entry
stringlengths 6
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| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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A7XDQ9
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B3GTK_ARATH
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Hydroxyproline O-galactosyltransferase GALT2 (AtGALT2) (EC 2.4.1.-) (Beta-1,3-galactosyltransferase 20)
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MKRVKSESFRGVYSSRRFKLSHFLLAIAGFYLVFLAFKFPHFIEMVAMLSGDTGLDGALSDTSLDVSLSGSLRNDMLNRKLEDEDHQSGPSTTQKVSPEEKINGSKQIQPLLFRYGRISGEVMRRRNRTIHMSPFERMADEAWILGSKAWEDVDKFEVDKINESASIFEGKVESCPSQISMNGDDLNKANRIMLLPCGLAAGSSITILGTPQYAHKESVPQRSRLTRSYGMVLVSQFMVELQGLKTGDGEYPPKILHLNPRIKGDWNHRPVIEHNTCYRMQWGVAQRCDGTPSKKDADVLVDGFRRCEKWTQNDIIDMVDSKESKTTSWFKRFIGREQKPEVTWSFPFAEGKVFVLTLRAGIDGFHINVGGRHVSSFPYRPGFTIEDATGLAVTGDVDIHSIHATSLSTSHPSFSPQKAIEFSSEWKAPPLPGTPFRLFMGVLSATNHFSERMAVRKTWMQHPSIKSSDVVARFFVALNPRKEVNAMLKKEAEYFGDIVILPFMDRYELVVLKTIAICEFGVQNVTAPYIMKCDDDTFIRVESILKQIDGVSPEKSLYMGNLNLRHRPLRTGKWTVTWEEWPEAVYPPYANGPGYIISSNIAKYIVSQNSRHKLRLFKMEDVSMGLWVEQFNASMQPVEYSHSWKFCQYGCTLNYYTAHYQSPSQMMCLWDNLLKGRPQCCNFR
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Possesses hydroxyproline O-galactosyltransferase activity. Transfers galactose from UDP-galactose to hydroxyproline residues in the arabinogalactan proteins (AGPs). Is specific for AGPs containing non-contiguous peptidyl hydroxyproline residues. Utilizes UDP-galactose solely as sugar donor. The addition of galactose onto the peptidyl hydroxyproline residues in AGP core proteins represents the first committed step in arabinogalactan polysaccharide addition. AGP glycans play essential roles in both vegetative and reproductive plant growth.
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A7XGN8
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LOV1B_ARATH
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Disease susceptibility protein LOV1 (Disease resistance protein RPP8-like protein 1) (Protein LONG VEGETATIVE PHASE1)
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MAEGVVLFGVHKLWELLNRESARLNGIGEQVDGLKRQLGRLQSLLKDADAKKHESERVRNFLEDVRDIVYDAEDIIESFLLNEFRTKEKGIKKHARRLACFLVDRRKFASDIKGITKKISEVIGGMKSLGIQEIIDGASSMSLQERQREQKEIRQTFANSSESDLVGVEQSVEALAGHLVENDNIQVVSISGMGGIGKTTLARQVFHHDMVQRHFDGFAWVFVSQQFTQKHVWQRIWQELQPQNGDISHMDEHILQGKLFKLLETGRYLVVLDDVWKEEDWDRIKAVFPRKRGWKMLLTSRNEGVGIHADPKSFGFKTRILTPEESWKLCEKIVFHRRDETGTLSEVRVDEDMEAMGKEMVTCCGGLPLAVKVLGGLLATKHTVPEWKRVYDNIGPHLAGRSSLDDNLNSIYRVLSLSYEDLPMCLKHCFLYLAHFPEYYEIHVKRLFNYLAAEGIITSSDDGTTIQDKGEDYLEELARRNMITIDKNYMFLRKKHCQMHDMMREVCLSKAKEENFLEIFKVSTATSAINARSLSKSRRLSVHGGNALQSLGQTINKKVRSLLYFAFEDEFCILESTTPCFRSLPLLRVLDLSRVKFEGGKLPSSIGDLIHLRFLSLHRAWISHLPSSLRNLKLLLYLNLGFNGMVHVPNVLKEMQELRYLQLPMSMHDKTKLELSDLVNLESLMNFSTKYASVMDLLHMTKLRELSLFITDGSSDTLSSSLGQLRSLEVLHLYDRQEPRVAYHGGEIVLNCIHLKELELAIHMPRFPDQYLFHPHLSHIYLWCCSMEEDPIPILERLLHLKSVILTFGAFVGRRMVCSKGGFPQLCFLKLEELEELEEWIVEEGSMPLLRALTICNCRKLKLPGGINYITSLKELTIVGMKWKEKLVPGGEDYYKVQNIPNVQFINCDE
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Confers susceptibility to the fungus Cochliobolus victoriae by conditioning victorin-dependent (victorin is a toxin synthesized by C.victoriae) induction of defense-associated proteins.
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A7XUJ6
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TRAF6_PIG
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TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
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MSLLHCENSCGSSQSESDCCAAMAASSCGAAAKDDGVSGTASTGNLSSSFMEEIQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACIIKSIRDAGHKCPVDNEILLENQLFPDNFAKREILSLTVKCPNVGCLHKMELRHLEDHQAHCEFALMNCPQCQRPFQKCQLNIHILKECPRRQVSCVNCAVSMAFEDKEIHDQNCPLANVICEYCNTVLIREQMPNHYDLDCPTAPVPCTFSTFGCHEKMQRNHLARHLQENTQSHMRMMAQALQGLSLAVAPVPQRDMLPYDSSPLSRISSGCCSDQNFQETIQQLEGRLVRQDHQIRELTAKMETQSMYVSELKRTIRSLEDKVAEIEAQQCNGIYIWKIGNFGMHLKSQEEEKPVVIHSPGFYTGKPGYKLCMRLHLQLPTAQRCANYISLFVHTMQGEYDSHLPWPFQGTIRLTILDQSEAPIRQNHEEIMDAKPELLAFQRPTIPRNPKGFGYVTFMHLDALRQRTFIKDDTLLVRCEVSTRFDMGSLRREGFQPRSTDSGT
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E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as ECSIT, IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation. Leads to the activation of NF-kappa-B and JUN (By similarity). Seems to also play a role in dendritic cells (DCs) maturation and/or activation (By similarity). Represses c-Myb-mediated transactivation, in B-lymphocytes. Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor (By similarity). Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation. Together with MAP3K8, mediates CD40 signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production (By similarity). Participates also in the TCR signaling by ubiquitinating LAT (By similarity).
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A7XY94
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NMDE2_XENLA
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Glutamate receptor ionotropic, NMDA 2B (GluN2B) (N-methyl D-aspartate receptor subtype 2B) (NMDAR2B) (NR2B)
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MRPTEACCYLKISLIILFYMGCYAQKHPNMDIAVILVGTTEEVAIKDVHEKDDFHHLPVTPRVALVTMNESDPKSIITRICDLMSDKKVQGVVFGDDTDQEAIAQILDFISVQTLTPILGIHGGSSMIMADKEEASMFFQFGPSIEQQASVMLNIMEEYDWYIFSIVTTYFPGYQDFENKVRSTIENSFVGWELEEVIHLDMSLDDIDSKIQNQLKKLQSPVILLYCTKEEATYIFEVAHSVGLTGYGFTWIVPSLVAGDTDTVPDEFPTGLISVSYDEWDYDLPARVRDGIAIITTAASTMLSEHNSIPQSKSSCNNIQESRVYEAHMLKRYLINVTFEGRNLSFSEDGYQMHPKLVIILLNQERKWERVGKYKDRSLKMKYYVWPVFDLYPNSEEHKDEHLSIVTLEEAPFVIVEDVDPLSGTCMRNTVPCRKQIRPENRTEEGGNYIKRCCKGFCIDILKKIAKTVKFTYDLYLVTNGKHGKKINGTWNGMIGEVVTKRAYMAVGSLTINEERSEVVDFSVPFIETGISVMVSRSNGTVSPSAFLEPFSADVWVMMFVMLLIVSAVAVFVFEYFSPVGYNRCLADGREPGGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEYVDQVSGLSDKKFQRPNDFSPAFRFGTVPNGSTERNIRNNYLEMHSYMVKFNQRSVQDALLSLKSGKLDAFIYDAAVLNYMAGRDEGCKLVTIGSGKVFATTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTGICHNEKNEVMSSQLDIDNMAGVFYMLAAAMALSLITFIMEHLFFWQLRHCFMGVCSGKPGMVFSISRGIYSCIHGVAIEDRQSALDSPSATMNNTHSNILRLLRTAKNMANLSGVNGSPQSALDFIRRESSVYDISEHRRSFTHSDCKSFQPEENLFSDYISEVERTFGNLQLKDSNVYQDHFHHHRPHSIGSNSSIDGLYDCDNAPFTTQPRSLSKKPLDIGLPSKHPSPQIGDLYGKFSFKSDHYGAPDDLIRSDVSDISTHTVTYGNIEGNAKRRKQYKDSLKKRPASAKSRREFDEIELAYRRRQRSPDHKRYFRDKEGLRDFYLDQFRTKENNPHWEHVDLTHIYAERADDFKHDTSCSNRQHQKHVGEFVQTDRKHGSGGNAWEKNMSNIEWEDRASSNFCRNCPSKMHNYTGQNTNRPACIRCEVCKKAGNLYDISEDNSLQDLEARPIQAPNSKYPQSPNGKAQKRNRSKLHRQHSYDTFVDLQKEDVTLAPRSVSLKDKERFLDGSPYAHMFEMPNETSFTSKSHGPTHNPGGYMLSRSLYPDRVTQNPFIPTFGDDQCLLHGSKPYYFRQPAIGGLKGRADFRGAGKSLSAQHSGPSGHFQKDICIGNQPNACVSNNKNPRSFNNSTNGHVYEKLSSIESDV
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Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition (Probable).
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A7XYQ1
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SOBP_HUMAN
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Sine oculis-binding protein homolog (Jackson circler protein 1)
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MAEMEKEGRPPENKRSRKPAHPVKREINEEMKNFAENTMNELLGWYGYDKVELKDGEDIEFRSYPTDGESRQHISVLKENSLPKPKLPEDSVISPYNISTGYSGLATGNGLSDSPAGSKDHGSVPIIVPLIPPPFIKPPAEDDVSNVQIMCAWCQKVGIKRYSLSMGSEVKSFCSEKCFAACRRAYFKRNKARDEDGHAENFPQQHYAKETPRLAFKNNCELLVCDWCKHIRHTKEYLDFGDGERRLQFCSAKCLNQYKMDIFYKETQANLPAGLCSTLHPPMENKAEGTGVQLLTPDSWNIPLTDARRKAPSPVATAGQSQGPGPSASTTVSPSDTANCSVTKIPTPVPKSIPISETPNIPPVSVQPPASIGPPLGVPPRSPPMVMTNRGPVPLPIFMEQQIMQQIRPPFIRGPPHHASNPNSPLSNPMLPGIGPPPGGPRNLGPTSSPMHRPMLSPHIHPPSTPTMPGNPPGLLPPPPPGAPLPSLPFPPVSMMPNGPMPVPQMMNFGLPSLAPLVPPPTLLVPYPVIVPLPVPIPIPIPIPHVSDSKPPNGFSSNGENFIPNAPGDSAAAGGKPSGHSLSPRDSKQGSSKSADSPPGCSGQALSLAPTPAEHGRSEVVDLTRRAGSPPGPPGAGGQLGFPGVLQGPQDGVIDLTVGHRARLHNVIHRALHAHVKAEREPSAAERRTCGGCRDGHCSPPAAGDPGPGAPAGPEAAAACNVIVNGTRGAAAEGAKSAEPPPEQPPPPPPPAPPKKLLSPEEPAVSELESVKENNCASNCHLDGEAAKKLMGEEALAGGDKSDPNLNNPADEDHAYALRMLPKTGCVIQPVPKPAEKAAMAPCIISSPMLSAGPEDLEPPLKRRCLRIRNQNK
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Implicated in development of the cochlea.
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A7YE96
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IT70A_DANRE
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Intraflagellar transport protein 70A (Protein fleer) (Tetratricopeptide repeat protein 30A) (TPR repeat protein 30A)
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MPPMTIKDGEYTATVYKMIKEGRYGDAIHILSKEHQKHTKSRAALSLLGYCYYHMQDFTNAAECYEQLTQLHPEVEDYKLYYAQSLYGACAFPEAMKSTFLLDNTTSHTKMIKLQAAIKYGEEDYSGAKTLVEQLPQEDPDYDVDLGCLLYKEGEFEEACKKFMSSMNVLGYQPDLAYNIALCYYSLKQYASALKYIAEIIERGIREHPELSIGMTTEGIDVRSVGNTLILHETALIEAFNLKAAIEYQLKNYAAAQEALTDMPPRSEEELDPVTLHNQALMNMDTKPTEGFEKLAFLLQQNPFPPVTFGNLLLLYCKYEYFDLAADVLAENAHLTYKFLTPYLYEFLDAMITCQTAPEEAFRKFDENAGKLTEQLRKVTKQVQEARHNRDDESLKKYVQDYDEVLEKYIPVLMAQAKIYWNRENYSMVEKIFHKSLEFCNEHDTWKLNVAHVLFMQDNKYKEAIGFYEPIVKKHYENILNVSAIVLANLCVSYIMTSQNEEAEELMRKIEKEEEQISYDDPDKKIFHLCIVNLVIGTLYCAKGNYDFGISRVIKSLEPYNKKLGTDTWFYAKRCFLSLLENMAKHMIMLRDSVVQECIQFLEHCELYGKDVLAIIEQPLEEDRMHIGKNTVTYESRLIKALFYEVTGWNE
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Plays a role in anterograde intraflagellar transport (IFT), the process by which cilia precursors are transported from the base of the cilium to the site of their incorporation at the tip (By similarity). Required for polyglutamylation of axonemal tubulin, which is a prerequisite for correct assembly of cilia and for normal cilia beat amplitude. Does not seem to be required for neuronal microtubule polyglutamylation. {ECO:0000250, ECO:0000269|PubMed:17761526}.
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A7YW45
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ANM5_BOVIN
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Protein arginine N-methyltransferase 5 (PRMT5) (EC 2.1.1.320) (Histone-arginine N-methyltransferase PRMT5) (Shk1 kinase-binding protein 1 homolog) (SKB1 homolog)
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MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFTQEPAKSRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTSHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNIQVLMVLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPESLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRSYTIGL
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Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3) such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H and may regulate its transcriptional elongation properties (By similarity). May methylate the N-terminal region of MBD2 (By similarity). Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. Methylates histone H2A and H4 'Arg-3' during germ cell development (By similarity). Methylates histone H3 'Arg-8', which may repress transcription (By similarity). Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (By similarity). Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9. Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (By similarity). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (By similarity). Methylates GM130/GOLGA2, regulating Golgi ribbon formation. Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner. Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. Along with LYAR, binds the promoter of gamma-globin HBG1/HBG2 and represses its expression. Symmetrically methylates NCL. Methylates p53/TP53 methylation might possibly affect p53/TP53 target gene specificity (By similarity). Involved in spliceosome maturation and mRNA splicing in prophase I spermatocytes through the catalysis of the symmetrical arginine dimethylation of SNRPB (small nuclear ribonucleoprotein-associated protein) and the interaction with tudor domain-containing protein TDRD6 (By similarity).
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A7YWI9
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TYDP2_BOVIN
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Tyrosyl-DNA phosphodiesterase 2 (Tyr-DNA phosphodiesterase 2) (EC 3.1.4.-) (5'-tyrosyl-DNA phosphodiesterase) (5'-Tyr-DNA phosphodiesterase) (TRAF and TNF receptor-associated protein)
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MERNSGPEAGPEAELEEGEPEVKKRKLMCVEFASVASCDAAVAQCYLAENDWEMERALNSYFEPAVEESASESRPESLSEPGSCVDLTKEETNDSISSKTSTSEDKSVQQEDGSVFSFITWNIDGLDMNNLLERARGVCSYLTLYSPDVIFLQEVIPPYYAYLKKKASSYKIITGREEGYFTAIMLKKSRVKFKSQEIIPFPNTQMMRNLLCVHVSVSGNELCLMTSHLESTRGHAKERMNQFKMVLEKMQEAPGSATVIFAGDTNLRDQEVTKCGGLPNNILDVWEFLGKPKHCQYTWDTQMNSNLGIAANCKLRFDRIFFRAAAEGGHIIPQSLDLLGLEKLDCGRFPSDHWGLLCTLDVIL
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DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (TOP2) active site tyrosine residue. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DNA double-strand breaks/DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'-phosphate termini that are ready for ligation. Thereby, protects the transcription of many genes involved in neurological development and maintenance from the abortive activity of TOP2. Hydrolyzes 5'-phosphoglycolates on protruding 5' ends on DSBs due to DNA damage by radiation and free radicals. Has preference for single-stranded DNA or duplex DNA with a 4 base pair overhang as substrate. Has also 3'-tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. Constitutes the major if not only 5'-tyrosyl-DNA phosphodiesterase in cells. Also acts as an adapter by participating in the specific activation of MAP3K7/TAK1 in response to TGF-beta: associates with components of the TGF-beta receptor-TRAF6-TAK1 signaling module and promotes their ubiquitination dependent complex formation. Involved in non-canonical TGF-beta induced signaling routes. May also act as a negative regulator of ETS1 and may inhibit NF-kappa-B activation. Acts as a regulator of ribosome biogenesis following stress.
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A7YY44
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PAR1_BOVIN
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Proteinase-activated receptor 1 (PAR-1) (Thrombin receptor)
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MGPRWLLLWAAGLGLCSPLVSARTRGPRPGTDPTNGTLGPRSFFLRNSNDGYEQIPLPEDEDSSEGEFTEDRLSSGNRSSPPQKSPPGFISKSASGYLTSAWLTVFIPSVYTGVFLVSLPLNIMAVVVFVLKMKVKKPAVVYMLHLAAADVLFVCVLPFKISYYFSGSDWRFGSAMCRFVTAAFYGNMYASIMLMTAISVDRFLAVVYPIQSLSWRTLGRASFICLAIWAMAIAGVAPLLLQEQATQVPGLNITACHDVLNQTLLEGYYSYYFSAFSAVFFFVPLTLSTVSYVSIIRCLSSSTVANQNKKSRALLLSAAVFCIFILCFGPTNILLLLHYAFLSSDPMTEAAYFAYLLCVCVSSISCCIDPLIYYYASSECQRHLFAILHCKESSDPGSCNSSGQLMPSKMDTCSSNLSSSLYKKLLT
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High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis.
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A7YY55
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HACD3_BOVIN
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Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3 (EC 4.2.1.134) (3-hydroxyacyl-CoA dehydratase 3) (HACD3) (Protein-tyrosine phosphatase-like A domain-containing protein 1)
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MENQVLTPHVYWAQRHHELYLRVELSDVQNPAISITENVLHFKAQGHGAKGDNVYEFHLEFLDLVKPEPVYKLTQRQVNITVQKKESQWWERLTKQEKRPLFLAPDFDRWLDESDAEMELRAKEEEQLNKLRLESQGSPETLTSLKKGYLFMYNLVQFLGFSWIFVNMTVRFFILGKESFYDTFHTVADMMYFCQMLAAVESINAAIGVTKSPVVPSLFQLLGRNFILFIIFGTMEEMQNKAVVFFVFYIWSTVEIFRYPFYMLSCIDMDWKVLTWLRYTVWIPLYPMGCLAEAVSVIQSIPVFNETGRFSFTLPYPVKIKVRFSFFLQIYLILLFLGLYVNFRYLYKQRRRRFGQKKKKIH
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Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Involved in Rac1-signaling pathways leading to the modulation of gene expression. Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization (By similarity).
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A7Z019
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SMCA4_BOVIN
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Transcription activator BRG1 (EC 3.6.4.-) (ATP-dependent helicase SMARCA4) (BRG1-associated factor 190A) (BAF190A) (Protein brahma homolog 1) (SNF2-beta) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4)
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MSTPDPALGGTPRPGPSPGPGPSPGAMLGPSPGPSPGSAHSIMGPSPGPPSAGHPIPTQGPGGYPQDNMHQMHKPMESMHEKGMSDDPRYTQMKGMGMRSGGHAGMGPPPSPMDQHSQGYPSPLGGSEHASSPVPASGPSSGPQMSSGPGGAPLDGADPQALGQQNRGPTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQGKRPMPGMQPQMPALPPPSVSATGPGPSPGPAPPNYSRPHGMGGPNMPPPGPSGVPPGMPGQPPGGPPKPWPEGPMANAAAPTSTPQKLIPPQPTGRPSPAPPAVPPAASPVMPPQTQSPGQPAQPAPMVPLHQKQSRITPIQKPRGLDPVEILQEREYRLQARIAHRIQELENLPGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVCMRRDTALETALNAKAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAYLLQQTDEYVANLTELVRQHKAAQVAKEKKKKKKKKKAENAEGQTPAIGPDGEPLDETSQMSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPRSDSEESGSEEEEEEEEEEQPQPAQPPTLPVEEKKKIPDPDSDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMQAKGVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHLGFTGGIVQGLDLYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEQDEEEDEVPDDETVNQMIARHEEEFDLFMRMDLDRRREEARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWLKAIEEGTLEEIEEEVRQKKSSRKRKRDSDAGPSTPTTSTRSRDKDDESKKQKKRGRPPAEKLSPNPPNLTKKMKKIVDAVIKYKDSSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEKEDDSEGEESEEEEEGEEEGSESESRSVKVKIKLGRKEKAQDRLKGGRRRPSRGSRAKPVVSDDDSEEEQEEDRSGSGSEED
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Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating the calcium-dependent release of a repressor complex and the recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by SMARCA4-dependent recruitment of a phospho-RB1-HDAC repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves the release of HDAC1 and recruitment of CREBBP. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development, a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. SMARCA4/BAF190A may promote neural stem cell self-renewal/proliferation by enhancing Notch-dependent proliferative signals, while concurrently making the neural stem cell insensitive to SHH-dependent differentiating cues (By similarity). Acts as a corepressor of ZEB1 to regulate E-cadherin transcription and is required for induction of epithelial-mesenchymal transition (EMT) by ZEB1. Binds via DLX1 to enhancers located in the intergenic region between DLX5 and DLX6 and this binding is stabilized by the long non-coding RNA (lncRNA) Evf2 (By similarity). Binds to RNA in a promiscuous manner (By similarity). Binding to RNAs including lncRNA Evf2 leads to inhibition of SMARCA4 ATPase and chromatin remodeling activities (By similarity). In brown adipose tissue, involved in the regulation of thermogenic genes expression (By similarity).
