entry
stringlengths 6
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stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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G0WXL9
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CS2H_ACIS1
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Carbon disulfide hydrolase (CS(2) hydrolase) (EC 3.13.1.5) (Carbon disulfide lyase)
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MVSEYIDSELKRLEDYALRRVKGIPNNRRLWVLTCMDERVHIEQSLGIQPDDAHIYRNAGGIVTDDAIRSASLTTNFFGTKEIIVVTHTDCGMLRFTGEEVAKYFISKGIKPTEVQLDPLLPAFRISSEEDFIKWFKFYEDLGVKSPDEMALKGVEILRNHPLIPKDVRITGYVYEVETHRLRKPNQIIYNETSKFEHGTIVKE
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Catalyzes the conversion of carbon disulfide into hydrogen sulfide and carbon dioxide, with carbonyl sulfide as an intermediate. Likely plays a key role in sulfur metabolism that allows Acidianus sp. A1-3 to grow on carbon disulfide as the main carbon and energy source. Does not show carbonic anhydrase activity (hydration of CO(2) to carbonate).
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G0Y7D3
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TPS3_LITCU
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Alpha-thujene synthase TPS3, chloroplastic (EC 4.2.3.-) ((+)-sabinene synthase TPS3) (EC 4.2.3.110) (Terpene synthase 3) (LcTPS3)
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MALQLLTPSFSFQHSPSPHRLTTLRYTHHTIRCTASAPSYSDLVGRRSANYKPSKWDSNFVETLESDYKKENHEMYIEKLMGDVKHLMKKVVNPIEKMELVDTIQRLGLGYLFNKEIKEVLNTIATSKATFKTKKDLHAVALQFRLLRQHGYEVSPDAFHKFKDEKGGFKESLCMDIKGMLSLYEASHLSFQGEVVLDEAREFTSTHLKAIEGNIDPVLLKKVRHSLEMPLHWRMLRLEARWYIETYDEEDRKNPSLAELAKHDFNSVQTIYQRSLKRMSRWWRDLGLGERLEFSRDRLVECFFWTTGVIFDPQFERCRGVLTKVNQLVSTIDDVYDVYGSLEELELFTDAVDRWDIRAMEQLPEYMKICYLALYNTTNDIAYEALKEEGLDVIPYLKKVWTDLCKSYIVEARWYSNGYKPTLEEYLENAWTSIAGPVALGHAYFSFGQKMPFEALNYSNTSSLIKWSSMIFRLCDDLATSSDEVARGDVPKSIQCYMYEAGVSESVARDHIKYLIDEAWKKMNECLVPSTPFLQPLINAGFNLARMAHCMYEHGDGHGFSNELDKKRVLLLLAEPFKFM
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Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products used by traditional Chinese medicine to treat headache, inflammation and intoxication (Ref.1). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into alpha-thujene and (1R,5R)-sabinene (Ref.1). {ECO:0000269|Ref.1}.
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G1FC92
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MIG21_CAEEL
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Abnormal cell migration protein 21
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MERDSNTAKSEIFYSNPAIWRHLKDGKGEGMSKSEKRNKHGCRNFTYSIWNCIRPGGWSTWSKWSKCREGIRKRRRTCNNPLPIGTTCSGQKVEKQSCAISSNVPEYLFGSWTSWNPWSRCDCDRSLRIRTRHCKGNSCEGCDKDYEDCRPDECPISKKWSEWTDWVNYGIEQVRFSAWCSSSNVANTEVGIRKETQDSMKHANWSEWHMHPGVAYRYRLLHNSSISIEHHLLSRFTSSCLPLHFAIPIFCFCILTGFLLQNIIYCVVNRFKRRFIRLNYSYDSNPRDYPSHLIRSPGSPKDESFW
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Required for determination of left/right asymmetry in nervous system. Acts together with unc-40 to control an initial left-right asymmetric polarization of the Q neuroblasts. Mig-21 and unc-40 may control the asymmetry in Wnt signaling response by restricting posterior polarization to one of the 2 Q neuroblasts. Involved in left-side QL posterior migration. In right-side QR, unc-40 and mig-21 pathways mutually inhibit each other in posterior migration, allowing anterior QR migration.
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G1FNI6
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TFP_THLAR
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N-(sulfonatooxy)prop-2-enimidothioate sulfolyase (EC 4.8.1.8) (Thiocyanate-forming protein) (TaTFP)
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MARTLQGEWMKVEQKGGQVPAPRSSHGIAVIGDKLYCFGGEDPPYESIDNDLYVFDFNTHTWSIAPANGDVPKTRVLGTRMVAVGTKLYVFGGRNKQLEFEDFYSYDTVKEEWKFLTKLDEKGGPEARTFHSMTSDENHVYVFGGVSKGGLNATPFRFRTIEAYNIAEGKWAQLPDPGEDFEKRGMAGFLVVQGKLWVFYGFATANDPKIPTLYGSQDYESNRVHCYDPATQKWTEVETTGFEKPSRRSCFAHAAVGKYIIIFGGEIERDPEAHQGPGTLSREGFALDTETLVWERYEGGPIKPSNRGWVASTTTTINGKKGLLVHGGKLMTNERTDEMYFFAVNSST
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Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation (By similarity). Catalyzes allylthiocyanate and corresponding epithionitrile formation from allylglucosinolate in the presence of myrosinase. Converts also aliphatic glucosinolates, such as indol-3-ylmethylglucosinolate, 4-methylsulfinylbutylglucosinolate, 4-methylthiobutyl- and benzylisothiocyanate, to simple nitriles.
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G1JSL4
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PXG1_AVESA
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Peroxygenase 1 (AsPXG1) (EC 1.11.2.3)
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MAEDAVVSDAVVVSDAMSSVAKGAPVTAQRPVRDDLEKHIPKPYLARALVAVDVNNPEGTKGGRHEHGQKSVLQQHVSFFDQNGDGIIYPWETFRGLRRLGFNLIVSFIVAIGIHTGLSYPTLPTWRPSLLFPVYIDRIHKAKHGSDTATFDTEGRFMPVNFENIFSKNARSQPDKLTLREIWMMTNDHRLAYDPFGWVANKGEWILLYMLAKDDEGYLPKEAIRGVYDGSLFEFLAEQRTKKAHGKQH
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Calcium-binding peroxygenase involved in cutin monomers biosynthesis. Can catalyze epoxidation of fatty acid and sulfoxidation reactions that can proceede competitively, although in favor of the sulfoxidation. Can only use unsaturated fatty acids with double bonds in the cis configuration as substrates. The preferred substrate is oleic acid and is inactive toward ricinoleic acid. Free fatty acid and fatty acid methyl esters are effective substrate forms, but not phospholipids and acyl-CoA. Hydroperoxy-trienoic (HPOT) acids are preferred over Hydroperoxy-dienoic (HPODT) acids as oxygen donors.
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G1JUH1
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TPS3_SOLLC
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(-)-camphene/tricyclene synthase, chloroplastic (SlTPS3) (EC 4.2.3.105) (EC 4.2.3.117) ((4S)-limonene synthase) (EC 4.2.3.16) (Myrcene synthase) (EC 4.2.3.15)
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MSIFSTRYLVTPFSSFSPPKAFVSKACSLSTGQPLNYSPNISTNIISSSNGIINPIRRSGNYEPTMWNYEYIQSTHNHHVGEKYMKRFNELKAEMKKHLMMMLHEESQELEKLELIDNLQRLGVSYHFKDEIIQILRSIHDQSSSEATSANSLYYTALKFRILRQHGFYISQDILNDFKDEQGHFKQSLCKDTKGLLQLYEASFLSTKSETSTLLESANTFAMSHLKNYLNGGDEENNWMVKLVRHALEVPLHCMMLRVETRWYIDIYENIPNANPLLIELAKLDFNFVQAMHQQELRNLSRWWKKSMLAEKLPFARDRIVEAFQWITGMIFESQENEFCRIMLTKVTAMATVIDDIYDVYGTLDELEIFTHAIQRMEIKAMDELPHYMKLCYLALFNTSSEIAYQVLKEQGINIMPYLTKSWADLSKSYLQEARWYYSGYTPSLDEYMENAWISVGSLVMVVNAFFLVTNPITKEVLEYLFSNKYPDIIRWPATIIRLTDDLATSSNEMKRGDVPKSIQCYMKENGASEEEARKHINLMIKETWKMINTAQHDNSLFCEKFMGCAVNIARTGQTIYQHGDGHGIQNYKIQNRISKLFFEPITISMP
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Monoterpene synthase that catalyzes the formation of camphene and tricyclene from geranyl diphosphate. Produces also lower amounts of limonene and beta-myrcene, and traces of several other monoterpenoids.
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G1SRW8
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SLN14_RABIT
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Protein SLFN14 [Cleaved into: C-terminally truncated SLFN14 endoribonuclease (EC 3.1.-.-) (Schlafen family member 14)]
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MEIPKTGVETLYPEFVVEVGRVTFGEENRKKMTNSCLKRTENLNIIKATCALLNSGGGVIKAEIHDKNYNYQCHGLGHDLETSFQKLLPFGSQKYLDYMQQGHELLIFVKSWNPDVSSLLPLRICSLRSNLYQRDVTSAINLSASSALELLREKQHAAQRGRRRLHPPRASNSNLQEEEDMKMLASEVFKKDRLMYKEKLNFTESTHVEFKRFTTKKVVPRIKEMLPHYVSAFANTQGGYLIIGVDDKSKEVFGCKKEKVNPDLLKKEIENCIEKLPTFHFCHEKPKINFITKILNVYQKDVLYGYVCVVQVEPFCCAVFAEAPDSWVMRDNAATRLTAEDWVLMMLDIPSAPCNLVTDSNAHLKSPASSAFRSPVCPTKVLEFKGALQRHLFPVTQKTIQFKPESFCKKLFSDHKGLEDLMKTQTYPYSQGIVVFSRSWAGDVGLRKEDRVLCDALLIALHSPLVLYTVLIDPSWAGGREYAWNVALHLKRKLQSVGGYPGKVGIIPRLIQLAGTWCGPGDGSVHYPQSYQLATEDDMEDLLQALVVVSLCSRSLLSDQLGCEFFNLLIAEQCEVLSQSLQETRELFIHCFPGTRKTALAIKTLEKIRDLFRCRPKEILYVCESDFLRDFVIHQTACLAVTRKTFMQGEFPKIKHIVMDETENFCSKYGDWYSKARSITHPRVRGAGNEDLHHGILWIFLDPFQVRHSDVNGLPPPPAQFPRKTITNGIHCAQEIAKVMKGAMKRITENPPSNMSPHTLALFREAACGEALGAHALPGVCETKADLTVEQIANYVAERCHGLFQCGYLPKDVAILCRREEDRARYKLALLRAMELTETHSATEVVFSQAAGVQGEHIILDSVHQFSGLHRNIVFGLSPEQRLSEEFHQLCFASKAIKHLYLLYERGQVSENYYK
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[Protein SLFN14]: Shows no ribosome-associated and endoribonuclease activities. [C-terminally truncated SLFN14 endoribonuclease]: Displays polysome-associated endoribonuclease activity towards mRNAs and rRNAs. May play a role in RNA surveillance pathways by recognizing stalled ribosomes and triggering endonucleolytic cleavage of aberrant mRNAs (Probable). Cleaves RNAs in a magnesium-, manganese-dependent and ATP-independent manner. Involved in correct maturation of megakaryocytes and especially important for proplatelet extension (By similarity).
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G1SW77
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SERB1_RABIT
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SERPINE1 mRNA-binding protein 1
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MPGHLQEGFGCVVTNRFDQLFDDESDPFEVLKAAENKKKEAGGGGVGGPGAKSAAQAAAQTNSNAAGKQLRKESQKDRKNPLPPNVGVVDKKEETQPPVALKKEGIRRVGRRPDQQLQGEGKIIDRRPERRPPRERRFEKPLEEKGEGGEFSVDRPIIDRPIRGRGGLGRGRGGRGRGMGRGDGFDSRGKREFDRHSGSDRSSFSHYSGLKHEDKRGGSGSHNWGTVKDELTESPKYIQKQISYNCSDLDQSNVTEETPEGEEHPVADTENKENEVEEVKEEGPKEMTLDEWKAIQNKDRAKVEFNIRKPNEGADGQWKKGFVLHKSKSEEAHAEDSVMDHHFRKPANDITSQLEINFGDLGRPGRGGRGGRGGRGRGGRPNRGSRTDKSSASAPDVDDPEAFPALA
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Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation. Acts via its association with EEF2/eEF2 factor, sequestering EEF2/eEF2 at the A-site of the ribosome and promoting ribosome stabilization and storage in an inactive state. May also play a role in the regulation of mRNA stability: binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay. Seems to play a role in PML-nuclear bodies formation (By similarity).
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G1T469
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NOD2_RABIT
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Nucleotide-binding oligomerization domain-containing protein 2 (OcNOD2)
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MCSQEAFQAQRSQLVGLLVSGSLEGFESILDLLLSWEVLSWEDYEGLRLVGQPLSHLARRLLDTVWNKGTWGCQKLIAAVQEAQDSSQCPELHGCWDPHSLHPAQDLQSHRPAIVRRLYSHVEGVLDLALEQGFISQYECDEIRLPIFTSSQRARRLLDLATVKANGLAAFLLQHVQKLPVSLSLPFEAAACKKYMSKLRTIVAAQSRFLSTYDGAENLCLEDIYTENTLEVRTEVGMAGPLHKSPAALGLEELFSPNGHLNEDADTVLVVGEAGSGKSTLLQQVHLLWATGQDFQEFLFVFPFSCRQLQCVARPLSVMTLLFEHCCWPDVGQQDVFQFLLDHPDRILLTFDGFDEFKFKFTDHERHCSPTDPTSVQTLLFNLLQGNLLKNARKVLTSRPDAVSAFLRKYVRTEFNLKGFSEEGIELYLRKCHREPGVADRLIHLLQTTSALHGLCHLPVFSWMVSKCHQELLLQDGGSPKTTTDMYLLILQHFLRHASLPDSASQGLGPSLLQGRLPTLLRLGQLALWGLGMCCYVFSAQQLQAAQVDPDDISLGFLVQAQGVVPGSTAPLEFLHITFQCFLAAFYLVLSTDVPTASLRYLFNCRRPGSSPLSRLLPRLCVQGSEHKESTVAALLQKTEPHNLQITAAFLAGLLSREHRDLLAACQASERSLLRRRACARWCLARSLHKHFRSIPPAVPGEAKSMHAMPGFLWLIRSLYEMQEERLAQEAVRGLNVEHLKLTFCGVGPAECAALAFVLRHLRRPVALQLDHNSVGDIGVEQLLPCLGACKALYLRDNNISDRGICKLIEHALHCEQLQKLALFNNKLTDGCAHSVAQLLACKQNFLALRLGNNHITAEGAQVLAEGLRDNSSLQFLGFWGNKVGDKGAQALAEALSDHQSLKWLSLVGNNIGSVGAQALASMLEKNVALEELCLEENHLQDAGVCSLAEGLKRNSSLKVLKLSNNCITFVGAEALLQALASNDTILEVWLRGNPFSPEEMEALSHRDSRLLL
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Pattern recognition receptor (PRR) that detects bacterial peptidoglycan fragments and other danger signals and plays an important role in gastrointestinal immunity. Specifically activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan found in every bacterial peptidoglycan type. NOD2 specifically recognizes and binds 6-O-phospho-MDP, the phosphorylated form of MDP, which is generated by NAGK. 6-O-phospho-MDP-binding triggers oligomerization that facilitates the binding and subsequent activation of the proximal adapter receptor-interacting RIPK2. Following recruitment, RIPK2 undergoes 'Met-1'- (linear) and 'Lys-63'-linked polyubiquitination by E3 ubiquitin-protein ligases XIAP, BIRC2, BIRC3 and the LUBAC complex, becoming a scaffolding protein for downstream effectors, triggering activation of the NF-kappa-B and MAP kinases signaling. This in turn leads to the transcriptional activation of hundreds of genes involved in immune response (By similarity). Its ability to detect bacterial MDP plays a central role in maintaining the equilibrium between intestinal microbiota and host immune responses to control inflammation. An imbalance in this relationship results in dysbiosis, whereby pathogenic bacteria prevail on commensals, causing damage in the intestinal epithelial barrier as well as allowing bacterial invasion and inflammation. Acts as a regulator of appetite by sensing MDP in a subset of brain neurons: microbiota-derived MDP reach the brain, where they bind and activate NOD2 in inhibitory hypothalamic neurons, decreasing neuronal activity, thereby regulating satiety and body temperature. NOD2-dependent MDP-sensing of bacterial cell walls in the intestinal epithelial compartment contributes to sustained postnatal growth upon undernutrition (By similarity). Also plays a role in antiviral response by acting as a sensor of single-stranded RNA (ssRNA) from viruses: upon ssRNA-binding, interacts with MAVS, leading to activation of interferon regulatory factor-3/IRF3 and expression of type I interferon. Also acts as a regulator of autophagy in dendritic cells via its interaction with ATG16L1, possibly by recruiting ATG16L1 at the site of bacterial entry (By similarity). NOD2 activation in the small intestine crypt also contributes to intestinal stem cells survival and acts by promoting mitophagy via its association with ATG16L1. In addition to its main role in innate immunity, also regulates the adaptive immune system by acting as regulator of helper T-cell and regulatory T-cells (Tregs) (By similarity). Besides recognizing pathogens, also involved in the endoplasmic reticulum stress response: acts by sensing and binding to the cytosolic metabolite sphingosine-1-phosphate generated in response to endoplasmic reticulum stress, initiating an inflammation process that leads to activation of the NF-kappa-B and MAP kinases signaling. May also be involved in NLRP1 activation following activation by MDP, leading to CASP1 activation and IL1B release in macrophages (By similarity).
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G1T7U7
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NAAA_RABIT
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N-acylethanolamine-hydrolyzing acid amidase (EC 3.5.1.60) (Acylsphingosine deacylase NAAA) (EC 3.5.1.23) [Cleaved into: N-acylethanolamine-hydrolyzing acid amidase subunit alpha; N-acylethanolamine-hydrolyzing acid amidase subunit beta]
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MQGTGHPVRPVLELLLLLLLLAGVGGSTTASTPGPPLFNVSLDVAPERWLPVLRHYDVELVRAAVAQVIGDRVPKWVLALIEKGALKLERLLPPPFTAEIRGMCDFLNLSLADGLLVNLAYEYSAFCTSIVAQDSRGHVYHGRNLDYPYGSILRKLTVDVQFLKNGQIAFTGTTFIGYVGLWTGQSPHKFTVSGDERDRGWWWENLVAALFLRHSPISWLLRTTLSEAESFEAAVYRLAKTPLIADVYYIVGGTNPREGVVITRNRDGPADIWPLDPLKGVWFLVETNYDHWKPAPEEDDRRTPAIKALNATGQAKLSLETLFQVLSVVPVYNNYTIYTTVMSAASPDKYMTRIRNPS
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Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine > N-myristoylethanolamine > N-stearoylethanolamine > N-oleoylethanolamine > N-linoleoylethanolamine > N-arachidonoylethanolamine.
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G1TGF1
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TEBP_RABIT
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Prostaglandin E synthase 3 (EC 5.3.99.3) (Cytosolic prostaglandin E2 synthase) (cPGES)
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MQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMNNMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE
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Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway.
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G1TZA0
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PLM_RABIT
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Phospholemman (FXYD domain-containing ion transport regulator 1) (Sodium/potassium-transporting ATPase subunit FXYD1)
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MAYLHHTLLVCMGLLAMANAEAPQEQDPFTYDYQSLRIGGLIIAGILFILGILIILKRGAWERFDTARRTGEPDEEEGTFRSSIRRLSTRRR
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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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G1UB11
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ERG5_CANAL
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C-22 sterol desaturase ERG5 (EC 1.14.19.41) (Cytochrome P450 61) (Ergosterol biosynthetic protein 5)
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MNSTEVDNLPFQQQLTSFVELAVAKATGSPITTLFTIIFLILSYDQLSYQINKGSIAGPRFKFYPIIGPFLESLDPKFEEYKAKWDSGELSCVSIFHKFVVIASSRDLARKILSSPKYVKPCVVDVAIKILRPTNWVFLDGKQHTDYRRSLNGLFSSKALEIYIPVQEKYMDIYLERFCKYDGPREFFPEFRELLCALSLRTFCGDYITEDQIALVADNYYRVTAALELVNFPIIIPYTKTWYGKKIADDTMKIFENCAAMAKKHINENNGTPKCVMDEWIHLMKEAREKHSEDPDSKLLVREFSNREISEAIFTFLFASQDASSSLACWLFQIVADRPDIVAKIREEQLRVRNNNPDVRLSLDLINEMTYTNNVVKESLRYRPPVLMVPYVVKKSFPVTESYTAPKGAMIIPTLYPALHDPEVYDEPDSFIPERWENASGDMYKRNWLVFGTGPHVCLGKNYVLMLFTGMLGKFVMNSDMIHHKTDLSEEIKVFATIFPKDDLILEWKKRDPLKSL
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C-22 sterol desaturase part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (Probable). ERG5 converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable).
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G1UB61
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CDC11_CANAL
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Septin CDC11 (Cell division control protein 11)
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MNYSTENVSSAALRKRKTLKKSINFSIMIIGESGSGRSTLINTLCGGNSIVPTSSTATQDPFTKKLTLRHENVELEDNEGHKISLNIIDTPNFANSINCDDDFKIIVDFIRHQFDEVLLEESRVKRNPRFKDGRIHVLIYMINPTGHGLSDIDVKFLQHVNNLVNIIPIISKADSLTPKELKLNKELILEDLNNYGINFYKFNEYDYEQDYIDEEIIEYNKYLNSLIPFAIIGANEYRSNPNGSEDEDDILKLRILNKDFKPIDIDNAEINDFTILKNVLLVTHLNEFKDITHDSIYENYRTEALSGKQFQYVNKDSAKQEISESDYLMKEEQIKLEEERLRKFEERVHQDLINKRKELLERENELKEIEKRLLAEGLKFDENGDVVKVHEEESSENEVKVI
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Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinase GIN4. Septins are also involved in cell morphogenesis, chlamydospores morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization, and spore wall formation. CDC11 is required for the correct localization of SEC3 at bud tips and bud necks. Plays a key role in invasive growth and virulence.
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G1UB63
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CSA1_CANAL
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Cell wall protein 1 (Surface antigen protein 1) (Wall protein 1)
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MLPSIVISIVLASFVSAESSITEAPTTTAEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSICSVAGVWDPYWMVPANVQSSLSAAATAVASSSEQPVETSSEPAGSSQSVESSQPAETSSSEPAETSSSEPAETSSETSSEQPASSEPAETSSEESSTITSAPSTPEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSICSVAGVWDPYWMVPANVQSSLSAAATAVPSSSEQSVETSSESAESSQSVESSQPAETSSEQPSETSSETSSQQLSSITSAPDSSATSSSSTTSTFIRTASINGFADKLYDQLPECAKPCMFQNTGITPCPYWDAGCLCVMPQFAGAIGSCVADSCKGQDIVSVTSLGTSVCSVAGVNAPYWMLPASVKSSLSVAATAVPTSDSASETASQEPSETSSEQPSETASQQPAETSSEESSTITSAPSTPEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGSSICSVAGVWDPYWMLPANVQSSLNAAATAVATSDSASEVASASESASQVPQETSAASSQSANNSVASAAPSNSSVSAAPSSNSSGVPAAPSNNSSGASVVPSQSANNSSASAAPSNNSSSAISESVAPSSYGNSTIAQPSTSTKSDAASITGPITTDKVITNESGIVFTSTVIITHVSEYCDQTSAAAVQSSACEEQSSAKSEQASASSEQVKVITSVVWCESSIQSIESVKTSAEAAHKTEVIASCASELSSLSSAKSEAMKTVSSLVEVQKSAVAKQTSLAAVQSSAASVQLSAAHAQKSSEAVEVAQTAVAEASKAGDEISTEIVNITKTVSSGKETGVSQATVAANTHSVAIANMANTKFASTMSLLVASFVFVGLFI
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Heme-binding protein involved in heme-iron utilization. The ability to acquire iron from host tissues is a major virulence factor of pathogenic microorganisms. Required for biofilm formation.
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G1UB67
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EED1_CANAL
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Transcriptional regulator DEF1 (EFG1-dependent transcript protein 1)
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MERRQFNTSNIRNGTGRPRKTPRSKLYMVYPPLSGEDSTNPEPEEGSSQENNPTEPSSSQSNSVQNQDQSEDQSQLPQQESNTQQESNTQQESNTPSPRASNTSTETPAPLSPIQPGIRNIPSGLLLPQEKVGRLMGYPFYRDFNFTLNPERYQKLIYVFQILKNAARNHRNGASLLRKYFSLARRSKRTTDMFVTTIEEMRKRSLENSRKRELEEAQEREESNKRQHTESSAEPNAESSTESTTESNAESGAEPNAEPSAESTTESNVESGAEPNAESGAESGAEPTAESNAELKQRIWEILSYRLEQSNNETNNTGESNSTSQQPRQLPNNELIMNIRVLQKNTHAKPVLGRIKFTPDKSNKTSLTGSQNKVHSTNTQQSQKHPQQILTNSETHKPQQYSAQSQQQMVHQTNSHEPSQKRSPPPQQQQQKQPSVPTSSVPLQVSQKQNQQQQELPLPPQPQPQQRTAPSAVKQQQSMQMQPPPQQQQQQQRHQPLQQSPPTMPLQQQPVPPVQQVQTVPPPSSQPQTQLSQQQQQQQQAQLQMQVPRCYQYQNRPPSQQRQYSQTPQYNQPPPQQKVYALPPQQVYAPPPRQVYAQPTIACKQQYPQQLYEQAPQEGSSYQHHYQQVQQRQNQQPYMQSAPTYQQPHVQTPKSTRSNKQEKQRLPKGQEQVPKATRTMFEAFTGSNIAVEKLRQRTLDNGREPERLRTEYVNVLSSPERAAEKSTSRSKQSSNQKPVVKQQSSFPPPIKHQQTQEQQGNILPPVSQLLAIQSSTVTSRGSNASGAVMGSGNTQRVASRSFTNTFVAEAVVNNANNRGGPVPPTGPETNTRGGRASTRSSGRPRGNRSTQRAEGNVTGRVARSTDGSQSQNSGKASKISNIRNLLN
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Transcriptional regulator involved in extension of germ tubes into elongated hyphae and maintenance of filamentous growth. Regulates expression of UME6. Acts in a pathway that regulates maintenance of hyphal growth by repressing hyphal-to-yeast transition and allows dissemination within host epithelial tissues. Dispensable for invasion into both host oral epithelial cells and enterocytes, but required for epithelial damage.
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G1UBC2
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PGA47_CANAL
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Cell wall adhesin EAP1 (Enhanced adherence to polystyrene protein 1) (GPI-anchored protein 47)
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MKVSQILPLAGAISVASGFWIPDFSNKQNSNSYPGQYKGKGGYQDDCGDDYKKGYKSKTYSKVKPITSTDCTTPIQPTGTTTGYTKDVVESTSYTTDTAYTTTVITVTKCDGGSCSHTAVTTGVTIITVTTNDVITEYTTYCPLTSTPATESTPATESTPATESTPATESTPATESTPATESTPCTTSTETTPATESTPATESTPATESTPATESTPATESTPATESTPATESTPATESTPCTTSTETTPATESTASTETASSTPVESTVIVPSTTVITVSSCYEDKCSVSSVTTGVVTISSEETIYTTYCPITSSITIPVPNTSTPAAPGTPVESQPVIPGTETTPAAPGTPVESQPVIPGTETTPAAPGTPVESQPATTPVAPGTETTPAAPGTPVESQPATTPVAPGTETTPAAPGTPVESQPVIPGTETTPAAPGTPVESQPATTPVAPGTETTPAAPGTPVESQPVIPGTETTPAAPGTPVESQPATTPVAPGTETTPAAPGTPVESQPVIPGTETTPAAPGTPGTEATPVTTQPVSVLSTSQVVTASGEFSTVTAHSTSIVASCPEGGCVPEGQQTETSPSVPTNGPEVEASSSVLSIPVSSVTTSTIASSSETSVPPAQVSTFEGSGSALKKPYYGLAVAALVYFM
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Cell wall protein which mediates cell-cell and cell-substrate adhesion. Required for biofilm formation and plays a role in virulence.
