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TENS_BEABA
ID   TENS_BEABA              Reviewed;        4239 AA.
AC   A0JJU1;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Tenellin synthetase {ECO:0000303|PubMed:18266306};
DE            Short=TENS {ECO:0000303|PubMed:17216664};
DE            EC=2.3.1.- {ECO:0000269|PubMed:17216664, ECO:0000269|PubMed:18266306};
DE            EC=6.3.2.- {ECO:0000269|PubMed:17216664, ECO:0000269|PubMed:18266306};
DE   AltName: Full=Hybrid PKS-NRPS synthetase tenS {ECO:0000303|PubMed:17216664};
DE   AltName: Full=Tenellin-type 2-pyridones biosynthesis cluster protein S {ECO:0000303|PubMed:17216664};
GN   Name=tenS {ECO:0000303|PubMed:17216664};
OS   Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS   shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=176275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, CATALYTIC ACTIVITY,
RP   DOMAIN, AND DISRUPTION PHENOTYPE.
RC   STRAIN=CBS 110.25;
RX   PubMed=17216664; DOI=10.1002/cbic.200600398;
RA   Eley K.L., Halo L.M., Song Z., Powles H., Cox R.J., Bailey A.M.,
RA   Lazarus C.M., Simpson T.J.;
RT   "Biosynthesis of the 2-pyridone tenellin in the insect pathogenic fungus
RT   Beauveria bassiana.";
RL   ChemBioChem 8:289-297(2007).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=18266306; DOI=10.1002/cbic.200700390;
RA   Halo L.M., Marshall J.W., Yakasai A.A., Song Z., Butts C.P., Crump M.P.,
RA   Heneghan M., Bailey A.M., Simpson T.J., Lazarus C.M., Cox R.J.;
RT   "Authentic heterologous expression of the tenellin iterative polyketide
RT   synthase nonribosomal peptide synthetase requires coexpression with an
RT   enoyl reductase.";
RL   ChemBioChem 9:585-594(2008).
RN   [3]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=20575135; DOI=10.1002/cbic.201000259;
RA   Heneghan M.N., Yakasai A.A., Halo L.M., Song Z., Bailey A.M., Simpson T.J.,
RA   Cox R.J., Lazarus C.M.;
RT   "First heterologous reconstruction of a complete functional fungal
RT   biosynthetic multigene cluster.";
RL   ChemBioChem 11:1508-1512(2010).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, PATHWAY, AND INDUCTION.
RX   PubMed=34903054; DOI=10.1128/mbio.03279-21;
RA   Chen B., Sun Y., Li S., Yin Y., Wang C.;
RT   "Inductive production of the iron-chelating 2-pyridones benefits the
RT   producing fungus to compete for diverse niches.";
RL   MBio 12:e0327921-e0327921(2021).
CC   -!- FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that
CC       mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating
CC       compounds involved in iron stress tolerance, competition with the
CC       natural competitor fungus Metarhizium robertsii and insect hosts
CC       infection (PubMed:17216664, PubMed:18266306, PubMed:20575135,
CC       PubMed:34903054). TenS catalyzes the assembly of the polyketide-amino
CC       acid backbone (PubMed:18266306, PubMed:34903054). Because tenS lacks a
CC       designated enoylreductase (ER) domain, the required activity is
CC       provided the enoyl reductase tenC (PubMed:18266306, PubMed:34903054).
CC       Upon formation of the polyketide backbone on the thiotemplate, the
CC       triketide is transferred to the NRPS module and linked to tyrosine to
CC       produce the pyrrolidine-2-dione intermediates, including pretellinin A,
CC       11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A,
CC       14-hydropretellenin A, 12-oxopretellenin A and prototellinin D
CC       (PubMed:18266306, PubMed:34903054). The pathway begins with the
CC       assembly of the polyketide-amino acid backbone by the hybrid PKS-NRPS
CC       tenS with the help of the enoyl reductase tenC. These enzymes catalyze
CC       the synthesis of the pyrrolidine-2-dione intermediates pretellinin A,
CC       11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A,
CC       14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The
CC       cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring
CC       expansion of pretenellin A and 14-hydropretellenin A to form the 2-
CC       pyridone core, leading to pretenellin B and pyridovericin,
CC       respectively. The cytochrome P450 monooxygenase tenB is then required
CC       for the selective N-hydroxylation of the 2-pyridone nitrogen of yield
CC       tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP-
CC       glucosyltransferase GT1 and the methyltransferase MT1, located outside
CC       the tenS gene cluster, contribute to the stepwise glycosylation and
CC       methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O-
CC       methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds
CC       such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A
CC       are also produced but the enzymes involved in their biosynthesis have
CC       still to be determined (PubMed:34903054). {ECO:0000269|PubMed:17216664,
CC       ECO:0000269|PubMed:18266306, ECO:0000269|PubMed:20575135,
CC       ECO:0000269|PubMed:34903054}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:17216664, ECO:0000269|PubMed:18266306,
CC       ECO:0000269|PubMed:20575135, ECO:0000269|PubMed:34903054}.
