLRFHCQTAAATLTKPQYMVNVVRTSLQALSAVLGGAQSLHTNGYDEAFAIPTEDAMKMALRTQQIIAEESGVADVIDPLGGSYYVEALTTEYEKKIFEILEEVEKRGGTIKLIEQGWFQKQIADFAYETALRKQSGQKPVIGVNRFVENEEDVKIEIHPYDNTTAERQISRTRRVRAERDEAKVQAMLDQLVAVAKDESQNLMPLTIELVKAGATMGDIVEKLKGIWGTYRETPVF
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Together with HcmB, catalyzes the isomerization of 2-hydroxyisobutyryl-CoA and 3-hydroxybutyryl-CoA. Is specific for 2-hydroxyisobutyryl-CoA and (S)-3-hydroxybutyryl-CoA, and shows only very low activity with (R)-3-hydroxybutyryl-CoA, isobutyryl-CoA and butyryl-CoA. In vitro, can isomerize pivalyl-CoA and isovaleryl-CoA, with much lower efficiency. Plays a central role in the degradation of substrates bearing a tert-butyl moiety, such as the fuel oxygenate methyl tert-butyl ether (MTBE) and its metabolites.
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I4AY86
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NOTF_ASPVE
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Deoxybrevianamide E synthase (EC 2.5.1.109) (Brevianamide F reverse prenyltransferase) (Notoamide biosynthesis cluster protein A')
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MTAPELRAPAGHPQEPPARSSPAQALSSYHHFPTSDQERWYQETGSLCSRFLEAGQYGLHQQYQFMFFFMHHLIPALGPYPQKWRSTISRSGLPIEFSLNFQKGSHRLLRIGFEPVNFLSGSSQDPFNRIPIADLLAQLARLQLRGFDTQCFQQLLTRFQLSLDEVRQLPPDDQPLKSQGAFGFDFNPDGAILVKGYVFPYLKAKAAGVPVATLIAESVRAIDADRNQFMHAFSLINDYMQESTGYNEYTFLSCDLVEMSRQRVKIYGAHTEVTWAKIAEMWTLGGRLIEEPEIMEGLARLKQIWSLLQIGEGSRAFKGGFDYGKASATDQIPSPIIWNYEISPGSSFPVPKFYLPVHGENDLRVARSLAQFWDSLGWSEHACAYPDMLQQLYPDLDVSRTSRLQSWISYSYTAKKGVYMSVYFHSQSTYLWEED
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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 (Probable). 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 (Probable). 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 (Probable). 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 strain MF297-2 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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I4CHP3
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VSPI_GLOHA
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Thrombin-like enzyme AhV_TL-I (SVTLE AhV_TL-I) (EC 3.4.21.-)
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IIGGDECNINEHRFLVALYTSRSRTLFCGGTLINQEWVLTAAHCDRKNFRIKLGMHSKKVPNEDEQTRVPKEKFFCLSSKNYTLWDKDIMLIRLDSPVKNSKHIAPFSLPSSPPSVGSVCRIMGWGRISPTEGTYPDVPHCVNINLLEYEMCRAPYPEFELPATSRTLCAGILEGGKDTCKGDSGGPLICNGQFQGIASWGDDPCAQPHKPAAYTKVFDHLDWIENIIAGNTDASCPP
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Thrombin-like enzyme that shows fibrinogenolytic activity against both the Aalpha (FGA) and Bbeta (FGB) chains of bovine fibrinogen. This enzyme has poor esterolytic activity upon BAEE substrate. It induces mouse thoracic aortic ring contraction with EC(50)=147 nmol/L. It shows vasoconstrictor effects that are independent of the enzymatic activity, but related to the release of calcium ions form the calcium store, potentially through the activation of ryanodine receptors.
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I4DST8
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TCEA1_TULGE
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Tuliposide A-converting enzyme 1, chloroplastic (TgTCEA1) (EC 4.2.99.22)
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MSVASFFSSLPARPFGYKDGRGRTGMVPTTDIGRRMVKPPVLACRPIESNTYHGSVTSVFLTKSSRSPSPSLSPTPTALDDEIVLDLKPFLIIYKSGRIERFLGTTVIPACPEVATKDVVIDPATGVSVRLYLPNVVDLPSKKLPVLVYFHGGGFVIENTGSPNYHNYLTLLAAKAGVLIVSINYRLAPEYPLPASYDDCMAGFNWVVSHSAGPALEPWLAQHGDFSQILLSGDSAGGNVTHYVAMRADAGVIEGVAIVHPYFLGSEPVGNEINDPANIEFHDKLWRLAAPDTEGLDDPLINPVAPGAPSLAGLKCKRAVVFVAGNDFLVERGRMYYEALVKSGWRGEAELVQHEGVGHVFHLSDYSGDISVAMMTKLIAFLKGE
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Lactone-forming carboxylesterases, specifically catalyzing intramolecular transesterification, but not hydrolysis. Involved in the biosynthesis of tulipalins, defensive chemicals that show antimicrobial activities against a broad range of strains of bacteria and fungi. Substrates are 6-tuliposide A > 6-tuliposide B.
