ACE1_MAGO7
ID ACE1_MAGO7 Reviewed; 4034 AA.
AC G4MVZ2;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Polyketide synthase-nonribosomal peptide synthetase ACE1 {ECO:0000303|PubMed:18433432};
DE Short=PKS-NRPS ACE1 {ECO:0000303|PubMed:18433432};
DE EC=2.3.1.- {ECO:0000269|PubMed:29142718};
DE EC=6.3.2.- {ECO:0000269|PubMed:29142718};
DE AltName: Full=ACE1 cytochalasan biosynthesis cluster protein ACE1 {ECO:0000303|PubMed:29142718};
DE AltName: Full=Avirulence conferring enzyme {ECO:0000303|PubMed:12838393};
GN Name=ACE1 {ECO:0000303|PubMed:12838393};
GN Synonyms=Pi33 {ECO:0000303|PubMed:12838393}; ORFNames=MGG_12447;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=12838393; DOI=10.1007/s00122-003-1349-2;
RA Berruyer R., Adreit H., Milazzo J., Gaillard S., Berger A., Dioh W.,
RA Lebrun M.H., Tharreau D.;
RT "Identification and fine mapping of Pi33, the rice resistance gene
RT corresponding to the Magnaporthe grisea avirulence gene ACE1.";
RL Theor. Appl. Genet. 107:1139-1147(2003).
RN [3]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF
RP CYS-183.
RX PubMed=15319478; DOI=10.1105/tpc.104.022715;
RA Boehnert H.U., Fudal I., Dioh W., Tharreau D., Notteghem J.L., Lebrun M.H.;
RT "A putative polyketide synthase/peptide synthetase from Magnaporthe grisea
RT signals pathogen attack to resistant rice.";
RL Plant Cell 16:2499-2513(2004).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=17142568; DOI=10.1128/ec.00330-05;
RA Fudal I., Collemare J., Boehnert H.U., Melayah D., Lebrun M.H.;
RT "Expression of Magnaporthe grisea avirulence gene ACE1 is connected to the
RT initiation of appressorium-mediated penetration.";
RL Eukaryot. Cell 6:546-554(2007).
RN [5]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=18433432; DOI=10.1111/j.1469-8137.2008.02459.x;
RA Collemare J., Pianfetti M., Houlle A.E., Morin D., Camborde L., Gagey M.J.,
RA Barbisan C., Fudal I., Lebrun M.H., Boehnert H.U.;
RT "Magnaporthe grisea avirulence gene ACE1 belongs to an infection-specific
RT gene cluster involved in secondary metabolism.";
RL New Phytol. 179:196-208(2008).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=29142718; DOI=10.1039/c4sc03707c;
RA Song Z., Bakeer W., Marshall J.W., Yakasai A.A., Khalid R.M., Collemare J.,
RA Skellam E., Tharreau D., Lebrun M.H., Lazarus C.M., Bailey A.M.,
RA Simpson T.J., Cox R.J.;
RT "Heterologous expression of the avirulence gene ACE1 from the fungal rice
RT pathogen Magnaporthe oryzae.";
RL Chem. Sci. 6:4837-4845(2015).
RN [7]
RP FUNCTION.
RX PubMed=31644300; DOI=10.1021/acs.orglett.9b03372;
RA Wang C., Becker K., Pfuetze S., Kuhnert E., Stadler M., Cox R.J.,
RA Skellam E.;
RT "Investigating the function of cryptic cytochalasan cytochrome P450
RT monooxygenases using combinatorial biosynthesis.";
RL Org. Lett. 21:8756-8760(2019).
CC -!- FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that
CC mediates the biosynthesis of a tyrosine-derived cytochalasan acting as
CC a fungal signal recognized by resistant rice plants and leads to
CC avirulence in Pi33 resistant rice cultivars (PubMed:12838393,
CC PubMed:15319478, PubMed:17142568, PubMed:18433432, PubMed:29142718).
