AUSA_EMENI
ID AUSA_EMENI Reviewed; 2476 AA.
AC Q5ATJ7; C8VE81;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Non-reducing polyketide synthase ausA {ECO:0000303|PubMed:21658102};
DE EC=2.3.1.- {ECO:0000305|PubMed:21658102, ECO:0000305|PubMed:22329759};
DE AltName: Full=Austinoid biosynthesis clusters protein A {ECO:0000303|PubMed:22329759};
DE AltName: Full=Methylorcinaldehyde synthase ausA {ECO:0000303|PubMed:22329759};
GN Name=ausA {ECO:0000303|PubMed:21658102}; ORFNames=AN8383;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-1660.
RX PubMed=21658102; DOI=10.1111/j.1574-6968.2011.02327.x;
RA Nielsen M.L., Nielsen J.B., Rank C., Klejnstrup M.L., Holm D.K.,
RA Brogaard K.H., Hansen B.G., Frisvad J.C., Larsen T.O., Mortensen U.H.;
RT "A genome-wide polyketide synthase deletion library uncovers novel genetic
RT links to polyketides and meroterpenoids in Aspergillus nidulans.";
RL FEMS Microbiol. Lett. 321:157-166(2011).
RN [4]
RP FUNCTION.
RX PubMed=22234162; DOI=10.1021/cb200455u;
RA Rodriguez-Urra A.B., Jimenez C., Nieto M.I., Rodriguez J., Hayashi H.,
RA Ugalde U.;
RT "Signaling the induction of sporulation involves the interaction of two
RT secondary metabolites in Aspergillus nidulans.";
RL ACS Chem. Biol. 7:599-606(2012).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22329759; DOI=10.1021/ja209809t;
RA Lo H.C., Entwistle R., Guo C.J., Ahuja M., Szewczyk E., Hung J.H.,
RA Chiang Y.M., Oakley B.R., Wang C.C.;
RT "Two separate gene clusters encode the biosynthetic pathway for the
RT meroterpenoids austinol and dehydroaustinol in Aspergillus nidulans.";
RL J. Am. Chem. Soc. 134:4709-4720(2012).
RN [6]
RP FUNCTION.
RX PubMed=23865690; DOI=10.1021/ja405518u;
RA Matsuda Y., Awakawa T., Wakimoto T., Abe I.;
RT "Spiro-ring formation is catalyzed by a multifunctional dioxygenase in
RT austinol biosynthesis.";
RL J. Am. Chem. Soc. 135:10962-10965(2013).
RN [7]
RP DOMAIN, AND MUTAGENESIS OF SER-2251; ASP-2413 AND HIS-2445.
RX PubMed=23368695; DOI=10.1021/ol303328t;
RA Yeh H.H., Chang S.L., Chiang Y.M., Bruno K.S., Oakley B.R., Wu T.K.,
RA Wang C.C.;
RT "Engineering fungal nonreducing polyketide synthase by heterologous
RT expression and domain swapping.";
RL Org. Lett. 15:756-759(2013).
RN [8]
RP FUNCTION.
RX PubMed=29076725; DOI=10.1021/acschembio.7b00814;
RA Mattern D.J., Valiante V., Horn F., Petzke L., Brakhage A.A.;
RT "Rewiring of the austinoid biosynthetic pathway in filamentous fungi.";
RL ACS Chem. Biol. 12:2927-2933(2017).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster A
CC that mediates the biosynthesis of austinol and dehydroaustinol, two
CC fungal meroterpenoids (PubMed:22329759). The first step of the pathway
CC is the synthesis of 3,5-dimethylorsellinic acid by the polyketide
CC synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then
CC prenylated by the polyprenyl transferase ausN (PubMed:22329759).
