entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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C6KFA3
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AGRG6_DANRE
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Adhesion G-protein coupled receptor G6 (G-protein coupled receptor 126) [Cleaved into: ADGRG6 N-terminal fragment (ADGRG6-NTF); ADGRG6 C-terminal fragment (ADGRG6-CTF)]
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MISFISGRWWRWKFQNTLAVFLLLICLSTSVAQSCQSSTSCNVVLTDSQGSFTSPCYPNDYPPSQSCNWTIQAPAGFIVQITFLDFELEEAQGCIYDRVVVKTGTSDAKFCGLTANGLTLNSTGNVMEVFFNSDFSVQKKGFHISYKQVAVTLRNQKVTMPKSSKTILRVSNSISIPVLTAFTVCFEIARTAQKATETIFTLSDAAGTSILAFEKTSNGMELFIGASYCSVDNLLTSSDITATMKPLCLTWTKSSGLIGVYFGGHYFSSICSASQIYTLQSGGLLQIAGKGSSSVSVDDQNLDGFIYNFRLWDHAMLSSELSALTCDTVGNVVDWDHSYWTIPGSSTQTDSTLSCSTAITTLSPGTAGCASGLGCPATLTVTITSIATTNIIPTNATTHEDIFYRSTLVVTDEQTPDRDATAIISQWLNQTFQNWMYRVYVDGISLQLITVLSRITTTRQTYLALLVYKNTTDVNLAEVEIESMLRSAPAIGNGLTLDSVTVNLMENCQADEFPVHYRWPESRPTVTQYVPCFPYKDRNASRTCMINRDNYTSFWALPDRGNCTNITSITVSQENAMDVAVQLADISNNGLSKEELTQVVTKVMELVNIAKINATLASTVVTIISNVMVSSEDAQKDASETALKAVDELVQKIEFDGPSLTISSKNLVVGVSALDTTNFNGSTLSAFIATNTTDPQIDFDSEAHNALAVVTLPPTLLQNLSLSQIEKVSRINFMFFGRTGLFQDHQNNGLTLNSYVVASSVGNFTIKNLQDPVRIEIAHLEYQKDPNPQCVFWDFNLQNYSGGCNSDGCKVGSDSNSNRTVCLCNHLTHFGILMDVSRAAELIDEKNNRVLTFITYIGCGISAIFSAATLLTYIAFEKLRRDYPSKILMNLSTSLLFLNMVFLLDGWLASYEIKELCVTVAVFLHFFLLTSFTWMGLESIHMYIALVKVFNTYIRRYILKFCIVGWGVPAAIVGIVLAVSKDSYGKNYYGKGKDGQGTSEFCWILNPVVFYVTCVAYFSIIFLMNVAMFIVVMIQICGRNGKRSNRTLREDILRNLRSVVSLTFLLGMTWGFAFFAWGPVSLAFMYLFTIFNSLQGLFIFVFHCALKENVQKQWRRYLCCGKLRLADNSDWSKTATNNTKKVSSDNLGKSLSSSSFGSTTANWTSKAKATLNPFARHSNADSTLQ
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G-protein coupled receptor which is activated by type IV collagen, a major constituent of the basement membrane. Couples to G(i)-proteins as well as G(s)-proteins. Essential for normal differentiation of promyelinating Schwann cells and for normal myelination of axons. Also plays a role in inner ear development.
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C6KI89
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CTSG2_MOUSE
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Cation channel sperm-associated auxiliary subunit gamma 2
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MVSRPAMSPVSPVWPRKPNLWAFWVLRLVLLLSLKSWAEDALQHCTWLLVLNKFEKVGLHLSKDRFQDHEPIDTVAKVFQKLTDSPIDPSENYLSFPYYLQINFSCPGQNIEELARKGHLMGMKPMVQINYMYSVNFYRWEMENVQILMEAAPMRSTGYCPAEAMCVLNWYTPMPFKNGSVVSSVDIYTNGIGPFVSKKRFYVNMNGFLKRDASGKSLFAIGYESLVLKSSHFRLSKSRPLWYTVNHAPVFILGGFYDEKSILFSDSNFQDYVLLELSIDSCWVGSFYCPILGFSATIHDAIATESTLFIRQNQLVYYFTGTYITLFDKSHGSSRWVRVLPSECIKRLCPVYASGNGSEYVLALTTGKNEGYIHIGTITDGLVSFEMVPDGWSVCEKLPGKNCSIDWATYIADERNLLLLVKIDSGQFYLVNFNTEFKTLNILYKIPEFIPEAKELDFLVLLDTVTYTNTPMTPKGLFFNTLNNMLYIWGNFILQSYNREEFIFLADFPKESTIKYMVNSFKGQMAVVTENEEIWYFLEGGYDVYQVVPSQGWETYHNLQKMQKSSFHSEDESLVSLFFEDGKLFQLVYLFDVGKERLVKRLLPVGTLMEYNLPKPFTVVNQGNYQAISFTHTCPFKEIHLIDVPKKHHASRTESYVALPPLVSESLGFHNNNTLAVYQGLVYYLLWLHSKYDKPYADPVHDPTWRWWQHKTKDKDYFFYLFSNRLAAEGIYINMNAYQKLYNMSGDYGIPDLFFLDKGNWFTITVVLLSHQDTFTSSDSQGPTINVDKKLAIAVTIADPECLSVTVTQDVLLNRNAVINKIKVIDKKRCSEQGMIGRNIKKTSMMLKVLGAPGNCIQRTYLGGIIQGFKVVPIFIGCPPGKRLAFDVSYTIMHSEEINKHYFDCVIKDAEMPCFLFRDLFQPFFLVQDLVTGDSGSFLGSYVLKVVGGGRTLNTIRDYTEEEIFRYNSPLDTTNSLIWKTKVERTTEDKKFYIMSHESPGVEWLCLENSPCYDIIPQSIYPPEFFFKLLVSNRGVDNSTYCDYKLTFIVHIHGLPLSSKRTSFIVMVSTSFFIALVVFYILFCLVWPHIVKAWVSLRWRINNIMASESYYTYASSTAGFSLQSHSFEGPSRAGSKEDNVQAKTA
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Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization.
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C6KIE6
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XLG2_ARATH
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Extra-large guanine nucleotide-binding protein 2 (Extra-large GTP-binding protein 2) (Extra-large G-protein 2)
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MAAVIRKLLPFPSPNPKRDNRESDDDDETSSGYRIEYSFASEYKGPLIANVPRALPVEVDQIPTALPVSFSSLRSGISYPVAPLVMTKDTKRPPDSGIEKKNGFVDSAAGSSVVLIGRDVVSGSSSSSSSKRLDVPEEVKSPADFRLSPSSPLSASAREEDHLDDDRVSDVGPRAVRFVEPFQSSECDESSYVSDGESIAATHRAERKGKRGSCYRCQLGNRFTEKEVCIVCDAKYCFNCVRRAMGAMPEGRKCQACIGYRIDESKRASLGKCSRMLKRHLTDSELRQVMNAEITCKANQLPSRLIIVNDKPLSEDELYTLQTCPNPPKKLKPGHYWYDKVAGYWGKIGEKPSQIISPNNSIGGYISEKVSNGDTEIYINGREITKPELTMLKWAGVQCEGKPHFWVDSDGSYREEGQKHPIGNIWSKKRAKIACAVFSLPVPPASSAVEPYDVPLYEQKMLNKLLLIGSEKGGATTIYKQARSLYNVSFSLEDRERIKFIIQTNLYTYLAMVLEAHERFEKEMSNDQSSGNVGDETSAKPGNSINPRLKHFSDWVLKEKEDGNLKIFPPSSRENAQTVADLWRVPAIQATYKRLRDTLPRNAVYFLERILEISRSEYDPSDMDILQAEGLSSMEGLSCVDFSFPSTSQEESLESDYQHDTDMKYQLIRLNPRSLGENWKLLEMFEDADLVIFCVSLTDYAENIEDGEGNIVNKMLATKQLFENMVTHPSLANKRFLLVLTKFDLLEEKIEEVPLRTCEWFEDFNPLISQNQTSRHNPPMAQRAFHYIGYKFKRLYDSILEPVNMRGRSFKPKLFVCQVSLESDTVDNALRYAREILKWHVEETSMFQEMSTTSIEASSSS
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Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems (By similarity). Binds GTP with specificity. Plays a role in the root morphogenesis by regulation of the cell proliferation. Acts as a positive regulator in resistance to pathogen that triggers the salicylic acid (SA) pathway. Promotes the DNA binding activity of RTV1 specifically to promoter regions of FT and SOC1 in vivo leading to the activation of floral integrator genes. {ECO:0000250, ECO:0000269|PubMed:17999646, ECO:0000269|PubMed:19825634, ECO:0000269|PubMed:22232549}.
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C6KRL6
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ZHP3_CAEEL
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Zip homologous protein 3 (Zip3-homologous protein)
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MDFVHCNKCFNRKPPDGFFISSCFHIFCTKCAKADLAVCLICKKNVRLVRLDGNISSGIKIYFADPIKMVADSLAKIQKKIDFQQSTRDHLVKYLTKEKEKKRQMEVYFRTKGQEFDSQRKKLAEATAWIQMAEKKLQASEEERVKAEREIEECQAKLKSMTNLMSADTLGMNSQTPFPFSLAESQETAPSLVESSANSTFNMVSPLVSSPASSPNSINYNSFFENGSRTRPESLNEEAMFNTMLQSSGQSANANTSESSAFSVAFNNIFTPSRNNMGDSSMINKTTANQTIMDKTSMSLENWRQNRANSFGVHDISKRDSSLPTGGGSAIRVHHFKQNSRITPIAQNRRSAAGFDRQQIQEMRRISSQPGYLAQRKPINGRSFIGPAD
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Recruited co-dependently with zhp-4 to the synaptonemal complex between homologous chromosome pairs to regulate the formation and number of crossover events between homologs during meiotic recombination. In the early stages of pachytene, in complex with zhp-4, recruited by the zhp-1-zhp-2 heterodimer to designated crossover sites along the homolog pair to stabilize other pro-crossover factors such as rmh-1, msh-5 and cosa-1. This in turn facilitates crossover and promotes the formation of chiasma in each meiotic nucleus at the late pachytene stage of meiosis. Plays a role in the segregation of homologous chromosomes following the completion of crossovers. Together with him-14 and msh-5 plays a role in the activation of DNA damage-dependent apoptosis at the DNA damage checkpoint in pachytene cells.
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C6KRN1
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SAO1_CAEEL
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Suppressor of aph-1
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MHKNGNNGPVIDTKWHYLGPDSEKYGPYMSKDMLFWLQAGYFNDGLQLKTENEPNYHTLGEWSQLLGTHPFSMPVHSLDATIAQMNSMRPHGAMMMVPPGLQNQFQPPMPMRFPPFLPMPLLHQMNQNGPPMGAQMHSQPPSEPIDAGSLSHTPDSENETRLNEQTLQQPPSWLIALGLAGHGRKPHHHQQILAHQHIPQMQHANVATDQVVMKSVECQTEPVEISKEQASRVLSELLGQMVIIN
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Involved in negative regulation of early and late embryonic Notch signaling.
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C6KT50
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PDX1_PLAF7
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Pyridoxal 5'-phosphate synthase subunit Pdx1 (PLP synthase subunit Pdx1) (EC 4.3.3.6)
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MENHKDDAVLLKHGWCEMLKGGVIMDVKSVEQAKIAEEAGAIGVMVLENIPSELRNKEGVARSVDPSKVEEIKKCVSINVLAKVRIGHFVEAQILEELKIDMIDESEVLTIADEMHHIDKHKFKTPFVCGCTNLGEALRRISEGASMIRTKGEAGTGNIIEAIKHIRTVNNEIKYLCSLSDSEVYHFAKKINAPIDLVLLTKKLKRLPVVNFAAGGVATPADAAMCMQLGMDGVFVGSGIFESENPRKMAASIVSAVSNFNNPKILLDVSMNLGKAMCGSTRVSDKWKNKNEEHTKFLTPQ
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Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by Pdx2. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
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C6KT68
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FENR_PLAF7
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Ferredoxin--NADP reductase, apicoplast (EC 1.18.1.2)
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MKIRFVFILSVLISGVCCISKNVSRRVANRMTAHSRFLFVHDKYKRNKNFKLKNNKEENNFINLYTVKNPLKCKIVDKINLVRPNSPNEVYHLEINHNGLFKYLEGHTCGIIPYYNELDNNPNNQINKDHNIINTTNHTNHNNIALSHIKKQRCARLYSISSSNNMENLSVAIKIHKYEQTENAPNITNYGYCSGFIKNLKINDDIYLTGAHGYFNLPNDAIQKNTNFIFIATGTGISPYISFLKKLFAYDKNNLYNRNSNYTGYITIYYGVYNEDSILYLNELEYFQKMYPNNINIHYVFSYKQNSDATSFYVQDEIYKRKTEFLNLFNNYKCELYICGHKSIRYKVMDILKSHDQFDEKKKKRVHVEVY
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May play a role in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
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C6KTB8
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PK4_PLAF7
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Eukaryotic translation initiation factor 2-alpha kinase PK4 (eIF2alpha kinase PK4) (EC 2.7.11.1) (Protein kinase PK4) (PfPK4)
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MCNFIKKGIRFNGDKYIFLFDIFIKKYLLNVFVANILWEEENNICFLNRLKNKRKKSILFLKEEYLRYLMILNKEEKNKKKRLKKIYECIKVFSIKEFRWLINKLEIIYFYFFCHLLLLCIFQNIFLLTYMSKEYFLKNIHDYMINILSNDIKFNTCIEFTHNDKYEQKCITMAYYDFLLNKKGKLKKRNKYYDIKNIEPLTGKDKNLYSYYNFSPFFPMSSSDIINVNTNDKISNILWNDKYIDTLNHVNMKKKDIPLNIHSNNILMNNYAYRKYVRSYMIKKRINDLILYNLKNIFEKINNIEKLTNINNFMNFKKEYEKVSKEVCNNNNNNYDPSDYMLILPNSSKDHALYNNINNDEYMYKKFCNFISQAREIKKQREKEKCHRDEKCDRGENYDRGEKYDRDEKYDKEEKGLKEDNYRDVNEWNSNKSERCNKIYPSDYKFFLSEDKKYDTPYYSNERVDFHNSDIYMNDMDEELYYSSYHNNHHNNDITYNSNVYKRMLNEVIHPSVESNDVKKGPLNNDNIKNKESNVYEINDIIYQLNGEKKMNTNMCEKRGNKIFDSNNFHNINERKKKILDENDMITIDNNIDKKENILFPYFHMEILKDNEMNITKYYKDKQYYGQYKYDENIYIYDLIVLDTSGYIYKVSTDGSYHWKRKIVDHIQDYSNIEEKDDERKVLKKRNKLNEKDMYESNNKYESNMYDMNTYESNKYDINTYDKNISDSTKAHQNIYVLKKNVYDMNYDSKRALKISPYHNYFNTSIINSINRDKLKHSKPLYKNNIKTNDDNKKLRENKTKNKRLVSNYLGNLFYINENNEVIPLNINIKDVVNNSPFKSPLFPNMVFIGSRESTIINLDYDTGHVLRKYDEASNELLDKPPKKKSRKNKSIKNVKDINDNMKLYKEGSQNVEELSFTEEENKKKSILEGEKIEVASLNNEENMNKGFVCEKDDKINNYDNDEDDLFYEQYEDNNDNDNNKNDNNKNDNNKNDNNKNDNNNNNNNNNNNSYYYYNINGNASDDILVHSKNELLNNTYINKTNIKDENSNNNESFLNKIDGMNNFKLLPKRNMKRNRKKNLLKRLMVSTNKLSMLLNRYHLINRSLERMRKDIKRGKNKRILKKRQLQISLIKWVIKAVDENTLKKKWITTWVDVGSIFMTDVHRKDTSFINSLIEIVGNKLILRPIEKDKMKSTTYQILKIMNNDTDEIQMYRNEDMKYEVINNVDDINNVDNINNANNMNNVNNINNMNNMNNMNNMNNMNNMNNINNMNNINNMNNINNINNINNMNNILNDRLKNRINNKDNSNIKSKIFIFSESISSVFAVKYKNLSNIFTLDIIAKPNIKLYSDYDNLNNFTYNPVHVKKERTLFLPFSKDISDLDGDKFSCSFEDNIIYGKRLIHRLNSISVNISSIEKDMKYLLSNIIYVYDKNKRIPISYIYDMKNLIYEYQKVKQEFLYHLPWDEGDQKYLSRTDDVLNNSIIDNIGKKGPIFICEYINKFMDLYFEENDICYDYCSMLNIWDKIFNNTVSDGDSLLLSNLYRVVHNAFKNNNKYNNNNIYFDNNINININSSSSSSSRSRRNIYNFDNYYNNRRDYNSFWEDRHNILMNRENFLINTSTDKVFSGGKNNELKEFTSIRYKRRRWYWRVFYTIMFIIFFPVLFIYRRIIKRRKGSSKGNKIGTSSNNKLIKKNRTFKDYEDDENNIMSEDEEDDLDMNYDLIFDDDRLKVKKIKRMRKNYNNNNNNNNNKNNNNISNNNSNSNSKSNRFLSKLSNIDLANIDLNLIKKSHGKKMDNFEQPTLVDILARHARDSTHNDGVSYYPFNENETYNMLSLNYAWGGNHKHMNVERTSEYNMGNISHQLNYNNIRNLGDNKISAYELDIYEKELFHLYRRRAASQDVLNKKSFVMKKRIRSSYKVGSSNKYHKKNYTDNEKDKKKYRSYKEKHINEKMFDKKEFLNFLTNFNKKFMKKNSLVDHLIKMNDKAEDNYDGYNSSGSRYNNINDDGVELCGTKRYTNNKNNSDYDNYNNNNNMKNKRYSNKKHNNDNIIINNNNNKYTDERKYRNKSIKEDVDYTNDYYNIQLNNNKINNNQTKNKIDTIRNISHEKLGNNKSSSARNLSLIQTSHIPYDAPLADFLENGRFLRTFENISLIGQGGFGSVYKVSHRLEPGSPTYAVKFIYLKVSSLDNVSSRRYFREIAANRDIYSKHVVRYYTWWCEEPQFLPMHLMPKEIQNLVKKNKDTFKKRLTKNKKYSNNCISDSSNNNNSSCYSASSYNSSINSNYRNMKLWIKKKEQSPDMKRYKEVLRKNNAPNLVFYSDNDGLTSKNKENPEKNHNPFLSDKNFSDSIYKKKKSHDYNSSSHKLKKRKNKKKKSKKKRKSKSKIKTNAQGIYEESENDEGRDHFQYKKGKEQFSKFIGKHNSMGFTQSFQEYDPFDNGYLSEEDRDLIVFADNEESNGNDQQMIRHDNMNNENVIIKHRNEDDKNGLDGDKNGLDGDKNGLDGDKNGLDGDKNGLDGDKNELDGDKNGLDGDKNGLDGDKNGLDGDKNELDDNTKKLDDNTKKLDDLLMKQKINSLTRNDIVNIENENPAPHATNNIKNKKVDLNGELTYYDYVGKNEVIPNSRTETNVESINTNGMFNNKFSVMKDEGGEYKKKENMTWGDTKRDGLYENGKHEKDGLGVNKCITNKYIENDDDDDDDDDNNNNNNNIDERKKDLKKKQKNAITKGNEDLLATNGTNNKEKRKKDDDINKNMEKIKSYKKKTPVPEFSIVLLLQMELCKGYTLRKWLDRSTRSDKPLHFTYSDKKMNHPLEFDLFKQLIKGLKDIHATCFIHRDLKPENIFVDPDTYTLKIGDLGLVRFIEEKKREKDFNNIDCYKDNIYTDINQNAITSQISIKGQIIGTPGYTAPEGGALCDEKADIYSAALILLELLCPRFTTIMERYKRLNDFRNYYTVPDYVKIHLNPWYILMLQMSKPNPADRPSAADVYSKIKVLLDPHLTDFAFSFNDIHNEHMNKPPQGTNNFERITDNKDKFVIQSVVDMKNKVENEEIPIEKGLNSNVENIKNENNGADK
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During the asexual blood stage, phosphorylates translation factor eIF2alpha in late schizonts resulting in protein translation inhibition. Plays a role in trophozoite differentiation into schizonts.
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C6XZB6
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HEPB_PEDHD
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Heparin and heparin-sulfate lyase (Heparin lyase) (EC 4.2.2.7) (Heparin-sulfate lyase) (EC 4.2.2.8) (Heparinase II) (HepII)
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MKRQLYLYVIFVVVELMVFTTKGYSQTKADVVWKDVDGVSMPIPPKTHPRLYLREQQVPDLKNRMNDPKLKKVWADMIKMQEDWKPADIPEVKDFRFYFNQKGLTVRVELMALNYLMTKDPKVGREAITSIIDTLETATFKPAGDISRGIGLFMVTGAIVYDWCYDQLKPEEKTRFVKAFVRLAKMLECGYPPVKDKSIVGHASEWMIMRDLLSVGIAIYDEFPEMYNLAAGRFFKEHLVARNWFYPSHNYHQGMSYLNVRFTNDLFALWILDRMGAGNVFNPGQQFILYDAIYKRRPDGQILAGGDVDYSRKKPKYYTMPALLAGSYYKDEYLNYEFLKDPNVEPHCKLFEFLWRDTQLGSRKPDDLPLSRYSGSPFGWMIARTGWGPESVIAEMKVNEYSFLNHQHQDAGAFQIYYKGPLAIDAGSYTGSSGGYNSPHNKNFFKRTIAHNSLLIYDPKETFSSSGYGGSDHTDFAANDGGQRLPGKGWIAPRDLKEMLAGDFRTGKILAQGFGPDNQTPDYTYLKGDITAAYSAKVKEVKRSFLFLNLKDAKVPAAMIVFDKVVASNPDFKKFWLLHSIEQPEIKGNQITIKRTKNGDSGMLVNTALLPDAANSNITSIGGKGKDFWVFGTNYTNDPKPGTDEALERGEWRVEITPKKAAAEDYYLNVIQIADNTQQKLHEVKRIDGDKVVGVQLADRIVTFSKTSETVDRPFGFSVVGKGTFKFVMTDLLPGTWQVLKDGKILYPALSAKGDDGALYFEGTEGTYRFLR
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Cleaves both heparin and heparan sulfate glycosaminoglycans through a beta-elimination mechanism. Cleaves heparin at alpha-D-GlcNp2S6S(1->4) alpha-L-IdoAp2S and heparan sulfate at alpha-D-GlcNp2Ac(or 2S)6OH(1->4)beta-D-GlcAp.
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C6ZJZ3
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IF4E1_SOYBN
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Eukaryotic translation initiation factor 4E-1 (eIF4E-1) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein)
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MVVEDTQKSVITEDQYPSRVVSDNNNDDDDDDLEEGEIPVDGEDSGATATTKPPAALARNPHPLENSWTFWFDNPSSKSKQAAWGSSIRPIYTFATVEEFWSIYNNIHHPSKLGLGADFHCFKHKIEPKWEDPICANGGKWTMTFPRGKSDTSWLYTLLAMIGEQFDHGDEICGAVVNVRSRQDKIAIWTKNASNEAAQVSIGKQWKEFLDYNDTIGFIFHEDAKKLDRGAKNKYVV
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Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses (e.g. soybean mosaic virus (SMV), bean common mosaic virus (BCMV) and watermelon mosaic virus (WMV), but not bean pod mottle virus (BPMV)).
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C7A2A0
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BALDH_ANTMA
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Benzaldehyde dehydrogenase, mitochondrial (EC 1.2.1.28) (2-phenylacetaldehyde dehydrogenase) (EC 1.2.1.39) (Acetaldehyde dehydrogenase) (EC 1.2.1.3)
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MAAHRFSSLLSRSVPLLSRGGKQSYLGRGVYRYGTAAAAALEEPIKPPVSVQYDKLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVVTALKNPAWL
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Component of the floral volatile benzenoid/phenylpropanoid (FVBP) biosynthetic pathway. Catalyzes the oxidation of benzaldehyde to benzoic acid (BA). Capable of oxidizing a broad spectrum of aliphatic aldehydes increased carbon chain length results in a decrease in its efficiency.
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C7AE94
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FAOMT_VITVI
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Flavonoid 3',5'-methyltransferase (EC 2.1.1.267) (Anthocyanin-O-methyltransferase) (VvAOMT)
|
MSSSSHRGILKTEALTKYLLETSAYPREHEQLKGLREATVEKHKYWSLMNVPVDEGLFISMLLKIMNAKKTIELGVFTGYSLLATALALPQDGKIIAVDPDKEAYQTGVPFIKKAGVEHKINFIQSDAMSVLNDLIADGKEEGTLDFAMVDADKENYLNYHELLLKLVRVGGIIAYDNTLWFGSVARSEEEEMMDFERAGRVHLMKLNKFLASDPRVELSHLSIGDGVALCRRLY
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Mediates O-methylation of anthocyanins. Anthocyanins are major pigments in grapes: at ripening initiation in red grapevine berries, the exocarp turns color from green to red and then to purple due to the accumulation and extent of methylation of anthocyanins. Catalyzes both 3' and 5' O-methylation of anthocyanins, with a preference for glycosylated substrates. Active on both anthocyanins and flavonols in vitro. Most active with delphinidin 3-glucoside but also acts on cyanidin 3-glucoside, cyanidin, myricetin, quercetin and quercetin 3-glucoside. Not able to methylate flavan type skeletons with chiral centers, such as catechins or dihydroquercetin.
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C7AJA4
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TUT7_TRYBB
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Terminal uridylyltransferase 7 (TUTase 7) (EC 2.7.7.52) (Mitochondrial editosome-like complex associated TUTase) (TbMEAT1)
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MNVAKREFIRGMMAHYRASLPPPEHSVVIHELQKRVLDIGMLAVNKAHVELFGSHVSGFCTPHSDADISLTYRNFSPWLQGMERVDEQNNKRMTRFGKEASAMGMEDVRYIRARIPVVQFTDGVTGIHCDVSIGNIGGVENSKILCAIRQVFPDFYGAYIHLVKAWGKAREVIAPERSTFNSFTVTTMALMVLQELGLLPVFSKPTGEFGELTVADAEMLLQEFKLPPIYDSLHDDDEKLGEAVFFCLQRFAEYYAKYDFSAGTVSLIHPRRHRTVYERVVRRHLELLGSRKRLEWEKHIAEHKEDGPLDENDFSASMQNETTQRPSNSPYVVEDFVNYVNCGRRVQASRVRHIQQEFNRLREMLIDKESELKFDEVFRESDTVPRFQGFEGVGTRDHRVKTFRPQ
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Terminal uridylyltransferase which, as part of the mitochondrial RNA editing core-like complex (RECC-like), is involved in the post-transcriptional editing of mitochondrial RNA, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA. Specifically, catalyzes the addition of U to single-stranded RNA with a preference for a 3'-terminal U and adds the number of Us specified by a guide RNA (gRNA) to precleaved double-stranded RNA editing substrates. Essential for insect and bloodstream developmental forms viability.
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C7ASJ5
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BGAL2_ARTSP
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Beta-galactosidase (Beta-gal) (EC 3.2.1.23)
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MGKRFPSGWFSPRVHPPRRQRSPMTNQATPGTASVWNNIEGIGFGGDYNPEQWPVSVRLEDLELMQEAGVNFLSVGIFSWALLEPAEGQYDFGWLDDVMDNLHGIGVKVALATATAAPPAWLVRKHPEILPVTADGTTLGPGSRRHYTPSSAVYRKYAAGITRVLAERYKDHPALALWHVDNELGCHVSEFYGEEDAAAFRLWLERRYGTIDALNAAWGTAFWSQHYGSFEEILPPGVAPSTLNPGQQLDFQRFNSWALMDYYRSLVAVLREVTPAVPCTTNLMASSATKSMDYFSWAKDLDVIANDHYLVAADPERHIELAFSADLTRGIAGGDPWILMEHSTSAVNWQPRNQPKMPGEMLRNSLAHVARGADAVMFFQWRQSFAGSEKFHSAMVPHGGRDTRVWREVVDLGAALQLLAPVRGSRVESRAAIVFDYEAWWASEIDSKPSIDVRYLDLLRAFHRSLFLRGVSVDMVHPSASLDGYDLVLVCTLYSVTDEAAANIAAAAAGGATVLVSYFSGITDEKDHVRLGGYPGAFRELLGVRVEEFHPLLAGSQLKLSDGTVSSIWSEHVHLDGAEAFQTFTGYPLEGVPSLTRRAVGTGAAWYLATFPDRDGIESLVDRLLAESGVSPVAEADAGVELTRRRSADGGSFLFAINHTRAAASVRASGTDVLSGERFTGTVEAGSVAVIAED
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Hydrolyzes p-nitrophenyl-beta-D-galactopyranoside (PNPG), o-nitrophenyl-beta-D-galactopyranoside (ONPG) and chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-gal), with highest activity against PNPG. Also acts on p-nitrophenyl-beta-D-glucopyranoside (PNPGlu) and o-nitrophenyl-beta-D-glucopyranoside (ONPGlu), but with significantly lower activity.
