STCK_EMENI
ID STCK_EMENI Reviewed; 1914 AA.
AC Q00706; C8VDT7; Q5AV66;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Fatty acid synthase beta subunit stcK {ECO:0000303|PubMed:8643646};
DE EC=2.3.1.86 {ECO:0000250|UniProtKB:Q8TGA1};
DE Includes:
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=4.2.1.59 {ECO:0000250|UniProtKB:Q8TGA1};
DE Includes:
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=1.3.1.9 {ECO:0000250|UniProtKB:Q8TGA1};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] acetyltransferase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=2.3.1.38 {ECO:0000250|UniProtKB:Q8TGA1};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] malonyltransferase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=2.3.1.39 {ECO:0000250|UniProtKB:Q8TGA1};
DE AltName: Full=S-acyl fatty acid synthase thioesterase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=3.1.2.14 {ECO:0000250|UniProtKB:Q8TGA1};
DE AltName: Full=Sterigmatocystin biosynthesis cluster protein K {ECO:0000303|PubMed:8643646};
GN Name=stcK {ECO:0000303|PubMed:8643646}; ORFNames=AN7814;
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.
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 beta 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). The first step
CC in the biosynthesis of sterigmatocystin is the production of hexanoate
CC by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148).
CC The polyketide backbone is assembled by the non-reducing polyketide
CC synthase stcA by condensation of the starter hexanoyl-CoA and 7
CC malonyl-CoA extender units followed by cyclization and release of
CC norsolorinic acid (By similarity). Norsolorinic acid is the first
CC stable intermediate in the biosynthesis of sterigmatocystin and is
CC converted into averantin (AVN) by the ketoreductase stcE which reduces
CC 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:Q8TGA1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA;
CC Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78446; EC=2.3.1.38;
CC Evidence={ECO:0000250|UniProtKB:Q8TGA1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449; EC=2.3.1.39;
CC Evidence={ECO:0000250|UniProtKB:Q8TGA1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC Evidence={ECO:0000250|UniProtKB:Q8TGA1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC Evidence={ECO:0000250|UniProtKB:Q8TGA1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) +
CC holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14;
CC Evidence={ECO:0000250|UniProtKB:Q8TGA1};
CC -!- PATHWAY: Mycotoxin biosynthesis; sterigmatocystin biosynthesis.
CC {ECO:0000269|PubMed:8643646}.
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 -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC49199.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U34740; AAC49199.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AACD01000132; EAA61602.1; -; Genomic_DNA.
DR EMBL; BN001304; CBF80162.1; -; Genomic_DNA.
DR RefSeq; XP_681083.1; XM_675991.1.
DR AlphaFoldDB; Q00706; -.
DR SMR; Q00706; -.
DR STRING; 162425.CADANIAP00000956; -.
DR PRIDE; Q00706; -.
DR EnsemblFungi; CBF80162; CBF80162; ANIA_07814.
DR EnsemblFungi; EAA61602; EAA61602; AN7814.2.
DR GeneID; 2869366; -.
DR KEGG; ani:AN7814.2; -.
DR VEuPathDB; FungiDB:AN7814; -.
DR eggNOG; ENOG502SKWI; Eukaryota.
DR HOGENOM; CLU_000114_5_0_1; -.
DR InParanoid; Q00706; -.
DR OMA; VCAGHFR; -.
DR OrthoDB; 8490at2759; -.
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:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:InterPro.
DR GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:InterPro.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0045461; P:sterigmatocystin biosynthetic process; IMP:AspGD.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.366.10; -; 3.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR016452; Fas1/AflB-like.
DR InterPro; IPR013565; Fas1/AflB-like_central.
DR InterPro; IPR040883; FAS_meander.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR039569; MaoC-like_dehydrat_N.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR032088; SAT.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08354; DUF1729; 1.
DR Pfam; PF17951; FAS_meander; 1.
DR Pfam; PF13452; MaoC_dehydrat_N; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF16073; SAT; 1.
DR PIRSF; PIRSF005562; FAS_yeast_beta; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; SSF52151; 2.
DR SUPFAM; SSF54637; SSF54637; 2.
