PKSA_DOTSN
ID PKSA_DOTSN Reviewed; 2399 AA.
AC M2XHZ5;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Norsolorinic acid synthase {ECO:0000250|UniProtKB:Q12053};
DE Short=NSAS {ECO:0000250|UniProtKB:Q12053};
DE EC=2.3.1.221 {ECO:0000250|UniProtKB:Q12053};
DE AltName: Full=Dothistromin biosynthesis polyketide synthase {ECO:0000303|PubMed:16649078};
DE AltName: Full=Polyketide synthase A {ECO:0000303|PubMed:16649078};
GN Name=pksA {ECO:0000303|PubMed:16649078}; ORFNames=DOTSEDRAFT_192192;
OS Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS fungus) (Mycosphaerella pini).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX NCBI_TaxID=675120;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990;
RX PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT but also signatures of common ancestry.";
RL PLoS Genet. 8:E1003088-E1003088(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990;
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [3]
RP FUNCTION.
RX PubMed=12039746; DOI=10.1128/aem.68.6.2885-2892.2002;
RA Bradshaw R.E., Bhatnagar D., Ganley R.J., Gillman C.J., Monahan B.J.,
RA Seconi J.M.;
RT "Dothistroma pini, a forest pathogen, contains homologs of aflatoxin
RT biosynthetic pathway genes.";
RL Appl. Environ. Microbiol. 68:2885-2892(2002).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16649078; DOI=10.1007/s11046-006-0240-5;
RA Bradshaw R.E., Jin H., Morgan B.S., Schwelm A., Teddy O.R., Young C.A.,
RA Zhang S.;
RT "A polyketide synthase gene required for biosynthesis of the aflatoxin-like
RT toxin, dothistromin.";
RL Mycopathologia 161:283-294(2006).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=17683963; DOI=10.1016/j.fgb.2007.06.005;
RA Zhang S., Schwelm A., Jin H., Collins L.J., Bradshaw R.E.;
RT "A fragmented aflatoxin-like gene cluster in the forest pathogen
RT Dothistroma septosporum.";
RL Fungal Genet. Biol. 44:1342-1354(2007).
RN [6]
RP INDUCTION.
RX PubMed=18262779; DOI=10.1016/j.mycres.2007.03.018;
RA Schwelm A., Barron N.J., Zhang S., Bradshaw R.E.;
RT "Early expression of aflatoxin-like dothistromin genes in the forest
RT pathogen Dothistroma septosporum.";
RL Mycol. Res. 112:138-146(2008).
RN [7]
RP REVIEW ON FUNCTION, AND PATHWAY.
RX PubMed=22069571; DOI=10.3390/toxins2112680;
RA Schwelm A., Bradshaw R.E.;
RT "Genetics of dothistromin biosynthesis of Dothistroma septosporum: an
RT update.";
RL Toxins 2:2680-2698(2010).
RN [8]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=23207690; DOI=10.1016/j.fgb.2012.11.006;
RA Chettri P., Ehrlich K.C., Cary J.W., Collemare J., Cox M.P.,
RA Griffiths S.A., Olson M.A., de Wit P.J., Bradshaw R.E.;
RT "Dothistromin genes at multiple separate loci are regulated by AflR.";
RL Fungal Genet. Biol. 51:12-20(2013).
RN [9]
RP FUNCTION.
RX PubMed=23448391; DOI=10.1111/nph.12161;
RA Bradshaw R.E., Slot J.C., Moore G.G., Chettri P., de Wit P.J.,
RA Ehrlich K.C., Ganley A.R., Olson M.A., Rokas A., Carbone I., Cox M.P.;
RT "Fragmentation of an aflatoxin-like gene cluster in a forest pathogen.";
RL New Phytol. 198:525-535(2013).
RN [10]
RP INDUCTION.
RX PubMed=25986547; DOI=10.1016/j.funbio.2015.01.007;
RA Chettri P., Ehrlich K.C., Bradshaw R.E.;
RT "Regulation of the aflatoxin-like toxin dothistromin by AflJ.";
RL Fungal Biol. 119:503-508(2015).
RN [11]
RP INDUCTION.
RX PubMed=31053329; DOI=10.1016/j.funbio.2019.02.006;
RA Ozturk I.K., Dupont P.Y., Chettri P., McDougal R., Boehl O.J., Cox R.J.,
RA Bradshaw R.E.;
RT "Evolutionary relics dominate the small number of secondary metabolism
RT genes in the hemibiotrophic fungus Dothistroma septosporum.";
RL Fungal Biol. 123:397-407(2019).