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C7AU21
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D27_ORYSJ
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Beta-carotene isomerase D27, chloroplastic (EC 5.2.1.14) (Protein DWARF-27)
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METTTLVLLLPHGGAGGVRPAAAATAKRSYVMRRCCSTVRAVMARPQEAPASAPAKKTETAAMMSTVQTETAAAPPATVYRDSWFDKLAIGYLSRNLQEASGLKNEKDGYESLIDAALAISRIFSLDKQSEIVTQALERALPSYILTMIKVMMPPSRFSREYFAAFTTIFFPWLVGPCEVMESEVEGRKEKNVVYIPKCRFLESTNCVGMCTNLCKIPCQKFIQDSLGMKVYMSPNFEDMSCEMIFGQQPPEDDPALKQPCFRTKCVAKQNHGVNCSI
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Involved in strigolactones biosynthesis by catalyzing the isomerization of the C9-C10 double bond in all-trans-beta-carotene leading to 9-cis-beta-carotene and providing the substrate for CCD7. Strigolactones are hormones that inhibit tillering and shoot branching through the MAX-dependent pathway, contribute to the regulation of shoot architectural response to phosphate-limiting conditions and function as rhizosphere signals that stimulate hyphal branching of arbuscular mycorrhizal fungi and trigger seed germination of root parasitic weeds.
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C7BKP9
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PATOX_PHOAA
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Toxin PAU_02230 (Photorhabdus asymbiotica toxin) (PaTox) [Includes: Protein N-acetylglucosaminyltransferase (Protein O-GlcNAc transferase) (EC 2.4.1.-) (PaToxG) (Tyrosine glycosyltransferase); Protein-glutamine amidohydrolase (EC 3.5.1.44) (Glutamine deamidase) (PaToxD) (Protein-glutamine glutaminase)]
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MKGIEGVIMLSHDILPEKLLVSEKKHENVGSYFSDDIGEQSEQTEVSHFNLSLDDAFDIYADISIENQQELKNKDNNTNIWSSLGRGDDDHNLKKIINDAFKEKLPQLMEYRRKGYNVIGLDKEGIKKLEGMLKAVPPEIQQPTMKNLYSAAQELLNTLKQHPLLPENQDMIQQSNLVIRNLSDALEAINAVSKVNQVEWWEEVHKTNKAQSDRLIAATLEELFFKVKDKRLPGSNDDYCQQEREETERKIKDLLLYDGYQLTAEHFKFGRLRKSLLAESRVTRLKLAEYLEKKSVGILTAARDAKMYAMKILLAQTRNNGFNAKDLINAGQVNDRLLSFQQYARHIRAVDGEIDGIILSNPLVVACIKETNDEPAHIKIARAILPVSEELGTVSKVLRETKEKVQPSKPKEELNHPHQDWWNRGDELWKYIKKTSWNIKETSVHVTQMVGYEASKTASRAKHKLKESSYSESINGAVKGTALLLLDEIQQAENRIRQIPQFAWDVQEAVEQHSSVIQRTAYPDELPELSELLNEQLKHEEARWQAVKKQSRDKLQELIAPITRLAQEKWAQDLYFQLGEELRKERQDRWKDIQQFDEIMAEAVGQFAEMARELDSEAVRLAEHGHSGGKELQEKVAKWLRDLSKLKGKVKAGVAKITGTSLDNFSRSGMLARGMSEWAEDLKQSYLQETLQEGSAVAAELFERTLMEVVEENRTHFAKESDPEAERFLKRLALALKHAAENTTVYPPTPEEILAGSRSLPEDIRHWAEKKVVSGAISAAFRGGFKLVTGTFSLPVRVVIRGAKTGGTLYRGVRAINRSVRLGQGPATQVKSKFINQELSKTAFRLTLSLSPLVAWGMAASITAGRLYNEKDYPEKIIKNIVIDLPEELLWIGGYAGINAAIRAHAEKAIQQAIQHALDEQADKLALRINKEIAGKSADVNVEIIPQETSVSPAETAQSTPEPLSDFASTSQLTMPELIDIQDNNSAQQPKVRRKRDVSVESEISIDNLNIINANTREDKVNSEIKSELRSELKRFENSDANSPMSDVERAIFIDLFLYKNKYEVSESQQDYKNTWLKFRRELESQENKEIKEYLRFRSIIEAYEIYDKKRLDDDTIPEAGTIIKEVIDFFQKLKKENPITFMKLAEAMVKFQYYYEEEDENEDRYFKMAEIYYFLNKTENEKKSKTFHLDIIDKYPNENNRLLDEFFLNKNNNNPDLDEIIYKLQSMQEKYRESYEMLSKVENIHQVLSDDSKNEENIFLDNRIIAAQVFDGSINISLQDKKKWLNRYDQIRNEEGSDGWKLMHIESILINLRRINTAINLTAMKSESALLLIDKLLNFQKKARENILHISETPHEDFTSYSQFKTRKELGNDDSKYYAQFDNYKDNHDAEKEAKEILSQVVARASLSFSELFDKVESIKLFSFVYKNRDGGAPLAAPGRTVVIKFPGKDTGGLVISNLFLRNHVKRISTKEMEDLKPLTEGMYTRATQHRSLGSYYHIGSQSEHTNALEILSGMNKEELKTHLKKQGIWFGEPALFSNEYPKQENTGHLENTTLKNAIIGVSTIQNNAAANYLRSTMYESTGWEKLGDRFIPFYEIGRRKHYDREYEINSEQLTLDIITSIAIAYPAARGIVATIRSSAIPSILKSGLRGSALFKSLSLELGKMGFNASKVFGGAVYELIEPYPINSHLNRHNVFNKVKDTAWEFHTDVGLKGGGLKDFIDRFTKEPKEITISGYKFKRIKYNQENFDTMQRMALDYAYNPDSKGKIAQAQQAYKTGKEDYNAPQYDNFNGLSLDKKIERYISPDTDATTKGVLAGKMNESIKDINAFQTAKDAQSWKKSANKANKVVLTPQNLYLKGKPSECLPESVLMGWALQSSQDAKLSKMLMGIYSSNDITSNPLYKSLKELHANGNASKFNASATSISNINVSNLATSETKLFPTEISSVRVDAPKHTMLISKIKNRENKIKYVFYDPNYGMAYFDKHSDMAAFFQKKMQQYDFPDDSVSFHPLDYSNVSDIKISGRNLNEIIDGEIPLLYKQEGVQLEGITPRDGIYRVPPKNTLGVQETKHYIIVNNDIYQVEWDQTNNTWRVFDPSNTNRSRPTVPVKQDTNGEWFKHSETGLKGGGPIDDIRKYIARKSAIKIFNQSINYSATKWPPEPIDKNIHMIWIGTKNISEKNIKLSIDTAKKNPDYNTSIIYDSGISGHEGAKKFMLEKFQDSNVNIIDFRKKSYFSQLKQEPSFAYYEQVIAENKYAQASDILRLLVLKYEGGIYKDIDDIQVKGFGSLTFPKGIGVMREYAPEAGKATAFPNTPIAVTKNNPIINKTLDLAVSNYQRGEKNVLKLAGPDVFTQALYQEIPGLDSKVLNAQLYQLELAKRQALGVPLEKPKNFADEQLTSAEKEKINRPYQSIRGLSGYVENGADHSWAVDTNIPSTSTQTSTIVTPLAPKTEMLPPVPSSSTKSSTSAPVLQEKISYNLATDIDATDYLNQLKQKTNINNKISSPAGQCESLMKPVSDFMRENGFTDIRYRGMFIWNNATEQIPMNHFVVVGKKVGKDYVFDVSAHQFENKGMPDLNGPLILAAEDWAKKYRGATTRKLIYYSDFKNASTATNTYNALPRELVLESMEGKTFITSPNWYQTFKRTHNIHPEVTVSDPATFSLNYSVNPTAENLSPPPPPPIPSHGQVPKTVTPPPPPMRSPLSLSQPLERLPANKTKPIGFNPGENKASFSKLEEAGKHYYKDDKSRQAAPVNTMSDFDNRYLSHTTEAPAPSNVAHLAPGNIYNTKVTAKGAEKPAYDIYISKDGESLITSSSYKVDDITTDSKFGKPLPYSEIMFNSLKKSGVDPKNLKRSVQASIENKVTQDVISAIGTRIQRGQVIRVSPTENPDAFYTLLGTDNCKATLHMLNQHAEEFGHKVVTSIEFKGTGYLVMNIGTSTQTSTIVTPPPMPGTSQLVQ
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Toxin that acts on host cells by modifying Rho proteins by tyrosine GlcNAcylation and heterotrimeric G alpha proteins by deamidation. Catalyzes the mono-O-GlcNAcylation of small GTPases of the Rho family (RhoA, RhoB, RhoC, Rac1, Rac2, Rac3, Cdc42) in eukaryotic host cells at the conserved tyrosine residue located in the switch I region (Tyr-32/34), using UDP-N-acetylglucosamine (UDP-GlcNAc) as the sugar donor other GTPases of the Rho, Ras or Rab families are not substrates. Tyrosine glycosylation inhibits Rho activation and prevents interaction with downstream effectors, resulting in actin disassembly, inhibition of phagocytosis, cell rounding, and toxicity toward insects and mammalian cells. Also catalyzes the deamidation of the catalytic glutamine in heterotrimeric G alpha proteins (Gi, Gq/11), which blocks GTP hydrolysis and arrests the G proteins in a permanent active state leading to activation of Rho GTPases. Thus, PaTox hijacks host GTPase signaling in a bidirectional manner by deamidation-induced activation and glycosylation-induced inactivation of GTPases.
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C7C422
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BLAN1_KLEPN
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Metallo-beta-lactamase type 2 (EC 3.5.2.6) (B2 metallo-beta-lactamase) (Beta-lactamase type II) (Metallo-beta-lactamase NDM-1) (Metallo-beta-lactamase type II) (New Delhi metallo-beta-lactamase-1) (NDM-1)
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MELPNIMHPVAKLSTALAAALMLSGCMPGEIRPTIGQQMETGDQRFGDLVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRVLVVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAAGIATYANALSNQLAPQEGMVAAQHSLTFAANGWVEPATAPNFGPLKVFYPGPGHTSDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMADKLR
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Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Does not confer resistance to the polymixin colistin or the fluoroquinolone ciprofloxacin.
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C7DLJ6
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OLHYD_ELIME
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Oleate hydratase (EC 4.2.1.53) (Fatty acid double bond hydratase) (Fatty acid hydratase)
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MNPITSKFDKVLNASSEYGHVNHEPDSSKEQQRNTPQKSMPFSDQIGNYQRNKGIPVQSYDNSKIYIIGSGIAGMSAAYYFIRDGHVPAKNITFLEQLHIDGGSLDGAGNPTDGYIIRGGREMDMTYENLWDMFQDIPALEMPAPYSVLDEYRLINDNDSNYSKARLINNKGEIKDFSKFGLNKMDQLAIIRLLLKNKEELDDLTIEDYFSESFLKSNFWTFWRTMFAFENWHSLLELKLYMHRFLHAIDGLNDLSSLVFPKYNQYDTFVTPLRKFLQEKGVNIHLNTLVKDLDIHINTEGKVVEGIITEQDGKEVKIPVGKNDYVIVTTGSMTEDTFYGNNKTAPIIGIDNSTSGQSAGWKLWKNLAAKSEIFGKPEKFCSNIEKSAWESATLTCKPSALIDKLKEYSVNDPYSGKTVTGGIITITDSNWLMSFTCNRQPHFPEQPDDVLVLWVYALFMDKEGNYIKKTMLECTGDEILAELCYHLGIEDQLENVQKNTIVRTAFMPYITSMFMPRAKGDRPRVVPEGCKNLGLVGQFVETNNDVVFTMESSVRTARIAVYKLLNLNKQVPDINPLQYDIRHLLKAAKTLNDDKPFVGEGLLRKVLKGTYFEHVLPAGAAEEEEHESFIAEHVNKFREWVKGIRG
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Catalyzes the hydration of oleate at its cis-9-double bond to yield 10-hydroxyoctadecanoate. The hydration of unsaturated fatty acids is suggested to be a detoxification mechanism and a survival strategy for living in fatty acid-rich environments.
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C7E9W0
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SCH21_STACH
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Antigenic protein SchS21 (21 kDa secretory protein) (Alkaline exodeoxyribonuclease) (EC 3.1.11.-) (SchS21) (allergen Sta c 3.0101)
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ASVTFWTLDNVDRTLVFTGNPGSAAIETITVGPAENTTVEFPGSWVGNWYAYPTDAEDVPGMLGEVQFGGWNGLTYFDVSAIVNPTDHDNVKQMWPAESRKPMSGCEVFPCDNAYWLPDDIQTKVTHEVDLWTTLGAGSTGLTF
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Has exodeoxyribonuclease activity with lambda-DNA and salmon testes dsDNA. No activity with circular plasmid DNA. The physiological role of this enzyme may be to degrade environmental DNA, and thus mobilize nitrogen for uptake.
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C7EXK4
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AT8A2_BOVIN
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Phospholipid-transporting ATPase IB (EC 7.6.2.1) (ATPase class I type 8A member 2) (P4-ATPase flippase complex alpha subunit ATP8A2)
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MSRATSVGDQLDVPARTIYLNQPHLNKFCDNQISTAKYSVVTFLPRFLYEQIRRAANAFFLFIALLQQIPDVSPTGRYTTLVPLIIILTIAGIKEIVEDFKRHKADNAVNKKKTIVLRNGMWQTIVWKEVAVGDIVKVVNGQYLPADVVLLSSSEPQAMCYVETANLDGETNLKIRQGLSHTADMQTREVLMKLSGTIECEGPNRHLYDFTGNLNLDGKSPVALGPDQILLRGTQLRNTQWGFGIVVYTGHDTKLMQNSTKAPLKRSNVEKVTNVQILVLFGILLVMALVSSVGALYWNGSQGGKNWYIKKMDATSDNFGYNLLTFIILYNNLIPISLLVTLEVVKYTQALFINWDTDMYYLGNDTPAMARTSNLNEELGQVKYLFSDKTGTLTCNIMNFKKCSIAGVTYGHFPELTREPSSDDFSRIPPPPSDSCDFDDPRLLKNIEDHHPTAPCIQEFLTLLAVCHTVVPERDGDSIVYQASSPDEAALVKGARKLGFVFTARTPYSVIIEAMGQEQTFGILNVLEFSSDRKRMSVIVRTPSGQLRLYCKGADNVIFERLSKDSKYMEETLCHLEYFATEGLRTLCVAYADLSERDYEEWLKVYQEASTILKDRAQRLEECYEIIEKNLLLLGATAIEDRLQAGVPETIATLLKAEIKIWVLTGDKQETAINIGYSCRLVSQNMALILLKEDSLDATRAAITQHCADLGSLLGKENDAALIIDGHTLKYALSFEVRRSFLDLALSCKAVICCRVSPLQKSEIVDVVKKRVKAITLAIGDGANDVGMIQTAHVGVGISGNEGMQATNNSDYAIAQFSYLEKLLLVHGAWSYNRVTKCILYCFYKNVVLYIIELWFAFVNGFSGQILFERWCIGLYNVIFTALPPFTLGIFERSCSQESMLRFPQLYKITQNAEGFNTKVFWGHCINALVHSLILFWFPMKALEHDTVLANGHATDYLFVGNIVYTYVVVTVCLKAGLETTAWTKFSHLAVWGSMLIWLVFFGIYSTIWPTIPIAPDMKGQATMVLSSAHFWLGLFLVPTACLIEDVAWRAAKHTCKKTLLEEVQELEMKSRVMGRAMLRDSNGKRMNERDRLLKRLSRKTPPTLFRGSSLQQSMPHGYAFSQEEHGAVTQEEIVRAYDTTKQKSRKK
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Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Able to translocate phosphatidylserine, but not phosphatidylcholine (By similarity). Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. Reconstituted to liposomes, the ATP8A2:TMEM30A flippase complex predominantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). Phospholipid translocation is not associated with a countertransport of an inorganic ion or other charged substrate from the cytoplasmic side toward the exoplasm in connection with the phosphorylation from ATP. ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth. Proposed to function in the generation and maintenance of phospholipid asymmetry in photoreceptor disk membranes and neuronal axon membranes. May be involved in vesicle trafficking in neuronal cells. Required for normal visual and auditory function involved in photoreceptor and inner ear spiral ganglion cell survival.
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C7F6X3
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IBP_LEUSY
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Ice-binding protein (Antifreeze protein) (AFP) (LeIBP)
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MSLLSIITIGLAGLGGLVNGQRDLSVELGVASNFAILAKAGISSVPDSAILGDIGVSPAAATYITGFGLTQDSSTTYATSPQVTGLIYAADYSTPTPNYLAAAVANAETAYNQAAGFVDPDFLELGAGELRDQTLVPGLYKWTSSVSVPTDLTFEGNGDATWVFQIAGGLSLADGVAFTLAGGANSTNIAFQVGDDVTVGKGAHFEGVLLAKRFVTLQTGSSLNGRVLSQTEVALQKATVNSPFVPAPEVVQKRSNARQWL
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Confers freeze tolerance. Binds to the surface of ice crystals and inhibits their growth. Has low thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point. The TH activity of this protein is approximately 0.2 degrees Celsius at 50 uM and 0.3 degrees Celsius at 400 uM.
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C7G3A0
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MPPE1_CRIGR
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Metallophosphoesterase 1 (EC 3.1.-.-) (Post-GPI attachment to proteins factor 5)
|
MALVRWRLRRGNFHLLSRVLLLKLTVVIISVLLFCEYFIYHLVIFQCHWPEVKTLAHGDRQKPVLKAMFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWWLQPEVIFILGDIFDEGKWSTTEAWADDVQRFRKIFRHGSHVQLKVVIGNHDIGFHYQMSKYRIKRFEKVFSSERLFSWKGVNFVMVNSVAMEGDGCSICSEAEAELREISRKLNCSREVQGSSQCEGEQRLPFSAPVLLQHYPLYRASDANCSGEDAAPPEERNVPFEEKYDVLSREASQKLLWWLQPRLVLSGHTHSACEVLHPGGVPEVSVPSFSWRNRNNPSFIMGSLTSKDYALSKCYLPFEDRVLATYGAAAVFLVVLILAHLERLPSSFLFGWKLRKMHMRG
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Metallophosphoesterase required for transport of GPI-anchor proteins from the endoplasmic reticulum to the Golgi. Acts in lipid remodeling steps of GPI-anchor maturation by mediating the removal of a side-chain ethanolamine-phosphate (EtNP) from the second Man (Man2) of the GPI intermediate, an essential step for efficient transport of GPI-anchor proteins.
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C7GIN5
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ARO1_YEAS2
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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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MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFKASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMIAIGGGVIGDMIGFVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAKREFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGAKNVKVTNQLTNEIDEISNTDIEAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYFGILSPTQVARLSKILVAYGLPVSPDEKWFKELTLHKKTPLDILLKKMSIDKKNEGSKKKVVILESIGKCYGDSAQFVSDEDLRFILTDETLVYPFKDIPADQQKVVIPPGSKSISNRALIIAALGEGQCKIKNLLHSDDTKHMLTAVHELKGATISWEDNGETVVVEGHGGSTLSACADPLYLGNAGTASRFLTSLAALVNSTPSQKYIVLTGNARMQQRPIAPLVDSLRANGTKIEYLNNEGSLPIKVYTDSVFKGGRIELAATVSSQYVSSILMCAPYAEEPVTLALVGGKPISKLYVDMTIKMMEKFGINVETSTTEPYTYYIPKGHYINPSEYVIESDASSATYPLAFAAMTGTTVTVPNIGFESLQGDARFARDVLKPMGCKITQTATSTTVSGPPVGTLKPLKHVDMEPMTDAFLTACVVAAISHDSDPNSANTTTIEGIANQRVKECNRILAMATELAKFGVKTTELPDGIQVHGLNSIKDLKVPSDSSGPVGVCTYDDHRVAMSFSLLAGMVNSQNERDEVANPVRILERHCTGKTWPGWWDVLHSELGAKLDGAEPLECTSKKNSKKSVVIIGMRAAGKTTISKWCASALGYKLVDLDELFEQQHNNQSVKQFVVENGWEKFREEETRIFKEVIQNYGDDGYVFSTGGGIVESAESRKALKDFASSGGYVLHLHRDIEETIVFLQSDPSRPAYVEEIREVWNRREEWYKECSNFSFFAPHCSAEAEFQALRRSFSKYIATITGVREIEIPSGRSAFVCLTFDDLTEQTENLTPICYGCEAVEVRVDHLANYSADFVSKQLSILRKATDSIPIIFTVRTKKQGGNFPDEEFKTLRELYDIALKNGVEFLDLELTLPTDIQYEVINKRGNTKIIGSHHDFQGLYSWDDAEWENRFNQALTLDVDVVKFVGTAVNFEDNLRLEHFRDTHKNKPLIAVNMTSKGSISRVLNNVLTPVTSDLLPNSAAPGQLTVAQINKMYTSMGGIEPKELFVVGKPIGHSRSPILHNTGYEILGLPHKFDKFETESAQLVKEKLLDGNKNFGGAAVTIPLKLDIMQYMDELTDAAKVIGAVNTVIPLGNKKFKGDNTDWLGIRNALINNGVPEYVGHTAGLVIGAGGTSRAALYALHSLGCKKIFIINRTTSKLKPLIESLPSEFNIIGIESTKSIEEIKEHVGVAVSCVPADKPLDDELLSKLERFLVKGAHAAFAPTLLEAAYKPSVTPVMTISQDKYQWHVVPGSQMLVHQGVAQFEKWTGFKAPFKAIFDAVTKE
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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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C7IVR4
|
PQN41_CAEEL
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Polyglutamine-repeat protein pqn-41 (Prion-like-(Q/N-rich)-domain-bearing protein 41)
|
MKPKKLQQGSDSAHTSDTESTKTCEKTAKKLPKTQKKLQKSKKTAKKRRDEEFRIFFPPPRVNPPIKTPFRLHNTNCEHRDWISDNLCLPKYASYQTGWRISHKSMKSLVLMDKRRAEWLKMHNLYRKSEIRKAIWTIERKGAKKLDEMPGNWRISREKRNSLDLQEFPIKIEQFPVKKREKTAKNWRKIAVLVCFKRKTTTKNRYLRRPKTKNQRKIEFRRPKTSKNRKLRLKIRPRVRFIDRKLIRRRECLVDPQNLISWIRRQEKAENLRIFQEKQKRLQEQQEDAEWEQIEAQRANSDDVIEDKSLKMEVLDIVKHKNRNWIVVEKKGCEIQGMEYLLVLESEFNEQQTVRYDRQNVDHKFRKMRDEKKEIVEFVSSLPFYKPKPPKINYPTNAGEYEEQEIELERRRLEEEERDQNDKKLEIEDRNHFKKWQKRRNLIKIYRNSIRREIWRRRRGRNSTENSDSESSSEASEPPDDVITKEEPTDFSEENLVKKEEICDDFEHKIEEDVKPDVYKLNINKMISPPSPPPKKGILLKKDTKKRGEKRVKTVQFKLTKRQKLAKLWKPPTWQIRQILRAAADAKGYKIRSGRSRYNEKIRRLNHFNGQKLGFKSAPTRIDTFEKGIDVREQPIPFVEEFVLDDHALLTFASFDDLKAYEEAYSLRQQDVIDEFWRHQCLKNIESFEKDDVERAEMRHEIEKLETEMRCQKMNENAEIDQENIESFETAGRQIENIIKNTGDCAFETLEEYFSISADFEKNEELRAEEEQLEIEMEHWERELEEMIDVIKREFSIENLMMRMLKNRHLLTMRLVVSGTNQSSIDRENLLRKTKKLLEELKNLRIAAQNRLKIDFDRNERMLYRLRNAKQKAAKRARKLVKNWKKSAQNKSGVLKINGNHVINHDVVVKKWKVELKIEGNGESPRKVVRKAKETSGYWDFRWNFTKFAWKSDVLKRKQRFGKHSARRAIAFGVKIEEIHSETEFEKLLSEYVEYEESDIQNQVSIDRKIDIITKIKTITLNDVRAKAIEMQKQIVEKAVDLMIKSRLDEAAREHQEWLQSDECKRENQLRQRQQNFFDLTSSSPATSSFVTTQVVVPRLTHLEERLIELGVEHEVVQHTQRLQSEFENYHHLQQQHNHQNFQQQQQGNHDFVTPKAPQDKQKRKYTKRKALLNTAVASSSDQNGMKSPGSSAMENAAAAAQAAQAQAQATIPTPTVNLPDVVAIAAAAATAQPSAAAAKRPASETPPNGLPKVPRHDEQQQQQNNAHSIVMGAREGFLAMNPSLAGHVFPASSASTSGAPGAHSATTSGGAGLIGISAATQAQLQAQQAAQAAAAAAAAAAAQATQSLYINTSVAPGAQAASAQGGGGGQVVAAQQSNQAATAEAIRLLQGLPPFLTAGSGSAGIPYFSALSQQLNQLGAAAPGAPGTLNGLQFPANAALGPQLAGAALLAAVPGAQQQIKRPGRWSGMHVKIATDIQNYKQSQEKKLPTDIQSTSSSSAAPASAPAPRAGAGAGATSSSAASSSTSTPSSSSHHKKSSPPHHQKSAAPSAPPRDVTSAHAPPPPASSAPIVGAPRQGATPQAAPATTPATTSQHQQSIQFSQFPPPQLSGGAAYAGNPQLMAAAINEATRRVAATPKPPVVRPPSAATQQQPVSVTSQASQQQQQFQQIQQQRAAAIAAAAAATSQQAPPAQASQATSAAQQIATSMGLQPAQVTDLVNQHAQQYLLLQQQQQQQQREQQQQQQLQAQQVQQQLIAHLLGGGHQAQQAAPAVSVAQQQQQQVAAAAAAQQQHNAQLQNIMILTALQQQMERGAAAGAAASLPYQLQLAQAQAQAQAQQAPPTSQPSQAATPQQQQQLDLIRQMEAVAQVQQAHAQAQAQAQAQAQQMQQQQIQQMLMAGQGGPNGQDLIRLLQAAQQQSQAQQQQQQQQAVVAAAQQQQQQQQHNQQLAAAQAAAAAAAAGRPTQNQYEALLQQQRLLAAQQQAAAGASAQQQAAAAAAQAQAQQFQQQLLGLQPNLLLAQVQQAQQAQAQAQAQAQQKPPQMPNGR
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[Isoform d]: In males, required for non-apoptotic death of the linker cell once it has finished guiding gonad elongation at the end of larval development. May be involved in nuclear envelope crenellation in the linker cell. [Isoform a]: In males, promotes linker cell survival. [Isoform b]: In males, promotes linker cell survival.
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C7IW64
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ROS1A_ORYSJ
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Protein ROS1A (EC 3.2.2.-) (Protein REPRESSOR OF SILENCING 1 homolog a) (Protein ROS1 homolog) (OsROS1) (Protein THICK ALEURONE 2)
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MQDFGQWLPQSQTTADLYFSSIPIPSQFDTSIETQTRTSAVVSSEKESANSFVPHNGTGLVERISNDAGLTEVVGSSAGPTECIDLNKTPARKPKKKKHRPKVLKDDKPSKTPKSATPIPSTEKVEKPSGKRKYVRKKTSPGQPPAEQAASSHCRSELKSVKRSLDFGGEVLQESTQSGSQVPVAEICTGPKRQSIPSTIQRDSQSQLACHVVSSTSSIHTSASQMVNAHLFPPDNMPNGVLLDLNNSTSQLQNEHAKFVDSPARLFGSRIRQTSGKNSLLEIYAGMSDRNVPDLNSSISQTHSMSTDFAQYLLSSSQASVRETQMANQMLNGHRMPENPITPSHCIERAALKEHLNHVPHAKAAVMNGQMPHSYRLAQNPILPPNHIEGYQVMENLSELVTTNDYLTASPFSQTGAANRQHNIGDSMHIHALDPRRESNASSGSWISLGVNFNQQNNGWASAGAADAASSHAPYFSEPHKRMRTAYLNNYPNGVVGHFSTSSTDLSNNENENVASAINSNVFTLADAQRLIAREKSRASQRMISFRSSKNDMVNRSEMVHQHGRPAPHGSACRESIEVPDKQFGLMTEELTQLPSMPNNPQREKYIPQTGSCQLQSLEHDMVKGHNLAGELHKQVTSPQVVIQSNFCVTPPDVLGRRTSGEHLRTLIAPTHASTCKDTLKALSCQLESSRDIIRPPVNPIGPSSADVPRTDNHQVKVSEETVTAKLPEKRKVGRPRKELKPGEKPKPRGRPRKGKVVGGELASKDSHTNPLQNESTSCSYGPYAGEASVGRAVKANRVGENISGAMVSLLDSLDIVIQKIKVLDINKSEDPVTAEPHGALVPYNGEFGPIVPFEGKVKRKRSRAKVDLDPVTALMWKLLMGPDMSDCAEGMDKDKEKWLNEERKIFQGRVDSFIARMHLVQGDRRFSPWKGSVVDSVVGVFLTQNVSDHLSSSAFMALAAKFPVKPEASEKPANVMFHTISENGDCSGLFGNSVKLQGEILVQEASNTAASFITTEDKEGSNSVELLGSSFGDGVDGAAGVYSNIYENLPARLHATRRPVVQTGNAVEAEDGSLEGVVSSENSTISSQNSSDYLFHMSDHMFSSMLLNFTAEDIGSRNMPKATRTTYTELLRMQELKNKSNETIESSEYHGVPVSCSNNIQVLNGIQNIGSKHQPLHSSISYHQTGQVHLPDIVHASDLEQSVYTGLNRVLDSNVTQTSYYPSPHPGIACNNETQKADSLSNMLYGIDRSDKTTSLSEPTPRIDNCFQPLSSEKMSFAREQSSSENYLSRNEAEAAFVKQHGTSNVQGDNTVRTEQNGGENSQSGYSQQDDNVGFQTATTSNLYSSNLCQNQKANSEVLHGVSSNLIENSKDDKKTSPKVPVDGSKAKRPRVGAGKKKTYDWDMLRKEVLYSHGNKERSQNAKDSIDWETIRQAEVKEISDTIRERGMNNMLAERIKDFLNRLVRDHGSIDLEWLRYVDSDKAKDYLLSIRGLGLKSVECVRLLTLHHMAFPVDTNVGRICVRLGWVPLQPLPESLQLHLLEMYPMLENIQKYLWPRLCKLDQRTLYELHYQMITFGKVFCTKSKPNCNACPMRAECKHFASAFASARLALPGPEEKSLVTSGTPIAAETFHQTYISSRPVVSQLEWNSNTCHHGMNNRQPIIEEPASPEPEHETEEMKECAIEDSFVDDPEEIPTIKLNFEEFTQNLKSYMQANNIEIEDADMSKALVAITPEVASIPTPKLKNVSRLRTEHQVYELPDSHPLLEGFNQREPDDPCPYLLSIWTPGETAQSTDAPKSVCNSQENGELCASNTCFSCNSIREAQAQKVRGTLLIPCRTAMRGSFPLNGTYFQVNEVFADHDSSRNPIDVPRSWIWNLPRRTVYFGTSIPTIFKGLTTEEIQHCFWRGFVCVRGFDRTSRAPRPLYARLHFPASKITRNKKSAGSAPGRDDE
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Bifunctional DNA glycosylase/lyase, which excises 5-methylcytosine (5-meC) and 5-hydroxymethylcytosine (5-hmeC), leaving an apyrimidinic (AP) site that is subsequently incised by the lyase activity (Probable). DNA demethylase that is indispensable in both male and female gametophyte development. Involved in the regulation of DNA methylation in the promoters of RISBZ1/BZIP58 and DOF3/RPBF, two transcription factors that functions synergistically to positively regulate genes that are key players in the development of aleurone layers. Active DNA demethylation carried out by ROS1A in rice endosperms may restrict the number of aleurone cell layers.
