ID   PKS1_DICDI              Reviewed;        3147 AA.
AC   Q55E72;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Probable polyketide synthase 1;
DE            Short=dipks1;
DE   Includes:
DE     RecName: Full=Polyketide synthase stlA;
DE              EC=2.3.1.-;
DE   Includes:
DE     RecName: Full=Chalcone synthase stlA;
DE              EC=2.3.1.74;
DE     AltName: Full=Steely1;
GN   Name=stlA; Synonyms=pks1; ORFNames=DDB_G0269364;
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   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   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 2776-3147, FUNCTION, DEVELOPMENTAL
RP   STAGE, AND SUBUNIT.
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).
CC   -!- FUNCTION: Probable polyketide synthase (By similarity). Produces only
CC       acylpyrones; in vitro. {ECO:0000250, ECO:0000269|PubMed:16906151}.
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   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 phosphopantetheine covalently. {ECO:0000250};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16906151}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during development. Expressed maximally
CC       in early development before cellular aggregation.
CC       {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   -!- 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}.
CC   -!- MISCELLANEOUS: Encoded by one of the numerous copies of polyketide
CC       synthase genes localized in chromosome 1.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the thiolase-like
CC       superfamily. Chalcone/stilbene synthases family. {ECO:0000305}.
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DR   EMBL; AAFI02000005; EAL72032.1; -; Genomic_DNA.
DR   RefSeq; XP_645909.1; XM_640817.1.
DR   PDB; 2H84; X-ray; 2.90 A; A/B=2776-3147.
DR   PDBsum; 2H84; -.
DR   SMR; Q55E72; -.
DR   STRING; 44689.Q55E72; -.
DR   PaxDb; 44689-DDB0234164; -.
DR   EnsemblProtists; EAL72032; EAL72032; DDB_G0269364.
DR   GeneID; 8616850; -.
DR   KEGG; ddi:DDB_G0269364; -.
DR   dictyBase; DDB_G0269364; stlA.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_5_1; -.
DR   InParanoid; Q55E72; -.
DR   OMA; KDVQHYT; -.
DR   PhylomeDB; Q55E72; -.
DR   Reactome; R-DDI-163765; ChREBP activates metabolic gene expression.
DR   Reactome; R-DDI-199220; Vitamin B5 (pantothenate) metabolism.
DR   Reactome; R-DDI-75105; Fatty acyl-CoA biosynthesis.
DR   UniPathway; UPA00154; -.
DR   EvolutionaryTrace; Q55E72; -.
DR   PRO; PR:Q55E72; -.
DR   Proteomes; UP000002195; Chromosome 1.
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:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR   GO; GO:0016210; F:naringenin-chalcone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR   GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:dictyBase.
DR   GO; GO:0030639; P:polyketide biosynthetic process; IDA:dictyBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR   GO; GO:0106070; P:regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:dictyBase.
DR   GO; GO:0019505; P:resorcinol metabolic process; IDA:dictyBase.
DR   GO; GO:0007165; P:signal transduction; IDA:dictyBase.
DR   GO; GO:0048837; P:sorocarp sorus development; IMP:dictyBase.
DR   GO; GO:0044671; P:sorocarp spore cell differentiation; IMP:dictyBase.
DR   GO; GO:0031149; P:sorocarp stalk cell differentiation; IGI:dictyBase.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd00831; CHS_like; 1.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd08954; KR_1_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 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   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; 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; 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; 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; IPR009081; PP-bd_ACP.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
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; 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; 2.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF08242; Methyltransf_12; 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   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; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
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; PS00012; PHOSPHOPANTETHEINE; 1.