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I4DST9
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TCEA2_TULGE
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Tuliposide A-converting enzyme 2, chloroplastic (TgTCEA2) (EC 4.2.99.22)
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MSVASFFSSLPARPFGYKDGRGRTGMVSTTDIGRRMVKPPVLACRPIESNTYHGSVFLTKSSRSPSPSLSPTPTALDDEIVLDLKPFLIIYKSGRIERFLGTTVIPACPEVATKDVVIDPATGVSVRLYLPNVVDLPSKKLPVLVYFHGGGFVIENTGSPNYHNYLTLLAAKAGVLIVSINYRLAPEYPLPASYDDCMAGFNWVVSHSAGPALEPWLAQHGDFSQILLSGDSAGGNVTHYVAMRADAGVIEGVAIVHPYFLGSEPVGNEINDPANIEFHDKLWRLAAPDTEGLDDPLINPVAPGAPILAGLKCKRAVVFVAGNDFLVERGRMYYEALVKSGWGGEAELVQHEGVGHVFHLSDYSGDISVAMMTKLIAFLKGE
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Lactone-forming carboxylesterases, specifically catalyzing intramolecular transesterification, but not hydrolysis. Involved in the biosynthesis of tulipalins, defensive chemicals that show antimicrobial activities against a broad range of strains of bacteria and fungi. Substrates are 6-tuliposide A > 6-tuliposide B.
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I6L8L6
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PA2H1_BOTBZ
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Basic phospholipase A2 homolog 2 (svPLA2 homolog) (Myotoxin II) (MTX-II)
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SLFQLGKMILQETGKNPAASYGAYGCNCGVLGRGKPKDATDRCCYVHKCCKKKLTGCDPKKDRYSYSWKDKTIVCGENNPCLKELCECDKAVAICLRENLNTYNKKYRYHLKPFCKKADPC
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Snake venom phospholipase A2 homolog that lacks enzymatic activity. Is myotoxic and displays edema-inducing activities in mouse paw. Also displays cytotoxic activity against some cell lines, and antimicrobial activities against E.coli, C.albicans and Leishmania. A model of myotoxic mechanism has been proposed: an apo Lys49-PLA2 is activated by the entrance of a hydrophobic molecule (e.g. fatty acid) at the hydrophobic channel of the protein leading to a reorientation of a monomer. This reorientation causes a transition between 'inactive' to 'active' states, causing alignment of C-terminal and membrane-docking sites (MDoS) side-by-side and putting the membrane-disruption sites (MDiS) in the same plane, exposed to solvent and in a symmetric position for both monomers. The MDoS region stabilizes the toxin on membrane by the interaction of charged residues with phospholipid head groups. Subsequently, the MDiS region destabilizes the membrane with penetration of hydrophobic residues. This insertion causes a disorganization of the membrane, allowing an uncontrolled influx of ions (i.e. calcium and sodium), and eventually triggering irreversible intracellular alterations and cell death.
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I6LNY0
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BSR_PSEPU
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Broad specificity amino-acid racemase (EC 5.1.1.10)
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MPFRRTLLAASLVLLITGQAPLYAAPPLSMDNGTNALTVQNSNAWVEVSASALQHNIRTLQAELAGKSRLCAVLKADAYGHGIGLVMPSIIAQGVPCVAVASNEEARVVRASGFTGQLVRVRAASLSELEDALQYDMEELVGSAEFARQADAIAARHGKTLRIHLAFNSSGMSRNGVEMATWSGRGEALQITDQKHLELVALMTHFAVEDKDDVRKGLAAFNEQTDWLIKHARLDRSKLTLHAANSFATLEVPEARLDMVRTGGALFGDTVPGRTEYKRAMQFKSRVAAVHSYPAGNTVGYDRTFTLARDSRLANITVGYSDGYRRVFTNKGHVLINGHRVPVVGKVSMNTLMVDVTDFPDVKGGNEVVLFGKQAGGEITQAEMEEINGALLADLYTVWGSSNPKILVD
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Amino-acid racemase that catalyzes the interconversion of L-lysine and D-lysine, and L-arginine and D-arginine. To a lesser extent, is also able to interconvert alanine and isoleucine enantiomers.