CC -!- FUNCTION: Polyketide synthase; part of the fragmented gene cluster that
CC mediates the biosynthesis of dothistromin (DOTH), a polyketide toxin
CC very similar in structure to the aflatoxin precursor, versicolorin B
CC (PubMed:12039746, PubMed:17683963, PubMed:22069571, PubMed:23207690,
CC PubMed:23448391). The first step of the pathway is the conversion of
CC acetate to norsolorinic acid (NOR) and requires the fatty acid synthase
CC subunits hexA and hexB, as well as the polyketide synthase pksA
CC (PubMed:16649078, PubMed:23207690). PksA combines a hexanoyl starter
CC unit and 7 malonyl-CoA extender units to synthesize the precursor NOR
CC (By similarity). The hexanoyl starter unit is provided to the acyl-
CC carrier protein (ACP) domain by the fungal fatty acid synthase
CC hexA/hexB (By similarity). The second step is the conversion of NOR to
CC averantin (AVN) and requires the norsolorinic acid ketoreductase nor1,
CC which catalyzes the dehydration of norsolorinic acid to form (1'S)-
CC averantin (PubMed:23207690). The cytochrome P450 monooxygenase avnA
CC then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN)
CC (PubMed:23207690). The next step is performed by adhA that transforms
CC HAVN to averufin (AVF) (PubMed:23207690). Averufin might then be
CC converted to hydroxyversicolorone by cypX and avfA (PubMed:23207690).
CC Hydroxyversicolorone is further converted versiconal hemiacetal acetate
CC (VHA) by moxY (PubMed:23207690). VHA is then the substrate for the
CC versiconal hemiacetal acetate esterase est1 to yield versiconal (VAL)
CC (PubMed:23207690). Versicolorin B synthase vbsA then converts VAL to
CC versicolorin B (VERB) by closing the bisfuran ring (PubMed:16649078,
CC PubMed:23207690). Then, the activity of the versicolorin B desaturase
CC verB leads to versicolorin A (VERA) (PubMed:23207690). DotB, a
CC predicted chloroperoxidase, may perform epoxidation of the A-ring of
CC VERA (PubMed:23207690). Alternatively, a cytochrome P450, such as cypX
CC or avnA could catalyze this step (PubMed:23207690). It is also possible
CC that another, uncharacterized, cytochrome P450 enzyme is responsible
CC for this step (PubMed:23207690). Opening of the epoxide could
CC potentially be achieved by the epoxide hydrolase epoA
CC (PubMed:23207690). However, epoA seems not to be required for DOTH
CC biosynthesis, but other epoxide hydrolases may have the ability to
CC complement this hydrolysis (PubMed:23207690). Alternatively, opening of
CC the epoxide ring could be achieved non-enzymatically (PubMed:23207690).
CC The next step is the deoxygenation of ring A to yield the 5,8-
CC dihydroxyanthraquinone which is most likely catalyzed by the NADPH
CC dehydrogenase encoded by ver1 (PubMed:23207690). The last stages of
CC DOTH biosynthesis are proposed to involve hydroxylation of the bisfuran
CC (PubMed:23207690). OrdB and norB might have oxidative roles here
CC (PubMed:23207690). An alternative possibility is that cytochrome P450
CC monoogenases such as avnA and cypX might perform these steps in
CC addition to previously proposed steps (PubMed:23207690).
CC {ECO:0000250|UniProtKB:Q12053, ECO:0000269|PubMed:12039746,
CC ECO:0000269|PubMed:16649078, ECO:0000303|PubMed:22069571,
CC ECO:0000305|PubMed:17683963, ECO:0000305|PubMed:23207690,
CC ECO:0000305|PubMed:23448391}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6 H(+) + hexanoyl-[ACP] + 7 malonyl-CoA = 7 CO2 + 7 CoA + 2
CC H2O + holo-[ACP] + noranthrone; Xref=Rhea:RHEA:35179, Rhea:RHEA-
CC COMP:9632, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:77904, ChEBI:CHEBI:78459;
CC EC=2.3.1.221; Evidence={ECO:0000250|UniProtKB:Q12053};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250|UniProtKB:Q12053};
CC Note=Binds 1 phosphopantetheine covalently.
CC {ECO:0000250|UniProtKB:Q12053};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000303|PubMed:22069571,
CC ECO:0000305|PubMed:23207690}.
CC -!- INDUCTION: Shows highest expression in the mid and late stages of
CC infection in planta (PubMed:31053329). Expression is positively
CC regulated by the dothistromin-specific transcription factors aflR and
CC aflJ (PubMed:23207690, PubMed:25986547). Dothistromin biosynthetic
CC proteins are co-regulated, showing a high level of expression at ealy
CC exponential phase with a subsequent decline in older cultures
CC (PubMed:17683963, PubMed:18262779). {ECO:0000269|PubMed:17683963,
CC ECO:0000269|PubMed:18262779, ECO:0000269|PubMed:23207690,
CC ECO:0000269|PubMed:25986547, ECO:0000269|PubMed:31053329}.