CC The first step in the pathway is catalyzed by the hybrid PKS-NRPS ACE1,
CC assisted by the enoyl reductase RAP1, that are responsible for fusion
CC of the tyrosine precursor and the polyketide backbone
CC (PubMed:29142718). The polyketide synthase module (PKS) of ACE1 is
CC responsible for the synthesis of the polyketide backbone and the
CC downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl
CC end of the polyketide with the tyrosine precursor (PubMed:29142718).
CC Because ACE1 lacks a designated enoylreductase (ER) domain, the
CC required activity is provided the enoyl reductase RAP1
CC (PubMed:29142718). Reduction by the hydrolyase ORFZ, followed by
CC dehydration and intra-molecular Diels-Alder cyclization by the Diels-
CC Alderase ORF3 then yield the required isoindolone-fused macrocycle
CC (Probable). A number of oxidative steps catalyzed by the tailoring
CC enymes identified within the cluster, including cytochrome P450
CC monooxygenases CYP1 to CYP4, the FAD-linked oxidoreductase OXR2 and the
CC short-chain dehydrogenase/reductase OXR1, are further required to
CC afford the final cytochalasans that confer avirulence and which have
CC still to be identified (Probable). The monooxygenase CYP1 has been
CC shown to be a site-selective C-18 hydroxylase whereas the function of
CC CYP3 is the site-selective epoxidation of the C-6/C-7 olefin that is
CC present in some intermediate compounds (PubMed:31644300). Finally, SYN2
CC and RAP2 are not required for avirulence in Pi33 resistant rice
CC cultivars (PubMed:18433432). {ECO:0000269|PubMed:12838393,
CC ECO:0000269|PubMed:15319478, ECO:0000269|PubMed:17142568,
CC ECO:0000269|PubMed:18433432, ECO:0000269|PubMed:29142718,
CC ECO:0000269|PubMed:31644300, ECO:0000305|PubMed:18433432,
CC ECO:0000305|PubMed:29142718}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:29142718}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15319478}.
CC Note=Localizes in the cytoplasm of the appressorium.
CC {ECO:0000269|PubMed:15319478}.
CC -!- INDUCTION: Expressed exclusively during fungal penetration of host
CC leaves, the time point at which plant defense reactions are triggered.
CC {ECO:0000269|PubMed:15319478, ECO:0000269|PubMed:17142568,
CC ECO:0000269|PubMed:18433432}.
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. Occasionally,
CC epimerase (E) domains (responsible for L- to D- amino acid conversion)
CC are present within the NRP synthetase. CcsA contains also a polyketide
CC synthase module (PKS) consisting of several catalytic domains including
CC a ketoacyl synthase domain (KS), an acyl transferase domain (AT), a
CC dehydratase domain (DH), a methyltransferase domain (MT), and a
CC ketoreductase domain (KR). Instead of a thioesterase domain (TE), ACE1
CC finishes with a reductase-like domain (R) for peptide release. ACE1 has
CC the following architecture: KS-AT-DH-MT-KR-PCP-C-A-T-R.
CC {ECO:0000250|UniProtKB:Q4WAZ9, ECO:0000305|PubMed:15319478}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; CM001232; EHA55860.1; -; Genomic_DNA.
DR RefSeq; XP_003715667.1; XM_003715619.1.
DR SMR; G4MVZ2; -.
DR STRING; 318829.MGG_12447T0; -.
DR EnsemblFungi; MGG_12447T0; MGG_12447T0; MGG_12447.
DR GeneID; 5051040; -.
DR KEGG; mgr:MGG_12447; -.
DR VEuPathDB; FungiDB:MGG_12447; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_48_0_1; -.
DR InParanoid; G4MVZ2; -.
DR OMA; VAQFGSH; -.
DR OrthoDB; 19161at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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:0006633; P:fatty acid biosynthetic process; 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; -; 1.
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; 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; IPR018201; Ketoacyl_synth_AS.
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; 1.