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G1UBD1
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PMOB_METCA
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Particulate methane monooxygenase alpha subunit (EC 1.14.18.3) (Methane monooxygenase B subunit) (Particulate methane monooxygenase 45 kDa subunit) (Particulate methane monooxygenase 47 kDa subunit) (Particulate methane monooxygenase hydroxylase 45 kDa subunit) (Particulate methane monooxygenase hydroxylase alpha subunit) (pMMO-H alpha subunit)
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MKTIKDRIAKWSAIGLLSAVAATAFYAPSASAHGEKSQAAFMRMRTIHWYDLSWSKEKVKINETVEIKGKFHVFEGWPETVDEPDVAFLNVGMPGPVFIRKESYIGGQLVPRSVRLEIGKTYDFRVVLKARRPGDWHVHTMMNVQGGGPIIGPGKWITVEGSMSEFRNPVTTLTGQTVDLENYNEGNTYFWHAFWFAIGVAWIGYWSRRPIFIPRLLMVDAGRADELVSATDRKVAMGFLAATILIVVMAMSSANSKYPITIPLQAGTMRGMKPLELPAPTVSVKVEDATYRVPGRAMRMKLTITNHGNSPIRLGEFYTASVRFLDSDVYKDTTGYPEDLLAEDGLSVSDNSPLAPGETRTVDVTASDAAWEVYRLSDIIYDPDSRFAGLLFFFDATGNRQVVQIDAPLIPSFM
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Methane monooxygenase is responsible for the initial oxygenation of methane to methanol in methanotrophs. At least in vitro, specific quinols can replace NADH as reductants.
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G1UH28
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CHIT_PUNGR
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Acidic endochitinase Pun g 14, amyloplastic (EC 3.2.1.14) (Chitinase III) (Pomegranate seed chitinase) (allergen Pun g 14)
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MAKTLPFSRALLLSLSILLVARAISAGDIAIYWGQNGGEGTLASTCDTGRYAYVIVSFVTTFGNFRAPVVNLAGHCDPAAGTCTGLSDEIRSCQGKDIKVLMSIGGGAGDYSLVSEADADNFADYLWNNFLGGQSSSRPLGDAVLDGIDFDIELGTTTFYDTLARALSSRSTQAAKVYLTAAPQCPHPDSHLDAALNTGLFDNVWIQFYNNPLAQCQYSSGNTNDILSSWNTWTSSTTAGKIFLGLPAAPEAAGSGYIPPDVLTGQILPQIKTSAKYGGVMLYSKFYDTTYSTTIKDQV
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Hydrolyzes chitin. Probable calcium storage protein of the seeds. Binds calcium ions with high capacity and low affinity. Involved in seed germination.
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G2IQQ5
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LIGJ_SPHSK
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2-keto-4-carboxy-3-hexenedioate hydratase (KCH hydratase) (EC 4.2.1.-)
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MMMIIDCHGHYTVLPKAHDEWREQQKAAFKAGQPAPPYPEISDDEIRETIEANQLRLIKERGADMTIFSPRASAMAPHVGDQSVAVPWAQACNNLIARVVDLFPETFAGVCMLPQSPEADMTSSIAELERCVNELGFIGCNLNPDPGGGHFKHPPLTDRFWYPFYEKMVELDVPAMIHVSGSCNPAMHATGAYYLAADTIAFMQLLQGNLFADFPTLRFIIPHGGGAVPYHWGRFRGLADMLKQPSLDTLLMNNVFFDTCVYHQPGINLLADVIDNKNILFGSEMVGAVRGIDPTTGHYFDDTKRYIDALDISDQERHAIFEGNTRRVFPRLDAKLKARGL
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Contributes to the degradation of lignin at the level of the protocatechuate 4,5-cleavage pathway. Catalyzes the hydration of the double bond of (3Z)-2-keto-4-carboxy-3-hexenedioate (KCH) to (4S)-4-carboxy-4-hydroxy-2-oxoadipate (CHA, also named (2S)-2-hydroxy-4-oxobutane-1,2,4-tricarboxylate). Is involved in the catabolism of both vanillate and syringate.
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G2IQQ8
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LIGK_SPHSK
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4-carboxy-4-hydroxy-2-oxoadipate aldolase (CHA aldolase) (EC 4.1.3.17) (Oxaloacetate decarboxylase) (OAA decarboxylase) (EC 4.1.1.112)
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MRGAAMGVVVQNIERAPLEVIDGLAACGVATVHEAQGRTGLLASYMRPIYRGARVAGSALTISAPPGDNWMVHVAIEQLKAGDILLLAPTSPCEDGYFGDLLATSAQARGCRGLVIDAGVRDVRDLTEMNFPVWSKAIYAQGTVKNTLGSVNVPVVCANALVNPGDVIVADDDGVCVVPLANAEKVLEAARAREANEGDKREKMANGVLGLDLYKMRERLEKEGLKYV
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Contributes to the degradation of lignin, being involved in the final step of the protocatechuate 4,5-cleavage pathway. Catalyzes the conversion of 4-carboxy-4-hydroxy-2-oxoadipate (CHA, also named 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate) to pyruvate and oxaloacetate but also the decarboxylation of oxaloacetate to pyruvate and CO2. Is essential for catabolism and utilization of vanillate and syringate. Is also able to catalyze the formation of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) from two molecules of pyruvate.
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G2IQS7
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LIGM_SPHSK
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Vanillate/3-O-methylgallate O-demethylase (Vanillate/3MGA O-demethylase) (EC 2.1.1.341)
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MSAPTNLEQVLAAGGNTVEMLRNSQIGAYVYPVVAPEFSNWRTEQWAWRNSAVLFDQTHHMVDLYIRGKDALKLLSDTMINSPKGWEPNKAKQYVPVTPYGHVIGDGIIFYLAEEEFVYVGRAPAANWLMYHAQTGGYNVDIVHDDRSPSRPMGKPVQRISWRFQIQGPKAWDVIEKLHGGTLEKLKFFNMAEMNIAGMKIRTLRHGMAGAPGLEIWGPYETQEKARNAILEAGKEFGLIPVGSRAYPSNTLESGWIPSPLPAIYTGDKLKAYREWLPANSYEASGAIGGSFVSSNIEDYYVNPYEIGYGPFVKFDHDFIGRDALEAIDPATQRKKVTLAWNGDDMAKIYASLFDTEADAHYKFFDLPLANYANTNADAVLDAAGNVVGMSMFTGYSYNEKRALSLATIDHEIPVGTELTVLWGEENGGTRKTTVEPHKQMAVRAVVSPVPYSVTARETYEGGWRKAAVTA
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Involved in the catabolism of vanillate and syringate. Catalyzes the transfer of a methyl moiety from vanillate or 3-O-methylgallate (3MGA) to tetrahydrofolate, forming protocatechuate (PCA) or gallate, respectively, and methyl-tetrahydrofolate. Has similar activities with both substrates. Cannot use syringate. Uses an ordered, sequential kinetic mechanism.
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G2NFJ9
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LAM55_STREK
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Exo-beta-1,3-glucanase (EC 3.2.1.58) (Glucan 1,3-beta-glucosidase) (Laminarinase) (SacteLam55A)
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MHVPPTDPARSAPPASPHRRRRPKALGLTALAAAMLMAVPTTQAAFGSDVRPAAAQEVVGGGDLGPNVLVFDPSTPDIQGKVDEVFRKQESNQFGTDRYALMFKPGTYNDINAQIGFYTSIAGLGLNPDDTTFNGDVTVDAGWFDGNATQNFWRSAENLALNPVNGTNRWAVSQAAPFRRMHVKGGLNLAPDGYGWASGGYIADSKIDGEVGPYSQQQWYTRDSSVGGWGNGVWNMTFSGVEGAPAQSFPEPPYTTLETTPVSREKPFLYLDGDDYKVFVPAKRTNARGTSWGNGTPEGESLPLDQFYVVKPGATAETINAAVDQGLHLLFTPGVYHVDQPIEIDRANTVALGLGLATIIPDNGVTALKVGDVDGVKVAGLLVDAGPVNSETLVEVGSDGASGDHAANPTSLQDVFVRIGGAGPGKATTSIVVNSNDTIIDHTWVWRADHGEGVGWETNRADYGVHVKGDNVLATGLFVEHFNKYDVQWSGENGKTIFYQNEKAYDAPDQAAIQNGDIKGYAAYKVDDSVTTHEGWGMGSYCYFNVNPDIRQQHGFQAPVKPGVKFHDLLVVSLGGKGQYEHVINDIGDPTSGDTTIPSQVVSFP
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Exo-beta-1,3-glucanase that specifically hydrolyzes laminarin and laminarioligosaccharides, producing glucose and laminaribiose as end products.
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G2Q0E2
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PEX10_THET4
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Peroxisome assembly protein 10 (EC 2.3.2.27) (Peroxin-10)
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MATQPPPARPPPPLTSSPYPYAAAPDIIRAHQKDAYFQGVLANRLSDLHRRLRGARSAHAWAAETRTFAAALYLCLTTLLGNRTLGEEYCDLVQVEEAPSKLFASSSSKAADDHIYENGLGGGGDGGPLLPSLPRRAGYILTAIVLPHLASRALPSVRSAIRKRLQSRLATLSRRRQQTGTKSGSGRGGRGGGGGITEYRVLRYLLTHLTPLTSGAHFRAATLAVFYFTGAYYELSKWVWGLRYVFTTRAGRVVDDDHNRHHHSPQHGGGNGGRAGYEVLGVLLVVQMAVRAWLHVREQLSSGSVAGGGGEEEEDGEDGFRERTAFGPGTNVDVSLDEHAFTSNNELLGGGGGGGGSSSQRSLGEIGAMAHTPVLKAGRARYDLGTSDKVMGWIKGAQQRKCTLCLEELKDPAATQCGHVFCWACIGDWVREKPECPLCRREAMVQHILPLRAA
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E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (By similarity). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12 each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (By similarity). PEX10 also regulates PEX5 recycling by acting as a E3 ubiquitin-protein ligase (By similarity). When PEX5 recycling is compromised, PEX10 catalyzes polyubiquitination of PEX5 during its passage through the retrotranslocation channel, leading to its degradation (By similarity).
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G2Q1C9
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PEX2_THET4
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Peroxisome assembly protein 2 (EC 2.3.2.36) (Peroxin-2)
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MSDSDPKPTAAKGAAPTSIPNSTRNPNPTPPNPNPNPNPISTPAPTPTATPSPPIASSSNNGNNSTRSTNIDTNNNTNNAFFQAQQRIAARREAREAAAAARQATQQSASRLRARIAASQSPLLRRLGTSTLSLWDTLTSREGTRPAFRVGQVDAELLDEELVELLRGQVREALRYVGGGGGGGGGGGGGGVGSGVAQDWEAEISLALRAVLFKLTVWDHDATYGAALQNLKYTDARRDGPALAPPSRWQKALYGLVTVGGRYLWAKWEDWLLEQDDGFEGPSPRVKRLARWTSALSTLHASAALVSFLVFLLHGRYRTLLDRLLRMRLAPPTSQVSREVSFEYLNRQLVWHAFTEFLLFVLPLVGINRWRRWLARTWRRTKKIMTADADGGAGDKKGEYSFLPERTCAICYRDQNSASSETELLAAASGGVVGSAQTDITNPYEAIPCGCTYCFVCLATRIEREEGEGWPCLRCGELIKECKPWNGDVLEEPQVKSSPATTKTVVFADDVKAPSDHEEEENEEEEEQQGELGENEGESSQVLVEADPDGGLNDLRPETPSVSSDQADDSRGSESEDYEAEEDGLDEDPES
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E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (By similarity). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12 each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (By similarity). PEX2 also regulates peroxisome organization by acting as a E3 ubiquitin-protein ligase (By similarity). PEX2 ubiquitinates PEX5 during its passage through the retrotranslocation channel: catalyzes monoubiquitination of PEX5 at 'Cys-6', a modification that acts as a signal for PEX5 extraction into the cytosol (By similarity).
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G2Q9A5
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MYCA_THET4
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Hybrid PKS-NRPS synthetase mycA (EC 2.3.1.-) (EC 6.3.2.-) (Myceliothermophin biosynthesis cluster protein A)
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MVQTPRQKKFGNEPIAIIGSACRFPGAASTPSKLWELLRKPKDLLTKIPPNRFNADSFYHPDGAHHGASNVTESYFLEEDPRLFDAAFFNVKPVEAHSIDPQHRMLLEVVYESLEAAGQSIEGLAKSQTGVFVGLMCADFSDHILRDLDAIPTYMATGTARSLISNRISYFFDWHGPSMTIDTACSSSLFAVHQAVQLLRSGDSDLAVAAGSNLILGPELYIGESKLKMLSPTGRSRMWDADADGYARGEGVAAVILKRLSDAIRDGDHIESIIRESGINSDGRTKGLTMPNELAQADLIVRTYQKAGLDPTKEEERCQYFEAHGTGTEAGDCREAEGISRAFFGYQGGNEGPAPPSQSEKLYVGSIKTVVGHTEGTAGLAGLLKASLAIQHSTIPPNMLFERLSPKVAPFYKGVEIATEAKPWPKASDVRRASVNSFGFGGANAHVILENYEPPAVAAAGTGAGAGDAASQTSFTPFVFSAASETALEGVLEAYAAHLRENPDLPLRDLSYTLHSRRSALGVRAALPAVASTQQLANSISDHLELARAGRNDKSAGQGASIGSRPIAATPRLLGVFTGQGAQWAAMGKELIQGSAFVRDRIKSLESALSDLPASARASWSLTDELLADAASSRLGEALLAQPLCTAVQIVLVDLLREAGIEFAAVVGHSSGEIAAAYAARIISAEEAIKIAYYRGLCVEEHVKTEGAMMAVGTSYEDATELCNLDAFSGRLGIAACNSPSSVTLSGDAAAIREAKDILDDEKKFARPLKVNKAYHSHHMAACSAPYKQALEACNIEPRQLAEEEGGCVWYSSVYPGTAMGTTAAHIEDLKGEYWKDNMLRPVLFAQALETAIERNEDSPFNLVIEVGPHPALKGPASETLTALYGKKQLPLPPYTGTLSRGSGDIAALSVTLGTAWSRFGSPFVNFAQYEALLTGEPRSARKVVPNLPTYKWDHDKVFWHDTRLSRAMRNRKELPNPLLGRRIPDGVTDEMRWRNIIRPSELPWISGHQLQGQMVYPAAAYLSTAIEACAFLAEGSVVESVEIRDFDLGKALVFDGNTEQTGVETLFSLSNIVKKGPKQITANFAFHAALGADADVLSRLGSGRVIVTLAGTGTGAGTGRLLLPPQRAPEPADTAEVREDEFYASLEKLGYEYTNDFRALSGMRRKLDHGSAYVRVPGHELAADAVLVHPALLDCALQAIFLAYWYPNDGSLDQLQVPTGIASLTVNTSLCRQDLAEGVRLPLESFLTEDPLSTATIGGDVEVYGRDGRTPLIQVQGVRITPLATRTGQADRQLFMENVWGPGAPDGTLAADNRAGAADFELASDLERLTIYFMRKLVRDIPPSQRQGLEWHHEALFDFVEHVLEQTANGRQRFCKPEWLDDTWESISHIRAKHPDSIEVELTHAVGENLAAAVRGETQILQHMFKDNLLNRYYVEALGIRETTAFLARTVAQIVHRYPHMDILEIGAGTGGATKAIFREIGRTFSSYTYTDISTGFFEKAQEVFAATADKMIFRALDIEKDVVEQGYREGAYDLIIGSLVLHATKSLDKTMRATRRLLKPGGYLVLLELTNLDVLRTGFAMSGLPGWWLGRDDGRRYSPCATSARWHQVLLGAGFSGIDTITPEVDVLPRPFSVIVSQAVEPRVNLLREPLSHPAESNASAADGGELVIVGGQSLATVILIDSVLDLTRHFGFAVTRLSSLDEFDAAAVSPTALVLNLAELDQPVFSNLTGETMRGLQSMLDYQRTILWVTQGCRAEQPYMSMSVGLGRTVALEAPGVKLQFLDLDISRKPNSKLVAEALIRLRFTRDEGSTRGILYSTEQELVEDDGRILVPRLLPIRPANERYNSSKRKITKLTEVGAESPALVLASTDAGYAVYEGASDDARAGASDDTAIIRVTASTLLPVIGNLYGVLGQEKDSGSWVLGLSSTNGSHVAVPRGQVRLVGDAILKEEAQQQQRLLLLALLAVEAQSSQILSAVPRDSKLLVNEPPAGLAGSLVRRAAERGTTVVFTASTTDAADLGLPHGHPVVSLSPLSSKRAVRAALPADVALFLDCSAEPEGVGLGSLIAACVPPSGQSIKLAELGEKLRQQPTLVDAPPSDTELASLPTLVDWSSGDKVPVSLQSVDSLIRFDGAKTYVLFGLTSDLGRSLVDWMASHGARNVVMTSRRPNIDPKWLEERRARGIRIQAFANDITDPAAVEDLVNSIRRSFPPIAGIMHGAMVLEDVPFSEMSLEIMNKVVRPKVMGTIHLDRLFQDEQLDFFVFFSSLASASGNRGQSNYSAANMYMTAKTFERRRKGLAASVLHLGAVMGIGYVMREASEIVFPAIRRAGFQWMDERAFRQCVAEAILAGRPDSGRSPEIVTGLRVINVDEEEPAPWMDNPRFQHCIVRGGTDSGAKKNQGGAAAGVKTRLLEAATPEEVLDIIRDSFLQKLQIMLQTELQTDDERANILAANAEDTGIDSLVAVEIRSWFQKEMDVDVPVLKILGGATMADLVAFAHEKLPEGLTPNLGNESAAAAAAAAAERSQSRVEITPAPDAVDTSRTSTTVFSAPPTLDPASSSTGSDHPTSVTSSGHTTPAHELETGLSPPSAPPCAPREQDVERTAPMSLGQSRFWFLRSYIEDQTTFNISFSVRLKGPLQVDKLESAIQTLGHRHQALRTAFVARPGQLLPDQAVLKRSLLRLEKRQIKEAAEASEAFEAMKNYVFAIERGESMRLVLLSLSPSDHFLVVGYHHINMDGASLEVFMADLMKLYTGRPLAPRPFQYPDFAAQQQLEVQQGKMDRDIAWWQDQLAGAALFRLLGTGDLCIGMADANRFEGDLASSVGMYLNLLPLRFRPSGDRTFRDTLKDVRRTAYAAMAHSHVPFDLVLNNLKIQRSTLHSPLFQAFINYRAGVAEKRSLGAVEGEGEQYHFGRSAYDISLDIMENPNSDPRLMFLVQEQLYSEHEANILADTYMHLLDLFARKPDSTLGSAPAFAPETAEEAIRLGRGNPVVSDWPQTIVHRVDDIIQRNPDTIAVREALGGRVWNYRQLRDRVGAIARALLAAGVTGGSRVALFQEPGFDWVSSLLAVMRVGAVFVPIDPGTPVERLAVIAAAARPAVALSHDATESAQEAALAVIRDAGGARVVNVSRGEGEGEGDVAGAGAPANLAQPDEAAVIFFTSGTTGVPKGAIVPHRGITNFMEHTCDIRGPEVVLFHSALGFDLAMWQCFSGLAHGGTLVVAPRSMRGDPVAITGLMAKEKITCTGATPSEYHTWIQYGFSKLAQSTSWRIAMTGGEQCTPKLVDDFRSLRLPGLRLWNCYGPSEVTVGSNQAEIPLSEPPQAPVTVGKAMPNRSVYILDDRLEPVCAGAPGEVVIGGVGVGLGYLGNDHLTAEKFVPDPFAPAGGSAKMYRTGDRGRLTRDGELEILGRIDGDSQIKLRGIRIEMQDVEQAILRSADGALASVCVTARGEPPTLVAHAVFRPDAPVPRRDRDAFLRRLASSLPLPQYMHPAVIVEIPSMPLNLHGKLDRRAVQELPTRVVAAKEEEEEKRPNGSSAAPLTQQELQLRSRVWERVIPEDVLSLYTVDRDTDFFHVGGNSMLLVEVQRRVKDEFGANLTIMRLFENSTLGAMAAAVHDAALESAGVDAAIDWEDETALTKDLADAVPSPEERAAAGRRRLDNNGPGGKVVVILTGATGFIGRELLARLLSSPDVAEVRCIAVRDPSRLADVVESNPGRVSVHAGDLTSVEETVGEEDEQRLFADAHAVIHCGADVSFLKTYATLRRANVGSTKALARLALRHGLDFHYVSTAATGRLLLVADPSSSPTARGDVFGEESVAAYPPPPGWLDHYVASKWASEAFLERAAARLGLRVWVHRPTSVTGPGAGETDVMSTVMRFAKKLRAVPVSSRWRGSLDFVPVETVADGIVGAVIRGGREHQQQQQQQETTPEEAGSVVPVKFLHHSGGLVIPIERLQSHLEEEDGVEYRTVPLGQWIEMAVAEGLNVLVAAYLASVDEMDTDIVFQAYVKG
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Hybrid PKS-NRPS synthetase part of the gene cluster that mediates the biosynthesis of myceliothermophins, mycotoxins that contain a trans-fused decalin ring system connected to a conjugated 3-pyrrolin-2-one moiety and that have potential anti-tumor properties. The polyketide synthase module (PKS) of the PKS-NRPS mycA is responsible for the synthesis of the octaketide backbone. The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the octaketide with a leucine. A reductase-like domain (R) at the C-terminus catalyzes the reductive release of the polyketide-amino acid intermediate. Because mycA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase mycC. Following mycA-catalyzed construction and release of aminoacyl polyketide aldehyde, Knoevenagel condensation yields the expected ketone. This C18 keto acyclic precursor is the substrate of the Diels-Alderase mycB, that catalyzes the Diels-Alder cycloaddition to produce myceliothermophin E. A yet unknown oxygenase involved in the production of myceliothermophin A, via substitution with a hydroxyl group at the C21, has still to be identified.
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G2QG48
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XYLO_THET4
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Xylooligosaccharide oxidase (XOS) (EC 1.1.3.-)
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MHLLPLTVSATAVVSAASSPHAKRAAIDECLKNAKVPVTARNSTEWKTDASPFNDRLPYTPAAIAKPATVEHIQAAVLCAAEVGVKANPKSGGHSYASFGLGGEDGHLVVELDRMYNVTLDPETHIATVQPGARLGHIATVLYEEGKRAFSHGTCPGVGVGGHSLHGGFGFSSHSHGLAVDWITSADVVLANGSLVTASETENPDLFWALRGAGSNFGIVASFRFKTFAAPPNVTSYEINLPWTNSSNVVKGWGALQEWLLNGGMPEEMNMRVLGNAFQTQLQGLYHGNASALKTAIQPLLALLDANLSSVQEHDWMEGFRHYAYSGEIDITDPGYDQSETFYSKSLVTSALPPDVLERVAEYWIETANKVRRSWYIIIDMYGGPNSAVTRVPPGAGSYAFRDPERHLFLYELYDRSFGPYPDDGFAFLDGWVHAFTGGLDSSDWGMYINYADPGLDRAEAQEVYYRQNLDRLRRIKQQLDPTELFYYPQAVEPAEV
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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. Xylooligosaccharide oxidase is able to oxidize a variety of substrates including D-xylose, D-cellobiose, lactose and arabinose. The enzyme acts primarily on xylooligosaccharides, indicating that it prefers pentose-based oligosaccharides over hexose-based oligosaccharides.
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G2QND5
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FAEB_THET4
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Feruloyl esterase B (EC 3.1.1.73) (Cinnamoyl esterase) (Ferulic acid esterase B) (FAEB)
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MLVRSFLGFAVLAATCLAASLQEVTEFGDNPTNIQMYIYVPDQLDTNPPVIVALHPCGGSAQQWFSGTQLPSYADDNGFILIYPSTPHMSNCWDIQNPDTLTHGQGGDALGIVSMVNYTLDKHSGDSSRVYAMGFSSGGMMTNQLAGSYPDVFEAGAVYSGVAFGCAAGAESATPFSPNQTCAQGLQKTAQEWGDFVRNAYAGYTGRRPRMQIFHGLEDTLVRPQCAEEALKQWSNVLGVELTQEVSGVPSPGWTQKIYGDGTQLQGFFGQGIGHQSTVNEQQLLQWFGLI
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Feruloyl esterase which acts in synergy with xylanases in degradation of plant cell walls. Hydrolyzes the ester linkage of hydroxycinnamic acids (ferulic acid (FA) and p-coumaric acid) and diferulates present in plant cell walls. Is active on substrates containing ferulic acid ester linked to the C-5 and C-2 linkages of arabinofuranose, while it was found capable of de-esterifying acetylated glucuronoxylans. Efficiently releases ferulic acid (FA) from destarched wheat bran when incubated with an M3 xylanase.
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G2QNH0
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ADT_THET4
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ADP/ATP translocase (ADP/ATP carrier) (TtAac)
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MSNKQETKILGMPPFVVDFLMGGVSAAVSKTAAAPIERIKLLVQNQDEMIKAGRLDRRYNGIIDCFRRTTADEGLMALWRGNTANVIRYFPTQALNFAFRDKFKAMFGYKKDKDGYAKWMAGNLASGGAAGATSLLFVYSLDYARTRLANDAKSAKGGGARQFNGLIDVYRKTLASDGIAGLYRGFGPSVAGIVVYRGLYFGMYDSIKPVVLVGPLANNFLASFLLGWCVTTGAGIASYPLDTVRRRMMMTSGEAVKYKSSIDAFRQIIAKEGVKSLFKGAGANILRGVAGAGVLSIYDQLQILLFGKAFKGGSG
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ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell. Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane.
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G2TRN4
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ERH_SCHPO
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Enhancer of rudimentary homolog 1
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MSPPPAESHIILLIQQGSDPKTRIWSDHCSLRSAIEYIVGVYQTNQAVSEKESIDVSRFFNFFDEIYDCVPLVYDRHFRAYIPHEKQWLLHHAQEYLTAARQIP
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Forms part of the erh1-mmi1 complex that recruits the CCR4-NOT complex and the NURS complex to target RNAs. Suppresses the meiotic program during vegetative growth and promotes the meiotic program during mating. Recruitment of the NURS complex to target mRNAs promotes mRNA decay by engagement of the nuclear exosome, and formation of heterochromatin islands at meiotic genes silenced by the exosome. Recruitment of the CCR4-NOT complex to target RNAs promotes heterochromatin formation at RNAi-dependent heterochromatin domains (HOODs), including a subset of meiotic genes, lncRNAs and retrotransposons. Recruitment of the CCR4-NOT complex to rDNA promotes rDNA heterochromatin assembly.
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G2X4G0
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424Y_VERDV
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Effector Vd424Y (EC 3.2.1.8) (Endo-1,4-beta-xylanase)
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MVSFTSLLAAFSVVSGVLTSPIAVVPEVNTALAKRTPSSTGTSGGFYYSFWTDTPNSVTYTNGDAGKFSVSWKNNNGNHVGGKGWRTGSARTIKYSGSYKPNGNSYLAIYGWTRSPLIEYYIVESFGTYNPSTGATSKGQFTVDGSVYDLYTSTRTNAPSIEGTRTFTQFWSVRRTKRTSGSVNTGAHFAAWKKAGMNLGSHDYQILAVEGYKSSGSATMTVS
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Secreted effector that localizes to the host nucleus to contribute to the virulence process. Induces host innate immunity responses triggers BAK1-and SOBIR1-dependent cell death, salicylic acid signaling and jasmonic acid signaling.