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A7Z056
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UBP20_BOVIN
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Ubiquitin carboxyl-terminal hydrolase 20 (EC 3.4.19.12) (Deubiquitinating enzyme 20) (Ubiquitin thioesterase 20) (Ubiquitin-specific-processing protease 20)
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MGDSRDLCPHLDSIGEVTKEDLLLKSKSTCQSCGVSGPNLWACLQVSCSYVGCGESFADHSTLHAQAKKHNLTVNLTTFRVWCYACEKEVFLEPRLAAHPPGPAPKFSEQDSPPPSHPLKAVPIAVADEGESESEDDDLKPRGLTGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLVSEVWHRKRPSYVVPTSLSHGIKLVNPMFRGYAQQDTQEFLRCLMDQLHEELKEPVVATAAALTEARDSDSSDTDEKREGDRSPSEDEFLSCDSSSDRGEGDGQGRSGGGSQAEAELLMADEAGRAISEKERMKDRKFSWGQQRTNSEQVDEDADVDTAMAALEQQPPETQPPSPRSTSPCRTPEPDNEAHMRSSRPCSPVHHHEGHAKLASSPHRASPVRMGPAYVLKKAQVPGSRRRKEQSYRSVISDIFDGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAKLHSAIYQNVPAKPGACGDSYVAQGWLAFIVEYIRRFVVSCTPSWFWGPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKISSHVSFPLEGLDLRPFLAKECTSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEAYVLFYRKSSEEAVRERQQVVSLAAMREPSLLRFYVSREWLNKFNTFAEPGPITNHTFLCSHGGIPPNKYHYIDDLVVILPQNVWEHLYSRFGGGPAVNHLYVCSICQVEIEALAKRRRVEIDTFIKLNKAFQAEESPSVIYCISMQWFREWEAFVKGKDNEPPGPIDNSRIAQVKGSGHIQLKPGADYGQISEETWVYLNNLYGGGPEIAIRQSVAQLPDPESLHGEQKIEAETRAL
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Deubiquitinating enzyme that plays a role in many cellular processes including autophagy, cellular antiviral response or membrane protein biogenesis. Attenuates TLR4-mediated NF-kappa-B signaling by cooperating with beta-arrestin-2/ARRB2 and inhibiting TRAF6 autoubiquitination. Promotes cellular antiviral responses by deconjugating 'Lys-33' and 'Lys-48'-linked ubiquitination of STING1 leading to its stabilization. Plays an essential role in autophagy induction by regulating the ULK1 stability through deubiquitination of ULK1. Acts as a positive regulator for NF-kappa-B activation by TNF-alpha through deubiquitinating 'Lys-48'-linked polyubiquitination of SQSTM1, leading to its increased stability. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, possibly leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. Deubiquitinates MCL1, a pivotal member of the anti-apoptotic Bcl-2 protein family to regulate its stability. Within the endoplasmic reticulum, participates with USP33 in the rescue of post-translationally targeted membrane proteins that are inappropriately ubiquitinated by the cytosolic protein quality control in the cytosol.
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A7Z063
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WASH1_BOVIN
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WASH complex subunit 1 (WAS protein family homolog 1)
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MTPTGTQHSLAGQTYAVPLIQPDLRREEAIQQVADALQYLQKVSGDIFSRISQRVELSRSQLQAIGERVSLAQAKIEKIKGSKKAIKVFSSAKYPAPERLQEYGSIFMGAQDPGLQRRPRHRIQSKHRPLDERALQEKLKFFPVCVNTKPEPEDEAEEGLGGLPSNISSVSSLLLFNTTENLYKKYVFLDPLAGAVTKTHVMLGAETEEKLFDAPLSISRREQLERQVPENYFYVPDLGQVPDIDVPSYLPDLPGVADDLMYSADLGPGIAPSAPGAIPELPTFHTEVAQPFKPDLEDGVLTARPPPPPPPPPPPAPAVLMSVPPPPPPPQAPPGQPAKGDDSGGASPSAPVQGAPKEVVDPSSGRATLLESIRQAGGIGKAKLRSVKERKLEKKKQKEQEQVRATSQGGDLMSDLFNKLAMRRKGISGKGPGSGASEGPGGAFARMSDSIPPLPPPQQPPGEEDEDDWES
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Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. Involved in endocytic trafficking of EGF. Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration. In T-cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL proposed to be implicated in T-cell proliferation and effector function. In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T-cell activation. Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By similarity).
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A7Z064
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HMDH_BOVIN
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3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase) (EC 1.1.1.34)
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MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKLEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLVDLSRASALAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTADNSKVSLGLDENVSKRIEPSVSLWQFYLSKMISMDIEQVITLSLALLLAVKYIFFEQAETESTLSLKNPITSPVVTQKKITDDCCRRDPVLVRNDQKFHAMEEETRKNRERKVEVIKPLLAENDTSHRATFVVGNSSLLGTSLELETQEPEMELPVEPRPNEECLQILENAEKGAKFLSDAEIIQLVNAKHIPAYKLETLMETHERGVSIRRQLLSKKLPEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDGKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRFPRACDSAEVKAWLETPEGFTVIKEAFDSTSRFARLQKLHMSVAGRNLYIRFQSRSGDAMGMNMISKGTEKALSKLQEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACRDNPGENARQLARIVCGTVMAGELSLMAALAAGHLVRSHMIHNRSKINLQDLQGTCTKKAA
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Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis.
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A7ZN88
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HCHA_ECO24
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Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
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MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDIAGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG
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Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}.
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A7ZU51
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FADB_ECO24
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLQFANSVFNRLEDLPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVKAEKLVEGAKAVLRQAINGDLDWKAKRQPKLEPLKLSKIEATMSFTIAKGMVAQTAGKHYPAPITAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQYVKGKAKKLTKDVETPKQAAVLGAGIMGGGIAYQSAWKGVPVVMKDINDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDVVVEAVVENPKVKKAVLAETEQKVRPDTVLASNTSTIPISELANALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKEDSKGKPKKEEDAVVDDLLAEVSQPKRDFSEEEIIARMMIPMVNEVVRCLEESIIATPAEADMALIYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQHLGPLYEVPEGLRNKARHNEPYYPPVEPARPVGDLKTA
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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A8A1G6
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HCHA_ECOHS
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Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
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MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG
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Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}.
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A8ACZ4
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FADB_CITK8
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGQALDVLEKQTDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTLSAINGYALGGGCECVLATDYRLVTPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDIGAEQALKIGLVDGVVKPEKLLDGAIAVLRQAIDGSLDWKAKRQPKLEPLKLSKIEAAMSFTIAKGMVAQTAGKHYPAPMIAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQFVKGKAKKLTKDVETPKQAAVLGAGIMGGGIAYQSAWKGVPVIMKDINDKSLTLGMTEAAKLLNKQLERGRIDGLKLAGVISTIHPTLNYAGFDRVDVVVEAVVENPKVKKAVLAETEDNVRPDTVLASNTSTIPISELASALKRPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKVDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDASRYGQKNGLGFWRYKEDSKGKPKKEEDAAVDSLLAEVSQPKRDFSDEEIIARMMIPMVNEVVRCLEEGIIASPAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQHLGPLYEVPEGLRNKARHNEPYYPPVEPARPVGDLKTA
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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A8AWU7
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HSA_STRGC
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Streptococcal hemagglutinin (Hs antigen) (Sialic acid-binding adhesin)
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MFFKRQKGQYHEVERVTRFKLIKSGKHWLRAATSQFGLLRLMKGADISSVEVKVAEEQSVEKGGLNYLKGIIATGAVLGGAVVTSSSVYAEEEQALEKVIDTRDVLATRGEAVLSEEAATTLSSEGANPVESLSDTLSASESASANSVSTSISISESFSVSASASLSSSSSLSQSSSESASASESLSVSASTSQSFSSTTSSTQSSNNESLISSDSSNSLNTNQSVSARNQNARVRTRRAVAANDTEAPQVKSGDYVVYRGESFEYYAEITDNSGQVNRVVIRNVEGGANSTYLSPNWVKYSTENLGRPGNATVQNPLRTRIFGEVPLNEIVNEKSYYTRYIVAWDPSGNATQMVDNANRNGLERFVLTVKSQNEKYDPADPSVTYVNNLSNLSTSEREAVAAAVRAANPNIPPTAKITVSQNGTVTITYPDKSTDTIPANRVVKDLQISKSNSASQSSSVSASQSASTSVSASISASMSASVSVSTSASTSASVSASESASTSASVSASESASTSASVSASKSSSTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESSSTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASTSASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASTSASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASISASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESSSTSASVSASESASTSSSVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASMSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESAYTSASASASESASTSASISASESASTSASVSASESAYTSASVSASESGSTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESSSTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSTSESASTSASVSASESASTSASVSASESASTSASVSASESSSTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSVSVSASESASTSASVSASESASSSASVSASKSASMSASVLASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESVSANESASTSASVSASTSASTSASVSSSESASTSASVSASESASTSASVSASESASTSASVSASESASISASISASESSSTSASVSASESASTSASVSASTSTSTSASVSASESASTSASVFASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASISASESASTSASISASESSSTSASVSASTSASTSASVSASESTSTSVSISASESVSISTSVSQSMSVSESLSLSVSTSTLHSQLNGIYESELNSLSLSESLSMSQSLSQSLSDSQSTSATQSMHDRISKGQLPRTGESESKASILALGIGALGLAFKKRKKNESED
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A cell wall protein involved with PadA in host cell interactions required for colonization and pathogensis (Probable). Mediates hemagglutination and adherence to ghst glycoproteins. Recognizes fetuin-A (AHSG), a highly glycosylated human plasma protein, also involved in recognition of human platelets, probably via platelet glycoprotein Ib alpha (GP1BA). Acts in concert with PadA to promote binding to glycosylated human fibronectin (FN1) and vitronectin (VTN), and biofilm formation. Plays a major role in fibronectin and vitronectin binding binding is mediated by glycosylated regions. Probably mediates interaction of PadA with resting platelets.
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A8AZP4
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PADA_STRGC
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Platelet adherence protein A (Adhesin PadA)
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MKDFLKKVLILFTVLLMSMPSSVLNLGTSVVRADDPLNIETRRIDEHTTITQNGCYRKIEKTDATDWTVPRKPIDLVILQDASGSFRTTIPSVKNALKRLTTYVSPEQYDENDPHLVKTDDPRTTDRVFVASYQGLDQVRYFENNDFSGNPANVYTDANSTGKNYTYGNSGLTSDQNKVHNFIDNIAVDGGTPTVPAIDDTIAQYNRVKGNMENGRKTVFLLVTDGVANGYRLPGTNTVVMDKSWTRTDAIQKAWRVDSYPEAAQDIIGRANELKAAGNQLKAAVGSEGSVVVGFWERVDNFTEKYYQYGPAYLNGFGNTINIGDNRSVQAIFHDALQSMASPDKVVNGKNVSFYVNEQNNIDVFSQKILESVAAALVKDDITGEFDITEGYKVDAIRINGKKIVPKVTDPSKEIRGTITQTGNKVKISVPDSVFNPGKNSFDYDLSKEARAPETDEDSEVDPPENYVPEKEEITVPELTGKFKAGDFETRQIGGRNQTVEVQKLEYCYPSATKTVKDADASNDIGVIPDPLELTKKPSYSAQLSKKDEEFTYTVDYNFNNVPYEFEKNVMLTDPIDYRLEVVSHSAQGPDGQSWPTRVVTQQDAGGNSQSVVVADVPPQGKDYNYLIMKKAKLKMTVRLKEEYRKNQASKAYLAILQNNNGYGLVNQGNIMWNGEDDSPNQDAHAKTKDKASTIRRSNPIYVKPPLDTEVDKKVNEKEHEGLQADGEEFEYKVTAPWPGIADKFTLTDTVVDELEIVPNSAKVTVAGKSYNALTKAISINGQTIDITLDKAQLTSLNRLISRRGGSEVQEIELIFKAKIRPGADLSKYKKNGAVNIPNTADVILNDKKKTSKEVTVTPPKPKEPTVSKKINNTLDSLVTFDGQPYTYNITTAVPSDVAGYKKFVISDKLDADLEFDGQASISGPLADVFEIQTNGQTVTATVKEGKFKELAKYSFVELTIPAKVKAGVTGKTIENKAKISFTNENNVAKEVESNPVTVTPPPVTKKINENLDHLDIATGQPYKYNVKTTLPSDITSYKEFVITDTLEDELSVINEGTDKPVISGPAAEFFDVTVSGQKVTATMKNFAGASALAGQEIELVIPAKINDGVTRSNIPNKATFSFKDKNDHKGEKETIPVTVTPPTEPNVSKKINGDQDNATIAAETDFTYNIKTTLPNDIDTYKSFAITDTLDENLGVVNPEPSISEEAKKFFDITVSGNTVTATMKDFAKASALANKEIELVIHAKVKKESVLPEIPNTAKITYTNKNNESKEKETEPVKVTPPPITKKVNGKDQEDLASLTSTFKYTVDSKVPIVADKFVLSDTLEEVLTFDGDATVTIDGQTVTDVTVAKKDQKLTVTFDKDQVKKYAGKAVQVAFDAKIKSGYTVDQLVAKYPNGDKAAIPNKASFVVNDNPETEKFSNPVTVTPPPPNTPEIEKKVNGADSYNLQTRLEEFTYSLNTAMPTNATEFTVTDELKSVLEFAGKKGDVQVKIDGKAANDQATISTDKNTLTVAFAEKAVKANAGKSIEVTFKAKIREGANLLDYLVPGQGIRIPNKASYDIDHNPKFHKDSNEVPVTPPSPEQPPIEKDVNDKAEATLEARDEEFTYHVKTKIPYEATAFNITDTLKEVLDFSGEKGQAEATVDGKKLSDDHIAINGQTITVTLNQEELKANADKEIKLTFKAKIRPNANLAAYVVGDKVVINNQASYNVDLPDNPGVHKDSNIVPVTPPSPEKPEIEKTVNDAKEATLANRDEIFTYKVKTKVPFDATAFSIDDTIKDVLEFADAGSATLNGEALEADRISIADQKITLTLTEDQVKNNGGKEVVLTFKAKIRQGANLSGYIEKGKTVINNQASYNAAFPNDPNFHKDSNIVPVTPPNPENPPIEKKVNEAESANLGARDEEFTYTIDTTVPLDVTGFAVYDTIEKVLEFSGENGQASATVDGQPLDASHITIKGQKITVKLTEDEAKALGGKAVHVSFKAKIKAGANLSDYIEKDGTTRIYNTAKYNFNNDPGTEQSSKPVPVIPPTPTEPELKKEVNGKEAETLANRDDVFTYTVKTTVPQDATAFSISDSLVPVLEFAGEDAEASLTLNGEKLDAKQIKLKDQTISAELTEAQVKANGGKEVVLNFKAKIREGANLADYIEADGVTRVPNKASYVANFPHRPKVEKDSNIVPVTPPSPENPPVEKKVNNKPSATLDSRDEEFTYTIDTKVPVDATGFKITDELKDVLEFSGKKGQAEVTVDGDKDVIEDSQITVDKQVLTVTLTKDQVKKYGNKAVHVSFKAKIRKNVSLAGYIEADGVTRIPNIAKYIINDDPKTEKSTEPVPVIPPSPEEPGIKKEVNGQPEATLKERYEEFTYKVTTSVPQDATAFSVSDTLVPVLEFSGEKGQATATLDGQEIDANRINVADQTISMALTEDEVKANGGKEVTLTFKAKIREGANLSAYIEKGKTSIPNTASYTAGFPNRPEIHKDSNRVPVTPPTPEEPEIKKDVNGKEEETLANRNDEFTYHINTKVPFDATAFSINDELKDVLEFADGTGRATASLNGQALDADRISINGQTITVNLTEEQVKNNGGKDVNLTFTAKIRQGVNLSGYIKDGKTSIPNKASYRVDFPNNPGVTKDSNEVPVTPPSPENPPIEKKVNEAESANLGARDEEFTYTIDTTVPLDVTGFAVYDTIEKVLEFSGENGQASATVDGQPLDASHITIKGQKITVKLTEDEAKALGGKAVHVSFKAKIKAGANLSDYIEKDGTTRIYNTAKYNFNNDPGTEQSSKPVPVIPPTPTEPELKKEVNGKEAETLANRDDVFTYTVKTTVPQDATAFSISDKLEDVLEFAGESSATLAGEDLKADQITTDGQIIKLTLTEDQVKANGGKEVVLNFKAKIREGANLSAYMKADKAEVPNKASYTVGFPNKPAVTKDSNEVPVTPPSPEQPPIEKDVNSKPSETIADRTEEFTYNIHTTMPQDATGFTVTDELKDVLEFAGDVQVTLGGKKADAAVAKNGQTLEVTFPEETVKANGGKKVQVTFKAKIKADADLTPYETANSYSVPNTASYLINNNPTSKKETKPVTVEVPKQPGPEVTKKINRTLDHLDVDRDVPYMYNVNTQIPKDIRLYKEFTVTDTLEPVLEITGTPVAYVDGYATDAVETKVEGNTVTVTVKDFARISGYKEIQLYIPAKLKADSDLSAYENQTVPNKATIAFKDSNGKNGTKESNPVTVRPRDPEKPEEPKPNEPAKTVGPADGSNPSTAYRLKELKEGFRFDVTAKVPTDPVDESGNPIKDAQGRDVKTELNSFTVTDELEKVLKVDRVAVKVEENKVAEAIAKITAKIEKAESDLKELEGKETNGTFAKKLAEAEKKVEELTAQLAAAKEKAAAAPATPAPASDSDAGNATATPAPADNNAEVAALEESLKAAQAELEQLKADGAKAGNLATPEEQKVEQDKLNKNLEQLKESKEKLEKALEAFTTVNDKGEITDEALAKIAKVTVEGQKVTVEVTDKAVLEALKGSTFRVIIYSSIKDGADLSSYLNKENNETKIPNKATVTFNDKPKVTNTVNVYPPEPTTPPQTPPHTPPTTPGTPPPTTPDTPPAPKGDLPPAPTPEPEKPKNILPKTGTSATMVNEVIIGMILVLMGLLLRRKPKH
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A cell wall protein involved with Hsa in host cell interactions required for colonization and pathogenesis. Involved in recognition of platelets. Interacts with human platelet integrin receptor GPIIbIIIa (a complex of ITGA2B and ITGB3). Involved in platelet spreading, presumably by activation of outside-in signaling leading to platelet activation and then spreading. Spreading also involves GPIIbIIIa. Binding to platelets under static conditions causes platelet dense granules to secrete ADP (similar to release induced by fibrinogen binding), has no effect on platelet alpha granule release. The N-terminal 656 aa residue fragment (called F2) also binds platelets, causes dense granule secretion and allows platelet spreading. Acts in concert with Hsa to promote binding to human fibronectin (FN1) and vitronectin (VTN), and biofilm formation. F2 bind activated platelets more strongly than unactivated platelets. Binding to both FN1 and VTN is mediated at least in part by their glycosylation.
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A8B2U2
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ALF_GIAIC
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Fructose-bisphosphate aldolase (Glfba) (glFBPA) (EC 4.1.2.13) (Fructose-1,6-bisphosphate aldolase)
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MPLCTLRQMLGEARKHKYGVGAFNVNNMEQIQGIMKAVVQLKSPVILQCSRGALKYSDMIYLKKLCEAALEKHPDIPICIHLDHGDTLESVKMAIDLGFSSVMIDASHHPFDENVRITKEVVAYAHARGVSVEAELGTLGGIEEDVQNTVQLTEPQDAKKFVELTGVDALAVAIGTSHGAYKFKSESDIRLAIDRVKTISDLTGIPLVMHGSSSVPKDVKDMINKYGGKMPDAVGVPIESIVHAIGEGVCKINVDSDSRMAMTGAIRKVFVEHPEKFDPRDYLGPGRDAITEMLIPKIKAFGSAGHAGDYKVVSLEEAKAWYK
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Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. Does not cleave D-tagatose-1,6-bisphosphate.
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A8C927
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NPMA_ECOLX
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16S rRNA (adenine(1408)-N(1))-methyltransferase (EC 2.1.1.180) (16S rRNA m1A1408 methyltransferase)
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MLILKGTKTVDLSKDELTEIIGQFDRVHIDLGTGDGRNIYKLAINDQNTFYIGIDPVKENLFDISKKIIKKPSKGGLSNVVFVIAAAESLPFELKNIADSISILFPWGTLLEYVIKPNRDILSNVADLAKKEAHFEFVTTYSDSYEEAEIKKRGLPLLSKAYFLSEQYKAELSNSGFRIDDVKELDNEYVKQFNSLWAKRLAFGRKRSFFRVSGHVSKH
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Specifically methylates the N(1) position of adenine 1408 in 16S rRNA. Confers resistance to various aminoglycosides, including kanamycin, neomycin, apramycin, ribostamycin and gentamicin. Methylates only fully assembled 30S subunits.
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A8C984
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MYLK3_DANRE
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Myosin light chain kinase 3 (EC 2.7.11.18) (Cardiac-MyBP-C-associated Ca/CaM kinase) (Cardiac-MLCK)
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MGTSLYRSTLLSTGGFSVSDYIRKFTKNKPDVNNIQPNVGFCHQSTQTSQQVKEVISAELELQQPEVTLPNDPSSQHSPEAHTGASEPLKPVSAGESSKALQKAKEISVKSSEPTHVQTFAPAVHLEQIDVHNVPKQETNSLVAAPADAKCVIETMTKVEKDIALQQERALERADDSHVANKVFLKSIIPGQQLEKIEDPQQQAEVSLFVDEDSLEKSVPGQHLDKKMEVLQKQAKDLPVVDEDSLNLSAPGQRQLEEKVDVPEKAEKKIDEAHKKMEEVPRKDELCIEKPVIRHAGIKTQHEETMGMETTVPKHDESKCPTETYVEKTENKNADVTLESDKIMICAVSPQNTSLDEDEKSKAAPLRKVESTLLIIDDSPPLPAPFDHRIVSAKQVPINSYYAVNPVEVLGGGRFGQVHKCAELSSGLTLAAKIIKVRGMKERDEVKNEIGVMNQLNHVNLIQLYDAFESRTNLTLIMEYVEGGELFERIIDESYQLTELDAIVFTRQICEGVQYLHQQYILHLDLKPENILCVNSTGNQIKIIDFGLARKYRPREKLKVNFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFMGDNDAETMNNILHAKWEFDTEAFENVSEEAKDFISSLLVSAKCSRLSASGCMKHSWLNNLEDKAKMYKVRLKSQMMLQRYLVAHRQWKKHFYAVAAANRLKRFQQSRSISTPN
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Kinase that phosphorylates MYL2 in vitro (By similarity). Increases cardiomyocyte contractility (By similarity). Required for sarcomere formation in the developing heart. {ECO:0000250, ECO:0000269|PubMed:17885681}.
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A8CG34
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P121C_HUMAN
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Nuclear envelope pore membrane protein POM 121C (Nuclear pore membrane protein 121-2) (POM121-2) (Pore membrane protein of 121 kDa C)
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MSPAAAAAGAGERRRPIASVRDGRGRGCGGPAGAALLGLSLVGLLLYLVPAAAALAWLAVGTTAAWWGLSREPRGSRPLSSFVQKARHRRTLFASPPAKSTANGNLLEPRTLLEGPDPAELLLMGSYLGKPGPPQPAPAPEGQDLRNRPGRRPPARPAPRSTPPSQPTHRVHHFYPSLPTPLLRPSGRPSPRDRGTLPDRFVITPRRRYPIHQTQYSCPGVLPTVCWNGYHKKAVLSPRNSRMVCSPVTVRIAPPDRRFSRSAIPEQIISSTLSSPSSNAPDPCAKETVLSALKEKKKKRTVEEEDQIFLDGQENKRRRHDSSGSGHSAFEPLVASGVPASFVPKPGSLKRGLNSQSSDDHLNKRSRSSSMSSLTGAYTSGIPSSSRNAITSSYSSTRGISQLWKRNGPSSSPFSSPASSRSQTPERPAKKIREEELCHHSSSSTPLAADKESQGEKAADTTPRKKQNSNSQSTPGSSGQRKRKVQLLPSRRGEQLTLPPPPQLGYSITAEDLDLEKKASLQWFNQALEDKSDAASNSVTETPPTTQPSFTFTLPAAATASPPTSLLAPSTNPLLESLKKMQTPPSLPPCPESAGAATTEALSPPKTPSLLPPLGLSQSGPPGLLPSPSFDSKPPTTLLGLIPAPSMVPATDTKAPPTLQAETATKPQATSAPSPAPKQSFLFGTQNTSPSSPAAPAASSASPMFKPIFTAPPKSEKEGLTPPGPSVSATAPSSSSLPTTTSTTAPTFQPVFSSMGPPASVPLPAPFFKQTTTPATAPTTTAPLFTGLASATSAVAPITSASPSTDSASKPAFGFGINSVSSSSVSTTTSTATAASQPFLFGAPQASAASFTPAMGSIFQFGKPPALPTTTTVTTFSQSLPTAVPTATSSSAADFSGFGSTLATSAPATSSQPTLTFSNTSTPTFNIPFGSSAKSPLPSYPGANPQPAFGAAEGQPPGAAKPALTPSFGSSFTFGNSAAPAPATAPTPAPASTIKIVPAHVPTPIQPTFGGATHSAFGLKATASAFGAPASSQPAFGGSTAVFSFGAATSSGFGATTQTASSGSSSSVFGSTTPSPFTFGGSAAPAGSGSFGINVATPGSSATTGAFSFGAGQSGSTATSTPFTGGLGQNALGTTGQSTPFAFNVGSTTESKPVFGGTATPTFGQNTPAPGVGTSGSSLSFGASSAPAQGFVGVGPFGSAAPSFSIGAGSKTPGARQRLQARRQHTRKK
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Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL).