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 PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Isomerase; Ligase; Methyltransferase;
KW Multifunctional enzyme; NADP; Oxidoreductase; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..4034
FT /note="Polyketide synthase-nonribosomal peptide synthetase
FT ACE1"
FT /id="PRO_0000449440"
FT DOMAIN 2424..2505
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3598..3678
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 13..451
FT /note="Ketoacyl synthase (KS) domain"
FT /evidence="ECO:0000250|UniProtKB:A1CLY8, ECO:0000255"
FT REGION 560..879
FT /note="Acyl transferase"
FT /evidence="ECO:0000250|UniProtKB:A1CLY8, ECO:0000255"
FT REGION 952..1252
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000250|UniProtKB:A1CLY8, ECO:0000255"
FT REGION 1396..1594
FT /note="Methyltransferase (MT) domain"
FT /evidence="ECO:0000250|UniProtKB:A1CLY8, ECO:0000255"
FT REGION 2144..2317
FT /note="Ketoreductase (KR)domain"
FT /evidence="ECO:0000250|UniProtKB:A1CLY8, ECO:0000255"
FT REGION 2512..2598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2608..3037
FT /note="Condensation"
FT /evidence="ECO:0000250|UniProtKB:A1CLY8, ECO:0000255"
FT REGION 3073..3473
FT /note="Adenylation"
FT /evidence="ECO:0000250|UniProtKB:A1CLY8, ECO:0000255"
FT REGION 3719..3944
FT /note="Reductase-like"
FT /evidence="ECO:0000250|UniProtKB:A1CLY8, ECO:0000255"
FT COMPBIAS 2529..2553
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2556..2598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /note="For ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2465
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3638
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MUTAGEN 183
FT /note="C->A: Abolishes recognition of the fungus by
FT resistant rice plants."
FT /evidence="ECO:0000269|PubMed:15319478"
SQ SEQUENCE 4034 AA; 438007 MW; 69EC2A696A287412 CRC64;
MRDEMWNTAT EPIAIIGSGC KFPGGSTTPS KLWELLKDPK DIVSEIRPDR FDVDKYFHPD
HKHHGTSNVR HSYFLEENFK HFDAKFFGIR PQEAMAMDPQ QRFLLETVYE SLEAAGITIS
DLKGSQAGVF VGNMGVDYSE LLSQDIDAFP TYFAPGTARS ILSNRISYFF DLHGPSVTVD
