STCJ_EMENI
ID STCJ_EMENI Reviewed; 1559 AA.
AC Q00681; C8VDT8; Q5AV65;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Fatty acid synthase alpha subunit stcJ {ECO:0000303|PubMed:8643646};
DE EC=2.3.1.86 {ECO:0000250|UniProtKB:Q8TGA2};
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase {ECO:0000250|UniProtKB:Q8TGA2};
DE EC=1.1.1.100 {ECO:0000250|UniProtKB:Q8TGA2};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase {ECO:0000250|UniProtKB:Q8TGA2};
DE EC=2.3.1.41 {ECO:0000250|UniProtKB:Q8TGA2};
DE AltName: Full=Sterigmatocystin biosynthesis cluster protein J {ECO:0000303|PubMed:8643646};
GN Name=stcJ {ECO:0000303|PubMed:8643646}; ORFNames=AN7815;
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 [GENOMIC DNA], INDUCTION, FUNCTION, AND PATHWAY.
RC STRAIN=FGSC 26;
RX PubMed=8643646; DOI=10.1073/pnas.93.4.1418;
RA Brown D.W., Yu J.-H., Kelkar H.S., Fernandes M., Nesbitt T.C., Keller N.P.,
RA Adams T.H., Leonard T.J.;
RT "Twenty-five coregulated transcripts define a sterigmatocystin gene cluster
RT in Aspergillus nidulans.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:1418-1422(1996).
RN [2]
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 [3]
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 [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=8017929; DOI=10.1128/aem.60.5.1444-1450.1994;
RA Keller N.P., Kantz N.J., Adams T.H.;
RT "Aspergillus nidulans verA is required for production of the mycotoxin
RT sterigmatocystin.";
RL Appl. Environ. Microbiol. 60:1444-1450(1994).
RN [5]
RP FUNCTION.
RX PubMed=7486998; DOI=10.1128/aem.61.10.3628-3632.1995;
RA Keller N.P., Segner S., Bhatnagar D., Adams T.H.;
RT "StcS, a putative P-450 monooxygenase, is required for the conversion of
RT versicolorin A to sterigmatocystin in Aspergillus nidulans.";
RL Appl. Environ. Microbiol. 61:3628-3632(1995).
RN [6]
RP FUNCTION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=7642507; DOI=10.1128/jb.177.16.4792-4800.1995;
RA Yu J.-H., Leonard T.J.;
RT "Sterigmatocystin biosynthesis in Aspergillus nidulans requires a novel
RT type I polyketide synthase.";
RL J. Bacteriol. 177:4792-4800(1995).
RN [7]
RP FUNCTION.
RX PubMed=8900026; DOI=10.1128/aem.62.11.4296-4298.1996;
RA Kelkar H.S., Keller N.P., Adams T.H.;
RT "Aspergillus nidulans stcP encodes an O-methyltransferase that is required
RT for sterigmatocystin biosynthesis.";
RL Appl. Environ. Microbiol. 62:4296-4298(1996).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=8962148; DOI=10.1073/pnas.93.25.14873;
RA Brown D.W., Adams T.H., Keller N.P.;
RT "Aspergillus has distinct fatty acid synthases for primary and secondary
RT metabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14873-14877(1996).
RN [9]
RP FUNCTION.
RX PubMed=8999832; DOI=10.1074/jbc.272.3.1589;
RA Kelkar H.S., Skloss T.W., Haw J.F., Keller N.P., Adams T.H.;
RT "Aspergillus nidulans stcL encodes a putative cytochrome P-450
RT monooxygenase required for bisfuran desaturation during
RT aflatoxin/sterigmatocystin biosynthesis.";
RL J. Biol. Chem. 272:1589-1594(1997).
RN [10]
RP INDUCTION.
