MYCA_MYCTT
ID MYCA_MYCTT Reviewed; 4011 AA.
AC G2Q9A5;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Hybrid PKS-NRPS synthetase mycA {ECO:0000303|PubMed:27960349};
DE EC=2.3.1.- {ECO:0000269|PubMed:27960349};
DE EC=6.3.2.- {ECO:0000269|PubMed:27960349};
DE AltName: Full=Myceliothermophin biosynthesis cluster protein A {ECO:0000303|PubMed:27960349};
GN Name=mycA {ECO:0000303|PubMed:27960349}; ORFNames=MYCTH_78013;
OS Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799)
OS (Sporotrichum thermophile).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces.
OX NCBI_TaxID=573729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799;
RX PubMed=21964414; DOI=10.1038/nbt.1976;
RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA Tsang A.;
RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT Myceliophthora thermophila and Thielavia terrestris.";
RL Nat. Biotechnol. 29:922-927(2011).
RN [2]
RP FUNCTION, DOMAIN, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=27960349; DOI=10.1021/jacs.6b10452;
RA Li L., Yu P., Tang M.C., Zou Y., Gao S.S., Hung Y.S., Zhao M., Watanabe K.,
RA Houk K.N., Tang Y.;
RT "Biochemical characterization of a eukaryotic decalin-forming Diels-
RT Alderase.";
RL J. Am. Chem. Soc. 138:15837-15840(2016).
CC -!- FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that
CC mediates the biosynthesis of myceliothermophins, mycotoxins that
CC contain a trans-fused decalin ring system connected to a conjugated 3-
CC pyrrolin-2-one moiety and that have potential anti-tumor properties
CC (PubMed:27960349). The polyketide synthase module (PKS) of the PKS-NRPS
CC mycA is responsible for the synthesis of the octaketide backbone
CC (PubMed:27960349). The downstream nonribosomal peptide synthetase
CC (NRPS) module then amidates the carboxyl end of the octaketide with a
CC leucine (PubMed:27960349). A reductase-like domain (R) at the C-
CC terminus catalyzes the reductive release of the polyketide-amino acid
CC intermediate (PubMed:27960349). Because mycA lacks a designated
CC enoylreductase (ER) domain, the required activity is provided the enoyl
CC reductase mycC (PubMed:27960349). Following mycA-catalyzed construction
CC and release of aminoacyl polyketide aldehyde, Knoevenagel condensation
CC yields the expected ketone (PubMed:27960349). This C18 keto acyclic
CC precursor is the substrate of the Diels-Alderase mycB, that catalyzes
CC the Diels-Alder cycloaddition to produce myceliothermophin E
CC (PubMed:27960349). A yet unknown oxygenase involved in the production
CC of myceliothermophin A, via substitution with a hydroxyl group at the
CC C21, has still to be identified (PubMed:27960349).
CC {ECO:0000269|PubMed:27960349}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 12 H(+) + L-leucine + 8 malonyl-CoA + 9 NADPH + 4 S-
CC adenosyl-L-methionine = (5S)-5-(2-methylpropyl)-3-
CC [(2E,6R,8E,10E,12E)-6,8,10,12-tetramethyltetradeca-2,8,10,12-
CC tetraenoyl]-2,5-dihydro-1H-pyrrol-2-one + AMP + 8 CO2 + 8 CoA +
CC diphosphate + 7 H2O + 9 NADP(+) + 4 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:67288, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57856, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:169930, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:27960349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67289;
CC Evidence={ECO:0000269|PubMed:27960349};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:27960349}.
CC -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC (C) domains) which when grouped together are referred to as a single
CC module. Each module is responsible for the recognition (via the A
CC domain) and incorporation of a single amino acid into the growing
CC peptide product. Thus, an NRP synthetase is generally composed of one
CC or more modules and can terminate in a thioesterase domain (TE) that
CC releases the newly synthesized peptide from the enzyme. Occasionally,
CC epimerase (E) domains (responsible for L- to D-amino acid conversion)
CC are present within the NRP synthetase (Probable). MycA contains also a
CC polyketide synthase module (PKS) consisting of several catalytic
CC domains including a ketoacyl synthase domain (KS), an acyl transferase
CC domain (AT), a dehydratase domain (DH), a methyltransferase domain
CC (MT), and a ketoreductase domain (KR) (Probable). Instead of a
CC thioesterase domain (TE), mycA finishes with a reductase-like domain
CC (R) for peptide release (Probable). MycA has the following
CC architecture: KS-AT-DH-MT-KR-PCP-C-A-T-R (Probable).
