ID FSL1_GIBZE Reviewed; 2642 AA.
AC I1S166; A0A098DD60;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Fusarielin synthase FSL1 {ECO:0000303|PubMed:22252016};
DE EC=2.3.1.- {ECO:0000305|PubMed:27983606};
DE AltName: Full=Fusarielin biosynthesis cluster protein 1 {ECO:0000303|PubMed:22252016};
DE AltName: Full=Reducing polyketide synthase FSL1 {ECO:0000303|PubMed:22252016};
GN Name=FSL1 {ECO:0000303|PubMed:22252016};
GN Synonyms=PKS9 {ECO:0000303|PubMed:22252016};
GN ORFNames=FG10464, FGRAMPH1_01T08165;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP IDENTIFICATION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=16278459; DOI=10.1128/ec.4.11.1926-1933.2005;
RA Gaffoor I., Brown D.W., Plattner R., Proctor R.H., Qi W., Trail F.;
RT "Functional analysis of the polyketide synthase genes in the filamentous
RT fungus Gibberella zeae (anamorph Fusarium graminearum).";
RL Eukaryot. Cell 4:1926-1933(2005).
RN [5]
RP INDUCTION, FUNCTION, DOMAIN, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=22252016; DOI=10.1111/j.1462-2920.2011.02696.x;
RA Soerensen J.L., Hansen F.T., Sondergaard T.E., Staerk D., Lee T.V.,
RA Wimmer R., Klitgaard L.G., Purup S., Giese H., Frandsen R.J.;
RT "Production of novel fusarielins by ectopic activation of the polyketide
RT synthase 9 cluster in Fusarium graminearum.";
RL Environ. Microbiol. 14:1159-1170(2012).
RN [6]
RP INDUCTION.
RX PubMed=23290226; DOI=10.1016/j.ijfoodmicro.2012.10.016;
RA Soerensen J.L., Akk E., Thrane U., Giese H., Sondergaard T.E.;
RT "Production of fusarielins by Fusarium.";
RL Int. J. Food Microbiol. 160:206-211(2013).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=27983606; DOI=10.3390/molecules21121710;
RA Droce A., Saei W., Joergensen S.H., Wimmer R., Giese H., Wollenberg R.D.,
RA Sondergaard T.E., Soerensen J.L.;
RT "Functional Analysis of the Fusarielin Biosynthetic Gene Cluster.";
RL Molecules 21:0-0(2016).
CC -!- FUNCTION: Reducing polyketide synthase; part of the gene cluster that
CC mediates the biosynthesis of fusarielins F, G and H, decaketide
CC compounds with 5 methylations and a decaline core that act as
CC mycoestrogens as they stimulate growth of MCF-7 breast cancer cells
CC (PubMed:22252016, PubMed:27983606). The initial compound in the pathway
CC is produced by the reducing polyketide synthase FSL1. FSL1 lacks an
CC active enoyl reductase (ER) domain and biosynthesis of fusarielins
CC relies on the trans-acting enoyl reductase FSL5, before it is released
CC through hydrolysis catalyzed by the thioesterase FSL2 (PubMed:22252016,
CC PubMed:27983606). Fusarielins F, G, and H have a C11=C12 cis double
CC bond and is fully reduced between C10 and C11 and between C12 and C13.
CC FSL3 can be involved in the formation of the C11=C12 cis double bond by
CC moving a hypothetical C10=C11 or C12=C13 trans double bond to form
CC prefusarielin (PubMed:27983606). Prefusarielin is oxygenated at C15 and
CC C16 by the cytochrome P450 monooxygenase FSL4, resulting in fusarielin
CC F, which subsequently is epoxidized into fusarielin G by the same
CC enzyme (PubMed:27983606). The final step in the pathway is a reduction
CC of the carboxylic acid moiety to yield fusarielin H via a still
CC undetermined mechanism (PubMed:27983606). {ECO:0000269|PubMed:22252016,
CC ECO:0000269|PubMed:27983606}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250|UniProtKB:Q9Y8A5};
CC Note=Binds 1 phosphopantetheine covalently.
CC {ECO:0000250|UniProtKB:Q9Y8A5};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:22252016, ECO:0000269|PubMed:27983606}.
CC -!- INDUCTION: Expressed during sexual development (PubMed:16278459). Is
CC not expressed during infection of wheat plants (PubMed:23290226).
CC Expression is positively regulated by the fusarielin biosynthesis
CC cluster-specific transcription factor FSL7, probably via its binding at
CC the 5'-CGGNNNCCG-3' motif present in the promoter of all the cluster
CC genes (PubMed:22252016). {ECO:0000269|PubMed:16278459,
CC ECO:0000269|PubMed:22252016, ECO:0000269|PubMed:23290226}.
