TENS_BEAB2
ID TENS_BEAB2 Reviewed; 4235 AA.
AC J4KMC1;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Tenellin synthetase {ECO:0000303|PubMed:17216664};
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 biosynthesis protein S {ECO:0000303|PubMed:17216664};
GN Name=tenS {ECO:0000303|PubMed:34903054}; ORFNames=BBA_07338;
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860;
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.-H., Zheng P., Wang Z.-L., Zhang S., Xie X.-Q., Shang Y.,
RA St Leger R.J., Zhao G.-P., Wang C., Feng M.-G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
RN [2]
RP FUNCTION, PATHWAY, CATALYTIC ACTIVITY, DOMAIN, AND DISRUPTION PHENOTYPE.
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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 [4]
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 [5]
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; JH725173; EJP63694.1; -; Genomic_DNA.
DR RefSeq; XP_008600657.1; XM_008602435.1.
DR EnsemblFungi; EJP63694; EJP63694; BBA_07338.
DR GeneID; 19890350; -.
DR HOGENOM; CLU_000022_37_4_1; -.
DR InParanoid; J4KMC1; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
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; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..4235
FT /note="Tenellin synthetase"
FT /id="PRO_0000455686"
FT DOMAIN 2500..2580
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3748..3833
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 18..458
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000250|UniProtKB:A0JJU1, ECO:0000255"
FT REGION 590..924
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000250|UniProtKB:A0JJU1, ECO:0000255"
FT REGION 993..1310
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000250|UniProtKB:A0JJU1, ECO:0000255"
FT REGION 1459..1652
FT /note="Methyltransferase (MT) domain"
FT /evidence="ECO:0000250|UniProtKB:A0JJU1, ECO:0000255"
FT REGION 2208..2381
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000250|UniProtKB:A0JJU1, ECO:0000255"
FT REGION 2587..2709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2720..3163
FT /note="Condensation (C) domain"
FT /evidence="ECO:0000250|UniProtKB:A0JJU1, ECO:0000255"
FT REGION 3197..3609
FT /note="Adenylation (A) (KR) domain"
FT /evidence="ECO:0000250|UniProtKB:A0JJU1, ECO:0000255"
FT REGION 3724..3750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3860..3889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3896..4141
FT /note="Reductase (RED) domain"