PE 2: Evidence at transcript level;
KW Hydrolase; Lyase; Multifunctional enzyme; NAD; NADP; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..1914
FT /note="Fatty acid synthase beta subunit stcK"
FT /id="PRO_0000180290"
FT DOMAIN 1398..1532
FT /note="MaoC-like"
FT /evidence="ECO:0000255"
FT REGION 17..395
FT /note="Acetyltransferase (AT) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA1, ECO:0000255"
FT REGION 446..692
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA1, ECO:0000255"
FT REGION 1009..1509
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA1, ECO:0000255"
FT REGION 1548..1900
FT /note="Malonyl/palmitoyl transferase (MT/PT) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA1, ECO:0000255"
FT CONFLICT 525
FT /note="I -> T (in Ref. 1; AAC49199)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1914 AA; 211238 MW; EE42E46F43442BD6 CRC64;
MTPSPFLDAV DAGLSRLYAC FGGQGPSNWA GLDELVHLSH AYADCAPIQD LLDSSARRLE
SLAAIPHRSS FFAGRGFQLQ AWLNDAAASA PLPEDLALSP YSFPINTLLS LLHYAITAYS
LQLDPGQLRQ KLQGAIGHSQ GVFVAAAIAI SHTDHGWPSF YRAADLALQL SFWVGLESHH
ASPRSILCAN EVIDCLENGE GAPSHLLSVT GLDINHLERL VRKLNDQGGD SLYISLINGH
NKFVLAGAPH ALRGVCIALR SVKASPELDQ SRVPFPLRRS VVDVQFLPVS APYHSSLLSS
VELRVTDAIG GLRLRGNDLA IPVYCQANGS LRNLQDYGTH DILLTLIQSV TVERVNWPAL
CWAMNDATHV LSFGPGAVGS LVQDVLEGTG MNVVNLSGQS MASNLSLLNL SAFALPLGKD
WGRKYRPRLR KAAEGSAHAS IETKMTRLLG TPHVMVAGMT PTTCSPELVA AIIQADYHVE
FACGGYYNRA TLETALRQLS RSIPPHRSIT CNVIYASPKA LSWQIQVLRR LIMEEGLPID
GITVGAGIPS PEVVKEWIDM LAISHIWFKP GSVDAIDRVL TIARQYPTLP VGIQWTGGRA
GGHHSCEDFH LPILDCYARI RNCENVILVA GSGFGGAEDT WPYMNGSWSC KLGYAPMPFD
GILLGSRMMV AREAKTSFAV KQLIVEAPGV KDDGNDNGAW AKCEHDAVGG VISVTSEMGQ
PIHVLATRAM RLWKEFDDRF FSIRDPKRLK AALKQHRVEI INRLNNDFAR PWFAQTDSSK
PTEIEELSYR QVLRRLCQLT YVQHQARWID SSYLSLVHDF LRLAQGRLGS GSEAELRFLS
CNTPIELEAS FDAAYGVQGD QILYPEDVSL LINLFRRQGQ KPVPFIPRLD ADFQTWFKKD
SLWQSEDVDA VVDQDAQRVC IIQGPVAVRH SRVCDEPVKD ILDGITEAHL KMMLKEAASD
NGYTWANQRD EKGNRLPGIE TSQEGSLCRY YLVGPTLPST EAIVEHLVGE CAWGYAALSQ
KKVVFGQNRA PNPIRDAFKP DIGDVIEAKY MDGCLREITL YHSLRRQGDP RAIRAALGLI
HLDGNKVSVT LLTRSKGKRP ALEFKMELLG GTMGPLILKM HRTDYLDSVR RLYTDLWIGR
DLPSPTSVGL NSEFTGDRVT ITAEDVNTFL AIVGQAGPAR CRAWGTRGPV VPIDYAVVIA
WTALTKPILL EALDADPLRL LHQSASTRFV PGIRPLHVGD TVTTSSRITE RTITTIGQRV
EISAELLREG KPVVRLQTTF IIQRRPEESV SQQQFRCVEE PDMVIRVDSH TKLRVLMSRK
WFLLDGPCSD LIGKILIFQL HSQTVFDAAG APASLQVSGS VSLAPSDTSV VCVSSVGTRI
GRVYMEEEGF GANPVMDFLN RHGAPRVQRQ PLPRAGWTGD DAASISFTAP AQSEGYAMVS
GDTNPIHVCP LFSRFAGLGQ PVVHGLHLSA TVRRILEWII GDNERTRFCS WAPSFDGLVR
ANDRLRMEIQ HFAMADGCMV VHVRVLKEST GEQVMHAEAV LEQAQTTYVF TGQGTQERGM
GMALYDTNAA ARAVWDRAER HFRSQYGISL LHIVRENPTS LTVNFGSRRG RQIRDIYLSM
SDSDPSMLPG LTRDSRSYTF NYPSGLLMST QFAQPALAVM EIAEYAHLQA QGVVQTQAIF
AGHSLGEYSS LGACTTIMPF ESLLSLILYR GLKMQNTLPR NANGRTDYGM VAADPSRIRS
DFTEDRLIEL VRLVSQATGV LLEVVNYNVH SRQYVCAGHV RSLWVLSHAC DDLSRSTSPN
SPQTMSECIA HHIPSSCSVT NETELSRGRA TIPLAGVDIP FHSQMLRGHI DGYRQYLRHH
LRVSDIKPEE LVGRWIPNVT GKPFALDAPY IRLVQGVTQS RPLLELLRRV EENR