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G2X4M1
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ISC1_VERDV
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Secreted isochorismatase effector Isc1 (EC 3.3.2.1)
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MSSFRSMLGVPPSTASTQDSVLVIIDAQGEYAEGKLKISNIEASRPNISSLLEKYRAANAPIVHVVHETPAGAPLFTQGTKLAEIFDELTPKEGEAVVTKHHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVIVAEDAVGDRDIPGVDAAQLVKVALAEIADVFGTLVSSKDIN
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Secreted isochorismatase required for full virulence of V.dahliae. Suppresses salicylate-mediated innate immunity of the host by disrupting the plant salicylate metabolism pathway via hydrolysis of its isochorismate precursor.
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G2X7W6
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ATC3_VERDV
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Phospholipid-transporting ATPase DRS2 (EC 7.6.2.1) (VdDRS2)
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MAGRPTGGPQGAPSHDLLLDLENDQPVYGGGQRSTLNDDDLMRTYTRDQESGQDQGRPSVSYDDFIGAGQSRQHGTGSQPGGPGQSSSSNNNNNNNVSAPYSRSGRQYSQTSDLGNYQRYADDFDDYPADGDSFYQQGGALNGGGADAAARHNARNRNSVLTMGGGFFGKMKNRLGMGQGYSEMDLPLTEPGGGGGGAGGGGHSRADSSGIDPPKRDKKFDMGNFKFGFGRSKPDPSTLGPRIIHLNNPPANAANKYVNNHVSTAKYNIATFLPKFLLEQFSKIANVFFLFTAALQQIPGLSPTNRFTTIIPLVAVLMVSAGKELVEDYRRKQADAALNTSRAQVLRGSTFEETKWINVAVGDIVRVESEEPFPADIVLLASSEPEGLCYIETANLDGETNLKIKQALPETSQMVSSSELSRLGGRMKSEQPNSSLYTYEATLTMQTGGGEKELPLNPEQLLLRGATLRNTPWIHGVVVFTGHETKLMRNATAAPIKRTKVEKKLNTLVLLLVGILMVLSIISTVGDLIIRRVEGDAISYLMLDQPDTAGKIAETFFKDMVTYWVLFSSLVPISLFVTVEMVKYWHGILINDDLDMYYDRNDTPANCRTSNLVEELGMVEFVFSDKTGTLTCNMMEFKQASIAGIQYADEVPEDRRATIQDGVEVGLHDYKRLKENRKNHSSAPAIDHFLALLATCHTVIPEKGDEKGGKIKYQAASPDEGALVDGAATLGYTFTDRKPKAVFIEVDGQTLEYELLAVCEFNSTRKRMSTIYRCPDGVIRVYCKGADTVILERLNENNPHVEQTLTHLEEYASEGLRTLCLAMREVSEQEFQEWNQVYEKAATTVGGNRAEELDKASEMIEHDFFLLGATAIEDRLQDGVPETIHTLQEANIKVWVLTGDRQETAINIGMSCKLLSEEMMLLIINEESAAATRDNIEKKLEAIRAQGDRTIELETLALVIDGKSLTYALEKDLEKMFLDLAIMCKAVICCRVSPLQKALVVKLVKKYQKESILLAIGDGANDVSMIQAAHIGVGISGEEGLQAARSADVSIAQFRFLKKLLLVHGAWSYQRVAKTILYSFYKNITLYMTQFWYTFRNVFSGAVIYESWTLTFYNVFYTVLPPLALGILDQFISARLLDRYPQLYSMGQQNQFFRMKVFIEWLLNAVYHSIILYVFGELIWHGDLILENGQIAGHWMWGTALYAPVLLTVLGKAGLVTSNWTKYHVIAIPGSMAIWWIFIAVYGTVAPMIPFSPEFHGIVPKLYSSPIFWLQSFALAILCLLRDFAWKYAKRMYRPESYHHIQEIQKYNIQDYRPRMEQFQKAIRKVRQVQRMRKQRGYAFSQADESQARVLQAYDTTQNRGRYGEMTSSRPQGQGT
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Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylserine and small amounts of ethanolamine from the lumen to the cytosolic leaflet of the trans-Golgi network and cell membrane and ensures the maintenance of asymmetric distribution of phospholipids (By similarity). Required for efficient vesicle transport during toxin secretion.
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G2XDH0
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SCP41_VERDV
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Effector SCP41 (Cysteine-containing protein 41) (VdSCP41)
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MRTETASLLLLAALSVAEELTPNDVPLACANMCGPIVELSYKCDVDGTDELRKLKRRKLFSPQQQQQQQQQQQQSAPKAKRQADPEPQAPAPVPSSTNNQQAADVIFIPGSIGKFKTIPTPLPPADTGVPSMAVTPAAPAPTLPVLDLRPTTTPTNLNPNLPILATPILPSVPASTPLATASSTQVPLPVGNEADAGDGVDAGPAPSNSLNGNVGDMVDDAGNLWPGQKGRQAASDLETACICSNTSFNVRRVAGLCGDCLEQVSGDQGPMRAILASCNFTTERYEPEKESLVANVRVEATKPSFTQTAAASYSWRVSGPTWAVVVGAGMLLGMGW
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Effector that binds transcription regulators in the host plant to suppress the host's innate immune response. Inhibits the host plant transcription regulators CBP60G and SARD1.
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G2XKQ0
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SUMO5_HUMAN
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Small ubiquitin-related modifier 5 (SUMO-5) (SUMO1 pseudogene 1) (Ubiquitin-like 2) (Ubiquitin-like 6)
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MSDLEAKPSTEHLGDKIKDEDIKLRVIGQDSSEIHFKVKMTTPLKKLKKSYCQRQGVPVNSLRFLFEGQRIADNHTPEELGMEEEDVIEVYQEQIGGHSTV
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Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Regulates the life cycle of promyelocytic leukemia nuclear bodies (PML-NBs). PolySUMO1P1/SUMO5 conjugation on 'Lys-160' of PML facilitates recruitment of PML-NB components, which enlarges PML-NB. SUMO1P1/SUMO5 also increases polySUMO2/3 conjugation of PML, resulting in RNF4-mediated disruption of PML-NBs.
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G3C7W6
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S2611_CAVPO
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Sodium-independent sulfate anion transporter (Solute carrier family 26 member 11)
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MPSSLKGLGQAWLSSSSMALSACCSVSAWQKRLPVLAWLPRYSLQWLKMDFIAGLSVGLTVIPQALAYAEVAGLPPQYGLYSAFTGCFVYVFLGTSRDVTLGPTAIMSLLVSFYTFHEPAYAVLLTFLSGCIQLAMGLLHLGFLLDFISCPVIKGFTSAAAIIIGFGQIKNLLGLHNIPRQFFLQVYHTFLSVGETRLGDAILGLVCMVLLLVLKLMRDRIPPVHPEMPLCVRLSCGLVWTTATARNALVVSFAALVAYSFEVTGYQPFILTGEIAKGLPPVRVPPFSVTMANGTVSFTRMVQDLGAGLAVVPLIGLLESIAVAKAFASQNDYHVDANQELLAIGLTNMLGSFVSSYPITGSFGRTAVNAQSGVCTPAGGLVTGALVLLSLDYLTSLFYYIPKAALAAVIIMAVVPLFDTKIFGMLWRVKRLDLLPLCATFLLCFWEVQYGILAGTLVSTLFLLHFVARPKTQVSEGPVLILQLASGLHFPAIETLRDIVLSRALEVTSPRPAVLECSHVCSIDYTVVLGLAGLLEDFRKQGVSLVFSGLQAPVLHTLLAADLKGFQNFPTLEKAEQYVRQELGMEPYNVCEDSVPEHKVTLLTA
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Sodium-independent anion exchanger mediating bicarbonate, chloride, sulfate and oxalate transport. Exhibits sodium-independent sulfate anion transporter activity that may cooperate with SLC26A2 to mediate DIDS-sensitive sulfate uptake into high endothelial venules endothelial cells (HEVEC) (By similarity). In the kidney, mediates chloride-bicarbonate exchange, facilitating V-ATPase-mediated acid secretion (By similarity). May function as a chloride channel, playing an important role in moderating chloride homeostasis and neuronal activity in the cerebellum (By similarity).
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G3ECR1
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CAS9_STRTR
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CRISPR-associated endonuclease Cas9 (EC 3.1.-.-) (St-Cas9)
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MLFNKCIIISINLDFSNKEKCMTKPYSIGLDIGTNSVGWAVITDNYKVPSKKMKVLGNTSKKYIKKNLLGVLLFDSGITAEGRRLKRTARRRYTRRRNRILYLQEIFSTEMATLDDAFFQRLDDSFLVPDDKRDSKYPIFGNLVEEKVYHDEFPTIYHLRKYLADSTKKADLRLVYLALAHMIKYRGHFLIEGEFNSKNNDIQKNFQDFLDTYNAIFESDLSLENSKQLEEIVKDKISKLEKKDRILKLFPGEKNSGIFSEFLKLIVGNQADFRKCFNLDEKASLHFSKESYDEDLETLLGYIGDDYSDVFLKAKKLYDAILLSGFLTVTDNETEAPLSSAMIKRYNEHKEDLALLKEYIRNISLKTYNEVFKDDTKNGYAGYIDGKTNQEDFYVYLKNLLAEFEGADYFLEKIDREDFLRKQRTFDNGSIPYQIHLQEMRAILDKQAKFYPFLAKNKERIEKILTFRIPYYVGPLARGNSDFAWSIRKRNEKITPWNFEDVIDKESSAEAFINRMTSFDLYLPEEKVLPKHSLLYETFNVYNELTKVRFIAESMRDYQFLDSKQKKDIVRLYFKDKRKVTDKDIIEYLHAIYGYDGIELKGIEKQFNSSLSTYHDLLNIINDKEFLDDSSNEAIIEEIIHTLTIFEDREMIKQRLSKFENIFDKSVLKKLSRRHYTGWGKLSAKLINGIRDEKSGNTILDYLIDDGISNRNFMQLIHDDALSFKKKIQKAQIIGDEDKGNIKEVVKSLPGSPAIKKGILQSIKIVDELVKVMGGRKPESIVVEMARENQYTNQGKSNSQQRLKRLEKSLKELGSKILKENIPAKLSKIDNNALQNDRLYLYYLQNGKDMYTGDDLDIDRLSNYDIDHIIPQAFLKDNSIDNKVLVSSASNRGKSDDFPSLEVVKKRKTFWYQLLKSKLISQRKFDNLTKAERGGLLPEDKAGFIQRQLVETRQITKHVARLLDEKFNNKKDENNRAVRTVKIITLKSTLVSQFRKDFELYKVREINDFHHAHDAYLNAVIASALLKKYPKLEPEFVYGDYPKYNSFRERKSATEKVYFYSNIMNIFKKSISLADGRVIERPLIEVNEETGESVWNKESDLATVRRVLSYPQVNVVKKVEEQNHGLDRGKPKGLFNANLSSKPKPNSNENLVGAKEYLDPKKYGGYAGISNSFAVLVKGTIEKGAKKKITNVLEFQGISILDRINYRKDKLNFLLEKGYKDIELIIELPKYSLFELSDGSRRMLASILSTNNKRGEIHKGNQIFLSQKFVKLLYHAKRISNTINENHRKYVENHKKEFEELFYYILEFNENYVGAKKNGKLLNSAFQSWQNHSIDELCSSFIGPTGSERKGLFELTSRGSAADFEFLGVKIPRYRDYTPSSLLKDATLIHQSVTGLYETRIDLAKLGEG
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CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). In type II CRISPR systems correct processing of pre-crRNA requires a trans-encoded small RNA (tracrRNA), endogenous ribonuclease 3 (rnc) and Cas9. The tracrRNA serves as a guide for ribonuclease 3-aided processing of pre-crRNA (Probable). Cas9/crRNA/tracrRNA endonucleolytically cleaves linear or circular dsDNA target complementary to the spacer yielding blunt ends Cas9 is inactive in the absence of the 2 guide RNAs (gRNA). Cas9 recognizes a 3'-G-rich protospacer adjacent motif (PAM, TGGTG in this organism) in the CRISPR repeat sequences to help distinguish self versus nonself, as targets within the bacterial CRISPR locus do not have PAMs. PAM recognition is also required for catalytic activity. When the CRISPR3/cas system consisting of cas9-cas1-cas2-csn2-CRISPR3 or just cas9-CRISPR3 is expressed in E.coli it prevents plasmids homologous to spacers 1 or 2 from transforming.
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G3FEX6
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POLG_JAEVM
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Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
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MTKKPGGPGKNRAINMLKRGLPRVFPLVGVKRVVMSLLDGRGPVRFVLALITFFKFTALAPTKALLGRWRAVEKSVAMKHLTSFKRELGTLIDAVNKRGKKQNKRGGNESSIMWLASLAIVIACAGAMKLSNFQGKLLMTINNTDIADVIVIPTSKGENRCWVRAIDVGYMCEDTITYECPKLAVGNDPEDVDCWCDNQEVYVQYGRCTRTRHSKRSRRSVSVQTHGESSLVNKKEAWLDSTKATRYLMKTENWIIRNPGYAFLAAALGWMLGSNSGQRVVFTILLLLVAPAYSFNCLGMGNRDFIEGASGATWVDLVLEGDSCLTIMANDKPTLDVRMINIEASQLAEVRSYCYHASVTDISTVARCPTTGEAHNEKRADSSYVCKQGFTDRGWGNGCGLFGKGSIDTCAKFSCTSKAIGRTIQPENIKYEVGVFVHGTTTSENHGNYSAQVGASQAAKFTVTPNAPSITLKLGDYGEVTLDCEPRSGLNTEAFYVMTVGSKSFLVHREWFHDLSLPWTSPSSTAWRNRELLMEFEEAHATKQSVVALGSQEGGLHQALAGAIVVEYSSSVKLTSGHLKCRLKMDKLALKGTTYGMCTEKFSFAKNPADTGHGTVVIELTYSGSDGPCKIPIVSVASLNDMTPVGRLVTVNPFVATSSSNSKVLVEMEPPFGDSYIVVGRGDKQINHHWYKAGSTLGKAFSTTLKGAQRLAALGDTAWDFGSIGGVFNSIGKAVHQVFGGAFRTLFGGMSWITQGLMGALLLWMGVNARDRSIALAFLATGGVLVFLATNVHADTGCAIDITRKEMRCGSGIFVHNDVEAWVDRYKYLPETPRSLAKIVHKAHQEGVCGVRSVTRLEHQMWESVRDELNVLLKENAVDLSVVVNKPVGRYRSAPKRLSMTQEKFEMGWKAWGKSILFAPELANSTFVVDGPETKECPDERRAWNSMQIEDFGFGITSTRVWLKIREENTDECDGAIIGTAVKGHVAVHSDLSYWIESRLNDTWKLERAVFGEVKSCTWPETHTLWGDGVEESELIIPHTIAGPRSKHNRREGYKTQNQGPWDENGIVLDFDYCPGTKVTITEDCGKRGPSIRTTTDSGKLITDWCCRSCSLPPLRFRTENGCWYGMEIRPVRHDETTLVRSQVDAFNGEMIDPFQLGLLVMFLATQEVLRKRWTARLTIPAVLGALLVLMLGGITYIDLARYVVLVAAAFAEANSGGDVLHLALIAVFKIQPAFLVMNMLSARWTNQENMVLVLGAAFFQLASVDLQIGVHGILNAAAIAWMIVRAITFPTTSTVAMPVLALLTPGMRALYLDTYRIILLVIGICSLLQERRKTMAKKKGAVLLGLALTSTGWFSPTTIAAGLMVCNPNKKRGWPATEFLSAVGLMFAIVGGLAELDIESMSIPFMLAGLMAVSYVISGKATDMWLDRAADISWEMEAAITGSSRRLDVKLDDDGDFHLIDDPGVPWKVWLLRMSCIGLAALTPWAIVPAAFGYWLTLKTTKRGGVFWDTPSPKPCLKGDTTTGVYRIMARGILGTYQAGVGVMYENVFHTLWHTTRGAAIMSGEGKLTPYWGSVKEDRISYGGPWRFDRKWNGTDDVQVIVVEPGKPAVNIQTKPGVFRTPFGEIGAVSLDYPRGTSGSPILDSNGDIIGLYGNGVELGDGSYVSAIVQGDRQEEPVPDAYTPSMLKKRQMTVLDLHPGSGKTRKILPQIIKDAIQQRLRTAVLAPTRVVAAEMAEALRGLPVRYQTSAVQREHQGNEIVDVMCHATLTHRLMSPNRVPNYNLFVMDEAHFTDPASIAARGYIATKVELGEAAAIFMTATPPGTTDPFPDSNAPIHDLQDEIPDRAWSSGYEWITEYAGKTVWFVASVKMGNEIAMCLQRAGKKVIQLNRKSYDTEYPKCKNGDWDFVITTDISEMGANFGASRVIDCRKSVKPTILEEGEGRVILGNPSPITSASAAQRRGRVGRNPNQVGDEYHYGGATSEDDSNLAHWTEAKIMLDNIHMPNGLVAQLYGPEREKAFTMDGEYRLRGEEKKNFLELLRTADLPVWLAYKVASNGIQYTDRKWCFDGPRTNAILEDNTEVEIVTRMGERKILKPRWLDARVYADHQALKWFKDFAAGKRSAVSFIEVLGRMPEHFMGKTREALDTMYLVATAEKGGKAHRMALEELPDALETITLIVAITVMTGGFFLLMMQRKGIGKMGLGALVLTLATFFLWAAEVPGTKIAGTLLVALLLMVVLIPEPEKQRSQTDNQLAVFLICVLTVVGVVAANEYGMLEKTKADLKSMFGGRTQAPGLTGLPSMALDLRPATAWALYGGSTVVLTPLLKHLITSEYVTTSLASISSQAGSLFVLPRGVPFTDLDLTVGLVFLGCWGQITLTTFLTAMVLVTLHYGYMLPGWQAEALRAAQRRTAAGIMKNAVVDGMVATDVPELERTTPLMQKKVGQVLLIGVSVAAFLVNPNVTTVREAGVLVTAATLTLWDNGASAVWNSTTATGLCHVMRGSYLAGGSIAWTLIKNADKPSLKRGRPGGRTLGEQWKEKLNAMSRDEFFKYRREAIIEVDRTEARRARRENNIVGGHPVSRGSAKLRWLVEKGFVSPIGKVIDLGCGRGGWSYYAATLKKVQEVKGYTKGGAGHEEPMLMQSYGWNLVSLKSGVDVFYKPSEPSDTLFCDIGESSPSPEVEEQRTLRVLEMTSDWLHRGPREFCIKVLCPYMPKVIEKMEVLQRRFGGGLVRLPLSRNSNHEMYWVSGAAGNVVHAVNMTSQVLLGRMDRTVWRGPKYEEDVNLGSGTRAVGKGEVHSNQEKIRKRIQKLREEFATTWHQDPEHPYRTWTYHGSYEVKATGSASSLVNGVVKLMSKPWDAIANVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPAGVKEVLNETTNWLWAHLSREKRPRLCTKEEFIKKVNSNAALGAVFAEQNQWSTAREAVGDPLFWEMVDEERENHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARYLEFEALGFLNEDHWLSRENSGGGVEGSGVQKLGYILRDIAGKQGGKMYADDTAGWDTRITRTDLENEAKVLELLDGEHRMLARAIIELTYRHKVVKVMRPAAGGKTVMDVISREDQRGSGQVVTYALNTFTNIAVQLVRLMEAEGVIGPQHLEQLPRKNKIAVRTWLFENGEERVTRMAISGDDCVVKPLDDRFATALHFLNAMSKVRKDIQEWKPSHGWHDWQQVPFCSNHFQEIVMKDGRSIVVPCRGQDELIGRARISPGAGWNVKDTACLAKAYAQMWLLLYFHRRDLRLMANAICSAVPVDWVPTGRTSWSIHSKGEWMTTEDMLQVWNRVWIEENEWMMDKTPITSWTDVPYVGKREDIWCGSLIGTRSRATWAENIYAAINQVRAVIGKENYVDYMSSLRRYEDVLIQEDRVI
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[Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Efficient virus attachment to cell is, at least in part, mediated by host HSPA5. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE-ProRule:PRU00860}. [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to conserve energy during unwinding (By similarity). [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place (By similarity). Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway (By similarity). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (By similarity). [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome (By similarity). Performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (By similarity). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity).
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G3FNQ9
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SPAZ_ORBOL
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Cuticle-degrading serine protease (EC 3.4.21.-) (Neutral serine protease Aoz1) (Aoz) (PII)
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MLTNGLISLLAIAGLATNAFAGPIRKVSNAGAAGAIADKYIVVLKKGLSDSAVSKHTNRISSFHSNVARDLTGARAHGVGRKFRFSSTGFNGYVGGFDKATLQEILNSPEVDYVEQDTVVTTYAEQTDSTWGLDRISHEDYSAPYTYEYDETAAGAGTTVYVIDTGIRISHDEFQTVNGSSRATWGFNSVDKTDSDGNGHGTHCAGTIAGKTYGVSKKAKVVAVKVLSAGGSGSTAGVVSGMNWVAENATPNFSVASMSLGGSKSTALNAAVDCIFNAGITIVVAAGNENQDAKNVSPASAPNAITVGAIDSSNKIASLSNWGTLIDVFAPGVGVLSSWATSDKETKTISGTSMACPHVAGLAAYYISASEGGADPATITDKITSSRRQWSGHREHPWLPKQDRLQRICLSTHSPKTNHQVTIVAS
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Hydrolyzes gelatin, casein, the chromogenic substrate azocoll and the cuticle of the nematode P.redivivus. Immobilizes P.redivivus. {ECO:0000269|Ref.1}.
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G3GTP0
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DNLI4_CRIGR
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DNA ligase 4 (EC 6.5.1.1) (DNA ligase IV) (Polydeoxyribonucleotide synthase [ATP] 4)
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MATSQTSQTVAAHVPFADLCSTLERIQKSKERAEKIRHFKEFLDSWRKFHDALHKNKKDVTDSFYPAMRLILPQLERERMAYGIKETMLAKLYIELLNLPREGKDALKLLNYRTPSGARTDAGDFAVIAYFVLKPRCLQKGSLTIQQVNELLDLVASNNSGKRKDLVKKSLLQLITQSSALEQKWLIRMIIKDLKLGVSQQTILNIFHNDAVELHNVTTDLEKVCRQLHDPAVGLSDISITLFSAFKPMLAAVADVERVEKDMKQQSFYIETKLDGERMQMHKDGSVYQYFSRNGYNYTDQFGASPQEGTLTPFIHDAFRTDVQVCILDGEMMAYNPTTQTFMQKGVKFDIKRMVEDSDLQTCYCVFDVLMVNNKKLGRETLRKRYDILNSTFTPIQGRIEIVQKKLAQTKNEVVDALNEAIDKREEGIMIKHPLSIYKPDKRGEGWLKIKPEYVSGLMDELDLLIVGGYWGKGSRGGMMSHFLCAVAEKPPHGEKPSVFHTLCRVGSGYTMKELYDLGLKLAKYWKPFHKKSPPSSILCGTEKPEVYIEPCNSVIVQIKAAEIVPSDMYKTGTTLRFPRIEKIRDDKEWHECMTLGDLEELRGKASGKLATKHLHVGDDDEPREKRRKPVSKMKKTIGIIEHLKAPNLSNISKVSNVFEDVEFCVMSGLDGYPKSDLENRIAEFGGYIVQNPGPDTYCVIAGCENIRVKNIISSDQHDVVKPEWLLECFKTKTCVPWQPRFMIHMCPSTKQHFAREYDCYGDSYFVDTDLDQLKEVFLGIKKAGEHQTPEEMAPVIADLEYRYSWDHSPLCMFRHCTVYLDLYAVINDSSSKIKATRLDVTALELRFHGAKVVSHLSEGVSHVIIGENQSRVSDFKVFRRTLKKKFKILQERWVTDSVDKGELQEENQYLL
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DNA ligase involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. Catalyzes the NHEJ ligation step of the broken DNA during DSB repair by resealing the DNA breaks after the gap filling is completed. Joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. LIG4 is mechanistically flexible: it can ligate nicks as well as compatible DNA overhangs alone, while in the presence of XRCC4, it can ligate ends with 2-nucleotides (nt) microhomology and 1-nt gaps. Forms a subcomplex with XRCC4 the LIG4-XRCC4 subcomplex is responsible for the NHEJ ligation step and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends. LIG4 regulates nuclear localization of XRCC4.
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G3HIK4
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CETP_CRIGR
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Cholesteryl ester transfer protein (Lipid transfer protein I)
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MLAVTLLSLALLGSTCACSTSTSYEAGIVCRITKAALLVLNQETAKVIQTAFQRASYPDIKGERSMMLLGRVTYGLHNIQISHLSIASSQVELVEAKSVDVSIQNASVIFKGTLNYGYKGAWGLNIEQSVDFEIESAIDLQINTKLTCDSGHVRTDAPDCSISFHKLLLHLQGEREPGWTKQLFTNIISFTLKMVLKGQVCKEINVISNIMADFVQTRAANIISDRDIEVDISLTRSPIITATYLESHHKGHFIYKNISEVLPLPAFSPTLLGDTRMLYFWFSEQVLDSLAKAAFQDGRLQLNLAETELKVVLETWHFNPNQEIIPEVITGFPSPGQVTVHCPRRPTISCQNKGVVVSSPVVMEFLFPHKDGQDSVTHTFEEDIVATIQASYSKKKLFLSLVDFQIKPKTTSNMAESSESIQNFLQLMITTVGIPEIMSRLEVALTTLMNSKGLDLFDIINPEIITRDGFLLLQMDFGFPEHLLVDFLQSLN
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Involved in the transfer of neutral lipids, including cholesteryl ester and triglyceride, among lipoprotein particles. Allows the net movement of cholesteryl ester from high density lipoproteins/HDL to triglyceride-rich very low density lipoproteins/VLDL, and the equimolar transport of triglyceride from VLDL to HDL. Regulates the reverse cholesterol transport, by which excess cholesterol is removed from peripheral tissues and returned to the liver for elimination (By similarity).