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I6PL68
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HEI10_ORYSJ
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E3 ubiquitin-protein ligase CCNB1IP1 homolog (EC 2.3.2.27) (RING finger-containing protein HEI10) (OsHEI10) (RING-type E3 ubiquitin transferase HEI10)
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MKCNACWRELEGQAVSTTCGHLLCTEDAKKILSNDAACPICDQVLSKSHMRPVDTNPNDDWTNMSMAGVSPQILMKSAYRSVMFYIGQKELEMQYKMNRIVGQCRQKCELMQAKFTEKLEEVHTAYQKMAKKCQLMEQEVENLSRDKQELQEKFAEKSRQKRKLDEMYDQLRSEYESAKRSAIQPANNYFPRAQPDLFSGVPNIMDSSDPLRQGLAGLPETPGRRDEGWAPPPRQRRSTSGPFELSAGSPAHNAAPPVDIRPRQPARPVFGTAMNNTSAALRNMIISPVKRPQLSRNRPHMFT
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Ubiquitin E3 ligase required for class I crossover (CO) formation during meiosis.
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I6VSD2
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TM147_CAPHI
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BOS complex subunit TMEM147 (Transmembrane protein 147)
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MTLFHFGNCFALAYFPYFITYKCSGLSEYNAFWKCVQAGVTYLFVQLCKMLFLATFFPTWEGGIYDFIGEFMKASVDVADLIGLNLVMSRNAGKGEYKIMVAALGWATAELIMSRCIPLWVGARGIEFDWKYIQMSIDSNISLVHYIVASAQVWMITRYDLYHTYRPAVLLLMFLSVYKAFVMETFVHLCSLGSWTALLARALVTGLLALSTLALYVAVVNVHS
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Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes. The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions. Also acts as a negative regulator of CHRM3 function, most likely by interfering with its trafficking to the cell membrane. Negatively regulates CHRM3-mediated calcium mobilization and activation of RPS6KA1/p90RSK activity. Regulates LBR localization to the nucleus inner membrane.
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I6WU39
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OLIAC_CANSA
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Olivetolic acid cyclase (EC 4.4.1.26)
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MAVKHLIVLKFKDEITEAQKEEFFKTYVNLVNIIPAMKDVYWGKDVTQKNKEEGYTHIVEVTFESVETIQDYIIHPAHVGFGDVYRSFWEKLLIFDYTPRK
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Involved in the biosynthesis of cannabinoids-related terpenophenolic natural products, which have pharmacological activity. Polyketide cyclase which functions in concert with OLS/TKS to form olivetolic acid. Has no intrinsic polyketide synthase activity and requires the presence of OLS to produce olivetolic acid.
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I6WXK4
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PTPB_MYCTU
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Triple specificity protein phosphatase PtpB (EC 3.1.3.-) (EC 3.1.3.16) (EC 3.1.3.48) (MPtpB) (Phosphoinositide phosphatase) (Protein-serine/threonine phosphatase) (Protein-tyrosine phosphatase B) (TSP PTP)
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MAVRELPGAWNFRDVADTATALRPGRLFRSSELSRLDDAGRATLRRLGITDVADLRSSREVARRGPGRVPDGIDVHLLPFPDLADDDADDSAPHETAFKRLLTNDGSNGESGESSQSINDAATRYMTDEYRQFPTRNGAQRALHRVVTLLAAGRPVLTHCFAGKDRTGFVVALVLEAVGLDRDVIVADYLRSNDSVPQLRARISEMIQQRFDTELAPEVVTFTKARLSDGVLGVRAEYLAAARQTIDETYGSLGGYLRDAGISQATVNRMRGVLLG
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Essential virulence factor that promotes mycobacterial survival within host macrophages. Acts as a phosphatase that possesses triple substrate specificity toward phosphotyrosine, phosphoserine/threonine and phosphoinositides. Supports mycobacteria survival during infection by modulating the normal host signaling pathways, attenuating the bactericidal immune responses and promoting the host cell survival. Inhibits host pyroptosis by disrupting the membrane localization of host gasdermin-D (GSDMD): acts by catalyzing dephosphorylation of phosphatidylinositol (4,5)-bisphosphate and phosphatidylinositol 4-phosphate, thereby inhibiting the membrane targeting of GSDMD and subsequent cytokine release and pyroptosis. Inhibits host inflammatory responses and apoptosis through impeding the NF-kappa-B and MAPK signal pathways and TP53/p53 expression in the macrophage. Blocks the IL6/IL-6 production by down-regulating ERK1/2, p38 and p65 activity. Prevents macrophage cell death by activating the Akt pathway and blocking caspase 3 activity. Reduces the expression of iNOS in activated macrophages and inhibits the generation of destroying reactive nitrogen intermediate NO.