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C7NBY4
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CS13A_LEPBD
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CRISPR-associated endoribonuclease Cas13a (EC 3.1.-.-) (CRISPR-associated endoribonuclease C2c2) (EndoRNase) (LbuC2c2)
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MKVTKVGGISHKKYTSEGRLVKSESEENRTDERLSALLNMRLDMYIKNPSSTETKENQKRIGKLKKFFSNKMVYLKDNTLSLKNGKKENIDREYSETDILESDVRDKKNFAVLKKIYLNENVNSEELEVFRNDIKKKLNKINSLKYSFEKNKANYQKINENNIEKVEGKSKRNIIYDYYRESAKRDAYVSNVKEAFDKLYKEEDIAKLVLEIENLTKLEKYKIREFYHEIIGRKNDKENFAKIIYEEIQNVNNMKELIEKVPDMSELKKSQVFYKYYLDKEELNDKNIKYAFCHFVEIEMSQLLKNYVYKRLSNISNDKIKRIFEYQNLKKLIENKLLNKLDTYVRNCGKYNYYLQDGEIATSDFIARNRQNEAFLRNIIGVSSVAYFSLRNILETENENDITGRMRGKTVKNNKGEEKYVSGEVDKIYNENKKNEVKENLKMFYSYDFNMDNKNEIEDFFANIDEAISSIRHGIVHFNLELEGKDIFAFKNIAPSEISKKMFQNEINEKKLKLKIFRQLNSANVFRYLEKYKILNYLKRTRFEFVNKNIPFVPSFTKLYSRIDDLKNSLGIYWKTPKTNDDNKTKEIIDAQIYLLKNIYYGEFLNYFMSNNGNFFEISKEIIELNKNDKRNLKTGFYKLQKFEDIQEKIPKEYLANIQSLYMINAGNQDEEEKDTYIDFIQKIFLKGFMTYLANNGRLSLIYIGSDEETNTSLAEKKQEFDKFLKKYEQNNNIKIPYEINEFLREIKLGNILKYTERLNMFYLILKLLNHKELTNLKGSLEKYQSANKEEAFSDQLELINLLNLDNNRVTEDFELEADEIGKFLDFNGNKVKDNKELKKFDTNKIYFDGENIIKHRAFYNIKKYGMLNLLEKIADKAGYKISIEELKKYSNKKNEIEKNHKMQENLHRKYARPRKDEKFTDEDYESYKQAIENIEEYTHLKNKVEFNELNLLQGLLLRILHRLVGYTSIWERDLRFRLKGEFPENQYIEEIFNFENKKNVKYKGGQIVEKYIKFYKELHQNDEVKINKYSSANIKVLKQEKKDLYIRNYIAHFNYIPHAEISLLEVLENLRKLLSYDRKLKNAVMKSVVDILKEYGFVATFKIGADKKIGIQTLESEKIVHLKNLKKKKLMTDRNSEELCKLVKIMFEYKMEEKKSEN
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CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements (spacer sequences) and target invading nucleic acids. Unlike many single-component effectors, this CRISPR-Cas system targets RNA. CRISPR clusters are transcribed from pre-CRISPR RNA (crRNA) and processed into crRNA by this protein. pre-crRNA processing yields a 5'-OH and probably a 2',3'-cyclic phosphate. Also cleaves pre-crRNA from several other type VI-A CRISPR systems. Cleaves linear target ssRNA in a crRNA-dependent fashion, preferentially before U residues. Cleavage of target ssRNA is about 80-fold faster than pre-crRNA processing and uses a different active site. Binding a viable target RNA target activates this protein for non-specific RNA degradation in vitro (called collateral RNA degradation). Activation occurs with 10 fM target RNA. crRNA maturation is not essential for activation of RNA degradation, but lack of mature crRNA (due to mutagenesis) decreases activation levels. This system has a 3' protospacer flanking site in the target RNA (PFS), which is C and unavailable to base pair with crRNA (PFS is equivalent to PAM, the protospacer adjacent motif).
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C7S340
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CABC2_PROVU
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Chondroitin sulfate ABC exolyase (EC 4.2.2.21) (Chondroitin ABC exoeliminase) (Chondroitin ABC lyase II) (Chondroitin sulfate ABC lyase II) (ChS ABC lyase II) (Chondroitinase ABC II) (cABC II) (Exochondroitinase ABC)
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LPTLSHEAFGDIYLFEGELPNTLTTSNNNQLSLSKQHAKDGEQSLKWQYQPQATLTLNNIVNYQDDKNTATPLTFMMWIYNEKPQSSPLTLAFKQNNKIALSFNAELNFTGWRGIAVPFRDMQGSATGQLDQLVITAPNQAGTLFFDQIIMSVPLDNRWAVPDYQTPYVNNAVNTMVSKNWSALLMYDQMFQAHYPTLNFDTEFRDDQTEMASIYQRFEYYQGIRSDKKITPDMLDKHLALWEKLVLTQHADGSITGKALDHPNRQHFMKVEGVFSEGTQKALLDANMLRDVGKTLLQTAIYLRSDSLSATDRKKLEERYLLGTRYVLEQGFTRGSGYQIITHVGYQTRELFDAWFIGRHVLAKNNLLAPTQQAMMWYNATGRIFEKNNEIVDANVDILNTQLQWMIKSLLMLPDYQQRQQALAQLQSWLNKTILSSKGVAGGFKSDGSIFHHSQHYPAYAKDAFGGLAPSVYALSDSPFRLSTSAHERLKDVLLKMRIYTKETQIPVVLSGRHPTGLHKIGIAPFKWMALAGTPDGKQKLDTTLSAAYAKLDNKTHFEGINAESEPVGAWAMNYASMAIQRRASTQSPQQSWLAIARGFSRYLVGNESYENNNRYGRYLQYGQLEIIPADLTQSGFSHAGWDWNRYPGTTTIHLPYNELEAKLNQLPAAGIEEMLLSTESYSGANTLNNNSMFAMKLHGHSKYQQQSLRANKSYFLFDNRVIALGSGIENDDKQHTTETTLFQFAVPKLQSVIINGKKVNQLDTQLTLNNADTLIDPTGNLYKLTKGQTVKFSYQKQHSLDDRNSKPTEQLFATAVISHGKAPSNENYEYAIAIEAQNNKAPEYTVLQHNDQLHAVKDKITQEEGYAFFEATKLKSADATLLSSDAPVMVMAKIQNQQLTLSIVNPDLNLYQGREKDQFDDKGNQIEVSVYSRHWLTAESQSTNSTITVKGIWKLTTPQPGVIIKHHNNNTLITTTTIQATPTVINLVK
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Broad-specificity glycosaminoglycan lyase, which acts in an exolytic fashion, and preferentially degrades the tetra- and hexasaccharide derivatives of chondroitin sulfate and dermatan sulfate produced by the chondroitin sulfate ABC endolyase, to yield the respective disaccharides. To a lesser extent, is also able to split off disaccharide residues directly from polymeric chondroitin 4- and 6-sulfate, dermatan sulfate, chondroitin, and hyaluronan. Is not active against keratan sulfate, heparan sulfate, and heparin.
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C7SG33
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IF4E1_CITLA
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Eukaryotic translation initiation factor 4E-1 (eIF-4E-1) (eIF4E-1) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein)
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MVVEETIKATSTEDLSNTIANQNPRGRGGDEDEELEEGEIVGDDDLDSSNLSAAIVHQPHPLEHSWTFWFDNPSAKSKQATWGASIRPIYTFSTVEEFWSVYNNIHHPSKLALRADLYCFKHKIEPKWEDPVCANGGKWTVNFSRGKSDNGWLYTLLAMIGEQFDCGDEICGAVVNVRSGQDKISIWTKNASNEAAQASIGKQWKEFLDYNDSIGFIFHEDAKKFDRHAKNKYSV
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Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses.
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C7YZ74
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ARO1_FUSV7
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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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MAEAKKPGPERISILGEANIIVDHGLWLNFVVDDLLQNTPTSTYVLITDTNLFDTYVPAFQAQFEAAAEGKATRLLTYTIPPGEASKSRETKAEIEDWMLSQQCTRDTVIIALGGGVMGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPMGKNLVGAFWQPKRIYIDLAFLETLPVREFINGMAEVVKTAAIWNETEFTVLEESAAHILECVRSKGEGRLTPIKDVLKRIVIGSAGVKAEVVSSDEREGGLRNLLNFGHSIGHAIEAILTPQLLHGEAVAIGMVKEAELARYLGVLRPGAVARLVKCIASYDLPTSIHDKRVVKLTAGKKCPVDVLLQKMGVDKKNDGQKKKIVLLSAIGKCHEPRASVVDDKTIRTILSPSIQVTPGVPSNLDVTVTPPGSKSISNRALVLAALGLGSCRIKNLLHSDDTEYMLSAIHQLGGASYSWQDAGEVLVVDGKGGNLQASKEALYLGNAGTASRFLTTVVALCSPSESASSTILTGNARMKVRPIGPLVDALRSNGVEIEYQGKENSLPLRVDAAGGLKGGVIELAATVSSQYVSSILMAAPYAKNPVTLRLVGGKPISQPYIDMTISMMASFGVHVTASSDEPNTYHIPQGQYQNPSEYIIESDASSATYPLAIAAITGTTCTIPNIGSKSLQGDARFAVDVLQPMGCTVNQSDYSTTVTGPAPGELKGLPHVDMEPMTDAFLTASVLAAVASGKTQITGIANQRVKECNRIAAMKDQLAKFGVQCNELDDGIEVLGKGQDGGISAPTVGIHCYDDHRVAMSFSVLAVASPSPVIVTERECVGKTWPGWWDILSQAFKVDMIGHEPDANADEEDSKSSVMERSVFIIGMRGAGKTTAGNWMAKMLGWKFIDLDQELERRAGCTIPEMIRGSRGWEGFRADELSLLKDVMAKNSHGHIFSCGGGLVETPEARQLLKDYGRNGGNVLLIHRDTEQVVEYLMRDKTRPAYTSEIREVYLRRKDFYQECSNLLYYSPHSESSGSKSEIPCDFQQFVSSISGRSTHLKDVMEKDHSFFVSLTVPDVSEAASLIPEVVVGSDAVELRVDLLQDRSVDSVTRQVSILRALAKKPIVFTLRTVSQGGKFPDEAYEEGLELYRLALRMGMEYVDVEMTLPENIIQTVTESRGHSRIIASHHDPQGTMSWKNASWIPFYNRALQFGDIIKLVGVARSSEDNFDLAKFKSRMQEAQKTPMIAMNMGKAGKLSRVLNKFLTPVSHPALPFKAAPGQMSAAEIRRGLALLGDLDPCNFYLFGKPISASRSPALHNTLFGQTGLPHQYHRLETDNIQDVREVLQAPDFGGASVTIPLKLDVMGQVDELSEAARTIGAVNTVVPIGKADASDRRRLLGDNTDWRGMVHALRDEGVEEQADSETKGAAMVVGSGGTTRAAIFALHSLGFGPIYIAARNQAKVDALAADFPAEYQLQGLSQPSDADKVSSNLNVVISTIPADRPIDPSLQELVGALLSRPAVGTERRVLLEMAYKPSHTPIMQLADEAGNWTTVPGLEVLASQGWYQFELWTGITPLYRDARSAVLGL
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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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C8KI33
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SUV2_ARATH
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Protein SENSITIVE TO UV 2 (ATR interacting protein) (AtATRIP) (Protein HYDROXYUREA-SENSITIVE 2)
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MSGNDEEFNDEFLLAIDSIETTLKKADMYRPLPPPYLPTFLPAPPPSTKISSSLSHPMQLQSSAGQQRKQIQVPDPFLSYSPPRELSQRVVSGFNDALMDYSNSTVVTAAKPISPTTSNRRCDSEKDLEIDRLKKELERVSKQLLDVEQECSQLKKGKSKETESRNLCADDNRGQCSTVHASKRIDLEPDVATSSVNHRENDSRMALDDKRSFKTTGVQADVANHSDLSKKLLDIWRTSNYQDPRKNLISELLLACSTDLQILFSFMKISTPPQELNKQEAKTSSDRQSSKALESEKVYQLYSAVTKISYGFVNLKTLVEPLLDLCKAETAVLVHRSLRVLHVLLEHICGDEKRFEASWDANWHSLFKLMNQIASKRTEQDVKQEALSIMNIIVMSTDAYTARESFVSKEVFESISLLLRKEGGLHVRKEAIHLFYLLLNCPKLYDTFDSLHEEKNSSDTENDSEGNFFALEAFGKIFEGLADCLTSPRKTSEDLELCRNVIMILALAASSGNSGYELLSSHKLPQDSSFLMLILHLLVAEIDSESTEFHPKAEIFKARTLLMREILILLNRLVSGLSSSATILKELTTSRDMASLTVDAATRLSRKRNLLGKPESSVERMRNTEIMDLARIFKKRVFAFLGDNTI
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Required for tolerance to DNA-damaging and cross-linking agents such as UVB irradiation, gamma-radiation, aphidicolin, ionizing radiation and hydroxyurea (HU), cisplatin (CDDP) and mitomycin C (MMC). Involved in cell-cycle G2/M arrest in response to DNA damage. Required for aluminum-dependent gene regulation and root growth inhibition in an ATR-dependent manner by halting cell cycle progression and triggering loss of the quiescent center (QC).
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C8V7P4
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IVOA_EMENI
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Nonribosomal peptide synthetase ivoA (NRPS ivoA) (EC 5.1.-.-) (Ivory mutation-related protein A)
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MASPIIQPAGAGIHDIFTQLELWESIDKGLSMITILRDNDVLWKPFLQLTLFNQLNIVRKAWSATIQKASESDKVPTLKDVYTSESSFIAQALLDTKNLQITPPATPRTALSGALLAKTIVIFHHSERAQEELGTELPEEVRSLVNQNAICLKVLYNANQWHIDLHYKRDSLSSAQAGEVAEIFEQYLEEALEAVASAIPPSPPVEDDNAGHGGLCKERTDCPKVNRCIHDLIEEQAIARPDQEGICAYDGSLSYAGLSKLSSVLAEQLKTFGARPEQRVAILMNKSFWYPVVVLAVLKSGAAFVPLDPSHPKNRLKQLISEIEPCALITTSVLSELADDLGCPSLAIDSDLTRSKEGSTTALLPNTSASPNNAAYIIFTSGSTGKPKGVVVEHSALSTSAITRGVVLGLGPDSRVLQYAPHTFDVSVDEILTTLIHGGCVCVPSEDDRFSIAHFMESARVTVALLTPTSARTLHPDEVPSLRILQTGGEVLTEDVNDKWSNRVTLFNVYGPTEASVACVISNRTGLKGAGHVLGQAVGGKLWIVDPDDIERHLPDNEVGELVISGAILARGYFRDPSRTESSFVRMRNGERVYRTGDLASMDSAGTIIYHGRKDLEVKIRGQRINIAEIEIAILQCDLVHSVVVEYPRSGLFEKKLVAVLRFEDSSSDAEDGLFGGAKGLTEDIYCLLLSHVSSVLTPAMIPSKWLSLPCVPQMPSGKADRKQVRGWLEDMDKRTYTRIFHPNGTDNLISDPSDSMVAIWLKVLKLEPQSLRLDQSFIRNGGDSIMAMEARHQAHEAGINIDVRELLGSRALQEIGEMATKTSAVEEVSKIEDDRDEPFPLSPVQQMYFDKVSDPSLGLQQRVCVEIMTKIQPDMLREALNHVIQKHRMLAARFTKHMGQWMQQVPFGKNLKHLSRCHIYSQAVGSLGDFCSEPMALEDGTLLHAHLQSSGERQTLVLCVHHLVVDFVSWRVILQDLHDALAAAQNGLPSGISRSTLTFQQWCREQTKYASTLIPEAVLPFAPGPVNLRFWQPSNVQAVSNTYSEIVQHDFRLSSTQTTQMLEKFTTATVHPTDLMLATFALAFKRIFTERDTPTIFIEGHGREPWHASLDVSQTVGWFTAAFPIHLPKDTLLNTTTAILGASERRRSVLANGHPYWACRYLSPNGQKVFGDDPRHQEMEFVFNYAGSIVQRAPGQTLFAENVRIAEIGHPNCERFSLFDIGAAIEMPSSELVVSFTFPKGIAHRERVAELVKTYQELLETAVERDLDLSAKLSSPLVCPADVVRSLEVNGVCIERDVEIVYTPSSIQQHMLWRQSQEPWFYRVQGDWTIEKTTTQSEPVDIDRLSHAWNQVVHRHTTLRTVFRYSSEEERFVAIVLHEVKPAISIIRKGIQTSGSLCRDDDLSPPHRMVLREKDNGSVVCELEFSHTIIDAASRSIVVQDLLDAYDGKLAHRPLDFPPFWEYIRLAQSSTPSARKEELHRAGRVVTLPFQPTHVLSKVPEACKKNEITISSFFMTAWSIVLAKHFVAHNQRVDSTSSQAVAFDYVLSDRSANIPGIESAVGPYIRLPTLETHVKEGVSLKNIARGLHAQCTFQSLSQSTQDGSSLELPSKATALQKYSTLVNIRNSGSDSLDLVSDSGEWKWILQGFSDPWDYDLVFAVNVHAGKVTGWTVEYADGVVEHSAADEIAKDLNDVVERMVCEII
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Nonribosomal peptide synthetase part of the pathway that mediates the biosynthesis of the gray-brown conidiophore pigment. The first step of the pathway is performed by the nonribosomal peptide synthetase ivoA that catalyzes ATP-dependent unidirectional stereoinversion of L-tryptophan to D-tryptophan with complete conversion. While the stereoinversion is catalyzed by the epimerization (E) domain of ivoA, the terminal condensation (C) domain stereoselectively hydrolyzes D-tryptophanyl-S-phosphopantetheine thioester and thus represents a non-canonical C domain function. D-tryptophan is acetylated, probably by an endogenous acetyltransferase (Probable). N-acetyltryptophan is further 6-hydroxylated into N-acetyl-6-hydroxytryptophan (AHT) by the cytochrome P450 monooxygenase ivoC. N-acetyl-6-hydroxytryptophan is substrate of the N-acetyl-6-hydroxytryptophan oxidase ivoB to produce the gray-brown conidiophore pigment (PubMed:2126551, PubMed:28108400, Ref.3).
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C8VBH4
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ESA1_EMENI
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Histone acetyltransferase esa1 (EC 2.3.1.48) (Protein 2-hydroxyisobutyryltransferase esa1) (EC 2.3.1.-) (Protein acetyltransferase esa1) (EC 2.3.1.-) (Protein crotonyltransferase esa1) (EC 2.3.1.-)
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MGVRDSHGEAAGTPDPVEKGIATLNTIRIGVKAMVHKDGALRKAEILSIKQRKDGLAFYVHYVDFNKRLDEWVASSRLDLSQEVEWPQPEKPEKKKSGPAKAPSKNKRVRAGSRDVSATPDTLTGKNTNVGKAQRPSKAGGKENRGDETPADLSMLASEAVSADGTPKAVSEDIDMMDASFTDAKEIKEEERALGLMSREEEIEKLRTSGSMTQNPTEVHRVRNLDRLQMGKYDIEPWYFSPYPASFSDAEVVYIDEFCLSYFDNKRAFERHRTKCTLTHPPGNEIYRDDNISFFEVDGRRQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMCTRDETGCHLVGYFSKEKESGEGYNLACILTLPQYQRRGYGRLLISFSYELSKREGKVGSPEKPLSDLGLLGYRQYWRETLVEILLDSGRETVSENELAMLTSMTEKDVHETLVTFKMLRYNKGQWIIVLTDEVIEERNKRLEKEKIKGSRKIDPARLQWKPPVFTASSRTWNW
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Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z (By similarity). Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac (By similarity). The NuA4 complex is involved in the DNA damage response and is required for chromosome segregation. The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) through homologous recombination (By similarity). Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins (By similarity). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively (By similarity).
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C8VG90
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ACON_EMENI
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Aconitate hydratase, mitochondrial (Aconitase) (EC 4.2.1.3) (Citrate hydro-lyase) (Homocitrate dehydratase) (EC 4.2.1.-)
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MITTRLARMGALAPKSRLLFGTRGMATVADLDKKVEMCNLEKGNYINYKKMSENLDVVRRRLTRPLTYAEKILYSHLDDPQNQDIERGKSYLKLRPDRVACQDATAQMAILQFMSAGMPSVATPTTVHCDHLIEAQLGGEKDLARANEINKEVYDFLASSTAKYNIGFWKPGSGIIHQIILENYAFPGGLMIGTDSHTPNAGGLAIAAIGVGGADAVDVMAGLPWELKAPKVIGVRLTGEMSGWTAPKDIILKVAGLLTVKGGTGAIIEYHGPGVNSLSATGMATICNMGAEIGATTSLFPFNDRMYDYLKATKRQQIGDFARSYAKDLREDEGAEYDQLIEINLSELEPHINGPFTPDLATPISQFKEAVKANGWPEELKVGLIGSCTNSSYEDMSRAASIAQDALDHGLKAKSIFTVTPGSEQIRATIERDGQLKTLEEFGGVILANACGPCIGQWDRKDVKKGTPNSIVSSYNRNFTGRNDANPATHAFVTSPDLVVALSIAGTLNFNPLTDTLKDKDGKEFKLKAPTGDGLPSRGYDPGRDTYQAPPTDRSSVDVAVSPSSDRLQLLAGFQPWDGKDATGIPILIKCQGKTTTDHISMAGPWLKYRGHLDNISNNMLIGAVNAENGEANKIKNVFTGEYGAVPATARDYKARGVKWVVIGDWNYGEGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGMLPLTFSDPADYDRIPPDATVDLLCTELAVDKPMTLRVHPKDGASFDVKLSHTFNESQIEWFKDGSALNTMARKSGN
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Catalyzes the isomerization of citrate to isocitrate via cis-aconitate, a step in the citric acid cycle. Also catalyzes the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.
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C8VJQ3
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ASQI_EMENI
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Cyclopenase asqI (EC 4.1.99.27) (4'-methoxyviridicatin/aspoquinolone biosynthesis cluster protein asqI) (Aspoquinolone biosynthesis protein I)
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MTCTLRDLNSLLEICCRCPAHNPSTAFAPTTKVRVSSDVRGIFALPVQKDHKPYNGLSPEHLETMKAVSLMLDAAGPKLEDGISKAKELLEERINPELMRDALGIYLTHSKDAQQRKIFPPPLKNHPFFSTKTRRPANVAGEICTADTLHGHALLSYWRDDYDLNDSHYYWHMVYRGAGGDNSKNVGDFDRHGEVFLYVHSQMVARYETESLCWSLPLVRPWNQYDDFLENGYAPISSLIEHYGGYPPFSTWYSIRNPDMPDTLNVTIPRARLEEWRDNIYAAIRKGQFETTSKDKPLVLTRDNCLNFVGGILDAQYPSLNKLLGGCSLDEERYGNLHNYGLGKFAEMAYRNKPGEKSPYGLTISNFGAPRDPCFWRWYKHLQYYGRLAATRYPQDITAHRAEVVLSNLVVRLQDRSSPHYLDGHITTFLGPPAVNFMESKAKLGHEPYEWNVQVKSCRRSPPSKENPQTLTLRLFIAAEDLMNDYHSWIEMDRATVQLTDESAITKVRLDTDSSVARKMGNYGEPDPRYASAVFRHGWPQNLMLPVGKVEGMPFVAFCIATDDGIPDPAPAPPFHHYHDPRGMGYPFNRAWTQLTEDSTGKASIRTIISNAELYPFITSTTFKIYRTTKFETKQIIQPTTVTWFNTIRGYFKDADRACMRSEYGYDLYNYDHVMLHADAILDATASKRMPLQMGKYTQDNPDPEHPLWTVKMCENFRAWLLNGCPKGTDPA
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Cyclopenase part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins. Within the pathway, the cyclopenase asqI catalyzes the conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin. Cyclopenin can also be converted into viridicatin by asqI. The first step of the pathway is catalyzed by the nonribosomal pepdide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin. 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ. AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin. The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI. 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B. The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene. The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain. The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin. Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (Probable).
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C8VJW0
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HXNR_EMENI
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Nicotinate catabolism cluster-specific transcription factor
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MKAKMKKHACTYPGCSKAFTRAEHLRRHSLNHETISNSQGYTCQRCMTHFSRADLLSRHLDRHAKKDAEAGGFGKGVLETRKRMRRAEDGSIVLRPPKRPSRHQQKTGPPVGAPLSSSGSVSAGSGRSSRSPDVSLHAAQAPVSPPRSASDPVSVSGVSIDDDGTDPDPMLAPMMPGGPFEPYVEPIPGQFDAADGSWGGFDALGDGMMLDTATDFNLPFAATGNYNWLFDVSSLDDAFHHLELPLGPDLVPFANSHGNYASVNTMELSGAGAENVQDSMLNLDLDIDLNGLPAGFVHDQGPDGSSASVLLQAASFVERGNINGSDPKRDFPDLDWMAGAPPIESTVPLRPQLSEDARRGILTLIAQSPPVDIHGQPLNLDSPLLSLSALQSYSDLFFSRFNTTYPLIHSATFDPNKTEPVFLASILSMGATYSSREAHQLAVGIHDGLRNQLFCHGAFSPQPDELWVLQAMLLIDCFGKMRAGPKQRERAQLFHCVLIKLIRRSTCCSIRADTHSDPGLGGLELEDAWKRAMDAEQRKRLAFQCFMWDTEHSVLFSQSLCMSAFEIRSSLPCSPAAWEAHTAEEWSRHASRDTEHAFLPVLKGYITPGSVSRPRDLNRFSRMVVLHGLMSISADLKRRDQTTLRAETPERVGAWTPRMGRAYDLWKADFDADCLNMKLGPVQVSADETRRFTSLKAAAMALYRAASLALHVEVLDLQIAAGASHILGRVVKQHDRERSRVMLSRWLSGPSPAATTASRHAAALLQDAVLSLHDWDQTDAFHFPWCLYLATLTVWAFHAREGCVPKPTDLSSLIVAMTTSNAADLEGLAGQYDTRPLIRAMAQQLATVRWAVVHDAMKVLLNLGV
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Transcription factor that specifically regulates the expression of the hxn gene cluster that mediates the degradation of nicotinate and related metabolites.