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G3I6Z6
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NOTC1_CRIGR
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Neurogenic locus notch homolog protein 1 (Notch 1) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]
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MGRSDSRAGALLEGGCEQNIDPRRAAHCHHPRLATSSLRCSQPSGTCLNGGRCEVANGTEACVCSGPFVGQRCQDPNPCLSTPCKNAGTCHVVEHGGTVNYACSCPLGFSGPLCLTPLDNACLANPCRNGGTCDLLTLTEYKCRCPPGWSGKSCQQADPCASNPCANGGQCLPFESSYICGCPPGFHGPTCRQDVNECSQNPGLCRHGGTCHNEIGSYRCVCRATHTGPHCELPYVPCSPSPCQNGGTCRPTGDTTHECACLPGFAGQNCEENVDDCPGNNCKNGGACVDGVNTYNCRCPPEWTGQYCTEDVDECQLMPNACQNGGTCHNTHGGYNCVCVNGWTGEDCSENIDDCASAACFQGATCHDRVASFYCECPHGRTGLLCHLNDACISNPCNEGSNCDTNPVNGKAICTCPSGYTGPACSQDVDECALGANPCEHAGKCLNTLGSFECQCLQGYTGPRCEIDVNECISNPCQNDATCLDQIGEFQCICMPGYEGVYCEINTDECASSPCLHNGHCMDKINEFLCQCPKGFSGHLCQYDVDECASTPCKNGAKCLDGPNTYTCVCTEGYTGTHCEVDIDECDPDPCHYGFCKDGVATFTCLCQPGYTGHHCETNINECHSQPCRHGGTCQDRDNSYLCLCLKGTTGPNCEINLDDCASNPCDSGTCLDKIDGYECACEPGYTGSMCNVNIDECAGSPCHNGGTCEDGIAGFTCRCPEGYHDPTCLSEVNECNSNPCIHGACRDGLNGYKCDCAPGWSGTNCDINNNECESNPCVNGGTCKDMTSGYVCTCREGFSGPNCQTNINECASNPCLNQGTCIDDVAGYKCNCPLPYTGATCEVVLAPCATSPCKNSGVCKESEDYESFSCVCPTGWQGQTCEIDINECVKSPCRHGASCQNTNGSYRCLCQAGYTGRNCESDIDDCRPNPCHNGGSCTDGINMAFCDCLPGFQGAFCEEDINECASNPCRNGANCTDCVDSYTCTCPAGFNGIHCENNTPDCTESSCFNGGTCVDGINSFTCLCPPGFTGSYCQYDVNECDSRPCLHGGTCQDSYGTYKCTCPQGYTGLNCQNLVHWCDSAPCKNGGKCWQTNTQYHCECRSGWTGFNCDVLSVSCEVAAQKRGIDVTLLCQHGGLCVDEEDKHYCHCQAGYTGSYCEDEVDECSPNPCQNGATCTDYLGGFSCKCVAGYHGSNCSEEINECLSQPCQNGGTCIDLTNTYKCSCPRGTQGVHCEINVDDCHPHLDPASRSPKCFNNGTCVDQVGGYSCTCPPGFVGERCEGDINECLSNPCDPRGTQDCVQRVNDFHCECRAGHTGRRCESVINGCRGKPCKNGGVCAVASNTARGFICRCPAGFEGATCENDARTCGSLRCLNGGTCISGPRSPTCLCLGSFTGPECQFPASSPCVGSNPCYNQGTCEPTSESPFYRCLCPAKFNGLLCHILDYSFTGGAGRDIPPPQIEEACELPECQEDAGNKVCNLQCNNHACGWDGGDCSLNFNDPWKNCTQSLQCWKYFSDGHCDSQCNSASCLFDGFDCQRTEGQCNPLYDQYCKDHFSDGHCDQGCNSAECDWDGLDCADHVPERLAAGTLVLVVLLPPEQLRNNSFHFLRELSHVLHTNVVFKRDAEGQQMIFPYYGHEEELRKHPIKRSAVGWTTSSLLPSTNGGRQRRELDPMDIRGSIVYLEIDNRQCVQSSSQCFQSATDVAAFLGALASLGNLNIPYKIEAVKSETVEPPLPSQLHLMYLAAAAFVLLFFVGCGVLLSRKRRRQHGQLWFPEGFKVSEASKKKRREPLGEDSVGLKPLKNASDGALMDDNQNEWGDEDLETKKFRFEEPVVVPDLDDQTDHRQWTQQHLDAADLRMSAMAPTPPQGEVDADCMDVNVRGPDGFTPLMIASCSGGGLETGNSEEEEDAPAVISDFIYQGASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILLRNRATDLDARMHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNKEETPLFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHHDIVRLLDEYNLVRSPQLHGTALGGTPTLSPTLCSPNGYLGNLKSATQGKKARKPSTKGLACGSKEAKDLKARRKKSQDGKGCLLDSSSMLSPVDSLESPHGYLSDVASPPLLPSPFQQSPSMPLSHLPGMPDTHLGISHLNVAAKPEMAALAGSSRLAFEPPPPRLPHLPVASSASTVLSTNGSXGEEEWLAPSQYNPLRPGVASGTLSTQAAGLQHGMMGPLHSSLSTNTLSPMIYQGLPNTRLATQPHLVQTQQVQPQNLQIQPQNLQPPSQPHLSVSSAANGHLGRSFLGGEHSQADVQPLGPSSLPVHTILPQESQALPTSLPSSMVPPMTTTQFLTPPSQHSYSSSPVDNTPSHQLQVPEHPFLTPSPESPDQWSSSSPHSNISDWSEGISSPPTSMPSQITHIPEAFK
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Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Involved in angiogenesis negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4(+) and CD8(+) cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. May be involved in mesoderm development, somite formation and neurogenesis. May enhance HIF1A function by sequestering HIF1AN away from HIF1A (By similarity). Required for the THBS4 function in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury. Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO) (By similarity).
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G3I8R9
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BIP_CRIGR
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Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
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MKFPMVAAALLLLCAVRAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTSEKDEL
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Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1. Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. May also play a role in apoptosis and cell proliferation (By similarity).
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G3KIM8
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ACRC_ANAPI
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Acryloyl-CoA reductase (NADH) (EC 1.3.1.95) (Propionyl-CoA dehydrogenase)
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MFLLKIKKERMKRMDFSLTREQEMLKKLARQFAEIELEPVAEEIDREHVFPAENFKKMAEIGLTGIGIPKEFGGSGGGTLEKVIAVSEFGKKCMASASILSIHLIAPQAIYKYGTKEQKETYLPRLTKGGELGAFALTEPNAGSDAGAVKTTAILDSQTNEYVLNGTKCFISGGGRAGVLVIFALTEPKKGLKGMSAIIVEKGTPGFSIGKVESKMGIAGSETAELIFEDCRVPAANLLGKEGKGFKIAMEALDGARIGVGAQAIGIAEGAIDLSVKYVHERIQFGKPIANLQGIQWYIADMATKTAAARALVEFAAYLEDAGKPFTKESAMCKLNASENARFVTNLALQIHGGYGYMKDYPLERMYRDAKITEIYEGTSEIHKVVIAREVMKR
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Probable catalytic subunit of the acryloyl-CoA reductase complex involved in the pathway of L-alanine fermentation. Catalyzes the irreversible NADH-dependent formation of propionyl-CoA from acryloyl-CoA. It can also use 3-buten-2-one as substrate.
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G3MZR2
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FUT7_BOVIN
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Alpha-(1,3)-fucosyltransferase 7 (bfut7) (EC 2.4.1.-) (Fucosyltransferase 7) (Fucosyltransferase VII) (Fuc-TVII) (FucT-VII) (Galactoside 3-L-fucosyltransferase) (Selectin ligand synthase)
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MQNAGLSPTPSLRALGGLAMAALLSTVWLWWRLGAAPGGAPAPQPTTTILVWHWPFASQPPELPGDTCTRYGVARCRLTVNRSLLAGADAVVFHHRELQTQQARLPLAERPRGQPWVWASMESPSHTRGLGRLRGVFNWVLSYRRDSDIFVPYGRLEPREGPAPPLPAKRGLAAWVVSNFQKRQRRVQLYRQLALHLRVDVFGRAAGQPLCASCLLRAVAGYRFYLSFENSEHRDYITEKFWRNALLAGAVPVVLGPPRAAYEAVAPPDAFVHVDDFGSARELAAFLTSMNESCYRRYFAWRDRFRVRLFSDWRERFCAICARFPQLPRGQVYQDLEGWFQA
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Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal alpha2,3 sialylated lactosamine unit of a glycoprotein or a glycolipid-linked sialopolylactosamines chain through an alpha-1,3 glycosidic linkage and participates in the final fucosylation step in the biosynthesis of the sialyl Lewis X (sLe(x)), a carbohydrate involved in cell and matrix adhesion during leukocyte trafficking and fertilization. In vitro, also synthesizes sialyl-dimeric-Lex structures, from VIM-2 structures and both di-fucosylated and trifucosylated structures from mono-fucosylated precursors. However does not catalyze alpha 1-3 fucosylation when an internal alpha 1-3 fucosylation is present in polylactosamine chain and the fucosylation rate of the internal GlcNAc residues is reduced once fucose has been added to the distal GlcNAc. Also catalyzes the transfer of a fucose from GDP-beta-fucose to the 6-sulfated a(2,3)sialylated substrate to produce 6-sulfo sLex mediating significant L-selectin-dependent cell adhesion. Through sialyl-Lewis(x) biosynthesis, can control SELE- and SELP-mediated cell adhesion with leukocytes and allows leukocytes tethering and rolling along the endothelial tissue thereby enabling the leukocytes to accumulate at a site of inflammation. May enhance embryo implantation through sialyl Lewis X (sLeX)-mediated adhesion of embryo cells to endometrium. May affect insulin signaling by up-regulating the phosphorylation and expression of some signaling molecules involved in the insulin-signaling pathway through SLe(x) which is present on the glycans of the INSRR alpha subunit (By similarity).
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G3QY98
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APOA1_GORGO
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Apolipoprotein A-I (Apo-AI) (ApoA-I) (Apolipoprotein A1) [Cleaved into: Proapolipoprotein A-I (ProapoA-I); Truncated apolipoprotein A-I]
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MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ
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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 (By similarity).
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G3UXB3
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NKX11_MOUSE
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NK1 transcription factor-related protein 1 (Homeobox protein SAX-2) (NKX-1.1)
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MSTSGPAAPGDVPALPPPPPGPGSGPAPPAPAATARDTMDGRAELPIFPRAGVPPLAASDTVPAVPEGAGAARPAAPPRPTSFSVLDILDPNKFNSRRRRCVLLGPVVPATCAPCAPAACVAVPAASGRSPRAELERRALSAATGVAAAAGAEPTSAGDSYRADEAEANGYSSGSGRSPTADSEDEAPEDEDEEEAPEVQDAQGTEEPRGGSGGLGARGSGCPGAAEVEASPVDDTAAPGPRGNSPGAPGPPATATGAGSAGSTPQGAAVTTKPKRKRTGSDSKSGKPRRARTAFTYEQLVALENKFKATRYLSVCERLNLALSLSLTETQVKIWFQNRRTKWKKQNPGADTSAPTGGGGGPGPGAGPGAGLPGGLSPLSPSPPMGAPLALHGPAGYPAHSPGGLVCAAQLPFLSSPAVLSPFVLGSQTYGAPAFYAPHL
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May be required for the coordinated crosstalk of factors involved in the maintenance of energy homeostasis, possibly by regulating the transcription of specific factors involved in energy balance.
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G3UZ78
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ADGB_MOUSE
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Androglobin (Calpain-7-like protein)
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MASKQAKRKEVHRINSAHGSDKSKDLYHFGSNVPPGSFEQKKGKFPIWPEWSEADINAEKWDAGKGGKEKDKTAKSPIFHFFEDPEGKIELPQSLKVFSWKRPQDFIFSRTPVVVKNEITFDLFSPNEHLLCSELMRWIISEIYAVWKIFNGGILSNYHKGNLGELPILPWKPWEHIYSLCKAVKGHVPLFNSYGKYVVKLYWMGCWRKITVDDFLPFDEENNLLLPATSYEFELWPMLLSKAIIKLANVDVHVAHRRELGELTVIHALTGWLPEVIPLHPAYVDRVWELLKEILPEFKLTEEPSSESKITTIDNKLKEATKENKDGKDGKNGKDLKDGKDMKDGKDGKDGKDGKDGKDGKDEKADARDLGKKNKKDGEKEKEKFKFSLHGSRPSSDVQYSMQSLSECSSAIQLPHMVVYATFTPLYLFENKIFSLEKMANSAEKLREYGLSHICSHPVLVTRSRSCPLVSPPKPPPLPAWKLIRHKKETVITDEAQDAVPKKPEQFLEISSPFLNYRMTPFTIPTETHFVQSVIKKGTPLGSSLPPLVENDLVASTSQGEMSIVNGNQSQGNIALQITLGKDEPSEPALADFHQLEATSLDRDLISLTTATLDKSQEELAINEGVAKEIWLDFEDFCVCFHHIYIFHKPHSYCLNFQKSEFKFVEERVPYYLFVDSLKPIELLVCFSALVRWGESGALTKDSPPVEPGLLTAEAITWKSLKPLSVVLRIHTYATKASVVRLPAGRHMLLFNAYSPVGHAIHVCSMTTFVIGDEDIVLPNFEPESYRFTEQSIIIMKAIGNVIANFKDKGKLPAALRDLQAAHYPIPLNNKELTAQHFRVFHISLWRLMKKSQVAKPPSNFKFAFRAMVFDTDLLDSFSEDVSLAEWVDLKYSTPINEKEYTSEEIAAAVKIQSMWKGCYVRLLMKARKPETKENVTVADTLQKIWAVLEMNLEQYALSLLRLMFKSKCKSMESYPCYQDEETKLAFADHTVNYADQPPNSWFIVFREIFLVPQDMIILPKVYTTLPICILHVINNDTLEQVPKVFQKVVPFLYTKNKKGYTFVAEAYTGDTFVSGARWKLRLIGSYNPLPFLARDSPCNTFSIKEIRDYYIPNDRKILFRYSIKVTVAQSITIQVRTSKPDTFIKLQVLESEEVITSTVGKGQAVIPAFYFLGNEKALSSQSSKQVLLSHPSPKKDPEVLTKKKSGQPGQKSFKGRSGGGLTDTGMPLLEEEILNIPTLEENSSTPQQCYKYIIQCLVLFNSWPLNETQLTFVQALKDMEKMDIKEKHEEPAPMGSPDSHAVSEGQKSVGVPKTTRKGKEKSAEKEKLAKEKQAPRFEPQQVQMPTAVHSQQEDPNKPYWILRLVSEHTDSDYVDVKKDTERADEIRAMKQAWETTEPGRAIKAAQARLKYLTQFIKKPVTTDTTTSAPSPETLSVSQSQTKSSEEGELDTGKYADIKELPPNAAGSVLWKKWQMTKTITSLTKFTSSESVPKEEPPQKEIPVVRQRSPTILETSPQQIRKALEFLDFSHYVRKTAAEAVLQTEELNKQQAMQKAEEIHQFRQHRSRILSIRDIDQEERFKQKDEVLEMYGEMRDSVDEARQKILDIREVYRNKLLEAERLRMEALAAQEAAVKIEIEKKSPASDSQKKKKVGKKK
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Required for sperm flagellum formation and maturation of elongating spermatids, thus playing an essential role in male fertility. Contributes to in vitro proteolytic cleavage of SEPT10 in a calmodulin-dependent manner.
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G3V6S8
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SRSF6_RAT
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Serine/arginine-rich splicing factor 6 (Pre-mRNA-splicing factor SRP55) (Splicing factor, arginine/serine-rich 6)
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MPRVYIGRLSYNVREKDIQRFFSGYGRLLEIDLKNGYGFVEFEDSRDADDAVYELNSKELCGERVIVEHARGPRRDRDGYSYGSRSGGGGYSSRRTSGRDKYGPPVRTEYRLIVENLSSRCSWQDLKDFMRQAGEVTYADAHKERTNEGVIEFRSYSDMKRALDKLDGTEINGRNIRLIEDKPRTSHRRSYSGSRSRSRSRRRSRSRSRRSSRSRSRSISKSRSRSRSRSKGRSRSRSKGRKSRSKSKSKPKSDRGSHSHSRSRSKDKYGKSRSRSRSRSPKENGKGDIKSKSRSRSQSRSHSPLPAPPSKARSMSPPPKRASRSRSRSRSRSRSSSRD
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Plays a role in constitutive splicing and modulates the selection of alternative splice sites. Plays a role in the alternative splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-mRNA and promotes the expression of alternatively spliced TNC. Plays a role in wound healing and in the regulation of keratinocyte differentiation and proliferation via its role in alternative splicing (By similarity).
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G3V6U9
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SETD3_RAT
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Actin-histidine N-methyltransferase (EC 2.1.1.85) (Protein-L-histidine N-tele-methyltransferase) (SET domain-containing protein 3)
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MGKKSRVKTQKSGTGATATVSPKEILNLTSELLQKCSSPAPGPGKEWEEYTQIRALVEKIRKKQKGLSVTFDGKREDYFPDLMKWASENGASVEGFEMVNFKEEGFGLRATRDIKAEELFLWVPRKLLMTVESAKNSILGPLYSQDRILQAMGNIALAFHLLCERASPNSFWQPYIQTLPSEYDTPLYFEEEEVRCLQSTQAIHDVFSQYKNTARQYAYFYKVIQTHPHANKLPLKDSFTYEDYRWAVSSVMTRQNQIPTEDGSRVTLALIPLWDMCNHTNGLITTGYNLEDDRCECVALQDFQAGDQIYIFYGTRSNAEFVIHSGFFFDNNSHDRVKIKLGVSKSDRLYAMKAEVLARAGIPTSSVFALHFTEPPISAQLLAFLRVFCMTEEELKEHLLGDSAIDRIFTLGNSEFPVSWDNEVKLWTFLEDRASLLLKTYKTTIEEDKTVLKNPDLSVRATMAIKLRLGEKEILEKAVKSAAMNREYYRKHMEERAPLPRYEESDLGLLEGGVGDSRLPLVLRKLEEEAGVQESLSLTETVSKVKAAENGLVNGESLIPNGTRSENESLSPEESENTTGDTEESSGSMDAVKERL
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Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation of actin at 'His-73'. Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery (By similarity). Does not have protein-lysine N-methyltransferase activity and probably only catalyzes histidine methylation of actin (By similarity).
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G3V7L1
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UTRN_RAT
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Utrophin (Dystrophin-related protein 1) (DRP-1)
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MAKYGHLEASPDDGQNQFSDIIKSRSDEHNDVQKKTFTKWINARFSKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIGGTDIVDGNPKLTLGLLWSIILHWQVKDVMKDIMSDLQQTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPEDVAVQLPDKKSIIMYLTSLFEVLPQQVTIDAIREVETLPRKYKKECEGEEINIQSAVLTEEGQSPRAETPSTVTEVDMDLDSYQIALEEVLTWLLSAEDTFQEQDDISDDVEDVKEQFATHETFMMELTAHQSSVGSVLQAGNQLMTQGTLSDEEEFEIQEQMTLLNARWEALRVESMERQSRLHDALMELQKKQLQQLSGWLTLTEERIQKMESLPVGDDLPSLQNLLEEHKSLQSDLEAEQVKVNSLTHMVVIVDENSGESATAVLEDQLQKLGERWTAVCRWTEERWNRLQEINILWQELLEEQCLLEAWLTEKEEALNKVQTGNFKDQKELGVSVRRLAILKEDMEMKRQTLDQLSEIGQDVGQLLSNPKASEKMNSDSEELTQRWDSLVQRLEDSSNQVTQAVAKLGMSQIPQKDLLETVHVREQGMIKKPKQELPPPPPPKKRQIHVDVEAKKKFDATSAELQSWILRSKAALQNTEMNEYKKSQETSGVRKKWKGLEKEQKEKIPQLDELNQTGQILQEQMGKEGLLAEEINDVLERVLLEWKMISQQLEDLGRKIQLQEDINAYFRQLDALEKTIRAKEEWLRDASFSESPQRSLPSLKDSCQRELTDLLGLHPRIEILCASCSALRSQPSVPGFVQQGFDDLRRHYQAVQKALEEYQQQLENELKSQPEPAYLDTLNTLKKMLSESEKAAQASLSALNDPSAVEQALQEKKALDETLENQKPTLHKLSEETKALEKNMLPDVGKTYRQEFDDAQGKWNKVKTKVSRDLRSLEEIIPRLRDFKADSEVIEKWTNGVKDFLMKEQAAQGDTTALQRQLDQCTTFANEIETIESSLKNLRDIETSLQRCPVTGVKTWVQTRLADYQSQLEKFSQEIDIQKSRLSDSQEKAMNLKKDLAEMQEWMAQAEEDYLERDFEYKSPEELESAVEEMKRAKEDVLQKEVRVKILKDSIKLVAARVPSGGQELTSEFNEVLESYQLLCNRIRGKCHTLEEVWSCWVELLHYLDLETSWLNTLEERMQSTEALPERAEAVHDALESLESVLRHPADNRTQIRELGQTLIDGGILDDIISEKLEAFNSRYEELSHLAESKQISLEKQLQVLRETDHMLQVLKESLGELDKQLTTYLTDRIDAFQLPQEAQKIQAEISAHELTLEELKKNVRPQPPTSPEGRTTRGGSQMDLLQRKLREVSTKFQLFQKPANFEQRMLDCKRVLDGVKAELHVLSVKDVDPDVIQTHLDKCMKLYKTLSEVKLEVETVIKTGRHIVQKQQTDNPKGMDEQLTSLKVLYNDLGAQVTEGKQDLERASQLSRKLKKEAAILSEWLSTTEAELVQKSTSEGVIGDLDTEISWAKNILKDLERRKVDLNAITESSAALQHLVVGSESVLEDTLCVLNAGWSRVRTWTEDWRNTLLNHQNQLEVFDGHVAHISTWLYQAEALLDEIEKKPASKQEEIVKRLLSELSDASIQVENVREQAIVLVNARGSSSRELVEPKLAELSKNFEKVSQHINSAQMLIGQDPAGTVEAVGPFSDLESLESDIENMLKVVEKHLDPSNDEKMDEERAQIEEVLQRGEHLLHEPMEDSKKEKIRLQLLLLHTRYNKIKAIPQRKTIPLSSGIMSSALPADYLVEINKILLTLDDIELSLNIPELNTTVYEDFSFQEDSLKRIKDQLDRLGEQLAAVHEKQPDVILEASGPEAIQIRDMLSQLNAKWDRVNRLYSDRRGSFARAVEEWKQFHCDLDDLTQWLSEAEDLLVGTCAPDGSLDLEKARTHQLELEDGLSSHQPCLIDVNQKGEDIVQRLRPSDASFLKDKLASLNQRWSALVAEVKDLQPRLKGESKQVSGYRKRLDEVVCWLTKVENAVQKRSTPDPEENPWELTDLAQEMDAQAENIKWLNRAELEMLSDKNLSLCERDNLSESLRNVNTMWTKICREVPSLLKTRTQDPCSAPQTRIAAHPNVQKVALVSSASDAPLRGPEISVPADLDKTITELADWLVLIDQMLKSNIVTVGDVKEINKTVSRMKITKADLEQRHPQLDFVFTLAQNLKNKASSSDLRTAITEKLEKLKTQWESTQHGVELRRQQLEDMVVDSLQWDDHREETEELMRKHEARFYMLQQARRDPLSKQVSDNQLLLQELGSGDGVIMAFDNVLQKLLEEYSSDDTRNVEETTEYLKTSWINLKQSIADRQSALEAELRTVQTSRRDLENFVKWLQEAETTANVLADASQRENALQDSVLARQLRQQMLDIQAEIDAHNDIFKSIDGNRQKMVKALGNSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWNRLLASLEELIKWLNMKDEELKKQMPIGGDVPALQLQYDHCKVLRRELKEKEYSVLNAVDQARVFLADQPIEAPEEPRRNPQSKTELTPEERAQKIAKAMRKQSSEVREKWESLNAVTSTWQKQVGKALEKLRDLQGAVDDLDADMKEVEAVRNGWKPVGDLLIDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLDLHPSPKMSRQLDDLNMRWKLLQVSVEDRLKQLQEAHRDFGPSSQHFLSTSVQLPWQRSISHNKVPYYINHQTQTTCWDHPKMTELFQSLGDLNNVRFSAYRTAIKIRRLQKALCLDLLELNTTNEVFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDWMRLEPQSMVWLPVLHRVAAAETAKHQAKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVEYCIPTTSGEDVRDFTKVLKNKFRSKKYFAKHPRLGYLPVQTVLEGDNLETPITLISMWPEHYDPSQSPQLFHDDTHSRIEQYATRLAQMERTNGSFLTDSSSTTGSVEDEHALIQQYCQTLGGESPVSQPQSPAQILKSVEKEERGELERIIADLEEEQRNLQVEYEQLKEQHLRRGLPLGSPPDSIVSPYHTSEDSELIAEAKLLRQHKGRLEARMQILEDHNKQLESQLHRLRQLLEQPDSDSRINGVSPWASPQHPSLSYSLDPDPGPQSHQAASEDLLAPPHDTSTDLTDVMEQLNSTFPSCSPNVPSRPQAI
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May play a role in anchoring the cytoskeleton to the plasma membrane.
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G3V7L5
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PO4F2_RAT
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POU domain, class 4, transcription factor 2 (Brain-specific homeobox/POU domain protein 3B) (Brain-3B) (Brn-3B) (Brn-3.2)
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MMMMSLNSKQAFSMPHAGSLHVEPKYSALHSASPGSSAPAAPSASSPSSSSNAGSGGGGGGGGGGGGGGRSSSSSSSGSGGGGGGGSEAMRRACLPTPPSNIFGGLDESLLARAEALAAVDIVSQSKSHHHHPPHHSPFKPDATYHTMNTIPCTSAASSSSVPISHPSALAGTHHHHHHHHHHHHQPHQALEGELLEHLSPGLALGAMAGPDGTVVSTPAHAPHMATMNPMHQAALSMAHAHGLPSHMGCMSDVDADPRDLEAFAERFKQRRIKLGVTQADVGSALANLKIPGVGSLSQSTICRFESLTLSHNNMIALKPILQAWLEEAEKSHREKLTKPELFNGAEKKRKRTSIAAPEKRSLEAYFAIQPRPSSEKIAAIAEKLDLKKNVVRVWFCNQRQKQKRMKYSAGI
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Tissue-specific DNA-binding transcription factor involved in the development and differentiation of target cells. Functions either as activator or repressor modulating the rate of target gene transcription through RNA polymerase II enzyme in a promoter-dependent manner. Binds to the consensus octamer motif 5'-AT[A/T]A[T/A]T[A/T]A-3' of promoter of target genes. Plays a fundamental role in the gene regulatory network essential for retinal ganglion cell (RGC) differentiation. Binds to an octamer site to form a ternary complex with ISL1 cooperates positively with ISL1 and ISL2 to potentiate transcriptional activation of RGC target genes being involved in RGC fate commitment in the developing retina and RGC axon formation and pathfinding. Inhibits DLX1 and DLX2 transcriptional activities preventing DLX1- and DLX2-mediated ability to promote amacrine cell fate specification. In cooperation with TP53 potentiates transcriptional activation of BAX promoter activity increasing neuronal cell apoptosis. Negatively regulates BAX promoter activity in the absence of TP53. Acts as a transcriptional coactivator via its interaction with the transcription factor ESR1 by enhancing its effect on estrogen response element (ERE)-containing promoter. Antagonizes the transcriptional stimulatory activity of POU4F1 by preventing its binding to an octamer motif. Involved in TNFSF11-mediated terminal osteoclast differentiation.
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G3V7P1
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STX12_RAT
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Syntaxin-12 (Syntaxin-13)
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MSYGPLDMYRNPGPSGPQPRDFNSIIQTCSGNIQRISQATAQIKNLMSQLGTKQDSSKLQENLQQFQHSTNQLAKETNELLKELGSLPLPLSASEQRQQKLQKERLMNDFSSALNNFQVVQRKVSEKEKESIARARAGSRLSAEDRQREEQLVSFDSHEEWNQMQSQEEEAAITEQDLELIKERETAIQQLEADILDVNQIFKDLAMMIHDQGDLIDSIEANVESSEVHVERASDQLQRAAYYQKKSRKKMCILVLVLSVIVTVLVVVIWVASK
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SNARE promoting fusion of transport vesicles with target membranes. Together with SNARE STX6, promotes movement of vesicles from endosomes to the cell membrane, and may therefore function in the endocytic recycling pathway. Through complex formation with GRIP1, GRIA2 and NSG1 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting.
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G3V7R4
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FOXO1_RAT
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Forkhead box protein O1 (Forkhead box protein O1A) (Forkhead in rhabdomyosarcoma)
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MAEAPQVVETDPDFEPLPRQRSCTWPLPRPEFNQSNSTTSSPAPSGSTAANPDATASLASASAVSTDFMSNLSLLEESEDFARAPGCVAVAAAAAASRGLCGDFQGPEAGCVHSAPPQPPPTGPLSQPPPVPPAAAGPLAGQPRKTSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRGRAAKKKASLQSGQEGPGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISGRLSPIMTEQDDLGDGDVHSLVYPPSAAKMASTLPSLSEISNPENMENLLDNLNLLSSPTSLTVSTQSSPGSMMQQTPCYSFAPPNTSLNSPSPNYAKYTYGQSSMSPVPQMPMQTLQDSKSSYGGLNQYNCAPGLLKELLTSDSPPHNDIMSPVDPGVAQPNSRVLGQNVLMGPNSVMPAYGSQAPHNKMMNPSSHTHPGHAQQTSSVNGRALPHVVNTMPHTSAMNRLTPVKTPLQVPLSHPMQMSALGNYSSVSSCNGYGRMGVLHQEKLPSDLDGMFIERLDCDMESIIRNDLMDGDTLDFNFDNVLPNQSFPHSVKTTTHSWVSG
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Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress (By similarity). Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3'. Activity suppressed by insulin (By similarity). Main regulator of redox balance and osteoblast numbers and controls bone mass (By similarity). Orchestrates the endocrine function of the skeleton in regulating glucose metabolism (By similarity). Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity (By similarity). Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP (By similarity). Acts as an inhibitor of glucose sensing in pancreatic beta cells by acting as a transcription repressor and suppressing expression of PDX1 (By similarity). In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC1 and PCK1 (By similarity). Also promotes gluconeogenesis by directly promoting expression of PPARGC1A and G6PC1 (By similarity). Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1 (By similarity). Promotes neural cell death (By similarity). Mediates insulin action on adipose tissue (By similarity). Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake (By similarity). Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells (By similarity). Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner (By similarity). Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling. Regulates endothelial cell (EC) viability and apoptosis in a PPIA/CYPA-dependent manner via transcription of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (By similarity).