RX PubMed=9680223; DOI=10.1046/j.1365-2958.1998.00907.x;
RA Fernandes M., Keller N.P., Adams T.H.;
RT "Sequence-specific binding by Aspergillus nidulans aflR, a C6 zinc cluster
RT protein regulating mycotoxin biosynthesis.";
RL Mol. Microbiol. 28:1355-1365(1998).
RN [11]
RP FUNCTION.
RX PubMed=10618248; DOI=10.1128/aem.66.1.359-362.2000;
RA Keller N.P., Watanabe C.M., Kelkar H.S., Adams T.H., Townsend C.A.;
RT "Requirement of monooxygenase-mediated steps for sterigmatocystin
RT biosynthesis by Aspergillus nidulans.";
RL Appl. Environ. Microbiol. 66:359-362(2000).
RN [12]
RP REVIEW ON STERIGMATOCYSTIN BIOSYNTHESIS.
RX PubMed=24957370; DOI=10.3390/metabo2010100;
RA Klejnstrup M.L., Frandsen R.J., Holm D.K., Nielsen M.T., Mortensen U.H.,
RA Larsen T.O., Nielsen J.B.;
RT "Genetics of polyketide metabolism in Aspergillus nidulans.";
RL Metabolites 2:100-133(2012).
CC -!- FUNCTION: Fatty acid synthase alpha subunit; part of the gene cluster
CC that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-
CC derived furanocoumarin which is part of the most toxic and carcinogenic
CC compounds among the known mycotoxins (PubMed:8643646, PubMed:8962148).
CC The first step in the biosynthesis of sterigmatocystin is the
CC production of hexanoate by the fatty acid synthase (FAS) units stcJ and
CC stcK (PubMed:8962148). The polyketide backbone is assembled by the non-
CC reducing polyketide synthase stcA by condensation of the starter
CC hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization
CC and release of norsolorinic acid (By similarity). Norsolorinic acid is
CC the first stable intermediate in the biosynthesis of sterigmatocystin
CC and is converted into averantin (AVN) by the ketoreductase stcE which
CC reduces the hexanoate ketone to an alcohol (PubMed:8643646) (Probable).
CC Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the
CC cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-
CC hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the
CC 5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step
CC is the conversion of OAVN into averufin (AVF) which is catalyzed by a
CC yet to be identified enzyme (PubMed:24957370). The cytochrome P450
CC monoxygenase stcB and the flavin-binding monooxygenase stcW are both
CC required for the conversion of averufin to 1-hydroxyversicolorone
CC (PubMed:10618248). The esterase stcI probably catalyzes the formation
CC of versiconal hemiacetal acetate from 1-hydroxyversicolorone
CC (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the
CC biosynthetic step from versiconal to versicolorin B (VERB)
CC (PubMed:24957370). The next step is performed by the versicolorin B
CC desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The
CC ketoreductase stcU and the cytochrome P450 monooxygenase stcS are
CC involved in the conversion of versicolorin A to
CC demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas
CC stcQ and the reductase stcR might be involved in the biosynthetic step
CC from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The
CC final step in the biosynthesis of sterigmatocystin is the methylation
CC of demethylsterigmatocystin catalyzed by the methyltransferase stcP
CC (PubMed:8900026). {ECO:0000250|UniProtKB:Q12053,
CC ECO:0000269|PubMed:10618248, ECO:0000269|PubMed:7486998,
CC ECO:0000269|PubMed:8643646, ECO:0000269|PubMed:8900026,
CC ECO:0000269|PubMed:8962148, ECO:0000269|PubMed:8999832,
CC ECO:0000303|PubMed:24957370, ECO:0000305|PubMed:8643646}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain
CC fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+);
CC Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:83139; EC=2.3.1.86;
CC Evidence={ECO:0000250|UniProtKB:Q8TGA2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC EC=2.3.1.41; Evidence={ECO:0000250|UniProtKB:Q8TGA2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC Evidence={ECO:0000250|UniProtKB:Q8TGA2};
CC -!- PATHWAY: Mycotoxin biosynthesis; sterigmatocystin biosynthesis.