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C8VQG9
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LAEA_EMENI
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Protein-methionine methyltransferase laeA (EC 2.1.1.-) (Secondary metabolism regulator laeA) (Velvet complex subunit laeA)
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MFEMGPVGTRLPAMTSPAHNHYSYHSPTSSDRGRSRQNSDAMDIQSITEREPATRYAVAGGPAPWNRNGSPSMSPMYSNNSERNQFHEENGRTYHGFRRGMYFLPCDEQEQDRLDIFHKLFTVARVSESLIYAPHPTNGRFLDLGCGTGIWAIEVANKYPDAFVAGVDLAPIQPPNHPKNCEFYAPFDFEAPWAMGEDSWDLIHLQMGCGSVMGWPNLYRRIFAHLRPGAWFEQVEIDFEPRCDDRSLDGTALRHWYDCLKQATAETMRPIAHSSRDTIKDLQDAGFTEIDHQIVGLPLNPWHQDEHERKVARWYNLAVSESIENLSLAPFSRVYRWPLERIQQLAADVKSEAFNKEIHAYNILHIYQARKPLR
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Methyltransferase that performs automethylation at Met-207. No other methyl-accepting substrate has been identified yet. Component of the velvet transcription factor complex that acts as a global regulator for secondary metabolite gene expression. Controls the expression of the sterigmatocystin, penicillin, and lovastatin gene clusters. Controls light-dependent formation of the velB-vosA complex, veA protein modification, and is required for light-mediated inhibition of sexual development. Within the velvet complex, controls light-dependent secondary metabolism. Involved in the defense response against Drosophila melanogaster larval grazing.
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C8VQY7
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YPT7_EMENI
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Ypt/Rab-type GTPase avaA (Aspergillus vacuolar morphology protein A) (YPT7 homolog avaA)
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MSSRKKVMLKVIILGDSGVGKTSLMNQYVNKKFSGSYKATIGADFLTKEVLVDDRLVTMQIWDTAGQERFQSLGVAFYRGADCCVLVYDVNNSKSFEALDSWRDEFLIQASPRDPESFPFVVIGNKIDMEESKRMISSKRAMTFCQSKGNIPYFETSAKEAVNVEQAFEVIARSALAQEEAEEYGGDYTDPINIHDTTERDGCAC
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Ypt/Rab-type GTPases are key regulators of membrane trafficking and intracellular vesicular transport. They act as molecular switches that convert between GTP-bound and GDP-bound states, and regulate virtually all steps of membrane traffic from the formation of the transport vesicle at the donor membrane to its fusion at the target membrane. In the GDP-bound state, Ypt proteins are predominantly cytosolic, solubilized through the interaction with a GDP dissociation inhibitor (GDI). In the GTP-bound state, the proteins are membrane bound and interact with specific effector proteins that select cargo, promote vesicle movement, or verify the correct site of fusion (By similarity). AvaA functions in vacuolar biogenesis.
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C8VSZ2
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XANA_EMENI
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Alpha-ketoglutarate-dependent xanthine dioxygenase xanA (EC 1.14.11.48)
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MPAITVKPLTPPAGSAIDFGAVITDVDLEHLTDGDFSTIRSALYTHLVVVLKNQHQLTPKAQYELTRRFDPSATQYGHGKTLDAKRSILHPDLKTIPHQPQVQVIGHGFIDSYEGLENITLKHPHHRTFHRDPIPQEDDYDSTRFYRWHIDAALYGLNPPIVTTLLAVKVPGGRRQTVRYDDGSGETMDVPLGTTAFASGERMFELLSEEDKEFALSSRVEYAPHPYIWMSPARSLPTGLGLHSDDLELPLSELPPIDESAIQILPMVWKNPATGKPALQIHPSAVRKIHCGDGTVIDDLKKVREIAYKLQRPAISPQYVYAHDWEEGDLVLFHNRGVLHSVVGAFGEGEVRLFRQCNLAAGEGVVPYRE
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Alpha-ketoglutarate-dependent xanthine dioxygenase is a non-heme mononuclear Fe(2+) enzyme that decarboxylates alpha-ketoglutarate to succinate and CO(2) while hydroxylating xanthine to generate uric acid. Allows xanthine utilization as a nitrogen source. Whereas xanA is highly specific for xanthine, alpha-ketoadipic acid can replace alpha-ketoglutarate as a cosubstrate. Exhibits ferroxidase activity in the absence of substrates.
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C8VTS4
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VELB_EMENI
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Velvet complex subunit B
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MYAVEDRAHSGHHPPPLSMDRIPPPSTMYPSSAGPSAMVSPAGQPEPESLSTVHDGRIWSLQVVQQPIRARMCGFGDKDRRPITPPPCIRLIVKDAQTQKEVDINSLDSSFYVVMADLWNADGTHEVNLVKHSATSPSISTAMSSSYPPPPHPTSSDYPASYQTNPYGQPVGQPVGQPVGYAGVGNYYGGSTQLQYQNAYPNPQAQYYQPMYGGMAQPQMPAAQPVTPGPGGMFTRNLIGCLSASAYRLYDTEDKIGVWFVLQDLSVRTEGIFRLKFSFVNVGKSVSDLPQSDIAEVINKGTAPILASTFSEPFQVFSAKKFPGVIESTPLSKVFANQGIKIPIRKDGVKGQGSRGRHSDEDDGLDNEY
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Component of the velvet transcription factor complex that controls sexual/asexual developmental ratio in response to light, promoting sexual development in the darkness while stimulating asexual sporulation under illumination. The velvet complex acts as a global regulator for secondary metabolite gene expression. Component of the velB-VosA heterodimeric complex that plays a dual role in activating genes associated with spore maturation and repressing certain development-associated genes. The velB-VosA complex binds DNA through the DNA-binding domain of vosA that recognizes an 11-nucleotide consensus sequence 5'-CTGGCCGCGGC-3' consisting of two motifs in the promoters of key developmental regulatory genes. The vosA-velB complex binds to the beta-glucan synthase fksA gene promoter in asexual spores for repression.
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C8VTV4
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VEA_EMENI
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Developmental and secondary metabolism regulator veA (Velvet complex subunit A)
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MATLAAPPPPLGESGNSNSVSRITREGKKITYKLNIMQQPKRARACGQGSKSHTDRRPVDPPPVIELNIFESDPHDDSNKTDITFVYNANFFLFATLEPERPIATGKLMTNQGSPVLTGVPVAGVAYLDKPNRAGYFIFPDLSVRNEGSYRFSFHLFEQIKDPKDATEGTQPMPSPVPGKLSSPQEFLEFRLEVISNPFIVYSAKKFPGLTTSTPISRMIAEQGCRVRIRRDVRMRRRGDKRTEDYDYDNERGYNNRRPDQYAGSDAYANAPERPRSTSISTNMDPYSYPSRRPSAVEYGQPIAQPYQRPMASTPAPSSTPIPAPIPMPGPVALPPSTPSPASAHAPAPPSVPLAAPPPLHTPSYQSHLSFGATQTQYPAPQLSHIPQQTTTPTHPYSPRSSISHSRNQSISEYEPSMGYPGSQTRLSAERPSYGQPSQTTSLPPLRHSLEPSVNSRSKTPSNMITSLPPIQSLSELPSTTSQPSSAIGSSPANEPGPRLWETNSMLSKRTYEESFGHDDRPLYNGMRPDSESYPGGMQRRPSYERSSLLDGPDQMAYKRANGRMVSKPATMR
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Component of the velvet transcription factor complex that controls sexual/asexual developmental ratio in response to light, promoting sexual development in the darkness while stimulating asexual sporulation under illumination. The velvet complex acts as a global regulator for secondary metabolite gene expression. Controls the expression of the sterigmatocystin and penicillin gene clusters. Represses the cryptic ors gene cluster producing orsellinic acid and its F9775 derivatives in a laeA-independent manner. Required for full induction of faoA gene expression by fructosyl amines. Positively regulates the expression of the early sexual development gene esdC. Controls the expression of mannoprotein mnpA.
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C8WLM1
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CGR2_EGGLE
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Digoxin reductase (EC 1.3.2.-) (Cardenolide reductase) (Cardiac glycoside reductase operon protein 2)
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MEYGKCRGIERGMGRRDFLKAATLLGATAAGAGMLAGCAPKSASEAQAQTAPAATGGLDPADVDWKYETDVVIVGSGSGGTCAAIEAAEAGADVVVFEKDKAMYGGNSALCGGYMLAAGWSTQEEITGYAGDTGEAFANQMLRWSQGLGNQDMIREACLRSGEAVDWMMDTGRTYEGASPLPPVWSCGDTEADVVPRSVYNHNAYGATEGHMATLKKRAESLSNIEIEMGCEVAHILKNAEGSVIGVQLADGSFAKARKGVVMACASVDNNLEMSKDLGLMQNVWGLTLEGAGLLAPGNPDMDSNTGDGVRMLREIGAELCMQQAVCMNDSIYVGGISDWGMSEILGKDVNIHDSSNIDAILVDKTGRRFCQDDAEWGYVMHECAQAAWKQGFTPDDPTTGYIFYVYDATGAPFFEMKGHTPDTCDTTFSADSVDGLAEFIGCDPTALASEVERWNSFCEAGLDADFGRRANMAPIATPPFYCDVVRPGPMGTFAGAKSNVEAEIIGLDGNPIPRLYGAGCIIGGNVSGAFYFGCGWSITNTVVWGREAGRNVAALEPWE
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Involved in the inactivation of the cardiac medication and plant natural product digoxin, thus decreasing drug efficacy and toxicity. Catalyzes the reduction of the alpha,beta-unsaturated butyrolactone ring of digoxin to the inactive metabolite dihydrodigoxin. Likely uses the cytochrome Cgr1 as the physiological electron donor, encoded by the adjacent gene in the locus. Only reduces digoxin and other cardenolide toxins, such as digitoxin, digoxigenin, ouabain and ouabagenin. Therefore is a specialized enzyme present in some gut bacteria E.lenta that protects their human host against ingested plant toxins.
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C8WR67
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ILVC_ALIAD
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Ketol-acid reductoisomerase (NADP(+)) (KARI) (EC 1.1.1.86) (Acetohydroxy-acid isomeroreductase) (AHIR) (Alpha-keto-beta-hydroxylacyl reductoisomerase) (Ketol-acid reductoisomerase type 1) (Ketol-acid reductoisomerase type I)
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MEKIYYDADISIQPLADKRIAVIGYGSQGHAHAQNLRDSGFDVVIGLRPGSSWAKAEADGFRVMAVGEAVEESDVIMILLPDERQPAVYEREIRPYLTAGKALAFAHGFNIHFSQIQPPKDVDVFMVAPKGPGHLVRRVYEAGGGVPALIAVHQDASGQAKDLALAYARGIGAGRAGILTTTFREETETDLFGEQAVLCGGLSALIKAGFETLVEAGYQPEIAYFECLHEMKLIVDLIYEGGLEYMRYSISDTAQWGDFTSGPRIINEETKKEMRRILADIQSGAFAKSWILENQANRPMFNAINRRELEHPIEVVGRKLRSMMPFIKAKRPGDDRVPATADRA
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Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:25849365}.
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C8XPA8
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POLG_BANV
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Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
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MVNPKGVNVMAARVKRAAQKTKKKAVQVSRGLRGFVLFVLTQLFMGRKLTPNVRRLWKSSDKNSLIHVLTKIKKIVGNLLMGVSRRKKRRSATTSGTVFMAMLGLTLAASVARHAHHTLINITKDDAHKLLTLRNGNCTVVATDIGNWCPDNVEYDCVTLQDNEDPDDVDCWCYRVNNVRVTYGRCKDGNTPRRSKRAVVITAHLDQGLTTKKETWLGSSHFETQVQKVEKWIIRNPTYAIAAILMSWYIGNSLKQRVVLLLLTLALGPAYATHCVGIPKRDFVQGVQGTTWVNLVLEQGGCVTIMAEGKPSVDVWMDNIKFTSPTLVRRISHTATISDTKIATACPSNGEAKLDEEHIKEYACKRLYSDRGWGNGCGLFGKGSLVACAKYESTGHMDVYEMDMTKVEYTVKTQVHSGAKSGDLSGVKTVSFAPTSGSQPVEFSGYGNMGLQCMIQSNVDFSTHYLVVMGNDAWLVHKAWVEDITLPWKHGEGGTWKDKQYMVEFGEPHATTVKVLALGPQEGALRNALAGAMIVTYESSGKTFKLHGGHVTCKATVSGLALKGTTYTNCRGGLSFVKTPTDTGHGTVVMQVKVAKSAPCRLTAIAADDASGHVNRGTLVTSNPIAASNNDEVMIEINPPYGTSYLIVGVGDDKLVYQWKKSGSTIGSLFSETVKGAQRMAIVGSSSWDFSSTSGFFSSVGKAIHTVFGTAFHGIFGGLSWMTRILIGVLLVWLGLNSRNGTATTLMMLTGFIILFLSLGVGAEVGCSVNWGQKELKCGDGIFVYNDVDDWMHKYKYHPEDPKVMAGLIAKAWEKGACGLTSVSELEHVMWVKIASEINAILEENEIDLTVVVHENKSVYRRGSRRFPRVETELTYGWESWGKNFITDGKVSNNTFHVDGKEDQCASKNRVWNSLEIEEFGFGVFHTNVFLRQKADKTNSCDTTLMGAAVKGNVAAHADPGFWMESQENNGTWEIQSIEFTAYRECEWPVSHTVHGTQVMESDMFMPKGIGGPVSHLNRMQGYKVQTNGAWAYGKTVVQRELCPDTSVVVDSSCSDRGKSIRSTTTEGKVIKEWCCRSCTLPPVSYWTSEGCWYAMEVRPMKTPEKHLVRSWVTAGDSYPAWSIGLVAMFLFVDIMARSRPTRKMMIGGTMLLLAIMIMGELSYLDLLRYIIVVGEHFIERENGGDVAYMAIMAASHLRPGLMAMVFAKSMWSPKQRVLLALGCAILQPFLTAQASALVWEWADSIGLVLLIVQGMVRNKEKNWALVLLALCSPVSMPVIRKASMIIGTGGLLLSLWKGGGSSMRKGLPLFAASAARVLGLTKAHLSVLFILLITKNGKRTWPISECLAAVGIFGAAFGTMFSEDETLLGPLALVGVVLIVYTMFTQSDGLELVKAADISWSDEAVVSGEARRFDVALNDSGEFKLLDEPPVSWLNVSFLVVAIVASSLHPIALVVTLVAWTYWRTEKRSGVLWDVPLAPKVEACEHLEDGVFRIIQKGLFGSSQVGIGVAKDGVFHTMWHVTRGAFLMHSGKQLTPTWGSVRKDLVCYGGTWKLDGAWNGVDEVQLIAVPPGKPATNVQTKPGTFVLPTGDEAGAVLLDFPSGTSGSPIIDRHGNILGLYGNGIVLENGAYASAISQAQPGSVAEVETPGLDKMLRKGEFTMLDYHPGAGKTRKHLPNILKECERKRLRTLVLAPTRVVLSEMKEALTSVQAKFHTQAFNSTTTGREIIDVMCHATFVHRMLEGLRSGNWEVIIMDEAHFLDPTSIAARGWAHHKSKTKESAVIFMTATPPGTSNEFPESNAEIEDVKKEIPSEPWSKGHEWILEDRRPTVWFLPSIKAANVMAACLRKAERSVVVLNRSTFENVYPTIKTKKPDFILATDIAEMGANLPVERVIDCRTAYKPVLVDERVALKGPLRIAAAAAAQRRGRVGRNPDRDGDTYVYSEDTCEQNDHLVCWTEGSMLLDNMQVKGGFVAPLYEEEASKTTMTPGECRLRDDQRKVFRTLIRKHDMPVWLSWQVAKSGLAADDRKWCFDGEDDNAILGDNGEVIKARSPGGQRKELKPRWSDARIASDNTSLMNFIAFAEGRRSLPLSILWSVPNQLSEKLVQSIDTLTILLRSEEGSRAHKLALQQAPEAVSTLLLLGMMAICTLGLVILLMKPKATDKMSMAMVTMAITGYLLKLGGMTHAQVGGILLVFFIMMVVIIPESGTQRSINDNKLAYVIILVGLVIGGVACNELGWLEKTKADLFGNNMTHAQTVVLPTINWNWLDFRPGAAWSLYVGMATFLTPVFVHWIKNEYGNASLTGITPTAGILGALNQGVPFVKLNTSVGVLLLSVWNNFTTSSMLAAMVMLACHCLFVLPGVRAQCLREAQIRVFHGVAKNPMVDGNPTVDLEKENDMPDLYEKKLALVALGMAAVLNAAMVRTALTTAEMVVLGSAAVGPLLEGNTSAFWNGPLAVAVAGVMRGNHYALIGIVYNLWLLKTARRGGSSALTYGEVWKRQLNLLGKQEFMNYKVSDILEVDRSHAREVLNSGNDAVGVAVSRGSSKLNWLIERGYLRPTGRVVDLGCGRGGWSYTCAAERQVTSVKAYTLGKEGHEKPRLIQSLGWNIIKFKDKSDITRMTPHASDTLLCDIGESSSNPEVEKERTLRVIEAVEKWMSPTTVSFCFKVLAPYKPDVIEALERFQLKHGGGIIRNPYSRNSTHEMYYVSGVRNNILHMVNSTSRMLMRRMSRPSGRSTVVPDLIYPTGTRSVASEAGPLDLEKVKARINRLKEEQESTWFVDSDHPYRTWHYHGSYVAKQSGTAASMINGVVKLLSGPWDRIEEVTNMAMTDTTPFGQQRVFKEKVDTRAPEPPQGTREIMKVVNQWLFDYLGRTKQPRICTKEEFINKVRSHAALGGILTEQEGWSSAAEAVADPRFWSLVDKERQAHLEGRCETCIYNMMGKREKKPSEFGRAKGSRAIWYMWLGARFLEFEALGFLNEDHWLGRENSKAGVEGIGLQYLGYVVEEVARKGNGLVYADDTAGWDTRITEADLEDEQYIMKRMSAEHRQLAWAVMELTYRNKVVKVPRPGPGGKILMDVISRRDQRGSGQVVTYPLNTATNMKVQLIRMAEAENVITRNDVEKVSLITLKELQLWLEVNGVNRLERMAVSGDDCIVAPVDESFAGALHHLNAMSKTRKDISEWENSRGWTDWESVPFCSHHFHTLYLKDGRTIIAPCRCQDELIGRARISPGNGWMIKETAGLSKAYTQMWTLMYFHRRDLRLMANAICSAVPIDWVPTGRTTWSIHATGEWMSSDDMLEVWNKVWIQDNPHVKDKTPIFAWRDVPYIQKGQDRACGSLVGTSLRASWAESIMTSVHRVRMLIGNERYVNYMESMDRYATQRCSAYGELL
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[Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity). [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition.
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C8XPB2
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POLG_EHV
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Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
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MPVRPRNKPKGVNVMAAGKVAQKIKNKLKSKAKAIGNISKGLRGFILFILAQIFWARKLTPRVRTMWKKVDKAKATRVLKGIRNIATQLITGLAGRKKRRSMTHGIILSLGVTMVIGASLHHHGGRYLLNVTHADLGKTFTIGSGNCTANIVEAGSWCSDSMEYECVTLAEAEEPDDIDCWCRGVERVRVTYGRCKNGLDSRRSRRAAVITAHIDKGLTTRQEKWLSTSMGERQIQRIERWMMRNPFYAAISLLLAWWVGSDIKQKVLIAFLVLAIGPAYSTHCVGIPKRDFVQGVQGNTWVNLVLDQGSCVTLSSDNKPSVDIWLDSIFISSPVLVRRVSHTATISDTKVQTACPTNGEAKLEEEASAEYECKKTYSDRGWGNGCGLFGKGSIVACAKYTSTGHMDVYEIDSTKIEYVTKAQVHAGMKHDDTTMVKEVKFEPTTGSMDVEFTGYGTLGLECHVQTMVDMANYYLVVMGQEAWLVHKQWVEDITLPWKIGEGGFWRDKHYMVEFTEPHATTMTVMVLGAQEGALRTALAGAMVVTYTDSSGTKKFSLKGGHVSCKARMNGLVLKGSTYTMCKGGFSFVKTPTDTGHGTAVMQVKVSKGTPCRIPVQAVDSSNGGTNRATLITANPIAATTEDEVMIELSPPYGESYIMIGTGDDKLTYHWHKSGSTIGSLFTETYKGAQRMAIIGDDAWDFSSSSNFFNSIGKALHTVFGNVFHSIFGGLSWITKIILGGMFLWLGVNSRNQTMCMVLMAVGGILLFMTLGVSGEVGCSLDIKRRELKCGDGLFLFNDVNDWTHKYKFHPEDPKLLASLIKKSHQEGRCGLSSVNEVEHRMWNSIKTEINAMFEENGVDLSVVVKDSKLHYKMGSHAFPKVEEGLSLGWKNWGKSLVFEPKQSNVSFIIDGTSEDCPFTNRIWNAFVVEEFGIGMFTTNVFLTHKVDFTKQCDASLLGAGVKGDVAVHGDPTLWMESRKENGTWQLHTIQMNGLRECFWPQTHTIHGSSVMESAMFLPKQYGGPVSHHNHYTGYAVQTAGPWNVQPLIVKRETCPGTQVRVDEQCRDRGNSVRSTTSEGKIIPEWCCRSCTLPPVSFWGPDSCWYAMEIRPQNVHEEHLVRSWASAGTGMAESSLGLVALFLFTDIFARKRMTRKFMVIGCLGVLSVMIVGGFTALDLIRYIIVVGQHFASMNHGGDVAYLAIIAVGKLRPGLLMMYSFKAAWSPKERVMVALGLLVFQAVLGDFVHTGLWEWADAAGMCILIIQGMATRKEKTYIMPILALLTPLSMEIIRKTGIFACVGLLGLSLWRGGDTTMRKGMPLLAGAATAASGLTRASLSVVFILCATAASRRSWPIGEIMAIVGIVGTGFGMAVNDQASLAGPMLVFGLIMIVYATLGRADGLTLKRVGDITWEEEAVHSGSSTRYDVTLNEAGEFKLVHEEPVVWSHVVFLVVALIAASVHPIALVVVTIIWTYGKKHLRGGVLWDIPIAPPVEEAEPLEDGVYAILQSGLMGKAQAGVGVAQEGVFHTMWHVTRGGFLMVGGKRLTPHWASVKRDLICYGGNWKLDGKWDGVEEVQLIAVAPGKAPTNVQTKPGVFRMADGTEIGAVALDYPSGTSGSPIVNEKGQVIGLYGNGIVIGGSGYVSSIAQIAGGEGVTEEPLLDTATMLRKGKLTVLDYHPGAGKTRIFLPYILKECVRRKLRTLVLAPTRVVLSEMREALRDVAVKYHTQAFQAAGTGRELVDAMCHATLSHRMLESSRSVNWEVIIMDEAHYMDPTSIAARGWAAHKANNHESAVIFMTATPPGSANEFPESNGEIEDLRRDIPTEPWNKGHEWILEDRRPTVWFLPSIRAANNIAACLRRSERSVVVLNRQTFETVYPTIKTKKPDFILATDIAEMGANLGVERVIDCRTSYKPVLTTDGRVVIKGPLRIPASAAAQRRGRVGRCKDRDTDSYVYSEETSEDNGHYVCWTEASMLLDNMEVKGGMVAPLYDVEAQKTEMVPGEARLRDDQRKVFRTLIKRYDLPVWVSWQVAKSGLMLEDRKWCFDGDDENTILNDNGEKILARSPGGQRKFLCPRWNDSRLYYDNASLMSFLAFAEGRRSYLGVWHAVQMAPLKLGEKLTESLDTMVMLMRSEEGTRAYKLASTNAPEAVTILLMTGIVVACTLGVGLAFMWPKGVDKMSMGMITMSIAGYLMLQGGLTPVQVASVLLIFFIFMVVLIPEAGTQRSINDNKTLYVLLGVALLIGAITANEMGYLEKTKRDLLGERVQNEWKLELPMFDLRPGAAWSIYVGLATLVMPVLDHWIRTEYGSLSLTGIAQQASILQAMDKGVPFFKLNMSVIVLLVSVWNNFSMLSVLCGVGLLGVHCAFVLPGLRAQAAKQAQRRVYHGVAKNPVVDGQTTAEIETAPEMPPLYEKKLALVLLGVVAIANGVMVRSAFSMAETVVLLSAAVGPLLEGNTSAIWNGPMAVAMAGIMRGNYYAGIGLAYNLWILQSPKRGRSTTMTLGELWKRQLNLMGKREFELYKITDIHEVDRSQAQAVMKAGIDNVGISVSRGTSKLKWMVDRNYVEPLGRVVDLGCGRGGWSYLCAASKRVSSVKAYTLGITGHEKPVNVQSLGWNIIKFKDKTDVFKMEPHACETLLCDIGESSSNPLVEMERTLKVIDNVERWMSPTTESYCFKVLAPYRPEVIERLERFQLKYGGGIVRVPFSRNSTHEMYYVSGVKNNLTHMVSCVSRLLLRRMTHPDGRCKVEADVVFPTGTRNVASDLGPMDLSKVKDRVNRLRSEQGTWFQDDSHPYRTWHYLGSYVAKQSGSAATMVNGVVKMLSMPWDRIENVTQLAMTDTTPYGQQRVFKEKVDTRAPPPPPGTRAIMEVVNKWMFDFLAREKAPRICTKEEFINKVRSNAALGNMLEEQDGWKDAATAVQDPRFWALVDRERQVHLEGRCETCIYNMMGKREKKPAEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWFGRENSLAGVEGVGLQYLGYVVKNVWEKSNGIMYADDTAGWDTRVTEADLDDEQYLLSKMEGYHKKLASAVMNMTYKYKVVKVPRPGPGGKVFMDVIARQDQRGSGQVVTYPLNTGTNMKVQLIRMAEGEGVISRHDIERVTIKTLNALRVWLAENGAERLSRMAVSGDDCVVAPLDERFGLALHHLNAMSKIRKDIDDWTESIPWRSWESVPFCSHHFHQLFLKDGRSIVVPCRDQDELVGRARVSPGNGWKLKETACLSKAYAQMWLLMYFHKRDLRLMGNAICSSVPAHWVPTGRTTWSIHAHNEWISSERMLDVWNKVWIVDNPHMPDKTCIDDWRDVPYLPKSQDRLCGSLIGITARASWAENIRAVVNKIRGMIGNEVYSDHLSVMGRYTYSVQEVGTVL
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[Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity). [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition.
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C8YUV0
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FFAR4_MACFA
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Free fatty acid receptor 4 (G-protein coupled receptor 120) (Omega-3 fatty acid receptor 1)
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MSPECARAAGDAPLRSLEQANRTRFSFFSDVKGDHRLLLAAVETTVLALIFAVSLLGNVCALVLVARRRRRGTTACLVLNLFCADLLFISAIPLVLAVRWTEAWLLGPVACHLLFYLMTLSGSVTILTLAAVSLERMVCIVHLQRGVRGPGRRARAVLLTLIWGYSAVAALPLCVFFRVVPQRLPGADQEISICTLIWPTIAGEISWDVSFVTLNFLVPGLVIVISYSKILQITKASRKRLTVSLAYSESHQIRVSQQDFRLFRTLFLLMVSFFIMWSPIIITILLILIQNFKQDLVIWPSLFFWVVAFTFANSALNPILYNMTLCRNEWKKIFCCFWFPEKGAILTDTSVKRNDLSVISG
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G-protein-coupled receptor for long-chain fatty acids (LCFAs) with a major role in adipogenesis, energy metabolism and inflammation. Signals via G-protein and beta-arrestin pathways. LCFAs sensing initiates activation of phosphoinositidase C-linked G proteins GNAQ and GNA11 (G(q)/G(11)), inducing a variety of cellular responses via second messenger pathways such as intracellular calcium mobilization, modulation of cyclic adenosine monophosphate (cAMP) production, and mitogen-activated protein kinases (MAPKs). After LCFAs binding, associates with beta-arrestin ARRB2 that acts as an adapter protein coupling the receptor to specific downstream signaling pathways, as well as mediating receptor endocytosis (By similarity). In response to dietary fats, plays an important role in the regulation of adipocyte proliferation and differentiation. Acts as a receptor for omega-3 polyunsaturated fatty acids (PUFAs) at primary cilium of perivascular preadipocytes, initiating an adipogenic program via cAMP and CTCF-dependent chromatin remodeling that ultimately results in transcriptional activation of adipogenic genes and cell cycle entry. Induces differentiation of brown and beige adipocytes probably via autocrine and endocrine functions of FGF21 hormone. Contributes to the thermogenic activation of brown adipose tissue and the browning of white adipose tissue. Activates brown adipocytes by initiating intracellular calcium signaling leading to mitochondrial depolarization and fission, and overall increased mitochondrial respiration. Consequently stimulates fatty acid uptake and oxidation in mitochondria together with UCP1-mediated thermogenic respiration, eventually reducing fat mass. Regulates bi-potential differentiation of bone marrow mesenchymal stem cells toward osteoblasts or adipocytes likely by up-regulating distinct integrins. In response to dietary fats regulates hormone secretion and appetite. Stimulates GIP and GLP1 secretion from enteroendocrine cells as well as GCG secretion in pancreatic alpha cells, thereby playing a role in the regulation of blood glucose levels. Negatively regulates glucose-induced SST secretion in pancreatic delta cells. Mediates LCFAs inhibition of GHRL secretion, an appetite-controlling hormone. In taste buds, contributes to sensing of dietary fatty acids by the gustatory system. During the inflammatory response, promotes anti-inflammatory M2 macrophage differentiation in adipose tissue (By similarity). Mediates the anti-inflammatory effects of omega-3 PUFAs via inhibition of NLRP3 inflammasome activation (By similarity). In this pathway, interacts with adapter protein ARRB2 and inhibits the priming step triggered by Toll-like receptors (TLRs) at the level of TAK1 and TAB1 (By similarity). Further inhibits the activation step when ARRB2 directly associates with NLRP3, leading to inhibition of pro-inflammatory cytokine release (By similarity). Mediates LCFAs anti-apoptotic effects (By similarity).