FT /evidence="ECO:0000250|UniProtKB:A0JJU1, ECO:0000255"
FT COMPBIAS 2644..2709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3726..3747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2540
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3793
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 4235 AA; 459439 MW; ED442D9BE30E6BF4 CRC64;
MSPMKQNESE SHSVSEPIAI VGSAYRFPGG CNTPSKLWDL LQQPRDILKE LDPERLNLRR
YYHPDGETHG STDVSNKAYT LEEDISRFDA SFFGISPLEA ASMDPQQRTL LEVVYESTET
AGIPLDKLRG SLTSVHVGVM TTDWAQVQRR DPETMPQYTA TGIASSIISN RISYIFDLKG
ASETIDTACS SSLVALHNAA RALQSGDCEK AIVAGVNLIL DPDPFIYESK LHMLSPDARS
RMWDAAANGY ARGEGAAAVV LKTLGHALRD GDRIEGVIRS TFVNSDGLSS GLTMPSSAAQ
TALIRQTYRK AGLDPVRDRP QFFECHGTGT RAGDPVEARA ISDAFLPSHR TNGGGAATTV
DDPLYVGSIK TVVGHLEGCA GLAGLVKVLL SLKHGIIPPN LWFDKLNPEI ARYYGPLQIP
TKAIPWPELA PGTPLRASVN SFGFGGTNAH AIIERYDASQ SYCSQWRRDM TEEKTIARTQ
NNDDVEIPVP LVLTAKTGGA LWRTVDAYAQ HLRQHPKLRV ANLSQFMHSR RSTHRVRASF
SGASREELVE NMANFVQAHA ADAKSPASQN RIGYSPLLID PKEVSGILGI FTGQGAQWPA
MGRDMMHQSP LFRKTIADCE SVLQALPLKD APAWSLSEEL KKDASTSRLG EAEISQPLCT
AVQLALVNVL TASGVYFDAV VGHSSGEIAA TYASGIINLK AAMQIAYYRG LYAKLARGQS
DEAGGMMAAG LSMDDAVKLC RLPEFEGRIQ VAASNAPQSV TLSGDKEAIK AAKAKLDADG
VFARELKVDT AYHSHHMLPC AEPYLKALLA CDIQVSAPTK TPGRKCMWSS SVRGDAELLR
RDRNLDSLKG PYWVANMVQT VQFSRAIQST IWHGGPFDLA VEVGPHPALK GPTEQTLKAV
YGSAPLYTGV LSRGANDAVA FSTAIGNIWS HLGPAFVDIT GYQSIFSGTC EGHGGSEAPF
ISDLPLYPWD HDEEYWRESR ISRRYRTGKD ESHELLGRRM PDDNEREIRW RNLLKVSELP
WTQGHRVLGE VLLPGAAYIS MAIEAGRRLA LDQGREVSLL EVSDVDILRP VVVADNKEGT
ETLFTVRLLD EYASTGKKSD ELMTASFSFY IYNSPASTSI VHTCEGRIAV HLGAKLGSEA
AANSTPQLPP REPSVSNLQQ LDCEKLYSVF ETIGLEYSGA FRRIVSSSRC LGHATATASW
PTADLNDCYL VHPAILDVAF QTIFVARAHP DSGQLSSALL PSRIERVRVV PSLAMGSKLQ
NNENFNAAID SWALNQTASS LTGNINVYDA DSERALIQVE GFEVRAVGEP DASKDRLLFY
ETVWGRDISI MGLSDPIRDE TSDAMVQNLS EAIERVSLFY VRQLMGELST ADRRQANWYH
TRMLAAFDHH LAKVHEETHL HLRPEWLADD WTVIQTIDEA YPDAVELQML HAVGQNVADV
IRGKKHLLEV LRVDNLLDRL YTEDKGMHMA NLFLANALKE ITFKFPRCKI LEIGAGTGAT
TWAALSAIGE AFDTYTYTDL SVGFFENAVE RFSAFRHRMV FRALDIEKDP ASQSFDLNSY
DIIIATNVLH ATRNLGVTLG NVRSLLKPGG YLLLNEKTGP DSLRATFNFG GLEGWWLAEE
KERQLSPLMS PDGWDAQLQK AQFSGVDHIV HDVQEDQQDK QQNSMIMSQA VDDTFYARLS
PLSEMANLLP MNEPLLIIGG QTTATLKMIK EIQKLLPRQW RHKVRLIASV NHLEAEGVPA
HSNVICLQEL DRGLFTTAMT SKCLDALKTL FINTRNLLWV TNAQHSSSMT PRASMFRGIT
RVLDGEIPHI RTQVLGIEPR ATSSATARNL LEAFLRLRSD DGRHAANVDE DGADGSSQQV
LWLHEPEAEL LSNGTMMIPR VKARKSLNDT YLASTRAIST TVDARCVSVQ AVAGPAKMLL
RPVEDFAVEH AISSQSTDSK VHIQVESTLH IPEALDGTCL YLVCGWTRTA ETSVPVIALS
