ID   STLB_DICDI              Reviewed;        2968 AA.
AC   Q54FI3;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=Polyketide synthase 37 {ECO:0000303|PubMed:16906151};
DE            Short=dipks37 {ECO:0000303|PubMed:16906151};
DE   Includes:
DE     RecName: Full=Highly reducing polyketide synthase StlB {ECO:0000303|PubMed:16906151};
DE              EC=2.3.1.- {ECO:0000269|PubMed:16906151};
DE   Includes:
DE     RecName: Full=Chalcone synthase {ECO:0000303|PubMed:16906151};
DE              EC=2.3.1.74 {ECO:0000269|PubMed:16906151};
DE     AltName: Full=Steely2 {ECO:0000303|PubMed:16906151};
GN   Name=StlB; Synonyms=pks37; ORFNames=DDB_G0290853;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   FUNCTION.
RX   PubMed=9446571; DOI=10.1074/jbc.273.5.2669;
RA   Kay R.R.;
RT   "The biosynthesis of differentiation-inducing factor, a chlorinated signal
RT   molecule regulating Dictyostelium development.";
RL   J. Biol. Chem. 273:2669-2675(1998).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, DOMAIN, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=16906151; DOI=10.1038/nchembio811;
RA   Austin M.B., Saito T., Bowman M.E., Haydock S., Kato A., Moore B.S.,
RA   Kay R.R., Noel J.P.;
RT   "Biosynthesis of Dictyostelium discoideum differentiation-inducing factor
RT   by a hybrid type I fatty acid-type III polyketide synthase.";
RL   Nat. Chem. Biol. 2:494-502(2006).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=17660200; DOI=10.1093/bioinformatics/btm381;
RA   Zucko J., Skunca N., Curk T., Zupan B., Long P.F., Cullum J., Kessin R.H.,
RA   Hranueli D.;
RT   "Polyketide synthase genes and the natural products potential of
RT   Dictyostelium discoideum.";
RL   Bioinformatics 23:2543-2549(2007).
RN   [5]
RP   FUNCTION.
RX   PubMed=20231486; DOI=10.1073/pnas.1001681107;
RA   Neumann C.S., Walsh C.T., Kay R.R.;
RT   "A flavin-dependent halogenase catalyzes the chlorination step in the
RT   biosynthesis of Dictyostelium differentiation-inducing factor 1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:5798-5803(2010).
CC   -!- FUNCTION: Polyketide synthase; part of the gene cluster that mediates
CC       the biosynthesis of DIF-1 (Differentiation Inducing Factor-1), a signal
CC       molecule involved in the differentiation of pstO (prestalk-O) cells
CC       (PubMed:16906151). The three-step process begins with the formation of
CC       (2,4,6-trihydroxyphenyl)-1-hexan-1-one (THPH) by the polyketide
CC       synthase StlB (PubMed:16906151). THPH is then dichlorinated by the
CC       flavin-dependent halogenase ChlA (PubMed:20231486). The last step of
CC       DIF-1 biosynthesis is the O-methylation of dichloro-THPH (or des-
CC       methyl-DIF-1) by the methyltransferase DmtA to yield DIF-1
CC       (PubMed:9446571). {ECO:0000269|PubMed:16906151,
CC       ECO:0000269|PubMed:20231486, ECO:0000269|PubMed:9446571}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-coumaroyl-CoA + 2 H(+) + 3 malonyl-CoA = 2',4,4',6'-
CC         tetrahydroxychalcone + 3 CO2 + 4 CoA; Xref=Rhea:RHEA:11128,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57355, ChEBI:CHEBI:57384, ChEBI:CHEBI:77645; EC=2.3.1.74;
CC         Evidence={ECO:0000269|PubMed:16906151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11129;
CC         Evidence={ECO:0000269|PubMed:16906151};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 H(+) + hexanoyl-CoA + 3 malonyl-CoA = 2,4,6-
CC         trihydroxyphenylhexan-1-one + 3 CO2 + 4 CoA; Xref=Rhea:RHEA:64352,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:62620, ChEBI:CHEBI:150865;
CC         Evidence={ECO:0000269|PubMed:16906151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64353;
CC         Evidence={ECO:0000269|PubMed:16906151};
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000250|UniProtKB:A0A0K0MCJ4};
CC       Note=Binds 1 phosphopantetheine covalently.