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I6WZG6
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ENCAP_MYCTU
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Type 1 encapsulin shell protein (Culture filtrate protein 29) (CFP29) [Cleaved into: Type 1 encapsulin shell protein, N-terminally processed]
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MNNLYRDLAPVTEAAWAEIELEAARTFKRHIAGRRVVDVSDPGGPVTAAVSTGRLIDVKAPTNGVIAHLRASKPLVRLRVPFTLSRNEIDDVERGSKDSDWEPVKEAAKKLAFVEDRTIFEGYSAASIEGIRSASSNPALTLPEDPREIPDVISQALSELRLAGVDGPYSVLLSADVYTKVSETSDHGYPIREHLNRLVDGDIIWAPAIDGAFVLTTRGGDFDLQLGTDVAIGYASHDTDTVRLYLQETLTFLCYTAEASVALSH
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Shell component of a type 1 encapsulin nanocompartment in situ its cargo protects against oxidative stress at low pH. In situ and in E.coli assembles into proteinaceous shells about 22 nm in diameter with 2.5 nm thick walls. Cargo proteins are targeted to the interior via their C-terminal extensions empty intact shells can be isolated in E.coli in the absence of cargo protein. There are at least 4 possible cargo proteins, DyP (encoded in the same locus), FolB, BfrB and Rv1762c DyP and Rv1762c have been identified in vivo. Probably involved in protection against oxidative damage from the host immune response (Probable). A T-cell antigen found in bacterial culture cell filtrates, stimulates mouse immune response. Does not have detectable bacteriocin activity.
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I6X235
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ADPP_MYCTU
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ADP-ribose pyrophosphatase (EC 3.6.1.13) (8-oxo-(d)GDP phosphatase) (EC 3.6.1.58) (ADPR hydrolase) (MT-ADPRase)
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MAEHDFETISSETLHTGAIFALRRDQVRMPGGGIVTREVVEHFGAVAIVAMDDNGNIPMVYQYRHTYGRRLWELPAGLLDVAGEPPHLTAARELREEVGLQASTWQVLVDLDTAPGFSDESVRVYLATGLREVGRPEAHHEEADMTMGWYPIAEAARRVLRGEIVNSIAIAGVLAVHAVTTGFAQPRPLDTEWIDRPTAFAARRAER
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Catalyzes the hydrolysis of ADP-ribose (ADPR) to AMP and ribose-5-phosphate. Can also hydrolyze ADP-mannose and ADP-glucose, with lower efficiency. Has weaker activity with NAD, GDP-sugars and UDP-sugars. Also catalyzes the conversion of 8-oxo-dGDP to 8-oxo-dGMP, and 8-oxo-GDP to 8-oxo-GMP. Functions in concert with MutT1 to detoxify 8-oxo-dGTP to 8-oxo-dGMP and may play an important role in supporting cellular growth under oxidative stress. The catalytic efficiency is much higher for the hydrolysis of ADPR than 8-oxo-dGTP, suggesting a more relevant biological role in hydrolysis of ADPR.