DR   PROSITE; PS52019; PKS_MFAS_DH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Flavonoid biosynthesis; Phosphopantetheine;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..3147
FT                   /note="Probable polyketide synthase 1"
FT                   /id="PRO_0000377901"
FT   DOMAIN          12..457
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   DOMAIN          976..1298
FT                   /note="PKS/mFAS DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   DOMAIN          2568..2645
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          345..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..705
FT                   /note="Acyl/malonyl transferase"
FT   REGION          976..1127
FT                   /note="N-terminal hotdog fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   REGION          1149..1298
FT                   /note="C-terminal hotdog fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   REGION          2723..2747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2789..3147
FT                   /note="Chalcone synthase"
FT   ACT_SITE        180
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        319
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        380
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        682
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        1014
FT                   /note="Proton acceptor; for dehydratase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   ACT_SITE        1209
FT                   /note="Proton donor; for dehydratase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   ACT_SITE        2930
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2605
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   STRAND          2788..2795
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   STRAND          2797..2799
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   HELIX           2803..2813
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   HELIX           2818..2829
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   HELIX           2845..2847
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   HELIX           2849..2854
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   HELIX           2857..2883
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   HELIX           2887..2889
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   STRAND          2892..2899
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   HELIX           2906..2914
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   STRAND          2921..2927
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   HELIX           2929..2931
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   HELIX           2932..2944
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   STRAND          2951..2958
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   HELIX           2961..2963
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   STRAND          2967..2969
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   HELIX           2970..2978
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   STRAND          2982..2991
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   STRAND          3000..3009
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   STRAND          3016..3022
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   STRAND          3025..3030
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   HELIX           3034..3053
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   TURN            3054..3056
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   STRAND          3063..3070
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   HELIX           3075..3084
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   HELIX           3089..3092
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   HELIX           3093..3102
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   HELIX           3108..3118