CC {ECO:0000269|PubMed:8643646, ECO:0000269|PubMed:8962148}.
CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC (alpha and beta). {ECO:0000250|UniProtKB:P19097}.
CC -!- INDUCTION: The genes forming the sterigmatocystin biosynthesis cluster
CC are co-regulated and induced on oatmeal porridge or the fungal isolates
CC were grown either on oatmeal porridge or in YEC medium (0.2% yeast
CC extract, 5.0% corn steep liquor) (PubMed:8643646, PubMed:8017929).
CC Expression is positively regulated by the cluster-specific
CC transcription factor aflR that binds the palindromic sequence 5'-
CC TCG(N5)CGA-3'found in the promoter (PubMed:9680223).
CC {ECO:0000269|PubMed:8017929, ECO:0000269|PubMed:8643646,
CC ECO:0000269|PubMed:9680223}.
CC -!- DISRUPTION PHENOTYPE: Fails to produce sterigmatocystin under
CC conditions that supports production by wild-type. Able to grow without
CC exogenous long-chain fatty acids. {ECO:0000269|PubMed:8962148}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Fungal fatty acid
CC synthetase subunit alpha family. {ECO:0000305}.
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DR EMBL; U34740; AAC49198.1; -; Genomic_DNA.
DR EMBL; AACD01000132; EAA61603.1; -; Genomic_DNA.
DR EMBL; BN001304; CBF80164.1; -; Genomic_DNA.
DR RefSeq; XP_681084.1; XM_675992.1.
DR AlphaFoldDB; Q00681; -.
DR SMR; Q00681; -.
DR STRING; 162425.CADANIAP00000957; -.
DR PRIDE; Q00681; -.
DR EnsemblFungi; CBF80164; CBF80164; ANIA_07815.
DR EnsemblFungi; EAA61603; EAA61603; AN7815.2.
DR GeneID; 2869411; -.
DR KEGG; ani:AN7815.2; -.
DR eggNOG; ENOG502SH82; Eukaryota.
DR HOGENOM; CLU_000114_0_0_1; -.
DR InParanoid; Q00681; -.
DR OMA; VGVAPKY; -.
DR OrthoDB; 39339at2759; -.
DR UniPathway; UPA00377; -.
DR Proteomes; UP000000560; Chromosome IV.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IBA:GO_Central.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0045461; P:sterigmatocystin biosynthetic process; IMP:GO_Central.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.470.20; -; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR040899; Fas_alpha_ACP.
DR InterPro; IPR026025; FAS_alpha_yeast.
DR InterPro; IPR041550; FASI_helical.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF01648; ACPS; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF18325; Fas_alpha_ACP; 1.
DR Pfam; PF18314; FAS_I_H; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR PIRSF; PIRSF000454; FAS_yeast_alpha; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR SUPFAM; SSF56214; SSF56214; 1.
DR TIGRFAMs; TIGR00556; pantethn_trn; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 2: Evidence at transcript level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Metal-binding; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase; Virulence.