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C8Z543
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ARO1_YEAS8
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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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MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFKASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMVAIGGGVIGDMIGFVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAKREFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGAKNVKVTNQLTNEIDEISNTDIEAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYFGILSPTQVARLSKILVAYGLPVSPDEKWFKELTLHKKTPLDILLKKMSIDKKNEGSKKKVVILESIGKCYGDSAQFVSDEDLRFILTDETLVYPFKDIPADQQKVVIPPGSKSISNRALILAALGEGQCKIKNLLHSDDTKHMLTAVHELKGATISWEDNGETVVVEGHGGSTLSACADPLYLGNAGTASRFLTSLAALVNSTPSQKYIVLTGNARMQQRPIAPLVDSLRANGTKIEYLNNEGSLPIKVYTDSVFKGGRIELAATVSSQYVSSILMCAPYAEEPVTLALVGGKPISKLYVDMTIKMMEKFGINVETSTTEPYTYYIPKGHYINPSEYVIESDASSATYPLAFAAMTGTTVTVPNIGFESLQGDARFARDVLKPMGCKITQTATSTTVSGPPVGTLKPLKHVDMEPMTDAFLTACVVAAISHDSDPNSANTTTIEGIANQRVKECNRILAMATELAKFGVKTTELPDGIQVHGLNSIKDLKVPSDSSGPVGVCTYDDHRVAMSFSLLAGMVNSQNERDEVANPVRILERHCTGKTWPGWWDVLHSELGAKLDGAEPLECTSKKNSKKSVVIIGMRAAGKTTISKWCASALGYKLVDLDELFEQQHNNQSVKQFVVENGWEKFREEETRIFKEVIQNYGDDGYVFSTGGGIVESAESRKALKDFASSGGYVLHLHRDIEETIVFLQSDPSRPAYVEEIREVWNRREGWYKECSNFSFFAPHCSAEAEFQALRRSFSKHIATITGVREIEIPSGRSAFVCLTFDDLTEQTENLTPICYGCEAVEVRVDHLANYSADFVSKQLSILRKATDSIPIIFTVRTMKQGGNFPDEEFKTLRELYDIALKNGVEFLDLELTLPTDIQYEVINKRGNTKIIGSHHDFQGLYSWDDAEWENRFNQALTLDVDVVKFVGTAVNFEDNLRLEHFRDTHKNKPLIAVNMTSKGSISRVLNNVLTPVTSDLLPNSAAPGQLTVAQINKMYTSMGGIEPKELFVVGKPIGHSRSPILHNTGYEILGLPHKFDKFETESAQLVKEKLLDGNKNFGGAAVTIPLKLDIMQYMDELTDAAKVIGAVNTVIPLGNKKFKGDNTDWLGIRNALINNGVPEYVGHTAGLVIGAGGTSRAALYALHSLGCKKIFIINRTTSKLKPLIESLPSEFNIIGIESTKSIEEIKEHVGVAVSCVPADKPLDDELLSKLERFLVKGAHAAFVPTLLEAAYKPSVTPVMTISQDKYQWHVVPGSQMLVHQGVAQFEKWTGFKGPFKAIFDAVTKE
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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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C9JE40
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PATL2_HUMAN
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Protein PAT1 homolog 2 (PAT1-like protein 2) (Protein PAT1 homolog a) (Pat1a) (hPat1a)
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MNCLEGPGKTCGPLASEEELVSACQLEKEEENEGEEEEEEEDEEDLDPDLDPDLEEEENDLGDPAVLGAVHNTQRALLSSPGVKAPGMLGMSLASLHFLWQTLDYLSPIPFWPTFPSTSSPAQHFGPRLPSPDPTLFCSLLTSWPPRFSHLTQLHPRHQRILQQQQHSQTPSPPAKKPWSQQPDPYANLMTRKEKDWVIKVQMVQLQSAKPRLDDYYYQEYYQKLEKKQADEELLGRRNRVESLKLVTPYIPKAEAYESVVRIEGSLGQVAVSTCFSPRRAIDAVPHGTQEQDIEAASSQRLRVLYRIEKMFLQLLEIEEGWKYRPPPPCFSEQQSNQVEKLFQTLKTQEQNNLEEAADGFLQVLSVRKGKALVARLLPFLPQDQAVTILLAITHHLPLLVRRDVADQALQMLFKPLGKCISHLTLHELLQGLQGLTLLPPGSSERPVTVVLQNQFGISLLYALLSHGEQLVSLHSSLEEPNSDHTAWTDMVVLIAWEIAQMPTASLAEPLAFPSNLLPLFCHHVDKQLVQQLEARMEFAWIY
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RNA-binding protein that acts as a translational repressor.
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C9JLW8
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MCRI1_HUMAN
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Mapk-regulated corepressor-interacting protein 1 (Granulin-2) (Protein FAM195B)
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MTSSPVSRVVYNGKRTSSPRSPPSSSEIFTPAHEENVRFIYEAWQGVERDLRGQVPGGERGLVEEYVEKVPNPSLKTFKPIDLSDLKRRSTQDAKKS
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The phosphorylation status of MCRIP1 functions as a molecular switch to regulate epithelial-mesenchymal transition. Unphosphorylated MCRIP1 binds to and inhibits the transcriptional corepressor CTBP(s). When phosphorylated by MAPK/ERK, MCRIP1 releases CTBP(s) resulting in transcriptional silencing of the E-cadherin gene and induction of epithelial-mesenchymal transition.
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C9JR72
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KBTBD_HUMAN
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Kelch repeat and BTB domain-containing protein 13
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MARGPQTLVQVWVGGQLFQADRALLVEHCGFFRGLFRSGMRETRAAEVRLGVLSAGGFRATLQVLRGDRPALAAEDELLQAVECAAFLQAPALARFLEHNLTSDNCALLCDAAAAFGLRDVFHSAALFICDGERELAAELALPEARAYVAALRPSSYAAVSTHTPAPGFLEDASRTLCYLDEEEDAWRTLAALPLEASTLLAGVATLGNKLYIVGGVRGASKEVVELGFCYDPDGGTWHEFPSPHQPRYDTALAGFDGRLYAIGGEFQRTPISSVERYDPAAGCWSFVADLPQPAAGVPCAQACGRLFVCLWRPADTTAVVEYAVRTDAWLPVAELRRPQSYGHCMVAHRDSLYVVRNGPSDDFLHCAIDCLNLATGQWTALPGQFVNSKGALFTAVVRGDTVYTVNRMFTLLYAIEGGTWRLLREKAGFPRPGSLQTFLLRLPPGAPGPVTSTTAEL
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Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex.
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C9JRZ8
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AK1BF_HUMAN
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Aldo-keto reductase family 1 member B15 (EC 1.1.1.-) (EC 1.1.1.300) (EC 1.1.1.54) (Estradiol 17-beta-dehydrogenase AKR1B15) (Farnesol dehydrogenase) (EC 1.1.1.216) (Testosterone 17beta-dehydrogenase) (EC 1.1.1.64)
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MATFVELSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDDFFPKDDKGNMISGKGTFLDAWEAMEELVDEGLVKALGVSNFNHFQIERLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWRAFDFKEFSHLEDFPFDAEY
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[Isoform 1]: Catalyzes the NADPH-dependent reduction of a variety of carbonyl substrates, like aromatic aldehydes, alkenals, ketones and alpha-dicarbonyl compounds. In addition, catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. Displays strong enzymatic activity toward all-trans-retinal and 9-cis-retinal. May play a physiological role in retinoid metabolism.
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C9K4X8
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GSS_PATPE
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Gonad-stimulating substance (Relaxin-like gonad-stimulating peptide) [Cleaved into: Gonad-stimulating substance B chain; Gonad-stimulating substance A chain]
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MTSNNRHLFQATCLVLLLLHAAFHGGALGEKYCDDDFHMAVFRTCAVSKRSQPGMSLSDVLTMNRFRGHNIKRSIDSTLEDNAFFMSGLEKRSEYSGIASYCCLHGCTPSELSVVC
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Induces oocyte maturation and ovulation in vitro in ovarian fragments and induces spawning behavior and gamete release in vivo. Probably mediates its effects by binding to a G-protein coupled receptor located in follicle cell membranes. Following receptor binding, stimulates GTP-dependent adenylyl cyclase activity in follicle cell membranes of fully grown ovaries at stage V but not in young ovaries at stage IV, leading to the production of cAMP. This stimulates the production of the maturation-inducing hormone, 1-methyladenine, in stage V but not stage IV ovaries. The lack of activity in stage IV ovaries may be due to the very low levels of the G-protein alpha s subunit which is not expressed at high levels in follicle cells until stage V.
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C9SE96
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ARO1_VERA1
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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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MSCSNNTEPTRIAILGTDNIVVDHGIWLNWVTKDLFDNVKSSTYVLVTDTNLYDTYVPPFKHAFDGATDTTAGPRLLTLAIPPGEISKSRQSKAHIEDWMLSQQCTRDTVIIALGGGVIGDMLGYVAATFMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPMGKNLVGAFWQPSRIYIDLAFLETLPSREFINGMAEVIKTAAIWDENEFATLEANAPSIVAAVNQPTGPGRLSPIREILKRIVLGSARVKAEVVSSDEREGGLRNLLNFGHSIGHAYEALLTPQLLHGEAVAIGMVKEAELARYLGVLRPSAVARLAKCISSYGLPTSLGDKRVIKLTAGKRCPVDILLQKMAVDKKNDGRKKKIVLLSAIGKTHEPRATTVEDAAIKVMLSASTLITPGVSTKLATTVTPPGSKSISNRALILAALGEGTCRIKNLLHSDDVEFMLTAITRLGGASYAWEDAGEVLVLTGKGGQLRASSDPLYLGNAGTASRFLTTVVALCSPADVSSTVLTGNARMQVRPIGPLVDALRSNGVSIDYLGPGKSLPLRIDAAGGFAGGVIELAATVSSQYVSSILMAAPYAKEPVTLRLVGGKPISQPYIDMTLAMMKTFGVQVERSSSDPNTYHIAKGTYKNPAEYTIESDASSATYPLAIAAITGTTCTVPNIGSSSLQGDARFAIDVLQPMGCTVQQTASSTTVTGPAPGGLLGLPHVDMEPMTDAFLTASVLAAVAAGTTKISGIANQRVKECNRIAAMREQLGKFGIATDEFDDGIIVTGQPLDTLKTPDAGVFCYDDHRVAMSFSVLSTVANAPVTILERECTGKTWPGWWDTLSQSFGLRLNGDDKHPGVEGRHQQDHTTRSVFIVGMRGAGKTTTGRWMAKLLKRPFIDLDEELERRSGMTIPEMIHGTKGWEGFRRDELQLLHDVMENQASGHVFSCGGGIVESPEARKLLIAYKEKGGCVLLVHRDTKQVVDYLLQDKTRPAYREDIEDVYYRRKPLYDECSNFQYFSPHPAASVASRDAPLDFRCFVDAICGDGSKVTKMTAKEQSFFVSLTVPSVDSAVDVIPQVVVGSDAVELRVDLLQDQTPESVARQVSALRSAAGMPIIFTLRTVSQGGCFPDADHTQALSLYILALRMGVEFIDLEMTWPEHILQTVTNLKGRSRIIASHHDPRGELSWKNGSWTPFYNRALQWGSVIKLVGTAQSMEDNYDLARFKSDMLASHPTPVIALNMGALGKLSRVLNGFLTPVSHPALPFKAAPGQLSAAEIRRALFLLGNINAQSFHLFGKPISKSRSPALHNSLFNLTGLPHKYGLVETDQADEVAAVIREPDFGGASVTIPLKLDVMPLLDEVSESAKVIGAVNTIIPMPLDGSQKRRLLGDNTDWRGMVHCLESIGVASESTASTTTASALVIGSGGTTRAAIFALKSHGYHPIYMLARNEQSLETIRASFPTDFDLRALGGPAEVFTLAVAPTVVISTIPADKPMDPSLRETLEVVLKSPVSEQRTRVLLEMAYQPRHTAAMRLAEDAGWRTIPGAEVLAAQGWHQFQMWTGITPRFIDAQAAVNGDEIPTSTD
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
|
C9XI63
|
TEPS3_ANOGA
|
Thioester-containing protein 1 allele S3 (TEP1s) (TEP1-F) [Cleaved into: Thioester-containing protein 1 N-terminal (TEP1-N); Thioester-containing protein 1 C-terminal (TEP1-C)]
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MWQFIRSRILTVIIFIGAAHGLLVVGPKFIRANQEYTLVISNFNSQLSKVDLLLKLEGETDNGLSVLNVTKMVDVRRNMNRMINFNMPEDLTAGNYKITIDGQRGFSFHKEAELVYLSKSISGLIQVDKPVFKPGDTVNFRVIVLDTELKPPARVKSVHVTIRDPQRNVIRKWSTAKLYAGVFESDLQIAPTPMLGVWNISVEVEGEELVSKTFEVKEYVLSTFDVQVMPSVIPLEEHQAVNLTIEANYHFGKPVQGVAKVELYLDDDKLNQKKELTVYGKGQVELRFDNFAMDADQQDVRVKVSFIEQYTNRTVVKQSQITVYRYAYRVELIKESPQFRPGLPFKCALQFTHHDGTPAKGITGKVEVSDVGFETTKTSDNDGLIKLELQPSEGSEQLGINFNAVDGFFFYEDVNKVETVTDAYIKLELKSPIKRNKLMRFMVTCTERMTFFVYYVMSKGNIIDAGFMRPNKQTKYLLQLNATEKMIPKAKILIATVAGRTVVYDYADLDFQELRNNFDLSIDEQEIKPGRQIELSMSGRPGAYVGLAAYDKALLLFNKNHDLFWEDIGQVFDGFHAINENEFDIFHSLGLFARTLDDILFDSANEKTGRNALQSGKPIGKLVSYRTNFQESWLWKNVSIGRSGSRKLIEVVPDTTTSWYLTGFSIDPVYGLGIIKKPIQFTTVQPFYIVENLPYSIKRGEAVVLQFTLFNNLGAEYIADVTLYNVANQTEFVGRPDTDLSYTKSVSVPPKVGVPISFLIKARKLGEMAVRVKASIMLGHETDALEKVIRVMPESLAQPKMDTSFFCFDDYKNQTFPFNLDINKKADNGSKKIEFRLNPNLLTMVIKNLDNLLAVPTGCGEQNMVKFVPNILVLDYLYATGSKEQHLIDKATNLLRQGYQNQMRYRQTDGSFGVWEKSGSSVFLTAFVATSMQTASKYMNDIDAAMVEKALDWLASKQHSSGRFDETGKVWHKDMQGGLRNGVALTSYVLTALLENDIAKVKHAVVIQNGMNYLSNQLAFINNAYDLSIATYAMMLNGHTMKKEALDKLIDMSISDNNKKERYWGTTNQIETTAYALLSFVMAEKYLDGIPIMNWLVNQRYVTGSFPRTQDTFVGLKALTKLAEKISPSRNDYTVQLKYKKSTKYFNINSEQIDFQNFLEIPEDTKKLEINVGGIGFGLLEVIYQFDLNLVNFEHRFKLDLEKQNTGSDYELRLRVCANYIPELTDSQSNMALIEVTLPSGYVVDRNPISEQTTVNPIQNMEIRYGGTSVVLYYYNMGTERNCFTVTAYRRFKVALKRPAYVVVYDYYNTNLNAIKVYEVDKQNVCEICEEEDCPAEC
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Plays an essential role in the innate immune response against bacteria, fungi and protozoa infection. After proteolytic cleavage, the protein C-terminus binds covalently through a thioester bond to the pathogen surface resulting in pathogen clearance either by melanization or lysis. Initiate the recruitment and activation of a cascade of proteases, mostly of CLIP-domain serine proteases, which leads to the proteolytic cleavage of the prophenoloxidase (PPO) into active phenoloxidase (PO), the rate-limiting enzyme in melanin biosynthesis. In response to parasite P.berghei-mediated infection, binds to and mediates killing of ookinetes, as they egress from midgut epithelial cells into the basal labyrinth, by both lysis and melanization. During bacterial infection, binds to both Gram-positive and Gram-negative bacteria but only promotes phagocytosis of Gram-negative bacteria. Promotes the accumulation of SPCLIP1 onto the surface of P.berghei ookinetes and bacterium E.coli which leads to the melanization of the pathogen. Recruits CLIPA2 to bacteria surface. In response to bacterial infection, required for periostial hemocyte aggregation, but not for the aggregation of sessile hemocytes in non-periostial regions. During the late stage of fungus B.bassiana-mediated infection, required for the initiation of hyphae melanization by binding to the surface of hyphae and recruiting prophenoloxidase PPO to them. Plays a role in male fertility by binding to defective sperm cells and promoting their removal during spermatogenesis (By similarity).
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C9XI66
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TEPR1_ANOGA
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Thioester-containing protein 1 allele R1 (TEP1r) (TEP1-F) [Cleaved into: Thioester-containing protein 1 N-terminal (TEP1-N); Thioester-containing protein 1 C-terminal (TEP1-C)]
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MWQFIRSRILTVIIFIGAAHGLLVVGPKFIRANQEYTLVISNFNSQLSKVDLLLKLEGETDNGLSVLNVTKMVDVRRNMNRMINFNMPEDLTAGNYKITIDGQRGFSFHKEAELVYLSKSISGLIQVDKPVFKPGDTVNFRVIVLDTELKPPARVKSVYVTIRDPQRNVIRKWSTAKLYAGVFESDLQIAPTPMLGVWNISVEVEGEELVSKTFEVKEYVLSTFDVQVMPSVIPLEEHQAVNLTIEANYHFGKPVQGVAKVELYLDDDKLKLKKELTVYGKGQVELRFDNFAMDADQQDVPVKVSFVEQYTNRTVVKQSQITVYRYAYRVELIKESPQFRPGLPFKCALQFTHHDGTPAKGISGKVEVSDVRFETTTTSDNDGLIKLELQPSEGTEQLSIHFNAVDGFFFYEDVNKVETVTDAYIKLELKSPIKRNKLMRFMVTCTERMTFFVYYVMSKGNIIDAGFMRPNKQPKYLLQLNATEKMIPRAKILIATVAGRTVVYDFADLDFQELRNNFDLSIDEQEIKPGRQIELSMSGRPGAYVGLAAYDKALLLFNKNHDLFWEDIGQVFDGFHAINENEFDIFHSLGLFARTLDDILFDSANEKTGRNALQSGKPIGKLVSYRTNFQESWLWKNVSIGRSGSRKLIEVVPDTTTSWYLTGFSIDPVYGLGIIKKPIQFTTVQPFYIVENLPYSIKRGEAVVLQFTLFNNLGAEYIADVTLYNVANQTEFVGRPNTDLSYTKSVSVPPKVGVPISFLIKARKLGEMAVRVKASIMLGHETDALEKVIRVMPESLVQPRMDTRFFCFDDHKNQTFPINLDINKKADSGSTKIEFRLNPNLLTTVIKNLDHLLGVPTGCGEQNMVKFVPNILVLDYLHAIGSKEQHLIDKATNLLRQGYQNQMRYRQTDGSFGLWETTNGSVFLTAFVGTSMQTAVKYISDIDAAMVEKALDWLASKQHFSGRFDKAGAEYHKEMQGGLRNGVALTSYVLMALLENDIAKAKHAEVIQKGMTYLSNQFGSINNAYDLSIATYAMMLNGHTMKEEALNKLIDMSFIDADKNERFWNTTNPIETTAYALLSFVMAEKYTDGIPVMNWLVNQRYVTGSFPSTQDTFVGLKALTKMAEKISPSRNDYTVQLKYKKSAKYFKINSEQIDVENFVDIPEDTKKLEINVGGIGFGLLEVVYQFNLNLVNFENRFQLDLEKQNTGSDYELRLKVCASYIPQLTDRRSNMALIEVTLPSGYVVDRNPISEQTKVNPIQKTEIRYGGTSVVLYYDNMGSERNCFTLTAYRRFKVALKRPAYVVVYDYYNTNLNAIKVYEVDKQNLCEICDEEDCPAEC
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Plays an essential role in the innate immune response against bacteria, fungi and protozoa infection. After proteolytic cleavage, the protein C-terminus binds covalently through a thioester bond to the pathogen surface resulting in pathogen clearance either by melanization or lysis. Initiate the recruitment and activation of a cascade of proteases, mostly of CLIP-domain serine proteases, which leads to the proteolytic cleavage of the prophenoloxidase (PPO) into active phenoloxidase (PO), the rate-limiting enzyme in melanin biosynthesis (By similarity). In response to parasite P.berghei-mediated infection, binds to and mediates killing of ookinetes, as they egress from midgut epithelial cells into the basal labyrinth, by both lysis and melanization. During bacterial infection, binds to both Gram-positive and Gram-negative bacteria but only promotes phagocytosis of Gram-negative bacteria (By similarity). Promotes the accumulation of SPCLIP1 onto the surface of P.berghei ookinetes and bacterium E.coli which leads to the melanization of the pathogen (By similarity). Recruits CLIPA2 to bacteria surface (By similarity). In response to bacterial infection, required for periostial hemocyte aggregation, but not for the aggregation of sessile hemocytes in non-periostial regions (By similarity). During the late stage of fungus B.bassiana-mediated infection, required for the initiation of hyphae melanization by binding to the surface of hyphae and recruiting prophenoloxidase PPO to them (By similarity). Plays a role in male fertility by binding to defective sperm cells and promoting their removal during spermatogenesis.
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D0E0C2
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SCNA1_PERAM
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Sodium channel protein PaFPC1 (PaFPC1) (NavPaS)
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MADNSPLIREERQRLFRPYTRAMLTAPSAQPAKENGKTEENKDNSRDKGRGANKDRDGSAHPDQALEQGSRLPARMRNIFPAELASTPLEDFDPFYKNKKTFVVVTKAGDIFRFSGEKSLWMLDPFTPIRRVAISTMVQPIFSYFIMITILIHCIFMIMPATQTTYILELVFLSIYTIEVVVKVLARGFILHPFAYLRDPWNWLDFLVTLIGYITLVVDLGHLYALRAFRVLRSWRTVTIVPGWRTIVDALSLSITSLKDLVLLLLFSLFVFAVLGLQIYMGVLTQKCVKHFPADGSWGNFTDERWFNYTSNSSHWYIPDDWIEYPLCGNSSGAGMCPPGYTCLQGYGGNPNYGYTSFDTFGWAFLSVFRLVTLDYWEDLYQLALRSAGPWHILFFIIVVFYGTFCFLNFILAVVVMSYTHMVKRADEEKAAERELKKEKKAASVANNTANGQEQTTIEMNGDEAVVIDNNDQAARQQSDPETPAPSVTQRLTDFLCVWDCCVPWQKLQGAIGAVVLSPFFELFIAVIIVLNITFMALDHHDMNIEFERILRTGNYIFTSIYIVEAVLKIIALSPKFYFKDSWNVFDFIIVVFAILELGLEGVQGLSVFRSFRLLRVFRLAKFWPTLNNFMSVMTKSYGAFVNVMYVMFLLLFIFAIIGMQLFGMNYIDNMERFPDGDLPRWNFTDFLHSFMIVFRALCGEWIESMWDCMLVGDWSCIPFFVAVFFVGNLVILNLLIALLLNNYGSFCTSPTSDEEDSKDEDALAQIVRIFKRFKPNLNAVKLSPMKPDSEDIVESQEIQGNNIADAEDVLAGEFPPDCCCNAFYKCFPSRPARDSSVQRMWSNIRRVCFLLAKNKYFQKFVTAVLVITSVLLALEDIYLPQRPVLVNITLYVDYVLTAFFVIEMIIMLFAVGFKKYFTSKWYWLDFIVVVAYLLNFVLMCAGIEALQTLRLLRVFRLFRPLSKVNGMQVVTSTLVEAVPHIFNVILVGIFFWLVFAIMGVQLFAGKFYKCVDENSTVLSHEITMDRNDCLHENYTWENSPMNFDHVGNAYLSLLQVATFKGWLQIMNDAIDSREVHKQPIRETNIYMYLYFIFFIVFGSFFILKLFVCILIDIFRQQRRKAEGLSATDSRTQLIYRRAVMRTMSAKPVKRIPKPTCHPQSLMYDISVNRKFEYTMMILIILNVAVMAIDHYGQSMEFSEVLDYLNLIFIIIFFVECVIKVSGLRHHYFKDPWNIIDFLYVVLAIAGLMLSDVIEKYFISPTLLRILRILRVGRLLRYFQSARGMRLLLLALRKALRTLFNVSFLLFVIMFVYAVFGMEFFMHIRDAGAIDDVYNFKTFGQSIILLFQLATSAGWDGVYFAIANEEDCRAPDHELGYPGNCGSRALGIAYLVSYLIITCLVVINMYAAVILDYVLEVYEDSKEGLTDDDYDMFFEVWQQFDPEATQYIRYDQLSELLEALQPPLQVQKPNKYKILSMNIPICKDDHIFYKDVLEALVKDVFSRRGSPVEAGDVQAPNVDEAEYKPVSSTLQRQREEYCVRLIQNAWRKHKQQN
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Mediates the voltage-dependent sodium ion permeability of excitable membranes.
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D0E8I5
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PHNZ_UNCHF
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2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming) (EC 1.13.11.78) (Di-iron oxygenase) (Nonheme iron-dependent oxygenase)
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MSLSNSSKVSVLISLLEKSRDLDYIGEAINQLEHSLQCAYFAQRSGADNEMVLAALLHDLGHYCNDTSFEDMGGYGVWQHEKVGADYLRGLGFSERVACLIEGHVAAKRYLVSSKASYLKNLSDASRKTLEYQGGPMDEGERRLFEEREDFKDCLKIRAWDEKGKQTDLKVPGPEHYRKMMEEHLSENQN
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Involved in the degradation of the organophosphonate 2-aminoethylphosphonic acid (2-AEP) (Probable). Catalyzes the cleavage of the carbon-phosphorus bond of (2-amino-1-hydroxyethyl)phosphonic acid to yield glycine and phosphate through an oxidative mechanism. It reacts stereospecifically with the R-enantiomer of (2-amino-1-hydroxyethyl)phosphonic acid and is also able to use (R,R)-2-amino-1-hydroxypropylphosphonate as substrate.
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D0EM77
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KLY_TANFA
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Karilysin (EC 3.4.24.-) (Matrix metalloprotease-like enzyme) (MMP-like enzyme) [Cleaved into: Karilysin long form Kly38; Karilysin short form Kly18]
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MKRFILLFFLSTIAIFKVYSQRLYDNGPLTGDNNYVLQGSKWNKTTLKYYIYNSSSHLTTTERENAIRSAFALWSDKSTLSFIQVYNPNQADIKIKWEKGNHGDGYPFDGNTGILAHAFYPPPAGGNYAGHLHFDGDENWSINGSGIDLITVAAHEIGHLLGIEHSNVSSALMYPYYTGIKRQLDNDDCLAVWDLYGYPFSISGPSSVCDQATYTVENLLSGATVQWSVSNPNIATINSSNGVLTCRGNGICEVRATINNSSVALTPLKICLGTPISQDITLTVESLNSNGTLCTDNPNAIMADHPGGNHLGYIREYEWRISNGWQIAHHPGDNGIYADHFIVTVIPLSPLPGSPTVSVRARSECGWGTWKEVQIPAVSCSRTISPFTLSPNPATDEVILQLMETDEVSGLSVLSTDRSAYEIQIWSGMRMLRSFRTNEPTFQISMTGLPAGLYFVRVVKNGQTYTQKLIKK
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Metalloprotease able to cleave casein, gelatin, elastin, fibrinogen and fibronectin. Shows exclusive preference for hydrophobic residues, especially Leu, Tyr and Met, at the P1' position of substrates, and for Pro or Ala at P3. Can efficiently cleave the antimicrobial peptide LL-37 which is a component of the immune system, leading to a significant reduction of its bactericidal activity. Is also able to inhibit all pathways of the human complement system. The classical and lectin complement pathways are inhibited because of the efficient degradation of mannose-binding lectin, ficolin-2, ficolin-3, and C4 by karilysin, whereas inhibition of the terminal pathway is caused by cleavage of C5. Thus, karilysin appears to be a major virulence factor of T.forsythia that contributes to evasion of the human immune response and periodontal disease. Seems to act synergistically with gingipains from the periodontal pathogen P.gingivalis present at the same sites of infection.