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   STRAND          3125..3133
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   TURN            3134..3136
FT                   /evidence="ECO:0007829|PDB:2H84"
FT   STRAND          3137..3145
FT                   /evidence="ECO:0007829|PDB:2H84"
SQ   SEQUENCE   3147 AA;  352195 MW;  6B67391AB6596F46 CRC64;
     MNKNSKIQSP NSSDVAVIGV GFRFPGNSND PESLWNNLLD GFDAITQVPK ERWATSFREM
     GLIKNKFGGF LKDSEWKNFD PLFFGIGPKE APFIDPQQRL LLSIVWESLE DAYIRPDELR
     GSNTGVFIGV SNNDYTKLGF QDNYSISPYT MTGSNSSLNS NRISYCFDFR GPSITVDTAC
     SSSLVSVNLG VQSIQMGECK IAICGGVNAL FDPSTSVAFS KLGVLSENGR CNSFSDQASG
     YVRSEGAGVV VLKSLEQAKL DGDRIYGVIK GVSSNEDGAS NGDKNSLTTP SCEAQSINIS
     KAMEKASLSP SDIYYIEAHG TGTPVGDPIE VKALSKIFSN SNNNQLNNFS TDGNDNDDDD
     DDNTSPEPLL IGSFKSNIGH LESAAGIASL IKCCLMLKNR MLVPSINCSN LNPSIPFDQY
     NISVIREIRQ FPTDKLVNIG INSFGFGGSN CHLIIQEYNN NFKNNSTICN NNNNNNNNID
     YLIPISSKTK KSLDKYLILI KTNSNYHKDI SFDDFVKFQI KSKQYNLSNR MTTIANDWNS
     FIKGSNEFHN LIESKDGEGG SSSSNRGIDS ANQINTTTTS TINDIEPLLV FVFCGQGPQW
     NGMIKTLYNS ENVFKNTVDH VDSILYKYFG YSILNVLSKI DDNDDSINHP IVAQPSLFLL
     QIGLVELFKY WGIYPSISVG HSFGEVSSYY LSGIISLETA CKIVYVRSSN QNKTMGSGKM
     LVVSMGFKQW NDQFSAEWSD IEIACYNAPD SIVVTGNEER LKELSIKLSD ESNQIFNTFL
     RSPCSFHSSH QEVIKGSMFE ELSNLQSTGE TEIPLFSTVT GRQVLSGHVT AQHIYDNVRE
     PVLFQKTIES ITSYIKSHYP SNQKVIYVEI APHPTLFSLI KKSIPSSNKN SSSVLCPLNR
     KENSNNSYKK FVSQLYFNGV NVDFNFQLNS ICDNVNNDHH LNNVKQNSFK ETTNSLPRYQ
     WEQDEYWSEP LISRKNRLEG PTTSLLGHRI IYSFPVFQSV LDLQSDNYKY LLDHLVNGKP
     VFPGAGYLDI IIEFFDYQKQ QLNSSDSSNS YIINVDKIQF LNPIHLTENK LQTLQSSFEP
     IVTKKSAFSV NFFIKDTVED QSKVKSMSDE TWTNTCKATI SLEQQQPSPS STLTLSKKQD
     LQILRNRCDI SKLDKFELYD KISKNLGLQY NSLFQVVDTI ETGKDCSFAT LSLPEDTLFT
     TILNPCLLDN CFHGLLTLIN EKGSFVVESI SSVSIYLENI GSFNQTSVGN VQFYLYTTIS
     KATSFSSEGT CKLFTKDGSL ILSIGKFIIK STNPKSTKTN ETIESPLDET FSIEWQSKDS
     PIPTPQQIQQ QSPLNSNPSF IRSTILKDIQ FEQYCSSIIH KELINHEKYK NQQSFDINSL
     ENHLNDDQLM ESLSISKEYL RFFTRIISII KQYPKILNEK ELKELKEIIE LKYPSEVQLL
     EFEVIEKVSM IIPKLLFEND KQSSMTLFQD NLLTRFYSNS NSTRFYLERV SEMVLESIRP
     IVREKRVFRI LEIGAGTGSL SNVVLTKLNT YLSTLNSNGG SGYNIIIEYT FTDISANFII
     GEIQETMCNL YPNVTFKFSV LDLEKEIINS SDFLMGDYDI VLMAYVIHAV SNIKFSIEQL
     YKLLSPRGWL LCIEPKSNVV FSDLVFGCFN QWWNYYDDIR TTHCSLSESQ WNQLLLNQSL
     NNESSSSSNC YGGFSNVSFI GGEKDVDSHS FILHCQKESI SQMKLATTIN NGLSSGSIVI
     VLNSQQLTNM KSYPKVIEYI QEATSLCKTI EIIDSKDVLN STNSVLEKIQ KSLLVFCLLG
     YDLLENNYQE QSFEYVKLLN LISTTASSSN DKKPPKVLLI TKQSERISRS FYSRSLIGIS
     RTSMNEYPNL SITSIDLDTN DYSLQSLLKP IFSNSKFSDN EFIFKKGLMF VSRIFKNKQL
     LESSNAFETD SSNLYCKASS DLSYKYAIKQ SMLTENQIEI KVECVGINFK DNLFYKGLLP
     QEIFRMGDIY NPPYGLECSG VITRIGSNVT EYSVGQNVFG FARHSLGSHV VTNKDLVILK
     PDTISFSEAA SIPVVYCTAW YSLFNIGQLS NEESILIHSA TGGVGLASLN LLKMKNQQQQ
     PLTNVYATVG SNEKKKFLID NFNNLFKEDG ENIFSTRDKE YSNQLESKID VILNTLSGEF
     VESNFKSLRS FGRLIDLSAT HVYANQQIGL GNFKFDHLYS AVDLERLIDE KPKLLQSILQ
     RITNSIVNGS LEKIPITIFP STETKDAIEL LSKRSHIGKV VVDCTDISKC NPVGDVITNF
     SMRLPKPNYQ LNLNSTLLIT GQSGLSIPLL NWLLSKSGGN VKNVVIISKS TMKWKLQTMI
     SHFVSGFGIH FNYVQVDISN YDALSEAIKQ LPSDLPPITS VFHLAAIYND VPMDQVTMST
     VESVHNPKVL GAVNLHRISV SFGWKLNHFV LFSSITAITG YPDQSIYNSA NSILDALSNF
     RRFMGLPSFS INLGPMKDEG KVSTNKSIKK LFKSRGLPSL SLNKLFGLLE VVINNPSNHV
     IPSQLICSPI DFKTYIESFS TMRPKLLHLQ PTISKQQSSI INDSTKASSN ISLQDKITSK
     VSDLLSIPIS KINFDHPLKH YGLDSLLTVQ FKSWIDKEFE KNLFTHIQLA TISINSFLEK
     VNGLSTNNNN NNNSNVKSSP SIVKEEIVTL DKDQQPLLLK EHQHIIISPD IRINKPKRES
     LIRTPILNKF NQITESIITP STPSLSQSDV LKTPPIKSLN NTKNSSLINT PPIQSVQQHQ
     KQQQKVQVIQ QQQQPLSRLS YKSNNNSFVL GIGISVPGEP ISQQSLKDSI SNDFSDKAET
     NEKVKRIFEQ SQIKTRHLVR DYTKPENSIK FRHLETITDV NNQFKKVVPD LAQQACLRAL
     KDWGGDKGDI THIVSVTSTG IIIPDVNFKL IDLLGLNKDV ERVSLNLMGC LAGLSSLRTA
     ASLAKASPRN RILVVCTEVC SLHFSNTDGG DQMVASSIFA DGSAAYIIGC NPRIEETPLY
     EVMCSINRSF PNTENAMVWD LEKEGWNLGL DASIPIVIGS GIEAFVDTLL DKAKLQTSTA
     ISAKDCEFLI HTGGKSILMN IENSLGIDPK QTKNTWDVYH AYGNMSSASV IFVMDHARKS
     KSLPTYSISL AFGPGLAFEG CFLKNVV
//