CC       {ECO:0000250|UniProtKB:A0A0K0MCJ4};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC   -!- DEVELOPMENTAL STAGE: Expressed during development. Coordinately
CC       expressed with dmtA. {ECO:0000269|PubMed:16906151}.
CC   -!- DOMAIN: Modular protein possessing six classical catalytic domains and
CC       a type III polyketide synthase domain. May facilitate covalent transfer
CC       of steely N-terminal acyl products directly to the C-terminal type III
CC       PKS active sites, which catalyze both iterative polyketide extension
CC       and cyclization.
CC   -!- DISRUPTION PHENOTYPE: Developed to the slug stage, in which dif-1
CC       accumulation is maximal, though the Steely2- mutant slugs were thin and
CC       tended to break up. However, two independent Steely2 mutant strains
CC       both failed to accumulate any detectable dif-1 at this or any other
CC       stage of development. {ECO:0000269|PubMed:16906151}.
CC   -!- MISCELLANEOUS: Encoded by one of the numerous copies of polyketide
CC       synthase genes localized in chromosome 5.
CC   -!- MISCELLANEOUS: In reference to their hybrid nature and to their
CC       discovery in D.discoideum, authors term these type I FAS-type III PKS
CC       fusion enzymes 'steely'. {ECO:0000305|PubMed:16906151}.
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DR   EMBL; AAFI02000171; EAL62021.1; -; Genomic_DNA.
DR   RefSeq; XP_635518.1; XM_630426.1.
DR   SMR; Q54FI3; -.
DR   STRING; 44689.Q54FI3; -.
DR   PaxDb; 44689-DDB0234163; -.
DR   EnsemblProtists; EAL62021; EAL62021; DDB_G0290853.
DR   GeneID; 8627855; -.
DR   KEGG; ddi:DDB_G0290853; -.
DR   dictyBase; DDB_G0290853; stlB.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_5_1; -.
DR   InParanoid; Q54FI3; -.
DR   OMA; KMRGGEF; -.
DR   PhylomeDB; Q54FI3; -.
DR   UniPathway; UPA00154; -.
DR   PRO; PR:Q54FI3; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0102128; F:chalcone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016210; F:naringenin-chalcone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0106265; F:THPH synthase activity; IEA:RHEA.
DR   GO; GO:0048102; P:autophagic cell death; IMP:dictyBase.
DR   GO; GO:0018893; P:dibenzofuran metabolic process; IMP:dictyBase.
DR   GO; GO:0031148; P:DIF-1 biosynthetic process; IMP:dictyBase.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0010629; P:negative regulation of gene expression; IGI:dictyBase.
DR   GO; GO:0030639; P:polyketide biosynthetic process; IDA:dictyBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; IGI:dictyBase.
DR   GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR   GO; GO:0031149; P:sorocarp stalk cell differentiation; IMP:dictyBase.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd08954; KR_1_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 3.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR013154; ADH-like_N.
DR   InterPro; IPR012328; Chalcone/stilbene_synt_C.
DR   InterPro; IPR001099; Chalcone/stilbene_synt_N.
DR   InterPro; IPR011032; GroES-like_sf.
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; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR45681:SF6; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   Pfam; PF02797; Chal_sti_synt_C; 1.