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D0EZM8
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NS1_HBOC1
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Initiator protein NS1 (NS1) (EC 3.1.21.-) (EC 3.6.4.12) (Non-structural protein 1) (Non-structural protein NS1)
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MAFNPPVIRAFSQPAFTYVFKFPYPQWKEKEWLLHALLAHGTEQSMIQLRNCAPHPDEDIIRDDLLISLEDRHFGAVLCKAVYMATTTLMSHKQRNMFPRCDIIVQSELGEKNLHCHIIVGGEGLSKRNAKSSCAQFYGLILAEIIQRCKSLLATRPFEPEEADIFHTLKKAEREAWGGVTGGNMQILQYRDRRGDLHAQTVDPLRFFKNYLLPKNRCISSYSKPDVCTSPDNWFILAEKTYSHTLINGLPLPEHYRKNYHATLDNEVIPGPQTMAYGGRGPWEHLPEVGDQRLAASSVSTTYKPNKKEKLMLNLLDKCKELNLLVYEDLVANCPELLLMLEGQPGGARLIEQVLGMHHINVCSNFTALTYLFHLHPVTSLDSDNKALQLLLIQGYNPLAVGHALCCVLNKQFGKQNTVCFYGPASTGKTNMAKAIVQGIRLYGCVNHLNKGFVFNDCRQRLVVWWEECLMHQDWVEPAKCILGGTECRIDVKHRDSVLLTQTPVIISTNHDIYAVVGGNSVSHVHAAPLKERVIQLNFMKQLPQTFGEITATEIAALLQWCFNEYDCTLTGFKQKWNLDKIPNSFPLGVLCPTHSQDFTLHENGYCTDCGGYLPHSADNSMYTDRASETSTGDITPSDLGDSDGEDTEPETSQVDYCPPKKRRLTAPASPPNSPASSVSTITFFNTWHAQPRDEDELREYERQASLLQKKRESRKRGEEETLADNSSQEQEPQPDPTQWGERLGFISSGTPNQPPIVLHCFEDLRPSDEDEGEYIGEKRQ
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Multifunctional protein which displays endonuclease and helicase activities required for initiating and directing viral DNA replication. Also plays a role in viral packaging and transactivation of several promoters. Binds site-specifically to 2-3 approximate tandem copies within the origins of replication (Ori), unwinds this hairpin region and nicks one DNA strand thereby initiating the rolling circle replication (RCR). Becomes covalently attached to the 5' end of the nick and provides a 3'OH for priming DNA synthesis. The helicase activity unwinds DNA in a 3'-5' direction on the longer strand. Participates in the transcriptional regulation of several promoters.
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D0FH76
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VPS4_BOMMO
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Vacuolar protein sorting-associated protein 4 (EC 3.6.4.6) (BmVps4) (Vacuolar protein sorting 4)
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MTSSNTLQKAIDLVTKATEEDKNKNYEEALRLYEHGVEYFLHAVKYEAQGERAKESIRAKCLQYLDRAEKLKEYLKKDQKKKPVKDGESKSDDKKSDSDSDSDDPEKKKLQGKLEGAIVVEKPHVKWSDVAGLEAAKEALKEAVILPIKFPHLFTGKRIPWKGILLFGPPGTGKSYLAKAVATEANNSTFFSVSSSDLVSKWLGESEKLVKNLFDLARQHKPSIIFIDEIDSLCSSRSDNESESARRIKTEFLVQMQGVGNDMDGILVLGATNIPWVLDSAIRRRFEKRIYIALPEEHARLDMFKLHLGNTRHQLSEQDMKLLAAKSEGYSGADISIVVRDALMQPVRKVQSATHFKKISGPSPTDPNVIVNDLLTPCSPGDPGAIEMTWIDVPSDKLGEPPVTMSDMLRSLAVSKPTVNDDDMVKLRKFMEDFGQEG
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Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane.
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D0NPN8
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A3AEM_PHYIT
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RxLR effector protein Avr3a (Avirulence protein 3a)
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MRLAIMLSATAVAINFATSSAIDQTKVLVYGTPAHYIHDSAGRRLLRKNEENEETSEERAPNFNLANLNEEMFNVAALTERADAKKLAKQLMGNDKLADAAYMWWQHNRVTLDQIDTFLKLASRKTQGAKYNQIYNSYMMHLGLTGY
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Multifunctional effector that can suppress host BAK1/SERK3-mediated immunity through at least two different pathways. Manipulates plant immunity by targeting and stabilizing host E3 ligase CMPG1. By preventing the normal 26S proteasome-dependent degradation of potato CMPG1, and thus potentially of its protein substrates in the host cell, Avr3a further abolishes host cell death during the biotrophic phase of infection. Associates with and affects also the function of the dynamin-related protein 2 (DRP2), a plant GTPase involved in immune receptor-mediated endocytosis. The Avr3a(EM) form evades recognition by R3a, thus does not trigger R3a-mediated hypersensitivity and does not suppress INF1-induced cell death.
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D0P3S7
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ABLB1_PHYIT
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RxLR effector protein Avrblb1 (Avirulence protein Avrblb1) (In planta-induced protein O1) (IPI-O1)
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MRSLLLTVLLNLVVLLATTGAVSSNLNTAVNYASTSKIRFLSTEYNADEKRSLRGDYNNEVTKEPNTSDEERAFSISKSAEYVKMVLYGFKLGFSPRTQSKTVLRYEDKLFTALYKSGETPRSLRTKHLDKASASVFFNRFKKWYDKNVGPS
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Secreted effector that acts as an elicitor of hypersensitive response (HR) specifically on plants carrying defense protein RGA2/Rpi-blb1. Enhances P.infestans colonization of plant hosts Nicotiana benthamiana and potato Solanum bulbocastanum leaves. Associates with host legume-type lectin receptor kinases and disrupts attachments between the host plasma membrane and cell wall.
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D0PRN2
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NRX1B_CHICK
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Neurexin-1-beta (Neurexin I-beta)
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MGGFLRGSPEPGPAGGSGGSAGGRLALLWIVPLTLSGLLGVAWGASSLGAHHIHHFHGSSKHHSVPIAIYRSPASLRGGHAGTTYIFSKGGGQITYTWPPNDRPSTRADRLAIGFSTVQKEAVLVRVDSSTGLGDYLELHIHQGKIGVKFNVGTDDIAIEEINAIINDGKYHVVRFTRSGGNATLQVDNWPVIERYPAGNNDNERLAIARQRIPYRLGRVVDEWLLDKGRQLTIFNSQATIKIGGKERGHPFQGQLSGLYYNGLKVLNMAAENDANIVIEGNVRLVGEVPSSMTTESTATAMQSEMSTSVMETTTTLATSTARRGKAPTKEPIGQTTDDILVASAECPSDDEDIDPCEPSSGGLANPTRAGGGREYPGSSEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYHVDESRNYISNSAQSNGAVIKEKQPNSAKSSNKNKKNKDKEYYV
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Neuronal cell surface protein that may be involved in cell recognition and cell adhesion by forming intracellular junctions through binding to neuroligins. May play a role in formation or maintenance of synaptic junctions. May mediate intracellular signaling (By similarity). Plays a role in angiogenesis. {ECO:0000250, ECO:0000269|PubMed:19926856}.
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D0PV95
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DDX3_CAEEL
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ATP-dependent RNA helicase laf-1 (EC 3.6.4.13) (DEAD-box RNA helicase laf-1)
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MESNQSNNGGSGNAALNRGGRYVPPHLRGGDGGAAAAASAGGDDRRGGAGGGGYRRGGGNSGGGGGGGYDRGYNDNRDDRDNRGGSGGYGRDRNYEDRGYNGGGGGGGNRGYNNNRGGGGGGYNRQDRGDGGSSNFSRGGYNNRDEGSDNRGSGRSYNNDRRDNGGDGQNTRWNNLDAPPSRGTSKWENRGARDERIEQELFSGQLSGINFDKYEEIPVEATGDDVPQPISLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDGPDAVHRSVTSSGGRKKQYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGRENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRMLDMGFEPQIRQIVECNRMPSKEERITAMFSATFPKEIQLLAQDFLKENYVFLAVGRVGSTSENIMQKIVWVEEDEKRSYLMDLLDATGDSSLTLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSFFNDKNRNIARELMDLIVEANQELPDWLEGMSGDMRSGGGYRGRGGRGNGQRFGGRDHRYQGGSGNGGGGNGGGGGFGGGGQRSGGGGGFQSGGGGGRQQQQQQRAQPQQDWWS
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Multifunctional ATP-dependent RNA helicase. Plays a role in RNA remodeling, but is not required for RNA unwinding. Binds to RNA in a concentration-dependent manner to stimulate annealing between two complementary strands of RNA. This process is also dependent upon ATP ATP reduces binding to RNA and subsequently diminishes RNA annealing. Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities. Involved in the regulation of transcription and translation initiation. Involved in innate immunity (By similarity). Involved in both stress and inflammatory responses (By similarity). Promotes liquid-liquid phase separation of P granules, which is a process important for intracellular organization and stress granule assembly. Required for embryonic development. Plays a role in sexual cell fate determination by negatively regulating the translation of the sex determining protein tra-2. May play a protective role in the response to heat and oxidative stress. May negatively regulate extrinsic apoptotic signaling pathway via death domain receptors. May be involved in mitotic chromosome segregation (By similarity).
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D0Q0Y7
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CNIH3_RAT
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Protein cornichon homolog 3 (CNIH-3) (Cornichon family AMPA receptor auxiliary protein 3)
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MAFTFAAFCYMLSLVLCAALIFFAIWHIIAFDELRTDFKSPIDQCNPVHARERLRNIERICFLLRKLVLPEYSIHSLFCVMFLCAQEWLTLGLNVPLLFYHFWRYFHCPADSSELAYDPPVVMNADTLSYCQKEAWCKLAFYLLSFFYYLYCMIYTLVSS
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Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by regulating their rates of activation, deactivation and desensitization.
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D0QMC3
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MNDAL_MOUSE
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Myeloid cell nuclear differentiation antigen-like protein
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MAEYKKIVLLKGLESMEDYQFRTVKSLLRKELKLTKKLQEDYDRIQLADWMEDKFPKYAGLDKLIKVCEHIKDLKDLAKKLKTEKAKVQKKKQGKCKTAVKKKGQDELSSSESLFINKESYKSVPSSKKKGKAIAKTEGEKKNKLTQDQDHLPETSGTDIKTEEDCLQNSPKPPPTSPSSSSNKKKRKEITKTEGGKKKKLTQEQAQLPEPLGTDIKKDEDCLQTPPKPPPTPPSSSLNKKRKSRREEETGVKKSKAAKEPDQPPCCEEPTARCQSPILHSSSSASSNIPSATNQKPQPQNQNIPRGAVLHSEPLTVMVLTATDPFEYESPEHEVKNMFHATVATVSQYFHVKVFNINLKEKFTKKNFIIISNYFESKGILEINETSSVLKADPDQMIEVPNNIIRNANASPKICDIQKGTSGAVFYGVFTLHKKKVKTQNTSYEIKDGSGSIEVEGSGQWHNINCKEGDKLHLFCFHLKRERGQPKLVCGDHSFVKIKVTKAGKKKEASTVLSSTKNEEENNYPKDGIKVEMPDYHV
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Suppresses cell growth when expressed ectopically.
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D0TZF0
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ISOA1_ORYSJ
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Isoamylase 1, chloroplastic (OsISA1) (EC 3.2.1.68) (Protein SUGARY-1)
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MASLPHCLSARPLVVAAAPGRPGPGPGPWLRGGARRRNAAFSAGNAGRRVGLRRSVASAVEVGVGEDEEEGVEEEEEEVEAVVMPERYALGGACRVLAGMPAPLGATALDGGVNFAVYSAGASAASLCLFTPDDLEADEVTEEVPLDPLFNRTGNVWHVFIEGELHNMLYGYRFDGMFAPHCGQYFDVSNVVVDPYAKAVISRGEYGVPGPGGDCWPQMAGMIPLPYSTFDWQGDLPLRYPQKDLVIYEMHLRGFTKHSSSNVEHPGTYIGAISKLDYLKELGVNCVELMPCHEFNELEYFSCSSKMNFWGYSTINFFSPMIRYSSGGIRNCGRDAINEFKTFVREAHKRGIEVIMDVVFNHTAEGNEKGPILSFRGIDNSTYYMLAPKGEFYNYSGCGNTFNCNHPVVREFIVDCLRYWVTEMHVDGFRFDLASIMTRGCSLWDPVNVYGSPVEGDMTTTGTPLATPPLIDMISNDPILGDVKLIAEAWDAGGLYQVGQFPHWKIWSEWNGKYRDIVRQFIKGTDGFAGGFAECLCGSPHLYQAGGRKPWHSINFVCAHDGFTLADLVTYNKKYNSSNGEDNRDGENHNLSWNCGEEGEFAGLSVKRLRKRQMRNFFVSLMVSQGVPMFYMGDEYGHTKGGNNNTYCHDHYVNYFRWDKKEESSDLQRFCSLMTKFRKQCESLGLADFPTAQRLHWHGHQPGKPDWSETSRFVAFSTKDETKGEIYVAFNASHLPAVVGLPERPGYRWEPLVDTGKPAPYDFLTDDLPDRAHAVHLFSHFLNSNLYPMLSYSSIILELQPDD
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Starch-debranching enzyme involved in amylopectin biosynthesis in endosperm. Functions by removing excess branches or improper branches that interfere with the formation of double helices of the cluster chains of amylopectin and crystallization of starch. Works as ISA1 homooligomer or together with ISA2 as heterooligomer. The heterooligomer ISA1 and ISA2 possesses higher affinity than the ISA1 homooligomer for various branched polyglucans in vitro, but no marked differences exist in chain preferences for debranching of amylopectin and phytoglycogen between these forms.
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D0VWM8
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TADBP_CAEEL
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Tar DNA-binding protein homolog 1
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MADETPKVKTEPAAEVKSPLDEVKEIRKEAELTQTGSDEKKTTDPEFITVQDPNGDEPIELPTVDGVVLMTTLQASFPGATGLKYKNPKTGANRAVQVDPSGLKLIAPADGWENKTFFVIVAPQSERVRALSSADATSAKRRKVGSSDDSDSDDGRDGRSGRKRAVERDSQPVDLIVLGVDFKTTDECFQKYFEDIGTVVFCEIKRKSDGNSKGFGFVRMSSVGEQNKVLAIPQHMIDGRRCDVKVPDGRSLQDKQGRPSISRIFVGRLTDKVDEHQLRKVFGDEAKSYIETAVVTDVFIPKPFRGFAFVTLSSAEAAERIVSKGSLTVNGLSVGLSIAQPREENNQSVGPDYGLPAGYRNRRERDRPDRRPIQNEAPLPMPFVRPPQDYSYRQQNSPLERRYWAPGDSRGPGW
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RNA-binding protein which regulates transcription, splicing and RNA-editing. Limits the accumulation of double-stranded RNA by maintaining the abundance of the mature RNA transcripts that are formed from double-stranded precursor RNAs. Stress response protein that acts downstream of daf-16 in the insulin/IGF pathway to regulate longevity and the cellular stress response to osmotic, oxidative, proteotoxic and endoplasmic reticulum stress. Involved in the regulation of physiological processes including aging, fertility, growth and locomotion. Plays a role in maintaining localization of chromobox protein homolog hpl-2 to gene bodies, perhaps acting via binding to nascent RNA transcripts.
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D0VWR8
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PSBD_THEVL
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Photosystem II D2 protein (PSII D2 protein) (EC 1.10.3.9) (Photosystem Q(A) protein)
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ERGWFDILDDWLKRDRFVFVGWSGILLFPCAYLALGGWLTGTTFVTSWYTHGLASSYLEGCNFLTVAVSTPANSMGHSLLLLWGPEAQGDFTRWCQLGGLWTFIALHGAFGLIGFMLRQFEIARLVGVRPYNAIAFSAPIAVFVSVFLIYPLGQSSWFFAPSFGVAAIFRFLLFFQGFHNWTLNPFHMMGVAGVLGGALLCAIHGATVENTLFQDGEGASTFRAFNPTQAEETYSMVTANRFWSQIFGIAFSNKRWLHFFMLFVPVTGLWMSAIGVVGLALNLRSYDFISQEIRAAEDPEFETFYTKNLLLNEGIRAWMAPQDQPHENFVFPEEVLPRGNAL
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Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex. {ECO:0000255|HAMAP-Rule:MF_01383, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:23426624}.
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D0VWU3
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LAC1_TRAMX
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Laccase (EC 1.10.3.2) (Benzenediol:oxygen oxidoreductase) (Diphenol oxidase) (Urishiol oxidase)
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AVGPVADNTITDAATSPDGFSRQAVVVNGVTPGPLVAGNIGDRFQLNVIDNLTNHTMLKTTSVHWHGFFQQGTNWADGPAFINQCPISPGHSFLYDFQVPNQAGTFWYHSHLSTQYCDGLRGPFVVYDPNDPHASRYDVDNDDTVITLADWYHTAAKLGPRFPAGADATLINGKGRAPSDTSAELSVIKVTKGKRYRFRLVSLSCDPNFTFSIDGHNLTIIEVDSSNSQPLSVDSIQIFAAQRYSFVLNANQAVDNYWIRANPNFGNVGFNGGINSAILRYDGAPAVEPTTNQTTSVKPLNEVNLHPLVSTPVPGSPSSGGVDKAINMAFNFNGSNFFINGASFVPPSVPVLLQILSGAQTAQDLLPSGSVYVLPSNASIEISFPATAAAPGAPHPFHLHGHTFAVVRSAGSTVYNYSNPIFRDVVSTGTPAAGDNVTIRFLTNNPGPWFLHCHIDFHLEGGFAVVQAEDVPDVKATNPVPQAWSDLCPTYDANAPSDQ
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Lignin degradation and detoxification of lignin-derived products.
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D0VWV4
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C560_PIG
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Succinate dehydrogenase cytochrome b560 subunit, mitochondrial (Succinate-ubiquinone oxidoreductase cytochrome B large subunit) (CYBL)
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MAALLLRHVGRHCLRAHLSPQLCIRNAVPLGTTAKEEMERFWNKNLGSNRPLSPHITIYRWSLPMAMSICHRGTGIALSAGVSLFGLSALLLPGNFESHLELVKSLCLGPTLIYTAKFGIVFPLMYHTWNGIRHLIWDLGKGLTIPQLTQSGVVVLILTVLSSVGLAAM
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Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
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D0VWY5
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GASHR_MARGR
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Glutathione amide reductase (GAR) (EC 1.8.1.16)
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MTQHFDLIAIGGGSGGLAVAEKAAAFGKRVALIESKALGGTCVNVGCVPKKVMWYASHLAEAVRDAPGFGVQASGGTLDWPRLVAGRDRYIGAINSFWDGYVERLGITRVDGHARFVDAHTIEVEGQRLSADHIVIATGGRPIVPRLPGAELGITSDGFFALQQQPKRVAIIGAGYIGIELAGLLRSFGSEVTVVALEDRLLFQFDPLLSATLAENMHAQGIETHLEFAVAALERDAQGTTLVAQDGTRLEGFDSVIWAVGRAPNTRDLGLEAAGIEVQSNGMVPTDAYQNTNVPGVYALGDITGRDQLTPVAIAAGRRLAERLFDGQSERKLDYDNIPTVVFAHPPLSKVGLSEPEARERLGDVLTVYETSFTPMRYALNEHGPKTAMKLVCAGPEQRVVGVHVIGDGADEMLQGFAVAVKMGATKADFDNTVAIHPGSAEELVTLKEPVRRPGDPLPEGAA
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Catalyzes the reduction of glutathione amide disulfide (GASSAG) to restore glutathione amide (GASH) in the presence of NADH. May play a role in GASH metabolism under anaerobic conditions as a sulfide carrier necessary for cytoplasmic sulfide oxidation.
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D0VYS2
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HSF3_MOUSE
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Heat shock factor protein 3 (HSF 3) (Heat shock transcription factor 3) (HSTF 3) (mHSF3)
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MEQFRKTMVPHFLTKLWILVDDAVLDHVIRWGKDGHSFQIVNEETFAREVLPKYFKHNKITSFIRQLNMYGSRKVFALQTEKTSQENKISIEFQHPLFKRGEACLLANIKRKVPTIKIEGASLYSDEFQKIVTEMQEFKDMQRKMDAKYTQMKQDYSNLYHEVTNLRKKYCAQQQLLTRVLHFILDLMSENHTVLKKRKRSLSFISEDSDSEWDHQYFRIPEDKKEAMEILKDGYELVEDKYKSLLDRVMPILKESKKLISSGDQPSGDDGEHPKVPVQDKPMNEESLTIQLDLTIPVLPEQITEESVEQEPKDISLELDLSSQDSILMKDKSDNLYNNIINRDKKDMHHTEGNLLELNSLLSRKALNYDSDHFSESLSLMKNEEEKSQLDLSGGKDNHMIQCMETPELFLLDEIPMCDFGENLQDYDRLLEDLKNPPNVISALCDHDYVTSNISTLQEDTIENSIPQLCMEANGESSVFPFLILNPVTNIF
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DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription of non-classical heat-shock genes such as PDZD2 and PROM2. Protects cells against heat shock and proteotoxic stress.
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D0WGK0
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ILVC_SLAES
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Ketol-acid reductoisomerase (NADP(+)) (KARI) (EC 1.1.1.86) (Acetohydroxy-acid isomeroreductase) (AHIR) (Alpha-keto-beta-hydroxylacyl reductoisomerase) (Ketol-acid reductoisomerase type 1) (Ketol-acid reductoisomerase type I)
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MSVKTKEKEMAVTILYEQDVDPKVIQGLKVGIIGYGSQGHAHALNLMDSGVDVRVGLREGSSSWKTAEEAGLKVTDMDTAAEEADVIMVLVPDEIQPKVYQEHIAAHLKAGNTLAFAHGFNIHYGYIVPPEDVNVIMCAPKGPGHIVRRQFTEGSGVPDLACVQQDATGNAWDIVLSYCWGVGGARSGIIKATFAEETEEDLFGEQAVLCGGLVELVKAGFETLTEAGYPPELAYFECYHEMKMIVDLMYESGIHFMNYSISNTAEYGEYYAGPKVINEQSREAMKEILKRIQDGSFAQEFVDDCNNGHKRLLEQREAINTHPIETTGAQIRSMFSWIKKED
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Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23776225}.
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D0Z5N4
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E2AKB_CAEEL
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Eukaryotic translation initiation factor 2-alpha kinase gcn-2 (EC 2.7.11.1) (General control nonderepressible kinase 2)
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MTKENQIVLDERVKENQHLQEEEKLALDAVYLNQITYIKAHWHVWVPTNCHILLKALDSCFLNGDPLGKSKLSVILHVKCSEDYPQRKPAVDLLDPQGLSKEDVQNLLTILRQMADTWEGCVVIAELAHRVREFLTDHTPRPAGSFHDDMLANKVRTEAEKQRKRLDTEQKELELLEEEMRQRNAIEMEKTLNGTRQENETRIIGGRRIVVLSNMPNTQLLISEWTFRFSSNRNPAEGKRKDFAPFLQKLDAVYNEIQKLCEIKGLDQNLVEYAFVHLQKISVSPDQILIQLNVAQKIFSSEENMQDTYELIVQKSNLLRLLAAQAICGLRYLHEASMTHKHLTLGSVWTRNSTGDCVFRFSDFGSMGPLLDLVKMFGDICSGKYVARDEDKEKEYDRRRKDLFQLGTLLDGLILATRGSTYSRVPTPVEGNQNTGTNLLGNFIAKCQEAKNIDQLVEDPFLKEECQSESENIFTPFGGAMSPDGRMLADNVIIRVLGRGGFGDVVLVRNKMDSTDYAIKRIPLNAKSDKLNRKIAKEAKFFAKLNHPNMVRYYYAWAEDLIPIVEETSDDDSSLGAVPIPGKEKIGKKGKLKTGKSLEDKENKANLGGGDSLMPMNLRGLVKDHSIGVDAKEWSTPFGKPEGPKCASRMRQSKRSTPSGGLKHLSECSSDDEDDDDSSEIDWDAESEEVEDEESDDSDEEDEDDGERLVQLNTETSTGADSVFERSTADEDVVFTAESEDLNAKRRESIELMEINTTTTSKSKLAIDVVPVRKPRILCIQMEYCDRATLRQYIDENHCFNAPTEVWRIFSEVLCGLKYMHDMAMIHRDIKPLNIFLTSQNGVKIGDFGLATLEAMSSKGKIVGGAAEKSTSIEAMLSPNGVKSKGSDVHQTRDIGTQLYMAPELFVDELVHKAPYTSKIDIYSAGVVLFEMFYRPLPPSMDRVSTLNNLRDDIKIPSDFGAGLAAPMAGLARRTVEKMLQRNPDERPTADDLLNDEDLPMHTKEDATFRNLCEKVIKKRDGRMNAWLLDKQFKEEVPTSLNYCYDVDICLERAKYNNREVLVETLRAEFCKILKIHSFEKLHTHTLMPVSTALAAASVRTKPVEVLDRSGVPVALPMDLRQNFVRFCVRNSVQRMKRFNFGRVYSQTSANGHPHERWECCVDCIGPQCSSPSLEAELLLVACEMMIGSLPGMKFTLKIGHAQLIEAQIRHLKLSDDVRAELLDALHLISVSDRPHSHKEKMDMLTPKIGAKAANIITKLLIPVEDNFGAFKEKVACFRKKLKVDAARVLVDKAIRDLEEIVGTFKFCRTEAIEQISIVYDSQTCYRPRTFGDGLLFQIQVEKPSTIANNKRGRRQNVLAGGRYDSALLRERHPRDFVYEIPLCISGFGVAMDVVSQIRDSINKSANIPKTPQNHCKVLICSMVQPDGSNLITQKFELAKKLWSMGIEADVFHIPVDDLESLTEHRNRASITHILAVYNTLNEVICKTETSSETMDVDSAISSVWRGVQALDGQSIHMTPCGGGPISSISTPGEAHHHDDHHPGTPVIASKCFRSSVSTTVATTSIRPISATVANLNVILVTSADRFHKVMKEKKRVESQVRNHLTEFVAHFTSKTRIEVLVCDIPADVIKKIVSELTKTSSEAEIDKLFDQLIQKHGKVDLSPLRRQFHITLNGISTGSAQVAILFYRQSDNFYRYLV
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Serine/threonine-protein kinase which phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (eIF2alpha), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis (By similarity). Involved in the unfolded protein response (UPR) triggered by several stresses including mitochondrial, osmotic and oxidative stresses, amino acid deprivation and UV irradiation, probably by phosphorylating and inhibiting eIF2alpha. In addition, leads to the selective translation/transcription of some mRNA including atf-5, pha-4 and gpdh-1 which are part of the UPR. Required for maintaining lifespan during amino acid starvation. Involved in hypoxia-mediated adaptive protective response.
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D0ZKX9
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RSEP_SALT1
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Regulator of sigma-E protease RseP (EC 3.4.24.-) (S2P endopeptidase) (Site-2 protease RseP) (S2P protease RseP) (Site-2-type intramembrane protease)
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MLSILWNLAAFIIALGVLITVHEFGHFWVARRCGVRVERFSIGFGKALWRRTDRYGTEYVIALIPLGGYVKMLDERAEPVAPELRRHAFNNKTVGQRAAIIAAGPVANFIFAIFAYWLVFIIGVPGVRPVIGEITPNSIAAQAQIAPGTELKAVDGIETPDWDAVRLQLVSKIGDQQTTVSVAPFGSDQRQDKTLDLRHWAFEPDKQDPVSSLGIRPRGPQIEPVLSEVQANSAASKAGLQAGDRIVKVDGQPLTQWMKFVTFVRDNPGKPLALEIERQGSALSLTLTPDTKSVNGKAEGFAGVVPKIIPLPEEYKTIRQYGPFSAILEATDKTWQLMKLTVSMLGKLITGDVKLNNLSGPISIAQGAGMSAEFGVIYYLMFLALISVNLGIINLFPLPVLDGGHLLFLAIEKLKGGPVSERVQDFSYRIGSILLVLLMGLALFNDFSRL
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A site-2 regulated intramembrane protease that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA.
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D0ZPH9
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SSPH2_SALT1
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E3 ubiquitin-protein ligase SspH2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SspH2) (Salmonella secreted protein H2) (Secreted effector protein sspH2)
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MPFHIGSGCLPATISNRRIYRIAWSDTPPEMSSWEKMKEFFCSTHQTEALECIWTICHPPAGTTREDVINRFELLRTLAYAGWEESIHSGQHGENYFCILDEDSQEILSVTLDDAGNYTVNCQGYSETHRLTLDTAQGEEGTGHAEGASGTFRTSFLPATTAPQTPAEYDAVWSAWRRAAPAEESRGRAAVVQKMRACLNNGNAVLNVGESGLTTLPDCLPAHITTLVIPDNNLTSLPALPPELRTLEVSGNQLTSLPVLPPGLLELSIFSNPLTHLPALPSGLCKLWIFGNQLTSLPVLPPGLQELSVSDNQLASLPALPSELCKLWAYNNQLTSLPMLPSGLQELSVSDNQLASLPTLPSELYKLWAYNNRLTSLPALPSGLKELIVSGNRLTSLPVLPSELKELMVSGNRLTSLPMLPSGLLSLSVYRNQLTRLPESLIHLSSETTVNLEGNPLSERTLQALREITSAPGYSGPIIRFDMAGASAPRETRALHLAAADWLVPAREGEPAPADRWHMFGQEDNADAFSLFLDRLSETENFIKDAGFKAQISSWLAQLAEDEALRANTFAMATEATSSCEDRVTFFLHQMKNVQLVHNAEKGQYDNDLAALVATGREMFRLGKLEQIAREKVRTLALVDEIEVWLAYQNKLKKSLGLTSVTSEMRFFDVSGVTVTDLQDAELQVKAAEKSEFREWILQWGPLHRVLERKAPERVNALREKQISDYEETYRMLSDTELRPSGLVGNTDAERTIGARAMESAKKTFLDGLRPLVEEMLGSYLNVQWRRN
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Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Contributes to virulence in calves.