CC {ECO:0000305|PubMed:27960349}.
CC -!- DISRUPTION PHENOTYPE: Completely abolishes the production of
CC myceliothermophins A and E. {ECO:0000269|PubMed:27960349}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000305}.
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DR EMBL; CP003003; AEO57197.1; -; Genomic_DNA.
DR RefSeq; XP_003662442.1; XM_003662394.1.
DR SMR; G2Q9A5; -.
DR STRING; 78579.XP_003662442.1; -.
DR EnsemblFungi; AEO57197; AEO57197; MYCTH_78013.
DR GeneID; 11512495; -.
DR KEGG; mtm:MYCTH_78013; -.
DR VEuPathDB; FungiDB:MYCTH_78013; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_37_4_1; -.
DR InParanoid; G2Q9A5; -.
DR OrthoDB; 19161at2759; -.
DR Proteomes; UP000007322; Chromosome 2.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR013120; Far_NAD-bd.
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; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 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; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF51735; SSF51735; 3.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Isomerase; Ligase; Methyltransferase;
KW Multifunctional enzyme; NADP; Oxidoreductase; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..4011
FT /note="Hybrid PKS-NRPS synthetase mycA"
FT /id="PRO_0000450500"
FT DOMAIN 2429..2504
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3541..3621
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 11..536
FT /note="Ketoacyl synthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27960349"
FT REGION 576..903
FT /note="Acyl transferase (AT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27960349"
FT REGION 978..1287
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27960349"
FT REGION 1434..1626
FT /note="Methyltransferase (MT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27960349"
FT REGION 2138..2311
FT /note="Ketoreductase (KR)domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27960349"
FT REGION 2519..2607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2604..2975
FT /note="Condensation"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27960349"
FT REGION 3009..3414
FT /note="Adenylation"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27960349"
FT REGION 3525..3544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3671..3978
FT /note="Reductase-like"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27960349"