TACSSSLVAV HQAVQSLRLG ETPVAIVCGA NLLLGPAQYI AESKLQMLSP NGRSRMWDAS
ADGYARGEGF ASIVLKPLSV ALANGDHIEC IIRETGCNQD GRTKGITMPS PLAQCKLIQE
TYKRAGLDLS KSSDRPQYFE AHGTGTPAGD PVEAEAISTA FFGPESGFRR TSHDPKLYVG
SVKTVIGHTE GTAGLAGLIK ASLAMKAKSI PPNLHLERVN PAVQPFYGNL EIPTRLMDWP
EPAPGQPLRA SVNSFGFGGA NAHVILESYT PAAEVAMVTP TAAAGPVFSP FVFSASSDKA
LASMLSAYSD YLSLNPTVDL RSVAYTLSQH RSVFDKRAAI SAPDLDTLKT KLKARSEEAS
PSGKTAAVQS LERRPRYLGV FTGQGAQWAR MGVDVINASP AARAIFEDLE QSLKTLPEED
RPSWSMLEEL LAPPETSRVY QANISQTVCT AVQVMMVQLL RAAGIEFSCV VGHSSGEMAA
AYTAGYLSAR DAVRAAYFRG VHSQLAKGSN GQPGGMIAVG TNFEDAEELC ELDDFKGRLC
VAASNSAELV TLSGDLDAVQ EVKKILDAEE KFNKQLQVDK GYHSHHMLPC SEPYVASLQK
CGIQAQVPGD ATACRWISSV YVDDMTNLDC RVQDRYWIEN LAKPVMFSQA LSHALGGDDK
FDSVIEVGPH PALKGPASQT IQACLGERLP YFGCLSRGTD SNEAFAEFLG GVWSTFGSSA
VDLAAYERFA TGGCDQRLVK GLPSYTWDHD VEHYFQSRLS KVVLHRSTPP NELLGTRLPD
DTAGEVRWRN SLHPGELPWL LQHSAQGQTV FPGTGYIATT LEAVKQLFDS SGVQTVEIRD
MVIGNALVIE ANTGVETLFS LTFINTQTDR ITAHFSFCSQ QGGSTKLVEN ASGDLVVLLG
EPSEDALPRS FHPGTQMKDI DEERFYEAID KLGYGYEGPF RALSQLQRRM GAATGLVAIP
EKTKHFDQMV LHPAALDAMV QTVLLAYCYP GDTRLQGISL PTGIDCIRFN YGMLSEAARP
GCQLPFLSCT AFEGDDVLGG VGGDVGGDVD VFSEDKRFAL IQLQGLHTKP LSPPSAATDL
QIFSEMEWKT ASPEGADMEV RGEKRAYVAD LYSSMERVAY FYMRHVDREI GKDRSGLAPH
QVRFLEWVDH MCGRVEAGTL PHISRKWDHD TRQDILKIIA KYPDSIDLEL MHAVGENLCS
VFRGEMNALE PMVKKNMLNR FYSDALGMSP YTEDLARMVG HITHRYPHMN ILEVGAGTGG
ATKVMLRRLQ DAFASYTYTD ISSGFFADAR QVFKAHESKM LFKTLDIEKD IVDQGYEENS
FDLVIANLVV HATADLDATM GRLRRLVKPG GHLVLLEITT NDPLRFGFIF GPLPGWWLGG
EDGRVHSPCV DVEWWDRVMK RNGFSGADIV TPHHTLGPLS VIMTQAVDHR VQLLRQPTSA
DFGDFTIDPE RLTIVGGVKP LAEGLEQLLK PRYQSVAWIP TLEEVSSHSL PVMGSVLSLV
ELDEPLFKDM TAQTLEGFKF VFQQSRSVYW ITCGASGANP YSNMAAGVAR TVALEMRHLR
LGFLDFEDAK DATVQRLADR FLEFEILGTL EQQGKLDHLT WYQEPELRFD GKNLLVPRMK
LSKDRNGRYN SRRRQLTKNV NPREVPVSLV PTTSGKDFVL KESLSSSSTK HGAQDTVSLR
VHYASQRSLR LESSDYLFLV LGTNLSSGEA MFALADSNRS IVHVDRQWTT SYLGNLDHGR
HALADLYTQI MASTVVAGLS AGDSLVVLDA ETPLSQALSA RCAAKGVRLT LLSTTTATSH
SEADGTNKTN VRIHPLESRR SIESKLPSNA TCFLDLSTNN GSEAAAVINS YIPAQCRVET
RDTLTATACQ VTRSTSTGGL GPAVGDVLPA CWANVEAAGR DLSFFSAAVV TPTELTAAAG