CC -!- DOMAIN: The domain architecture includes starter unit:ACP transacylase
CC (SAT), beta-ketoacyl synthase (KS), malonyl-CoA:ACP transacylase (MAT),
CC product template (PT), 3 acyl-carrier domain (ACP), and
CC thioesterase/Claisen cyclase (TE/CLC) domains (PubMed:16649078).
CC Although duplicated ACP domains are common, pksA is the only fungal PKS
CC containing 3 ACP domains (PubMed:16649078). The third (C-terminal) ACP
CC is less similar in sequence to the first two and to that of the
CC aflatoxin biosynthetic enzyme aflC (PubMed:16649078). It is possible
CC that the third ACP domain was acquired by unequal recombination and has
CC since diverged into a slightly different form that may have less
CC functionality or altered specificity (PubMed:16649078).
CC {ECO:0000305|PubMed:16649078}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of dothistromin but still
CC enables the conversion of exogenous aflatoxin precursors, including
CC norsolorinic acid, into dothistromin (PubMed:16649078).
CC {ECO:0000269|PubMed:16649078}.
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DR EMBL; KB446546; EME39092.1; -; Genomic_DNA.
DR AlphaFoldDB; M2XHZ5; -.
DR SMR; M2XHZ5; -.
DR STRING; 675120.M2XHZ5; -.
DR EnsemblFungi; EME39092; EME39092; DOTSEDRAFT_192192.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_0_1; -.
DR OMA; KWGCWLD; -.
DR OrthoDB; 68112at2759; -.
DR Proteomes; UP000016933; Unassembled WGS sequence.
DR GO; GO:0102973; F:norsolorinate anthrone synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.1200.10; -; 3.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 3.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 3.
DR SUPFAM; SSF47336; SSF47336; 3.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR PROSITE; PS50075; CARRIER; 3.
PE 2: Evidence at transcript level;
KW Acyltransferase; Multifunctional enzyme; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Repeat; Transferase.
FT CHAIN 1..2399
FT /note="Norsolorinic acid synthase"
FT /id="PRO_0000443455"
FT DOMAIN 1733..1812
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1877..1953
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2020..2099
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 10..247
FT /note="Starter unit:ACP transacylase (SAT) domain"
FT /evidence="ECO:0000255"
FT REGION 375..808
FT /note="Ketoacyl synthase (KS)domain"
FT /evidence="ECO:0000250|UniProtKB:Q12053, ECO:0000255"
FT REGION 905..1192
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000250|UniProtKB:Q12053, ECO:0000255"
FT REGION 1307..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1353..1658
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1665..1734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2098..2149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2164..2393
FT /note="Thioesterase/Claisen cyclase (TE/CLC) domain"
FT /evidence="ECO:0000255"
FT COMPBIAS 1711..1726
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2098..2122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 544