FT COMPBIAS 2540..2582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 185
FT /note="For ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2464
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3581
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 4011 AA; 434115 MW; F4A6EC728782E18A CRC64;
MVQTPRQKKF GNEPIAIIGS ACRFPGAAST PSKLWELLRK PKDLLTKIPP NRFNADSFYH
PDGAHHGASN VTESYFLEED PRLFDAAFFN VKPVEAHSID PQHRMLLEVV YESLEAAGQS
IEGLAKSQTG VFVGLMCADF SDHILRDLDA IPTYMATGTA RSLISNRISY FFDWHGPSMT
IDTACSSSLF AVHQAVQLLR SGDSDLAVAA GSNLILGPEL YIGESKLKML SPTGRSRMWD
ADADGYARGE GVAAVILKRL SDAIRDGDHI ESIIRESGIN SDGRTKGLTM PNELAQADLI
VRTYQKAGLD PTKEEERCQY FEAHGTGTEA GDCREAEGIS RAFFGYQGGN EGPAPPSQSE
KLYVGSIKTV VGHTEGTAGL AGLLKASLAI QHSTIPPNML FERLSPKVAP FYKGVEIATE
AKPWPKASDV RRASVNSFGF GGANAHVILE NYEPPAVAAA GTGAGAGDAA SQTSFTPFVF
SAASETALEG VLEAYAAHLR ENPDLPLRDL SYTLHSRRSA LGVRAALPAV ASTQQLANSI
SDHLELARAG RNDKSAGQGA SIGSRPIAAT PRLLGVFTGQ GAQWAAMGKE LIQGSAFVRD
RIKSLESALS DLPASARASW SLTDELLADA ASSRLGEALL AQPLCTAVQI VLVDLLREAG
IEFAAVVGHS SGEIAAAYAA RIISAEEAIK IAYYRGLCVE EHVKTEGAMM AVGTSYEDAT
ELCNLDAFSG RLGIAACNSP SSVTLSGDAA AIREAKDILD DEKKFARPLK VNKAYHSHHM
AACSAPYKQA LEACNIEPRQ LAEEEGGCVW YSSVYPGTAM GTTAAHIEDL KGEYWKDNML
RPVLFAQALE TAIERNEDSP FNLVIEVGPH PALKGPASET LTALYGKKQL PLPPYTGTLS
RGSGDIAALS VTLGTAWSRF GSPFVNFAQY EALLTGEPRS ARKVVPNLPT YKWDHDKVFW
HDTRLSRAMR NRKELPNPLL GRRIPDGVTD EMRWRNIIRP SELPWISGHQ LQGQMVYPAA
AYLSTAIEAC AFLAEGSVVE SVEIRDFDLG KALVFDGNTE QTGVETLFSL SNIVKKGPKQ
ITANFAFHAA LGADADVLSR LGSGRVIVTL AGTGTGAGTG RLLLPPQRAP EPADTAEVRE
DEFYASLEKL GYEYTNDFRA LSGMRRKLDH GSAYVRVPGH ELAADAVLVH PALLDCALQA
IFLAYWYPND GSLDQLQVPT GIASLTVNTS LCRQDLAEGV RLPLESFLTE DPLSTATIGG
DVEVYGRDGR TPLIQVQGVR ITPLATRTGQ ADRQLFMENV WGPGAPDGTL AADNRAGAAD
FELASDLERL TIYFMRKLVR DIPPSQRQGL EWHHEALFDF VEHVLEQTAN GRQRFCKPEW
LDDTWESISH IRAKHPDSIE VELTHAVGEN LAAAVRGETQ ILQHMFKDNL LNRYYVEALG
IRETTAFLAR TVAQIVHRYP HMDILEIGAG TGGATKAIFR EIGRTFSSYT YTDISTGFFE
KAQEVFAATA DKMIFRALDI EKDVVEQGYR EGAYDLIIGS LVLHATKSLD KTMRATRRLL
KPGGYLVLLE LTNLDVLRTG FAMSGLPGWW LGRDDGRRYS PCATSARWHQ VLLGAGFSGI
DTITPEVDVL PRPFSVIVSQ AVEPRVNLLR EPLSHPAESN ASAADGGELV IVGGQSLATV
ILIDSVLDLT RHFGFAVTRL SSLDEFDAAA VSPTALVLNL AELDQPVFSN LTGETMRGLQ
SMLDYQRTIL WVTQGCRAEQ PYMSMSVGLG RTVALEAPGV KLQFLDLDIS RKPNSKLVAE
ALIRLRFTRD EGSTRGILYS TEQELVEDDG RILVPRLLPI RPANERYNSS KRKITKLTEV