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D0ZV89
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PHOQ_SALT1
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Virulence sensor histidine kinase PhoQ (EC 2.7.13.3) (EC 3.1.3.-) (Sensor histidine protein kinase/phosphatase PhoQ)
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MNKFARHFLPLSLRVRFLLATAGVVLVLSLAYGIVALVGYSVSFDKTTFRLLRGESNLFYTLAKWENNKISVELPENLDMQSPTMTLIYDETGKLLWTQRNIPWLIKSIQPEWLKTNGFHEIETNVDATSTLLSEDHSAQEKLKEVREDDDDAEMTHSVAVNIYPATARMPQLTIVVVDTIPIELKRSYMVWSWFVYVLAANLLLVIPLLWIAAWWSLRPIEALAREVRELEDHHREMLNPETTRELTSLVRNLNQLLKSERERYNKYRTTLTDLTHSLKTPLAVLQSTLRSLRNEKMSVSKAEPVMLEQISRISQQIGYYLHRASMRGSGVLLSRELHPVAPLLDNLISALNKVYQRKGVNISMDISPEISFVGEQNDFVEVMGNVLDNACKYCLEFVEISARQTDDHLHIFVEDDGPGIPHSKRSLVFDRGQRADTLRPGQGVGLAVAREITEQYAGQIIASDSLLGGARMEVVFGRQHPTQKEE
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Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG. Essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional and post-transcriptional levels respectively. Promotes expression of the two-component regulatory system PmrA/PmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Negatively regulates prgH, which is required for invasion of epithelial cells. Involved in acid tolerance.
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D0ZVG2
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SSPH1_SALT1
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E3 ubiquitin-protein ligase SspH1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SspH1) (Salmonella secreted protein H1) (Secreted effector protein SspH1)
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MFNIRNTQPSVSMQAIAGAAAPEASPEEIVWEKIQVFFPQENYEEAQQCLAELCHPARGMLPDHISSQFARLKALTFPAWEENIQCNRDGINQFCILDAGSKEILSITLDDAGNYTVNCQGYSEAHDFIMDTEPGEECTEFAEGASGTSLRPATTVSQKAAEYDAVWSKWERDAPAGESPGRAAVVQEMRDCLNNGNPVLNVGASGLTTLPDRLPPHITTLVIPDNNLTSLPELPEGLRELEVSGNLQLTSLPSLPQGLQKLWAYNNWLASLPTLPPGLGDLAVSNNQLTSLPEMPPALRELRVSGNNLTSLPALPSGLQKLWAYNNRLTSLPEMSPGLQELDVSHNQLTRLPQSLTGLSSAARVYLDGNPLSVRTLQALRDIIGHSGIRIHFDMAGPSVPREARALHLAVADWLTSAREGEAAQADRWQAFGLEDNAAAFSLVLDRLRETENFKKDAGFKAQISSWLTQLAEDAALRAKTFAMATEATSTCEDRVTHALHQMNNVQLVHNAEKGEYDNNLQGLVSTGREMFRLATLEQIAREKAGTLALVDDVEVYLAFQNKLKESLELTSVTSEMRFFDVSGVTVSDLQAAELQVKTAENSGFSKWILQWGPLHSVLERKVPERFNALREKQISDYEDTYRKLYDEVLKSSGLVDDTDAERTIGVSAMDSAKKEFLDGLRALVDEVLGSYLTARWRLN
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Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin-protein ligase that interferes with the host's ubiquitination pathway and targets host proteins for proteasomal degradation. Can ubiquitinate ubiquitin, giving rise to polyubiquitin chains (in vitro). Polyubiquitinates host PKN1, leading to its proteasomal degradation. Down-modulates production of host pro-inflammatory cytokines by inhibiting NF-kappa-B-dependent gene expression this depends only partially on its E3 ubiquitin-protein ligase activity.
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D1A4G7
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ECCC_THECD
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ESX secretion system protein EccC (Type VII secretion system protein EccC) (T7SS protein EccC)
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MSTVLVRRKERRQPPQMPRGEILLESPPELPEVVTNSFQNVLMYLPMAAGSAAMVFTFLNHRNTLQLVAGGMFALSMFGMMFGQLSQQSGERKTKLNSARRDYLRYLGQVRQRVRKAAKQQREALEWNNPAPGRLWSMVMSPRLWERRSSDADFAQVRIGAGPQRLAVQLIPPETKPVEDLEPMSAGALRRFLRAHSTVPDLPVAISLRSFARILPDGDPKAVYGMVRALIMQLAAFHSPDDVRITVCASRERMPQWQWMKWLPHSLHPTEYDAAGQVRLLTHSLVELESMLGPEIKDRGMFGASRAPAEPFHLVIVDGGQASYDSQIASDGIDGVCVIDLTGSVAETNEATMLRLRVTPERVYVVKRDRAGKEVLSSVGRPDQASIAEAEALARQLAPFRTSAADEPEEDVLSANMTLTSLLHIDNPYNLDPAVLWRPRPQRNRLRVPIGLDADGRPLELDIKESAQGGMGPHGLCIGATGSGKSELLRTLVLALAMTHSPEVLNFVLVDFKGGATFLGMEGLRHVSAIITNLEEELPLVDRMYDALHGEMVRRQEHLRHSGNYASLRDYEKARMEGAPLPPMPTLFIVLDEFSELLSAKPDFAELFVMIGRLGRSLGVHLLLASQRLEEGKLRGLDTHLSYRIGLRTFSAMESRVVLGVPDAYELPPSPGNGYLKFATEPLVRFKAAYVSGPVDEEPQTRSEGPQIVRQVLPYLTDYIRPQVVEQPQPEQRAEENKSSESLFDVVVRQLAGHGPEPHQIWLPPLDVPPTLDELLPPLSPSAAHGYTADGWEWRGRLHAVVGLVDRPFDQRRDPYWLDLSGGAGHVGVAGGPQTGKSTMLRTLITSLALLHTPQEVQFYCLDFGGGTLAGLAELPHVGSVATRLDADRIRRTVAEVSALLEQREQEFTERGIDSMATYRRLRATGEYAGDGFGDVFLVVDNWLTLRQDYEALEDSITQLAARGLGYGIHVVLSSNKWSEFRTSIRDLLGTKLELRLGDPYESEVDRKKAANVPENRPGRGLTRDGYHFLTALPRIDGDTSAETLTEGIATTVKTIREAWHGPTAPPVRMLPNVLPAAQLPSAAESGTRIPIGIDEDSLSPVYLDFNTDPHFLVFGDTECGKSNLLRLITAGIIERYTPQQARLIFIDYSRSLLDVATTEHQIGYAASSTAASSLVRDIKGAMEARLPPPDLTPEQLRSRSWWTGAELFLVVDDYEMVATSDNPLRPLAELLPQARDIGLHLIIARSMGGAGRALYEPIIQRIKEMASPGLVMSGNKDEGILLGNVKPHKLPQGRGYFVERRSGTRLIQTAYRES
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Part of the ESX specialized secretion system, which exports proteins from the cell including EsxA (ESAT-6) and EsxB (CFP-10). Has weak intrinsic ATPase activity probably only the first FtsK domain can hydrolyze ATP. Might be the translocase subunit.
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D1A7C3
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FGE_THECD
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Formylglycine-generating enzyme (FGE) (EC 1.8.3.7)
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MPSFDFDIPRRSPQEIAKGMVAIPGGTFRMGGEDPDAFPEDGEGPVRTVRLSPFLIDRYAVSNRQFAAFVKATGYVTDAERYGWSFVFHAHVAPGTPVMDAVVPEAPWWVAVPGAYWKAPEGPGSSITDRPNHPVVHVSWNDAVAYATWAGKRLPTEAEWEMAARGGLDQARYPWGNELTPRGRHRCNIWQGTFPVHDTGEDGYTGTAPVNAFAPNGYGLYNVAGNVWEWCADWWSADWHATESPATRIDPRGPETGTARVTKGGSFLCHESYCNRYRVAARTCNTPDSSAAHTGFRCAADPL
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Oxidase that catalyzes the conversion of cysteine to 3-oxoalanine on target proteins. 3-oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile.
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D1D8L6
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CDNTP_ASPFM
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Cyclic dipeptide prenyltransferase (CdpNPT) (EC 2.5.1.-) (Tryptophan aminopeptidase CdpNPT) (EC 3.4.11.17)
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MDGEMTASPPDISACDTSAVDEQTGQSGQSQAPIPKDIAYHTLTKALLFPDIDQYQHWHHVAPMLAKMLVDGKYSIHQQYEYLCLFAQLVAPVLGPYPSPGRDVYRCTLGGNMTVELSQNFQRSGSTTRIAFEPVRYQASVGHDRFNRTSVNAFFSQLQLLVKSVNIELHHLLSEHLTLTAKDERNLNEEQLTKYLTNFQVKTQYVVALDLRKTGIVAKEYFFPGIKCAATGQTGSNACFGAIRAVDKDGHLDSLCQLIEAHFQQSKIDDAFLCCDLVDPAHTRFKVYIADPLVTLARAEEHWTLGGRLTDEDAAVGLEIIRGLWSELGIIQGPLEPSAMMEKGLLPIMLNYEMKAGQRLPKPKLYMPLTGIPETKIARIMTAFFQRHDMPEQAEVFMENLQAYYEGKNLEEATRYQAWLSFAYTKEKGPYLSIYYFWPE
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Prenyltransferase that catalyzes reverse prenylation at position N-1 of tryptophan-containing cyclic dipeptides. Accepts only dimethylallyl diphosphate (DMAPP) as the prenyl donor but shows broad substrate specificities toward its aromatic substrates. Shows also tryptophan aminopeptidase activity with preference for linear peptides containing a tryptophanyl moiety at the N-terminus.
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D1FVF0
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BSLS_BEABA
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Bassianolide nonribosomal cyclodepsipeptide synthetase (BSLS) [Includes: Nonribosomal peptide synthetase (EC 6.1.2.-); S-adenosyl-L-methionine-dependent N-methyltransferase (EC 2.1.1.-)]
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MEPPNNANTGQLGPTLPNGTVDLPTDLSREITRHFGLEQDEIEEILPCTPFQRDVIECASDDKRRAVGHVVYEIPEDVDTERLAAAWKATVRYTPALRTCIFTSETGNAFQVVLRDYFIFARMYCPSAHLKSAIVKDEATAAVAGPRCNRYVLTGEPNSKRRVLVWTFSHSFVDSAFQGRILQQVLAAYKDGHGRVFSLQPTTDLTESENGDHLSTPASERTVVIERATQFWQEKLHGLDASVFPHLPSHKRVPAIDARADHYLPCPPFIQHEWSSTTVCRTALAILLARYTHSSEALFGVVTEQSHEEHPLLLDGPTSTVVPFRVLCALNQSVSKVMEAITTYDHDMRQFAHAGLCNISRIGDDASAACGFQTVLMVTDSRTAGDDEIHQVLEESEKFIPCTDRALLLSCQMTDEGVLLVARYDQSILEPLQMARFLRQLGFLINKLQSTDGSPCVGQLDVLAPEDRTEIEGWNSEPLQTQDCLIHSEVVRNAGDTPNKPAVCAWDGEWTYSELNNVSSRLASYISSLDLGQQLIVPIYLEKSKWVMAAILAVLKAGHAFTLIDPNDPPARTAQIIKQASASIALTSALHQSKMQAVVGRCITVDDDLVQTLTTFEGSQVASAAKPGDLAYVIFTSGSTGDPKGIMIEHRAFYSSVVKFGKALGIRSSTRALQFATHGFGAFLLEVLTTLIHGGCICVPSDHDRMHNIPGFIRQNQINWMMATPSYMTTMKPEDVPGLETLVLVGEQMSSSINDVWLSELQLLDGYGQSESSSICFVGKIDDSSRDPNNLGWAIGAHSWIINPDNPDQLVPIGAIGELLIESPGIARGYLFSQSTETPFLERAPAWYASKQPPYGVKFYRTGDLARYAPDGTVICLGRMDSQVKIRGQRVELDAIENLLRRQFPSDVTVVAEAVKRSDLPSSVVITGFLISSEYVVGAPSTEDTYILDQVVTQEINAKMRQILPAHSIPSFYICMKSLPRTATGKVDRRKLRSIGSSLLALQAQSTAPRSSQAPDASAGVTKLEEVWMDIFNLTPNSHNIGGNFFALGGDSITAIKMVNMARAAGIQLKVSDIFQNPTLASLQAAIGGSSMTVTSIPALALDGPVEQSYSQGRLWFLDQLEIGANWYTIPYAVRLRGPLDVDALNRALLALEKRHETLRTTFEDQDGVGVQIIHETLLDQLRIINADHADYVQLLKQEQTAPFNLASESGWRVSLIRLDDDDNILSIVMHHIISDGWSIDVLRRELGQLYAAALHGADLFGSALSPLPIQYRDFSVWQKQDAQVAEHERQLQYWQKQLADCSPAKLPTDFHRPALLSGKATTVPVTITSELYYRLQEFCSTFNTTSFVVLLATFRAAHYRLTGVDDAVIGTPIANRNRHELENLIGFFVNTQCMRITINEDEDTFESLVRQVRSTTTAAFEHEDVPFERVVSAMLPGSRDLSQNPLAQLVFAIHSHKDLGKFELEALESEPLQNEVYTRFDAEFHFFQAPDGLTGYINFATELFKVETIQNVVSVFLQILRHGLEHPQTLISVVPLTDGLAELRSMGLLEIKKVEYPRDSSVVDVFRTQVASYPDTLAVVDSSSRLTYAELDHQSDLLATWLRQQNLPTEALVVVLAPRSCETIITFLGILKANLAYLPLDIRSPITRMRDVLSTLPGRTIALLCSDEVAPDFQLPSIELVRIADALEEAAGMTSLNGHEHVPVPSPSPTSLAYVLYTSGSTGRPKGVMIEHRAIVRLARSDIIPDYRPACGDTMAHMFNTAFDGATYEIYTMLLNGGTLVCVDYMDTLSPKSLEAVFKKEQVNATIMAPALLKLYLADARDALKGLDVLISGGDRFDPQDAVDAQSLVRGSCYNGYGPTENGVFSTVYKVDKNDPFVNGVPLGRAVNNSGAYVVDRNQQLVGPGIIGELVVTGDGLARGYTERAFDQNRFTQLKVEGQSVRGYRTGDRVRYRVGEGLIEFFGRMDFQFKIRSNRIEAGEVEAAILSHPAVRNAAVILRVEEKLEPEIVGFVVAEHDDTAEQEEAGDQVEGWQAFFESTTYTELDTVSSSEIGKDFKGWTSMYDGNEIDKAEMQEWLDDTIHTLTDGQALGHVLEIGTGSGMVLFNLGSGLQSFVGLEPSKSAAAFVNNAIKSTPALAGKAQVFVGTATDTNKLDDLHPDLVIFNSVLQYFPTRDYLERVVDALVHLRSAKRIFFGDVRSYATNRHFLAARAIYTLGNHTTKDEVRKKMAEMEEREEEFLVEPAFFTTLVNRLPDVRHVEIIPKNMQATNELSAYRYAAVVHLRGSDELTRPVHPIKMDDWVDFQASHMHKDALREYLRLAENTKTVAISNIPYGKTIFERQVVESLDETSEDAPHASLDGAAWISAVRSDAKARSSLSVPDLVLLAKETGFRVEVSAARQWSQSGALDAVFHRYPAEPGVRTLFQFPTDNDVRMSAPLTNQPLQRLQKRRVAVQVREWLQDRIPSYMIPSHIVALDQMPLNTSGKVDRKELSRQAKAIKKVQKSAPPTAPAFPLSEVEVMLCEELTKTFEMDVNITDDFFQLGGHSLLATRLVARISHRLGARLTVKDVFDYPVFSELADIIRQQLASKNTLLPTASAGGGGQDKKESAGVAPTTDMEAMLCEEFANILGMDVGITDNFFDLGGHSLMATRLAARIGHRLNTTISVKDIFSHPVIFQLSAKLEVSQLESSSGGTDIKMPDYTAFQLIPAADAEKFMQDHIYPQINFSQDMVQDVYLATHLQQCFLRDVFGRPKPLVPFYVEFPPDSNPHTLATACTSLVDKYDIFRTIFVEAEGNLYQVVLKHLNLDIDVVETDANVHKTSSDLVDAIAKEPVRLGQPMIQVKVLKQTSSVRVLLWLSHALYDGLSWEHIVRDLHILSKERSLPPATQFSRYMQYVDHTRGPGCDFWRDVLQNAPITNLSDAGSGGRPTKAGDPRVWHAGKVISGPSQAIRSSITQATVFNAACAIVLSKETGTDNVVFGRIVSGRQGLPVRWQNIIGPCTNAVPVRAVVDAHGNHQQMLRDLQEQYLLSLPYETIGFDEIKRSCTDWPDSARNYGCCVTYQNFEYHPESEVDQQRVEMGILAKKAELIKEEPLYNVAIAGEVEPDGVHLQVTVVVDSQLFSQEGATHLMEQVCNTFQALNASL
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Bassianolide nonribosomal synthetase that mediates the biosynthesis of bassianolide (BSL), a non-ribosomal cyclodepsipeptide that shows insecticidal and cancer cell antiproliferative activity. BSLS first catalyzes the iterative synthesis of an enzyme-bound dipeptidol monomer intermediate from D-2-hydroxyisovalerate and L-leucine before performing the condensation and cyclization of 4 dipeptidol monomers to yield the cyclic tetrameric ester bassianolide. The N-methyltransferase MT domain is responsible for the methylation of the leucine residues of bassianolide. BSLS is flexible with both the amino acid and hydroxyl acid precursors, and produces bassianolide as the major product (containing N-methyl-L-Leu), together with small amounts of beauvericin and its analogs beauvericins A-C (containing N-methyl-L-Phe).
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D1KF50
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SRS2L_ARATH
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ATP-dependent DNA helicase SRS2-like protein At4g25120 (EC 5.6.2.4) (AtSRS2) (DNA 3'-5' helicase At4g25120)
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MENLPPNRGMWNQEYSHGRISQSFRSAKPLLDRKRPIENAPNSSNPLPQRMKESMDTESVSHNINFNSTPLMELSANTPYKRLKPEIESYADGHPCGLRTPPPRFDLDKEIINGFQTDIYADVGSLSEAFVTPLKEPERVTLSNGCSTSSILDDDFDDSILEEIDLICEQSARKAACQTPTTSIYQTPSKDNKSSDPKASLDFRDVEKFEPDSNVKLKLDEETPTIAADPALLNSMPDECSKYMLSLNDRQRDAACSNISTPLMVIAGPGSGKTSTMVGRVLVLLNEGLLPSNILAMTFTKAATSEMRERIGKSAGKKAAKDITISTFHSFSLQLCRMHADKLQRTSEFSVYGHGQQRRAIIEAVRLYEEEKKNGSKTSVPCESGEGLNGAGAGAVCPEYAKDLSKKWQKFVTQGKASGKSPEQCRKMGNEIGAKILGNYNDILKACDALDYHDLISCSVTLLSDFPEVFKECQDTWKAIIVDEFQDTSTMQYKLLRMLGSHNHITIVGDDDQSIFGFNGADSSGFDSFRRDFPNYKEVRLIKNYRSSRHIVEAASSIIKNNTKRCQSKSISSENSQGSKITVKECHNEEAQCAYVIDKIIEITNDGSTPCCSHGDIAILYRRQVSGKVFQNAFRQRKIPFNVHGVAFYRKKVVQVILAMLKTTFSECDDASYRRVFKALLPFEKEEKKRIIEHIEKISTSRKCSFISAASDIFNAKISGTFKRSQLTQGRKVLQTLDMVAKLVDREQSLSAVVTCVANMIPQKYLLEQRAVVDNDGGKLLNEDNDLRSVLQYLMDDVAEFISTHCTTTEEEDAIKEKKGCNQLHSFINYISERETENFRSRRRDNENSVTLTTIHQSKGLEWDIVFIVKANENEIPLLHESNGNASESGTSLEEERRLLYVAMTRARKKLFFLYVTVDSNWQVLQPSRFLKEIPGHLLQGDMSVNDCRKVHENLPNKTEQSVSSFGTDIKHEESKLTDNDVMNIPEDYASEESIAAYALNGNNFLKRFDVEVRSVVSHLFHNWAKKQAFQEPKRLIDKVRFVIGERLAIKKNKHKDVLRALKSSLTSEEAFQYAEHVLRWEQLPADTRAHIVREKQEHFQKLRIENSMGTSEATSKQIAFLHSLGCTVVPTSRLHASRLIEQYKSL
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ATP-dependent 3'- to 5'-DNA helicase that could disrupt recombinogenic DNA intermediates and facilitate single strand annealing. Unwinds nicked and partial Holliday junctions in vitro. Anneals two single strands into a dsDNA molecule in vitro.
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D1LYT2
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GBRB2_MACMU
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Gamma-aminobutyric acid receptor subunit beta-2 (GABA(A) receptor subunit beta-2)
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MWRVRKRGYFGIWSFPLIIAAVCAQSVNDPSNMSLVKETVDRLLKGYDIRLRPDFGGPPVAVGMNIDIASIDMVSEVNMDYTLTMYFQQAWRDKRLSYNVIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGDDNAVTGVTKIELPQFSIVDYKLITKKVVFSTGSYPRLSLSFKLKRNIGYFILQTYMPSILITILSWVSFWINYDASAARVALGITTVLTMTTINTHLRETLPKIPYVKAIDMYLMGCFVFVFMALLEYALVNYIFFGRGPQRQKKAAEKAASANNEKMRLDVNKIFYKDIKQNGTQYRSLWDPTGNLSPTRRTTNYDFSLYTMDPHENILLSTLEIKNEMATSEAVMGLGDPRSTMLAYDASSIQYRKAGLPRHSFGRNALERHVAQKKSRLRRRASQLKITIPDLTDVNAIDRWSRIFFPVVFSFFNIVYWLYYVN
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Ligand-gated chloride channel which is a component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the brain (By similarity). Plays an important role in the formation of functional inhibitory GABAergic synapses in addition to mediating synaptic inhibition as a GABA-gated ion channel (By similarity). The gamma2 subunit is necessary but not sufficient for a rapid formation of active synaptic contacts and the synaptogenic effect of this subunit is influenced by the type of alpha and beta subunits present in the receptor pentamer (By similarity). The alpha1/beta2/gamma2 receptor and the alpha2/beta2/gamma2 receptor exhibit synaptogenic activity (By similarity). Functions also as histamine receptor and mediates cellular responses to histamine (By similarity).
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D1MEI7
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MASTA_EUMPO
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Venom peptide 2a (EpVP2a) (VP2a) (Eumenine mastoparan VP2a)
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MRGTSFILFAVVVILGFLNANAEPLANPAPLANPDPLANPDPLANPEAFDLLGLVKKVASALG
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Antimicrobial peptide. Shows activities against Gram-positive bacteria (S.aureus MIC=50 uM and 200 ug/ml, and B.subtilis MIC=200 ug/ml), Gram-negative bacterium E.coli (MIC=100 uM and 200 ug/ml) and fungi (B.cinerea MIC=5 uM, S.cerevisiae MIC=128 ug/ml, S.pombe MIC=128 ug/ml, A.nidulans MIC=128 ug/ml, and C.albicans MIC=64-100 uM). Shows cytolytic activity against insect cell lines. Its hemolytic activity is controversial, as Baek and colleagues report no activity while Bea and colleagues note an hemolytic activity. In vivo, peptide injection in the vicinity of the head and thorax of lepidopteran larvae induces feeding disorder followed by death due to starvation. Is weakly lethal when tested on water flies (D.magna), but is not lethal on lady beetles (H.convergens).
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D1ZA70
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ARO1_SORMK
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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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MAESSSNPTRINILGKDNIIIDHGIWLNFVAQDLLQNIKSSTYILITDTNLYATYVPSFQSVFEKAAPQDVRLLTYAIPPGEYSKGRDTKAEIEDWMLSHQCTRDTVIIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDVPMGKNLIGAFWQPERIYIDLTFLNTLPVREFINGMAEVIKTAAIWDESEFTTLEENAKAILEAVRSKNKSADRLAPIRDILKRIVLGSARVKAEVVSSDEREGGLRNLLNFGHSIGHAYEAILTPQVLHGEAVAIGMVKEAELARFLGVLKPSAVARLTKCIASYDLPTSLQDKRIVKLTAGKECPVDVLLQKMAVDKKNEGRKKKIVLLSAIGKTYEPKASVVEDRAIRIVLTPCIRVHAGVPKDLKVSVTPPGSKSISNRALTLAALGEGTTRIYNLLHSDDTQVMLNAVAQLQGASFSWEDSDVLVVKGNGGRLQATSTPLYLGNAGTASRFLTSVVALCNPTDVNSTVLTGNARMKQRPIGALVDALRANGVGVKYLEKEHSLPVQVDAAGGLAGGVMELAATISSQYVSSLLMAAPYAREPVTLRLVGGKPISQPYIDMTIAMMASFGVQVQRSAEDPNTYHIPQGTYKNPETYIVESDASSATYPLAVAAITGTTCTVPNIGSKSLQGDARFAIEVLRPMGCTVEQTDASTTVTGPPVGTLKAIPHVDMEPMTDAFLTASVLAAVASGTTQITGIANQRVKECNRIKAMKDELAKFGVTCNELEDGIEVTGIPYTELKNPTEGIYCYDDHRVAMSFGVLSTISPHPVLILERECTGKTWPGWWDTMSNYFKSHLEGEEEPHSSHVSHEKPRKGNPKSIFIIGMRGAGKSTAGKWMSEVLNRPLIDLDHELERREGQTIPEIIRSERGWEGFRKAELDLLEDVIKNNPTGHIFSCGGGIVESEAARKLLISYSQNGGIVLLVHRDTDQVVEYLMRDKTRPAYSENIREVYYRRKPWFEECSNFRYYSPHPDGSKALTEPPFDFSQFLSVICGHSNHLEEAKKKPQSSFVSLTVPNVSKALDIIPKVVVGSDAVELRVDLLEDYDPEFVAKQVALLRSAARIPIVYTVRTVSQGGKFPDDDYALALKLYRTGLQAGVEYLDLEMTMPDEVIEAVTNEKGYTHIIASHHDPKATLSWKNGGWIQYYNKALQHGDVVKLVGVARELSDNFALARFKASLAAAHDKPFIGLNMGTAGKLSRVLNGFLTPVSHPALPSKAAPGQLSAAEIRQALALIGELEPRSFYLFGKPISASRSPALHNALFRDNGLPHQYSLFETDNAADVKELIRATDFGGASVTIPLKLDIMPLLDEVSDAAKVIGAVNTIIPVGSGDKVTLRGDNTDWMGMVYALRNAGVVKVSKESPAAGMVVGSGGTTRAAVYALHDLGFAPIYVVARNADRIKALAESFPADYDIRSLSTPEEVAAESTAQPSVVISTIPADKPIEQSMREVLVASLRHPSVTNGKHVLLEMAYTPRHTPLMQLAEDAHWQTIPGLEVLAAQGWYQFQLWTGITPIYTDAQAAVMGN
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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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D2CLZ9
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ATOH8_DANRE
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Transcription factor atoh8 (Atonal bHLH transcription factor 8) (Protein atonal homolog 8)
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MKNPHLNSPCKILNTVSGDKKMKRKAREPIKHVSEDHYPYFKLYKNPHLMAETLGDGSPQETHRSEIITSRDDSVRNDVLNTAVDMRINTITAAEVPDSKLRSVSEKTVNSKIVQASPQVSVLSAPQVFPLERVVLSQRAASQAPAGGSERAESPRKRAGEPSGVVTEIKAIQQTRRLLANARERTRVHTISAAFEALRKQVPCYSYGQKLSKLAILRIACNYILSLAQLADLDYTPDHRNMSFRECVEQCTRTLQAEGRSKKRKE
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Transcription factor that binds a palindromic (canonical) core consensus DNA sequence 5'-CANNTG- 3' known as an E-box element, possibly as a heterodimer with other bHLH proteins (By similarity). During development, is required for heart looping and swim bladder formation by acting in concert with GATA4 and ZFPM1. During the development of both the retina and skeletal muscles is required for neural retinal cell through modulating PAX6 and NEUROG3 expression and myogenic differentiation.
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D2CSU4
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CM1_PETHY
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Chorismate mutase 1, chloroplastic (PhCM1) (EC 5.4.99.5)
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METQLLRFPSHTITSSITTNSSRNTTPFLPHKKWSHFVKFQLVNSSSSIKHGIRPLQASATSLGLGNKNRVDETESYTLDGIRHSLIRQEDSIIFSLVERAQYCYNAETYDPDVFAMDGFHGSLVEYIVRETEKLHATVGRYKSPDEHPFFPKVLPEPVLPPMQYPKVLHPIADSININVKIWEMYFENLLPRLVKEGDDGNYGSTAVCDTICVQALSKRIHYGKFVAEAKYRASPEVYNAAIRAQDRNGLMDLLTYPAVEEAIKRRVEIKTRTYGQELHINGPENGGDPVYKIKPSLVAELYGDWIMPLTKEVQVQYLLRRLD
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Component of the floral volatile benzenoid/phenylpropanoid (FVBPs) biosynthetic pathway. Mediates the conversion of chorismate to prephenate, thus coupling metabolites from the shikimate pathway to the synthesis of FVBPs in the corolla.