CC Further epoxidation by the FAD-dependent monooxygenase ausM and
CC cyclization by the probable terpene cyclase ausL lead to the formation
CC of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then
CC oxidized to spiro-lactone preaustinoid A3 by the combined action of the
CC FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE
CC (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement
CC and ring contraction of the tetraketide portion of preaustinoid A3 by
CC ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The
CC aldo-keto reductase ausK, with the help of ausH, is involved in the
CC next step by transforming preaustinoid A4 into isoaustinone which is in
CC turn hydroxylated by the P450 monooxygenase ausI to form austinolide
CC (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG
CC modifies austinolide to austinol (PubMed:22329759). Austinol can be
CC further modified to dehydroaustinol which forms a diffusible complex
CC with diorcinol that initiates conidiation (PubMed:22234162,
CC PubMed:22329759). Due to genetic rearrangements of the clusters and the
CC subsequent loss of some enzymes, the end products of the Emericella
CC nidulans austinoid biosynthesis clusters are austinol and
CC dehydroaustinol, even if additional enzymes, such as the O-
CC acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are
CC still functional (PubMed:29076725). {ECO:0000269|PubMed:22234162,
CC ECO:0000269|PubMed:22329759, ECO:0000269|PubMed:23865690,
CC ECO:0000269|PubMed:29076725}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 3 malonyl-CoA + 2 S-adenosyl-L-methionine = 3,5-
CC dimethylorsellinate + 3 CO2 + 4 CoA + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:49628, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:131856;
CC Evidence={ECO:0000305|PubMed:21658102, ECO:0000305|PubMed:22329759};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49629;
CC Evidence={ECO:0000305|PubMed:21658102, ECO:0000305|PubMed:22329759};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:21658102, ECO:0000269|PubMed:22329759}.
CC -!- DOMAIN: Multidomain protein; including a starter unit:ACP transacylase
CC (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes
CC repeated decarboxylative condensation to elongate the polyketide
CC backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and
CC transfers the extender unit malonyl-CoA; a product template (PT) domain
CC that controls the immediate cyclization regioselectivity of the
CC reactive polyketide backbone; and an acyl-carrier protein (ACP) that
CC serves as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm (PubMed:22329759).
CC {ECO:0000250|UniProtKB:Q5B0D0, ECO:0000305|PubMed:22329759}.
CC -!- DOMAIN: The release of the polyketide chain from the non-reducing
CC polyketide synthase is mediated by the thioesterase (TE) domain
CC localized at the C-terminus of the protein (PubMed:23368695).
CC {ECO:0000269|PubMed:23368695}.
CC -!- DISRUPTION PHENOTYPE: Impairs the synthesis of austinol and
CC dehydroaustinol (PubMed:21658102, PubMed:22329759).
CC {ECO:0000269|PubMed:21658102, ECO:0000269|PubMed:22329759}.
CC -!- MISCELLANEOUS: In A.calidoustus, the austinoid gene cluster lies on a
CC contiguous DNA region, while clusters from E.nidulans and P.brasilianum
CC are split in their respective genomes (Probable). Genetic
CC rearrangements provoked variability among the clusters and E.nidulans
CC produces the least number of austionoid derivatives with the end
CC products austinol and dehydroaustinol, while P.brasilianum can produce
CC until acetoxydehydroaustin, and A.calidoustus produces the highest
CC number of identified derivatives (Probable).
CC {ECO:0000305|PubMed:29076725}.
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DR EMBL; BN001305; CBF80428.1; -; Genomic_DNA.
DR EMBL; AACD01000153; EAA67005.1; -; Genomic_DNA.
DR RefSeq; XP_681652.1; XM_676560.1.
DR AlphaFoldDB; Q5ATJ7; -.
DR SMR; Q5ATJ7; -.
DR STRING; 162425.CADANIAP00002854; -.
DR ESTHER; emeni-q5atj7; Hormone-sensitive_lipase_like.
DR EnsemblFungi; CBF80428; CBF80428; ANIA_08383.
DR EnsemblFungi; EAA67005; EAA67005; AN8383.2.
DR GeneID; 2868762; -.
DR KEGG; ani:AN8383.2; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_3_1; -.