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I6X8D2
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PKS13_MYCTU
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Polyketide synthase Pks13 (EC 2.3.1.-)
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MADVAESQENAPAERAELTVPEMRQWLRNWVGKAVGKAPDSIDESVPMVELGLSSRDAVAMAADIEDLTGVTLSVAVAFAHPTIESLATRIIEGEPETDLAGDDAEDWSRTGPAERVDIAIVGLSTRFPGEMNTPEQTWQALLEGRDGITDLPDGRWSEFLEEPRLAARVAGARTRGGYLKDIKGFDSEFFAVAKTEADNIDPQQRMALELTWEALEHARIPASSLRGQAVGVYIGSSTNDYSFLAVSDPTVAHPYAITGTSSSIIANRVSYFYDFHGPSVTIDTACSSSLVAIHQGVQALRNGEADVVVAGGVNALITPMVTLGFDEIGAVLAPDGRIKSFSADADGYTRSEGGGMLVLKRVDDARRDGDAILAVIAGSAVNHDGRSNGLIAPNQDAQADVLRRAYKDAGIDPRTVDYIEAHGTGTILGDPIEAEALGRVVGRGRPADRPALLGAVKTNVGHLESAAGAASMAKVVLALQHDKLPPSINFAGPSPYIDFDAMRLKMITTPTDWPRYGGYALAGVSSFGFGGANAHVVVREVLPRDVVEKEPEPEPEPKAAAEPAEAPTLAGHALRFDEFGNIITDSAVAEEPEPELPGVTEEALRLKEAALEELAAQEVTAPLVPLAVSAFLTSRKKAAAAELADWMQSPEGQASSLESIGRSLSRRNHGRSRAVVLAHDHDEAIKGLRAVAAGKQAPNVFSVDGPVTTGPVWVLAGFGAQHRKMGKSLYLRNEVFAAWIEKVDALVQDELGYSVLELILDDAQDYGIETTQVTIFAIQIALGELLRHHGAKPAAVIGQSLGEAASAYFAGGLSLRDATRAICSRSHLMGEGEAMLFGEYIRLMALVEYSADEIREVFSDFPDLEVCVYAAPTQTVIGGPPEQVDAILARAEAEGKFARKFATKGASHTSQMDPLLGELTAELQGIKPTSPTCGIFSTVHEGRYIKPGGEPIHDVEYWKKGLRHSVYFTHGIRNAVDSGHTTFLELAPNPVALMQVALTTADAGLHDAQLIPTLARKQDEVSSMVSTMAQLYVYGHDLDIRTLFSRASGPQDYANIPPTRFKRKEHWLPAHFSGDGSTYMPGTHVALPDGRHVWEYAPRDGNVDLAALVRAAAAHVLPDAQLTAAEQRAVPGDGARLVTTMTRHPGGASVQVHARIDESFTLVYDALVSRAGSESVLPTAVGAATAIAVADGAPVAPETPAEDADAETLSDSLTTRYMPSGMTRWSPDSGETIAERLGLIVGSAMGYEPEDLPWEVPLIELGLDSLMAVRIKNRVEYDFDLPPIQLTAVRDANLYNVEKLIEYAVEHRDEVQQLHEHQKTQTAEEIARAQAELLHGKVGKTEPVDSEAGVALPSPQNGEQPNPTGPALNVDVPPRDAAERVTFATWAIVTGKSPGGIFNELPRLDDEAAAKIAQRLSERAEGPITAEDVLTSSNIEALADKVRTYLEAGQIDGFVRTLRARPEAGGKVPVFVFHPAGGSTVVYEPLLGRLPADTPMYGFERVEGSIEERAQQYVPKLIEMQGDGPYVLVGWSLGGVLAYACAIGLRRLGKDVRFVGLIDAVRAGEEIPQTKEEIRKRWDRYAAFAEKTFNVTIPAIPYEQLEELDDEGQVRFVLDAVSQSGVQIPAGIIEHQRTSYLDNRAIDTAQIQPYDGHVTLYMADRYHDDAIMFEPRYAVRQPDGGWGEYVSDLEVVPIGGEHIQAIDEPIIAKVGEHMSRALGQIEADRTSEVGKQ
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Involved in the biosynthesis of mycolic acids. Forms, with FadD32, the initiation module of the mycolic condensation system. Synthesizes, in coupled reaction with FadD32, the biosynthetic precursors of mycolic acids, alpha-alkyl beta-ketoacids, via the condensation of two long chain fatty acid derivatives, a very long meromycoloyl-AMP and a shorter 2-carboxyacyl-CoA. The acyl chain of the acyl-AMP produced by FadD32 is specifically transferred onto the N-terminal ACP domain of Pks13, and then transferred onto the KS domain. The extender unit carboxyacyl-CoA is specifically loaded onto the AT domain, which catalyzes the covalent attachment of the carboxyacyl chain to its active site, and its subsequent transfer onto the P-pant arm of the C-terminal ACP domain. The KS domain catalyzes the condensation between the two loaded fatty acyl chains to produce an alpha-alkyl beta-ketothioester linked to the C-ACP domain. Then, the thioesterase-like domain acts as a transacylase and is responsible for both the release and the transfer of the alpha-alkyl beta-ketoacyl chain onto a polyol acceptor molecule, particularly trehalose, leading to the formation of the trehalose monomycolate precursor.