CC -!- DOMAIN: Multidomain protein; including a ketosynthase (KS) that
CC catalyzes repeated decarboxylative condensation to elongate the
CC polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects
CC and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain
CC that reduces hydroxyl groups to enoyl groups; a methyltransferase (MET)
CC domain that transfers methyl groups to the growing polyketide; a
CC ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and
CC an acyl-carrier protein (ACP) that serves as the tether of the growing
CC and completed polyketide via its phosphopantetheinyl arm (Probable).
CC Lacks an active enoyl reductase (ER) domain that reduces enoyl groups
CC to alkyl groups, and biosynthesis of fusarielins relies on the trans-
CC acting enoyl reductase FSL5 (Probable). {ECO:0000305|PubMed:22252016}.
CC -!- DISRUPTION PHENOTYPE: Leads to significant increase in growth
CC (PubMed:16278459). Abolishes the production of fusarielins F, G and H
CC (PubMed:22252016, PubMed:27983606). {ECO:0000269|PubMed:16278459,
CC ECO:0000269|PubMed:22252016, ECO:0000269|PubMed:27983606}.
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DR EMBL; HG970332; CEF75886.1; -; Genomic_DNA.
DR RefSeq; XP_011319443.1; XM_011321141.1.
DR AlphaFoldDB; I1S166; -.
DR SMR; I1S166; -.
DR STRING; 229533.I1S166; -.
DR GeneID; 23557369; -.
DR KEGG; fgr:FGSG_10464; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G08165; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_37_5_1; -.
DR InParanoid; I1S166; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; 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; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF20; HYBRID PKS-NRPS SYNTHETASE APDA; 1.
DR Pfam; PF00698; Acyl_transf_1; 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; PF08242; Methyltransf_12; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
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; 1.
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 2: Evidence at transcript level;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..2642
FT /note="Fusarielin synthase FSL1"
FT /id="PRO_0000444959"
FT DOMAIN 6..450
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348,
FT ECO:0000305|PubMed:22252016"
FT DOMAIN 965..1280
FT /note="PKS/mFAS DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT DOMAIN 2556..2635
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:22252016"
FT REGION 566..890
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22252016"
FT REGION 965..1279
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22252016"
FT REGION 965..1101
FT /note="N-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1126..1280
FT /note="C-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1423..1622
FT /note="Methyltransferase (MET) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22252016"
FT REGION 2244..2423
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22252016"
FT ACT_SITE 179
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 318
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 370
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 659