DR InParanoid; Q5ATJ7; -.
DR OMA; WINLPPY; -.
DR OrthoDB; 93381at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:1900563; P:dehydroaustinol biosynthetic process; IMP:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
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; IPR041068; HTH_51.
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; 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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 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; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Multifunctional enzyme; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..2476
FT /note="Non-reducing polyketide synthase ausA"
FT /id="PRO_0000436482"
FT DOMAIN 1626..1700
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 14..253
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255"
FT REGION 379..742
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 906..1210
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1280..1583
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1862..2095
FT /note="Methyltransferase (CMeT) domain"
FT /evidence="ECO:0000255"
FT REGION 2128..2476
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000269|PubMed:23368695"
FT ACT_SITE 544
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 993
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 2251
FT /note="For thioesterase activity"
FT /evidence="ECO:0000269|PubMed:23368695"
FT ACT_SITE 2413
FT /note="For thioesterase activity"
FT /evidence="ECO:0000269|PubMed:23368695"
FT ACT_SITE 2445
FT /note="For thioesterase activity"
FT /evidence="ECO:0000269|PubMed:23368695"
FT MOD_RES 1660
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MUTAGEN 1660
FT /note="S->A: Impairs the production of austinol and
FT dehydroaustinol."
FT /evidence="ECO:0000269|PubMed:21658102"
FT MUTAGEN 2251
FT /note="S->A: Abolishes the function of the TE domain."
FT /evidence="ECO:0000269|PubMed:23368695"
FT MUTAGEN 2413
FT /note="D->N: Abolishes the function of the TE domain."
FT /evidence="ECO:0000269|PubMed:23368695"
FT MUTAGEN 2445
FT /note="H->F: Abolishes the function of the TE domain."
FT /evidence="ECO:0000269|PubMed:23368695"
SQ SEQUENCE 2476 AA; 271827 MW; 1CFA270B5B7E319E CRC64;
MGSLDDNTLQ QVSVLFGPKY PEVELPAGHI RRYLSNQRNA NWLHDAIRDL PSVWHDILRL
WPAAEKLHGD ARLRQLSAFL GGGTLRPDMA EPMNFLLVPA TVLRHLVDFL ELKEDKNYDV
CDIQGFCVGF LAAIAAACWS DNEDEFGKVV STVLRLAVYI GAAVDLDELC EQPARSIAVR
WRTAQEHKLL TEVLTRYQGA YISCVTDENA VTVTVWDSQS VSFAKELEKH GLSVKTTTLR