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I6XD65
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PNCA_MYCTU
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Nicotinamidase/pyrazinamidase (Nicotinamidase) (EC 3.5.1.19) (Nicotinamide deamidase) (NAMase) (Pyrazinamidase) (PZAase) (EC 3.5.1.-)
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MRALIIVDVQNDFCEGGSLAVTGGAALARAISDYLAEAADYHHVVATKDFHIDPGDHFSGTPDYSSSWPPHCVSGTPGADFHPSLDTSAIEAVFYKGAYTGAYSGFEGVDENGTPLLNWLRQRGVDEVDVVGIATDHCVRQTAEDAVRNGLATRVLVDLTAGVSADTTVAALEEMRTASVELVCSS
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Catalyzes the deamidation of nicotinamide (NAM) into nicotinate. Likely functions in the cyclical salvage pathway for production of NAD from nicotinamide (By similarity). Is involved in the activation of the first-line antituberculous drug pyrazinamide (PZA) by converting it into the active form, pyrazinoic acid.
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I6XD69
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PKS12_MYCTU
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Mycoketide-CoA synthase (EC 2.3.1.295) (Polyketide synthase Pks12)
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MVDQLQHATEALRKALVQVERLKRTNRALLERSSEPIAIVGMSCRFPGGVDSPEGLWQMVADARDVMSEFPTDRGWDLAGLFDPDPDVRHKSYARTGGFVDGVADFDPAFFGISPSEALAMDPQHRMLLELSWEALERAGIDPTGLRGSATGVFAGLIVGGYGMLAEEIEGYRLTGMTSSVASGRVAYVLGLEGPAVSVDTACSSSLVALHMAVGSLRSGECDLALAGGVTVNATPTVFVEFSRHRGLAPDGRCKPYAGRADGVGWSEGGGMLVLQRLSDARRLGHPVLAVVVGSAVNQDGASNGLTAPNGPSQQRVVRAALANAGLSAAEVDVVEGHGTGTTLGDPIEAQALLATYGQDRGEPGEPLWLGSVKSNMGHTQAAAGVAGVIKMVLAMRHELLPATLHVDVPSPHVDWSAGAVELLTAPRVWPAGARTRRAGVSSFGISGTNAHVIIEAVPVVPRREAGWAGPVVPWVVSAKSESALRGQAARLAAYVRGDDGLDVADVGWSLAGRSVFEHRAVVVGGDRDRLLAGLDELAGDQLGGSVVRGTATAAGKTVFVFPGQGSQWLGMGIELLDTAPAFAQQIDACAEAFAEFVDWSLVDVLRGAPGAPGLDRVDVVQPVLFAVMVSLAELWKSVAVHPDAVIGHSQGEIAAAYVAGALSLRDAARVVTLRSKLLAGLAGPGGMVSIACGADQARDLLAPFGDRVSIAVVNGPSAVVVSGEVGALEELIAVCSTKELRTRRIEVDYASHSVEVEAIRGPLAEALSGIEPRSTRTVFFSTVTGNRLDTAGLDADYWYRNVRQTVLFDQAVRNACEQGYRTFIESSPHPALITGVEETFAACTDGDSEAIVVPTLGRGDGGLHRFLLSAASAFVAGVAVNWRGTLDGAGYVELPTYAFDKRRFWLSAEGSGADVSGLGLGASEHPLLGAVVDLPASGGVVLTGRLSPNVQPWLADHAVSDVVLFPGTGFVELAIRAGDEVGCSVLDELTLAAPLLLPATGSVAVQVVVDAGRDSNSRGVSIFSRADAQAGWLLHAEGILRPGSVEPGADLSVWPPAGAVTVDVADGYERLATRGYRYGPAFRGLTAMWARGEEIFAEVRLPEAAGGVGGFGVHPALLDAVLHAVVIAGDPDELALPFAWQGVSLHATGASAVRARIAPAGPSAVSVELADGLGLPVLSVASMVARPVTERQLLAAVSGSGPDRLFEVIWSPASAATSPGPTPAYQIFESVAADQDPVAGSYVRSHQALAAVQSWLTDHESGVLVVATRGAMALPREDVADLAGAAVWGLVRSAQTEHPGRIVLVDSDAATDDAAIAMALATGEPQVVLRGGQVYTARVRGSRAADAILVPPGDGPWRLGLGSAGTFENLRLEPVPNADAPLGPGQVRVAMRAIAANFRDIMITLGMFTHDALLGGEGAGVVVEVGPGVTEFSVGDSVFGFFPDGSGTLVAGDVRLLLPMPADWSYAEAAAISAVFTTAYYAFIHLADVQPGQRVLIHAGTGGVGMAAVQLARHLGLEVFATASKGKWDTLRAMGFDDDHISDSRSLEFEDKFRAATGGRGFDVVLDSLAGEFVDASLRLVAPGGVFLEMGKTDIRDPGVIAQQYPGVRYRAFDLFEPGRPRMHQYMLELATLFGDGVLRPLPVTTFDVRRAPAALRYLSQARHTGKVVMLMPGSWAAGTVLITGGTGMAGSAVARHVVARHGVRNLVLVSRRGPDAPGAAELVAELAAAGAQVQVVACDAADRAALAKVIADIPVQHPLSGVIHTAGALDDAVVMSLTPDRVDVVLRSKVDAAWHLHELTRDLDVSAFVMFSSMAGLVGSSGQANYAAANSFLDALAAHRRAHGLPAISLGWGLWDQASAMTGGLDAADLARLGREGVLALSTAEALELFDTAMIVDEPFLAPARIDLTALRAHAVAVPPMFSDLASAPTRRQVDDSVAAAKSKSALAHRLHGLPEAEQHAVLLGLVRLHIATVLGNITPEAIDPDKAFQDLGFDSLTAVEMRNRLKSATGLSLSPTLIFDYPTPNRLASYIRTELAGLPQEIKHTPAVRTTSEDPIAIVGMACRYPGGVNSPDDMWDMLIQGRDVLSEFPADRGWDLAGLYNPDPDAAGACYTRTGGFVDGVGDFDPAFFGVGPSEALAMDPQHRMLLELSWEALERAGIDPTGLRGSATGVFAGVMTQGYGMFAAEPVEGFRLTGQLSSVASGRVAYVLGLEGPAVSVDTACSSSLVALHMAVGSLRSGECDLALAGGVTVNATPDIFVEFSRWRGLSPDGRCKAFAAAADGTGFSEGGGMLVLQRLSDARRLGHPVLAVVVGSAVNQDGASNGLTAPNGPSQQRVVRAALANAGLSAAEVDVVEGHGTGTTLGDPIEAQALLATYGQDRGEPGEPLWLGSVKSNMGHTQAAAGVAGVIKMVLAMRHELLPATLHVDVPSPHVDWSAGAVELLTAPRVWPAGARTRRAGVSSFGISGTNAHVIIEAVPVVPRREAGWAGPVVPWVVSAKSESALRGQAARLAAYVRGDDGLDVADVGWSLAGRSVFEHRAVVVGGDRDRLLAGLDELAGDQLGGSVVRGTATAAGKTVFVFPGQGSQWLGMGMGLHAGYPVFAEAFNTVVGELDRHLLRPLREVMWGHDENLLNSTEFAQPALFAVEVALFRLLGSWGVRPDFVMGHSIGELSAAHVAGVLSLENAAVLVAARGRLMQALPAGGAMVAVQAAEEEVRPLLSAEVDIAAVNGPASLVISGAQNAVAAVADQLRADGRRVHQLAVSHAFHSPLMDPMIDEFAAVAAGIAIGRPTIGVISNVTGQLAGDDFGSAAYWRRHIRQAVRFADSVRFAQAAGGSRFLEVGPSGGLVASIEESLPDVAVTTMSALRKDRPEPATLTNAVAQGFVTGMDLDWRAVVGEAQFVELPTYAFQRRRFWLSGDGVAADAAGLGLAASEHALLGAVIDLPASGGVVLTGRLSPSVQGWLADHSVAGVTIFPGAGFVELAIRAGDEVGCGVVDELTLAAPLVLPASGSVAVQVVVNGPDESGVRGVSVYSRGDVGTGWVLHAEGALRAGSAEPTADLAMWPPAGAVPVEVADGYQQLAERGYGYGPAFRGLTAMWRRGDEVFAEVALPADAGVSVTGFGVHPVLLDAALHAVVLSAESAERGQGSVLVPFSWQGVSLHAAGASAVRARIAPVGPSAVSIELADGLGLPVLSVASMLARPVTDQQLRAAVSSSGPDRLFEVTWSPQPSAAVEPLPVCAWGTTEDSAAVVFESVPLAGDVVAGVYAATSSVLDVLQSWLTRDGAGVLVVMTRGAVALPGEDVTDLAGAAVWGLVRSAQTEHPGRIVLVDSDAPLDDSALAAVVTTGEPQVLWRRGEVYTARVHGSRAVGGLLVPPSDRPWRLAMSTAGTFENLRLELIPDADAPLGPGQVRVAVSAIAANFRDVMIALGLYPDPDAVMGVEACGVVIETSLNKGSFAVGDRVMGLFPEGTGTVASTDQRLLVKVPAGWSHTAAATTSVVFATAHYALVDLAAARSGQRVLIHAGTGGVGMAAVQLARHLGLEVFATASKGKWDTLRAMGFDDDHISDSRSLEFEDKFRAATGGRGFDVVLDSLAGEFVDASLRLVAPGGVFLEMGKTDIRDPGVIAQQYPGVRYRAFDLFEPGPDRIAQILAELATLFGDGVLRPLPVTTFDVRCAPAALRYLSQARHTGKVVMLMPGSWAAGTVLITGGTGMAGSAVARHVVARHGVRNLVLVSRRGPDAPGAAELVAELAAAGAQVQVVACDAADRAALAKVIADIPVQHPLSGVIHTAGALDDAVVMSLTPDRVDVVLRSKVDAAWHLHELTRDLDVSAFVMFSSMAGLVGSSGQANYAAANSFLDALAAHRRAHGLPAISLGWGLWDQASAMTGGLATVDFKRFARDGIVAMSSADALQLFDTAMIVDEPFMLPAHIDFAALKVKFDGGTLPPMFVDLINAPTRRQVDDSLAAAKSKSALLQRLEGLPEDEQHAVLLDLVRSHIATVLGSASPEAIDPDRAFQELGFDSLTAVEMRNRLKSATGLALSPTLIFDYPNSAALAGYMRRELLGSSPQDTSAVAAGEAELQRIVASIPVKRLRQAGVLDLLLALANETETSGQDPALAPTAEQEIADMDLDDLVNAAFRNDDE