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 995
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 2234
FT /note="For thioesterase activity"
FT /evidence="ECO:0000250|UniProtKB:Q12053"
FT MOD_RES 1770
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1911
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2057
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2399 AA; 259252 MW; C82F86A242F2AFE4 CRC64;
MTHSNATRVL VFGDQTYDFV PKLRELFHVK DNPILTAFLE QSHYVVRAQM IQTLPPAEHK
AARTFDLADM LKKYVAGKLN PAFQTALSCI TQLGVFMREF HDFTKPYPRH DSSYVLGICT
GSLAAAAVSS SNSLSELLPI AVQTALIAFR LGLCVTDMRD RLESSEEDRT QPWSVVLFDT
DEQTVTKAIK DFCTSNVLPK TKQPWITSAS SKTITISGAP RVLKKLSQEP ALKDKKTRQI
PIYVPAHNSA LFTPEDVKSI LETTPVDTWS NYPTKLPFIS SVSGKMAWAD NYLAVIHLAL
NQCLLESIGW GKVETELPRL LKSRGAENVL ITPITTSADR ALSAALSPTI SNIEVEKPTI
NESFAHRPGS GKSKLAIVSM SGRFPEAQST DAFWDLLYKG LDVVKEVPKR RWDVETHVDP
TGRARNKGAT KWGCWLDFAG EFDPRFFSIS PKEAPQMDPA QRMALMSTWE AMERGGIVPD
TTPSTQRNRI GVFHGVTSND WMETNTAQNI DTYFITGGNR GFIPGRINFC FEFSGPSFTN
DTACSSSLAA IHLACNSLWR GDCDTAVAGG TNMIFTPDGH AGLDKGFFLS RTGNCKPFDD
KADGYCRAEG VGTVMVKRLE DALADGDPIL GTILDAKTNH SAMSDSMTRP FVPAQIDNME
ACLSTAGVDP TSLDYIEMHG TGTQVGDAVE MESVLSVFAP NEQFRGKDQP LYVGSAKANI
GHGEGVSGVT SLIKVLLMMQ NNTIPPHCGI KPGSKINHNY PDLAARNVHI AFEPKPFLRR
EGKLRRVLIN NFSAAGGNTA LLIEDAPDRM PLSGQDPRTT QTVTISGHVG KSLSNNVANL
LAHLKKNPTI DLSQLAYTVS ARRWHHLHRV AVAGTTVADI TAKLEKAIEN KEGVNRPKAK
PSVFFAFTGQ GSQYLGMGKQ LYDSYPMFRS ELQGYDRLAQ SQGFPSFAHI FTETKGDVEQ
NLPVVVQLAI TCLQMALFNL VTSFGIKASA VVGHSLGEYA ALYAAGVLSA SDTIYLVGKR
AELLQDHCQR GTHAMLACKA SEWSLAEITA GKNVEVACVN GPEDTVLSGT VEEIGEVQKT
LSAKSIKATL LKLPFAFHSA QVQPILEDFE ELAAGATFEK PKLAVISPLL GSVVEDEGVV
GPNYLARHCR EAVGMVKALG VAKEKGIINE KTIVIEIGPK PLLCGMIKNI LGQNIVALPT
LKDKGPDVWQ NLSNIFTTLY TGGLDINWTA FHAPFEPAKK VLQLPDYGWD LKDYFIQYEG
DWVLHRHKIH CNCADAGKDV HNTSHYCPGK HTFAENVVVP GGAQKAVQEA PAAKTETKKM
SKLDPTKEAY PGIPLTTTVH KVIEEKTEPL GAQFTVETDI SRKDVNSIAQ GHTVDSIPLC
TPSFYADIAL QVGKYAMDRI RAGHPGAGAI DGRVDVTDLV VDKALIPHGK APQLLRTNVT
MSWPPKMAAT TRSAKVTFKT YTADGKLDTD HAYCTVRFTT DSQQKSLQKK VPEYKAAIAK
LRARDAKGEL THYNTKSGYK LMSSMAHFHP DYKLLDNLVL NEAENEAVSV MNFSSCTDAG
IYAAHPAYVD AITQVGGFAM NAKDDTDIDK EVYVNHGWES FQVYKKMEKS VEYVVYSKMT
KDPKGDMVHG DTIVLDGDEV VAFFRGLSLR SVPRKALRAV LQSAMDKGIR QRGGKPGAAK
GAVAAPAPAK KMVEPVKAAS KKETPAAAAP PSPSKAAPPP APKPAALKAS VPKADPGKVD
EALKIISEES GIALDELTDD SNFTDMGVDS LSSMVITSRL REDLELDLAP DFALFADCPT
VASLRTFLAG AAGGPTDSPA AIATLEFGEP TPAKELEAGP ALKSTPISPG VQALQPVPAP
TPAPKPVITS PAAPVSSKVF DDALQIISEE SGIALDELTD DSNFTDMGVD SLSSMVITSR
LREDLELDLS PDWALFADCP TVASLRSFLG GSGPGSTAPA DADTPVDTTA AEIEAPVPNE
AASYMPNSSQ ADVDDAVAAV IGNDPPRRPE PPKQAAAPAV ARTEALNAAL DIIAEESGVA
AEDFTDDTIF SDIGIDSLCS MVISSRFREE LELDLDSQFS LFVDLPTVAQ LREFLTGSSA
DSDSSSVASN PADPAATPPR SESSDTEPDD EAPSKPKSGP GSTDSCRSTN SVILQGKPKT
AAKTLFLLPD GGGSASSYSV IPKLQSDVAV VGINCPYARD PENMTCTWQA MMQSFINEIK
RRQPKGPYHL GGWSSGGAFA YVTAEKMIKQ GDEVGSLFIF DAPVPQVMEK LPREFYEAVN
FTESTAVGTA EPPPYLIPHF MAVVDVMLDY KCKPLQTKKM PNVGLIWADS TVMKEDEAPK
MKGMHFMIQK RTNFGPDGWD EVCPGAKFEI VKAVDTNHFT LMTKARVNYV SDLIDKVMG