DR   Pfam; PF00195; Chal_sti_synt_N; 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; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF53901; Thiolase-like; 3.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS52019; PKS_MFAS_DH; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Multifunctional enzyme; Phosphopantetheine;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..2968
FT                   /note="Polyketide synthase 37"
FT                   /id="PRO_0000377902"
FT   DOMAIN          32..454
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348,
FT                   ECO:0000305|PubMed:16906151"
FT   DOMAIN          1017..1350
FT                   /note="PKS/mFAS DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   DOMAIN          2421..2498
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          624..950
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:16906151"
FT   REGION          1017..1157
FT                   /note="N-terminal hotdog fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   REGION          1031..1345
FT                   /note="Dehydratase (DH) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:16906151"
FT   REGION          1183..1350
FT                   /note="C-terminal hotdog fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   REGION          1522..1547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1718..2053
FT                   /note="Enoyl reductase (ER) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:16906151"
FT   REGION          2083..2277
FT                   /note="Ketoreductase (KR) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:16906151"
FT   REGION          2379..2400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2568..2589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2707..2968
FT                   /note="Chalcone synthase"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:16906151"
FT   COMPBIAS        2568..2585
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        198
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        338
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        378
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        718
FT                   /note="For malonyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        1049
FT                   /note="Proton acceptor; for dehydratase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   ACT_SITE        1257
FT                   /note="Proton donor; for dehydratase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   ACT_SITE        2747
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2458
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2968 AA;  329909 MW;  98AA21F6256A8A57 CRC64;
     MNNNKSINDL SGNSNNNIAN SNINNYNNLI KKEPIAIIGI GCRFPGNVSN YSDFVNIIKN
     GSDCLTKIPD DRWNADIISR KQWKLNNRIG GYLKNIDQFD NQFFGISPKE AQHIDPQQRL
     LLHLAIETLE DGKISLDEIK GKKVGVFIGS SSGDYLRGFD SSEINQFTTP GTNSSFLSNR
     LSYFLDVNGP SMTVNTACSA SMVAIHLGLQ SLWNGESELS MVGGVNIISS PLQSLDFGKA
     GLLNQETDGR CYSFDPRASG YVRSEGGGIL LLKPLSAALR DNDEIYSLLL NSANNSNGKT