NGKTSAPRVG DDALLLITDW TAEAEVGVLV QPADSMVRFR QDKTYWLVGL TGGLALSLCR
WMVNRGARYV VMTSRNPKID KEWLQGVESC GATVKIFSND VTDRAAVNSA YRTISATLPP
IAGVVQGAMV LRDTMFAETT METIESILGP KVRGSIYLDE IFYSTPLDFF VFLSSVTATS
GNPGQSIYAG ANMFMNSLAA QRRKRGVAGS SVEIGCIMGN GSVTTILSYE HQKYLFSVGN
TWLAEQDFLT MFGEAVLASP PDAPDSVTSV TGLRLQFNDD KPDITWFSNP IFQHLVLQSG
NAMQTSLSVA RQGTPVKSLL QEAKSSEEVL DILKDAFTAK LVSSLQADPD SNLLEVDLET
LGMDSLVAVD LRSWFLAELS VDVPVLKILN GSTARLLLEF VQGLIPASMT PKLDGSDGAD
AAAQEAPPVA PPVTKPKPDV SVKVPPPHQP VASLKPSGPA SPTSPSSATA SPGRSRSVAS
PVTADTPVSP TTSASMASLN DSRKLIRTVP VSFGQSRFWF LGSYNPDPLA FNITSLMRIS
GPLRTNDFGK AVDKVLNHHE ALRTSFVSEN DAPVQKIWSS PAFALEQRKI ADDESEVVKA
YTEVQNTRYN LEAGQTMRIM LLTKSPTKHV LVLGYHHINM DGVSFEVLFS DIEKAYNRTP
LDRSVMQFPD FTIREAGEYK SGAWRSELQY WQSKFTSLPE PTPLLSVSKR RTRPVNLSYT
THSVSRRINA EQSQAIHTVG RKFKATPFHF YLSVFKTLIA RFSGADDFCI GIADANRKED
KVMGAVGLYL NLLPLRVRSA LGQTFGETLA DMKKVSQEAF ANSKVPFDVL LNELSVPRSS
SQTPLFQTFV NYRRGVSEER SFCGCTGAGE LISGGQIGYD ISLDIVENPG GDALVTLSVQ
KDLYNVDMAN LLLDSYFRLV DSFAKNPATS LNRPAIYDPV AVDKALTLGC GPTLEDSSWP
ETLIHRIENM SVKYATKFAL RNGQNGGLTY SQMIARINDI AAKLIDAKVG TGIVGVMQAS
TMDFICSILA VWKAGAIYTP LDPRLNSTDR LKAVVDECQP ACILVDATTK PLFDSLATNA
VQIDVSMVQS SKTLEASPKV AIHAKAPSAA AVFYTSGSTG VPKGITLSHA SLTYNIMAAT
RQFGFKEGVD IMLQQSSFSF DMALAQMLTS LSNGGTLVVV PSHLRGDALG LSQLIVAENV
SIVQASPTEY KSLIGVNAQH LKTSKWRVAL SGGENMTQSL LEVFRSLGKP DLVLFNGYGP
TEATINANTR IVPYHEPNSN PDLPLLTWPN YSISIVDLEL NPVPVGVFGE VCIGGAGVGL
GYFKNDELTA KAFVADKTAP AEFVAKGWKT KFRTGDLGRL SPDGGLIIEG RIDGDTQVKL
RGMRIDLKNI ESAILQAGAG KIIDAAVSVR RGGADESEPQ YLVGHVVLDA DQTPEDSQQD
FLAQLIPRLR LPRHMKPSLL VPIRALPQTA SHKLDRRALQ QLPISDAGQI AKQSQQGAEL
GSDQARMWKL WKQVIPRDVV SQYSITPQSD FFHVGGTSLL LVNLQSLIAR EHGRAPPLHA
MFESSTVAAM TDLVLSDDAS GSTALIDWEQ ETSIPTLPPH IIPGGAGNKV SVPPRVVLLT
GATGFLGRQL MAFLLRQPSV KRIHCLAVRG GAPPSSAAPF SDPRVSIHAG DLNAPHLGLG
EAVAELLFAQ ADVIIHNGAD VSFLKTYATL RATNVGSTRE LARLAAPRRI PFHFVSSASI
TQLTGLDEFG EASMAAWAPP ADPRGMSGGY AAAKWASEVL LEKAARAWGL PVVIHRPSSI
TGEGTNSLDL MGNMFKYIEQ LEAVPESDSW KGNFDFVSVE NVAADIVQAV VAANVVAAGG
VKFIYEAGDI VYPLSMVKDM SEGGAKLPVK TMPLAKWVEK AAEKGLDSML AEYLIKAAST
GTSLAFPRLL KDGN