CC   -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC       transcription factor tenR and is induced during cocultures with the
CC       natural competitor fungus Metarhizium robertsii.
CC       {ECO:0000269|PubMed:17216664}.
CC   -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC       (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC       (C) domains) which when grouped together are referred to as a single
CC       module. Each module is responsible for the recognition (via the A
CC       domain) and incorporation of a single amino acid into the growing
CC       peptide product. Thus, an NRP synthetase is generally composed of one
CC       or more modules and can terminate in a thioesterase domain (TE) that
CC       releases the newly synthesized peptide from the enzyme. TenS contains
CC       also a polyketide synthase module (PKS) consisting of several catalytic
CC       domains including a ketoacyl synthase domain (KS), a malonyl-CoA:ACP
CC       transacylase domain (MAT), a dehydratase domain (DH), a
CC       methyltransferase domain (MT), and a ketoreductase domain (KR). Instead
CC       of a thioesterase domain (TE), tenS finishes with a reductase-like
CC       domain (RED) for peptide release. TenS has the following architecture:
CC       KS-MAT-DH-MT-KR-PCP-C-A-T-RED. {ECO:0000305|PubMed:17216664}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the production of tenellin-type 2-
CC       pyridones and their intermediates. {ECO:0000269|PubMed:17216664,
CC       ECO:0000269|PubMed:34903054}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC       family. {ECO:0000305}.
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DR   EMBL; AM409327; CAL69597.1; -; Genomic_DNA.
DR   SMR; A0JJU1; -.
DR   STRING; 176275.XP_008600657.1; -.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 1.10.1200.10; -; 2.
DR   Gene3D; 3.10.129.110; -; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 3.40.366.10; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR013217; Methyltransf_12.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020807; PKS_dehydratase.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF47336; SSF47336; 2.
DR   SUPFAM; SSF51735; SSF51735; 2.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Ligase; Methyltransferase; Multifunctional enzyme; Oxidoreductase;
KW   Phosphopantetheine; Phosphoprotein; Repeat; Transferase.
FT   CHAIN           1..4239
FT                   /note="Tenellin synthetase"
FT                   /id="PRO_0000438443"
FT   DOMAIN          2502..2582
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          3751..3835
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          18..457
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:17216664"
FT   REGION          589..923
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:17216664"
FT   REGION          993..1310
FT                   /note="Dehydratase (DH) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:17216664"
FT   REGION          1459..1652
FT                   /note="Methyltransferase (MT) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:17216664"