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Involved in the synthesis of beta-D-mannosyl phosphomycoketide (MPM), an antigenic mycobacterial polyketide. Binds a fatty acyl-CoA as a starter unit, and extends it by five rounds of alternative additions of malonyl-CoA and methylmalonyl-CoA extender units. Depending on the starter unit, the enzyme forms mycoketide-CoAs of different lengths. Shows preference for small-/medium-chain starter fatty acyl substrates. Uses a hybrid modularly iterative mechanism, by forming a supramolecular assembly to perform repetitive cycles of iterations.
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I6XHI4
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FADA5_MYCTU
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Steroid 3-ketoacyl-CoA thiolase (EC 2.3.1.16) (Acetyl-CoA acetyltransferase FadA5) (Beta-ketoacyl-CoA thiolase)
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MGYPVIVEATRSPIGKRNGWLSGLHATELLGAVQKAVVDKAGIQSGLHAGDVEQVIGGCVTQFGEQSNNISRVAWLTAGLPEHVGATTVDCQCGSGQQANHLIAGLIAAGAIDVGIACGIEAMSRVGLGANAGPDRSLIRAQSWDIDLPNQFEAAERIAKRRGITREDVDVFGLESQRRAQRAWAEGRFDREISPIQAPVLDEQNQPTGERRLVFRDQGLRETTMAGLGELKPVLEGGIHTAGTSSQISDGAAAVLWMDEAVARAHGLTPRARIVAQALVGAEPYYHLDGPVQSTAKVLEKAGMKIGDIDIVEINEAFASVVLSWARVHEPDMDRVNVNGGAIALGHPVGCTGSRLITTALHELERTDQSLALITMCAGGALSTGTIIERI
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Involved in the beta-oxidation of the cholesterol side chain. It is important for utilization of cholesterol as a sole carbon source in vitro and for full virulence in the chronic stage of mouse lung infection. Catalyzes the thiolysis of 3,22-dioxochol-4-en-24-oyl-CoA to yield 3-oxo-4-pregnene-20-carboxyl-CoA (3-OPC-CoA) and acetyl-CoA. Also able to use acetoacetyl-CoA (AcAcCoA) as substrate.
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I6XU97
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EST45_MYCTU
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Esterase Rv0045c (EC 3.1.1.1)
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MLSDDELTGLDEFALLAENAEQAGVNGPLPEVERVQAGAISALRWGGSAPRVIFLHGGGQNAHTWDTVIVGLGEPALAVDLPGHGHSAWREDGNYSPQLNSETLAPVLRELAPGAEFVVGMSLGGLTAIRLAAMAPDLVGELVLVDVTPSALQRHAELTAEQRGTVALMHGEREFPSFQAMLDLTIAAAPHRDVKSLRRGVFHNSRRLDNGNWVWRYDAIRTFGDFAGLWDDVDALSAPITLVRGGSSGFVTDQDTAELHRRATHFRGVHIVEKSGHSVQSDQPRALIEIVRGVLDTR
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Esterase likely involved in ester/lipid metabolism. Shows strong substrate selectivity toward short, straight chain alkyl esters with the highest activity toward four atom chains. The physiological substrate is unknown. Is able to hydrolyze ester bonds within a wide range of p-nitrophenyl derivatives (C2-C14) in vitro.
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