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 997
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 1189
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT MOD_RES 2595
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2642 AA; 286924 MW; F23B2B3301E70356 CRC64;
MQGPTNEPIA IIGTGCRFPG GSNTASKLWD LLKDPKDVSK EVPEDRFNLD RFYHKDSSHH
GTANVRRSYL LDEDVRLFDT QFFGISPGEA QAMDPQHRVL LEVVYEAIES AGKTIHGLHN
SDTAVYVGLM CTDYYVIQAA DLNSVPTYNA TGVANSNASS RVSYFFNWHG PSMTIDTACS
SSLVAVHEAV QALRNGTSRM AVACGTNLIL SPLPFISESN LSMLSPTGKS RMWDADADGY
ARGEGVAAVV LKPLSAAIED NDVIECIIRE VGVNQDGKTR GITMPSAQAQ ASLIRQTYAK
AGLDPATPEG RCQFFEAHGT GTPAGDPQEA EALKTAFFPN ETDSVTNGTN GLLSEADNLL
VGSIKTVIGH TEGTAGLAGL IKACMALKHG AVPPNLLFNR LNPALEPFTK HLSIPTSLTP
WPTLLTNVPR RASVNSFGFG GTNAHAILEA YSQAPQNSFA TPSSSPLVVP AIPFVFSAAS
ETSLRGVLES FLEYLNTSKD KDESLDLTSL AYILSTKRTV LSQRVSIIAS TFEQLLEKVE
AVLDDSASSV VGSKAATLSH PALLGVFTGQ GAQWATMGTK LMRSNPLAQS VIQDLDAVLA
SLPECHRPRW SLGRELLADT TSRIKEAELS QPLCTAVQIM LVDLLKANGV QFQGVVGHSS
GEIAAAYAAG FVSSADAIKI AYYRGYFAKL ASGSSSTGKD SSVKGSMMAV GTTYEDAIEL
CQLEDFRGRI SLAAHNGPNS VTLSGDSDAI NQAHFIFSEE EKKFARLLKV DTAYHSSHMQ
PCVSPYTEAL QACGIVAREP ASDAPKWFSS VRSGKPVLDV DGLDCQYWVD NLLSPVMFHE
AVQGCLDSSD TYNAILEIGP HAALKGPLDE SVLELMGNKL PYTSALVRGK DDIESFSTAL
GFLWTQFGNQ CVDLGTFQKR VSKDTGSKLC STMDDLPTYA WTHDKPLWAE SRSTKLFRTM
PGSFHDLLGI QTADGTAEEW RWQNILKTKE LPWMVGHALQ GQIVFPGTGY IALAMEASLQ
IAQGRPVSKI DLYDLEIRKA IAVNESASGT ELLVTMTNVS AIHPDVETIT ADFATYSTIS
RESGSMALNC CGKVCIFLQT ETVTTTGSDG HAAEQFATRS TPVPGMAGID VERFYSAMQH
DLGYMYSGPF RGLSRLSRKL GFSEGSIQRP PFGEDGSETT LIFHPGMLDN ALQGLFAAYS
APGDGRLWSM RAPTACRRVS LVPSLCGPNM TEEVDFDCTL TDSRDDFITG DVEVYASGYS
QRIIEIEGLS FSPFAAATDR DDRQLFQEQI WCVNEADGPL VLGNMAPTFE ERTKALDAER
AAFFYLKKLH LSVPSDQRSQ LPWYRQSLLD NAERLYDLVC SGTHSYAPQS WIQDTKEDVY
AMMESYGPQD ADFNLTKAVG ENLPLPDVIK GDTNILQYMT QNNYLDRYYT HAIGFGWLNV
LISGVVGQIA DKHPKMRFLE IGAGTGGATG AVLDRIGQAY SSYTYTDISS GFFERAVDKF
QDHAGKMLFK MLDIEKDPVS QGFPEHSYDI ILAANVLHAT KNLTETLQNT RRLLKPGGFL
VLMEILGNDV MRIGLVMGGL PGWWVGKDDG RRWGPTITLE EWDTLLKGTG FAGVDTNTPM
PDKVQMPGSV FVAQAVDDRI VKLRDPLQHD ALPSAATDHV NGIQNGHTPS PTISKGTSHL
VVIGGSSTSG SKLASDIIRV LSPLFAEIIH IPQLDSKDAI AKIPSNVDLH ILSLTECDTG
GTFFHNISNT AWQNFQHLLA TSPASLLWVV PNTRSGNPLG AIGTGLFRSL FYEIPETKFQ
VLDLDEKATG YLSGCAGLIA KLVQQLRLVT DTSSARGPST LTPETSEDDL QSVNDGTATV
EMLWTVEPEL YLHDGRLYIS RVRLQKAQND RYNSWRRPIL QLTESKSTVD PSLSTSSLGR
QTSLELQWKD DAYYNLKEIN WFAKPLSTDS ATIDVSCSLA SCLKTPAGFF FVQVGTDVNT
GEKKLCLSTE NRSRVTVHSS WTETLKQEHD VADGQYMSFI VADMIVQQIM YMLPPTGILL
LHEPDPGLAS LLTRQLANIG RKVVFTTTRS DKSTNLLSKA NWIFMHPRLN KRLIESALPH
GVTFFIDCGQ AEDVIHEGSH GKDHGLGLRL HNSLSRTCVK RTLQDLTSRT ASVAPHEATG
EVVKLLHRIT TFAAAQLNSV PDGAPLKVKS LSEIVSRAKT RALATAEGCS TGPFCLVNWH
AESQVPISVA PVWDRDDLFR SDRTYWMLGL TGDLGRSLAE FMISRGARHV VLSSRTPQPD
EMWVERQQKK YGATVVYIAV DLTSLDSVQK AHKQIVKSMP PLAGVANGAL VLKDSSVAKM
TIEQLQAVLR PKVDGTLHLQ SVVDANSGSE EQPLDWFIAF SSIVGTTGNL GQAAYSAANG
FLKAWVSQQR SMFGHNAAVI DISRVLGVGY VERETQSNSG RLTREQTDRL MNRTGTLAMS
ETDLHQLFAE AVVAADHCSA SNTGLSVGAR DAEIITGIAP ISSAQAEDVF WARNPRFGLL
VIDSNAAVGG DDQDGKGSER RQVPVKTQLA AANTPQEVTS VLTSCIVTKL RASLFLSASD
SFSETVALVD QGVDSLVGVD IRTWCIKELD VDVPVLKILG GASVVDLADY ILESLPVKEK
SK
//