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D2CVN6
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TEB1_TETTS
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Telomeric repeat-binding subunit 1 (Telomerase-associated protein of 82 kDa) (p82)
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MKLTKGGSYILKKVDRKQFYQDEEIVMQIKKILGQKTTDCKQYIKCECIDGLGDEALIYFEMLANQNQHLQKNDVIMIQDYLNDKTQNDKIVVLVTRFQFCKASHVQPKTAQKESIQLLNTEKTIIQKSKITKNPAEEVLKFIEVNEKDNSSNSEDMIIEQQKQEIKNNQKEKQSINGFNLEDSYSNISDITNFGGKSNFNIGSLSDQLSKQTLLISQLQVGKNRFSFKFEGRVVYKSSTFQNQQDSKYFFITAQDANNQEINLSFWQKVDQSYQTLKVGQYYYFIGGEVKQFKNNLELKFKFGDYQIIPKETLSANYVQPLALQPSKQFGNDSIGDSDYSIHNLIEKEESIAQKGYNGQKNNKYRQNNNNSKHTLLISEVLKTSKQYLSVLAQVVDIQSSDKNIRLKICDNSCNQELKVVIFPDLCYEWRDKFSINKWYYFNEFVRQIYNDEVQLKNNIHSSIKESDDQRKVITYNQEQGVFKKSISINSNDSFEIKPKISYKNNSNQEQRIYSSIEEIIQQAQASEIGQKKEFYVYGNLVSIQMKNKLYYYRCTCQGKSVLKYHGDSFFCESCQQFINPQVHLMLRAFVQDSTGTIPVMIFDQQSSQLINQIDPSIHVQEAGQYVKNCIENGQEEIIRQLFSKLDFARFIFEIQFENKEFNNEQEIAYKVLKIEKENIKEESKYLLKKLEHLINNNQNN
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Single-stranded DNA (ssDNA)-binding protein that mediates the recruitment of telomerase to telomeric DNA. Telomerase is an essential ribonucleoprotein (RNP) enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER. Acts as part of a replication protein A (RPA)-related subcomplex of the holoenzyme telomerase ribonucleoprotein complex: TEB1 specifically recognizes and binds telomeric ssDNA, thereby mediating the recruitment of the holoenzyme telomerase RNP complex to telomeres. TEB1 is related to RPA1 subunit of the RPA complex but is specific to telomeric DNA, which is not the case of RPA1.
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D2EAC2
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ZBED6_MOUSE
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Zinc finger BED domain-containing protein 6 (Muscle growth regulator) (MGR)
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MSVCTLSVPVSSISPGRRCSTFGDAGILGCVSINSNTDEDDVVEGKMVAEGANKETKLPAKKKRKKGLRIKGKRRRKKLILAKKFSKDLGSGRPVADAPASLASGAPEQDEESLFEGNIEKQIYLPSTRAKTSIVWHFFHVDPQYTWRAICNLCEKSVSRGKPGSHLGTSTLQRHLQARHSPHWTRANKFGVTNGEEDFTLDLSLSPPSPGSNGSFEYIPTDSVDENRMGKKRDKSASDALRAKRGRFLIKSNIVKHALIPGTRAKTSAVWNFFYTDPQHISRAVCNICKRSVSRGRPGSHLGTSTLQRHLQATHPIHWAVANKDSGAIGNGLDETETESSDLLNDTMPGEKSSGSQDLTAEDLSDSDTDEPPCLEVENRSESPIPVADQDNPVHAQERETTTHCENAAANQISQAVIQMIVEDLHPYNYFSTPAFQRFLQIVAPDYRLPSETYFFTKAVPQLYDSVREKIFLTLENVQSQKIHLTADIWTHDPSTDYFIVTVHWVSLETASSPSNGGTPNFRKWAVLCVTGLAKDCLITNILQELNDQIGLWLSPNFLTPSFIVSDNSSNVVHAIKGGGFTHVPCFLHCLNIVIQDFFCEHKSIENMLVAARKTCHHFSHSVKARQILQEFQNDHQLPWKNLKQDETGHWISTFYMLKWLLEHCYSVHHSLGRASGVVLTSLQWTLMTYVCDILKPFEEATQRVSVKTTGLNQVLPLIHHLLFSLQRLREDFQVRGITQALNLVDSLSLKLESDALLSAMLKSKHCILATLLDPCFKNSLEDFFPQGADLETYKQILAEEVCNYMESSPGACQISSSETSGPLVRLGTDSFTSIKEGTSSAGSLDSSAAGSVAVGSKSSLLPAAVAVVDEYFKEKYSELSGGDDPLVYWQRKVSIWPALTQVAIQYLSCPMCSWQSECMFTTNSHFHPKQIMNMDFDNIEQLIFLKMNLENVNYDYSTLILSWDPENKAVQSNEKEILP
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Transcriptional repressor which binds to the consensus sequence 5'-GCTCGC-3', transcription regulation may be tissue-specific. Regulates the expression of target genes such as: IGF2, PGAP6/TMEM8, ENHO, and PIANP. Acts as a transcriptional repressor of growth factor IGF2, thereby negatively regulating postnatal growth of muscles and internal organs, especially in females. Negatively regulates myoblast differentiation and myoblast mitochondrial activity via its regulation of IGF2 transcription. Negatively regulates the cell cycle of myoblasts, potentially via transcriptional regulation of the E2F family of transcription factors such as: E2F1 and E2F2. Positively regulates the cell cycle and survival of pancreatic beta cells. Binds to the CDH2 gene and may directly repress CDH2 transcription. Probably by controlling CDH2 expression, regulates pancreatic beta cell adhesion, and formation of cell-to-cell junctions between pancreatic beta cells and neural crest stem cells. May also play a role in embryonic beta cell differentiation. May play a role in insulin sensitivity and glucose clearance.
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D2GXM8
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CBPC5_AILME
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Cytosolic carboxypeptidase-like protein 5 (EC 3.4.17.-) (EC 3.4.17.24) (ATP/GTP-binding protein-like 5) (Protein deglutamylase CCP5)
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MELRCGGLLFSSRFDSGNLAHVEKVDSVSGDGEGGAAGASAPFSSIASSPDYEFNVWTRPDCAETEFENGNRSWFYFSVRGGTPGKLIKINIMNMNKQSKLYSQGMAPFVRTLPTRPRWERIRDRPTFEMTETQFVLSFVHRFVEGRGATTFFAFCYPFSYSDCQDLLNQLDQRFLENHPTHSSPLDTIYYHREILCYSLDGLRVDLLTITSCHGLREDREPRLQQLFPDTGTPRPFCFTGKRIFFLSSRVHPGETPSSFVFNGFLDFILRPDDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDAALHPAIYGAKAVLLYHHVHSRLHPQSPSEHQHSPCLPPDAPLSDLEKANHLRNEAHLGHTSDGDSPEDWTQTRPAEQKASGVWLMPQQCADAEQPAPDTIPPKESGVAYYVDLHGHASKRGCFMYGNSFSDESTQVENMLYPKLISLNSAHFDFQGCNFSEKNMYARDRRDGQSKEGSGRVAIYKASGIIHSYTLECNYNTGRSVNSIPAACHDNGRASPPPPPAFPSRYTVELFEQVGRAMAIAALDMAECNPWPRIVLSEHSSLTNLRAWMLKHVRSSRGLSSTVSGAVNKKRGSRTPPRSNSGLPVSCSENPLSRARSFSTGTSAGGSSSSQQNSPQMKNSPSFPFHGSRPTGLPGLGSSTQKVSHRVLGPVREPRSQDRRRRQQPLTHRPTSSSLAPSPNPTSSSPASSHSTGPCLLPSAFSVSGSSCSLLSSGDKPEAVMVIGKGLLGPRIPCIRTRLQVRPRLGQGSPPTCRGMSGSSGPTSPIPRTRESSEPEPGPHSAPGLPQAGPPRPRSAPAFSPISCSLSDSQSRICYSGGPLGQPEVCFGPKSPPLTVSPRV
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Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Cleaves alpha- and gamma-linked polyglutamate tubulin side-chain, as well as the branching point glutamate. Also catalyzes the removal of alpha-linked glutamate residues from the carboxy-terminus of alpha-tubulin. Mediates deglutamylation of nucleotidyltransferase CGAS, leading to CGAS antiviral defense response activation.
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D2GZV9
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ENTP5_AILME
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Ectonucleoside triphosphate diphosphohydrolase 5 (NTPDase 5) (EC 3.6.1.6) (Guanosine-diphosphatase ENTPD5) (GDPase ENTPD5) (Uridine-diphosphatase ENTPD5) (UDPase ENTPD5)
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MATTWGAAFFMLVASCVCSTVFHRDQQTWFEGVFLSSMCPINVSASTLYGIMFDAGSTGTRIHIYTFVQKIPGQLPILEGEIFESVKPGLSAFVDQPKQGAETVEELLEVAKDSVPRSHWKRTPVVLKATAGLRLLPEQKAEALLFEVREIFRKSPFLVPDDSVSIMDGSYEGILAWVTVNFLTGQLHGHSQKTVGTLDLGGASTQITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETEGIDGHTFRSACLPRWLEAEWIFGGVKYQYGGNKEGNEGSGEVGFEPCYAEVLRVVQGKLHQPDEVRKSSFYAFSYYYDRAADTDMIDYETGGVLKVEDFERKAREVCDNLEKFTSGSPFLCMDLSYITALLKDGFGFADSTILQLSKKVNNIETGWALGATFHLLQSLGISH
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Hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP (By similarity). In the lumen of the endoplasmic reticulum, hydrolyzes UDP that acts as an end-product feedback inhibitor of the UDP-Glc:glycoprotein glucosyltransferases. UMP can be transported back by an UDP-sugar antiporter to the cytosol where it is consumed to regenerate UDP-glucose. Therefore, it positively regulates protein reglucosylation by clearing UDP from the ER lumen and by promoting the regeneration of UDP-glucose. Protein reglucosylation is essential to proper glycoprotein folding and quality control in the ER (By similarity).
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D2H526
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CDK12_AILME
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Cyclin-dependent kinase 12 (EC 2.7.11.22) (EC 2.7.11.23) (Cell division protein kinase 12)
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MPNPERHGGKKDGSGGASGTLQPSSGGGSSNSRERHRLVSKHKRHKSKHSKDMGLVTPEAAPLGTIIKPLVEYDDISSDSDTFSDDMAFKLDRRENDERRGTDRSDRLHKHRHHQHRRSRDLLKTKQTEKEKNQEVSSKSGSMKDRISGSSKRSNEENEDYGKAQISKSSSNKESRSSKLHKEKTRKERELKSGHKDRSKSHRKRETPKSYKTVDSPKRRSRSPHRKWSDSPKQDDSPSGASYGQDYDLSPPRSHTSSNYDSYKKSPGSTSRRQSISPPYKEPSAYQSSTRSPSPYSRRQRSVSPYSRRRSSSYERSGSYSGRSPSPYGRRRSSSPFMSKRSLSRSPLPSRKSMKSRSRSPAYSRHSSSHSKKKRSGSRSRHSSISPVRLPLNSSLGAELSRKKKERAAAAAAAKMDGKESKGSPIFLPRKENSLVEAKDSGLESKKLTRGVKLEKSAPDTELVNIPHLNTEVKNSLDTGKVKLDENSEKHPIKDLKAQGSRDSKPIALKEEIVTPKETETSEKETPPPVPAVTSPPPPLPTTSPPPQTPPLPPLPPLPAIPQQPPLPPPQPAFSHVLASSTSTLPPSTHPRTSTLSSQANSQPLAQVSVKTQVSVTAAIPHLKTSTLPPLPLPPLLPGDDDMDSPKETPPSKPVKKEKEQRPRHLLTDLPLPPELPGGDPSPPDSPEPKAVTPPQQPYKKRPKICCPRYGERRQTESDWGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLIHRSVVNMKEIVTDKQDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSGQIKLADFGLARLYNSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVELSKMDPPDLPHWQDCHELWSKKRRRQRQSGVVIEEPPPSKASRKETTSGTSAEPVKNSSPAPPQPASGKVEPGTGDAIGLGDITQQLNQSELAVLLNLLQSQTDLSIPQMAQLLNIHSNPEMQQQLEALNQSISALTEATSQQQDSEHMAPEESLKEAPPALVVQPSAEQTTSEASSTPADMQNMLAVLLSQLMKTQEPAGSLEENNSDKNSGPQGPRRTPTMPQEEAAACPPHILPPEKRPPEPPGPPPPPPPPPLIEGDLSSAPQELNPAVTAALLQLLSQPEAEPPGHLPHEHQALRPMEYSTRPHPNRTYGNTDGPETGFSATDTDERNSGPALTESLTQTLVKNRTFSGSVSHLGESSSYQGTGSVQFPGDQDLRFARVPLPLHSVVGQPFLKAEGSSNSVVHAETKLQNYGELGPGTTGASSSGAGLNWGGSAQSSAYGKLYRGPTRVPPRGGRGRGVPY
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Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors (By similarity).
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D2HBJ8
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UBP44_AILME
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Ubiquitin carboxyl-terminal hydrolase 44 (EC 3.4.19.12) (Deubiquitinating enzyme 44) (Ubiquitin thioesterase 44) (Ubiquitin-specific-processing protease 44)
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MLTMDKCKHIGQLRLAQDHSILNPQKWHCVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVNEMYVFCYLCDDYVLNDNATGDLKLLRSMLSAIKSQNYQCTTRSGRVLRSMGTSDDTYYLHDGTQSLLQNEDQMYTALWHRRRILMSKIFRTWFEQSPTGRKRQEEQFQEKIAKREVKKRRQELEYQVKAELETIHPRKSLRLQGLAQSTTVEIVPVQVPLQTPASPAKDKVVSTSEDVRLKKASDSSGKRRPIVTPGVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWLAVTASDKTRSPYKHPSITDTVYQMNECQETDTGSAPSRHPSLSLGLSGGASKSRKMELIQPREPSSQYISLCHELHTLFQVMWSGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKIQHELETTGTRLPALIPTSQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQCNGKDIASQPCRVTEMLAKFTETEALEGKIYVCDHCNSKRRRFSSKSVVLTEAQKQLMICHLPQVLRLHLKRFRWSGRNNREKIGVHVGFEEILNMEPYCCRESLKSLRPECFIYDLSAVVMHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQAYILFYTQRVTENGHSKLLPPELLSGSQHPNEEADTSSNEILS
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Deubiquitinase that plays a key regulatory role in the spindle assembly checkpoint or mitotic checkpoint by preventing premature anaphase onset. Acts by specifically mediating deubiquitination of CDC20, a negative regulator of the anaphase promoting complex/cyclosome (APC/C). Deubiquitination of CDC20 leads to stabilize the MAD2L1-CDC20-APC/C ternary complex (also named mitotic checkpoint complex), thereby preventing premature activation of the APC/C. Promotes association of MAD2L1 with CDC20 and reinforces the spindle assembly checkpoint. Promotes also the deubiquitination of histone H2A and H2B. Recruited to RNF8/RNF168-ubiquitinated chromatin surrounding double stranded breaks (DSBs), promotes hydrolysis of such ubiquitin conjugates, thus negatively regulating protein recruitment to damaged chromatin (By similarity). Participates in nucleotide excision repair (NER) pathway by deubiquitinating DDB2 to prevent its premature degradation so it can remain on damaged chromatin (By similarity). Promotes FOXP3 stabilization through 'Lys-48'-linked deubiquitination leading to increased stability and increased regulatory T-cell lineage stability. Plays also a positive role in innate immune response to DNA viruses by deubiquitinating STING1, selectively removing its 'Lys-48'-linked polyubiquitin chains and stabilizing it (By similarity).
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D2HEW7
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KLH22_AILME
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Kelch-like protein 22
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MAEEQEFTQLCKLPVQPSHPHCVNNTYRSAQHSQALLRGLLALRDSGILFDVVLVVEGRHIEAHRILLAASCDYFRGMFAGGLKEMEQEEVLIHGVSYNAMCQILHFIYTSELELSLSNVQETLVAACQLQIPEIIHFCCDFLMSWVDEENILDVYRLAELFDLSRLTEQLDTYILKNFVAFSRTDKYRQLPLEKVYSLLSSNRLEVSCETEVYEGALLYHYTLEQVQADQISLHEPPKLLETVRFPLMEAEVLQRLHDKLDPSPLRDTVANALMYHRNESLQPSLQGPHTELRSDFQCVVGFGGIHSTPSTVLSDQAKYLNPLLGEWKHFTASLAPRMSNQGIAVLNNFVYLIGGDNNVQGFRAESRCWRYDPRHNRWFQIQSLQQEHADLCVCVVGRYIYAVAGRDYHNDLNAVERYDPTTNSWAYVAPLKREVYAHAGATLEGKMYVTCGRRGEDYLKETHCYDPDSNTWHSLADGPVRRAWHGMATLLDKLYVIGGSNNDAGYRRDVHQVACYSCTSGQWSSVCPLPAGHGEPGIAVLDTRIYVLGGRSHNRGSRTGYVHIYDVEKDCWEEGPQLDNSISGLAACVLTLPRTLLLEPPRGTPDRSQADPDFASEVMSVSDWEEFDNSSED
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Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of PLK1 at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. Monoubiquitination of PLK1 does not lead to PLK1 degradation. The BCR(KLHL22) ubiquitin ligase complex is also responsible for the amino acid-stimulated 'Lys-48' polyubiquitination and proteasomal degradation of DEPDC5. Through the degradation of DEPDC5, releases the GATOR1 complex-mediated inhibition of the TORC1 pathway. It is therefore an amino acid-dependent activator within the amino acid-sensing branch of the TORC1 pathway, indirectly regulating different cellular processes including cell growth and autophagy.
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D2HHP1
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WEE2_AILME
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Wee1-like protein kinase 2 (EC 2.7.10.2) (Wee1-like protein kinase 1B) (Wee1B kinase)
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MDDSSINKELKQKLNFSYCEEESESEGQEAWETRDAHSQIPDRAEGQESEAKFTPPGPPLSSVHEVGTFQEKTKKSPEQVLMTPVSGFRNYPETPAQPDSRSKLLDCESPFTPKGLLSQSVISSTEKIPSRGSKHLRFTPVPFVDEMTSSALVNINPFTPESYRKQFLKSNGKRKTRGDFEEAGPGEGNVEQGLPAKRCVLQETNMASRYEKEFLEVEKIGVGEFGTVYKCIKRLDGCVYAIKRSTKPFAGLSNENLALHEVYAHAVLGHHPHVVRYYSAWAEDDHMIIQNEYCNGGSLQTAISENTKSGNHFQEPKLKDILLQISLGLKYIHSSGMVHLDIKPSNIFICHKMQSDSPVVPEEIENEADWFLSANVMYKIGDLGHVTSISKPKVEEGDSRFLANEILQEDYQHLPKADIFALGLTIAVAAGAESLPTNGAAWHHIREGKLPDIPQKLSEEFYNLLKNMIHPDPRERPSAAALARSRVLRPSLGKAEELQQQLNLEKFKTATLERELREAQQAWFSQEERGDAGVSGTPTGSRSTKRLVGGKSAKSSSFTWGKSSP
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Oocyte-specific protein tyrosine kinase that phosphorylates and inhibits CDK1 and acts as a key regulator of meiosis during both prophase I and metaphase II. Required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, by phosphorylating CDK1 at 'Tyr-15', leading to inhibit CDK1 activity and prevent meiotic reentry. Also required for metaphase II exit during egg activation by phosphorylating CDK1 at 'Tyr-15', to ensure exit from meiosis in oocytes and promote pronuclear formation (By similarity).
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D2HNY3
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FAN1_AILME
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Fanconi-associated nuclease 1 (EC 3.1.21.-) (EC 3.1.4.1) (FANCD2/FANCI-associated nuclease 1) (Myotubularin-related protein 15)
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MSEGKSPAKKRARRSLSISKTKKNECNSIISFFNNVPPAKLACPICSKMVPRYDLNWHLDEKCANNDNITPVDLRHVGFTDSSGSTVNLTNTVLENVTPGKLSPSKASLTPDPSDSAKMGIKQQTSPYFKNNKDLVFKNQDKLRHHNVKVITLGSLSSKLSRRYTEARRSICKKNEEFASKSPQSPSSTVVRSPVDNCSEIEDKDQILENSSQKENVFTCDSLNEQRTEHSVEDTKVLEAESQEATQECGRSPLTPAFSDNAFVLFSPDLTRGNPLRSTSEDSLEWETITGIDGKDVEKCEAGSCEEVKVTVASEAKTQLSDWEAKCHSSTPDDSKGCNIQDLLLEGDSDLKNEITCRIPLEQGSSCDVPDKTVTVPPSHPYYLRSFLVVLKAVFENEEDRMLFDEHEKEIVTKFYQLSASAQKLYVRLFQRKFSWLKMNKLEYEEIAPDLTPVIGELQQAGFLQTESELQELSEVLELLSAPELKTLAKTFHLVNPNGQKQQLVDTFLKLAKQPSVCTWGKNQPGIGAVILKRAKGLAGQALRVCKGPRAVFSRVLLLFSLTDSLEDEEAACGGQGQLSTVLLVNLGRMEFPRYTINRKTQIFQDRDDLIRYAAAAHMLSDISTAMANGNWKEANELSQCAKSDWNKLKSHPSLRYHENLPLFLRCFTVGWIYTRILSRTVEILQRLHMYEEAVKELESLLSQRVYCPDSRGRWWDRLALNLHQHLKRLEPAIKCITEGLADPEVRTGHRLSLYQRALRLRESPSCQKYRHLFHQLPEVTVGDVKHVTITGRLCPQRGMGKSVFVMEAGGPTAPATVLCSVEEVALAYYRRSGFDQGIHGEGSTFSTLYGLLLWDIIFMDGIPDVFRNAYQASPLDLCTDSFFASRGPAIEARLQRIHSAPAESLRAWVAAAWQAQEGRVASIVSWDRFASLQQAQDLVSCLGGPVLSGVCRRLAADFRHCRGGLPDLVVWNSQSRHFKLVEVKGPNDRLSHKQMLWLDELQKLGADVEVCHVVAVGAKSKSLT
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Nuclease required for the repair of DNA interstrand cross-links (ICL) recruited at sites of DNA damage by monoubiquitinated FANCD2. Specifically involved in repair of ICL-induced DNA breaks by being required for efficient homologous recombination, probably in the resolution of homologous recombination intermediates. Not involved in DNA double-strand breaks resection. Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions. Probably keeps excising with 3'-flap annealing until it reaches and unhooks the ICL. Acts at sites that have a 5'-terminal phosphate anchor at a nick or a 1- or 2-nucleotide flap and is augmented by a 3' flap. Also has endonuclease activity toward 5'-flaps.
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D2HS90
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STPAP_AILME
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Speckle targeted PIP5K1A-regulated poly(A) polymerase (Star-PAP) (EC 2.7.7.19) (RNA-binding motif protein 21) (RNA-binding protein 21) (U6 snRNA-specific terminal uridylyltransferase 1) (U6-TUTase) (EC 2.7.7.52)
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MAAVDLDVQSLPRGGFRCCLCHVTTANRPSLDAHLGGRKHRHLVELRATRKAQGLRSVFVSGFPRDVDSAQLTQYFQAFGPVASVVMDKDKGVFAIVEMGDVGTREAVLSQPQHTLGGHRLRVRPREQKEFQSPASKSPKGAAPDSHQLTKALAEAPDVGAQMVKLVGLRELSEAERQLRNLVVALMQEVFTEFFPGCVVHPFGSSINSFDVHGCDLDLFLDLGDLEESQPAPKAPESPSLDSALASPLDPQALACTPASPPDSQPPSPQDSEALDFETPSSSLAPQTPDSALASETLASPQSLPPASPLQEDRGEGDLGKALELAEALSGEKTEGVAMLELVGSILRGCVPGVYRVQTVPSARRPVVKFCHRPSGLHGDVSLSNRLALHNSRFLSLCSELDGRVRPLVYTLRCWAQGRGLSGSGPLLSNYALTLLVIYFLQTRDPPVLPTVSQLTQKAGEGEQVEVDGWDCSFPRDASGLEPSTNKEPLSSLLAQFFSCVSCWDLRGSLLSLREGQALPVAGDLPSNRWEGLRLGPMNLQDPFDLSHNVAANVTSRVAGRLQNSCQAAANYCRSLQYQRRSSRGRDWGLLPLLQPSSPSSLLSATPIPLPPAPFTQLTAALAQVLREALGCHIEQGTKRLRSDRGGPEESPQGGTSKRLKLDGEEKSCEEGREEQQGYIRDHSEDGVEEMVVEVGEMVQDWVQSPGRPGEPPQMLREQLATGEEGQSGHAALAEQGPKGPEAAREGSQGETGRGVSLSSVSWRCALWHRVWQGRRRARRRLQQQTKERGRGSAGTAEWLAVEAQVTRELRGLSSAAQRPEAEPLLTFVASASQVNQTLTVTPIQDSQGLFPDLHHFLQVFLPQALRNL
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Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication-dependent histone mRNA degradation.
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D2HWM5
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RFWD3_AILME
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E3 ubiquitin-protein ligase RFWD3 (EC 2.3.2.27) (RING finger and WD repeat domain-containing protein 3) (RING finger protein 201)
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MAQEAMEYNVDEQLEHRVAEQPVPAEVVSTQGGPPPLQPLPTEVVSSQGAPPLLQPAPAEGTSSQVGPHLLQPAAQLSVDLTEEVELLGEDRVENINPGASEEHRQPSRVNRPIPVSSLDSMNSFISGLQRLHGMLEFLRPPSDHNVGPVRSRRRRGSASRRSRTVGSQRTDSARSRAPLDAYFQVSRTQPHLPSMSQDSETRNPVSEDLQVSSSSSSDSESSAEYEEVVVQAEDTRAVVSEEQGGTAAEQEVTCVGGGETLPKQSPQKTNPLLPSVSKDDEEGDTCTICFEHWTNAGDHRLSALRCGHLFGYKCISKWLKGQARKCPQCNKKAKHSDIVVLYARTLRALDTSEHERMKSSLLKEQMLRKQAELESAQCRLQLQVLTDECSKLHSRVQDLQKLTVQHRDQISQSPSGSQARSLNCLPSSQNQRKYHFQKTFTVSPTGNCRIMTYCDALSCLVVSQPSPQASFLPGFGVKMLSTANMKSSQYVPMHGKQIRGLAFSSRSKGLLLSASLDSTVKLTSLETNTVVQTYNAGRPVWSCCWCLDESNHIYAGLVNGSILVYDLRNTSSHIQELVPQKARCPLVSLSYIPRAASAAFPYGGVLAGTLENASFWELKMGFSHWPHVLPMEPGGCVDFQTESSTRHCLVTYRPDKNHNTLRSVLMEMSYKLNDAGEPVCSCRPVQTFLGGPTCKLLTKSAIFQNPENDGSILVCTGDEASNSALLWDAGSGSLLQELQADQPVLDICPFEANHSSCLATLTEKMVHIYRWE
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E3 ubiquitin-protein ligase required for the repair of DNA interstrand cross-links (ICL) in response to DNA damage. Plays a key role in RPA-mediated DNA damage signaling and repair. Acts by mediating ubiquitination of the RPA complex (RPA1, RPA2 and RPA3 subunits) and RAD51 at stalled replication forks, leading to remove them from DNA damage sites and promote homologous recombination. Also mediates the ubiquitination of p53/TP53 in the late response to DNA damage, and acts as a positive regulator of p53/TP53 stability, thereby regulating the G1/S DNA damage checkpoint. May act by catalyzing the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome. In response to ionizing radiation, interacts with MDM2 and enhances p53/TP53 ubiquitination, possibly by restricting MDM2 from extending polyubiquitin chains on ubiquitinated p53/TP53.
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D2HXI8
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GWL_AILME
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Serine/threonine-protein kinase greatwall (GW) (GWL) (EC 2.7.11.1) (Microtubule-associated serine/threonine-protein kinase-like) (MAST-L)
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MEPTAGSEKESEGDTVTGECVNRIPVPRPPSIEEFTIVKPISRGAFGKVYLGQKGGKLYAVKVVKKADMINKNMTHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNRDINMMDILTTPSMAKPRQDYSRTPGQVLSLISSLGFFTPVAEKNKDSANILSTHVSETSQLSQGLVCPMSVDHRDTTPYSSKLLNSCLETVAPNPGMPVKCLTSHLLQSRRRLATSSASSQSHTFVSSVESECHSSPRWEKDCQESDHALGYTVMSWNIIEKPSCTDSRDAIETKGFNKKDLELALSPIHNSSTIPETGRSCVNLAKKGFPGEVSWEARELDINNIHVATDTAQSGFHQSDQWAVDSGDATEEHLGKRGFKRNFELVDSSPCQNIIQHKKNCIEHKPRNAMSDGYINQRTGLTTEVQDLKLSVCGGQQSDCANKENMVNSFIDKPQTPEKSPVPMIAKNLLCELDEDCDKNNKRDLLSSSLLCSDDERASKSICMDSDSSFPGISVMESSLERQSLDPDKSIKESSFEESNIEDLLTVSPRWQENILPKGDENPAVQDSSQKMLAPSSKVLKTLTLSKRNAVAFRSFNSHINASNNSEPSKMSLTSLDGMDISCVYSGSYPMAITPNQKGTSYIPYQQTPNQVKSGTPYRTPKSVRRGAAPVDDGRILGTPDYLAPELLLGRAHGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILKRDIPWPEGEEKLSDNSQNAVEILLTIDNAKRAGMKELKRHHLFSDVDWENLQHQTMPFIPQPDDETDTSYFEARNNAQHLTISGFSL
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Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and ENSA at 'Ser-62' and 'Ser-67', respectively. ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited (By similarity).
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