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G3V7W1
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PDCD6_RAT
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Programmed cell death protein 6 (Apoptosis-linked gene 2 protein homolog) (ALG-2)
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MAAYSYRPGPGAGPGPAAGAALPDQSFLWNVFQRVDKDRSGVISDNELQQALSNGTWTPFNPVTVRSIISMFDRENKAGVNFSEFTGVWKYITDWQNVFRTYDRDNSGMIDKHELKQALSGFGYRLSDQFHDILIRKFDRQGRGQIAFDDFIQGCIVLQRLTDIFRRYDTDQDGWIQVSYEQYLSMVFSIV
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Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair (By similarity). Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium: calcium-binding triggers exposure of apolar surface, promoting interaction with different sets of proteins thanks to 3 different hydrophobic pockets, leading to translocation to membranes (By similarity). Involved in ER-Golgi transport. Regulates ER-Golgi transport by promoting the association between PDCD6IP and TSG101, thereby bridging together the ESCRT-III and ESCRT-I complexes (By similarity). Together with PEF1, acts as calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in ER-Golgi transport by regulating the size of COPII coats (By similarity). In response to cytosolic calcium increase, the heterodimer formed with PEF1 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification (By similarity). Involved in the regulation of the distribution and function of MCOLN1 in the endosomal pathway (By similarity). Promotes localization and polymerization of TFG at endoplasmic reticulum exit site (By similarity). Required for T-cell receptor-, Fas-, and glucocorticoid-induced apoptosis (By similarity). May mediate Ca(2+)-regulated signals along the death pathway: interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity (By similarity). Its role in apoptosis may however be indirect, as suggested by knockout experiments (By similarity). May inhibit KDR/VEGFR2-dependent angiogenesis the function involves inhibition of VEGF-induced phosphorylation of the Akt signaling pathway (By similarity).
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G3V7X8
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CP26B_RAT
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Cytochrome P450 26B1 (EC 1.14.13.-)
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MLFEGLELVSALATLAACLVSVTLLLAVSQQLWQLRWAATRDKSCKLPIPKGSMGFPLIGETGHWLLQGSGFQSSRREKYGNVFKTHLLGRPLIRVTGAENVRKILLGEHQLVSTEWPRSARVLLGPNTVANSIGDIHRNKRKVFSKIFSHEALESYLPKIQLVIQDTLRAWSSQPEAINVYQEAQRLTFRMAVRVLLGFSIPEEDLGNLFEVYQQFVENVFSLPVDLPFSGYRRGIQARQILQKGLEKAIREKLQCTQGKDYSDALDILIESSKEHGKEMTMQELKDGTLELIFAAYATTASASTSLIMQLLKHPAVLEKLREELRAQGLLHGGGCPCEGTLRLDMLSGLRYLDCVIKEVMRLFTPVSGGYRTVLQTFELDGFQIPKGWSVMYSIRDTHDTAPVFKDVNVFDPDRFSQARSEDKDGRFHYLPFGGGVRTCLGKHLAKLFLKVLAVELASTSRFELATRTFPRITLVPVLHPVDGLSVKFFGLDSNQNEILPETEAMLSATV
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A cytochrome P450 monooxygenase involved in the metabolism of retinoates (RAs), the active metabolites of vitamin A, and critical signaling molecules in animals (By similarity). RAs exist as at least four different isomers: all-trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-dicis-RA, where atRA is considered to be the biologically active isomer, although 9-cis-RA and 13-cis-RA also have activity (By similarity). Catalyzes the hydroxylation of atRA primarily at C-4 and C-18, thereby contributing to the regulation of atRA homeostasis and signaling (By similarity). Hydroxylation of atRA limits its biological activity and initiates a degradative process leading to its eventual elimination (By similarity). Involved in the convertion of atRA to all-trans-4-oxo-RA. Can oxidize all-trans-13,14-dihydroretinoate (DRA) to metabolites which could include all-trans-4-oxo-DRA, all-trans-4-hydroxy-DRA, all-trans-5,8-epoxy-DRA, and all-trans-18-hydroxy-DRA (By similarity). Shows preference for the following substrates: atRA > 9-cis-RA > 13-cis-RA (By similarity). Plays a central role in germ cell development: acts by degrading RAs in the developing testis, preventing STRA8 expression, thereby leading to delay of meiosis. Required for the maintenance of the undifferentiated state of male germ cells during embryonic development in Sertoli cells, inducing arrest in G0 phase of the cell cycle and preventing meiotic entry. Plays a role in skeletal development, both at the level of patterning and in the ossification of bone and the establishment of some synovial joints. Essential for postnatal survival (By similarity).
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G3V893
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ZN335_RAT
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Zinc finger protein 335 (NRC-interacting factor 1) (NIF-1)
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MEENEVESSSDAAPRPGQPEEPSESGLGVGTSEAVSADSTDAATAPGLTEADDSGVGQSSDSGSRSVEEVSESISTEPLPQGYLPDSSSVSRGPVAEVPGGPPALVHSSALPDPSMLVSDCTASSSDLGSAIDKIIESTIGPDLIQSCITVTSGEEGGAETTQYLILQGPDDGAPMASSMSTSTLANSLAAIEALADGPTSTSTCLEPAEQPPGEPSSLAQPPAPVVEELDLQGLEAMMEVVVVQQFKCKMCQYRSSTKATLLRHMRERHFRPALAVAAAAAGKRGRVRKWGTSTKTTEEEGPEEEEEDDDIVDAGAIDDLEEDSDYNPAEDEPRGRQLRLQRPTPSTLRPRRRPGRPRKLPRLETSDLHDGIGEPLVSSQSTQSPPELQDLEAPSSSDLRALGKVGRGLVETGVSQSDAENAAPSCQDEADVPPRRRGRPSRRFLGKKYRKYYYKSPKPLLRPYLCRICGSRFLSHEDLRFHVNSHEAGDPQLFKCLQCSYRSRRWSSLKEHMFNHVGSKPYKCDECSYTSVYRKDVIRHAAVHSQDRKKRPDPTPKLSSFPCPVCGRVYPMQKRLTQHMKTHSTEKPHMCDKCGKSFKKRYTFKMHLLTHIQAVANRRFKCEFCEFVCEDKKALLNHQLSHVSDKPFKCSFCPYRTFREDFLLSHVAVKHTGAKPFACEYCHFSTRHKKNLRLHVRCRHANSFEEWGRRHPEEPPSRRRPFFSLQQIEELKQQHSAAPGPPLSSAGPEAPQEPAPFQPPETPPLLCPDALGGATIIYQQGAEESTAMATQTALDLLLNMSAQRELGATALQVAVVKSEDVEAELTSTARQPSSEDTTPRVVTLHVAESGSSVAAESQLGPSDLQQIALPPGPFSGASYSVITAPPVEGRASASGPPYREEPPGEAAQAVVVNDTLKEAGTHYIMAADGTQLHHIELTADGSISFPSPDTLAPGTKWPLLQCGGPPRDGPEVLSPTKTHHTGGSQGSSTPPPATSHALGLLVPHSPPSAAASSTKKFSCKVCSEAFPSRAEMESHKRAHAGPAAFKCPDCPFSARQWPEVRAHMAQHSSLRPHQCNQCSFASKNKKDLRRHMLTHTNEKPFSCHVCGQRFNRNGHLKFHIQRLHSIDGRKTGTSTARAPAQTIILNSEEETLATLHTAFQSNHGTLGTERLQQALSQEHIIVAQEQTVANQEEATYIQEITADGQTVQHLVTSDNQVQYIISQDGVQHLLPQEYVVVPDGHHIQVQEGQITHIQYEQGTPFLQESQIQYVPVSPSQQLVTQAQLEAAAHSAVTAVADAAMAQAQGLFGTEEAVPEHIQQLQHQGIEYDVITLSDD
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Component or associated component of some histone methyltransferase complexes may regulate transcription through recruitment of those complexes on gene promoters (By similarity). Enhances ligand-dependent transcriptional activation by nuclear hormone receptors (By similarity). Plays an important role in neural progenitor cell proliferation and self-renewal through the regulation of specific genes involved brain development, including REST (By similarity). Also controls the expression of genes involved in somatic development and regulates, for instance, lymphoblast proliferation (By similarity).
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G3V8D4
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APOC2_RAT
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Apolipoprotein C-II (Apo-CII) (ApoC-II) (Apolipoprotein C2) [Cleaved into: Proapolipoprotein C-II (ProapoC-II)]
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MGSRFFLALFLALLVLGNEVQGTEEDDPGSSALLDTVQEHLFSYWNSAKAAAGELYQKTYLTSVDEKLRDMYSKSSAAMTTYAGIFTDQLLTLLKGE
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Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase.
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G3V8H4
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CBLC_RAT
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E3 ubiquitin-protein ligase CBL-C (EC 2.3.2.27) (RING-type E3 ubiquitin transferase CBL-C)
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MAAATAPQGWQWGEPRALGRAVKLLQRLEEQCRDLRLFVGPPSLRDLLPRTAQLLREVAKARSDKTRGDPEGPGGAGDFLVIYLTNLEAKGRQVAELLPHRGKKDANQDVFPEGSRFRRQLAKLALIFSHMHAELSALFPEGKYCGHLYQITKGSANTFWRENCGVRCVLPWAEFQSLLCSCHPVEPGPIMQALRSTLDLTCSGHVSVFEFDIFTRLFQPWPTLLKNWQLLAVNHPGYMAFLTYDEVQTRLQAYRDKPGSYIFRPSCTRLGQWAIGYVSSNGSILQTIPLNKPLLQVLLKGQKDGIFLYPDGKNHNPDLTELCRAVLNQCIQVSQEQLQLYQAMNSTFELCKICTERDKDVRIEPCGHLLCSCCLAAWQHSDSQTCPFCRCEIKGREAVSICQAQERSMEVRTTAGDSGDNCHQEAAEWKLESVTPSAPPLPPEVPCPQRPQNKGWLTLAPFTLPRLRPPLPLPKMASVLWEVTSRPQVREGATESS
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Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Functionally coupled with the E2 ubiquitin-protein ligases UB2D1, UB2D2 and UB2D3. Regulator of EGFR mediated signal transduction upon EGF activation, ubiquitinates EGFR. Inhibits EGF stimulated MAPK1 activation. Promotes ubiquitination of SRC phosphorylated at 'Tyr-419', has the highest ubiquitin ligase activity among CBL family proteins. In collaboration with CD2AP may act as regulatory checkpoint for Ret signaling by modulating the rate of RET degradation after ligand activation CD2AP converts it from an inhibitor to a promoter of RET degradation the function limits the potency of GDNF on neuronal survival.
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G3V8V5
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KCNK4_RAT
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Potassium channel subfamily K member 4 (TWIK-related arachidonic acid-stimulated potassium channel protein) (TRAAK)
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MRSTTLLALLALVLLYLVSGALVFQALEQPHEQQVQKDLEDGRDQFLKDHPCVSQKNLEGFIKLVAEALGGGANPETSWTNSSNHSSAWNLGSAFFFSGTIITTIGYGNIALHTDAGRLFCIFYALVGIPLFGMLLAGVGDRLGSSLRRGIGHIEAVFLKWHVPPGLVRMLSAVLFLLIGCLLFVLTPTFVFSYMESWSKLEAIYFVIVTLTTVGFGDYVPGDGTGQNSPAYQPLVWFWILFGLAYFASVLTTIGNWLRAVSRRTRAEMGGLTAQAASWTGTVTARVTQRTGPSAPPPEKEQPLLPSSLPAPPAVAEPAHRPGSPAPAEKVETPPPTASALDYPSENLAFIDESSDTQSERGCALPRAPRGRRRPNPTKKPSRPRGPGRLRDKAVPV
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Voltage-insensitive potassium channel. Channel opening is triggered by mechanical forces that deform the membrane, and by raising the intracellular pH to basic levels. The channel is inactive at 24 degrees Celsius (in vitro) raising the temperature to 37 degrees Celsius increases the frequency of channel opening, with a further increase in channel activity when the temperature is raised to 42 degrees Celsius. Plays a role in the perception of pain caused by heat (By similarity). Plays a role in the sensory perception of pain caused by pressure (By similarity).
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G3V909
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ATF6A_RAT
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Cyclic AMP-dependent transcription factor ATF-6 alpha (cAMP-dependent transcription factor ATF-6 alpha) (Activating transcription factor 6 alpha) (ATF6-alpha) [Cleaved into: Processed cyclic AMP-dependent transcription factor ATF-6 alpha]
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MESPFSPVLPHGPGEDWESTLFAELGYFTDTDDVQFDAAHETYENNFDHLNFDLDLMPWESDIWSPSSHFCSDIKAEPQPLSPASSSCSVSSPRSTDSCSSTQHVPEELDLLSSSQSPLSLYGDSCHSPSSAEPLKEEKPVTGPGNKTEHGLTPKKKIQMSSKPSVQPKPLLLPAAPKTPANASVPAKTIIIQTLPALMPLAKQQSIISIQPAPTKGQTVLLSQPAVVQLQTPGVLPSAQPVLAVTGGATQLPNHVVNVVPAPVVNSPVNGKLCVTKPVLQSSTRSTGSDIAVLRRQQRMIKNRESACQSRKKKKEYMLGLEARLKAALSENEQLKKENGSLKRQLDQVVSENQRLKVPSPKRRAVCVMIVLAFIMLNYGPMSMLEQDSRRVKPSVSPANQRRHLLEFSAKEVKDTSDGDNQKNSYRYDHSVSNDKALMVLSEEPLLYIPPPPCQPLINTTESLRLNHELRGWVHRHEVERTKSRRMTNSQQKTRILQGALEQGSNSQLMAVQYTETTSISRNSGSELQVYYASPGSYQGFFDAIRRRGDTFYVVSFRRDHLLLPATTHNKTTRPKMSIVLPAININDNVINGQDYEVMMQIDCQVMDTRILHIKSSSVPPYLRDHQRNQTSTFFGSPPTATETTHVVSTLPESVQ
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[Cyclic AMP-dependent transcription factor ATF-6 alpha]: Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 alpha), which is embedded in the endoplasmic reticulum membrane. Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR).
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G3V928
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LRP1_RAT
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Prolow-density lipoprotein receptor-related protein 1 (LRP-1) [Cleaved into: Low-density lipoprotein receptor-related protein 1 85 kDa subunit (LRP-85); Low-density lipoprotein receptor-related protein 1 515 kDa subunit (LRP-515); Low-density lipoprotein receptor-related protein 1 intracellular domain (LRPICD)]
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MLTPPLLLLLPLLSALVAGATMDAPKTCSPKQFACRDQITCISKGWRCDGERDCPDGSDEAPEICPQSKAQRCPPNEHSCLGTELCVPMSRLCNGIQDCMDGSDEGAHCRELRVNCSRMGCQHHCVPTPSGPTCYCNNSFQLQADGKTCKDFDECSVYGTCSQLCTNTDGSFTCGCVEGYLLQPDNRSCKAKNEPVDRPPVLLIANSQNILATYLSGAQVSTITPTSTRQTTAMDFSYANETVCWVHVGDSAAQTQLKCARMPSLKGFVDEHTINISLSLHHVEQMAIDWLTGNFYFVDDIDDRIFVCNRNGDTCVTLLDLELYNPKGIALDPAMGKVFFTDYGQIPKVERCDMDGQNRTKLVDSKIVFPHGITLDLVSRLVYWADAYLDYIEVVDYEGKGRQTIIQGILIEHLYGLTVFENYLYATNSDNANTQQKTSVIRVNRFNSTEYQVVTRVDKGGALHIYHQRRQPRVRSHACENDQYGKPGGCSDICLLANSHKARTCRCRSGFSLGSDGKSCKKPEHELFLVYGKGRPGIIRGMDMGAKVPDEHMIPIENLMNPRALDFHAETGFIYFADTTSYLIGRQKIDGTERETILKDGIHNVEGVAVDWMGDNLYWTDDGPKKTISVARLEKAAQTRKTLIEGKMTHPRAIVVDPLNGWMYWTDWEEDPKDSRRGRLERAWMDGSHRDIFVTSKTVLWPNGLSLDIPAGRLYWVDAFYDRIETILLNGTDRKIVYEGPELNHAFGLCHHGNYLFWTEYRSGSVYRLERGVAGAQPTVTLLRSERPPIFEIRMYDAQQQQVGTNKCRVNNGGCSSLCLATPGSRQCACAEDQVLDADGVTCLANPSYVPPPQCQPGEFACANNRCIQERWKCDGDNDCLDNSDEAPALCHQHTCPSDRFKCENNRCIPNRWLCDGDNDCGNSEDESNATCSARTCPPNQFSCASGRCIPISWTCDLDDDCGDRSDESASCAYPTCFPLTQFTCNNGRCININWRCDNDNDCGDNSDEAGCSHSCSSTQFKCNSGRCIPEHWTCDGDNDCGDYSDETHANCTNQATRPPGGCHSDEFQCRLDGLCIPLRWRCDGDTDCMDSSDEKGCEGVTHVCDPNVKFGCKDSARCISKAWVCDGDSDCEDNSDEENCEALACRPPSHPCANNTSVCLSPDKLCDGKDDCGDGSDEGELCDQCSLNNGGCSHNCSVAPGEGIVCSCPLGMELGPDNHTCQIQSYCAKHLKCSQKCDQNKFSVKCSCYEGWVLEPDGESCRSLDPFKPFIIFSNRHEIRRIDLHKGDYSVLVPGLRNTIALDFHLSQSALYWTDVVEDKIYRGKLLDNGALTSFEVVIQYGLATPEGLAVDWIAGNIYWVESNLDQIEVAKLDGTLRTTLLAGDIEHPRAIALDPRDGILFWTDWDASLPRIEAASMSGAGRRTIHRETGSGGWPNGLTVDYLEKRILWIDARSDAIYSARYDGSGHMEVLRGHEFLSHPFAVTLYGGEVYWTDWRTNTLAKANKWTGHNVTVVQRTNTQPFDLQVYHPSRQPMAPNPCEANGGRGPCSHLCLINYNRTVSCACPHLMKLHNDNTTCYEFKKFLLYARQMEIRGVDLDAPYYNYIISFTVPDIDNVTVLDYDAREQRVYWSDVRTQAIKRAFINGTGVETVVSADLPNAHGLAVDWVSRNLFWTSYDTNKKQINVARLDGSFKNAVVQGLEQPHGLVVHPLRGKLYWTDGDNISMVNMDGSNRTLLFSGQKGPVGLAIDFPESKLYWISSGNHTINRCNLDGSELEVIDTMRSQLGKATALAIMGDKLWWADQVSEKMGTCNKADGSGSVVLRNSTTLVMHMKVYDESIQLEHEGTNPCSVNNGDCSQLCLPTSETTRSCMCTAGYSLRSGQQACEGVGSFLLYSVHEGIRGIPLDPNDKSDALVPVSGTSLAVGIDFHAENDTIYWVDMGLSTISRAKRDQTWREDVVTNGIGRVEGIAVDWIAGNIYWTDQGFDVIEVARLNGSFRYVVISQGLDKPRAITVHPEKGYLFWTEWGHYPRIERSRLDGTERVVLVNVSISWPNGISVDYQGGKLYWCDARMDKIERIDLETGENREVVLSSNNMDMFSVSVFEDFIYWSDRTHANGSIKRGCKDNATDSVPLRTGIGVQLKDIKVFNRDRQKGTNVCAVANGGCQQLCLYRGGGQRACACAHGMLAEDGASCREYAGYLLYSERTILKSIHLSDERNLNAPVQPFEDPEHMKNVIALAFDYRAGTSPGTPNRIFFSDIHFGNIQQINDDGSGRTTIVENVGSVEGLAYHRGWDTLYWTSYTTSTITRHTVDQTRPGAFERETVITMSGDDHPRAFVLDECQNLMFWTNWNELHPSIMRAALSGANVLTLIEKDIRTPNGLAIDHRAEKLYFSDATLDKIERCEYDGSHRYVILKSEPVHPFGLAVYGEHIFWTDWVRRAVQRANKYVGSDMKLLRVDIPQQPMGIIAVANDTNSCELSPCRINNGGCQDLCLLTHQGHVNCSCRGGRILQEDFTCRAMNSSCRAQDEFECANGECISFSLTCDGVSHCKDKSDEKPSYCNSRRCKKTFRQCNNGRCVSNMLWCNGVDDCGDGSDEIPCNKTACGVGEFRCRDGSCIGNSSRCNQFVDCEDASDEMNCSATDCSSYFRLGVKGVLFQPCERTSLCYAPSWVCDGANDCGDYSDERDCPGVKRPRCPLNYFACPSGRCIPMSWTCDKEDDCENGEDETHCNKFCSEAQFECQNHRCISKQWLCDGSDDCGDGSDEAAHCEGKTCGPSSFSCPGTHVCVPERWLCDGDKDCADGADESISAGCLYNSTCDDREFMCQNRLCIPKHFVCDHDRDCADGSDESPECEYPTCGPNEFRCANGRCLSSRQWECDGENDCHDHSDEAPKNPHCTSPEHKCNASSQFLCSSGRCVAEALLCNGQDDCGDGSDERGCHVNECLSRKLSGCSQDCEDLKIGFKCRCRPGFRLKDDGRTCADVDECSTTFPCSQLCINTHGSYKCLCVEGYAPRGGDPHSCKAVTDEEPFLIFANRYYLRKLNLDGSNYTLLKQGLNNAVALDFDYRGQMIYWTDVTTQGSMIRRMHLNGSNVQVLHRTGLSNPDGLAVDWVGGNLYWCDKGRDTIEVSKLNGAYRTVLVSSGLREPRALVVDVQNGYLYWTDWGDHSLIGRIGMDGSGRSIIVDTKITWPNGLTVDYVTERIYWADAREDYIEFASLDGSNRHVVLSQDIPHIFALTLFEDYVYWTDWETKSINRAHKTTGANKTLLISTLHRPMDLHVFHALRQPDVPNHPCKVNNGGCSNLCLLSPGGGHKCACPTNFYLGGDGRTCVSNCTASQFVCKNDKCIPFWWKCDTEDDCGDHSDEPPDCPEFKCRPGQFQCSTGICTNPAFICDGDNDCQDNSDEANCDIHVCLPSQFKCTNTNRCIPGIFRCNGQDNCGDGEDERDCPEVTCAPNQFQCSITKRCIPRVWVCDRDNDCVDGSDEPANCTQMTCGVDEFRCKDSGRCIPARWKCDGEDDCGDGSDEPKEECDERTCEPYQFRCKNNRCVPGRWQCDYDNDCGDNSDEESCTPRPCSESEFSCANGRCIAGRWKCDGDHDCADGSDEKDCTPRCDMDQFQCKSGHCIPLRWRCDADADCMDGSDEEACGTGVRTCPLDEFQCNNTLCKPLAWKCDGEDDCGDNSDENPEECTRFQCPPNRPFRCKNDRVCLWIGRQCDGTDNCGDGTDEEDCEPPTAQNPHCKDKKEFLCRNQRCLSSSLRCNMFDDCGDGSDEEDCSIDPKLTSCATNASMCGDEARCVRTEKAAYCACRPGFHTVPGQPGCQDINECLRFGTCSQLCNNTKGGHLCSCARNFMKTHNTCKAEGSEYQVLYIADDNEIRSLFPGHPHSAYEQAFQGDESVRIDAMDVHVKAGRVYWTNWHTGTISYRSLPPAAPPTTSNRHRRQIDRGVTHLNISGLKMPRGIAIDWVAGNVYWTDSGRDVIEVAQMKGENRKTLISGMIDEPHAIVVDPLRGTMYWSDWGNHPKIETAAMDGTLRETLVQDNIQWPTGLAVDYHNERLYWADAKLSVIGSIRLNGTDPIVAVDSKRGLSHPFSIDVFEDYIYGVTYINNRVFKIHKFGHSPLINLTGGLSHASDVVLYHQHKQPEVTNPCDRKKCEWLCLLSPSGPVCTCPNGKRLDNGTCVPVPSPTPPPDAPRPGTCTLQCFNGGSCFLNARRQPKCRCQPRYTGDKCELDQCWEYCHNGGTCAASPSGMPTCRCPTGFTGPRCTQQVCAGYCANNSTCTVNQGNQPQCRCLPGFLGDRCQYRQCSGFCENFGTCQMAADGSRQCRCTVYFEGTRCEVNKCSRCLQGACVVNKQTGDVTCNCTDGRVAPSCLTCIDHCSNGGSCTMNSKMMPECQCPPHMTGPRCEEQVVSQQQPGHMTSILIPLLLLLLLLLVAGVVFWYKRRVRGAKGFQHQRMTNGAMNVEIGNPTYKMYEGGEPDDVGGLLDADFALDPDKPTNFTNPVYATLYMGGHGSRHSLASTDEKRELLGRGPEDEIGDPLA
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Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells (By similarity). Required for early embryonic development (By similarity). Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. Acts as an LRPAP1 alpha-2-macroglobulin receptor. Acts as TAU/MAPT receptor and controls the endocytosis of TAU/MAPT as well as its subsequent spread. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission (By similarity).
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G3V9D0
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PGLT1_RAT
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Protein O-glucosyltransferase 1 (EC 2.4.1.376) (O-glucosyltransferase Rumi homolog) (Protein O-xylosyltransferase) (EC 2.4.2.63)
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MERLSGCRLRPWMLLLLLFPVQGRQKDSGSKWKVFIDQINRALENYEPCSSQNCSCYHGVIEEDLTPFRGGISRKMMAEVVRRRLGTHYQIIKHRLFREDDCMFPSRCSGVEHFILEVIRRLPDMEMVINVRDYPQVPKWMEPTIPVFSFSKTSEYHDIMYPAWTFWEGGPAVWPLYPTGLGRWDLFREDLLRSAAQWPWEKKNSTAYFRGSRTSPERDPLILLSRKNPKLVDAEYTKNQAWKSMKDTLGKPAAKDVHLIDHCKYKYLFNFRGVAASFRFKHLFLCGSLVFHVGDEWVEFFYPQLKPWVHYIPVKTDLSDVQELLQFVKANDDLAQEIAKRGSQFIINHLQMDDITCYWENLLTEYSKFLSYNVTRRKDYYQIIPRRLKTEL
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Dual specificity glycosyltransferase that catalyzes the transfer of glucose and xylose from UDP-glucose and UDP-xylose, respectively, to a serine residue found in the consensus sequence of C-X-S-X-P-C. Specifically targets extracellular EGF repeats of protein such as CRB2, F7, F9 and NOTCH2 (By similarity). Acts as a positive regulator of Notch signaling by mediating O-glucosylation of Notch, leading to regulate muscle development (By similarity). Notch glucosylation does not affect Notch ligand binding (By similarity). Required during early development to promote gastrulation: acts by mediating O-glucosylation of CRB2, which is required for CRB2 localization to the cell membrane (By similarity).