FT   REGION          2209..2382
FT                   /note="Ketoreductase (KR) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:17216664"
FT   REGION          2587..2629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2642..2712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2723..3169
FT                   /note="Condensation (C) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:17216664"
FT   REGION          3203..3614
FT                   /note="Adenylation (A) (KR) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:17216664"
FT   REGION          3728..3752
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3862..3892
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3899..4145
FT                   /note="Reductase (RED) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:17216664"
FT   COMPBIAS        2647..2712
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3729..3750
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2542
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3795
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   4239 AA;  460365 MW;  4DF488E427353542 CRC64;
     MSPMKQNESE SHSVSEPIAI IGSAYRFPGG CNTPSKLWDL LRQPRDILKE IDPERLNLRR
     YYHPDGETHG STDVANKAYT LEEDISRFDA SFFGISPLEA ASMDPQQRTL LEVVYESTET
     AGIPLDKLRG SLTSVHVGVM TTDWAQMQRR DPETMPQYTA TGIASSIISN RISYIFDLKG
     ASETIDTACS SSLVALHNAA RALQSGDCEK AIVAGVNLIL DPDPFIYESK LHMLSPDARS
     RMWDAAANGY ARGEGAAAVV LKTLGHALRD GDRIEGVIRS TFVNSDGLSS GLTMPSSAAQ
     TALIRQTYRK AGLDPVRDRP QFFECHGTGT KAGDPVEARA ISDAFLPPSH RTNGAATTVD
     APLYVGSIKT VVGHLEGCAG LAGLVKVLLS LKHGIIPPNL WFDKLNPEIA RYYGPLQIPT
     KAIPWPKLAP GTPLRASVNS FGFGGTNAHA IIERYDASQS YCSQWRRNMT EEKTIARTQN
     NESIEIPVPL VLTAKTGRAL WRTVDAYAQH LRQHPKLRVT NLSQFMHSRR STHRVRASFS
     GASREELVEN MAKFVQAHAA DAKSPASQNR IGYSPLHIDP KEAPGILGVF TGQGAQWPAM
     GRDMMHQSPL FRKTIADCES VLQALPAKDA PVWSLSEELK KDASTSRLGE AEISQPLCTA
     VQLALVNVLL ASGVHFDAVV GHSSGEIAAT YASGIINLEA AMQIAYYRGL YAKLARGETD
     AAGGMMAAGL SMNDAVKLCR LPEFEGRIHV AASNAPQSVT LSGDKEAIKA AKAKLDADGV
     FARELKVDTA YHSHHMLPCA EPYLKALLAC DIQVSAPTTT PGRKCMWSSS VRGDAELLRH
     DRNLDSLKGP YWVANMVQTV LFSRAVQSTI WHGGPFDLAV EVGPHPALKG PTEQTLKAVY
     GSAPLYTGVL SRGANDAVAF STAIGNIWSH LGPAFVDITG YQSIFSSTCE GHGGGSAAPF
     ISDLPLYPWD HDEEYWRESR ISRRHRTGKD ESHELLGRRT PDDNEREIRW RNLLKVSELP
     WTQGHRVLGE VLLPGAAYIS MAIEAGRRLA LDQGREARLL EVSDVDILRP VVVADNKEGT
     ETLFTVRLLD EYASTGKKSD ELITASFSFY IYNSPASTSI VHTCEGRIAV QLGAKLGSEA
     GANSMPQLPH REPSISNLQQ LDCEKLYSVF ETIGLEYSGA FRRIVSSSRC LGHATATASW
     PTTDLNDCYL IHPAILDVAF QTIFVARAHP DSGQLSSALL PSRIERVRVV PSLAMGSKLQ
     NNENFNAAID SWALNQTASS LTGNINVYDA ESGRALIQVE GFEVRAVGEP DASKDRLLFY
     ETVWGRDISI MGLSDPIRDE TSDAMVHNLS EAIERVSLFY VRQLMGELST ADRRQANWYH
     TRMLAAFDYH LAKVHEETHL HLRPEWLADD WAVIQTIDEA YPDAVELQML HAVGQNVADV
     IRGKKHLLEV LRVDNLLDRL YTEDKGMHMA NLFLANALEE ITFKFPRCKI LEIGAGTGAT
     TWAALSAIGE AFDTYTYTDL SVGFFENAVE RFSAFRHRMV FRALDIEKDP ASQSFDLNSY
     DIIIATNVLH ATRNLGVTLG NVRALLKPGG YLLLNEKTGP ESLRATFNFG GLEGWWLAEE
     KERQLSPLMS PDGWDAQLQK ASFSGVDHIV HDVQEDQQDK QQNSMIMSQA VDDTFYARLS