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A8CG86
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PA2A1_DABRR
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Acidic phospholipase A2 Drk-a1 (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (Phospholipase A2 Drk-a1') (Phospholipase A2-I)
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MRTLWIVAVCLIGVEGNLFQFAEMIVKMTGKEAVHSYAIYGCYCGWGGQGKPQDATDRCCFVHDCCYGTVNDCNPKMATYSYSFENGDIVCGDNNLCLKTVCECDRAAAICLGQNVNTYDKNYENYAISHCTEESEQC
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Snake venom phospholipase A2 (PLA2) that exhibits high hydrolytic activities and shows strong preference for the anionic micelles (dPPC with deoxycholate) to the zwitterionic micelles (dPPC with Triton X-100). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
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A8CL69
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PBAN_APIME
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PBAN-type neuropeptides (Pheromone/pyrokinin biosynthesis-activating neuropeptide) [Cleaved into: TSQDITSGMWFGPRL-amide (Pyrokinin-1); QITQFTPRL-amide (Pyrokinin-2); IYLPLFASRL-amide; VPWTPSPRL-amide]
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MIGFAVFSSFNRFTTIFVCVLLCVVYLLSYASGEYDGRDSSSGSNNDRAPSNEFGSCTDGKCIKRTSQDITSGMWFGPRLGRRRRADRKPEINSDIEAFANAFEEPHWAIVTIPETEKRQITQFTPRLGRESGEDYFSYGFPKDQEELYTEEQIYLPLFASRLGRRVPWTPSPRLGRQLHNIVDKPRQNFNDPRF
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A hormone that controls sex pheromone production in females and pheromone responsiveness in male. Also mediates visceral muscle contractile activity (myotropic activity) (By similarity).
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A8CVX7
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TTLL6_DANRE
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Tubulin polyglutamylase ttll6 (EC 6.3.2.-) (Protein polyglutamylase TTLL6) (Tubulin tyrosine ligase-like family member 6)
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MGTPAERSVSEVCRCEPDPGLEGEGWGSDTHAEPSNTPIPLPVANKKKKRKKKLWINLTNCKYESVRRAARRYGIREAAEGEDWTLYWTDCSVSLDRVMDMKRYQKINHFPGMNEICRKDLLARNMNRMLKLFPKEYNIFPRTWCLPADYSDFQAYTRAKKHKTFICKPDSGCQGRGIYLTKSSKDIRPGEHMICQVYMSKPFIIDGFKFDLRIYVLVTSCDPFRVFMYDEGLVRFCTTHYTEPTVSNLEDVCMHLTNYAINKHSENFVRDEDTGSKRKLSSFKKHMEDMSYDTEKLWTDIEDAIIKTLISAHPILKHNYQTCFPNHASGSACFEILGFDVLLDRRLKPWLLEVNHSPSFTTDSRLDREVKDSLLYDTLVLINLGACDRRKITEEEKRRVKERLQQNRSREARNEEPRQSQAASMELMQKYEAKHMGGFRRIFPRDGGEKYEKYFQHSSSLFQETAASKAREECARQQLQELRLKQEQKERDKKGSRKQDLQGESAGEKVKPRKSQPPHKTSNSLPAMLELSSVREETPVSLERIEKEEAERVRELQQRETLLLNMGVVNQVRQLLQSANRLTQCINHSHEQASFPPHCRHDHKLDTLAEISWRQKNIYSTMQHQILARNRPSLPNVHSQTLQNRKPWPSLEHGLLQPVQTQAAALKHYGLEEMVASNAEEQANLIKATSAQQIPLTINGSFIWRQGSLSSSLAESRARATMLAMPPLGPGRLHRPTIFHDPNSLSIISTPAPLVPRPHLSHDLRKAPRRVLPHEHSL
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Polyglutamylase which modifies both tubulin and non-tubulin proteins, generating alpha-linked polyglutamate side chains on the gamma-carboxyl group of specific glutamate residues of target proteins (By similarity). Preferentially mediates ATP-dependent long polyglutamate chain elongation over the initiation step of the polyglutamylation reaction (By similarity). Preferentially modifies the alpha-tubulin tail over a beta-tail (By similarity). Mediates microtubule polyglutamylation in cilia axoneme, which is important for ciliary structural formation and motility. Polyglutamylates olfactory cilia, necessary for the regulation of ciliary sructure and beating.
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A8D8P8
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SIWI_BOMMO
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Piwi-like protein Siwi (EC 3.1.26.-)
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MSEPRGRGRARGRAGRGGDGGGPAPRRPGEQAGPSQQSMPPGPRPQPPSGWGPQSSVPPVRAGVPTPTAQAGRASHRVTPTTHEHPGDIDVQQRMQKLELGPHSSGGGDASSVVGRGSRRGGGRVLPETISILRTRPEAVTSKKGTSGTPLDLLANYFTVETTPKWGLYQYHVDISPEEDSTGVRKALMRVHSKTLGGYLFDGTVLYTVNRLHPDPMELYSDRKTDNERMRILIKLTCEVSPGDYHYIQIFNIIIRKCFNLLKLQLMGRDYFDPEAKIDIPEFKLQIWPGYKTTINQYEDRLLLVTEIAHKVLRMDTVLQMLSEYAATKGNNYKKIFLEDVVGKIVMTDYNKRTYRVDDVAWNVSPKSTFKMRDENITYIEYYYKKYNLRIQDPGQPLLISRSKPREIRAGLPELIYLVPELCRQTGLSDEMRANFKLMRSLDVHTKIGPDKRIEKLNNFNRRFTSTPEVVEELATWSLKLSKELVKIKGRQLPPENIIQANNVKYPAGDTTEGWTRDMRSKHLLAIAQLNSWVVITPERQRRDTESFIDLIIKTGGGVGFRMRSPDLVVIRHDGPIEYANMCEEVIARKNPALILCVLARNYADRYEAIKKKCTVDRAVPTQVVCARNMSSKSAMSIATKVAIQINCKLGGSPWTVDIPLPSLMVVGYDVCHDTRSKEKSFGAFVATLDKQMTQYYSIVNAHTSGEELSSHMGFNIASAVKKFREKNGTYPARIFIYRDGVGDGQIPYVHSHEVAEIKKKLAEIYAGVEIKLAFIIVSKRINTRIFVQRGRSGENPRPGTVIDDVVTLPERYDFYLVSQNVREGTIAPTSYNVIEDTTGLNPDRIQRLTYKLTHLYFNCSSQVRVPSVCQYAHKLAFLAANSLHNQPHYSLNETLYFL
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Endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Plays an essential role in meiotic differentiation of spermatocytes, germ cell differentiation and in self-renewal of spermatogonial stem cells. Its presence in oocytes suggests that it may participate in similar functions during oogenesis in females. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. Recognizes piRNAs containing a phosphate at the 5'-end and a 2'-O-methylation modification at the 3'-end. Strongly prefers a uridine in the first position of their guide (g1U preference, also named 1U-bias) and a complementary adenosine in the target (t1A bias). Plays a key role in the piRNA amplification loop, also named ping-pong amplification cycle: antisense piRNA-bound Siwi and sense piRNA-bound Ago3 reciprocally cleave complementary transcripts, to couple the amplification of piRNAs with the repression of transposable elements. In this process Siwi acts as a 'slicer-competent' piRNA endoribonuclease that cleaves primary piRNAs, which are then loaded onto Ago3. In this process, Siwi requires the RNA unwinding activity of the RNA helicase Vasa for the release of the cleavage products.
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A8DS38
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ERVC2_TABDI
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Ervatamin-C (EC 3.4.22.-)
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MSTLFIISILLFLASFSYAMDISTIEYKYDKSSAWRTDEEVKEIYELWLAKHDKVYSGLVEYEKRFEIFKDNLKFIDEHNSENHTYKMGLTPYTDLTNEEFQAIYLGTRSDTIHRLKRTINISERYAYEAGDNLPEQIDWRKKGAVTPVKNQGKCGSCWAFSTVSTVESINQIRTGNLISLSEQQLVDCNKKNHGCKGGAFVYAYQYIIDNGGIDTEANYPYKAVQGPCRAAKKVVRIDGYKGVPHCNENALKKAVASQPSVVAIDASSKQFQHYKSGIFSGPCGTKLNHGVVIVGYWKDYWIVRNSWGRYWGEQGYIRMKRVGGCGLCGIARLPYYPTKAAGDENSKLETPELLQWSEEAFPLA
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Cysteine proteinase. Hydrolyzes denatured natural substrates such as casein, hemoglobin, azoalbumin and azocasein with a high specific activity (By similarity). Has little or no activity against synthetic substrates (By similarity).
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A8DYE2
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TRPCG_DROME
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Transient receptor potential cation channel trpm (Transient receptor potential cation channel, subfamily M ortholog)
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MVVTDSPLAPHKYVRRISKDFSTVRRYSNTPAVVVGSFRASTSAFIAAESAAHLPTCSSPTTRTPVSTPRGIRRRQRMRKRSSVSSTLSKVLILNVRDLLKAHAGSEPLKEHQPRSWIETNFQKRECIKFIPCPKDDTKCCCGQAQITHQTIPGIESGSPGDLWLPTKHTRPQPTDAYGTIEFQGGAHPTKAQYVRLSFDTRPELLVQLFTKEWNLELPKLLITVQGGKANFDLQAKLKKEIRKGLLKAAKTTGAWIFTGGTNTGVTKQVGDALLLEGQQRTGRVVSIGIAPWGIVERNHELLGHNREVPCHSISSPRSKLAVLNNRHAYFLLVDNGTQAKYGAELILRRKLEKFISNLKLHPFTHSSTPVVCLVIEGGTNTIRAVLEYVTDSPPVPVVVCDGSGRAADLLAFVHKYASDGEEQPVLESMRDYLIGTIQKTFEVGLDQSEKLYQELLQCTRNKNLITVFRIQEKPEGEAQELDQTILTALFKSQHLSPPEQLSLALTWNRVDIARSEIFVYGQEWPNGALDEAMMQALEHDRIDFVKLLLENGVSMKKFLTIPRLEELYNTKHGPANTLGYILRDVRPHIPKGYIYTLHDIGLVINKLMGGAYRSYYTRRKFRPIYAKVMNSYANACRKSSTYQYQRYAGANSLSLVTGLLPFTSEMALFEFPFNELLIWAVLTKRQQMALLMWTHGEEALAKSLVSCKLYKAMAHEAAEDDLDTEIYEELRSYAKEFESKGNKLLDFSYRQDAEKAQRLLTCELHSWSNQSCLSLAVAANHRALLAHPCSQVILADLWMGGLRTRKNTNFKVILGLAMPFYIRQLDFKSKEELQQMPQTEEEHLENQNLDNDDSDRSQPDAEALLADTYSVRDTKVHENGKVSLTDSDTAQFREFFNLSEYNEVKQHQPLRLKKKFYEFYTAPITKFWADSIAYMFFLIMFSFTVLVKMEQMPRWQEWYSIAYITTLGFEKVREIISSEPVAITHKFSVWAWNMWNPCDGAAIILFVIGLAFRFRENTMDIGRVIYCVDSIYWYLRILNILGVNKYLGPLVTMMGKMVKNMIYFVVLLAVVLMSFGVSRQAILYPNKQPTWSLIKEVTFQPYFMLYGEVFAGDIDPPCGEDPSQPGCVTGHWVTPITMSMYLLIANILLINLLIAVFNNIFNEVNSVSHQVWMFQRFTVVMEYQQKPVLPPPFIALCHFYSLLKYCVRKAKGLEVQRDNGLKLFLEKDDLERLYDFEEECVEGFFHEQEIILNQSTDERVKNTTERVETMSQKIEDINQKENIQTATVQNIEFRLRKMEESSEQILSHLAVIHRFMSTHTAGADDLRGSTINIPGEMQRMRTISISDTEGGSGPGGNGGGGGGGGAIVPLGLGAGLNLNSLQVTTRRRFNRSLTEVRPDAYIFDEGTHFEVVPLPEEPDEVVKSREALNEQVVRKASMQSEADSDIYIPVSQRPSTCETVKRTPYVTVRQDTGASTESKDTLTPMGNNDDDQTLVGGDNSDDATPDINFEAARHRALRQRTVSLCRRNSETYSLTGADINRSHISLNQLASLSRRQMSLTQSEPDSDKDAPIAQGSAHPGKSVLHAKPSRNILLKLHSEYTSITDELESVCHMIASPTVSLPSNKASLDRPKTEMSRAEAAALLEKKHLKECEENDYMILEGLIESRGSIDASAQGFEIGVSIDYSHRYPLRRETAVELSPSKPSVDGDLMGGGEGGGAGGGDSSDTSGAGSCGAMVGISSGFQLKNERPWQRNSSMEQQTYPSPLVPTRATSDFLNPPYEGRLFKKSSESLQKNSSTETDYSAHPYRFIKQSSNETNTSLTGSYNVDTPSLTAEPSLDAGDSHSATGISISVGAVGGTATARYQPIRTASVGAADGRRLREESSSSLDLSSSGPVTMQAAPAPPVRPMLLKKQFSVDQGKPSQTAAEAVPQTPEAAQAGQAKLISTLKPQPFASKLGMNVLKESSSSTDESVGSSAKSSNPALSIPQISTHLVQDEIAKLSSNIKSSTESEKDPPFNETMC
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Calcium channel mediating constitutive calcium ion entry.
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A8DYP0
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OBSCN_DROME
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Obscurin (Inactive serine/threonine-protein kinase obscurin) (Muscle M-line assembly protein Unc-89)
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MDAVADIVFVSRDYQAQSLATDEISVSRGDLVELISSKASEKSRCFVRMFDSGDSPKEGWVPIDILEFNPTMSSSNGKESGDAEFRKLTILRELVETEEEFSRDLLHVVEKYIKGIDKPVVPRSVRDNKDIIFCNFLQIAEFHNNVLKEGLKCYSNQPNMVAKTFLRLERDFDKHVVYCQNEPLAQDYLGSSPDAKKYFQELSKQLGDDKSLAEHLKLPIQRINDYQLLFKDFIKYSLSLKENVKDLERALELMLSVPSRAYDNRFLSSIEGCRGNIYKLGRLLLHAWCNVVDKEGKAHDRYCFLFKSRILVTKVRKISENRSVFILQNIVKLPLCNIELKADEKQIHLSLKAPEANSFLPIDIKPHGPEAHLTWFNEISSHINQDVTLQEHNADDLKVDASQIASESELILHLPQRAEAHDPNLSVRPSDVAENYFLSKETKERLQHEQQELLKLEQEAIELYKKQQSSKSVSSKTESVEITSSQVKSSSEVRKVVSPPPPPQAQVKEVTPVKVVSSPPPPKEITPAKVATPPPQPQVVTSPVKEVAPPPQPRAVASPAKEVTPSQSEPVKAPSPIKEVRKEVPPSASHSKEVEALVATEIRESLTETRSTVVESGQSSEIREEIVVTEESSLEGKQVVALEREPSPCSIPKIQVYRPVECENPVVTKHKPIELKDIVGYSESLRDGDTAPAGGSPGRQQGYSANITDHASLTIWNNRLANIAGDRSGANQHLQQSGPPPPPIPPNFTRMPGFFQPLPLIAYETTIEILIVKARPPSPPPPPPPTIKRVLVHTESLEQKTQNFFEGIYDAASSDTSLRNAKQKIRSIKSTVLKSKDSTNYAQDTVQKAKARDFLHIFTPPVKKRPIYEIVEEPVNIFELEGDYTESIADDFREPSADFEARGQSVGGMDDYYSGYSRASTRRYETKTRDYDRGTSYDSTVERSQYGISSRRDRSSVDKVEARSSLLATGRTESRAASRAESRAESRASYSVAESRAGIRSSSRLQEDRPLRSVDKPVVVKMLKSVQVEPGETAHFEIQFKDQPGLVTWLKDNKPLEDRLADRITQTAAPMNSYRLDIKNCSETDAGTYTIRAQSASETTTVSAQLAVGQAPGHDETKTNTEPAFLVSLKDAEMIENTLFRFMVKIIGDPKPRVKFYKDEKEILETNDRIQIIRDKDYLGFYELVIADVQKTDAGTYSCKATNKHGEANCEAIATTVEDKNPFGALSGQILPAGEKPVFQWKRNGEEFDPEERFKVLFGEDEDSLALVFQHVKPEDAGIYTCVAQTSTGNISCSAELSVQGAIQTLNREPEKPTLVIEHREANASIGGSAILELQCKGFPKPAVQWKHDGEVIQVDDRHKFMYEDEESMSLVIKNVDTVDAGVYTIEAINELGQDESSINLVVKAPPKIKKITDITCSAGETIKMEIEVEGFPQPTVQVTNNGKDVTAESNVKISSSSIGKSLEKVVVEVKEIKLSQAGNYSIKATNDLSQTSEYWSCTVKSKPVIVKNFESEYIHGEKENVQMTVRIDAYPEAKLTWYHDETEIKITDSKYTVSSDGNAYTLKITGATRVDAGKYTVKATNEHGSATSSTQLLIKCAPEFTHKLKNITVAEGDSNVELVVGVDAYPRPHAKWYIDGIEIDEKRNDFRHVEEGNDFKLIMNQVATNMQGNYTCKIMNDYGKLEDNCVVTVNCKPKVKRGLKNVEVQEGKSFTLEVEVYSEPEAKIKWFKDGHEIYEDARIKISRDTQRIENYYLTLNLARTEDAGTYEMKATNFIGETTSTCKVAVLTSEALSLEQTVTKTLIATTEEPEEGAVPEIVHVDVFQQHSYESVPLKYEVIATGIPKPEAIWYHDGKPITPDKHTAITVDGDHYKLEVQSLDLVDAGEYKVVVQNKVGEKSHQGELSLSGIAEYRKPILTQGPGLKDIKVNKGDKVCEPVVFTADPAPEIVLLKDGQPVVETNNVKLKVDKKDAENGLVQYTCTLNILEAEIKDSGRYELKVKNKYGELVTSGWIDVLAKPEISGLNDTKCLPGDTICFEALVQANPKPKVSWTRGNENLCNHENCEVIADVDADKYRLVFQSVSPCEDGKYTITATNSEGRAAVDFNLAVLVEKPTFIVQPESQSIHDYRPVSTKVLVHGVPLPTIEWFKDDKPINYEAINKPGKDKLYAKEDTKKGTDQIESVLDIKSFRENDVGAYTCVATNEIGVTKAPFKLAMLSLAPSFVKKLDNALDVLQGEPLVLECCVDGSPLPTVQWLKDGDEVKPSESIKISTNPDGLVKLEINSCQPNDSGAYKLIISNPHGEKVALCAVAVKPEEMQPKFLKPITSQTVVVGEPLKLEAQVTGFPAPEVKWYKDGMLLRPSPEINFINSPNGQIGLIIDAAQPLDAGVYKCLIANKGGEIEGVSKVEIVPKESKPVFVAELQDASSIEGFPVKMDIKVVGNPKPKLQWFHNGHEIKPDASHIAIVENPDNSSSLIIEKTAPGDSGLYEVIAQNPEGSTASKAKLYVAPKADETATEEAPQFVSALRDVNADEGQELVLSAPFISNPMPEVIWSKDGVTLTPNERLLMTCDGKHIGLTIKPAEAADSGNYTCLLANPLGEDSSACNANVRKVYKPPVFTQKISDQQQVFGNNAKIPVTVSGVPYPDLEWYFQDKPIPKSEKYSIKNDGDHHMLIVNNCEKGDQGVYKCIASNREGKDITQGRLDIVNEIKKHSRSEPPVFLKKIGDCDIYEGMVAKFTACATGYPEPEVEWFKNDQKLFPSDRFLIDIEPNGLLRLTIKNVTEYDVGRYSCRIFNPYGDDICHAELFYDSLDSQQKPLEDQYTDFKKYKKSGAPPPLSEGPIISRMTDRGLLLSWNPSVPLTPRYPITYQIEMMDLPEGDWRTLRTGVRSCACDIRNLEPFRDYRFRVRVENKFGVSDPSPYTQTYRQKLVPDPPKTYTYLPPGTDFRPETSPYFPKDFDIERPPHDGLAQAPQFLLREQDISYGVKDHNTELMWFVYGYPKPKMTYYFDDMLIESGGRFDQSYTRNGQATLFINKMLDRDVGWYEAVATNEHGEARQRVRLEIAEHPRFLKRPDETFIMARKNGRIEAKLVGIPLPEVHWFKDWKPIVDSSRIKISSYDPDIYVLSIHDSIIKDGGLYSISARNIAGSISTSVTVHIEENEDQYIYKTYGRHPYVRSKQLRYQDKYDIGDELGRGTQGITYHAVERSSGDNYAAKIMYGRPELRPFMLNELEMMNTFNHKNLIRPYDAYDTDRSVTLIMELAAGGELVRDNLLRRDYYTERDIAHYIRQTLWGLEHMHEMGVGHMGLTIKDLLISVVGGDIIKVSDFGLSRKINRHNLSTLDYGMPEFVSPEVVNKEGVNFSHDMWTVGLITYVLLGGHNPFLGIDDRETLTKIREGRWDFKDEIWTHISDDGRDFISRLLLYSPEERMDVKTALKHPWFFMLDRPVYDHDYQIGTDRLRNYYDHFRDWYANASCKNYFRRRRLSGCFQHPSKMVYPPGHVYTPENTPEPLPEPRIRAKREEVVSKYLHPDYELGLIQSESHYQYGPDTYLLQLRDVNFPVRLREYMKVAHRRSPSFALNDSVDWSLPVIRERRRFTDIMDEEIDDERTRSRISMYAANESYSIRRLRTELGPRLDEYTEADAMIETQREGYPPFFREKPQTIAITENQPSHIHCFAVGDPKPCVQWFKNDMVLTESKRIKISVDEDGRSILRFEPALHFDVGVYKVVARNKVGQTVARCRIVVATLPDAPDSPEISANSGTEILLRWKQPRDDGHSTVLCYSLQYKLSNCDAWTTVADNIDHEFYLLHDLQPNTNYQFRLASKNRIGWSEMGIPVSASTVGGDAPKIHITKAMKHLQQLTENGHQVVPEEERVHTDYHCEREPPNWVTDSSVSDKYSFISEIARGEFSTIVKGIQKSTDTVVVAKILEVTDENEDNVVAEFDNFKTLRHERIPALFSAYKPLNVPIAIFVMEKLQGADVLTYFSSRHEYSEQMVATVVTQLLDALQYLHWRGYCHLNIQPDNVVMASVRSIQVKLVDFGSAKKVNKLGMKVTPCGSLDFQPPEMINDEPIFPQSDIWSLGALTYLLLSGCSPFRGADEYETKQNISFVRYRFENLFKEVTPEATRFIMLLFKRHPTKRPYTEDCLEHRWLMSSDYMVRKRERAIFLGSRLKTFCDEYHDLKNASATSSKVLNTVAGGPTPTQLLRSNSIQEELLTTF
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Structural component of the muscle M line which is involved in assembly and organization of sarcomere. Required for the development and organization of indirect flight muscle sarcomeres by regulating the formation of M line and H zone and the correct assembly of thick and thin filaments in the sarcomere. Lacks serine/threonine-protein kinase activity.