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G3V9H8
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RET_RAT
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Proto-oncogene tyrosine-protein kinase receptor Ret (EC 2.7.10.1) [Cleaved into: Soluble RET kinase fragment; Extracellular cell-membrane anchored RET cadherin 120 kDa fragment]
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MAKARSGAAGLGLKLFLLLPLLGEAPLGLYFSRDAYWERLYVDQPAGTPLLYVHALRDAPGEVPSFRLGQYLYGVYRTRLHENDWIHIDSGTGLLYLNQSLDHSSWEQLSIRNGGFPLLTVFLQVFLGSTAQREGECHWPGCARVYFSFINDTFPNCSSFKARDLCTPETGVSFRIRENRPPGTFYQFRMLPVQFLCPNISVKYKLLEGDGLPFRCDPDCLEVSTRWALDRELQEKYVLEAECAVAGPGANKEKVAVSFPVTVYDEDDSPPTFSGGVGTASAVVEFKRKEGTVVATLQVFDADVVPASGELVRRYTSTLLSGDSWAQQTFRVEHTPNETLVQSNNNSVRATMHNYKLVLNRSLSISESRVLQLVVLVNDSDFQGPGSGVLFLHFNVSVLPVTLNLPMAYSFPVNRRARRYAQIGKVCVENCQEFSGVSIQYKLQPSSTNCSALGVVTSTEDTSGTLYVNDTEALRRPECTELQYTVVATDRQTRRQTQASLVVTVEGTYIAEEVGCPKSCAVNKRRPECEECGGLGSPTGRCEWRQGDGKGITRNFSTCSPSTRTCPDGHCDALESRDINICPQDCLRGPIVGGHERGERQGIKAGYGICNCFPDEKKCFCEPEDSQGPLCDELCRTVITAAVLFSFIISVLLSTFCIHRYHKHAHKPPIASAEMTFCRPAQGFPISYSSSGTRRPSLDSMENQVSVDSFKIPEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFRLKGRAGYTTVAVKMLKENASQSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRDSRKIGPAYVSSGGSRNSSSLDHPDERVLTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKKSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKSRDYLDLAASTPSDSLLYDDGLSEEETPLVDCNSAPLPRSLPSTWIENKLYGMSDPNWPGESPVPLTRADGTSTGFPRYANDSVYANWMVSPSAAKLMDTFDS
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Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation upon binding with glial cell derived neurotrophic factor family ligands. Phosphorylates PTK2/FAK1. Regulates both cell death/survival balance and positional information. Required for the molecular mechanisms orchestration during intestine organogenesis involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue. Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e.g. ITGB1 and ITGB3)-dependent manner. Involved in the development of the neural crest. Active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage. Acts as a dependence receptor in the presence of the ligand GDNF in somatotrophs (within pituitary), promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF. Regulates nociceptor survival and size. Triggers the differentiation of rapidly adapting (RA) mechanoreceptors. Mediator of several diseases such as neuroendocrine cancers these diseases are characterized by aberrant integrins-regulated cell migration (By similarity). Mediates, through interaction with GDF15-receptor GFRAL, GDF15-induced cell-signaling in the brainstem which induces inhibition of food-intake. Activates MAPK- and AKT-signaling pathways (By similarity).
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G3V9M2
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JIP2_RAT
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C-Jun-amino-terminal kinase-interacting protein 2 (JIP-2) (JNK-interacting protein 2) (Islet-brain-2) (IB-2) (JNK MAP kinase scaffold protein 2) (Mitogen-activated protein kinase 8-interacting protein 2)
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MADRAEMFSLSTFHSLSPPGCRPPQDISLEEFDDEDLSEITDDCGLGLSYDSDHCEKDSLSLGRSEQPHPICSFQDDFQEFEMIDDNEEEEDEEEEEEEEEEEDGDGDGRAGGGSGSQELSGESLIPSPSIEESHKLRPTTLHLTTLGAQDSLNNNSNGGFTSAPPSSWQETVLRSPVQEPLKELPAPLLPAEEEHHEVQSLARPGCDCEGNQPPEPPASGGASPSSDPGIEADLRSHSSGGHEGRRSSQELSSPGSDSEEAGGARLGRMISSISETELELSSDSGSSSGRSSHLTNSIEEASSPASEPEPEPEPEPLHEPPRRPAFLPVGQDDTNSEYESGSESEPDLSEDADSPWLLSNLVSRMISEGSSPIRCPGQCLSPPAPRPPEEAASQANPVPQDCPDPEAVAGPHVELVDMDTLCGPPPPAPAAPRLGPAQSGPCLFLSNPTRDTITPLWAPPGRTARPGRSCSAACSEEEEEDEEEDEEDEEDAEDSVIPPGSRTTGSTAPLDASLVYDAVKYTLVVDEHTQLELVSLRRCAGLDNDSEEDSSCEASEEEAGATLLGSDQVPEDASPDSPDLTFSKKFLNVFVNSTSRSSSTESFGLFSCVVNGEEREQTHRAVFRFIPRHPDELELDVDDPVLVEAEEDDFWFRGFNMRTGERGVFPAFYAHAVPGPAKDLLGSKRSPCWVDRFDVQFLGSVEVPCHQGNGILCAAMQKIATARKLTVHLRPPASCDLEISLRGVKLSLSGGGPEFQRCSHFFQMKNISFCGCHPRNSCYFGFITKHPLLSRFACHVFVSQESMRPVARSVGRAFLEYYQEHLAFACPTEDIYLE
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The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. JIP2 inhibits IL1 beta-induced apoptosis in insulin-secreting cells.
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G3V9R8
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HNRPC_RAT
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Heterogeneous nuclear ribonucleoprotein C (hnRNP C) (hnRNP core protein C)
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MASNVTNKTDPRSMNSRVFIGNLNTLVVKKSDVEAIFSKYGKIVGCSVHKGFAFVQYVNERNARAAVAGEDGRMIAGQVLDINLAAEPKVNRGKAGVKRSAAEMYGSSFDLDYDFQRDYYDRMYSYPARVPPPPPIARAVVPSKRQRVSGNTSRRGKSGFNSKSGQRGSSSKSVKGDDLQAIKKELTQIKQKVDSLLESLEKIEKEQSKQADLSFSSPVEMKNEKSEEEQSSASVKKDETNVKMESEAGADDSAEEGDLLDDDDNEDRGDDQLELKDDEKEPEEGEDDRDSANGEDDS
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Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing.
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G3V9T7
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GET3_RAT
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ATPase Get3 (EC 3.6.-.-) (Arsenical pump-driving ATPase) (Arsenite-stimulated ATPase) (Guided entry of tail-anchored proteins factor 3, ATPase)
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MAAGVAGWGVEAEEFEDAPDVEPLEPTLSNIIEQRSLKWIFVGGKGGVGKTTCSCSLAVQLSKGRESVLIISTDPAHNISDAFDQKFSKVPTKVKGYDNLFAMEIDPSLGVAELPDEFFEEDNMLSMGKKMMQEAMSAFPGIDEAMSYAEVMRLVKGMNFSVVVFDTAPTGHTLRLLNFPTIVERGLGRLMQIKNQISPFISQMCNMLGLGDMNADQLASKLEETLPVIRSVSEQFKDPEQTTFICVCIAEFLSLYETERLIQELAKCKIDTHNIIVNQLVFPDPEKPCKMCEARHKIQAKYLDQMEDLYEDFHIVKLPLLPHEVRGADKVNTFSALLLEPYKPPSTQ
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ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1/WRB and CAMLG/GET2, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the GET1-CAMLG receptor, and returning it to the cytosol to initiate a new round of targeting. {ECO:0000255|HAMAP-Rule:MF_03112, ECO:0000269|PubMed:23041287, ECO:0000269|PubMed:27226539}.
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G3X745
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GPC1_BOVIN
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Glypican-1 [Cleaved into: Secreted glypican-1]
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MELRARGWWLLYAAAVLVACARGDPASKSRSCGEVRQIYGAKGFSLSDVPQAEISGEHLRICPQGYTCCTSEMEENLANRSRAELETALLEGTRALQATLAAQQRGFDDHFQRLLNDSERALQEAFPGAFGELYTQNAKAFRDLYAELRLYYGGANLHLQETLAEFWARLLERLFRQLHPQLLLPDDYLDCLGKQAEPLRPFGEAPRELRLRATRAFVAARTFVQGLGVAGDVVRKVAKVPLSPECSRAVMKLVYCAHCLGVPGARPCPDYCRNVLKGCLANQADLDAEWRNLLDSMVLITDKFWGPSGAESVVGGVHYWLAEAINALQDNSDTLTAKVIQGCGNPKVNPQGPGTEEKWPRGKLALQERPPAGTLQKLVSEAKAQLRDAQDFWISLPGTLCSEKLAMSSASDERCWNGMAKGRYLPEVMGDGLANQINNPEVEVDITKPDMTIRQQIMQLKIMTNRLRGAYNGNDLDFQDASDDGSGSGSGEGCPDEMCGRKVGRKSASSRTPLTHALPGLSEREGQQTSAAAPTPPQASPLLLLGLALALPAVAPRGR
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Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination (By similarity). May act as a catalyst in increasing the rate of conversion of prion protein PRPN (C) to PRNP (Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling (By similarity).
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G3X912
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SPRTN_MOUSE
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DNA-dependent metalloprotease SPRTN (EC 3.4.24.-) (Protein with SprT-like domain at the N terminus) (Spartan)
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MDEDLVVALRLQEEWDVQMARRAAAAREPVSLVDASWELVDPTPDLQALFLQFNDRFFWGQLEAVEVKWSVRMTLCAGICTYEGRGGMCSIRLSEPLLKLRPRKDLVETLLHEMIHAYLFVTNNDKDREGHGPEFCKHMHRINQLTGANITVYHTFHDEVDEYRRHWWRCNGPCQHRQPYYGYVKRATNRAPSVHDYWWADHQKTCGGTYIKIKEPENYSKKGRGKTKADKQPASAVENKDKLCRGEAQLLIPFSGKGYVLGDASTCPSAGKLNTSYMVNEAKGLSSQDHSVSGLRLNSNAEVKCEQNCLPKKPHLVSPLPTASHQSVLSSYFPRVSVANQKAFRNVNGSPVKNGTTGDGTKRPASGGSQRKVPPSRASLRNTSKVTAPASATVTSAAGTSATISREESGSEDQFLNKRPRLEDRTALDTIKEQTQSGGDLRSSSQPTAASAPQSLSSQRRLVNCPVCQGVVVESQINEHLDRCLEGNKTNLRPRRV
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DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde. Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis. Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as TOP1, TOP2A, histones H3 and H4 (By similarity). Mediates degradation of DPCs that are not ubiquitinated, while it is not able to degrade ubiquitinated DPCs. SPRTN activation requires polymerase collision with DPCs followed by helicase bypass of DPCs (By similarity). Involved in recruitment of VCP/p97 to sites of DNA damage. Also acts as an activator of CHEK1 during normal DNA replication by mediating proteolytic cleavage of CHEK1, thereby promoting CHEK1 removal from chromatin and subsequent activation. Does not activate CHEK1 in response to DNA damage. May also act as a 'reader' of ubiquitinated PCNA: recruited to sites of UV damage and interacts with ubiquitinated PCNA and RAD18, the E3 ubiquitin ligase that monoubiquitinates PCNA. Facilitates chromatin association of RAD18 and is required for efficient PCNA monoubiquitination, promoting a feed-forward loop to enhance PCNA ubiquitination and translesion DNA synthesis (By similarity).
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G3X939
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SL9A3_MOUSE
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Sodium/hydrogen exchanger 3
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MWHRALGPGWKLLLALALTSLQGARGAEEEPSSDGSFQVVTFKWHHVQDPYIIALWILVASLAKIVFHLSHKVTSIVPESALLIVLGLVLGGIVWAADHIASFTLTPTLFFFYLLPPIVLDAGYFMPNRLFFGNLGTILLYAVIGTIWNAATTGLSLYGVFLSGLMGELKIGLLDFLLFGSLIAAVDPVAVLAVFEEVHVNEVLFIIVFGESLLNDAVTVVLYNVFESFVTLGGDAVTGVDCVKGIVSFFVVSLGGTLVGVIFAFLLSLVTRFTKHVRIIEPGFVFVISYLSYLTSEMLSLSSILAITFCGICCQKYVKANISEQSATTVRYTMKMLASGAETIIFMFLGISAVNPDIWTWNTAFVLLTLVFISVYRAIGVVLQTWILNRYRMVQLETIDQVVMSYGGLRGAVAYALVVLLDEKKVKEKNLFVSTTLIVVFFTVIFQGLTIKPLVQWLKVKRSEHREPKLNEKLHGRAFDHILSAIEDISGQIGHNYLRDKWSNFDRKFLSKVLMRRSAQKSRDRILNVFHELNLKDAISYVAEGERRGSLAFIRSPSTDNMVNVDFNTPRPSTVEASVSYFLRENVSAVCLDMQSLEQRRRSIRDTEDMVTHHTLQQYLYKPRQEYKHLYSRHELTPNEDEKQDKEIFHRTMRKRLESFKSAKLGINQNKKAAKLYKRERAQKRRNSSIPNGKLPMENLAHNYTIKEKDLELSEHEEATNYEEISGGIEFLASVTQDVASDSGAGIDNPVFSPDEDLDPSILSRVPPWLSPGETVVPSQRARVQIPNSPSNFRRLTPFRLSNKSVDSFLQADGHEEQLQPAAPESTHM
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Plasma membrane Na(+)/H(+) antiporter. Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry, playing a key role in salt and fluid absorption and pH homeostasis (By similarity). Major apical Na(+)/H(+) exchanger in kidney and intestine playing an important role in renal and intestine Na(+) absorption and blood pressure regulation.
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G3X943
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S39A2_MOUSE
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Zinc transporter ZIP2 (Solute carrier family 39 member 2) (Zrt- and Irt-like protein 2) (ZIP-2) (hZIP2)
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MEVLLGVKIGCLLALLVLTLGCGLTPIYVKWFQMDAATGHHHRVLSLLGCTSAGVFLGAGLMHMTAEALEGIESEIQKFVEQNSTGSKGNSSRDAASSYVEYPYGELVISLGFFFVFLLESLALQCCHGAAGGSTVQEEEWGGTHAFGFHKHPAVPSPSRGPLRALVLLLSLSFHSVFEGLAVGLQATVAATIQLCVAVLAHKGLVVFSVGLRLGKIGTGPRWATFCILSLALMSPVGLALGLTVAGGASGQTQGLAQAVLEGIAAGTFLYVTFLEILPRELACPEAPLAKYSCVAAGFAFMALIALWA
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Transporter for the divalent cation Zn(2+). Mediates the influx of Zn(2+) into cells from extracellular space. The Zn(2+) uniporter activity is independent of H(+)-driving force, but is modulated by extracellular pH and membrane potential. Transports also other divalent cations Zn(2+), Cd2(+), Cu2(+), Co2(+) in the order of decreasing affinity, respectively (By similarity). In the skin, aids in the differentiation of keratinocytes in the epidermis.
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G3X982
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AOXC_MOUSE
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Aldehyde oxidase 3 (EC 1.2.3.1) (Aldehyde oxidase homolog 1) (Azaheterocycle hydroxylase 3) (EC 1.17.3.-)
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MSPSKESDELIFFVNGKKVTERNADPEVNLLFYLRKVIRLTGTKYGCGGGDCGACTVMISRYDPISKRISHFSATACLVPICSLHGAAVTTVEGIGSTKTRIHPVQERIAKGHGTQCGFCTPGMVMSIYTLLRNHPEPSTEQIMETLGGNLCRCTGYRPIVESAKSFCPSSTCCQMNGEGKCCLDEEKNEPERKNSVCTKLYEKKEFQPLDPTQELIFPPELMRMAEESQNTVLTFRGERTTWIAPGTLNDLLELKMKHPSAPLVIGNTYLGLHMKFTDVSYPIIISPARILELFVVTNTKQGLTLGAGLSLTQVKNVLSDVVSRLPKEKTQIYCALLKQLKTLAGQQIRNVASLGGHIISRLPTSDLNPILGIGNCILNVASTEGIQQIPLNDHFLAGVPDAILKPEQVLISVFVPRSSKWEFVSAFRQAPRQQNAFATVNAGMKVVFKEDTNTITDLGILYGGIGATVISADKSCRQLIGRCWDEEMLDDAGKMICEEVSLLMAAPGGMEEYRKTLAISFLFMFYLDVLKQLKTRDPHKYPDISQKLLHILEDFPLTMPYGMQSFQDVDFQQPLQDPIGRPIMHQSGIKHATGEAVFCDDMSVLPGELFLAVVTSSKSHAKIISLDASEALASLGVVDVVTARDVPGDNGREEESLYAQDEVICVGQIVCAVAADSYAHAQQAAKKVKIVYQDIEPMIVTVQDALQYESFIGPERKLEQGNVEEAFQCADQILEGEVHLGGQEHFYMETQSVRVVPKGEDKEMDIYVSSQDAAFTQEMVARTLGIPKNRINCHVKRVGGAFGGKASKPGLLASVAAVAAQKTGRPIRFILERRDDMLITGGRHPLLGKYKIGFMNNGKIKAADIQLYINGGCTPDDSELVIEYALLKLENAYKIPNLRVRGRVCKTNLPSNTAFRGFGFPQGAFVTETCMSAVAAKCRLPPEKVRELNMYRTIDRTIHNQEFDPTNLLQCWEACVENSSYYNRKKAVDEFNQQRFWKKRGIAIIPMKFSVGFPKTFYYQAAALVQIYTDGSVLVAHGGVELGQGINTKMIQVASRELKIPMSYIHLDEMSTVTVPNTVTTGASTGADVNGRAVQNACQILMKRLEPIIKQNPSGTWEEWVKEAFVQSISLSATGYFRGYQADMDWEKGEGDIFPYFVFGAACSEVEIDCLTGAHKNIRTDIVMDGSFSINPAVDIGQIEGAFVQGLGLYTLEELKYSPEGVLYTRGPHQYKIASVTDIPEEFHVSLLTPTPNPKAIYSSKGLGEAGTFLGCSVFFAIAAAVAAAREERGLSPIWAINSPATAEVIRMACEDQFTNLVPQTDSKCCKPWSIPVA
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Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and phthalazine, as well as aldehydes, such as benzaldehyde, retinal and pyridoxal. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. 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.
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G3X9J0
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SI1L3_MOUSE
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Signal-induced proliferation-associated 1-like protein 3 (SIPA1-like protein 3) (SPA-1-like protein 3)
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MTTYRPLPNDGVDLAASCGARSTDILPGPHPGDYTPMGFWAQNGSMPQPLGESPAATTTRPSPTTPAMPKMGVRARVADWPPKRDALREQSNPSPSQDTDGVKTTKVAHSMRNLQNGQLPSSTPASSGSRAFHRLSRRRSKDVEFQDGWPRSPGRAFLPLRHRSSSEITLSECDVEEPGDPRGTRHPGVLPLFREYGSTSSIDVQGVPEQSFFDILNEFRSEQPEARGSQNLRELLQVDPGALSGGSCGTKGDPRNGQPTKDSLQSLQPLKEKEKSRKKPVRGLGSGDTVDSSIFRKLRSSKPEGEVGRPLGETEESRSPPEASRPWVCQKSFAHFDVQSMLFDLNEAAANRVSVAQRRNTTTGASAASAASAMVTLTASRAHSLGTLDPAFTSTEDLNCKENLEQDLGDDNSNDLLLSCPHFRNEIGGERERNVSFSRASVGSPGGSSEAHMAEPTLSTHRTNASISVLEVPKEQQRTQSRPRQYSIEHVDLGARYYQDYFVGKEHANYFGVDEKLGPVAVSIKREKLEDHKDHGPQYQYRIIFRTRELITLRGSILEDATPTATKHGTGRGLPLKDALEYVIPELNIHCLRLALNTPKVTEQLLKLDEQGLCRKHKVGILYCKAGQSSEEEMYNNEEAGPAFEEFLDLLGDKVCLKGFTKYAAQLDVKTDSTGTHSLYTTYQDYEIMFHVSTLLPYTPNNRQQLLRKRHIGNDIVTIIFQEPGALPFTPKNIRSHFQHVFIIVRVHNPCTENVCYSMAVTRSKDAPPFGPPIPNGTTFRKSDVFRDFLLAKVINAENAAHKSDKFHTMATRTRQEYLKDLAENCVSNTPIDSSGKFNLISLTSKKKEKTKARAGAEQHSAGAIAWRVAAQDYAQGSEIDCILGISNEFVVLLDLRTKEVVFNCYCGDVIGWTPDSSTIKIFYGRGDHIFLQAAEGSVEDIRDIVQRLKVMTNGWETVDMTLRRNGLGQLGFHVKYDGTVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLSHDQMIDLLRTSVTVKVVIIPPFEDGTPRRGWPETYDMNASEPKTESETTTPGGRPPYRSNAPWQWSGPASHNSLPATKWTTPATPGHAQSLSRLPKQTPVVPFRESQPLHSKRPVSFPETPFAASPAGADRVPPYRQPSGSFSTPGSATYARYKPSPERYAAAPHPLLSFDPHFMHDGMSSGDSSSGGLTSQESTMERPKPEPLWHVPAQARLSAMTGSIGSKHPSRQDAAGKDSPNRHSKGEPQYSSHSSSNTLSSNASSSHSDDRWFDPLDPLEPEQDPFSKGGSSDSGIDTTLYTSSPSCMSLAKAPRPTKPHKPPGNIGLCGGGRESAGRPHPVDRRREVSPAPVVAGQNKGYRPKLYSSGSCTPPGLVGGSRDPPRQPSDMGSRAGYPTQVYKTASAETPRPSQLSQCSPFQLSTSVPKSFFSKQPAHNKHSTGWKRTDEPPPRPLPFTDSKKQVDTNAKNVFGQPRLRASLRDLRSPRKNYKSTIEDDLKKLIVMDNLGPEQERDTGQSPQKSLQRTLSDESLCSGRREPSFASPASLEPGLPSDVLFTSTCTFPSSTLPARRQHQHAHPPSGAPSTTPATGNGFPEKKSAISASELSLADGRDRPLRRLDPGMMPLPDTAAGLEWSSLVNAAKAYEVQRAVSLFSLNDPALSPEIPPAHSPVHSHLSLERGPQTPRATPTMSEESPLDLTGKVYQLEVMLKQLHTDLQKEKQDKVVLQSEVASLRQNNQRLQEESQAASEQLRKFAELFSREKKEL
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Plays a critical role in epithelial cell morphogenesis, polarity, adhesion and cytoskeletal organization in the lens.
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G3X9K3
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BIG1_MOUSE
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Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1) (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1)
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MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKVETEKQSPPHGEAKAGSGTLPPVKSKTNFIEADKYFLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGRAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVTSQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMERERHRQQQHLLQSPVSHHEPESPHLRYLPPQTVDHINQEHEGDLEPQTHDVDKSLQDDTEPENGSDISSAENEQTEADQATAAETLSKNDILYDGDYEEKPLDIVQSIVEEMVNIIVGDMGEGMAISASTEGNTGTVEDGSDSENIQANGIPGTPISVAYTPSLPDDRLSVSSNDTQESGNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPVFRTNEMFINAIKQYLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQSVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTLGQEKPSEQEISEVKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFNKKPKRGIQYLQEQGMLGTTPEDIAQFLHQEERLDSTQVGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRLFLEGFRLPGEAQKIDRLMEKFAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGKKISMKETKELTIPTKSTKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAFSVGLQDCDDTEVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGTKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFSVFHLAASDQDESIVELAFQTTGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQAFKEYTSDDMSVAPEDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKTYGHTYEKHWWQDLFRIVFRIFDNMKLPEQQTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIWDKTCNCTLDIFKTTIPHALLTWRPTSGEAEPPSPSAVSEKPLDAISQKSVDIHDSIQPRSSDNRQQAPLVSVSTVSEEVSKVKSTAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSKKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLFKLLDCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYMDESRVSAWEEVQQRLLNVCREALSYFLTLTSESHREAWTNLLLLFLTKVLKISDSRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGIVFQISQPPEQELGINRQ
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Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure the function may be independent of its GEF activity. Required for the maturaion of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined (By similarity).
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G3X9X1
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KBTB2_MOUSE
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Kelch repeat and BTB domain-containing protein 2
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MSTQEERQINTEYAVSLLEQLKLFYEQQLFTDIVLIVEGTEFPCHKMVLATCSSYFRAMFMSGLSESKQTHVHLRNVDAAALQMIIAYAYTGNLAVNDSTVEQLYETACFLQVEDVLQRCREYLIKKINAENCVRLLSFADLFSCEELKQSAKRMVEHKFTAVYRQEAFMQLSHDLLIDILSSDNLNVEKEETVREAAMLWLEYNTESRSQYLSSVLSQIRIDALSEVTQRAWFQGLPPNDKSVVVQGLYKSMPKFFKPRLGMTKEEMMIFIEASSENPCSLYSSVCYSPQAEKVYKLCSPPADLHKVGTVVTPDNDIYIAGGQVPLKNTKTNHSKTSKLQTAFRTVNCFYWFDAQQNTWFPKTPMLFVRVKPSLVCCEGYIYAIGGDSVGGELNRRTVERYDTEKDEWTMVSPLPCAWQWSAAVVVHDCIYVMTLNLMYCYFPRSDSWVEMAMRQTSRSFASAAAFGDKIFYIGGLHIATNSGIRLPSGTVDGSSVTVEIYDVNKNEWKMAANIPAKRYSDPCVRAVVISNSLCVFMRETHLNERAKYVTYQYDLELDRWSLRQHISERVLWDLGRDFRCTVGKLYPSCLEESPWKPPTYLFSPDGTEEFELDGEMVALPPV
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Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of the insulin signaling pathway, modulating insulin sensitivity by limiting PIK3R1/p85alpha abundance in adipocytes. Targets PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase (PI3K), for 'Lys-48'-linked polyubiquitination and proteasome-mediated degradation.
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G3XA57
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RFIP2_MOUSE
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Rab11 family-interacting protein 2 (Rab11-FIP2)
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MMLSEQAQKWFPTHVQVTVLQAKDLKPKGKSGTNDTYTIIQLGKEKYSTSVAEKTLEPVWKEEASFELPGLLMQGSPEKYILFLIVMHRSLVGLDKFLGQVAINLNDIFEDKQRRKTEWFRLESKQGKRIKNRGEIKVNIQFMRNNMTASMFDLSMKDKTRSPFAKLKDKMKGRKSDGVFSDTSSAIVPSTHMPDANPEFSSGEMQMKSKPKKPFLLGPQRLSSAHSMSDLTGSHLSSEKLKSSTVGPTHLLSRQIDSFGVVPESGSLKSPHRRTLSFDTSKLNQPGSIVDEGEHSFGRQSDPFTNVTASLPQKFATLPRKKNPFEESSEPWDSSMNLFSKPIEVRKESKREKREKVSLFERVTGKRDSRRPDKLNNGGSDSPCDLKSPSAFSENRQDYFEYESTNPFTAKFRASTIMPSSSFHVNPTSSEDLRKIPDNNPFDATAGYRSLTYEEVLQELVKHKELLRRKDTHIRELEDYIDNLLVRVMEETPSILRVPYEPSRKAGKFTNS
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A Rab11 effector binding preferentially phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA) and acting in the regulation of the transport of vesicles from the endosomal recycling compartment (ERC) to the plasma membrane. Involved in insulin granule exocytosis. Also involved in receptor-mediated endocytosis and membrane trafficking of recycling endosomes, probably originating from clathrin-coated vesicles. Required in a complex with MYO5B and RAB11 for the transport of NPC1L1 to the plasma membrane. Also acts as a regulator of cell polarity. Plays an essential role in phagocytosis through a mechanism involving TICAM2, RAC1 and CDC42 Rho GTPases for controlling actin-dynamics.