     PLSEMANLLP MNEPLLIIGG QTTATLKMIK EIQKLLPRQW RHKVRLIASV DHVEAEGLPA
     HSDVICLQEL DRGLFTTAMT SKCLDALKTL FINTRNLLWV TNAQNSSSMT PRASMFRGIT
     RVLDGEVPHI RTQVLGIEPR ETPSATARTL LEAFLRLRSD DGRHAGNVDE DGADGSSQQV
     LWLHEPEAEL LSNGTMMVPR VKARKSLNDT YLASTRAIST TVDARCVSVQ AVAGPAKMLL
     RPVEDFAGEH AISNQTSDSK VHIQVESTLH IPEALDGTCL YLVCGWTRTA ETSVPVIALS
     ANNASMVAVE SKAVAMIDEV DVKPETLLRV FQHMAMQALD SAVKRHGQGQ STALIYGADE
     ELAKLTSERF AVRESKVYFA SSRTFAPGDW LKVQPLLSKF ALSQMIPADV EVFIDCLGDT
     ESFDACRTLQ SCLSTTRTVQ HRLDACLLSQ MSRCSPDALV DAYSYAKTQS NAEFSWNGYV
     KTFTAAELAG KLSHSLIHSV YMTNWQKKDS ILVTVPPLQT RGLFKSDRTY LMVGAAGGLG
     TSICRWMVRN GARHVVVTSR NPKADPEMLN EAERYGAAVQ VVPMDACSKD SVQTVVDMIR
     ATMPPIAGVC NAAMVLRDKL FLDMNVDHMK DVLGPKMQGT EHLDSIFAQE PLDFFVLLSS
     SAAILNNTGQ SNYHCANLYM DSLVTNRRSR GLAASIIHVG HVCDTGYVAR LVDDTKVQMS
     LGTTRVMSVS ETDVHHAFAE AVRGGQPDSR SGSHNIIMGI EPPTKPLDLT KRKPVWISDP
     RLGPCLPFST LENQMMASEQ AAAASAVDSL AQQVSEATTD EEAAVAALKG FATKLEGILL
     LPLGSIGEDS AGRPVTDLGI DSLVAVEIRT WFLKQLRVDV PVMKILGGST VGQLSALAAK
     LARQDAKKRA QLEEPSGNQP VALPSPPPKD KAGGLNKNGK SPKLPEIAQV DTVVERMEPL
     VLEASDRGGS STANLTTSSS VSELDDSLHE STLQSSDNNG ESTPSKSSNC NSDSGSDNQA
     PKEIPSNGFF TQPAATARPN VLREAPMSPA QSRIWFLSKH IAEPDAYNMV FHYRVRGPLS
     MVRLRHALQT VTNHHECLCM CFYASADNGQ PMQGLLASSA FQMTHVPGGE EQDVQRELRK
     LKTRVWSVES GQTLELVVLG PRPGTAAAAE EEEEEFSLLF GYHHIVMDAI SFYIFLADLD
     KAYRMLPLDK ASAGSHLDLA AHQRQQERAG AWEESLEFWR AEFETIPEML PSLSVALPTL
     HRGAVGTHRV LRELAHEQGG DAAIKKMCKH LRVSPFNLHI AVLQVVIARL ASIEDVCVGI
     VDANRSDSRA SRMVGCFVNM LPVRSRILPT ATLADVARAA SSKALAAFAH GQVPLDSILD
     KVKAPRPAGS TPLFQVALNY RPAAAIASKQ ALGGECEMEL LADDFKDAEN PFEISVLVSE
     MSGGRIAVEV VCQKSRYTMQ ATEALLDAYL NVLAGFLSDS AQSVGDCVVH DQSKVEHALD
     LGRGAQKSFG WPRTLSERVM SICQQHSTKS AIKDGRNELS YAQLASRVNR TASAILGTGC
     SVGSRIAVLC NPSIDAIVAM LAILHIGGVY VPLDTSLPEA RHQSLASNCT PSLIISHAAT
     RERAHKLSAA ISAPGHEPAR ELTLDDLSPP EETGYMAPLN AEPNAPAILL YTSGSTGTPK
     GVLLTQANFG NHIALKTDIL GLQRGECVLQ QSSLGFDMSL VQVFCALANG GCLVIVRQDV
     RRDPVELTTL MTQHKVSLTI ATPSEYLAWL QYGSDALAQA TSWKNLCMGG EPIPPLLKDE
     LRRRLERKDL VVTNCYGPTE TTAAISFQSV ALDSEHGHEL PGESELAQYA VGKALPNYSI
     RIRDSAGGAW LPVNHTGEIV IGGAGVALGY LDMPEETRAR FLQTPGEEDG MMLYRTGDKG
     RLLSDGTLLC FGRITGDYQV KLRGLRIELG EVEAALLQAS HGLIHTAVVS RRGDVLVAHC
     ARSHESSRET TGGGEQQDAT AILRRVSELL PQYSVPAAIA LLPSLPTNAN GKLDRKAIAA
     LPLSPQDEAA AATSPSNNNI NNNTPSGGGG EKMTVRQGEL RLLWERVLPR DAATTTTNSV
     RITPESDFFL RGGNSLLLMK LQAAIRESMG VRVSTKALYQ ASTLSGMARC VAEQRSDDDE
     AEEDIDWAAE VAVPPSMLAQ IEKLQHSSAS SSSSSSSSSS AGSSSTQRPR KTSGLEILLT
     GATGFLGGQL LERLVQSPRV STVHCVAVPV DEQSLLEPFL QQQADGTRRK VRCYIGNLAA
     PALGLTAADQ TALSQTADVI VHAGSMGHCL NTYATLAAPN FASTRHLCSL ALSRSPPIPL
     AFASSNRVAL LTGSTAPPPA SAAAFPPPPG AQGFTASKWA SEAFLEKLAA SIMTSKTKST
     TTTTTTTVPW RVSIHRPCAL ISDRAPNSDA LNAILRYSTS MRCVPSLPEH RAEGYLDFGQ
     VDKVVEEMVG DILGLADERQ QEGPAVVYRH HSGGVKVPIH EFREHMESVY GGRFESVELG
     QWIVRAVDAG MDPLISAYLE TFLEGDASMV FPYMGEQAV
 
 
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