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A8DYP7
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CGLR2_DROME
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Cyclic GMP-AMP synthase-like receptor 2 (cGLR2) (EC 2.7.7.-) (EC 2.7.7.86)
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MKESRNLENFVEKKLYECKKKYVDIPKDEGQRYGGKHYEALTSKIFEILRKENPELDIIIAEFSLEGSVGMLKIAKPNEFDLVFKLKFPYYKSIAVTRDPKIPGNVLLDMTRVLELLKDDPREDFQRIRELIQGRLVDAQNFFVVDRLRSWLQSLFSQALNRISYRVELVAGVVSHLKYRTCGPAHTIYVYGDYEYSVDYVPAICLAAEQNVLPTKQLECFKRANTSYWEAIPKPLKPLTETSMISFRSSFYAVEKILLQDVHENCRNAIRFMKKFRDVKTNLGNCKSYYIKTLFLWKIIQEPESYWLNPLSFILADMFDDLAENLRRGVITFFWDPELNMIDALTRDQVWEMYLCVQRIPRDLRGAEISRNKWSFFVLREFSHKKERNVNLKCSSRRKRNVIKGLKTTSICKLRNARTNGTWTAGLWTRPGHAYRGPSETVSTWDTVKDAAWSEGIVE
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Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP from ATP and GTP and plays a key role in antiviral innate immunity. Directly binds some unknown nucleic acid, activating the nucleotidyltransferase activity, leading to synthesis of both 3',2'-cGAMP and 2',3'-cGAMP second messengers. 3',2'-cGAMP and 2',3'-cGAMP bind to and activate Sting, thereby triggering the antiviral immune response via activation of the NF-kappa-B transcription factor Rel (Relish).
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A8DYY6
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SCHI1_DROME
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Schwannomin-interacting protein 1 homolog
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MDIYITKGITNPNYPGFQKFAHTLSDDYIEYSDMECNESDLTDSDREDDPTFPSKMAKESGSETFKNGQDSILSNCDNGNTYISEEESVNRSENIPDIVNENYSATSENSKRALQKPDLIYNLSQNYTTNPEFPSWSCTINSKYEGQLQGQSPIDIVGDFGGEVEREFELLLTGYKNKKEADELKGSNLDKICDAELSNGTEALKQTSSTRLSGNSTRKNKKKNTPYGHQIVKTKHPKPSHDERQLPPDTFDYKTYSQRKYIICDADQYSSVPEKNKNDSPNLNQAEIPNMSSLEIGGSGSQQNLDEDNNKVASRKYSNQSRWSQYLEDPIKYSKDPCSTMVLEQFDAYKIANDMDVETLQNHYKKVKQIEKKRRFNRDEIRKRLAIGDKDSLNNDIKKEEFLTGSDNESYSSDSETCPKLSSGVLRKQSEFCETKRNKEFENDKIFQKNQINQDKSMNHMNGNPIGTTDYPSDENLFFFANQSKLQIEVRIALAQSKEIAQMKVKARKHGVTPIVDVIRSMLCDVGIKMNSNHRWISRQLLTGIQVPTLQLLVNNLQEYIENLNVTLLESLKERDDLNSDQDDILHDLEKINNFFVFQQQSGQQVNKIVRHGHLD
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Regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (hpo), in complex with its regulatory protein Salvador (sav), phosphorylates and activates Warts (wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (yki) oncoprotein. Schip1 promotes kinase activity of Tao and enhances phosphorylation of hpo by Tao.
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A8DZE6
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WTIP_DANRE
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Wilms tumor protein 1-interacting protein homolog (WT1-interacting protein homolog)
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MDEYDEDPGRRASKLMETLSIYDVYQDGMYGEPNPDMEKTKRMNGSSSTPGNKVYSAAPVRSVNGNRASVPLDFCSPQREAVYPDPDVYCTKSEVALPCYSGASDRLRRYTHAEVQGHRYSTGCAYDGLVLGKQVAVSGARSNSLCMSSPDGRYTATSPRSSLASSHSSQDQSKHTSPRSSISSPRSSLVSPGQGEGTSVISPRSSYASTASDTSKHSSPRTSLNSYDCGSKPSSNRTSGISMGYDQRHISPRSSTTSPRSSYSDSRFTPAGGHDPESAAVHGIPMASPRSSICSQPAVAANCVVSPRSSISSHSSRSSRSSRGSMSAYPELQLPMLGPGLPEDALLQDFTEPNGLHNNRVHLQTFPVLEEPQQQNSEVNIGFNYCKAGAGGQRFKLPYQVTPSRDSGPSQAERRLEALTLELEKELEIHMKKEYFGICVKCGKGVYGASQACQAMGNLYHTNCFTCCSCGRRLRGKAFYNVNGKVYCEEDFLYSGFQQTAEKCFVCGHLIMEMILQALGRSYHPGCFRCVICKEGLDGVPFTVDVENNIYCVKDYHTVFAPKCASCNQPILPAQGSEETIRVVSMDKDYHVDCYHCEDCGLQLNDEEGHRCYPLEGHLLCHRCHLHRLKTPLAPHPPPSYPLHVTEL
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May monitor slit diaphragm protein assembly, a specialized adherens junction characteristic of podocytes. In case of podocyte injury, it shuttles into the nucleus and acts as a transcription regulator. Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Acts as a transcriptional corepressor for snai1 and snai2/slug and plays a role in regulating neural crest development (By similarity).
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A8DZH4
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XPR1_DANRE
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Xenotropic and polytropic retrovirus receptor 1 homolog
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MKFTEHLSAHITPEWRKQYIQYEAFKEMLYSAQDQAPSIEVTDEDTVKRYYAKFEEKFFQTCEKELAKINTFYSEKLAEAQRRFATLQNELQSSLDAQRESSRAAGLRHRRTVFHLSQQERCKHRNIKDLQLAFSEFYLSLILLQNYQNLNFTGFRKILKKHDKIFETSRGADWRVAHVEVAPFYTCKKITQLISETETLVTTELEGGDRQKAMKRLRVPPLGAAQPAPAWTTFRVGLYCGVFVALTVTVIIAGVVKLVEHFGDNTDVWPLIRIYRGGFLLIEFLFLLGINTYGWRQAGVNHVLIFELNPRNNLSHQHLFEIAGFLGVLWCVSILSCLFAENTLIPIHMNPLALYGFFFLFLINPLKTCYYKSRFWLLKLLFRVVTAPFHRVGFADFWLADQLNSLVVVLMDLEYMICFYSLELNWTMSEGELWIKEGERICYSYSYGVRAVIKCLPAWFRFVQCLRRYRDTKRAFPHLVNAGKYSTTFFVVIFEALFKTHSGDERFVFLYIMIACRIVNSCYTLLWDLKMDWGLFDRNAGENTLLREEIVYPQKAYYYCAIVEDVILRFAWTIPLSLEVVYDRPVISNILGTVLPPLEVFRRFVWNFFRLENEHLNNCGEFRAVRDISVAPLNADDQTLLEQMMDQEDGVRNRLGKKNWKRSYSMSLRRPRLSSQSKVRDTKVLIEDTDDDT
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Plays a role in phosphate homeostasis. Mediates phosphate export from the cell. Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7) these are important intracellular signaling molecules (By similarity).
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A8E2V8
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PA2A_TRIGS
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Acidic phospholipase A2 Tgc-E6 (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
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MRTLWIMAVLLLGVEGSLMQFEMLIMKLAKSSGMFWYSAYGCYCGWGGQGRPQDATDRCCFVHDCCYGKATGCDPKKDVYTYSEENGDIVCGGDDPCRKEVCECDKAAAICFRDNMDTYNSKTYWMFPAKNCQEESEPC
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Snake venom phospholipase A2 (PLA2) that inhibits the ADP-(IC(50)=272 nM) and collagen-induced (IC(50)=518 nM) human platelet aggregation in platelet rich plasma. Exhibits very high hydrolytic activities toward the synthetic lecithin, and prefers the anionic micelles (dPPC with deoxycholate) to the zwitterionic micelles (dPPC with Triton X-100). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
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A8E5T6
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TCF21_XENTR
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Transcription factor 21 (TCF-21) (Capsulin) (Epicardin) (Podocyte-expressed 1) (Pod 1) (Pod-1)
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MSTGSLSDVEDFQEVEMLECDGIKLDPNKEFGISNDSNEESSTCDNGSPKKGRGTSGKRRKAPSKKSPLGNINQEGKQVQRNAANARERARMRVLSKAFSRLKTTLPWVPPDTKLSKLDTLRLASSYIAHLRQILANDKYENGYIHPVNLTWPFMVAGKPENDLKEVVSTSRLCGPTAS
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Involved in epithelial-mesenchymal interactions in kidney and lung morphogenesis that include epithelial differentiation and branching morphogenesis.
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A8E5V9
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STING_XENTR
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Stimulator of interferon genes protein (STING) (Transmembrane protein 173)
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MACVLAIGSILFVWILGKGKYSGAQLIYRMATNFAISQGCCLVTCACELTEEIKHLHTRYNGHYWRALKASFNLSCAAFVTAILCYVFYEPKLMASLPLTIDITLTLLSWLFCWILGIQGPTPATISEITEIKQLNVAHGLAWSYYVGYLQFVLPALKESIQKFNEENHNLLKFPETCRLHILIPLSCRLYGDLKDVDENITFLKEIPPLYIDRAGIKGRVFKNNVYRILDEDGRPYNCIVEYATPLASLLKMTDIPSAAFSADDRLQQTKLFYRTLKDILENAHELQNTYRLIVYEDFPETKDHSRHLLSQEILKHIRQQHSEEYSML
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Sensor of cytosolic DNA from bacteria and viruses that promotes autophagy. Acts by recognizing and binding cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA in the cytosol. Following cGAMP-binding, promotes the formation of autophagosomes, leading to target cytosolic DNA for degradation by the lysosome. Exhibits guanine base-specific ligand recognition. Binds 3'-3'linked cGAMP, 2'-3' linked cGAMP and 3'-3' linked c-di-GMP with much greater affinity as compared to 3'-3' linked c-di-AMP. Lacks the C-terminal tail (CTT) found in other vertebrate orthologs which is essential for interferon signaling.
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A8FNH9
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NSPC_CAMJ8
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Carboxynorspermidine/carboxyspermidine decarboxylase (CANS DC/CAS DC) (CANSDC/CASDC) (EC 4.1.1.96)
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MFYEKIQTPAYILEEDKLRKNCELLASVGEKSGAKVLLALKGFAFSGAMKIVGEYLKGCTCSGLWEAKFAKEYMDKEIHTYSPAFKEDEIGEIASLSHHIVFNSLAQFHKFQSKTQKNSLGLRCNVEFSLAPKELYNPCGRYSRLGIRAKDFENVDLNAIEGLHFHALCEESADALEAVLKVFKEKFGKWIGQMKWVNFGGGHHITKKGYDVEKLIALCKNFSDKYGVQVYLEPGEAVGWQTGNLVASVVDIIENEKQIAILDTSSEAHMPDTIIMPYTSEVLNARILATRENEKISDLKENEFAYLLTGNTCLAGDVMGEYAFDKKLKIGDKIVFLDQIHYTIVKNTTFNGIRLPNLMLLDHKNELQMIREFSYKDYSLRN
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Catalyzes the decarboxylation of carboxynorspermidine and carboxyspermidine in vitro. In vivo, responsible for synthesizing spermidine, but not sym-norspermidine.
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A8FP63
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FADB_SHESH
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MIYQSPTIQVELLEDNIARLCFNASGSVNKLDRETINSLDAALDAIQQDSHIQALVLTSAKGAFIVGADITEFLGLFAQEDSVLLPWIAEANVVFNKLEDLPFPTISAINGFALGGGFETVLATDFRIADTTAKIGLPETKLGLIPGFGGTVRLPRLIGTDNALEWITSGKDQRPEAALKVGAIDAVVAPENLQASAIKMLKDALAEKLDWQSRRARKQAALTLPKLEAMMSFATAKGMVFKIAGKHYPAPMAAISVIEQAARCGRADALKVEHQAFVKLAKTDVAQALIGIFLNDQLVKGKAKKAGKLAKNIDTAAVLGAGIMGGGIAYQSASKGTPIIMKDIAQPALELGLGEASKLLAAQIKRGRSTPQKMAKVLNNITATLDYTPVKDVDVVVEAVVEHPKVKSMVLAEVEQNVSDDAIITSNTSTISINLLAKSLKKPERFCGMHFFNPVHKMPLVEVIRGENSSEETIASVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSGLLADGADFAAIDKVMEKQFGWPMGPAYLLDVVGIDTGHHAQAVMAEGFPDRMGKNGKDAIDIMFEAERFGQKNSKGFYAYSVDRRGKPKKDVDPTSYELLGAEFGELKAFESEDIIARTMIPMIIETVRCLEEGIIATPAEADMGLVFGLGFPPFRGGVFRYIDTMGVANFVALADKYAHLGGLYQVTDAMRELAANNGSYYQS
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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A8G8D1
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FADB_SERP5
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MLYQGETLQLHWLDNGIAELVFNAPGSVNKLDTRTVASLGEALAVLEKQTELKGLLLRSTKAAFIVGADITEFLSLFAAPAEKLQEWLNFANAIFNRLEDLPVPTISAINGYALGGGCECILATDFRVASPDARIGLPETKLGIMPGFGGSVRLPRLLGNDSALEIIAAGKDVSAKDALKVGLVDAVVAPEKLVEAALKMLQQAIEGKLDWRAYRQPKLEPLKLSPIEAAMSFTTAKGMVMQTAGKHYPAPMTAVKTIEAAARLGRDEALKLETASFVPLARSKEARALVGIFLNDQFVKGQAKKLAKGIEAPKQAAVLGAGIMGGGIAYQSALKGVPVVMKDISDKSLTLGMNEAAKLLNKQLERGKLDGMKMAQVLSTIQPTLDYAGIERAQVIVEAVVENPKIKAAVLSEVEGLIGENTVLASNTSTIPINHLAKSLKRPQNFCGMHFFNPVHRMPLVEIIRGEQTSDSTIAAVVAYASRMGKTPIVVNDCPGFFVNRVLFPYFAGFSMLLRDGADFRQIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPERMGKDYRDAIDVMFDNQRFGQKNQLGFYRYSQDNKGKPRKDNDEQTDVLLAEVSQPRQTISDEEIIARMMIPMINEVVRCLEENIIASPAEADMALVYGIGFPPFHGGAFRYLDTLGTANYVELAQRYAHLGALYQVPAGLRAKAEHNESYYPVAAPLSDVSTGQPA
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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A8GYG0
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FADB_SHEPA
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MIYQSPTIEVELLEDNIAHLCFKAQGSVNKFDRETIDSLNAALDSIKQDSSIKALMLSSAKDAFVVGADITEFLGLFAEEDTVLQSWLEQANVVFNKLEDLPFPTISAINGFALGAGCETILATDFRIADTTARIGLPETKLGIIPGFGGTVRLPRVIGADNALEWITSGKDQRPEAALKVGAIDAVVAPEQLKPAALKMLKDALIEKLDWQTRRAKKQAPLTLPKLEAMMSFATAKGMVFKVAGKHYPAPMAVISVIEQAAQLDRAGALQVEHQAFIKLAKTEVAQALIGIFLNDQLVKGKAKKAGKLAKKVNSAAVLGAGIMGGGIAYQSASKGTPIVMKDIAQPALDLGLGEAAKLLTAQVKRGRSTPAKMAAVLNNITPALDYAPVKDADVVVEAVVEHPKVKSMVLAEVEQHVSEDAIITSNTSTISINLLAKSLKKPERFCGMHFFNPVHKMPLVEVIRGENSSDETVASVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSGLLADGADFAAIDKVMEKQFGWPMGPAYLLDVVGLDTGHHAQAVMAEGFPDRMGKTGKDAIDVMFEAERFGQKNSKGFYQYSVDRRGKPKKDLDPTSYELLQAEFGEQKAFESDEIIARTMIPMIIETVRCLEEGIIASPAEADMGLVYGLGFPPFRGGVFRYLDTMGVANFVALADKYAHLGGLYQVTDTMRELAANNGSYYQQA
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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A8HAL1
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UBP16_DANRE
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Ubiquitin carboxyl-terminal hydrolase 16 (EC 3.4.19.12) (Deubiquitinating enzyme 16) (Ubiquitin thioesterase 16) (Ubiquitin-specific-processing protease 16)
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MGKKKVKDRSAGTDSSSETAGPSCTHIRKGTENSVLKKACLNEHWSSCQDCEQDKPEEKQILEDQTDGESPAVWMCLKCGHRGCGRSGNQHAIKHYETPRSEPHCLVLSLDVWSVWCYICDDEVQYSSTGQLAQLITNIRKQVLTAPDKRNASKKSWKEDISVMNSAEQTQDEEKGKKGKQKSSSKQEDSPKSHQSAAAGSSAVVSVRGLSNLGNTCFFNAVVQSLSQTQYLRELLKQIAEEKSSFSITPALSSELDPLQIQLERPGSLTLAMCQLMNEIQETKKGVVTPKELFTQVCKKAPRFKGFQQQDSQELLRYLLDGMRAEEAKRVNSGILEALKSSGKNFEAEQTKKIVKEYEKDGAPKNFVDRVFGGAMSSTVMCKECKTVSLVTEMFLDLSLPVADEAYRKKNQKKAVQHRHSVSDDGDQDTSSLANGNEDMPTGTGSKYQQKKAKKQAKKQAKNQRRQQKQGGKVTLDAITNQSSTDPADSSMQTQTVSVNGSADAQPADTNQEDLSLEKHNEDQDDEEPEQEQAASVNNRFTALSEDQTTEDIAEQVNEDEDEIEQNCAEEEELVEELNTMSLTTPSEGDVENGEDTLEDVKEYTVVNRDPELAFRALASRTAPVKQECSVESCLYQFTEVEHLTENNRLMCVTCTKQQPGYKDGCKKAVYRDALKQMLISDPPVVLTLHLKRFQQVAYSVCKVNRHVQFPQILDLAPFCSLNCTGVKEGETQVLYSLYGIVEHSGTMRSGHYTAYVKSRPSTHNCVQNGTAAASGDAEASKGSWFHISDSSVHPVPEAKVQSSQAYLLFYEKIS
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Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B. {ECO:0000255|HAMAP-Rule:MF_03062}.
|
A8I4E9
|
CP100_CHLRE
|
Cilia- and flagella-associated protein 100 (Flagella-associated protein 100) (Modifier of inner arms 1 protein) (Mia1p)
|
MPIYDEASVPGTAAGRSTTDVGATAGANPFNIPADEEIFRFREEERARKEQDKLIAQTMRVADKTTFAAQMQATATADARTLLRELRPPKGPKATTTLAASSVGTLDRRKEKENMADFIAKKREIFLLQMSLDTKRAEIKKLEERARQREEALKKSEQMLEEDALRFDAFLKENDEKVQEAIKKAEAEAKAKQDKVLEIKRLNTATAALRSELNKYEEQLEDCRRYKEFLDSITPPEWFEQQAAKLQRRKDALVAEWQSQCEALKQRREAALAAKTAAESDYANARTQQQAERAERAIKESVAALKEIMKEKEPQPPNLDFEMDPEDEEMYFQEPGQLLAVYKQLEESNLFYIQNAQETEEALEELRQKLRDTKTRMDAEAQGLQGQVSTLQASIVAAREKAKRLKDRTLENEGAFTLSMGSSNAPTSSVTGSSGPGGPVNLKELGDKVREVYVRCGFDADASISTLQMLTNIEMKLEEYLNLAEGMTPDYVDGAEKAREKDRRKVARDEKLSTQHREHEARMARALERAAAPVFKKTGKPLMFRSAPPQRKKVVQADDRNDEEAELEAYLAQDMI
|
As part of MIA, a complex associated with the outer doublet microtubules of the axoneme, may play a role in ciliary/flagellar motility by regulating the assembly and the activity of axonemal inner dynein arm.
|
A8IKD2
|
CAH_AZOC5
|
Cyanuric acid amidohydrolase (CAH) (EC 3.5.2.15)
|
MPIAKVHRIATASPDDVSGLAAAIATGAIAPAGILAIFGKTEGNGCVNDFSRGFAVQSLQMLLRGHMGAAADEVCLVMSGGTEGGMSPHFLVFERAEGNAPEAAPALAIGRAHTPDLPFEALGRMGQVRMVAQAVRRAMAAAGITDPEDVHFVQVKCPLLTAMRVKEAEARGATTATSDTLKSMGLSRGASALGIALALGEVAEDALSDAVICADYGLWSARASCSSGIELLGHEIVVLGMSEGWSGPLAIAHGVMADAIDVTPVKAALSALGAEAGEATIVLAKAEPSRSGRIRGKRHTMLDDSDISPTRHARAFVAGALAGVVGHTEIYVSGGGEHQGPDGGGPVAVIAARTMG
|
Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which spontaneously decarboxylates to biuret. {ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:22730121}.