GAESPALVLA STDAGYAVYE GASDDARAGA SDDTAIIRVT ASTLLPVIGN LYGVLGQEKD
SGSWVLGLSS TNGSHVAVPR GQVRLVGDAI LKEEAQQQQR LLLLALLAVE AQSSQILSAV
PRDSKLLVNE PPAGLAGSLV RRAAERGTTV VFTASTTDAA DLGLPHGHPV VSLSPLSSKR
AVRAALPADV ALFLDCSAEP EGVGLGSLIA ACVPPSGQSI KLAELGEKLR QQPTLVDAPP
SDTELASLPT LVDWSSGDKV PVSLQSVDSL IRFDGAKTYV LFGLTSDLGR SLVDWMASHG
ARNVVMTSRR PNIDPKWLEE RRARGIRIQA FANDITDPAA VEDLVNSIRR SFPPIAGIMH
GAMVLEDVPF SEMSLEIMNK VVRPKVMGTI HLDRLFQDEQ LDFFVFFSSL ASASGNRGQS
NYSAANMYMT AKTFERRRKG LAASVLHLGA VMGIGYVMRE ASEIVFPAIR RAGFQWMDER
AFRQCVAEAI LAGRPDSGRS PEIVTGLRVI NVDEEEPAPW MDNPRFQHCI VRGGTDSGAK
KNQGGAAAGV KTRLLEAATP EEVLDIIRDS FLQKLQIMLQ TELQTDDERA NILAANAEDT
GIDSLVAVEI RSWFQKEMDV DVPVLKILGG ATMADLVAFA HEKLPEGLTP NLGNESAAAA
AAAAAERSQS RVEITPAPDA VDTSRTSTTV FSAPPTLDPA SSSTGSDHPT SVTSSGHTTP
AHELETGLSP PSAPPCAPRE QDVERTAPMS LGQSRFWFLR SYIEDQTTFN ISFSVRLKGP
LQVDKLESAI QTLGHRHQAL RTAFVARPGQ LLPDQAVLKR SLLRLEKRQI KEAAEASEAF
EAMKNYVFAI ERGESMRLVL LSLSPSDHFL VVGYHHINMD GASLEVFMAD LMKLYTGRPL
APRPFQYPDF AAQQQLEVQQ GKMDRDIAWW QDQLAGAALF RLLGTGDLCI GMADANRFEG
DLASSVGMYL NLLPLRFRPS GDRTFRDTLK DVRRTAYAAM AHSHVPFDLV LNNLKIQRST
LHSPLFQAFI NYRAGVAEKR SLGAVEGEGE QYHFGRSAYD ISLDIMENPN SDPRLMFLVQ
EQLYSEHEAN ILADTYMHLL DLFARKPDST LGSAPAFAPE TAEEAIRLGR GNPVVSDWPQ
TIVHRVDDII QRNPDTIAVR EALGGRVWNY RQLRDRVGAI ARALLAAGVT GGSRVALFQE
PGFDWVSSLL AVMRVGAVFV PIDPGTPVER LAVIAAAARP AVALSHDATE SAQEAALAVI
RDAGGARVVN VSRGEGEGEG DVAGAGAPAN LAQPDEAAVI FFTSGTTGVP KGAIVPHRGI
TNFMEHTCDI RGPEVVLFHS ALGFDLAMWQ CFSGLAHGGT LVVAPRSMRG DPVAITGLMA
KEKITCTGAT PSEYHTWIQY GFSKLAQSTS WRIAMTGGEQ CTPKLVDDFR SLRLPGLRLW
NCYGPSEVTV GSNQAEIPLS EPPQAPVTVG KAMPNRSVYI LDDRLEPVCA GAPGEVVIGG
VGVGLGYLGN DHLTAEKFVP DPFAPAGGSA KMYRTGDRGR LTRDGELEIL GRIDGDSQIK
LRGIRIEMQD VEQAILRSAD GALASVCVTA RGEPPTLVAH AVFRPDAPVP RRDRDAFLRR
LASSLPLPQY MHPAVIVEIP SMPLNLHGKL DRRAVQELPT RVVAAKEEEE EKRPNGSSAA
PLTQQELQLR SRVWERVIPE DVLSLYTVDR DTDFFHVGGN SMLLVEVQRR VKDEFGANLT
IMRLFENSTL GAMAAAVHDA ALESAGVDAA IDWEDETALT KDLADAVPSP EERAAAGRRR
LDNNGPGGKV VVILTGATGF IGRELLARLL SSPDVAEVRC IAVRDPSRLA DVVESNPGRV
SVHAGDLTSV EETVGEEDEQ RLFADAHAVI HCGADVSFLK TYATLRRANV GSTKALARLA
LRHGLDFHYV STAATGRLLL VADPSSSPTA RGDVFGEESV AAYPPPPGWL DHYVASKWAS
EAFLERAAAR LGLRVWVHRP TSVTGPGAGE TDVMSTVMRF AKKLRAVPVS SRWRGSLDFV
PVETVADGIV GAVIRGGREH QQQQQQQETT PEEAGSVVPV KFLHHSGGLV IPIERLQSHL
EEEDGVEYRT VPLGQWIEMA VAEGLNVLVA AYLASVDEMD TDIVFQAYVK G
