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 27-MAR-2024, entry version 96.
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 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:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd19532; C_PKS-NRPS; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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_com.
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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
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 NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF20; HYBRID PKS-NRPS SYNTHETASE APDA; 1.
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; PF21089; PKS_DH_N; 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; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS52019; PKS_MFAS_DH; 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 15..454
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348,
FT ECO:0000305|PubMed:17216664"
FT DOMAIN 993..1313
FT /note="PKS/mFAS DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
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 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 993..1135
FT /note="N-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1158..1313
FT /note="C-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
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 ACT_SITE 189
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 326
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 374
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 1025
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 1217
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
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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