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A8IU92
|
CFA20_CHLRE
|
Cilia- and flagella-associated protein 20 (Basal body up-regulated protein 22) (Bug22p) (Flagellar-associated protein 20)
|
MFKNAFQSGFLSVLYSIGSKPLEIWDKQVSNGHIKRITDADIQSSVLEIMGQNVSTTYITCPADPNKTLGIKLPFLVLIIKNLNKYFSFEVQVLDDKNVRRRFRASNYQSTTRVKPFICTMPMRLDSGWNQIQFNLSDFTRRAYGTNYIETLRVQVHANCRIRRIYFSDRLYSEEELPAEFKLFLPIQKS
|
Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility. Involved in the control of flagellar beating in an asymmetric and planar waveform. Stabilizes outer doublet microtubules (DMTs) of the axoneme and may work as a scaffold for intratubular proteins, such as tektin and PACRG, to produce the beak structures in DMT1, 5 and 6. Not essential for flagellar assembly.
|
A8J637
|
PETS_CHLRE
|
Polyprotein of EF-Ts, chloroplastic (110 kDa pro-protein) [Cleaved into: Plastid-specific ribosomal protein-7, chloroplastic (65 kDa protein PSRP-7) (CrePSRP-7); Elongation factor Ts, chloroplastic (55 kDa protein EF-Ts) (EF-Ts)]
|
MLRELGRTATVKAHGRSVLRPVRGPAGRRQVAFTGVRPSVRVFAEAPAAEQAAKAIKLEDVKEGSEYEGTVTTVEEFGAFVNFGANTNGLVHISKLASGFTKNAKDVVQPGQKVTVKVLSVDAEKKRVSLELKSAVAAEASAEESDDIITEPDREGADATDDDEDVEVELEDGQVEVRADLPGFEDIPFVMEEADMDAEMSEAAIAALEADLDGAEIRYELEAPAYMEEVTGKVARIEDYGVFLEFEWNGKTLTGLLAKDEMKVPSSALSAEAQAALRAEWADTGFEMPAFVELPDDELDVKKYYQPGESVPAFVLESSLVDGRGISLTHFTDEEVSAEAVAAYEELEDDEDEELDKMMADAAGLEDEVLAFDPEALMEEDEGEEAGAAADAGDDAEYEGVSADGLEGANGNYALGATRSGLIKGKNGYQVAPMGLPSRPLNDAVTSSGLAILGTSEVDFDGDEVQLVDYWTSEAFDNIPKDVLKKLGLKMSYTEAGEAEFEERADFEATDVPFYLYGGDVESRAKEFVADLLSDDVDEAELPARAGRAPIVLAAAVQNISAAEVKALREKTGAGMMDCKKALAECAGDAEAAAEWLRKKGLSGADKKAGRIAAEGAVARYIHPGSRLGVLLEVNCETDFVAASEKFQALVNELGMIIAATDCICVSPEDVPEEVLAKEREVEMGKEDLANKPEAIRAKIVEGRLQKMRDQVALTNQATLSNPDKTVAELVKETIAAVGENVKIRRFIKYRLGEGLEKKANDFAAEVAQQTQAKAAAPAAPKKEEPKKEEPKKATVAVSAGTVKELRDKTGAGMMDCKKALAENENDMEKATEWLRMKGLAGADKKAGRIAAEGVVASYIHPGSRLGVLLEVNCETDFVAASEKFNELVNYIAMGIVAGQNVQYVSADEIPAEVFEREKQLEMARDDLKGKPDAIRAKIAEGRAKKIATEMCLLDQPFLTDPSKTVAEAIKESIAAIGEKISVRRFVKFQLGEGLEKKSNDFAAEVAAATGAK
|
[Elongation factor Ts, chloroplastic]: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. [Plastid-specific ribosomal protein-7, chloroplastic]: Binds to psbD and psbA mRNAs 5'-untranslated regions (UTRs) in vitro.
|
A8JB22
|
DRC2_CHLRE
|
Dynein regulatory complex subunit 2 (Coiled-coil domain-containing protein 65 homolog) (Flagellar-associated protein 250)
|
MVKAGKKVKGASKVRENETEEEKKIRLEMEALAADEAERKAQEAARVALRERQLREQRYAHLNGIKIHNQWRKIMRMAKVEELRREIEILSQNHEREVDRKDAIMQMLDRDLEEAEEQYSLAVRSHMLVVDNLLDLQYQRMRALEAEFAADLKALEDEFETERTEIVNAHTRQRKDMGDMIAAMEGEFADAEAELRQEYEAQREEIKNRNSEEYNVLKIQLEGIIEELEKSFELAHRAYLESTEHRTNTFRTLTKDDAKAALKIERQMRKLVRLQEALQHWRTKIATNGREWEERNRALRNEKEIMARHYAKLKSSMDAFRAGQAERLKQLSLASSGAMETLRGKLAVAENVLKLAELARKYETEQEKVLPFWNPAQAVPSGEQGDEEAAAQAEAEAAALEPSAAELGELGLRASMPEDSSKEAPGPSKSSAGPGKPKFSSYGLDPSSGSEVDEWDYLNCFFRRYNKALLDKTAIDKEKSRLERENADLRSILKQYLDGISVNDDVLNNPVNPLLVVNNRLQITLTERNKARAAAMAQRAAAATGAGLSVTGQGAGGGGQKQLVEVQVVSRVS
|
Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays a critical role in the assembly of N-DRC and also stabilizes the assembly of multiple inner dynein arms and radial spokes. Coassembles with DRC1 to form a central scaffold needed for assembly of the N-DRC and its attachment to the outer doublet microtubules.
|
A8JQX3
|
NOCT_DROME
|
Nocturnin (EC 3.1.3.-) (Curled)
|
MDQKTTGLRENYGHRRQPALGKAMPVTALLLNLESNPLDYSRNDIGAELLEDDDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLAGERHREIPCSNCLKTAPGHLIDRQSAINEMCQRLCGPECRRPQGLTLDGVRQDFLRQYEIAEAVAKTSAMTSTVQMKQRLAARKLEFEKEMEMDEQLGVASPRNDINLGQSSTVAATGMGEFEFEPPRDLLLYLVRMGSFNSAPKINNVDSQDDGLVLPSGLSTPALLQHVQQLRGGGIEQPSLLTRGFLKPLLADEDVADGLRCLKLNSVSRVCSAPVEGDDIRLLQWNILSQTLGQHNDGFVRCPEEALTWEHRKYLIVQEILQNQPDVICLQEVDHFKFLQTVLGSQNYAGIFFPKPDSPCLYIEQNNGPDGCAIFYKRDKLQLQGYDTRILEVWRVQSNQVAIAARLRMRSSGREFCVATTHLKARHGALLAKLRNEQGRDLIRFVKQFAGDTPLLLCGDFNAEPVEPIYATILGCDLLRLGSAYADVKLDREEILHPNADVGEFVAKSMKREPPYTTWKIREEGEECHTIDYVFYTPDRLKIKNCLDFPAGEQIGKNRTPSFQYPSDHFSLVCDFELLPPTENGKESGSGSGSDGENETEVEGSKHGSIQ
|
Phosphatase which catalyzes the conversion of NADP(+) to NAD(+) and of NADPH to NADH. Shows a small preference for NADPH over NADP(+). Because of its association with the CCR4-NOT complex, has a role in mRNA deadenylation and decay. Required at the pupal stage for proper wing morphogenesis after eclosion. [Isoform D]: In dorsal neurons, contributes to the light-mediated behavioral response.
|
A8JUP7
|
HAYAN_DROME
|
Serine protease Hayan (EC 3.4.21.-)
|
MAMISARRYFLLGLLVLTTSAYVTVGDEGDPCQVRSDIPGICLSSSACENIRGYLKSGTLSTSQVPSCGFGAREEIICCPTVACCATDRGREVQFHATSSERSSLPEPKREPTPEPEPLPPTTTEGKRERESRLDENQNFFDFNKLLSTTVKPQKTHESLKLPTQESMKTPTHESMKMPTHESMKLPTHEPMKLPIQSVGAWGIAPSKTQPIASTQRSFMEPEWGREPRIVNRPLTTPRSRPQRPNNSNFNTNPSPNNNNLIHLVNDRLREQGMQIEPAREVPMVLQTTPTPTPAPTPTQLIDPFEPYRFRGQDRDKDTQPQEPWNDVSNNLDADPAPSIFNPAETRPTTPNPNPSRVNLPEKERPSVAACEKIRSGGKPLTVHILDGERVDRGVYPHMAAIAYNSFGSAAFRCGGSLIASRFVLTAAHCVNSDDSTPSFVRLGALNIENPEPGYQDINVIDVQIHPDYSGSSKYYDIAILQLAEDAKESDVIRPACLYTDRSDPPANYKYFVAGWGVMNVTNRAVSKILLRAALDLVPADECNASFAEQPSANRTLRRGVIASQLCAADKNQRKDACQGDSGGPLILEIDDVDGTYSIVGVISSGFGCATKTPGLYTRVSSFLDYIEGIVWPSNRF
|
Serine protease which, by converting prophenoloxidase 1 (PPO1) into its active form, plays an essential role in the melanization immune response to physical or septic wounding. May function in diverse PPO1-activating cascades that are negatively controlled by different serpin proteins Spn27A and Spn28D in the hemolymph, and Spn28D and Spn77BA in the trachea. Also required in the systematic wound response by mediating the redox-dependent activation of the JNK cytoprotective cascade in neuronal tissues after integument wounding.
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A8JUV0
|
SBNO_DROME
|
Protein strawberry notch
|
MTSKKRKTLLDADDDNDNFDEDDSGSDFDDDEDPDQIEVPGGGRDLNTAVTYAQNIRSGVGVAPKGGIPIPISGAKIVVGNNKIKPISLLRINNNNNNIVTSVNNRNNNNIISTNGSSNNNNNSINNNSQIIKTTTVTTTPTTVGATPTVGGVALGGKLTVIPIAGRNVALDNNLSNMPKKLNNMVTAMGSPAARSSGNAGTTGSSQGGAIGSTSSYLNSLTTNELMNLAAYVAAKGSNAPPPPPPSTAANSVRHSPTGGIPNPGGNFFGGSAAASTSASAANFNMAASLLAQMSYAGGASQIRALKVAGNIGGVGNNQKPPPIATTPGSGGPAGGAPGSGVKGNNSMMEAVQKLIAMNPEYLTSGIPNTVFQMFMQSMQRPQATPSPNQPMNPGAMVTSAAAAAAHASAVAYVQQEEDEVDYEEMGVAETYADYWPAKLKLGKKHPDAVVETASLSSVEPCDVYYKLSLPLETINSGHLSALQLESITYASQAHDHLLPDGSRAGFLIGDGAGVGKGRTIAGIIYENYLKGRKKALWISVSNDLKYDAERDLSDIGATRIEVHALNKFKYAKISSDVNNNCKRGVIFSTYSALIGESNNKTGKYRSRFRQLLQWCGEDFEGLIIFDECHKAKNLCPVGSGKPTKTGQTVLELQQKLPKARVVYASATGASEPKNMAYMVRLGLWGQGTAFGNFNDFITAVERRGVGAMEIVAMDMKLRGMYIARQLSFKGVSFKIEEVPLSKEFRKIYDQSVELWVEAMQKFTEAAELIDAESRMKKTMWGQFWSSHQRFFKYLCIAAKVNHAVLVARESIKYGKCVVIGLQSTGEARTLDQLERDDGELTDFVSTAKGVFQSFVERHFPAPDRNRINRILGLYDETPSLSSVADSTSSLSNNSNITTAAGKRKGSNNNDNRSTKIKKKKRSGSWECSDSEDENTDMKRNRKRDGGNSNSDSDEANSDDDLKSDIDDEDEDHDVDSDQRSVASDASSDFNPFFSGSDSDIDPWVNARSKKSKKAQKKSKKKVKKEKTKKEITTSSATDPSGSTAMSATVVAALNAVKNRKSQLSTQDKIQDLLQKKQELKGTVTPVGVNGVKLNYGPPPKDAIERACTMKEELLRKIERLGARLPPNTLDQLIDELGGPDNVAEMTGRRGRVVQTDDGSIQYESRTESDVPLETLNITEKQRFMDGEKDVAIISEAASSGISLQSDRRVFNQRRRVHITLELPWSADRAIQQFGRTHRSNQVNAPEYIFLISDLAGERRFASTVAKRLESLGALTHGDRRATETRDLSQFNIDNKYGRQALETVMRTIMGYESPLVPPPTDYSGEFFKDIAGALVGVGIIVNSESHPGVLSLDKDYNNISKFLNRILGCPVDLQNRLFKYFTDTMTAIIQQAKRGGRFDLGILDLGAAGENVTRVRLIRFVRKHATGVAPTEMHTVRVERGMIWQEAIDKYADLFNENEGFYLSHQLRNQKRTAIMVVILESRNSSSTSSTTDLDSGSKKKKTHSKKEIMCQIYRPNTGLQVRHESLFELEKKYRKVASEEAEPHWTEQYDASVNTCSHAYWNGNCRNVSLGNDCEVGLRQRLYHVLAGSVLSVWGRVEHILNTRSNSKMQVIRMKTTEGEKIVGTLIPKSCFEPLVADLRSDSEKQEEFNY
|
Notch pathway component, may contribute to the specificity between lateral and inductive Notch signaling pathways in the wing disk. Required during many developmental stages including oogenesis, embryogenesis and imaginal development of the eye, wing and leg. Ebi and sno regulate EGFR-dependent Delta transcription in the developing eye, by antagonizing a repressor function of Suppressor of Hairless (Su(H)). They are required in the R-cells for normal cone cell development.
|
A8K0Z3
|
WASH1_HUMAN
|
WASH complex subunit 1 (CXYorf1-like protein on chromosome 9) (Protein FAM39E) (WAS protein family homolog 1)
|
MTPVRMQHSLAGQTYAVPFIQPDLRREEAVQQMADALQYLQKVSGDIFSRISQQVEQSRSQVQAIGEKVSLAQAKIEKIKGSKKAIKVFSSAKYPAPGRLQEYGSIFTGAQDPGLQRRPRHRIQSKHRPLDERALQEKLKDFPVCVSTKPEPEDDAEEGLGGLPSNISSVSSLLLFNTTENLYKKYVFLDPLAGAVTKTHVMLGAETEEKLFDAPLSISKREQLEQQVPENYFYVPDLGQVPEIHVPSYLPDLPGIANDLMYSADLGPGIAPSAPGTIPELPTFHTEVAEPLKVDLQDGVLTPPPPPPPPPPAPEVLASAPPLPPSTAAPVGQGARQDDSSSSASPSVQGAPREVVDPSGGWATLLESIRQAGGIGKAKLRSMKERKLEKQQQKEQEQVRATSQGGHLMSDLFNKLVMRRKGISGKGPGAGEGPGGAFVRVSDSIPPLPPPQQPQAEEDEDDWES
|
Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. Involved in endocytic trafficking of EGF (By similarity). Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration. In T-cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL proposed to be implicated in T cell proliferation and effector function. In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T-cell activation (By similarity). Involved in Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling. Involved in the exocytosis of MMP14 leading to matrix remodeling during invasive migration and implicating late endosome-to-plasma membrane tubular connections and cooperation with the exocyst complex. Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By similarity).
|
A8K2U0
|
A2ML1_HUMAN
|
Alpha-2-macroglobulin-like protein 1 (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 9)
|
MWAQLLLGMLALSPAIAEELPNYLVTLPARLNFPSVQKVCLDLSPGYSDVKFTVTLETKDKTQKLLEYSGLKKRHLHCISFLVPPPAGGTEEVATIRVSGVGNNISFEEKKKVLIQRQGNGTFVQTDKPLYTPGQQVYFRIVTMDSNFVPVNDKYSMVELQDPNSNRIAQWLEVVPEQGIVDLSFQLAPEAMLGTYTVAVAEGKTFGTFSVEEYVLPKFKVEVVEPKELSTVQESFLVKICCRYTYGKPMLGAVQVSVCQKANTYWYREVEREQLPDKCRNLSGQTDKTGCFSAPVDMATFDLIGYAYSHQINIVATVVEEGTGVEANATQNIYISPQMGSMTFEDTSNFYHPNFPFSGKIRVRGHDDSFLKNHLVFLVIYGTNGTFNQTLVTDNNGLAPFTLETSGWNGTDVSLEGKFQMEDLVYNPEQVPRYYQNAYLHLRPFYSTTRSFLGIHRLNGPLKCGQPQEVLVDYYIDPADASPDQEISFSYYLIGKGSLVMEGQKHLNSKKKGLKASFSLSLTFTSRLAPDPSLVIYAIFPSGGVVADKIQFSVEMCFDNQVSLGFSPSQQLPGAEVELQLQAAPGSLCALRAVDESVLLLRPDRELSNRSVYGMFPFWYGHYPYQVAEYDQCPVSGPWDFPQPLIDPMPQGHSSQRSIIWRPSFSEGTDLFSFFRDVGLKILSNAKIKKPVDCSHRSPEYSTAMGAGGGHPEAFESSTPLHQAEDSQVRQYFPETWLWDLFPIGNSGKEAVHVTVPDAITEWKAMSFCTSQSRGFGLSPTVGLTAFKPFFVDLTLPYSVVRGESFRLTATIFNYLKDCIRVQTDLAKSHEYQLESWADSQTSSCLCADDAKTHHWNITAVKLGHINFTISTKILDSNEPCGGQKGFVPQKGRSDTLIKPVLVKPEGVLVEKTHSSLLCPKGKVASESVSLELPVDIVPDSTKAYVTVLGDIMGTALQNLDGLVQMPSGCGEQNMVLFAPIIYVLQYLEKAGLLTEEIRSRAVGFLEIGYQKELMYKHSNGSYSAFGERDGNGNTWLTAFVTKCFGQAQKFIFIDPKNIQDALKWMAGNQLPSGCYANVGNLLHTAMKGGVDDEVSLTAYVTAALLEMGKDVDDPMVSQGLRCLKNSATSTTNLYTQALLAYIFSLAGEMDIRNILLKQLDQQAIISGESIYWSQKPTPSSNASPWSEPAAVDVELTAYALLAQLTKPSLTQKEIAKATSIVAWLAKQHNAYGGFSSTQDTVVALQALAKYATTAYMPSEEINLVVKSTENFQRTFNIQSVNRLVFQQDTLPNVPGMYTLEASGQGCVYVQTVLRYNILPPTNMKTFSLSVEIGKARCEQPTSPRSLTLTIHTSYVGSRSSSNMAIVEVKMLSGFSPMEGTNQLLLQQPLVKKVEFGTDTLNIYLDELIKNTQTYTFTISQSVLVTNLKPATIKVYDYYLPDEQATIQYSDPCE
|
Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase (By similarity). Displays inhibitory activity against chymotrypsin, papain, thermolysin, subtilisin A and, to a lesser extent, elastase but not trypsin. May play an important role during desquamation by inhibiting extracellular proteases.
|
A8K4G0
|
CLM7_HUMAN
|
CMRF35-like molecule 7 (CLM-7) (CD300 antigen-like family member B) (CMRF35-A2) (Immune receptor expressed on myeloid cells 3) (IREM-3) (Leukocyte mono-Ig-like receptor 5) (Triggering receptor expressed on myeloid cells 5) (TREM-5) (CD antigen CD300b)
|
MWLPPALLLLSLSGCFSIQGPESVRAPEQGSLTVQCHYKQGWETYIKWWCRGVRWDTCKILIETRGSEQGEKSDRVSIKDNQKDRTFTVTMEGLRRDDADVYWCGIERRGPDLGTQVKVIVDPEGAASTTASSPTNSNMAVFIGSHKRNHYMLLVFVKVPILLILVTAILWLKGSQRVPEEPGEQPIYMNFSEPLTKDMAT
|
Acts as an activating immune receptor through its interaction with ITAM-bearing adapter TYROBP, and also independently by recruitment of GRB2.
|
A8K7I4
|
CLCA1_HUMAN
|
Calcium-activated chloride channel regulator 1 (EC 3.4.-.-) (Calcium-activated chloride channel family member 1) (hCLCA1) (Calcium-activated chloride channel protein 1) (CaCC-1) (hCaCC-1)
|
MGPFKSSVFILILHLLEGALSNSLIQLNNNGYEGIVVAIDPNVPEDETLIQQIKDMVTQASLYLLEATGKRFYFKNVAILIPETWKTKADYVRPKLETYKNADVLVAESTPPGNDEPYTEQMGNCGEKGERIHLTPDFIAGKKLAEYGPQGRAFVHEWAHLRWGVFDEYNNDEKFYLSNGRIQAVRCSAGITGTNVVKKCQGGSCYTKRCTFNKVTGLYEKGCEFVLQSRQTEKASIMFAQHVDSIVEFCTEQNHNKEAPNKQNQKCNLRSTWEVIRDSEDFKKTTPMTTQPPNPTFSLLQIGQRIVCLVLDKSGSMATGNRLNRLNQAGQLFLLQTVELGSWVGMVTFDSAAHVQNELIQINSGSDRDTLAKRLPAAASGGTSICSGLRSAFTVIRKKYPTDGSEIVLLTDGEDNTISGCFNEVKQSGAIIHTVALGPSAAQELEELSKMTGGLQTYASDQVQNNGLIDAFGALSSGNGAVSQRSIQLESKGLTLQNSQWMNGTVIVDSTVGKDTLFLITWTMQPPQILLWDPSGQKQGGFVVDKNTKMAYLQIPGIAKVGTWKYSLQASSQTLTLTVTSRASNATLPPITVTSKTNKDTSKFPSPLVVYANIRQGASPILRASVTALIESVNGKTVTLELLDNGAGADATKDDGVYSRYFTTYDTNGRYSVKVRALGGVNAARRRVIPQQSGALYIPGWIENDEIQWNPPRPEINKDDVQHKQVCFSRTSSGGSFVASDVPNAPIPDLFPPGQITDLKAEIHGGSLINLTWTAPGDDYDHGTAHKYIIRISTSILDLRDKFNESLQVNTTALIPKEANSEEVFLFKPENITFENGTDLFIAIQAVDKVDLKSEISNIARVSLFIPPQTPPETPSPDETSAPCPNIHINSTIPGIHILKIMWKWIGELQLSIA
|
May be involved in mediating calcium-activated chloride conductance. May play critical roles in goblet cell metaplasia, mucus hypersecretion, cystic fibrosis and AHR. May be involved in the regulation of mucus production and/or secretion by goblet cells. Involved in the regulation of tissue inflammation in the innate immune response. May play a role as a tumor suppressor. Induces MUC5AC.
|
A8K830
|
OCAT2_HUMAN
|
POU class 2 homeobox associating factor 3 (Cancer susceptibility candidate protein 13) (Colorectal cancer-associated protein 2) (Protein OCA-T2)
|
MSEKPKVYQGVRVKITVKELLQQRRAHQAASGGTRSGGSSVHLSDPVAPSSAGLYFEPEPISSTPNYLQRGEFSSCVSCEENSSCLDQIFDSYLQTEMHPEPLLNSTQSAPHHFPDSFQATPFCFNQSLIPGSPSNSSILSGSLDYSYSPVQLPSYAPENYNSPASLDTRTCGYPPEDHSYQHLSSHAQYSCFSSATTSICYCASCEAEDLDALQAAEYFYPSTDCVDFAPSAAATSDFYKRETNCDICYS
|
Transcriptional coactivator that specifically associates with POU2F3. This complex drives the development of tuft cells, a rare a rare chemosensory cells that coordinate immune and neural functions within mucosal epithelial tissues.
|
A8K8P3
|
SFI1_HUMAN
|
Protein SFI1 homolog (hSFI1)
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MKNLLTEKCISSHNFHQKVIKQRMEKKVDSRYFKDGAVKKPYSAKTLSNKKSSASFGIRRELPSTSHLVQYRGTHTCTRQGRLRELRIRCVARKFLYLWIRMTFGRVFPSKARFYYEQRLLRKVFEEWKEEWWVFQHEWKLCVRADCHYRYYLYNLMFQTWKTYVRQQQEMRNKYIRAEVHDAKQKMRQAWKSWLIYVVVRRTKLQMQTTALEFRQRIILRVWWSTWRQRLGQVRVSRALHASALKHRALSLQVQAWSQWREQLLYVQKEKQKVVSAVKHHQHWQKRRFLKAWLEYLQVRRVKRQQNEMAERFHHVTVLQIYFCDWQQAWERRESLYAHHAQVEKLARKMALRRAFTHWKHYMLLCAEEAAQFEMAEEHHRHSQLYFCFRALKDNVTHAHLQQIRRNLAHQQHGVTLLHRFWNLWRSQIEQKKERELLPLLHAAWDHYRIALLCKCIELWLQYTQKRRYKQLLQARADGHFQQRALPAAFHTWNRLWRWRHQENVLSARATRFHRETLEKQVFSLWRQKMFQHRENRLAERMAILHAERQLLYRSWFMWHQQAAARHQEQEWQTVACAHHRHGRLKKAFCLWRESAQGLRTERTGRVRAAEFHMAQLLRWAWSQWRECLALRGAERQKLMRADLHHQHSVLHRALQAWVTYQGRVRSILREVAARESQHNRQLLRGALRRWKENTMARVDEAKKTFQASTHYRRTICSKVLVQWREAVSVQMYYRQQEDCAIWEAQKVLDRGCLRTWFQRWWDCSRRSAQQRLQLERAVQHHHRQLLLEGLARWKTHHLQCVRKRLLHRQSTQLLAQRLSRTCFRQWRQQLAARRQEQRATVRALWFWAFSLQAKVWATWLAFVLERRRKKARLQWALQAYQGQLLQEGATRLLRFAASMKASRQQLQAQQQVQAAHSLHRAVRRCATLWKQKVLGRGGKPQPLAAIAPSRKVTFEGPLLNRIAAGAGDGTLETKRPQASRPLGALGRLAAEEPHALELNTAHSARKQPRRPHFLLEPAQSQRPQKPQEHGLGMAQPAAPSLTRPFLAEAPTALVPHSPLPGALSSAPGPKQPPTASTGPELLLLPLSSFMPCGAAAPARVSAQRATPRDKPPVPSSLASVPDPHLLLPGDFSATRAGPGLSTAGSLDLEAELEEIQQQLLHYQTTKQNLWSCRRQASSLRRWLELNREEPGPEDQEVEQQVQKELEQVEMQIQLLAEELQAQRQPIGACVARIQALRQALC
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Plays a role in the dynamic structure of centrosome-associated contractile fibers via its interaction with CETN2.
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A8K8V0
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ZN785_HUMAN
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Zinc finger protein 785
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MGPPLAPRPAHVPGEAGPRRTRESRPGAVSFADVAVYFSPEEWECLRPAQRALYRDVMRETFGHLGALGFSVPKPAFISWVEGEVEAWSPEAQDPDGESSAAFSRGQGQEAGSRDGNEEKERLKKCPKQKEVAHEVAVKEWWPSVACPEFCNPRQSPMNPWLKDTLTRRLPHSCPDCGRNFSYPSLLASHQRVHSGERPFSCGQCQARFSQRRYLLQHQFIHTGEKPYPCPDCGRRFRQRGSLAIHRRAHTGEKPYACSDCKSRFTYPYLLAIHQRKHTGEKPYSCPDCSLRFAYTSLLAIHRRIHTGEKPYPCPDCGRRFTYSSLLLSHRRIHSDSRPFPCVECGKGFKRKTALEAHRWIHRSCSERRAWQQAVVGRSEPIPVLGGKDPPVHFRHFPDIFQECG
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May be involved in transcriptional regulation.