     PTGITSPRSL CQEKLIQQLL RESSDQFSID DIGYFECHGT GTQMGDLNEI TAIGKSIGML
     KSHDDPLIIG SVKASIGHLE GASGICGVIK SIICLKEKIL PQQCKFSSYN PKIPFETLNL
     KVLTKTQPWN NSKRICGVNS FGVGGSNSSL FLSSFDKSTT ITEPTTTTTI ESLPSSSSSF
     DNLSVSSSIS TNNDNDKVSN IVNNRYGSSI DVITLSVTSP DKEDLKIRAN DVLESIKTLD
     DNFKIRDISN LTNIRTSHFS NRVAIIGDSI DSIKLNLQSF IKGENNNNKS IILPLINNGN
     NNNNNNNNSS GSSSSSSNNN NICFIFSGQG QQWNKMIFDL YENNKTFKNE MNNFSKQFEM
     ISGWSIIDKL YNSGGGGNEE LINETWLAQP SIVAVQYSLI KLFSKDIGIE GSIVLGHSLG
     ELMAAYYCGI INDFNDLLKL LYIRSTLQNK TNGSGRMHVC LSSKAEIEQL ISQLGFNGRI
     VICGNNTMKS CTISGDNESM NQFTKLISSQ QYGSVVHKEV RTNSAFHSHQ MDIIKDEFFK
     LFNQYFPTNQ ISTNQIYDGK SFYSTCYGKY LTPIECKQLL SSPNYWWKNI RESVLFKESI
     EQILQNHQQS LTFIEITCHP ILNYFLSQLL KSSSKSNTLL LSTLSKNSNS IDQLLILCSK
     LYVNNLSSIK WNWFYDKQQQ QQSESLVSSN FKLPGRRWKL EKYWIENCQR QMDRIKPPMF
     ISLDRKLFSV TPSFEVRLNQ DRFQYLNDHQ IQDIPLVPFS FYIELVYASI FNSISTTTTN
     TTASTMFEIE NFTIDSSIII DQKKSTLIGI NFNSDLTKFE IGSINSIGSG SSSNNNFIEN
     KWKIHSNGII KYGTNYLKSN SKSNSFNEST TTTTTTTTTT KCFKSFNSNE FYNEIIKYNY
     NYKSTFQCVK EFKQFDKQGT FYYSEIQFKK NDKQVIDQLL SKQLPSDFRC IHPCLLDAVL
     QSAIIPATNK TNCSWIPIKI GKLSVNIPSN SYFNFKDQLL YCLIKPSTST STSPSTYFSS
     DIQVFDKKNN NLICELTNLE FKGINSSSSS SSSSSTINSN VEANYESKIE ETNHDEDEDE
     ELPLVSEYVW CKEELINQSI KFTDNYQTVI FCSTNLNGND LLDSIITSAL ENGHDENKIF
     IVSPPPVESD QYNNRIIINY TNNESDFDAL FAIINSTTSI SGKSGLFSTR FIILPNFNSI
     TFSSGNSTPL ITNVNGNGNG KSCGGGGGST NNTISNSSSS ISSIDNGNNE DEEMVLKSFN
     DSNLSLFHLQ KSIIKNNIKG RLFLITNGGQ SISSSTPTST YNDQSYVNLS QYQLIGQIRV
     FSNEYPIMEC SMIDIQDSTR IDLITDQLNS TKLSKLEIAF RDNIGYSYKL LKPSIFDNSS
     LPSSSSEIET TATTKDEEKN NSINYNNNYY RVELSDNGII SDLKIKQFRQ MKCGVGQVLV
     RVEMCTLNFR DILKSLGRDY DPIHLNSMGD EFSGKVIEIG EGVNNLSVGQ YVFGINMSKS
     MGSFVCCNSD LVFPIPIPTP SSSSSSNENI DDQEIISKLL NQYCTIPIVF LTSWYSIVIQ
     GRLKKGEKIL IHSGCGGVGL ATIQISMMIG AEIHVTVGSN EKKQYLIKEF GIDEKRIYSS
     RSLQFYNDLM VNTDGQGVDM VLNSLSGEYL EKSIQCLSQY GRFIEIGKKD IYSNSSIHLE
     PFKNNLSFFA VDIAQMTENR RDYLREIMID QLLPCFKNGS LKPLNQHCFN SPCDLVKAIR
     FMSSGNHIGK ILINWSNLNN DKQFINHHSV VHLPIQSFSN RSTYIFTGFG GLTQTLLKYF
     STESDLTNVI IVSKNGLDDN SGSGSGNNEK LKLINQLKES GLNVLVEKCD LSSIKQVYKL
     FNKIFDNDAS GSDSGDFSDI KGIFHFASLI NDKRILKHNL ESFNYVYNSK ATSAWNLHQV
     SLKYNLNLDH FQTIGSVITI LGNIGQSNYT CANRFVEGLT HLRIGMGLKS SCIHLASIPD
     VGMASNDNVL NDLNSMGFVP FQSLNEMNLG FKKLLSSPNP IVVLGEINVD RFIEATPNFR
     AKDNFIITSL FNRIDPLLLV NESQDFIINN NINNNGGGGD GSFDDLNQLE DEGQQGFGNG
     DGYVDDNIDS VSMLSGTSSI FDNDFYTKSI RGMLCDILEL KDKDLNNTVS FSDYGLDSLL
     SSELSNTIQK NFSILIPSLT LVDNSTINST VELIKNKLKN STTSSISSSV SKKVSFKKNT
     QPLIIPTTAP ISIIKTQSYI KSEIIESLPI SSSTTIKPLV FDNLVYSSSS SNNSNSKNEL
     TSPPPSAKRE SVLPIISEDN NSDNDSSMAT VIYEISPIAA PYHRYQTDVL KEITQLTPHK
     EFIDNIYKKS KIRSRYCFND FSEKSMADIN KLDAGERVAL FREQTYQTVI NAGKTVIERA
     GIDPMLISHV VGVTSTGIMA PSFDVVLIDK LGLSINTSRT MINFMGCGAA VNSMRAATAY
     AKLKPGTFVL VVAVEASATC MKFNFDSRSD LLSQAIFTDG CVATLVTCQP KSSLVGKLEI
     IDDLSYLMPD SRDALNLFIG PTGIDLDLRP ELPIAINRHI NSAITSWLKK NSLQKSDIEF
     FATHPGGAKI ISAVHEGLGL SPEDLSDSYE VMKRYGNMIG VSTYYVLRRI LDKNQTLLQE
     GSLGYNYGMA MAFSPGASIE AILFKLIK
//