FT CHAIN 1..1559
FT /note="Fatty acid synthase alpha subunit stcJ"
FT /id="PRO_0000180289"
FT DOMAIN 68..147
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 457..693
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA2, ECO:0000255"
FT REGION 785..1316
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA2, ECO:0000255"
FT REGION 1105..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1058
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1058
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT BINDING 1432..1434
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P19097"
FT BINDING 1432
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P19097"
FT BINDING 1480..1490
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P19097"
FT BINDING 1504..1506
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P19097"
FT BINDING 1532..1534
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P19097"
FT BINDING 1533
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P19097"
FT MOD_RES 106
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT CONFLICT 215
FT /note="T -> N (in Ref. 1; AAC49198)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="A -> P (in Ref. 1; AAC49198)"
FT /evidence="ECO:0000305"
FT CONFLICT 1192
FT /note="I -> S (in Ref. 1; AAC49198)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1559 AA; 170114 MW; 41AF9FC53973B3B4 CRC64;
MTQKTIQQVP RQGLELLAST QDLAQLCYIY GEPAEGEDST ADESIINTPQ CSTIPEVAVE
PEVQPIPDTP LTAIFIIRAL VARKLRRSET EIDPSRSIKE LCGGKSTLQN ELIGELGNEF
QTSLPDRAED VSLADLDAAL GEVSLGPTSV SLLQRVFTAK MPARMTVSNV RERLAEIWGL
GFHRQTAVLV AALAAEPHSR LTSLEAAYQY WDGLTEAYGQ SLGLFLRKAI SQQAARSDDQ
GAQAIAPADS LGSKDLARKQ YEALREYLGI RTPTTKQDGL DLADLQQKLD CWTAEFSDDF
LSQISRRFDA RKTRWYRDWW NSARQELLTI CQNSNVQWTD KMREHFVQRA EEGLVEIARA
HSLAKPLVPD LIQAISLPPV VRLGRLATMM PRTVVTLKGE IQCEEHEREP SCFVEFFSSW
IQANNIRCTI QSNGEDLTSV FINSLVHASQ QGVSFANHTY LITGAGPGSI GQHIVRRLLT
GGARVIVTTS REPLPAAAFF KELYSKCGNR GSQLHLVPFN QASVVDCERL IGYIYDDLGL
DLDAILPFAA TSQVGAEIDG LDASNEAAFR LMLVNVLRLV GFVVSQKRRR GISCRPTQVV
LPLSPNHGIL GGDGLYAESK RGLETLIQRF HSESWKEELS ICGVSIGWTR STGLMAANDL
VAETAEKQGR VLTFSVDEMG DLISLLLTPQ LATRCEDAPV MADFSGNLSC WRDASAQLAA
ARASLRERAD TARALAQEDE REYRCRRAGS TQEPVDQRVS LHLGFPSLPE YDPLLHPDLV
PADAVVVVGF AELGPWGSAR IRWEMESRGC LSPAGYVETA WLMNLIRHVD NVNYVGWVDG
EDGKPVADAD IPKRYGERIL SNAGIRSLPS DNREVFQEIV LEQDLPSFET TRENAEALQQ
RHGDMVQVST LKNGLCLVQL QHGATIRVPK SIMSPPGVAG QLPTGWSPER YGIPAEIVQQ
VDPVALVLLC CVAEAFYSAG ISDPMEIFEH IHLSELGNFV GSSMGGVVNT RALYHDVCLD
KDVQSDALQE TYLNTAPAWV NMLYLGAAGP IKTPVGACAT ALESVDSAVE SIKAGQTKIC
LVGGYDDLQP EESAGFARMK ATVSVRDEQA RGREPGEMSR PTAASRSGFV ESQGCGVQLL
CRGDVALAMG LPIYGIIAGT GMASDGIGRS VPAPGQGILT FAQEDAQNPA PIRTALARWG
LGIDDITVAS LHATSTPAND TNEPLVIQRE MTHLGRTSGR PLWAICQKFV TGHPKAPAAA
WMLNGCLQVL DTGLVPGNRN ADDVDPALRS FSHLCFPIRS IQTDGIKAFL LNSCGFGQKE
AQLVGVHPRY FLGLLSEPEF EEYRTRRQLR IAGAERAYIS AMMTNSIVCV QSHPPFGPAE
MHSILLDPSA RICLDSSTNS YRVTKASTPV YTGFQRPHDK REDPRPSTIG VDTVTLSSFN
AHENAIFLQR NYTERERQSL QLQSHRSFRS AVASGWCAKE AVFKCLQTVS KGAGAAMSEI
EIVRVQGAPS VLHGDALAAA QKAGLDNIQL SLSYGDDCVV AVALGVRKWC LWPLASIIR