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A8KBF3
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PIWL2_XENTR
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Piwi-like protein 2 (EC 3.1.26.-)
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MDPTRPPFRGSPFHTPLGVRPPVLETKEEGPHGRAVLLPRGRALLGASAPSSDTTQRDPSDSRNVLPALFRGMGIETKPSGIPGRGGPVFGRGFLSTMSSGDGPDQPLSEPSIRPSLSTRVQQASDFSTERVALGRARFPIPPVSMEKPHVPTGRGLLFPSVLPTLTSDPVPKESPIATLQIEKEEKWEPLPKKGSKGSPCQLGLNLIKINFQNEAVYQYHVTFTPIVECRSMRFGMMKDHRSVTGPVTAFDGSILYLPVKLAQTVELESERRTDGQKIKITIQMTKILDPSSDLCLPFYNVVMRRVFKILDLKLVGRNFYDPASSTVLQQYRLQVWPGYAANIRKTDGGLFLLVDITHKIIRSDSVLDIMNILYQQSPENFQDEVTKQLVGSIVITRYNNRTYRIDDIEWNMSPKDSFSMSDGSKISFIDYYSKNYGITVKELDQPLLLHRPSERKAPKGKALDIVLLLPELAFMTGIPEKMRKDFRAMKDLTQQIHLSPKQHHISLGKLLKRIESSADAKNELQRWGLFLDTDIHMTTGRILPIEKINLRNNSFPAGEDLNWNREVTREACRSSVHLLYWAMIYPKRASAQAQELSSMLERIGGPIGIRVNHPNCVELRDDRVETYARSIKSLLEGEGKVQLLVCLISGTRDDLYGAIKKLCCVQNPVPSQVINTRTISQPQKLRSIAQKILLQINCKLGGELWGVDIPLKSVMVIGMDVYHDPSRGMRSVLGFVASINSCLTAWYSRVVFQLPNQEIMDSLKLCLVAALQKFFEVNHSLPEKIVVYRDGVSDGQLNTVENYEIPQLQTCFQTFDNYNPRMVVIVVQKRVSTNLYSTATGQFLTPQPGTVIDHTVTNRKWIDFFLMSHHVRQGCGIPTHYICVMNTANLGPDHLQRLTFKLCHMYWNWPGTIRVPAPCKYAHKLAFLSGQFLHHEPSIKLCDKLFFL
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Endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Plays an essential role in meiotic differentiation of spermatocytes, germ cell differentiation and in self-renewal of spermatogonial stem cells. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. During piRNA biosynthesis, plays a key role in the piRNA amplification loop, also named ping-pong amplification cycle, by acting as a 'slicer-competent' piRNA endoribonuclease that cleaves primary piRNAs, which are then loaded onto 'slicer-incompetent' piwil4. Piwil2 slicing produces a pre-miRNA intermediate, which is then processed in mature piRNAs, and as well as a 16 nucleotide by-product that is degraded. Required for piwil4/miwi2 nuclear localization and association with secondary piRNAs antisense. Represses circadian rhythms by promoting the stability and activity of core clock components BMAL1 and CLOCK (By similarity).
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A8KBH6
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KPCB_XENTR
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Protein kinase C beta type (PKC-B) (PKC-beta) (EC 2.7.11.13)
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MADPAACEPGEDTTTRFARKGALRQKNVHEVKEHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCETCMMNVHKRCVMNVPSLCGTDHTERRGRIHIKAEIREEVLTVTVGDARNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPTWNESFKFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELLKAGVDGWFKLLSQEEGEYFNVPVPPEGEEGNEELRQKFERAKIGPGTKAVEEKVVNPMPKVDNNETRDRMKVSDFNFLKVLGKGSFGKVILAERKGTDELYAIKILKKDVVIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYQIQQVGRFKEPHAVFYAAEIAIGLLFLHSKGIVYRDLKLDNVMLDSEGHIKIADFGMCKENMWDGVTTKTFCGTPDYIAPEIIAYQPYAKSVDWWAFGILLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKDHAFFRYIDWEKLERNEIQPPYKPKACGRNAENFDKFFTRHPPVLTPPDHEVIRNIDQSEFEGFSYVNSDFAKEEEKD
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Calcium-activated and phospholipid-dependent serine/threonine-protein kinase involved in various processes such as regulation of the B-cell receptor (BCR) signalosome, apoptosis and transcription regulation. Plays a key role in B-cell activation and function by regulating BCR-induced NF-kappa-B activation and B-cell survival. Required for recruitment and activation of the IKK kinase to lipid rafts and mediates phosphorylation of card11/carma1, leading to activate the NF-kappa-B signaling. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates isoform p66Shc of shc1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (andr)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation (By similarity).
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A8MPH9
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FOSLD_DROME
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Transcription factor kayak, isoforms D/sro (AP-1) (Fos-related antigen) (Dfos) (dFra)
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MIALKATEMQHNNNALQQQQQLQHQLLQQHQQQHQQQLQQQLNSPDNNYIWATTHNANISRNNAMLQLQQQQLRAPWITDCNKQHHINNNNSMNVNYNQQLTQQPQQQQQQTQYMQHNYNNYTQQQQQQHLVPATTSQSNSHFYQCNQQQQQQQFLAPTTTTAAVVVAAAHQQHQTQQQHQSQQQQQHQRQDYASLQMGRQLGNFETGQSVLTLTTPTLTPTTTRNIEDTLGHLLSDTQTDRVAGCAGFAVPKVLPNAIDVLGMGIPTGVSSLPLQQTFDLSLGQGSESEDSNASYNDTQMNEEQDTTDTSSAHTDSTSYQAGHIMAGSVNGGGVNNFSNVLAAVSSSRGSASVGSSNANTSNTPARRGGGRRPNRSTNMTPEEEQKRAVRRERNKQAAARCRKRRVDQTNELTEEVEQLEKRGESMRKEIEVLTNSKNQLEYLLATHRATCQKIRSDMLSVVTCNGLIAPAGLLSAGSSGSGASSHHNHNSNDSSNGTITGMDATLNSTGRSNSPLDLKPAANIDSLLMHIKDEPLDGAIDSGSSLDQDGPPPSKRITLPPMSTMPHVHLSTILTPTGASSGSLQTPITSTAPGGFGSAFPVTSNGSSINNINSIGNNMNSPTLNAHNKVPKERPNTLAFQRPLGQMHLTMANNKAGGPTQIQGVPIQTPSTGTFNFDSLMDGGTGLTPVSGPLVPNSSSTNKHPLELPTPTAEPSKLVSL
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Developmentally regulated transcription factor AP-1 binds and recognizes the enhancer DNA sequence: 5'-TGA[CG]TCA-3'. May play a role in the function or determination of a particular subset of cells in the developing embryo. It is able to carry out its function either independently of or in conjunction with Jra.
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A8MPR5
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FTSI2_ARATH
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Probable inactive ATP-dependent zinc metalloprotease FTSHI 2, chloroplastic (AtFTSHI2) (Protein EMBRYO DEFECTIVE 2083) (Protein FTSH INACTIVE PROTEASE 2)
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MACRFPLHSSSPSQFLSPENRQRLPRNYPSISCQNNSATNVVHEDGDDNDKAKTNQVNLLAIPITLTIISASLAKPSFAAAKVTERKRTQKKPQEALTLEQLKAWSKDLPVVSNRIPYTDILSLKAEGKLKHVIKPPNLSLRQKAEPVLVVLEDSRVLRTVLPSLEGNKRFWEQWDELGIDVQCVNAYTPPVKRPPVPSPYLGFLWKVPAYMLTWVKPKKESKRAAELKRMREDFKRQRKEEIETMKEERVMMEKTMKAQKKQQERKKRKAVRKKKYEESLREARKNYRDMADMWARLAQDPNVATALGLVFFYIFYRVVVLNYRKQKKDYEDRLKIEKAEADERKKMRELEREMEGIEEEDEEVEEGTGEKNPYLQMAMQFMKSGARVRRASNKRLPEYLERGVDVKFTDVAGLGKIRLELEEIVKFFTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERDATLNQLLVSLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIFIPKPGLIGRMEILQVHARKKPMAEDLDYMAVASMTDGMVGAELANIVEIAAINMMRDGRTELTTDDLLQAAQIEERGMLDRKDRSLETWRQVAINEAAMAVVAVNFPDMKNIEFLTINPRAGRELGYVRVKMDHIKFKEGMLSRQSILDHITVQLAPRAADELWYGEDQLSTIWAETSDNARSAARSLVLGGLSDKHHGLNNFWVADRINDIDVEALRILNMCYERAKEILGRNRTLMDEVVEKLVQKKSLTKQEFFTLVELYGSSKPMPPSILELRKIKRLELEEMVLKLDMTTARNSS
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Required for plastid development during embryogenesis. Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex.
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A8MPY1
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GBRR3_HUMAN
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Gamma-aminobutyric acid receptor subunit rho-3 (GABA(A) receptor subunit rho-3) (GABA(C) receptor)
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MVLAFQLVSFTYIWIILKPNVCAASNIKMTHQRCSSSMKQTCKQETRMKKDDSTKARPQKYEQLLHIEDNDFAMRPGFGGSPVPVGIDVHVESIDSISETNMDFTMTFYLRHYWKDERLSFPSTANKSMTFDHRLTRKIWVPDIFFVHSKRSFIHDTTMENIMLRVHPDGNVLLSLRITVSAMCFMDFSRFPLDTQNCSLELESYAYNEDDLMLYWKHGNKSLNTEEHMSLSQFFIEDFSASSGLAFYSSTGWYNRLFINFVLRRHVFFFVLQTYFPAILMVMLSWVSFWIDRRAVPARVSLGITTVLTMSTIITAVSASMPQVSYLKAVDVYLWVSSLFVFLSVIEYAAVNYLTTVEERKQFKKTGKISRMYNIDAVQAMAFDGCYHDSEIDMDQTSLSLNSEDFMRRKSICSPSTDSSRIKRRKSLGGHVGRIILENNHVIDTYSRILFPIVYILFNLFYWGVYV
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GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.
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A8MQ03
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CRTP1_HUMAN
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Cysteine-rich tail protein 1
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MDPQEMVVKNPYAHISIPRAHLRPDLGQQLEVASTCSSSSEMQPLPVGPCAPEPTHLLQPTEVPGPKGAKGNQGAAPIQNQQAWQQPGNPYSSSQRQAGLTYAGPPPAGRGDDIAHHCCCCPCCHCCHCPPFCRCHSCCCCVIS
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Component of the stratum corneum that may contribute to epidermal antimicrobial host defenses.
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A8MQ27
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NEU1B_HUMAN
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E3 ubiquitin-protein ligase NEURL1B (EC 2.3.2.27) (Neuralized-2) (NEUR2) (Neuralized-like protein 1B) (Neuralized-like protein 3) (RING-type E3 ubiquitin transferase NEURL1B)
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MGNTVHRTLPDPSPPARLLATRPCCGPGPERRPVLGEAPRFHAQAKGKNVRLDGHSRRATRRNSFCNGVTFTQRPIRLYEQVRLRLVAVRPGWSGALRFGFTAHDPSLMSAQDIPKYACPDLVTRPGYWAKALPENLALRDTVLAYWADRHGRVFYSVNDGEPVLFHCGVAVGGPLWALIDVYGITDEVQLLESAFADTLTPARLSQARFSACLPPSSHDAANFDNNELENNQVVAKLGHLALGRAPGPPPADAAAAAIPCGPRERPRPASSPALLEADLRFHATRGPDVSLSADRKVACAPRPDGGRTLVFSERPLRPGESLFVEVGRPGLAAPGALAFGITSCDPGVLRPNELPADPDALLDRKEYWVVARAGPVPSGGDALSFTLRPGGDVLLGINGRPRGRLLCVDTTQALWAFFAVRGGVAGQLRLLGTLQSSPATTTPSGSLSGSQDDSDSDMTFSVNQSSSASESSLVTAPSSPLSPPVSPVFSPPEPAGIKNGECTVCFDGEVDTVIYTCGHMCLCHSCGLRLKRQARACCPICRRPIKDVIKIYRP
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E3 ubiquitin-protein ligase involved in regulation of the Notch pathway through influencing the stability and activity of several Notch ligands.
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A8MQA5
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ESF13_ARATH
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EMBRYO SURROUNDING FACTOR 1.3 (Maternally expressed family protein 1.3) (Maternally expressed gene 1.3)
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MKSSHTTLICIIMLSLFALHECEKMEVKEIGRSSKIILPACMHETCSGGFSLKNDCWCCLRLKTKQARCWKEKEFPNAKELCFANCPPLE
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Maternally-contributed central cell peptide regulating suspensor development and correct auxin distribution in early developing embryos.
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A8MQL1
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TRF1B_ARATH
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TNF receptor-associated factor homolog 1b (Protein MUTANT SNC1-ENHANCING 13)
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MAEAVDEDSGVGRSLEESSNGQHSQAGEALSEWRSSGQVENGTPSTSPSYWDIDDDDDYGLKPSELYGQYTWKIPKFSEITKREHRSNVFEAGGYKWYILIYPQGCDVCNHLSLFLCVANYDKLLPGSFAILEAGWSQFAQFTISVLSQDLKKSKFSDTLHRFWKKEHDWGWKKFMELPKLKDGFIDESGCLTIEAKVQVIRERVDRPFRCLDCGYRRELVRVYFQNVEQICRRFVEEKRSKLGRLIEDKARWTSFGVFWLGMDQNSRRRMCREKVDVILKGVVKHFFVEKEVSSTLVMDSLYSGLKALEGQTKNMKARSRLLDAKQLPAPIVSVDKDMFVLVDDVLLLLERAALEPLPPKDEKGRQNRTKDGNDGEEVNKEADERDERRLTELGRRTVEIFILSHIFSTKIEVAHQEAIALKRQEELIREEEEAWLAETEQRAKRGAAEREKKSKKKQAKQKRNKNKGKDKRKEEKVSFATHAKDLEENQNQNQNDEEEKDSVTEKAQSSAEKPDTLGDVSDISDSVDGSADILQPDLEDRDSSSVLWDTDALEIHPPSSEGSSRGRGISISTPNGITEGKSHSTMDDSSSTCSNDSIRSGVTNGSYQGNSLNFRNQKSPNKGKNQQVKAMTDAHSLASETDDQPSTLGTDPKGQNYSSEASNVGESDWVVVSHIQEPEGSRNRIPVGRERKTVQSIVNSVDMDRPKEKSTAVLSSPRNVAKNPSPLTQTKPEKKSISTADGIPNRKVLATGPPSSSQVVLPSDIQSQTVGLRADMQKLSAPKQPPATTISRPSSAPIIPAMRPSPITVSSSVQTTTSLPRSVSSAGRLGPDPSLHNQQTYTPQSYKNAIVGNSLGSSSSSFNHHPSSHGVVPTTLPSSSYSQAPTSSYQSSFPYSQDGLLWTGRSPSSVNMGMYNNTYSPAVTSNRSLNHMDVQIAQQQAQSMMTDEFPHLDIINDLLEDEQCSNMVYNGSIFNPQPQVFNGQYSSYHGELLSGGRTRSFGEEGLHYMARGPYGTDGMMPRQWQMTNMDLSLPAMRSNGMEDGTSSAANYHHSYFGLDASNPSFTSGINGYTEFRPSNGH
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Functions redundantly with TRAF1A in the regulation of plant immune response. Contributes to the turnover of the nucleotide-binding domain and leucine-rich repeat-containing (NB-LRR) immune receptors SNC1 and RPS2. May associate with an E3 ubiquitin-protein ligase complex, which modulates ubiquitination and subsequent degradation of NB-LRR immune sensors to maintain their homeostasis. Functions redundantly with TRAF1A in the regulation of autophagosome formation. Required for SINAT1- and SINAT2-mediated ubiquitination and destabilization of ATG6. Functions as molecular adapter that helps to regulate autophagy by modulating ATG6 stability.
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A8MQN2
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LNK1_ARATH
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Protein LNK1 (Night light-inducible and clock-regulated 1)
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MSDLYIHELGDYLSDEFHGNDDGIVPDSAYEDGGQFPILVSNRKKRRNDDMGSGTNHLKSNTFIKREANMLGKNPWPEKDSGGSSVSRDTGTGKDVQDMTLEDTNTSDHGFNGGHVDVVENFSTGDPMLCDTSAATNDGVYNYSLNSIPDAENDLSFFDNGDKEKNDLFYGWGDIGNFEDVDNMLRSCDSTFGLDSLNNEGDLGWFSSAQPNEETAGAMTDDLKPDKMLENQRTAMLQVEDFLNNSEPNHAVEDEYGYTIEDDSAQGKSSQNVFDTSLQKKDILMLDVEANLEKKQTDHLHHLDGKSDGFSENSFTLQHSGISREIMDTNQYYPPSAFQQRDVPYSHFNCEQPSVQVSACESKSGIKSENKPSPSSASNESYTSNHAQSIESLQGPTVDDRFRKVFETRANLLPGQDMPPSFAANTKKSSKTDSMVFPDAAPIQKIGLENDHRKAATELETSNMQGSSCVSSVVDDISLEATSFRQLQQVIEQLDVRTKLCIRDSLYRLAKSAEQRHHGGNRPEKGAGSHLVTGEADKYAGFMDIETDTNPIDRSIAHLLFHRPSDSSLSSDNNVLSYKSHPMIPQPNSSPSLRIEKQEETTELRPEAEVVTSDNN
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Transcriptional coactivator necessary for expression of the clock genes PRR5 and TOC1. Antagonizes REV8 function in the regulation of anthocyanin accumulation. Involved in red light input to the clock. Activates clock-controlled genes with afternoon peak. Mediates light inhibition of hypocotyl elongation.
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A8MQY1
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NAC68_ARATH
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NAC domain-containing protein 68 (ANAC068) (Protein NAC WITH TRANSMEMBRANE MOTIF 1) (Protein NTM1-like 12)
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MMKGLIGYRFSPTGEEVINHYLKNKLLGKYWLVDEAISEINILSHKPSKDLPKLARIQSEDLEWYFFSPIEYTNPNKMKMKRTTGSGFWKPTGVDREIRDKRGNGVVIGIKKTLVYHEGKSPHGVRTPWVMHEYHITCLPHHKRKYVVCQVKYKGEAAEISYEPSPSLVSDSHTVIAITGEPEPELQVEQPGKENLLGMSVDDLIEPMNQQEEPQGPHLAPNDDEFIRGLRHVDRGTVEYLFANEENMDGLSMNDLRIPMIVQQEDLSEWEGFNADTFFSDNNNNYNLNVHHQLTPYGDGYLNAFSGYNEGNPPDHELVMQENRNDHMPRKPVTGTIDYSSDSGSDAGSISTTSYQGTSSPNISVGSSSRHLSSCSSTDSCKDLQTCTDPSIISREIRELTQEVKQEIPRAVDAPMNNESSLVKTEKKGLFIVEDAMERNRKKPRFIYLMKMIIGNIISVLLPVKRLIPVKKL
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Transcription activator activated by proteolytic cleavage through regulated intramembrane proteolysis (RIP) mediated by calpain or its functional homolog. Regulates cytokinin signaling during cell division.
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A8MR65
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FHL_ARATH
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Protein FAR-RED-ELONGATED HYPOCOTYL 1-LIKE
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MDDADKSCSPSLDHSDINDPMIVAVESLDTSKKRKLHAEESDLLPLPKHFCSEHQASLVNSSCPSSVIDYAECSYAMENTKTSDEASSSASFTGPSLYMFKDSIYSTGSSSSGYAATSSIEQCFSKVDHKTQEDTQDFTHMEFIYHDSEFAVEDLQEVLNPVESYILSSARWSVSNQDSKEATTKPTIDQEFEQYFSTLMM
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Can activate transcription (By similarity). Essential for light-regulated PHYA nuclear accumulation and subsequent PHYA phototropic signaling processes. PHYA-specific signal transducer in response to continuous FR lights. Mediates the association of PHYA with HFR1 and LAF1 in the nucleus in response to FR conditions. Contributes to inhibition of hypocotyl elongation in continuous blue light (B).
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A8MR93
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ALG12_ARATH
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Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase (EC 2.4.1.260) (Alpha-1,6-mannosyltransferase ALG12) (Asparagine-linked glycosylation protein 12) (EMS-mutagenized BRI1 suppressor 4)
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MPTDSKMAKFLQSYGYDLILGSVAAIYVVMAPYTKVEESFNVQSMHDILYHRHHLDSYDHLEFPGVVPRTFIGAFIVSVFASPVVSIISCLGFPKVYSLVAARLVLGCIILSTLRFFRIQIKKKFGNQVETFFVLFTSLQFHFLFYCTRPLPNILALGLVNLAYGNWLKGNFYPALSFLIFATVIFRCDTMLLLGPIGLELLLTKSISFWKALKYCVGTALLAVGLTIFVDSIMWKKFVWPEFEVFWFNSILNRSSDWGTHSIHWYFTSALPRSLLVAYPLSLLGTLVDRRVPFFIVPVLSFVILYSKLPHKELRFIISSVPMFNLSAAVAASRIYNNRKKTIWKLVNMVMLAFFAISAGCTVVTFMASYYNYPSGYALKRLHQIGHPANVAGEEWVHIDTFGAMNGISRFCEDDFPWRYSKEEEIVVEELRNRNFTYLVNEHSSVDGYKCLFYEEGFERLELRRGFPPIVLVKKAKVYLHREMKKEDPFHKKWPGC
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Required for N-linked oligosaccharide assembly. Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor dolichol-PP-Man(7)GlcNAc(2).
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A8MRD9
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PDS5D_ARATH
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Sister chromatid cohesion protein PDS5 homolog D (Precocious dissociation of sisters protein 5-D) (AtPDS5D)
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MTAIVGFDQLSKALIDAGTNLLSPPSSTDDLLTLLDETESLLKNVEQDQPLSMQSALIPSRNALVSVDLLSHPDSDVRVSVVSCLTEIVRITAPETPYSDDLMKEIFRLTIEAFEKLADASSRSYKKAEFVLDNVAKVKSCLVMLDLECYDLILQMFRNFFKFIRSDHPQLVFSSMELIMIAIIDETEQVSTDLLDSLLATVKKENQNVSPMSWSLAEKVLSRCARKLKPYIIEALKSRGTSLDMYSPVVSSICQSVFNTPKVHSPVNTKEHEEKLDLGHSRKENLSKSSSKRPARHETRGINEKEKVRNGNKSSLLKQSLKQVRSESTDAEITGKRGRKPNSLMNPEDYDISWLSGKRDPLKTSSNKKIQKKGSGGVSSLGKVPAKKTPLPKENSPATSSRSLTGSLKRSRVKMDESDYDSDSLSSPRLKKLASCFRDEEPNQEDDRKIGNSSKQTRSKNGLEKSQKTAKKKPVVEAKIVNSSGKRLSARSVAKRRNLERAPLDTLVPQSSKRKKMVSQVAARQLANESEEETPKSHPTRRRTVRKEVESDGFGEDLVGKRVNIWWPLDKTFYEGVIDSYCTRKKMHRVIYSDGDSEELNLTEERWELLEDDTSADEDKEIDLPESIPLSDIMQRQKVKKSKNVAVSVEPTSSSGVRSSSRTLMKKDCGKRLNKQVEKTREGKNLRSLKELNAETDRTAEEQEVSLEAESDDRSEEQEYEDDCSDKKEQSQDKGVEAETKEEEKQYPNSEGESEGEDSESEEEPKWRETDDMEDDEEEEEEEIDHMEDEAEEEKEEVDDKEASANMSEIEKEEEEEEEDEEKRKS
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Cohesin cofactor dispensable during the meiotic division but playing an important role in DNA repair by homologous recombination (HR) probably by helping SMC5/SMC6 complex. Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication (By similarity). Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair.