TSNASIVAVE SKAVAMIDEA DVKPETLFRV FQHMAMQALD SAVGRHGQGQ STALIYGADE
ELAKLTSERF AVRESKVYFA STRTSAPGDW LKVQPLLSKF ALSQMMPADV EVFIDCLGDT
ESFDACRTLE SCLSTTSTVH RLDACLLSRM SQCSPDTLAD AYSHAKTQSN AEFSWNGNVQ
TFTAAELAGK LSHSLMHSVY MTDWQEKDSI LVTVPPLQTR GLFKSDRTYL MVGAAGGLGT
SICRWMVRNG ARHVVVTSRN PKADPEMLNE ARRYGAAVKV VPMDACSKDC VQTVVDMIRD
TMPPIAGVCN AAMVLRDKLF LDMNVDHMNN VLGPKMQGTE HLDSIFAQEP LDFFVLLSSS
AAILNNTGQS NYHCANLYMD SLVTNRRSRG LAASIIHVGH VCDTGYVARL VDDSKVQMSL
GTTRVMSVSE TDVHHAFAEA VRGGQPDSRS GSHNIIMGIE PPTKPLDVAK RKPVWISDPR
LGHMLPFSTL ENQMVASEQA AASAADSLAQ QVSEATTDEE AAAAALKGFA TKLEGILLLP
LGSIGEDSAG RPVTDLGIDS LVAVEIRTWF LKQLRVDVPV MKILGGSTVG QLSALAAKLA
RQDAKKRAQL EEASGNQPVA LPPLNDKETG PSKKGKAQEF PETVQVVGTA AERTEPLVLE
ASDRGGSSTA NFTTSSSVSE LDDSLQESTL QSSENNGEST PSKSSNCNSD SGSDNQAPRE
ISSNGFFTQP AATARPNVLR EAPMSPAQSR IWFLSKHIAE PDAYNMVFHY RVRGPLSMVR
LRHALQTVTN HHECLCMCFY ASADNGQPMQ GLLASSASQM TIVPGGEEQD LQRELRKLKT
RVWSVESGQT LELVVVGPRP GTAAAEEEEF SLLFGYHHIV MDAISFSIFL ADLDKAYRML
PLDKASAGSH LDLAAHQRQQ EHAGAWKESL EFWQAEFETI PEMLPPLSVA LPTLQRGAVG
THRVLRELAH EQGGDAAIKK TCKNLRVSPF NLHIAVLQVV IARLGSIEDV CVGIVDANRS
DSRASRMVGC FVNMLPVRSR ILPSATLADV ARAASSKALA AFAHGQVPLD SILDKVKAPR
PAGSTPLFQV ALNYRPAAAI ASKQSLGGEC EMELLADDFK DAENPFEISV LVSEMPGGRI
AVEVVCQKSR YTMQATEALL DAYLNVLAGF LSDTAQSVGD CVVHDQSKVE HALDLGKGAQ
KSFGWPRTLS ERVMSICQQH STKSAIKDGR NELSYAQLAS KVNHTASALV NAGCSVGSRI
AVLCNPSIDA IVAMLAILHI GGVYVPLDTS LPEARHQSLA SNCTPSLIIS HAATRERAHK
LSAVISAPGH EPARELTLDD LSPDETGYMA PLNAEPNAPA ILLYTSGSTG TPKGVLLTQA
NFGNHIALKT DILGLQRGEC VLQQSSLGFD MSLVQVFCAL ANGGCLVIVP QDVRRDPMEL
TSLMAQHKVS LTIATPSEYL AWLQYGSDAL AQATSWKHLC MGGEPIPQLL KDELRRRLER
KDLVVVSNCY GPTETTAAIS FQSIALDSQD SHEQLPGESE LANYAVGKAL PNYSIRIRDP
AGGAWLPVNH TGEIVIGGAG VALGYLDMPE ETRARFLQTP GEEDGMLLYR TGDKGRLLSD
GTLLCFGRIT GDNQVKLRGL RIELGEVEAA LLQASQGLIH TAVVSRRGDV LVAHCARSHE
SSRETTGGGG EQQDAATAIL RRVSELLPQY SVPAAIALLP SLPTNANGKL DRTAIAALPL
SPQDEAAAAT SPSNDNNNNN TPSGGGGEKM TVRQGELRLL WERVLPRDAT TTTTTNSVRI
TPESDFFLRG GNSLLLMKLQ AAIRESMGVR VSTKALYQAS TLSGMARCVA EQRSDDDEAE
EDIDWAAEVA VPPSMLAQIE KLQHSSASSS SSSSSSSAGS SSTQRPRKTS GLQILLTGAT
GFLGGQLLER LVQSPRVSTV HCVAVPVDEQ SLLEPFLQQQ ADGTRRKVRC YIGNLAAPAL
GLTAADQTAL SQTADVIVHA GSMGHCLNTY ATLSAPNFAS TRHLCALALS RSPPIPLAFA
SSNRVALLTG STAPPPGSAA AFPPPPGAQG FTASKWASEA FLEKLTASMS DVSKTKTKTT
TTVMPWRVSI HRPCALISDR APNSDALNAI LRYSTSMRCV PSLPEHRAEG YLDFGQVDKV
VEEMVGDILG LADERPQEGP AVVYRHHSGG VKVPIHEFRE HMESVYGGRF ESVQLGQWII
RAVDAGMDPL ISAYLETFLE GDASMVFPYM GEQAV