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G3XA59
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LRC32_MOUSE
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Transforming growth factor beta activator LRRC32 (Garpin) (Glycoprotein A repetitions predominant) (GARP) (Leucine-rich repeat-containing protein 32)
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MSHQILLLLAMLTLGLAISQRREQVPCRTVNKEALCHGLGLLQVPSVLSLDIQALYLSGNQLQSILVSPLGFYTALRHLDLSDNQISFLQAGVFQALPYLEHLNLAHNRLATGMALNSGGLGRLPLLVSLDLSGNSLHGNLVERLLGETPRLRTLSLAENSLTRLARHTFWGMPAVEQLDLHSNVLMDIEDGAFEALPHLTHLNLSRNSLTCISDFSLQQLQVLDLSCNSIEAFQTAPEPQAQFQLAWLDLRENKLLHFPDLAVFPRLIYLNVSNNLIQLPAGLPRGSEDLHAPSEGWSASPLSNPSRNASTHPLSQLLNLDLSYNEIELVPASFLEHLTSLRFLNLSRNCLRSFEARQVDSLPCLVLLDLSHNVLEALELGTKVLGSLQTLLLQDNALQELPPYTFASLASLQRLNLQGNQVSPCGGPAEPGPPGCVDFSGIPTLHVLNMAGNSMGMLRAGSFLHTPLTELDLSTNPGLDVATGALVGLEASLEVLELQGNGLTVLRVDLPCFLRLKRLNLAENQLSHLPAWTRAVSLEVLDLRNNSFSLLPGNAMGGLETSLRRLYLQGNPLSCCGNGWLAAQLHQGRVDVDATQDLICRFGSQEELSLSLVRPEDCEKGGLKNVNLILLLSFTLVSAIVLTTLATICFLRRQKLSQQYKA
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Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space. Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta. Able to outcompete LTBP1 for binding to LAP regulatory chain of TGF-beta (By similarity). Controls activation of TGF-beta-1 (TGFB1) on the surface of activated regulatory T-cells (Tregs). Required for epithelial fusion during palate development by regulating activation of TGF-beta-3 (TGFB3).
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G3XCV0
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FLEQ_PSEAE
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Transcriptional regulator FleQ
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MWRETKLLLIDDNLDRSRDLAVILNFLGEDQLTCNSEDWREVAAGLSNSREALCVLLGSVESKGGAVELLKQLASWDEYLPILLIGEPAPADWPEELRRRVLASLEMPPSYNKLLDSLHRAQVYREMYDQARERGRSREPNLFRSLVGTSRAIQQVRQMMQQVADTDASVLILGESGTGKEVVARNLHYHSKRREGPFVPVNCGAIPAELLESELFGHEKGAFTGAITSRAGRFELANGGTLFLDEIGDMPLPMQVKLLRVLQERTFERVGSNKTQNVDVRIIAATHKNLEKMIEDGTFREDLYYRLNVFPIEMAPLRERVEDIALLLNELISRMEHEKRGSIRFNSAAIMSLCRHDWPGNVRELANLVERLAIMHPYGVIGVGELPKKFRHVDDEDEQLASSLREELEERAAINAGLPGMDAPAMLPAEGLDLKDYLANLEQGLIQQALDDAGGVVARAAERLRIRRTTLVEKMRKYGMSRRDDDLSDD
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AAA+ ATPase enhancer-binding protein that acts as a transcription regulator and plays a role in the modulation of mucin adhesion and flagellar gene expression. In addition to flagella genes, regulates also expression of biofilm-related genes. Functions as a transcriptional repressor in the absence of c-di-GMP and as an activator when c-di-GMP is present.
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G3XCX3
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PILU_PSEAE
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Type IV pilus ATPase PilU
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MEFEKLLRLMVEKGGSDLFITAGVPPSMKVNGRVMPVTKTPLSPEQTRETVLGVMNEQQRRDFAENHECNFAISARGIGRFRVSAFYQRNLVGMVLRRIETNIPTLEELKLPEILKKLALTKRGLVIFVGATGTGKSTSLAAMIGYRNKNSTGHIISIEDPIEYIHQHQGCIVTQREVGLDTDSFEVALKNTLRQAPDVIMIGEVRSRETMDHAVAFAETGHLCLATLHANNANQALERIIHFFPADRHGQVWMDLSLNLKAIVAQQLVPTPDGKGRRAVIEVLLNTPLAADLIRKGEVHELKPLMKRSTEQGMQTFDQALYQLYTQGEITYEDALAHADSANDLRLMIKLGSESDADHLSSLTQGLSLEITDDDPAGRRFR
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ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers. Functions as a PilT-dependent retraction ATPase, providing a functional coupling between PilT and PilU and an optimal mechanism for pilus retraction.
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G3XCY4
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AMRZ_PSEAE
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Transcription factor AmrZ (Alginate and motility regulator Z)
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MRPLKQATPTYSSRTADKFVVRLPEGMREQIAEVARSHHRSMNSEIIARLEQSLLQEGALQDNLGVRLDSPELSLHERELLQRFRQLTHRQQNALVALIAHDAELAQA
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Functions as both a transcriptional activator and repressor of multiple genes encoding virulence factors as well as genes involved in environmental adaptation. Plays a role in alginate production via the activation of AlgD which is the first gene in the alginate biosynthetic operon. Regulates also the transcription of genes responsible for type IV pili localization and twitching motility. Mediates transition of P.aeruginosa biofilm infections from colonizing to chronic biofilms through repression of the psl operon. Represses also its own transcription by binding to two sites on amrZ promoter, amrZ1 and amrZ2.
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G3XCY6
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GLTR_PSEAE
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Transcriptional regulatory protein GltR
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MSANGRSILLVDDDQEIRELLETYLSRAGFQVRSVSRGADFRQALCEEEASLAILDVMLPDEDGFSLCRWIRSHQRLACMPIIMLTASSDEADRVIGLELGADDYLGKPFSPRELLARIKALLRRAQFTQVRGGDVLAFEDWRLDTVSHRLFHEDGEEFFLSGADFALLKLFLDHPQQILDRDTIANATRGREVLPLERIVDMAVSRLRQRLRDTGKAPRLIQTVRGSGYLLAAQVRPHLQP
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Member of the two-component regulatory system GtrS/GltR involved in the regulation of glucose metabolism and transport, as well as regulation of the exotoxin A gene expression. GltR controls the transcription of genes involved in glucose metabolism (glk and edd/gap-1) and transport (oprB) as well as the expression of toxA that encodes exotoxin A, the primary virulence factor. Acts as a repressor that is released from its target operators upon phosphorylation.
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G3XD01
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WBPD_PSEAE
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UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronate N-acetyltransferase (UDP-D-GlcNAc3NA N-acetyltransferase) (EC 2.3.1.201) (UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronic acid 3-N-acetyltransferase)
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MSYYQHPSAIVDDGAQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTLEEGVFCGPSMVFTNVYNPRSLIERKDQYRNTLVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQIGWMSEFGEQLQLNEQGEAVCSHSGARYVLNGKILSKVDV
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Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the transfer of an acetyl group to the C-3 amino position of UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate (UDP-D-GlcNAc3NA).
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G3XD23
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WBPB_PSEAE
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UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate oxidase (EC 1.1.1.335) (UDP-2-acetamido-2-deoxy-alpha-D-glucuronic acid 3-dehydrogenase) (UDP-N-acetyl-D-glucosaminuronic acid 3-oxidase) (UDP-D-GlcNAcA 3-oxidase)
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MKNFALIGAAGYIAPRHMRAIKDTGNCLVSAYDINDSVGIIDSISPQSEFFTEFEFFLDHASNLKRDSATALDYVSICSPNYLHYPHIAAGLRLGCDVICEKPLVPTPEMLDQLAVIERETDKRLYNILQLRHHQAIIALKDKVAREKSPHKYEVDLTYITSRGNWYLKSWKGDPRKSFGVATNIGVHFYDMLHFIFGKLQRNVVHFTSEYKAAGYLEYEQARVRWFLSVDANDLPESVKGKKPTYRSITVNGEEMEFSEGFTDLHTTSYEEILAGRGYGIDDARHCVETVNTIRSAVIVPASDNEGHPFVAALAR
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Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the NAD-dependent oxidation of UDP-N-acetylglucosaminuronic acid (UDP-D-GlcNAcA) to UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronic acid (UDP-3-oxo-D-GlcNAcA). Cannot use UDP-GlcNAc or UDP-GalNAc as the nucleotide sugar substrate, and can use only poorly UDP-D-glucuronic acid (UDP-GlcA). Undergoes an NAD(+) recycling mechanism using 2-oxoglutarate as an oxidant.
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G3XD24
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PCTA_PSEAE
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Methyl-accepting chemotaxis protein PctA
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MIKSLKFSHKILLAASLVVFAAFALFTLYNDYLQRNAIREDLESYLREMGDVTSSNIQNWLGGRLLLVEQTAQTLARDHSPETVSALLEQPALTSTFSFTYLGQQDGVFTMRPDSPMPAGYDPRSRPWYKDAVAAGGLTLTEPYVDAATQELIITAATPVKAAGNTLGVVGGDLSLKTLVQIINSLDFSGMGYAFLVSGDGKILVHPDKEQVMKTLSEVYPQNTPKIATGFSEAELHGHTRILAFTPIKGLPSVTWYLALSIDKDKAYAMLSKFRVSAIAAALISIVAILVLLGLLIRLLMQPLHLMGRAMQDIAQGEGDLTKRLAVTSRDEFGVLGDAFNQFVERIHRSIREVAGTAHKLHDVSQLVVNASNSSMANSDEQSNRTNSVAAAINELGAAAQEIARNAADASHHASDANHQAEDGKQVVEQTIRAMNELSEKISASCANIEALNSRTVNIGQILEVIKGISEQTNLLALNAAIEAARAGEAGRGFAVVADEVRNLAHRAQESAQQIQKMIEELQVGAREAVATMTESQRYSLESVEIANRAGESLSSVTRRIGEIDGMNQSVATATEEQTAVVDSLNMDITEINTLNQEGVENLQATLRACGELETQAGRLRQLVDSFKI
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Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Major receptor that responds to all naturally occurring L-amino acids, except L-Gln and L-Asp. Also involved in repellent responses to trichloroethylene (TCE), chloroform and methylthiocyanate. Also mediates chemotaxis to histamine, but does not bind histamine. In addition, binds the quorum-sensing signal autoinducer 2 (AI-2), thus inducing chemotaxis toward AI-2 and biofilm formation.
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G3XD94
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UGND_PSEAE
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UDP-N-acetyl-D-glucosamine 6-dehydrogenase (UDP-D-GlcNAc 6-dehydrogenase) (EC 1.1.1.136) (UDP-N-acetylglucosamine 6-dehydrogenase)
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MIDVNTVVEKFKSRQALIGIVGLGYVGLPLMLRYNAIGFDVLGIDIDDVKVDKLNAGQCYIEHIPQAKIAKARASGFEATTDFSRVSECDALILCVPTPLNKYREPDMSFVINTTDALKPYLRVGQVVSLESTTYPGTTEEELLPRVQEGGLVVGRDIYLVYSPEREDPGNPNFETRTIPKVIGGHTPQCLEVGIALYEQAIDRVVPVSSTKAAEMTKLLENIHRAVNIGLVNEMKIVADRMGIDIFEVVDAAATKPFGFTPYYPGPGLGGHCIPIDPFYLTWKAREYGLHTRFIELSGEVNQAMPEYVLGKLMDGLNEAGRALKGSRVLVLGIAYKKNVDDMRESPSVEIMELIEAKGGMVAYSDPHVPVFPKMREHHFELSSEPLTAENLARFDAVVLATDHDKFDYELIKAEAKLVVDSRGKYRSPAAHIIKA
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Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the C-6 dehydrogenation of UDP-D-GlcNAc to UDP-N-acetylglucosaminuronic acid (UDP-D-GlcNAcA).
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G3XD97
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PTXS_PSEAE
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HTH-type transcriptional regulator PtxS
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MNGSVLPSRGRVTINQVAEAAGVSKASVSRYIGGDRQLLADATARRIERAIDQLDYRPNQMARGLKRGRTRLIGMLVADILNPYSVAVMHGVETACREHGYSLVVCNTDRDDEQERHHLAALQSYNVEGLIVNTLGHHPGELRALHRELPMVLVDRQLAELDTDLVGLDNADAVEQALDHLQHRGFRDILLVTEPLDGTSSRIERVQAFNASIGRRPALKGQVLQTDDFFRDGLRAFLSASGPGPKALFTCNGVATLCATRQLRDLGCRLFDEVGLLALDELDWYPLVGSGITALAQPTDEIGRTAFERLLARLEGDREPARRVTFPAQLIVRGSTHPRG
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Negatively regulates glucose metabolism by binding directly to the promoter region of the kgu and gad operons. It also negatively regulates its own synthesis. In addition, in pathogenic strains, PtxS modulates PtxR activity in response to 2-ketogluconate. In the presence of PtxR, which also binds to the kgu and gad promoter regions, PtxS and PtxR form a tight complex, creating a DNA-loop that prevents RNA polymerase promoter access and expression of the glucose metabolism genes. Binding of the 2-ketogluconate effector to PtxS causes PtxS/PtxR complex dissociation and leads to the dissolution of the repression DNA-loop, facilitating the entry of the RNA polymerase and enabling the transcription of the genes. Also plays an important role in the regulation of the expression of the virulence factor exotoxin A (toxA). PtxS does not bind directly to the toxA promoter but negatively regulates the production of exotoxin A by binding to PtxR and interfering with its positive regulator activity. In the presence of 2-ketogluconate, PtxS is released and PtxR can recruit RNA polymerase.
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G3XDA8
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PSTS_PSEAE
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Phosphate-binding protein PstS
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MKLKRLMAALTFVAAGVGAASAVAAIDPALPEYQKASGVSGNLSSVGSDTLANLMTMWAEEYKRLYPNVNIQIQAAGSSTAPPALTEGTANLGPMSRKMKDVELQAFEQKYGYKPTAVPVAVDALAIFVHKDNPIKGLTMQQVDAIFSATRLCGSKQDVKTWGDLGLTGDWAKKPVQLFGRNSVSGTYGYFKEEALCKGDFRPNVNEQPGSASVVQSVSQSLNGIGYSGIGYKTASVKTVALAKKEGAAFVEDNEQNALNGTYPLSRFLYVYVNKAPNKPLDPLEAQFLKLVLSKTGQQVVVKDGYIPLPAKVAEKAIKELGL
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Binds 1 inorganic phosphate per subunit with a KD of 0.34 uM. Required for phosphate transport (Ref.5). In strain PAO1 implicated in host cell adhesion in some virulent strains (e.g. MDR25 which expresses very high levels of this protein) antibody fragments against this protein decrease host cell adhesion and increase transepithelial resistance of human epithelial cell monolayers. Its ability to bind phosphate may allow it to acquire phosphate from its host.
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G3XP38
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OTASE_ASPNA
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Ochratoxinase (OTase) (EC 3.4.17.-) (Amidohydrolase 2) (Amidase 2) (Carboxypeptidase Am2)
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MVRRIASATPMVQSPMSPLGTTYCVRPNSVSMNLQRRPLVIASTDEAKVTIIYAGLLIPGDGEPLRNAALVISDKIIAFVGSEADIPKKYLRSTQSTHRVPVLMPGLWDCHMHFGGDDDYYNDYTSGLATHPASSGARLARGCWEALQNGYTSYRDLAGYGCEVAKAINDGTIVGPNVYSSGAALSQTAGHGDIFALPAGEVLGSYGVMNPRPGYWGAGPLCIADGVEEVRRAVRLQIRRGAKVIKVMASGGVMSRDDNPNFAQFSPEELKVIVEEAARQNRIVSAHVHGKAGIMAAIKAGCKSLEHVSYADEEVWELMKEKGILYVATRSVIEIFLASNGEGLVKESWAKLQALADSHLKAYQGAIKAGVTIALGTDTAPGGPTALELQFAVERGGMTPLEAIKAATANAPLSVGPQAPLTGQLREGYEADVIALEENPLEDIKVFQEPKAVTHVWKGGKLFKGPGIGPWGEDARNPFL
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Carboxypeptidase that catalyzes the release of a C-terminal amino acid with specific catalytic activity for aromatic amino acids such as phenylalanine. Is able to degrade ochratoxin A, one of the five major mycotoxins most harmful to humans and animals that is produced by Aspergillus and Penicillium species and occurs in a wide range of agricultural products.
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G3Y419
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YANA_ASPNA
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6-methylsalicylic acid synthase (6MSAS) (EC 2.3.1.165) (Non-reducing polyketide synthase yanA) (Yanuthone D biosynthesis cluster protein A)
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MSASRSSTKFSTPAEGSDNGKEFTTPATSTEGHEVPDRPGDALADVAIIGMACRTPGDVRSPDSLWQYLLKKGDASGSLPDWRWEPYRQRHPRNAALLAQTTAKGYFLDDIDHFDAAFFSISPREAEQMDPQQRLALEVAWEALENAGISPPQLAGSNTSVYMGVNSDDYAKLLLEDLPNVDAHMGVGTAYCGIPSRISYILDLMGPSVALDAACASSLVAVHHARQAIRAGETDLAIAGGVNALLGPGLTRVLDEAGAISTDGKCRSFDETASGYGRGEGAGVVILKRLDKALADGDHVLAVLKGSAVASDGKTLGIMAPNARAQLLVAQKALAEAKVSADSINYVEAHATSTSLGDPTETNALAEVYGAGSGRSPSDPCYIGSIKPNIGHLEAGAGVMGLIKAVLVLRHGQVPPQANLKTLNSKIAWNENLLCPPRELVTLPCPGPIHPLRAAVASYGYSGTVSHAVLEAFAGHSEFAERLSQIPTGDDPSPVLLLISAPQARRVSAAAGALKQWLSENEASISLKTVSSTLAQRRAHHRYRHAIVADSVPDAIAALDDVSKEAPNRWVIKDKIDSKAAKGPVWIFSGHGAQWADMGRELFESSPAFEEVVRNLEPIIQDEVGFSAIETLQKGCPDRSDVVQVMTFLMHLGIAAVLEIESGPPSAVVGHSLGEAAAAVVSGALTWREGALVVCRRARLYRELMGQGAMALVRVSAEEARTRIGRQTGVWVAIETSPSACVLSGEVDAIKQLSDRWREEGIEVRMVASDVPFHTPMLERLAKPLYESLRGELHPRVPNRALFSTSQPDPRSEVLRDAQYWVTNMIQPVRLQSAIAAIAQDGFRALVEVSSHPIVTHSVVETMGECTEDPVLVTPTMVRRQPALKSILAATGRLHCFGCAIKFIELDPNAPWNSSVPSTVWHHQPFYRAVSQTSASSQLETTHDPAANNLLGKRIALWGTEEVLYQTRLEEENRPFPGHHPLHGSEIVPAAVLLRTFLQALTPRCVEQVSLQVPVVVSPARKVQIRHNTRNITITSCLEESSSQEDGSWLVNTTAAVGAANVVPSQSRMDLSELRKRLPQKLADSFSIDYLASVGVSAMGFPWQVTHHVASDDEMLARVDANPDNMGGMNDFLTSLMDAATSISSTLWHRQPLLRMPTSVRRVVAVHEIPIPRVVYIHCTKVASTSECTADVTLTGEDGTVLMEIQGMSFAGLEGESFSRKSTAGLVHQIQWPPAALVEDPSEFSHIAFVTPDITDPRLEQYQSQLDALAITSSVHQAASDLPLTSHTSLAVVYLPQTMTDVFDTATRSCNDLVSIIQTITAAASSTTRVFVLTAGTELGHSALLGLSRIIQAEHPDIWGSLIEVEDTFSLPLMAMRYVRDADVIRIKDGVPRIARLRPLPSASSSLTPLTFSPASTYLITGGLGALGLSVAHWMVTQGARRLLLLSRRALPPRSTWSSTHMNNPTIQSILALERLGATVHCLPIDISLPMAASGLRSTLETLNLPSVAGVIHAAGIVSDQLVEQVTPDVLESVLAPKIKGALNLHDVFPPASLDFFVLFSSCGQLLGFPGQASYASGNAFLDGLARSRRAQGDNAISLLWTTWRGMGMGQSANGAMEAELYARGITDITPDEAFRAWSAVASTGGGGTDHAVIVRARVLEGGEPLPHPILTDIATRKAEVVNAGEHPAGSQEVKLSGRELEQHLRDVINGCVSKTLSVKEDEIDDAVALAEMGMDSVMTVNFRMTLQQTLKVPVGPTLIWKCPTVQHLVKHFTKELDA
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Non-reducing polyketide synthase part of the gene cluster that mediates the biosynthesis of yanuthone D, a fungal isoprenoid epoxycyclohexenone that acts as an antibiotic against fungi and bacteria. The first step of the pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by the polyketide synthase yanA. 6-MSA is then converted to m-cresol by the decarboxylase yanB. The cytochrome P450 monooxygenase yanC then catalyzes the oxidation of m-cresol to toluquinol. Epoxidation of toluquinol is then performed by the short chain dehydrogenase yanD, with the help of yanE, and a further prenylation by yanG leads to 7-deacetoxyyanuthone A. The next step is the hydroxylation of C-22 of 7-deacetoxyyanuthone A by the cytochrome P450 monooxygenase yanH to yield 22-deacetylyanuthone A. O-Mevalon transferase yanI then attaches mevalon to the hydroxyl group of 22-deacetylyanuthone A to produce yanuthone E. Finally, the FAD-dependent monooxygenase yanF oxidizes the hydroxyl group at C15 of yanuthone E to form yanuthone D. Furthermore, several branching points in the pathway lead to the production of yanuthones F and G from 7-deacetoxyyanuthone A yanuthones H and I from 22-deacetylyanuthone A and yanuthone J from yanuthone E.
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G4FEF4
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AGAL_THEMA
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Alpha-galactosidase (EC 3.2.1.22) (Melibiase)
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MEIFGKTFREGRFVLKEKNFTVEFAVEKIHLGWKISGRVKGSPGRLEVLRTKAPEKVLVNNWQSWGPCRVVDAFSFKPPEIDPNWRYTASVVPDVLERNLQSDYFVAEEGKVYGFLSSKIAHPFFAVEDGELVAYLEYFDVEFDDFVPLEPLVVLEDPNTPLLLEKYAELVGMENNARVPKHTPTGWCSWYHYFLDLTWEETLKNLKLAKNFPFEVFQIDDAYEKDIGDWLVTRGDFPSVEEMAKVIAENGFIPGIWTAPFSVSETSDVFNEHPDWVVKENGEPKMAYRNWNKKIYALDLSKDEVLNWLFDLFSSLRKMGYRYFKIDFLFAGAVPGERKKNITPIQAFRKGIETIRKAVGEDSFILGCGSPLLPAVGCVDGMRIGPDTAPFWGEHIEDNGAPAARWALRNAITRYFMHDRFWLNDPDCLILREEKTDLTQKEKELYSYTCGVLDNMIIESDDLSLVRDHGKKVLKETLELLGGRPRVQNIMSEDLRYEIVSSGTLSGNVKIVVDLNSREYHLEKEGKSSLKKRVVKREDGRNFYFYEEGERE
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Hydrolyzes the short-chain alpha-galactosaccharides raffinose, melibiose and stachyose.
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G4MVZ2
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ACE1_MAGO7
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Polyketide synthase-nonribosomal peptide synthetase ACE1 (PKS-NRPS ACE1) (EC 2.3.1.-) (EC 6.3.2.-) (ACE1 cytochalasan biosynthesis cluster protein ACE1) (Avirulence conferring enzyme)
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MRDEMWNTATEPIAIIGSGCKFPGGSTTPSKLWELLKDPKDIVSEIRPDRFDVDKYFHPDHKHHGTSNVRHSYFLEENFKHFDAKFFGIRPQEAMAMDPQQRFLLETVYESLEAAGITISDLKGSQAGVFVGNMGVDYSELLSQDIDAFPTYFAPGTARSILSNRISYFFDLHGPSVTVDTACSSSLVAVHQAVQSLRLGETPVAIVCGANLLLGPAQYIAESKLQMLSPNGRSRMWDASADGYARGEGFASIVLKPLSVALANGDHIECIIRETGCNQDGRTKGITMPSPLAQCKLIQETYKRAGLDLSKSSDRPQYFEAHGTGTPAGDPVEAEAISTAFFGPESGFRRTSHDPKLYVGSVKTVIGHTEGTAGLAGLIKASLAMKAKSIPPNLHLERVNPAVQPFYGNLEIPTRLMDWPEPAPGQPLRASVNSFGFGGANAHVILESYTPAAEVAMVTPTAAAGPVFSPFVFSASSDKALASMLSAYSDYLSLNPTVDLRSVAYTLSQHRSVFDKRAAISAPDLDTLKTKLKARSEEASPSGKTAAVQSLERRPRYLGVFTGQGAQWARMGVDVINASPAARAIFEDLEQSLKTLPEEDRPSWSMLEELLAPPETSRVYQANISQTVCTAVQVMMVQLLRAAGIEFSCVVGHSSGEMAAAYTAGYLSARDAVRAAYFRGVHSQLAKGSNGQPGGMIAVGTNFEDAEELCELDDFKGRLCVAASNSAELVTLSGDLDAVQEVKKILDAEEKFNKQLQVDKGYHSHHMLPCSEPYVASLQKCGIQAQVPGDATACRWISSVYVDDMTNLDCRVQDRYWIENLAKPVMFSQALSHALGGDDKFDSVIEVGPHPALKGPASQTIQACLGERLPYFGCLSRGTDSNEAFAEFLGGVWSTFGSSAVDLAAYERFATGGCDQRLVKGLPSYTWDHDVEHYFQSRLSKVVLHRSTPPNELLGTRLPDDTAGEVRWRNSLHPGELPWLLQHSAQGQTVFPGTGYIATTLEAVKQLFDSSGVQTVEIRDMVIGNALVIEANTGVETLFSLTFINTQTDRITAHFSFCSQQGGSTKLVENASGDLVVLLGEPSEDALPRSFHPGTQMKDIDEERFYEAIDKLGYGYEGPFRALSQLQRRMGAATGLVAIPEKTKHFDQMVLHPAALDAMVQTVLLAYCYPGDTRLQGISLPTGIDCIRFNYGMLSEAARPGCQLPFLSCTAFEGDDVLGGVGGDVGGDVDVFSEDKRFALIQLQGLHTKPLSPPSAATDLQIFSEMEWKTASPEGADMEVRGEKRAYVADLYSSMERVAYFYMRHVDREIGKDRSGLAPHQVRFLEWVDHMCGRVEAGTLPHISRKWDHDTRQDILKIIAKYPDSIDLELMHAVGENLCSVFRGEMNALEPMVKKNMLNRFYSDALGMSPYTEDLARMVGHITHRYPHMNILEVGAGTGGATKVMLRRLQDAFASYTYTDISSGFFADARQVFKAHESKMLFKTLDIEKDIVDQGYEENSFDLVIANLVVHATADLDATMGRLRRLVKPGGHLVLLEITTNDPLRFGFIFGPLPGWWLGGEDGRVHSPCVDVEWWDRVMKRNGFSGADIVTPHHTLGPLSVIMTQAVDHRVQLLRQPTSADFGDFTIDPERLTIVGGVKPLAEGLEQLLKPRYQSVAWIPTLEEVSSHSLPVMGSVLSLVELDEPLFKDMTAQTLEGFKFVFQQSRSVYWITCGASGANPYSNMAAGVARTVALEMRHLRLGFLDFEDAKDATVQRLADRFLEFEILGTLEQQGKLDHLTWYQEPELRFDGKNLLVPRMKLSKDRNGRYNSRRRQLTKNVNPREVPVSLVPTTSGKDFVLKESLSSSSTKHGAQDTVSLRVHYASQRSLRLESSDYLFLVLGTNLSSGEAMFALADSNRSIVHVDRQWTTSYLGNLDHGRHALADLYTQIMASTVVAGLSAGDSLVVLDAETPLSQALSARCAAKGVRLTLLSTTTATSHSEADGTNKTNVRIHPLESRRSIESKLPSNATCFLDLSTNNGSEAAAVINSYIPAQCRVETRDTLTATACQVTRSTSTGGLGPAVGDVLPACWANVEAAGRDLSFFSAAVVTPTELTAAAGNGKTSAPRVGDDALLLITDWTAEAEVGVLVQPADSMVRFRQDKTYWLVGLTGGLALSLCRWMVNRGARYVVMTSRNPKIDKEWLQGVESCGATVKIFSNDVTDRAAVNSAYRTISATLPPIAGVVQGAMVLRDTMFAETTMETIESILGPKVRGSIYLDEIFYSTPLDFFVFLSSVTATSGNPGQSIYAGANMFMNSLAAQRRKRGVAGSSVEIGCIMGNGSVTTILSYEHQKYLFSVGNTWLAEQDFLTMFGEAVLASPPDAPDSVTSVTGLRLQFNDDKPDITWFSNPIFQHLVLQSGNAMQTSLSVARQGTPVKSLLQEAKSSEEVLDILKDAFTAKLVSSLQADPDSNLLEVDLETLGMDSLVAVDLRSWFLAELSVDVPVLKILNGSTARLLLEFVQGLIPASMTPKLDGSDGADAAAQEAPPVAPPVTKPKPDVSVKVPPPHQPVASLKPSGPASPTSPSSATASPGRSRSVASPVTADTPVSPTTSASMASLNDSRKLIRTVPVSFGQSRFWFLGSYNPDPLAFNITSLMRISGPLRTNDFGKAVDKVLNHHEALRTSFVSENDAPVQKIWSSPAFALEQRKIADDESEVVKAYTEVQNTRYNLEAGQTMRIMLLTKSPTKHVLVLGYHHINMDGVSFEVLFSDIEKAYNRTPLDRSVMQFPDFTIREAGEYKSGAWRSELQYWQSKFTSLPEPTPLLSVSKRRTRPVNLSYTTHSVSRRINAEQSQAIHTVGRKFKATPFHFYLSVFKTLIARFSGADDFCIGIADANRKEDKVMGAVGLYLNLLPLRVRSALGQTFGETLADMKKVSQEAFANSKVPFDVLLNELSVPRSSSQTPLFQTFVNYRRGVSEERSFCGCTGAGELISGGQIGYDISLDIVENPGGDALVTLSVQKDLYNVDMANLLLDSYFRLVDSFAKNPATSLNRPAIYDPVAVDKALTLGCGPTLEDSSWPETLIHRIENMSVKYATKFALRNGQNGGLTYSQMIARINDIAAKLIDAKVGTGIVGVMQASTMDFICSILAVWKAGAIYTPLDPRLNSTDRLKAVVDECQPACILVDATTKPLFDSLATNAVQIDVSMVQSSKTLEASPKVAIHAKAPSAAAVFYTSGSTGVPKGITLSHASLTYNIMAATRQFGFKEGVDIMLQQSSFSFDMALAQMLTSLSNGGTLVVVPSHLRGDALGLSQLIVAENVSIVQASPTEYKSLIGVNAQHLKTSKWRVALSGGENMTQSLLEVFRSLGKPDLVLFNGYGPTEATINANTRIVPYHEPNSNPDLPLLTWPNYSISIVDLELNPVPVGVFGEVCIGGAGVGLGYFKNDELTAKAFVADKTAPAEFVAKGWKTKFRTGDLGRLSPDGGLIIEGRIDGDTQVKLRGMRIDLKNIESAILQAGAGKIIDAAVSVRRGGADESEPQYLVGHVVLDADQTPEDSQQDFLAQLIPRLRLPRHMKPSLLVPIRALPQTASHKLDRRALQQLPISDAGQIAKQSQQGAELGSDQARMWKLWKQVIPRDVVSQYSITPQSDFFHVGGTSLLLVNLQSLIAREHGRAPPLHAMFESSTVAAMTDLVLSDDASGSTALIDWEQETSIPTLPPHIIPGGAGNKVSVPPRVVLLTGATGFLGRQLMAFLLRQPSVKRIHCLAVRGGAPPSSAAPFSDPRVSIHAGDLNAPHLGLGEAVAELLFAQADVIIHNGADVSFLKTYATLRATNVGSTRELARLAAPRRIPFHFVSSASITQLTGLDEFGEASMAAWAPPADPRGMSGGYAAAKWASEVLLEKAARAWGLPVVIHRPSSITGEGTNSLDLMGNMFKYIEQLEAVPESDSWKGNFDFVSVENVAADIVQAVVAANVVAAGGVKFIYEAGDIVYPLSMVKDMSEGGAKLPVKTMPLAKWVEKAAEKGLDSMLAEYLIKAASTGTSLAFPRLLKDGN
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Hybrid PKS-NRPS synthetase part of the gene cluster that mediates the biosynthesis of a tyrosine-derived cytochalasan acting as a fungal signal recognized by resistant rice plants and leads to avirulence in Pi33 resistant rice cultivars. The first step in the pathway is catalyzed by the hybrid PKS-NRPS ACE1, assisted by the enoyl reductase RAP1, that are responsible for fusion of the tyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of ACE1 is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the tyrosine precursor. Because ACE1 lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase RAP1. Reduction by the hydrolyase ORFZ, followed by dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase ORF3 then yield the required isoindolone-fused macrocycle (Probable). A number of oxidative steps catalyzed by the tailoring enzymes identified within the cluster, including cytochrome P450 monooxygenases CYP1 to CYP4, the FAD-linked oxidoreductase OXR2 and the short-chain dehydrogenase/reductase OXR1, are further required to afford the final cytochalasans that confer avirulence and which have still to be identified (Probable). The monooxygenase CYP1 has been shown to be a site-selective C-18 hydroxylase whereas the function of CYP3 is the site-selective epoxidation of the C-6/C-7 olefin that is present in some intermediate compounds. Finally, SYN2 and RAP2 are not required for avirulence in Pi33 resistant rice cultivars.