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A8MRX0
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GSOX5_ARATH
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Flavin-containing monooxygenase FMO GS-OX5 (EC 1.14.13.237) (Flavin-monooxygenase glucosinolate S-oxygenase 5)
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MAPARTRVNSLNVAVIGAGAAGLVAARELRRENHTVVVFERDSKVGGLWVYTPNSEPDPLSLDPNRTIVHSSVYDSLRTNLPRECMGYRDFPFVPRPEDDESRDSRRYPSHREVLAYLEDFAREFKLVEMVRFKTEVVLVEPEDKKWRVQSKNSDGISKDEIFDAVVVCNGHYTEPRVAHVPGIDSWPGKQIHSHNYRVPDQFKDQVVVVIGNFASGADISRDITGVAKEVHIASRSNPSKTYSKLPGSNNLWLHSMIESVHEDGTIVFQNGKVVQADTIVHCTGYKYHFPFLNTNGYITVEDNCVGPLYEHVFPPALAPGLSFIGLPWMTLQFFMFELQSKWVAAALSGRVTLPSEEKMMEDVTAYYAKREAFGQPKRYTHRLGGGQVDYLNWIAEQIGAPPGEQWRYQEINGGYYRLATQSDTFRDKWDDDHLIVEAYEDFLRQKLISSLPSQLLES
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Catalyzes the conversion of methylthioalkyl glucosinolates into methylsulfinylalkyl glucosinolates. Specific for 8-methylthiooctyl (8-MTO) glucosinolates.
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A8MS41
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CCR4D_ARATH
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Carbon catabolite repressor protein 4 homolog 4 (CCR4 homolog 4) (EC 3.1.13.4) (Protein HESPERIN) (AtHESP) (AtHesperin)
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MFSSTTLHHLPRPNLLLPRKVISRRMSTNPAIEPKVRKFESVEGVDIGSRNKSDGFFAIPLYLSKLVALYNCISLSRIGTSNENFVFSGIRFRLVSYNILAQVYVKSALLPHSPPACLKWKARSHAILSVLKNLQADFFCLQEVDEYDSFYRNNMDSLGYSGIYIQRTGQRKRDGCAIFYKPSCAELVTKERIEYNDLVDSIKADSVSCSEQKIETSNEGKDSRKDSRDLNDPLVRLKRDCVGIMAAFRINKPFQHIVIVANTHLYWDPELADVKLAQAKYLLSRLAQFKTLISDEFECTPSLLLAGDFNSIPGDMVYSYLVSGNAKPTETIEEEEAPVPLSSVYEVTRGEPKFTNCTPGFTNTLDYIFISPSDFIKPVSILQLPEPDSPDVVGFLPNHHHPSDHLPIGAEFEIRRE
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Acts as catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover (By similarity). Transcriptional regulator of circadian rhythms with poly(A)-degrading activity that affects the expression and rhythmicity of the clock core oscillator genes TOC1 and CCA1. Deadenylation may be a mechanism involved in the regulation of the circadian clock. May play a negative role in response against oxidative stress. Possesses magnesium-dependent poly(A)-specific exoribonuclease activity in vitro and is almost inactive with poly(U), poly(C) and poly(G) as substrates.
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A8MS68
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PLPD1_ARATH
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Dihydrolipoyl dehydrogenase 1, chloroplastic (ptLPD1) (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase 1) (Protein LIPOAMIDE DEHYDROGENASE 1) (Pyruvate dehydrogenase complex E3 subunit 1) (E3-1) (PDC-E3 1)
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MQSAMALSFSQTSFTRPNHVLGSSGSVFSTPRSLRFCGLRREAFGFSTSNQLAIRSNRIQFLSRKSFQVSASASSNGNGAPPKSFDYDLIIIGAGVGGHGAALHAVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSGRMRELQNEHHMKSFGLQVSAAGYDRQGVADHANNLATKIRNNLTNSMKAIGVDILTGFGSVLGPQKVKYGKDNIITAKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVPEWIAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINPRKIDYHTGVFASKITPARDGKPVLIELIDAKTKEPKDTLEVDAALIATGRAPFTNGLGLENVNVVTQRGFIPVDERMRVIDGKGTLVPNLYCIGDANGKLMLAHAASAQGISVVEQVSGRDHVLNHLSIPAACFTHPEISMVGLTEPQAKEKGEKEGFKVSVVKTSFKANTKALAENEGEGIAKMIYRPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVLDELFKAAKVESHATTRTGDAKIKLNTNQEDRKGRRRGGDDEKQPSVSKDLKDISTRPSSFFENISVGVLSLLSLIFV
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Lipoamide dehydrogenase is a component of the plastidial pyruvate dehydrogenase complex (PDC).
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A8MS85
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SPT61_ARATH
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Transcription elongation factor SPT6 homolog (AtSPT6)
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MARNAISDDEEDHELEDDDGEPVHGDPAEHDENDDEEDDDDVGNEYENDGFIVNDEDEEEEEEEDEERKDSDEERQKKKKKRKKKDEGLDEDDYLLLQDNNVKFKKRQYKRLKKAQREQGNGQGESSDDEFDSRGGTRRSAEDKIKDRLFDDVDVDDPPDDVGDEEDLVVEEDVVGSEDEMADFIVDEDDEHGPPKRGNSKKKKYRQGSDITAMRDANEIFGDVDELLTIRKKGLASNQRMERRLEDEFEPTVLSEKYMTGNDDEIRQLDIPERMQISEESTGSPPVDEISIEEESNWIYAQLASQLRESDGTFDGRGFSVNKDDIAKFLELHHVQKLEIPFIAMYRKEQCRSLLDTGDFDGANQGKKPETKWHKVFWMIHDLDKKWLLLRKRKMALHGYYTKRYEEESRRVYDETRLNLNQYLFESVIKSLKVAETEREVDDVDSKFNLHFPPGEIGVDEGQYKRPKRKSQYSICSKAGLWEVANKFGYSAEQLGLALSLEKLVDELEDAKETPEEMAKNFVCAMFENSLAVLKGARHMAAVEISCEPSVKKYVRGIYMENAVVSTSPTADGNTVIDSFHQFSGIKWLREKPLSKFEGAQWLLIQKGEEEKLLQVTFKLPENYMNRLISDCNEHYLSVGVSKYAQLWNEQRKLILEDALHAFLLPSMEKEARSLLTSRAKSRLLSEYGQALWNKVSAGPYQKKEMDINLDEEAAPRVMACCWGPGKPPNTFVMLDSSGEVLDVLYAGSLTSRSQNVNDQQRKKSDQDRVLKFMMDHQPHVVALGAVNLSCTRLKDDIYEVIFQMVEEKPRDVGHGMDDLSIVYVDESLPRLYENSRISGEQLPQQSGNVRRAVALGRYLQNPLAMVATLCGPGREILSWKLHPLENFLQLDEKYGMVEQVMVDITNQVGIDINLAASHDWFFSPLQFISGLGPRKAASLQRSLVRAGSIFVRKDLIMHGLGKKVFVNAAGFLRIRRSGLAASSSQFIDLLDDTRIHPESYSLAQELAKDIYDEDVRGDSNDDEDAIEMAIEHVRDRPASLRKVVLDEYLASKKRENKKETYSNIIRELSCGFQDWRIPFKEPSPDEEFYMISGETEDTIAEGRIVQASVRRLQNGRAICVLDSGLTGMLMKEDFSDDGRDIVDLADQLKEGDILTCKIKSIQKQRYQVFLICKESEMRNNRHQHNQNVDAYYHEDRNSLQLVKEKARKEKELVRKHFKSRMIVHPRFQNITADQATEYLSDKDFGESIVRPSSRGLNFLTLTLKIYDGVYAHKEIAEGGKENKDITSLQCIGKTLTIGEDTFEDLDEVMDRYVDPLVSHLKTMLNYRKFRKGTKSEVDDLLRIEKGENPSRIVYCFGISHEHPGTFILSYIRSTNPHHEYIGLYPKGFKFRKRMFEDIDRLVAYFQRHIDDPLQESAPSIRSIAAKVPMRSPADHGSSGGSGWGSSQSEGGWKGNSDRSGSGRGGEYRNGGGRDGHPSGAPRPYGGRGRGRGRGRRDDMNSDRQDGNGDWGNNDTGTADGGWGNSGGGGWGSESAGKKTGGGSTGGWGSESGGNKSDGAGSWGSGSGGGGSGGWGNDSGGKKSSEDGGFGSGSGGGGSDWGNESGGKKSSADGGWGSESGGKKSDGEGGWGNEPSSRKSDGGGGGW
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Transcription elongation factor that enhances the transcription elongation by RNA polymerase II (RNAPII) (By similarity). Plays an important role in regulating embryo apical and basal patterning during early embryogenesis, partly through negative regulation of the transcription factors PHABULOSA and PHAVOLUTA.
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A8MT69
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CENPX_HUMAN
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Centromere protein X (CENP-X) (FANCM-associated histone fold protein 2) (FANCM-interacting histone fold protein 2) (Fanconi anemia-associated polypeptide of 10 kDa) (Retinoic acid-inducible gene D9 protein homolog) (Stimulated by retinoic acid gene 13 protein homolog)
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MEGAGAGSGFRKELVSRLLHLHFKDDKTKVSGDALQLMVELLKVFVVEAAVRGVRQAQAEDALRVDVDQLEKVLPQLLLDF
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DNA-binding component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS (MHF heterodimer), crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. Stabilizes FANCM. In complex with CENPS and FANCM (but not other FANC proteins), rapidly recruited to blocked forks and promotes gene conversion at blocked replication forks. In complex with CENPS, CENPT and CENPW (CENP-T-W-S-X heterotetramer), involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression. As a component of MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a nucleosome-like structure. DNA-binding function is fulfilled in the presence of CENPS, with the following preference for DNA substates: Holliday junction > double-stranded > splay arm > single-stranded. Does not bind DNA on its own.
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A8MTA8
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CMI2B_HUMAN
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Ciliary microtubule inner protein 2B
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MAVASTFIPGLNPQNPHYIPGYTGHCPLLRFSVGQTYGQVTGQLLRGPPGLAWPPVHRTLLPPIRPPRSPEVPRESLPVRRGQERLSSSMIPGYTGFVPRAQFIFAKNCSQVWAEALSDFTHLHEKQGSEELPKEAKGRKDTEKDQVPEPEGQLEEPTLEVVEQASPYSMDDRDPRKFFMSGFTGYVPCARFLFGSSFPVLTNQALQEFGQKHSPGSAQDPKHLPPLPRTYPQNLGLLPNYGGYVPGYKFQFGHTFGHLTHDALGLSTFQKQLLA
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Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
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A8MTJ3
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GNAT3_HUMAN
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Guanine nucleotide-binding protein G(t) subunit alpha-3 (Gustducin alpha-3 chain)
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MGSGISSESKESAKRSKELEKKLQEDAERDARTVKLLLLGAGESGKSTIVKQMKIIHKNGYSEQECMEFKAVIYSNTLQSILAIVKAMTTLGIDYVNPRSAEDQRQLYAMANTLEDGGMTPQLAEVIKRLWRDPGIQACFERASEYQLNDSAAYYLNDLDRITASGYVPNEQDVLHSRVKTTGIIETQFSFKDLHFRMFDVGGQRSERKKWIHCFEGVTCIIFCAALSAYDMVLVEDEEVNRMHESLHLFNSICNHKYFSTTSIVLFLNKKDIFQEKVTKVHLSICFPEYTGPNTFEDAGNYIKNQFLDLNLKKEDKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF
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Guanine nucleotide-binding protein (G protein) alpha subunit playing a prominent role in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction. Transduction by this alpha subunit involves coupling of specific cell-surface receptors with a cGMP-phosphodiesterase Activation of phosphodiesterase lowers intracellular levels of cAMP and cGMP which may open a cyclic nucleotide-suppressible cation channel leading to influx of calcium, ultimately leading to release of neurotransmitter. Indeed, denatonium and strychnine induce transient reduction in cAMP and cGMP in taste tissue, whereas this decrease is inhibited by GNAT3 antibody. Gustducin heterotrimer transduces response to bitter and sweet compounds via regulation of phosphodiesterase for alpha subunit, as well as via activation of phospholipase C for beta and gamma subunits, with ultimate increase inositol trisphosphate and increase of intracellular Calcium. GNAT3 can functionally couple to taste receptors to transmit intracellular signal: receptor heterodimer TAS1R2/TAS1R3 senses sweetness and TAS1R1/TAS1R3 transduces umami taste, whereas the T2R family GPCRs act as bitter sensors. Functions also as lumenal sugar sensors in the gut to control the expression of the Na+-glucose transporter SGLT1 in response to dietaty sugar, as well as the secretion of Glucagon-like peptide-1, GLP-1 and glucose-dependent insulinotropic polypeptide, GIP. Thus, may modulate the gut capacity to absorb sugars, with implications in malabsorption syndromes and diet-related disorders including diabetes and obesity.
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A8MTJ6
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FOXI3_HUMAN
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Forkhead box protein I3
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MALYCGDNFGVYSQPGLPPPAATAAAPGAPPAARAPYGLADYAAPPAAAANPYLWLNGPGVGGPPSAAAAAAAAYLGAPPPPPPPGAAAGPFLQPPPAAGTFGCSQRPFAQPAPAAPASPAAPAGPGELGWLSMASREDLMKMVRPPYSYSALIAMAIQSAPERKLTLSHIYQFVADSFPFYQRSKAGWQNSIRHNLSLNDCFKKVPRDEDDPGKGNYWTLDPNCEKMFDNGNFRRKRKRRSEASNGSTVAAGTSKSEEGLSSGLGSGVGGKPEEESPSTLLRPSHSPEPPEGTKSTASSPGGPMLTSTPCLNTFFSSLSSLSVSSSVSTQRALPGSRHLGIQGAQLPSSGVFSPTSISEASADTLQLSNSTSNSTGQRSSYYSPFPASTSGGQSSPFSSPFHNFSMVNSLIYPREGSEV
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Transcription factor required for pharyngeal arch development, which is involved in hair, ear, jaw and dental development. May act as a pioneer transcription factor during pharyngeal arch development (By similarity). Required for epithelial cell differentiation within the epidermis (By similarity). Acts at multiple stages of otic placode induction: necessary for preplacodal ectoderm to execute an inner ear program (By similarity). Required for hair follicle stem cell specification (By similarity). Acts downstream of TBX1 for the formation of the thymus and parathyroid glands from the third pharyngeal pouch (By similarity).
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A8MTQ0
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NOTO_HUMAN
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Homeobox protein notochord
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MPSPRPRGSPPPAPSGSRVRPPRSGRSPAPRSPTGPNTPRAPGRFESPFSVEAILARPDPCAPAASQPSGSACVHPAFWTAASLCATGGLPWACPTSWLPAYLSVGFYPVPGPRVAPVCGLLGFGVTGLELAHCSGLWAFPDWAPTEDLQDTERQQKRVRTMFNLEQLEELEKVFAKQHNLVGKKRAQLAARLKLTENQVRVWFQNRRVKYQKQQKLRAAVTSAEAASLDEPSSSSIASIQSDDAESGVDG
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Transcription regulator acting downstream of both FOXA2 and Brachyury (T) during notochord development. Required for node morphogenesis. Is essential for cilia formation in the posterior notochord (PNC) and for left-right patterning acts upstream of FOXJ1 and RFX3 in this process and is required for the expression of various components important for axonemal assembly and function. Plays a role in regulating axial versus paraxial cell fate. Activates the transcription of ciliary proteins C11orf97 homolog, FAM183B and SPACA9 in the embryonic ventral node (By similarity).
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A8MTZ0
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BBIP1_HUMAN
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BBSome-interacting protein 1 (BBSome-interacting protein of 10 kDa)
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MLKAAAKRPELSGKNTISNNSDMAEVKSMFREVLPKQGPLFVEDIMTMVLCKPKLLPLKSLTLEKLEKMHQAAQNTIRQQEMAEKDQRQITH
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The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. Required for primary cilia assembly and BBSome stability. Regulates cytoplasmic microtubule stability and acetylation. {ECO:0000269|Ref.4}.
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A8MU46
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SMTL1_HUMAN
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Smoothelin-like protein 1
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MEQKEGKLSEDGTTVSPAADNPEMSGGGAPAEETKGTAGKAINEGPPTESGKQEKAPAEDGMSAELQGEANGLDEVKVESQREAGGKEDAEAELKKEDGEKEETTVGSQEMTGRKEETKSEPKEAEEKESTLASEKQKAEEKEAKPESGQKADANDRDKPEPKATVEEEDAKTASQEETGQRKECSTEPKEKATDEEAKAESQKAVVEDEAKAEPKEPDGKEEAKHGAKEEADAKEEAEDAEEAEPGSPSEEQEQDVEKEPEGGAGVIPSSPEEWPESPTGEGHNLSTDGLGPDCVASGQTSPSASESSPSDVPQSPPESPSSGEKKEKAPERRVSAPARPRGPRAQNRKAIVDKFGGAASGPTALFRNTKAAGAAIGGVKNMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLDVDDMVRLAVPDSKCVYTYIQELYRSLVQKGLVKTKKK
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Plays a role in the regulation of contractile properties of both striated and smooth muscles. When unphosphorylated, may inhibit myosin dephosphorylation. Phosphorylation at Ser-299 reduces this inhibitory activity (By similarity).
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A8MUP2
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CSKMT_HUMAN
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Citrate synthase-lysine N-methyltransferase CSKMT, mitochondrial (CS-KMT) (EC 2.1.1.-) (Methyltransferase-like protein 12, mitochondrial)
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MAALRRMLHLPSLMMGTCRPFAGSLADSCLADRCLWDRLHAQPRLGTVPTFDWFFGYDEVQGLLLPLLQEAQAASPLRVLDVGCGTSSLCTGLYTKSPHPVDVLGVDFSPVAVAHMNSLLEGGPGQTPLCPGHPASSLHFMHADAQNLGAVASSGSFQLLLDKGTWDAVARGGLPRAYQLLSECLRVLNPQGTLIQFSDEDPDVRLPCLEQGSYGWTVTVQELGPFRGITYFAYLIQGSH
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Protein-lysine methyltransferase that selectively trimethylates citrate synthase (CS) in mitochondria. Seems to conduct trimethylation in a highly distributive manner rather than in a processive manner, and thus introduces a single methyl group per binding event.
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A8MV65
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VGLL3_HUMAN
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Transcription cofactor vestigial-like protein 3 (Vgl-3)
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MSCAEVMYHPQPYGASQYLPNPMAATTCPTAYYQPAPQPGQQKKLAVFSKMQDSLEVTLPSKQEEEDEEEEEEEKDQPAEMEYLNSRCVLFTYFQGDIGSVVDEHFSRALGQAITLHPESAISKSKMGLTPLWRDSSALSSQRNSFPTSFWTSSYQPPPAPCLGGVHPDFQVTGPPGTFSAADPSPWPGHNLHQTGPAPPPAVSESWPYPLTSQVSPSYSHMHDVYMRHHHPHAHMHHRHRHHHHHHHPPAGSALDPSYGPLLMPSVHAARIPAPQCDITKTEPTTVTSATSAWAGAFHGTVDIVPSVGFDTGLQHQDKSKESPWY
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May act as a specific coactivator for the mammalian TEFs.
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A8MVW5
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HECA2_HUMAN
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HEPACAM family member 2 (Mitotic kinetics regulator)
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MGQDAFMEPFGDTLGVFQCKIYLLLFGACSGLKVTVPSHTVHGVRGQALYLPVHYGFHTPASDIQIIWLFERPHTMPKYLLGSVNKSVVPDLEYQHKFTMMPPNASLLINPLQFPDEGNYIVKVNIQGNGTLSASQKIQVTVDDPVTKPVVQIHPPSGAVEYVGNMTLTCHVEGGTRLAYQWLKNGRPVHTSSTYSFSPQNNTLHIAPVTKEDIGNYSCLVRNPVSEMESDIIMPIIYYGPYGLQVNSDKGLKVGEVFTVDLGEAILFDCSADSHPPNTYSWIRRTDNTTYIIKHGPRLEVASEKVAQKTMDYVCCAYNNITGRQDETHFTVIITSVGLEKLAQKGKSLSPLASITGISLFLIISMCLLFLWKKYQPYKVIKQKLEGRPETEYRKAQTFSGHEDALDDFGIYEFVAFPDVSGVSRIPSRSVPASDCVSGQDLHSTVYEVIQHIPAQQQDHPE
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Required during prometaphase for centrosome maturation. Following poly-ADP-ribosylation (PARsylation) by TNKS, translocates from the Golgi apparatus to mitotic centrosomes and plays a key role in the formation of robust microtubules for prompt movement of chromosomes: anchors AKAP9/CG-NAP, a scaffold protein of the gamma-tubulin ring complex and promotes centrosome maturation.
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A8MW92
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P20L1_HUMAN
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PHD finger protein 20-like protein 1
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MSKKPPNRPGITFEIGARLEALDYLQKWYPSRIEKIDYEEGKMLVHFERWSHRYDEWIYWDSNRLRPLERPALRKEGLKDEEDFFDFKAGEEVLARWTDCRYYPAKIEAINKEGTFTVQFYDGVIRCLKRMHIKAMPEDAKGQVKSQHPLSWCCPIDPAGSCNQSMGSEDWIALVKAAAAAAAKNKTGSKPRTSANSNKDKDKDERKWFKVPSKKEETSTCIATPDVEKKEDLPTSSETFGLHVENVPKMVFPQPESTLSNKRKNNQGNSFQAKRARLNKITGLLASKAVGVDGAEKKEDYNETAPMLEQAISPKPQSQKKNEADISSSANTQKPALLSSTLSSGKARSKKCKHESGDSSGCIKPPKSPLSPELIQVEDLTLVSQLSSSVINKTSPPQPVNPPRPFKHSERRRRSQRLATLPMPDDSVEKVSSPSPATDGKVFSISSQNQQESSVPEVPDVAHLPLEKLGPCLPLDLSRGSEVTAPVASDSSYRNECPRAEKEDTQMLPNPSSKAIADGRGAPAAAGISKTEKKVKLEDKSSTAFGKRKEKDKERREKRDKDHYRPKQKKKKKKKKKSKQHDYSDYEDSSLEFLERCSSPLTRSSGSSLASRSMFTEKTTTYQYPRAILSVDLSGENLSDVDFLDDSSTESLLLSGDEYNQDFDSTNFEESQDEDDALNEIVRCICEMDEENGFMIQCEECLCWQHSVCMGLLEESIPEQYICYICRDPPGQRWSAKYRYDKEWLNNGRMCGLSFFKENYSHLNAKKIVSTHHLLADVYGVTEVLHGLQLKIGILKNKHHPDLHLWACSGKRKDQDQIIAGVEKKIAQDTVNREEKKYVQNHKEPPRLPLKMEGTYITSEHSYQKPQSFGQDCKSLADPGSSDDDDVSSLEEEQEFHMRSKNSLQYSAKEHGMPEKNPAEGNTVFVYNDKKGTEDPGDSHLQWQLNLLTHIENVQNEVTSRMDLIEKEVDVLESWLDFTGELEPPDPLARLPQLKRHIKQLLIDMGKVQQIATLCSV
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Is a negative regulator of proteasomal degradation of a set of methylated proteins, including DNMT1 and SOX2. Involved in the maintainance of embryonic stem cells pluripotency, through the regulation of SOX2 levels (By similarity).