GRFHHSNHTQ AVEDILQSCE RNSRLCLPSK CHKRSLPRSN INGRVCEADS LFTVAVESIL
TTQANWKITV TATLDNMGQS DARSIIPIGA GQFVPRHARC RMLNIVEFNK GEHINGRRKM
QSATALDVGV NVTAPETTAV PIAVTGMACR YPQADSVEEL WRILDLGQCT VSPMPNSRLK
SGSLQREPKG PFFGNYLARP DAFDHRFFGI SAREAESMDP QQRVLLQVAY EAMESAGYCG
LRRSKLPDDI GCYVGVGCDD YSENVGSRNA TAFSATGTLQ AFNSGRISHY FGWSGPSVTV
DTACSSAAVA IHLACQAIRT NDCAIAVAGG VNIMTDPRWS QNLAGASFLS PTGASKAFDA
DANGYCRGEG AGLLVLRPLE AALRDGDPIH AVITGTSVNQ GANCSPITVP DSNSQRSLYL
KALSLSGLTP DVVGYVEAHG TGTQVGDPIE FESIRKTFSG PNRATKLYVG SIKDNIGHTE
TSSGVAGMLK TILMIQKRRI PKQANFRRLN PRITLNERNH IEIPTQSIDW EAEKRVAMVT
NYGAAGSNAA IVLREPASTP ATSNSAHRET LPSHVPFYVS ARTEESLRSY CEALQSTIRE
VAQSGTNTVQ HIAYNLARKQ NRDMEHFVTF PAAAGEPSEL MTRLGSIASA HTQVERRSQS
FHPVIICFGG QTGDTASISR NLFESCELLR FHVDECENAC NALDLPSLFP AIVSPFPNKD
IVNLHCVLFS IQYATAKAWL DSGLQVTRMI GHSFGQLTAL CVAGGLSLID GMRLVATRAQ
LIQKHWGPHT GVMLSLRASK EKVQALLDAA SGHADLACLN GPDNFVVAGD EESIRRIEII
ATEKGMHVEL KRLKNTHAFH SRLVDAILPG LSEVANTLTF RQLDIPVEAC AEQEDDWLWV
TGDKIVQHSR KPVFFHDAVE RTLSRVDGPC VWLEAGTASP VINMVRRVVE ASRPLKSHVY
LPTDLSGAQA QANLAKVTCT LWSKAVPVQF WPFHPSETGY RWINLPPYQF AKTSHWIEYN
PDAFRSPPQV PDQENVQEAS LVRLLRQDGK EALFTINNKD NVFRMCTAGH AVANQNLCPA
SLYFELVVQA ALLVSSTATK PTMYHIESLN ICSPLVLGMP GAVLLQLTQQ DESHGQWSFV
LSTRDGLQDA VTHATGRVSL QAAGSNTGIC ARLSSLQRLL NLASWNSIAT SPSSSGLKRS
TVYQAFARAV NYADYYRGVE EVYAVGHEAT GRVILPSSPT KCNPCDPILI DNFIQVAGIH
VNCLSETHDD EVFVCSSVGD VLIGESFVRR DTAATVPWAV YSNYEPESKK KIVCDVFVLD
HTTGALAVCM LSATFTGVSI QSLKRTLNRL SNHTARPTEA EQVSINVAAE ATALSSTPVA
HVSSSDGDLL AVQTMLGELL GISADELSAA AALGDIGVDS LMSTEVLTEI NKRFGVAISN
AELTQIPDVG GLVQRIFPGH SVVRIKTHSQ GAVETEITIT DREPKSISVD LAPVCDTSPT
AFVDKASKLF ATTRTSAEFS RKTRFAGFCD TVFPQQMELV TSYVVEAFHA LGADLASLTP
GQVVPPVKIL PQHGKVMNQL VAVLEYSDLI ERRESEIIRS QQPVGTVPSL ILYKKILNKH
AQHASEHKLL HTTGSRLAEC LSGKADPLSL LFQNAEARAL MTDVYSNAPM FKSATIQLAQ
YLKDLLFNLG TQREIKVLEI GAGTGGTTNY LVQELAAVPG LRFQYTFTDI SSSLVTLARK
RFKAYDFMRY TTLDIENDPS PELQGQYDII ISTNCIHATR NLITSCTNIR RLLRPEGILC
LIELTRNLFW FDLVFGLLEG WWLFNDGRSH ALAHERLWDH NLRQAGFNWV DWTDNDSAES
DILRLIVASS TQPFYALEGD DECEADCNTV QEQTVLYNTR DGLELFADIY YPEKTDRSGA
KRPIALLIHG GGHIMLSRKE IHHEQVRMLF DMGFLPVSID YRLCPEVSLL DGPMQDACDA
LAWARNKLPQ LQLQRRDILP DGNNVVAVGW STGGHLAMTL AWTAPARGVS APEAILSFYS
PTDYTDPFWS KPNFPYRVDV STSDIQTGNP LDALQDAPIS GYNPPPSKRA LGGWMAPSDP
RSRIALYMNW TGQTLPVLFY GCNYRARAAE SGQDYEVVLP EPILSEVQKV CPFSQISAGS
YRAPTFLIHG TLDDLIPVQQ AQRTHDKMQA CGVDSDLRIV RDGLHLFDLE ANFAGNQHAF
QAVVDGYEFL RRHVGL