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G4MY67
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FNTB_MAGO7
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Protein farnesyltransferase subunit beta (FTase-beta) (PFTase beta) (EC 2.5.1.58) (CAAX farnesyltransferase subunit beta) (Ras proteins prenyltransferase subunit beta)
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MRHHTKNLRRRAIFLRTTPRGNMDSSSSVATSTSSSSNHRLVRSSEGSPSAGGDDIEEVIMTPGIATGRVQPAVSVAIPDLFTQLPPVKDDLATSTSKTQDETVAICLPYLAGSDANADVEHNAHGVPHIDRKKHVRFLRNMLRQLPAPFIAADASRPWFLYWSLNAMAILGENVKEDYAESLADTARSMQNESGGFSGGHGQTSHLATTYAVVLALAVVGDEEGLSLIDRRALWKWLCDLKEADGGFRMSLGGEEDVRGAYCAAVIISLLNLPLDLCKDSEAYIRDPTANLFTGLGDYVRKCQTFEGGISGQPDAEAHGAYAFCALGCLSLLGTPSETIPKYLNIERLISWLSSRQYAPEGGFSGRTNKLVDGCYSHWVGGCWPLIEACLNGPVKVSSLDVEPQPLFSREGLMRYILCCCQEQGKRGGLRDKPGKPSDAYHSCYVLSGLSSAQNRWQLVVGDDDMPAWMVSPFPNEEEIFDEKDRVGTVHPVYVIPEDKVAKVQTFFASRDGF
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Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The beta subunit is responsible for peptide-binding.
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G4N0Z0
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PMK1_MAGO7
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Mitogen-activated protein kinase PMK11 (MAPK PMK1) (EC 2.7.11.24)
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MSRANPPSNSSGSRKISFNVSEQYDIQDVVGEGAYGVVCSAIHKPSGQKVAIKKITPFDHSMFCLRTLREMKLLRYFNHENIISILDIQKPRSYETFNEVYLIQELMETDMHRVIRTQDLSDDHCQYFIYQTLRALKAMHSANVLHRDLKPSNLLLNANCDLKVCDFGLARSAASQEDNSGFMTEYVATRWYRAPEIMLTFKEYTKAIDVWSVGCILAEMLSGKPLFPGKDYHHQLTLILDVLGTPTMEDYYGIKSRRAREYIRSLPFKKKVPFRTLFPKTSDLALDLLEKLLAFNPVKRITVEEALKHPYLEPYHDPDDEPTAPPIPEEFFDFDKHKDNLSKEQLKQFIYQEIMR
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Mitogen-activated protein kinase part of the MST11-MST7-PMK1 MAP kinase (MAPK) cascade that is essential for appressorium formation, penetration and invasive growth. Central regulator of appressorium development that acts downstream of the cAMP signal. The MST11-MST7-PMK1 MAP kinase cascade transduces signals from the cell surface sensors MDB2 and SHO1 that recognize various surface signals such as surface hydrophobicity, cutin monomers, and rice leaf waxes. Regulates expression of secreted fungal effector proteins implicated of host immune defenses, preventing reactive oxygen species generation and excessive callose deposition at plasmodesmata. Furthermore, controls the hyphal constriction required for fungal growth from one rice cell to the neighboring cell, enabling host tissue colonization and blast disease. Targets downstream of the PMK1-MAPK pathway include transcription factor MST12 and pathogenicity-related genes GAS1 and GAS2, both of which are expressed during appressorium formation, even if regulation of MST12 is not associated with expression of GAS1 or GAS2.
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G4N137
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TAS1_MAGO7
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Hybrid PKS-NRPS synthetase TAS1 (EC 6.3.2.50) (Tenuazonic acid biosynthesis cluster protein 1) (Tenuazonic acid synthetase 1)
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MYNRCCRKVWIQGRVAYRPAYIRQSPPQQTLYRGIDLLPFTTIVMDHQSGFQNPSPSGGLMFSASAKRFISRIVGFVGRGAEVQQKAVGLCPLKTERRRAAAGGLLLPTGLRMGRSIIMSVRPLPFLTGPAPSPDTAAGFKPSPPTGNLVSVSPLSKAQMALWFDYLQHPTSTHYFLTLKVELDKQPLSLDKIIQVIRGLGKQHAMLRTTFHVDTDTDDMSKSYMAVHDDSWDQEIHVLMNDAQLYEALRKPFQLSSESPVRWVVQMKLQPGSARSTYTVYAAGHHIGVDGASMSVLSNQLLEAVASEVEDQPDHSGPHYGDYIQRQARYLRSSAGAAAGRFWLSQLRHTQPFRWRMEPPEEINTPNYRQLDTWNFFPTAEIQEWGNLYKTSWFRVATSIVGLVTAAMAEPQAHHDHALMVAFGARPRGFENNVSHMANTMPVKFPLSSLLRDDATFSDAVKAMGRNVSTAKKHENFPFMSLMEQANRHMDPTLLDFKVAITYSPKLANKSCELFPVEGIWDLFFCFLEQEDGVALGVISNPRVFGAEALGQLQSLFNEVFALSKARPSFKLSDLAFLQNRTPARFISGPALDDVESISKSRVYRLIKARAASQPDLVALMSAEKGVQMTYRELAAQSSQVAHFLQKQRLCKGDAVLVHLERGFAQIVWILGVMEAGACYVALDKTWPAARKEAILRTANGKLLVTDDEQMDFEKQDTTVVFLAPSAAEIASMPQSTCECEVADDDLAYVVFTSGSTGQPKGVMVEHSNLSHYVSATRSLVKTGPHSRMLQLASFAFDAIVLEYAVTLAHGGTLCFANHPEVLVGEYLADVIDSNQVNFFHCTPSVLSTLPAGRRLPSLRIVSVGGEASPPGLLDHWRKRVELLHAYGPTECTVICTLESLTQDESTQTAIDATVIGKALPNLDIRICEEGKLEPLAPNQVGEICVVGPQVSRGYMGQEELTASKFHNITLADGHPSRLYRTGDKGFIDDDGKLHIQGRIGNREIKVRGYRLDLYEVEKNVMAFDPEVTQVSIQQVGESLVALVVPASIDCDRIRSKLLKDMPRYAVPTRFIRVASLPLNTNGKIDHTQASSLAAELVMHDTVLPTVDATPTPTAAVRAVGVTEENLRLKTKENGMERQEMLRRHLTAEVTALWAKLLGSSRQFDPEVGFFDAGGHSLLLTQLHKLIKERFGTGSRPSLLDIFSMSSIRKQVDCLMGIVDQDAMLGSEPTGGSSSRSQSRRSAETSSSSTSAPSSVPVDAERNLYAIVGISCRFPGANTAEQLWNVLMEQRDAITTFCPAENLGFALEENSVFVPRYGMIDALKDFEPSAYSMSDAEAQTIDPQKRVFLDVAADALADAGTSASPGNPLDPVGVFVGAATNTFLSSRDNPGSKPPGDEEPQSFANHYQQLLDCPIGTFASFKLNLTGPVVTLNTACSSALAALHLACASLSHGDCNAAVVGGVSMAYPQEGGYVTARPGGDSSAVFSPSGVCHPLDSRADGCVPADGAAALVIKRLADARADGCRVYAVIEGVAVSADGSDDKAGLGVPSSSGQSRTVEAALRRAGPQALSRLRYVEMHGSGTPWGDALEVQGLKMAFDRLSKTGAAEQSGTGRAQPEADRIYLGSNKGNCGNTEAASGLLSLIKASMALNLGVVPPLPNLAEPNPKCEFEETKFEPLGKQLALAPGDRVMNKRQRIVRSPNWISDATWFVISTVDNLLPKLTPAAVA
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Hybrid PKS-NRPS synthetase part of the gene cluster that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-termainal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.
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G4N2X9
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OXEAS_MAGO7
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Bifunctional dioxygenase (DOX)-epoxy alcohol synthase (EAS) (10R-DOX-EAS) [Includes: Fatty acid alpha-dioxygenase (DOX) (EC 1.13.11.-) (EC 1.13.11.62); Epoxy alcohol synthase (EAS) (EC 1.-.-.-) (Cytochrome P450 monooxygenase) (CYP)]
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MDGAVRLDWTGLDLTGHEIHDGVPIASRVQVMVSFPLFKDQHIIMSSKESPSRKSSTIGQSTRNGSCQADTQKGQLPPVGEKPKPVKENPMKKLKEMSQRPLPTQHGDGTYPTEKKLTGIGEDLKHIRGYDVKTLLAMVKSKLKGEKLKDDKTMLMERVMQLVARLPTESKKRAELTDSLINELWESLDHPPLNYLGPEHSYRTPDGSYNHPFNPQLGAAGSRYARSVIPTVTPPGALPDPGLIFDSIMGRTPNSYRKHPNNVSSILWYWATIIIHDIFWTDPRDINTNKSSSYLDLAPLYGNSQEMQDSIRTFKDGRMKPDCYADKRLAGMPPGVSVLLIMFNRFHNHVAENLALINEGGRFNKPSDLLEGEAREAAWKKYDNDLFQVARLVTSGLYINITLVDYVRNIVNLNRVDTTWTLDPRQDAGAHVGTADGAERGTGNAVSAEFNLCYRWHSCISEKDSKFVEAQFQNIFGKPASEVRPDEMWKGFAKMEQNTPADPGQRTFGGFKRGPDGKFDDDDLVRCISEAVEDVAGAFGARNVPQAMKVVETMGIIQGRKWNVAGLNEFRKHFHLKPYSTFEDINSDPGVAEALRRLYDHPDNVELYPGLVAEEDKQPMVPGVGIAPTYTISRVVLSDAVCLVRGDRFYTTDFTPRNLTNWGYKEVDYDLSVNHGCVFYKLFIRAFPNHFKQNSVYAHYPMVVPSENKRILEALGRADLFDFEAPKYIPPRVNITSYGGAEYILETQEKYKVTWHEGLGFLMGEGGLKFMLSGDDPLHAQQRKCMAAQLYKDGWTEAVKAFYAGMMEELLVSKSYFLGNNKHRHVDIIRDVGNMVHVHFASQVFGLPLKTAKNPTGVFTEQEMYGILAAIFTTIFFDLDPSKSFPLRTKTREVCQKLAKLVEANVKLINKIPWSRGMFVGKPAKDEPLSIYGKTMIKGLKAHGLSDYDIAWSHVVPTSGAMVPNQAQVFAQAVDYYLSPAGMHYIPEIHMVALQPSTPETDALLLGYAMEGIRLAGTFGSYREAAVDDVVKEDNGRQVPVKAGDRVFVSFVDAARDPKHFPDPEVVNPRRPAKKYIHYGVGPHACLGRDASQIAITEMFRCLFRRRNVRRVPGPQGELKKVPRPGGFYVYMREDWGGLFPFPVTMRVMWDDE
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Bifunctional dioxygenase (DOX)-epoxy alcohol synthase (EAS) that converts linoleic acid (18:2n-6) sequentially to 10(R)-hydroperoxy-8(E),12(Z)-octadecadienoic acid (10R-HPODE) and 10R-HPODE further to 12 S(13R)-epoxy-10(R)-hydroxy-8(E)-octadecenoic acid as the end product. Oxygenation at C-10 occurs by retention of the pro-R hydrogen of C-8 of 18:2n-6, suggesting antarafacial hydrogen abstraction and oxygenation. The epoxy alcohol is formed from 10R-HPODE, likely by heterolytic cleavage of the dioxygen bond and subsequent intramolecular epoxidation of the 12(Z) double bond. The DOX domain is also able to oxygenate position C-8 of linoleic acid to produce 8(R)-hydroperoxy-8(E),12(Z)-octadecadienoic acid (8R-HPODE). Moreover, the DOX domain can oxygenate alpha-linolenic acid (18:3n-3) at C-8 or C-10 to produce respectively 8HOTrE and 10HOTrE, oleic acid (18:1n-9) at C-8 or C-10 to produce respectively 8-H(P)OME and 10-H(P)OME (with 8R stereoisomer to over 95%), eicosadienoic acid (20:2n-6) at C-10 or C-12 to produce respectively 10(11)-epoxy-12-hydroxy-14(Z)-eicosenoic acid and 14(15)-epoxy-12-hydroxy-10(E)-eicosenoic acid, as well as eicosatrienoic acid (20:3n-3) at C-10 or C-12 to produce respectively 10(11)-epoxy-12-hydroxy-14(Z),17(Z)-eicosadienoic acid and 14(15)-epoxy-12-hydroxy-14(Z),17(Z)-eicosadienoic acid. On the other side, the enzyme EAS domain can also catalyze the conversion of 10HOTrE into 12(13)-epoxy-10(R)-hydroxy-8(E),15(Z)-octadecadienoic acid, 13-R-HPODE into the stereoisomers of 12(13)-epoxy-11-hydroxy-9(Z)-octadecenoic acids (erythro/threo, 1:4), as well as 13S-HPODE into the stereoisomers of 12(13)-epoxy-11-hydroxy-9(Z)-octadecenoic acids (erythro/threo, 1:4) (EAS activity). Gamma-linolenic acid (18:3n-6) is not a substrate.
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G4N374
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MPS1_MAGO7
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Mitogen-activated protein kinase MPS1 (MAPK MPS1) (EC 2.7.11.24)
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MSDLQGRKIFKVFNQDFIVDERYTVTKELGQGAYGIVCAAVNNQTSEGVAIKKVTNVFSKKILAKRALREIKLLQHFRGHRNITCLYDMDIPRPDNFNETYLYEELMECDLAAIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFSVDPEENAGYMTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGGRPFFKGRDYVDQLNQILHILGTPNEETLSRIGSPRAQEYVRNLPFMAKKPFPTLFPNANPDALDLLDRMLAFDPSSRISVEQALEHPYLHIWHDASDEPDCPTTFNFDFEVVEDVGEMRKMILDEVYRFRQLVRTAPGAGGHGAPHAPQVPIPAGAGQGQWKAEDPRPQEYVGQMNDLEAELAGGLDQRR
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Mitogen-activated protein kinase part of the MCK1-MKK2-MPS1 MAP kinase (MAPK) signal transduction cascade that is essential for cell wall integrity and plant infection, but not for plant defense responses. Beside its role in pathogenesis, the MPS1 cascade is active in conidiation and cellular stress responses. Targets downstream of the MPS1-MAPK pathway include transcription factors MIG1 and SWI6, as well as GSK1 and MPG1.
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G4N4J5
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LIDS_MAGO7
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7,8-linoleate diol synthase (LDS) [Includes: Linoleate 8R-lipoxygenase (EC 1.13.11.60); 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase (EC 5.4.4.6)]
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MASSSSSGSSTRSSSPSDPPSSFFQKLGAFLGLFSKPQPPRPDYPHAPGNSAREEQTDITEDIQKLGFKDVETLLLYLNSSVKGVNDDKQLLLERLIQLLSKLPPTSTNGKKVTDGLITGLWESLDHPPVSSLGEKYRFREADGSNNNIHNPTLGVAGSHYARSAKPMVYQNPNPPAPETIFDTLMARDPAKFRPHPNQISSVLFYFATIITHDIFQTSSRDPSINLTSSYLDLSPLYGRNLEEQLSVRAMKDGLLKPDTFCSKRVHGFPPGVGVLLIMFNRFHNYVVTSLAKINEGNRFKKPVGDDTAAWEKYDNDLFQTGRLITCGLYVNIVLVDYVRTILNLNRVDSSWILDPRTEEGKSLLSKPTPEAVGNQVSVEFNLIYRWHCGMSQRDDKWTTDMLTEALGGKDPATATLPEFFGALGRFESSFPNEPEKRTLAGLKRQEDGSFEDEGLIKIMQESIEEVAGAFGPNHVPACMRAIEILGMNQARSWNVATLNEFREFIGLKRYDTFEDINPDPKVANLLAEFYGSPDAVELYPGINAEAPKPVIVPGSGLCPPSTTGRAILSDAVTLVRGDRFFTVDYTPRNLTNFGYQEAATDKSVDNGNVIYKLFFRAFPNHYAQNSIYAHFPFVIPSENKKIMESLGLADKYSWQPPQRKPATQMIRSHAAAVKILNNQKDFKVVWGESIGFLTKFPTGENPGLGFALAGDAPANQQSRDQLMKCIFSPKAWEDEVRQFCEATTWDLLRRYSAKVQDKGPHLKVHTHEIDVIRDVISLANARFFAAVYSLPLKTENGDDGVYSDHEMYRSLMLIFSAIFWDNDVSKSFKLRRDARAATQKLGALVEKHIVEMGSLFHSFKHSHSAVSDKTNGLANGGANGHANGNANGHTNGNGIHQNGGAAPSMLRSYGDLMLRRMIEAYGEGKSVKEAVYGQIMPSIAAGTANQTQIMAQCLDYYMSDDGAEHLPEMKRLASLETPEAFNTLMKYLFEGARIRNTTAVPRLVATDQTVEDNIPCLPDPKDSTFLRPIPNPQQAETTRTVKLSRGSMVLVDLTVAAHDATAFPDPEKVRLDRDLDSYTFFGLGPHRCAGDKVVRITMTAVFKVLLQLDGLRRAEGGRGVFKSLPASQWNGQAGRVAGEKPQWSGLRTYVNADESAFSQTPMNMKIRWDD
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7,8-linoleate diol synthase is a bifunctional enzyme that converts linoleic acid (18:2n-6) into 8-hydroperoxy-8(E),12(Z)-octadecadienoic acid (8-HPODE) and then catalyzes the isomerization of the resulting hydroperoxide to 7,8-dihydroxy-9(Z),12(Z)-octadecadienoic acid (7,8-DiHODE).
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G4N6Z6
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MKK2_MAGO7
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Mitogen-activated protein kinase kinae MKK2 (MAPKK MKK2) (EC 2.7.11.24) (MEK MKK2)
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MHDQEAANGGETATNPISSLDVPTPPATTIPTLSSPAPLLRPAIPGARSAGARTPRLGLAIPPSPNVKPVGGAPGRPPLPTLHLATPMGSSVTPHEQPPGRPSIVTQQGQSASGGSESSAAHSRSGSFGPLDGRTSNPTSAGSQYSALSFASHFGIGSTRPQGTPDPASAVGSIYSERSDGGAGMDKDGNLKGLENFDKLTIDKARTADVEDLDVEGWKIASMEKRIVELGGLGEGAGGAVTRCKLTGGKTVFALKVITANPDPDVKKQIMRELDFNIQCASEHICRYYGAFEDPSTATISIAMEFCEGGSLDSIYKEVKRLGGRTGEKVLGKIAEGVLRGLTYLNSKKIIHRDIKPSNILLCRNGDVKLCDFGVSGDFGTKGEANTFIGTSYYMAPERITGQSYTITSDVWSTGVTLLEVAQHRFPFPADGTEMAPRAGLIDLLTYIVRQPIPKLKDEPSAQISWSENFKYFIECCLEKDPQRRASPWRMLEHPWMVDMKSKRVNMTRYLAQVWGWDDKGEAKPAE
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Mitogen-activated protein kinase kinase part of the MCK1-MKK2-MPS1 MAP kinase (MAPK) signal transduction cascade that is essential for appressorium formation, penetration and invasive growth. Beside its role in pathogenesis, the MPS1 cascade is active in conidiation and cellular stress responses (By similarity). Targets downstream of the the MPS1-MAPK pathway include transcription factors MIG1 and SWI6, as well as GSK1 and MPG1.
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G4N7S6
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HAT1_MAGO7
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Histone acetyltransferase type B catalytic subunit (EC 2.3.1.48)
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MAESDLWSVDANSALELSLVEPTEDGLTTVTRFHPRFTYPLFGEEEQIFGYQDLKINLQYHAPDMRPNVKITHSKKFKSIGETQPTDLDALLQGYLPPVAFAKKREFEDAIRLMPADWTPPGEILSEFDGVDGAKFEIRRSNLADDASRQIIDRVQLLILLFIEGGSYIGTDTTDSLDRWDIFFLYNIKPSTTDGTSRYQFAGYSTVYKFFPLQRFPLEPKEAHENLELPSGEFPFSNLRSRTRISQFLILPPFQKSGNGSRLYRTIYDYCLRDPNVIEVTVEDPNEAFDDMRDVADLDFLRQKSEFTDLRINTDIHIPKQGAAPRGVVDEVKSEEARCLYRIAPRQFSRVLEMHLMSRLAETVRPTLVDDKVVAKPTKIETHEYDLWKLFVKQRLYRHNKEVLSQLDRHDRIERLNETLGSVELEYARILALAERRTQATSSNLKRKLDDDENTEGSSSKKARVEDA
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Catalytic component of the histone acetylase B (HAT-B) complex. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG (By similarity). Involved in DNA double-strand break repair. Required for appressorium turgor pressure, autophagy and conidial nuclear degradation. During the germination process and upon starvation conditions, translocates from the nucleus to the cytoplasm where it acetylates ATG3 at 'lys-262' and 'Lys-267', thus influencing autophagy through controlling ATG3-ATG8 interaction. Also acetylates ATG9 at 'Lys-621' to regulate ATG9 binding to vesicles, which is also important for autophagy and pathogenicity.
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G4NAP4
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MNLOX_MAGO7
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Manganese lipoxygenase (MnLOX) (EC 1.13.11.-) (EC 1.13.11.45) (EC 1.13.11.58) (Manganese 9S/11S-lipoxygenase) (9S/11S-MnLOX)
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MRVLVWIAGLAPLAVAVPSSSYRVAVAARADNTSASVAPSQNVSGAAPPELVVYTLPCEDGNSTARTAEIRLKQATLLYGPSLLGNASYFPGGPLGDAISLRDQTVWEGAAVVQSLRAFTDAAKVAANIKQNGGLNSLDDFKVLYQDGWKGSVPQGIARGQSENYTSDLLFSMERLSVNPYILKRLHPTEDALPFQVDRATVKQLTKTSLKALHAAGRLFVADHSYQRNYTRLANRYSAACTALFYLDPRSNQFLPLAIKTNVGADLTYTPLDTDNNNWLLAKIMFNNNDLFHGQIFHVAYPHAIAEIVHLAALRTMSARHPVLALMERLMYQAYAVRPLGERVLFNKGGLFEQNFAYPQDMVYKFVGDSYPTTGRWRAGYLDTDVRARGLVDADYGPELPHFPFYEDGSRLVEVIRRFVRSFVDATYHESDEMVAKDAELQAWVAEANGPAGVEDFEPGPLDTRERLVEVLTHMAWLTGCAHHVLNQGEPVTASGVLPMHPTALYAPVPTSKANTTADLLGYLPSAQKSVDQVTLLARFNRPDVVPTNQTLRYMFAAPQLLLGNGEAYRRANQRFVRAMGRISDEVKARRFDDRGLSQGMPFIWQALDPGNIPFYLSV
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Lipoxygenase that metabolizes linoleic and alpha-linolenic acids to 9S-, 11- and 13R-hydroperoxy fatty acids. At the end of lipoxygenation, the intermediate product 11S-HPODE from linoleic acid is then transformed into 9S-HPODE and 13R-HPODE as the final products. The intermediate product 11R-HPOTrE from alpha-linolenic acid is transformed into 9S-HPOTrE and 13R-HPOTrE as the final products. 9S-HPOTrE is further oxidized by the enzyme to 9S,16S-DiHPOTrE as the end product.
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