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A8MW95
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BECN2_HUMAN
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Beclin-2 (Beclin-1 autophagy-related pseudogene 1) (Beclin-1-like protein 1)
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MSSIRFLCQRCHQALKLSGSSESRSLPAAPAPTSGQAEPGDTREPGVTTREVTDAEEQQDGASSRSPPGDGSVSKGHANIFTLLGELGAMHMLSSIQKAAGDIFDIVSGQAVVDHPLCEECTDSLLEQLDIQLALTEADSQNYQRCLETGELATSEDEAAALRAELRDLELEEARLVQELEDVDRNNARAAADLQAAQAEAAELDQQERQHYRDYSALKRQQLELLDQLGNVENQLQYARVQRDRLKEINCFTATFEIWVEGPLGVINNFRLGRLPTVRVGWNEINTAWGQAALLLLTLANTIGLQFQRYRLIPCGNHSYLKSLTDDRTELPLFCYGGQDVFLNNKYDRAMVAFLDCMQQFKEEAEKGELGLSLPYGIQVETGLMEDVGGRGECYSIRTHLNTQELWTKALKFMLINFKWSLIWVASRYQK
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Involved in 2 distinct lysosomal degradation pathways: acts as a regulator of autophagy and as a regulator of G-protein coupled receptors turnover. Regulates degradation in lysosomes of a variety of G-protein coupled receptors via its interaction with GPRASP1/GASP1.
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A8MW99
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MEI4_HUMAN
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Meiosis-specific protein MEI4
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MDVQKWYLRTSKLALALAIIRSKPADKSSREYTEHLAMLLSEEQSKWRSKVEILEAEVMQLRQKLLVSRLCSGSFKSGYVSSQLEAQEPKSSESTLTSMEDSGCDLSNEQRTESSDLSQHFVESCTPTHFPPLPLVKRPCAILQNPLSSHMQFLQYLLELKNLTESGNLKRDLTHFEKDSSTVSDSVFQLLDGLITFYRNPKLPFSRFWTEAVGTLASLISDYNLSSHILKKCSKKLEEFEKTLLHAILGNNHINQFQVQHYVSQSLVTLGNCSLLRKSIISLLLSEVNGFADDLGAINQEQASYDVSRYENIFYLFWVLEQLLQKETEEGNTSSIGHDDQEIKKFLQKHDETIFQLSDAFPLFTFYLWRVGILLSSAQIETLRK
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Required for DNA double-strand breaks (DSBs) formation in unsynapsed regions during meiotic recombination. Probably acts by forming a complex with IHO1 and REC114, which activates DSBs formation in unsynapsed regions, an essential step to ensure completion of synapsis.
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A8MXD5
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GRCR1_HUMAN
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Glutaredoxin domain-containing cysteine-rich protein 1
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MLKREMKPESDRPRKVRFRIASSHSGRVLKEVYEDGQPSGSLDSECASICGIDGLGDSDGQQNGHIESEGDENENDQDSLLVLARAASEKGFGTRRVNILSKNGTVRGVKYKVSAGQALFNNLTKVLQQPSTDLEFDRVVIYTTCLRVVRTTFERCELVRKIFQNHRVKFEEKNIALNGEYGKELDERCRRVSEAPSLPVVFIDGHYLGGAEKILSMNESGELQDILTKIERVQHPHECPSCGGFGFLPCSVCHGSKMSMFRNCFTDSFKALKCTACNENGLQRCKNCAG
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May play a role in actin filament architecture in developing stereocilia of sensory cells.
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A8MXV4
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NUD19_HUMAN
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Acyl-coenzyme A diphosphatase NUDT19 (EC 3.6.1.-) (Nucleoside diphosphate-linked moiety X motif 19) (Nudix motif 19)
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MSSSLRPGPSRWRRAASIVLAAGWSRPETATPPSRPPPAEGFRLLLLQRSPHQGFMPGAHVFSGGVLDAADRSADWLGLFAPHHGPPRFGLGPAPFSRTAFPSLPDTDDHKTDNTGTLPEDVAFRICAVREAFEEAGVLLLRPRTSPPGPAPGPGLALEPPPGLASWRDRVRQDPRHFLRLCAHLDCTPDIWALHNWSAWLTPFLRGTTRRFDTAFFLCCLREPPPVYPDLAEVVGYQWSSPSEATESFLSKEIWLPPPQFYEVRRLANFASLSDLHKFCLGRALEGLERWLPIILLTADGMVHLLPGDELYLEDSDFLENLMSTEKKTEEIMKEGKQFHRIVTYHRHLYDIHVTVQPKYKHVYPKNSVVRKSHL
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Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (By similarity). Mediates the hydrolysis of a wide range of CoA esters, including choloyl-CoA and branched-chain fatty-acyl-CoA esters and at low substrate concentrations medium and long-chain fatty-acyl-CoA esters are the primary substrates (By similarity). Highest activity seen with medium-chain acyl-CoA esters and higher rates of activity seen with the unsaturated acyl-CoA esters compared with the saturated esters (By similarity). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity).
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A8MYU2
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KCNU1_HUMAN
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Potassium channel subfamily U member 1 (Calcium-activated potassium channel subunit alpha-3) (Calcium-activated potassium channel, subfamily M subunit alpha-3) (KCa5) (Slowpoke homolog 3)
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MFQTKLRNETWEDLPKMSCTTEIQAAFILSSFVTFFSGLIILLIFRLIWRSVKKWQIIKGTGIILELFTSGTIARSHVRSLHFQGQFRDHIEMLLSAQTFVGQVLVILVFVLSIGSLIIYFINSADPVGSCSSYEDKTIPIDLVFNAFFSFYFGLRFMAADDKIKFWLEMNSIVDIFTIPPTFISYYLKSNWLGLRFLRALRLLELPQILQILRAIKTSNSVKFSKLLSIILSTWFTAAGFIHLVENSGDPWLKGRNSQNISYFESIYLVMATTSTVGFGDVVAKTSLGRTFIMFFTLGSLILFANYIPEMVELFANKRKYTSSYEALKGKKFIVVCGNITVDSVTAFLRNFLRDKSGEINTEIVFLGETPPSLELETIFKCYLAYTTFISGSAMKWEDLRRVAVESAEACLIIANPLCSDSHAEDISNIMRVLSIKNYDSTTRIIIQILQSHNKVYLPKIPSWNWDTGDNIICFAELKLGFIAQGCLVPGLCTFLTSLFVEQNKKVMPKQTWKKHFLNSMKNKILTQRLSDDFAGMSFPEVARLCFLKMHLLLIAIEYKSLFTDGFCGLILNPPPQVRIRKNTLGFFIAETPKDVRRALFYCSVCHDDVFIPELITNCGCKSRSRQHITVPSVKRMKKCLKGISSRISGQDSPPRVSASTSSISNFTTRTLQHDVEQDSDQLDSSGMFHWCKPTSLDKVTLKRTGKSKYKFRNHIVACVFGDAHSAPMGLRNFVMPLRASNYTRKELKDIVFIGSLDYLQREWRFLWNFPQIYILPGCALYSGDLHAANIEQCSMCAVLSPPPQPSSNQTLVDTEAIMATLTIGSLQIDSSSDPSPSVSEETPGYTNGHNEKSNCRKVPILTELKNPSNIHFIEQLGGLEGSLQETNLHLSTAFSTGTVFSGSFLDSLLATAFYNYHVLELLQMLVTGGVSSQLEQHLDKDKVYGVADSCTSLLSGRNRCKLGLLSLHETILSDVNPRNTFGQLFCGSLDLFGILCVGLYRIIDEEELNPENKRFVITRPANEFKLLPSDLVFCAIPFSTACYKRNEEFSLQKSYEIVNKASQTTETHSDTNCPPTIDSVTETLYSPVYSYQPRTNSLSFPKQIAWNQSRTNSIISSQIPLGDNAKENERKTSDEVYDEDPFAYSEPL
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Testis-specific potassium channel activated by both intracellular pH and membrane voltage that mediates export of K(+). May represent the primary spermatozoan K(+) current. In contrast to KCNMA1/SLO1, it is not activated by Ca(2+) or Mg(2+). Critical for fertility. May play an important role in sperm osmoregulation required for the acquisition of normal morphology and motility when faced with osmotic challenges, such as those experienced after mixing with seminal fluid and entry into the vagina.
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A8MZ59
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LEUTX_HUMAN
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Paired-like homeodomain transcription factor LEUTX (Leucine-twenty homeobox) (Paired-like homeobox transcription factor LEUTX) (PRD-LIKE homeobox transcription factor LEUTX)
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MFEGPRRYRRPRTRFLSKQLTALRELLEKTMHPSLATMGKLASKLQLDLSVVKIWFKNQRAKWKRQQRQQMQTRPSLGPANQTTSVKKEETPSAITTANIRPVSPGISDANDHDLREPSGIKNPGGASASARVSSWDSQSYDIEQICLGASNPPWASTLFEIDEFVKIYDLPGEDDTSSLNQYLFPVCLEYDQLQSSV
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[Isoform 1]: Paired-like homeobox transcription factor involved in embryogenesis. May act as a regulator of embryo genome activation. Binds to a 36 bp DNA elements containing a 5'-TAATCC-3' sequence motif, referred to as EEA motif (EGA-enriched Alu-motif), present in the promoters of target genes activated in early embryos.
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A8NMB4
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ARO1_COPC7
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Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
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MAVADDTKADLLKVSILGKESIHCGFHLTPYIVQTVLTTLPSSTYVLITDDNIAKLHLNKFEEAFAKGIEKSAANPKPRFLSHVIPPGETSKSREGKARIEDFLLFHKCTRDSVILALGGGVIGDLVGFVAATFMRGVRFCQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPEYIFIDAAYLETLPTREFSNGMAEVVKTAAIWDEKEFTSLESRSAELFAAIQTPSTNYAGRTLETRSEAQKLLLSTIAASIGVKAHIVTIDERETGLRNLVNFGHSIGHAIEAVLTPTILHGECVSIGMILEAELSRQLGILTQVGVGRLTRCLKAYNLPTSLSAPLIASLPQASLLTVPRLLDIMRIDKKNSGTNKKIVLLKRIGETYEQKASIVEDKAIEKTLAEAVTVVPSIPTGNVKGSPGEVRMSTPGSKSISNRALVLAALAKGTCRLRNLLHSDDTQGAVFTWEDGGETLVVEGGEGTLTVPTPGKELYLGNAGTAARFLTTVCALAQPAPASVQPPSTNTVITGNARMKQRPIGPLVDALRANGCSIGYRESEGCLPLSIPPNSFKGGKIQLAASVSSQYVSSILLCAPYAQDANGVTLELVGGEVISQPYIDMTIAMMKTFGVEVTRRTDASGKLLDIYDIPRGTYVNPPVYNIESDASSATYPLAVAAITGTKCTIENIGSSSLQGDAKFAVEVLQKMGCEVHQTADETTVQGPPLGQLKAIEEVDMEVMTDAFLTASVLAAVANGGENKAMKITGIANQRVKECNRIRAMMDELAKFGVHTTEQELGLTIYAVPISQLKKNVSVHCYDDHRVAMAFSVLSTVVEGAIIEEKRCVEKTWPGWWDDLENKIGIKVEGVDLAGLRAESSSAGVKESKPIDNSSILLIGMRGTGKTHIGQLAAASLPGWSFVDADHYFESKLKTGVKDFVKNEGWEKFREEELAVLAELIGLGVDGKAVSSPSSYSKNHVISLGGGIVETPAARSLLKAYLAKGGRVVHITRPIDEIVRYLNVETARPAYEEPILDVWKRREPWYKECSGWEFGNVVVEAPQGQAQAANVEAGPGKTKCVKTLAGRNEVKRFFGHLAGINPNFTHGGSVEGQQRRTYFLCLTYPDVRHAFPYIDELTEGADALELRVDLLKDAKAPEAPFPSVAYVKDQVTALRRVTGLPIIYTVRTKAQGGAFPDGNAKEYKELVEAGVRLGVEYLDVEVASIFSDKEVADLSKRTKKAGSTLVIASWHDWSGKMQWDGEDVKRKYDEARKFGDLVKIVGKAEKLEDNFKLLSFVKSATSLPNSPPIIAINMSTLGQSSRILNTTFTPVSHPLLPTKAAPGQLSFKQIQQALHLLGLLPSKHFHLFGTPIAHSMSPTLHNTGFELLGLPFKYGLLESKEVDCKEVRDVISDKEGFGGASVTIPFKVDVIELLDELTESAKEIGAVNTIIPVHRSSINAQGQEETTRVLVGDNTDWVGIRVCITQRVSEGELRNENTSGLVIGAGGTARAAIYALQDLGVPVIYLFNRTKEKAEDLAKAFVGGADKKWNGQLVVLDKLGGGWGDVGVAPRVIVSTVPASATALPSASTAAIAGQVDKSTNQIVLPADVFAYTSGSAVVVDMAYKPAETPLLKLAKELKEEGNWACVQGLEVLLEQGYIQFEKWTGRRCPKEQVSTRVWEKYGEV
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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A8NS89
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GOB1_BRUMA
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Trehalose-phosphatase (EC 3.1.3.12) (Trehalose-6-phosphate phosphatase) (TPP)
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MTETVTDQGKQRSSKLQKNEAAKDEQVEGKGKETLESGTDKSAEQNSSLLVGQPDVIDNDNVQTVDDFKNLMYKMQETRRAIVFALLNEKDLTKDDVEILKRAYEKLTDNQTHSFQREMCTLTTKLSVNIGDETRGLEKDLKYLDALMNIRREEPNLLWPIIMSRVDLFSILANYHPKGKETFLKEYEDTVKFLKTFISSEAITGKKPIFITDWDGTMKDYCSQYATNLQPVYSAVGMTRFAASFTRISAVLTAGPLRGPGILDLTAMPIDGPVMFSGSWGREWWLSGKRVVHQDGITDEGFNALQRLDDEMKDLLHTSDYAPFALVGSGVQRKVDRLTLGVQTVCHHVTSELSNRYQMAVKERMHRVDPNSQILVFDPSTELEVEVVAHNSGIIWNKGNGVERLIKSLGDSLQSPGKILICGDTLSDIPMVRQAVKQNPDGVLAIFVGAKMSLREEVKQVIGDESRCCFVSCPDVIHAAMSQILNEHCIGK
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Catalyzes the hydrolysis of trehalose 6-phosphate to trehalose and phosphate prevents the accumulation of toxic levels of trehalose 6-phosphate.
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A8QCB2
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ARO1_MALGO
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Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
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MSQVSGGKVPSYHAPPFDSPLSGATIHELRCLDTKVQLGFHLVPHIAKTLITELPSSAYVLVTDTNLAKLGAIDKFRKAFEAIPGARLLVYELAPGEESKSRETKAAIEDWMLEHRLTRDTVVLACGGGVIGDLVGFVAATFMRGLKYVQIPTTLLAMVDSSVGGKTAIDHPHGKNLIGAFHQPRYVFIDAAWLLTLPEREFSNGMAEVIKTAAIWDAADFEKLESESASIRAAVMGDEARQQSAAQGHTLATRTSSQSLLLDVIRGSVGVKAHIVTIDEKETGLRNLVNFGHSVGHAIEAVLTPDILHGECVAVGMVLEAEIARLVHGLPQVAIGRLVRCLRLYNLPVTLADARIMALSKVRELTTARVLDIMRVDKKNAGAQKKIVLLSRIGATVEERASTVSDAMIERVLAPAMLVRESVSAPRPPLTIHTPGSKSVSNRALVLAALSGGTCRLRHLLHSDDTQVMMQALAQLRAADFAWEDNGATLVVHGQGGRVLASDEPVYLQNAGTAARFVTAVACLASSASCSGSDESSCHGVVHLTGNARMKQRPIGPLVDALRSNGARIDYVEQSNCLPLNVTASGALQGGRIELAADVSSQYVSAVLLCAPYAQNDVELALVGGKVISQPYIDMTIAMMQSFGVRVERVAEHVYRIPRTTYVAPSTYEVECDASSATYPLAIAAITGTTVTVPSLGRASLQGDAAFARKVLAPMGCQVEQNDVSTTVTGPPVGMLKALGAIDMESMTDAFITAAMLFAVATAPCDEYASSSTSASPSSTRITGIANQRVKECDRLRAVVTELAKLGVRAVEHDDGIEVFSTPISQLLPHASIYCYDDHRIAMAFSVLACVVPGAGTEIQEKRCVEKTWPSWWDVLGGPLNVPIAGARLNDALVSLVARSRQRGPPTPTTLYGRDASIVLIGMRASGKSHVGRSLAKLLHRTFVDADVVFSDMYDIGAFVQDHGWDAFRAEESRILESLLTQCSVGHVIALGGGVIESAASRALLARFREHVGPVVHIVRDFALIESFLATSDRPAYGEPLADVYARRLPLYAESSCMEAVNTGNDAALALSRQLRTPLGTPVPISPAFFLSLTFPRVQDAWSILDHASAGVDVLELRVDLLHADGQPSIDDVREQVALLRQYTSLPILYTVRSVSQGGRLPDEANEAYFALTRLGLRMGCEYVDIELTRPSDGIEELAQAKGQTRIVASFHDTSGTMHWMAPAMRRLYTRACVLGDIAKLVGFARTWQDSLDLESFRTRVAQEAPFPLIAINMQAAGQLSRIVNPLLTPVTHPALPVPAAPGQMSVRDIHHARHLLGLLPKRHFFLFGSPITHSQSPLIHNTAFELLGLPHVYARHETDSVDASVEALVRAGDFGGASVTIPHKLSIMQLLDSVSPHAQVIGAVNTIVPHRDETTGHMALHGENTDWRAIVDLVAKHDGGRTRACTALVIGAGGSARAALYAMHKLGASRILLYNRTFEKAVNLAEQVPVEWRVEPVDSLALAAKAKPNVIVSNVPAQGTSFTPGGADIVLPLDLLSSDGGVAIDMAYRPEITPLLTLAQQHQSWHGVRGIEILLAQAFHQFRLWTGLPPPCLDIETTVYAAYRAAAASM
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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A8QL52
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OXLA_BUNFA
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L-amino-acid oxidase (Bf-LAAO) (LAO) (EC 1.4.3.2)
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MNVFSIFSLVFLAAFGSCADDRRSALEECFREADYEEFLEIARNGLKKTSNPKHVVVVGAGMAGLSAAYVLAGAGHRVTLLEASDRVGGRVNTYRDEKEGWYVNMGPMRLPERHRIVRTYIAKFGLKLNEFFQENENAWYFIRNIRKRVWEVKKDPGVFKYPVKPSEEGKSASQLYRESLKKVIEELKRTNCSYILDKYDTYSTKEYLIKEGNLSRGAVDMIGDLLNEDSSYYLSFIESLKNDDLFSYEKRFDEISDGFDQLPKSMHQAIAEMVHLNAQVIKIQRDAEKVRVAYQTPAKTLSYVTADYVIVCATSRAVRRISFEPPLPPKKAHALRSIHYKSATKIFLTCTRKFWEADGIHGGKSTTDLPSRFIYYPNHNFTSGVGVIVAYVLADDSDFFQALDIKTSADIVINDLSLIHQLPKNEIQALCYPSLIKKWSLDKYTMGALTSFTPYQFQDYIETVAAPVGRIYFAGEYTATVHGWLDSTIKSGLTAARNVNRASQKPSRIHLINDNQL
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Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Is highly active against L-Tyr, L-Asp, L-Phe, L-Glu, L-Trp, L-His, L-Gln, L-Ile, L-Met, L-Leu and moderately active against L-Lys, L-Arg, L-Ala and L-Asn. Exhibits diverse biological activities, such as edema, inflammatory cell infiltration, cytotoxicity and apoptosis, as well as induction of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. This protein may also induce hemorrhage, hemolysis, and have antibacterial and antiparasitic activities.
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A8QL56
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VSP1_OPHHA
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Alpha- and beta-fibrinogenase OhS1 (EC 3.4.21.-) (Snake venom serine protease) (SVSP)
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MALIRVLASLLILQLSYAVTPFDRIIGGFECNEYEHRSLVHLYNSSGFFCSGTLLNHEWVLTAAHCNRDDIQIKLGVHNVSVNYEDEQIRVPKEKLCCHSTNNCTQLGQDIMLIRLNSSVNYSEHIAPLSLPSNRPSMGSVCRVMGWGLLTSPEVTFPKVPHCVDINILHIQVCQAAYPSMSENYLLCAGVLEGGKDSCKGDSGGPLICNREIQGIVSWGGFPCAQLLEPGVYTKVFDYIDWIEGIIAGNTSVTCPSDNF
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Snake venom serine protease that possesses potent fibrinogenolytic (on both alpha- (FGA) and beta-chains (FGB)) and amidolytic activities. Selectively cleaves Arg-|-Xaa or Lys-|-Xaa bonds.
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A8QW53
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OMT3_SORBI
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5-pentadecatrienyl resorcinol O-methyltransferase (EC 2.1.1.n7) (O-methyltransferase 3) (SbOMT3)
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MVLISEDSRELLQAHVELWNQTYSFMKSVALAVALDLHIADAIHRRGGAATLSQILGEIGVRPCKLPGLHRIMRVLTVSGTFTIVQPSAETMSSESDGREPVYKLTTASSLLVSSESSATASLSPMLNHVLSPFRDSPLSMGLTAWFRHDEDEQAPGMCPFTLMYGTTLWEVCRRDDAINALFNNAMAADSNFLMQILLKEFSEVFLGIDSLVDVAGGVGGATMAIAAAFPCLKCTVLDLPHVVAKAPSSSIGNVQFVGGDMFESIPPANVVLLKWILHDWSNDECIKILKNCKQAIPSRDAGGKIIIIDVVVGSDSSDTKLLETQVIYDLHLMKIGGVERDEQEWKKIFLEAGFKDYKIMPILGLRSIIELYP
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O-methyltransferase involved in the biosynthetic pathway of the phytotoxin sorgoleone, a potent broad-spectrum inhibitor active against many agronomically important monocot and dicot weed species. Substrate specificity for alkylresorcinols. Strong preference for a five carbons alkyl side chain.
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A8R3S4
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QEDH_PSEPU
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Quinoprotein ethanol dehydrogenase (QEDH) (EC 1.1.2.8) (Quinoprotein alcohol dehydrogenase (cytochrome c)) (Quinoprotein alcohol dehydrogenase (cytochrome c550)) (Quinoprotein alcohol dehydrogenase ADH I) (ADH I)
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MTIRSLPAALSPLSMAVQAVLLVSSLALAPAANAKPVTWEDIANDHLNTQNVLQYGMGTNAQRWSPLAMVNDKNVFKLTPAWSYSFGDERQRGQESQAIINDGVIYVTGSYSRVFALDAKTGRRLWTYNHRLPDNIRPCCDVVNRGAAIFGDKIYFGTLDARVIALNKDTGKVVWNKKFGDHSAGYTMTGAPTLIKDQKSGKVLLIHGSSGDEFGVVGQLYARDPETGEEVWMRPFVEGHMGRLNGKDSTPTGDVKAPSWPDDPTTETGKVESWSHGGGAPWQSASFDPETNTIIVGAGNPGPWNTWARTSKDGNPHDFDSLYTSGQVGVDPTTGEVKWFYQHTPNDAWDFSGNNELVLFDYKDKDGKQYKATAHADRNGFFYVVDRTNGKLKNAFPFVDNITWASHIDLKTGRPVENEGQRPAKPLPGETKGKPVEVSPPFLGGKNWNPMAYSQDTGLFYVPANHWKEEYWTEEVNYKKGSAYLGIGFRIKRMYEDHVGSLRAMDPTTGKVVWEHNERLPLWAGVLATKGNLVFTGTGDGYFKAFNAKTGEELWKFQTGSGIVSPPITWEQDGEQYIGVTVGYGGAVPLWGGDMAELTKPVAQGGSFWVFKIPAWDTKTAKR
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Catalyzes the oxidation of ethanol and other primary alcohols to the corresponding aldehydes, except methanol, which is not a substrate. Uses a specific inducible cytochrome c550, encoded by the adjacent gene in the locus, as electron acceptor (By similarity). Is a key enzyme of the carbon and energy metabolism during growth of P.putida on ethanol as the sole carbon and energy source. Displays lower activity on secondary alcohols, aldehydes and diols. Is not active with sugar alcohols such as glycerol and D-sorbitol. In vitro, reacts well with phenazine methosulfate (PMS) as an electron acceptor but not with NAD(P), potassium ferricyanide, or molecular oxygen.
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