ID UCSA_ACRSP Reviewed; 3948 AA.
AC A0A411KUP8;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 1.
DT 27-NOV-2024, entry version 29.
DE RecName: Full=Hybrid PKS-NRPS synthetase ucsA {ECO:0000303|PubMed:29373009};
DE EC=2.3.1.- {ECO:0000269|PubMed:29373009};
DE EC=6.3.2.- {ECO:0000269|PubMed:29373009};
DE AltName: Full=UCS1025A pyrrolizidinone biosynthesis cluster protein A {ECO:0000303|PubMed:29373009};
GN Name=ucsA {ECO:0000303|PubMed:29373009};
OS Acremonium sp.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Acremonium.
OX NCBI_TaxID=2046025;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=KY4917;
RX PubMed=29373009; DOI=10.1021/jacs.8b00056;
RA Li L., Tang M.C., Tang S., Gao S., Soliman S., Hang L., Xu W., Ye T.,
RA Watanabe K., Tang Y.;
RT "Genome mining and assembly-line biosynthesis of the UCS1025A
RT pyrrolizidinone family of fungal alkaloids.";
RL J. Am. Chem. Soc. 140:2067-2071(2018).
CC -!- FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that
CC mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone
CC family that acts as a strong telomerase inhibitor and displays potent
CC antibacterial and antitumor properties (PubMed:29373009). These
CC compounds share a hemiaminal-containing pyrrolizidinone core fused with
CC a gamma-lactone, giving a furopyrrolizidine that is connected to a
CC decalin fragment (PubMed:29373009). The polyketide synthase module
CC (PKS) of the PKS-NRPS ucsA is responsible for the synthesis of the
CC polyketide backbone via the condensation of an acetyl-CoA starter unit
CC with 6 malonyl-CoA units (PubMed:29373009). The downstream nonribosomal
CC peptide synthetase (NRPS) module then amidates the carboxyl end of the
CC polyketide with a 2S,3S-methylproline derived from L-isoleucine by the
CC 2-oxoglutarate-dependent dioxygenase ucsF which converts L-isoleucine
CC to (4S,5S)-4-methylpyrroline-5-carboxylate that is further converted to
CC 2S,3S-methylproline by the pyrroline-5-carboxylate reductase ucsG
CC (PubMed:29373009). Reductive release of the completed aminoacyl
CC polyketide from the assembly line can form the 3-pyrrolin-2-one
CC structure via an intramolecular Knoevenagel reaction (PubMed:29373009).
CC Because ucsA lacks a designated enoylreductase (ER) domain, the
CC required activity is provided the enoyl reductase ucsL
CC (PubMed:29373009). This keto acyclic precursor is the substrate of the
CC Diels-Alderase ucsH, that catalyzes the Diels-Alder cycloaddition
CC (PubMed:29373009). Oxidation of the 3S-methyl group to a carboxylate by
CC the cytochrome P450 monooxygenase ucsK allows an oxa-Michael
CC cyclization that might involve the reductase/dehydrogenase ucsI and
CC which furnishes the furopyrrolizidine (PubMed:29373009). The oxidase
CC ucsJ likely plays a critical role in stereoselective reduction of the
CC C5-C6 double bond to afford the required R-configured carboxylate group
CC (Probable). Further enolization and oxidation at C5 by an unidentified
CC enzyme affords the last intermediate that can undergo oxa-Michael
CC cyclization to yield UCS1025A (Probable). {ECO:0000269|PubMed:29373009,
CC ECO:0000305|PubMed:29373009}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:29373009}.
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). UcsA 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), buaA finishes with a reductase-like domain
CC (R) for peptide release. UcsA has the following architecture: KS-AT-DH-
CC KR-PCP-C-A-T-R (Probable). {ECO:0000305|PubMed:29373009}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of UCS1025A.
CC {ECO:0000269|PubMed:29373009}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000305}.
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DR EMBL; MH375764; QBC88145.1; -; Genomic_DNA.
DR SMR; A0A411KUP8; -.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:TreeGrafter.
DR GO; GO:0016874; F:ligase 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:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:TreeGrafter.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:TreeGrafter.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd19532; C_PKS-NRPS; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation 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_dom.
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_com.
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; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013216; Methyltransf_11.
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; IPR049900; PKS_mFAS_DH.
DR InterPro; IPR050091; PKS_NRPS_Biosynth_Enz.
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 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; 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; PF08241; Methyltransf_11; 1.
DR Pfam; PF07993; NAD_binding_4; 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; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-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; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
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 Antibiotic biosynthesis; Ligase; Methyltransferase; Multifunctional enzyme;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Repeat; Transferase.
FT CHAIN 1..3948
FT /note="Hybrid PKS-NRPS synthetase ucsA"
FT /id="PRO_0000450530"
FT DOMAIN 11..440
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348,
FT ECO:0000305|PubMed:29373009"
FT DOMAIN 940..1256
FT /note="PKS/mFAS DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT DOMAIN 2275..2357
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:29373009"
FT DOMAIN 3513..3592
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:29373009"
FT REGION 548..881
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29373009"
FT REGION 940..1254
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29373009"
FT REGION 940..1079
FT /note="N-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1098..1256
FT /note="C-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1299..1460
FT /note="Methyltransferase (MT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29373009"
FT REGION 1989..2165
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29373009"
FT REGION 2381..2473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2489..2926
FT /note="Condensation (C) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29373009"
FT REGION 2950..3355
FT /note="Adenylation (A) (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29373009"
FT REGION 3483..3507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3633..3852
FT /note="Reductase (R) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29373009"
FT COMPBIAS 2397..2473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 323
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 363
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 972
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 1161
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT MOD_RES 2317
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3552
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 3948 AA; 428079 MW; D48D171412A790AA CRC64;
MGPPSQATAA NEPIAVIGSG CRFPGSASSP SKLWQLLSQP RDVLSEIPKS RFDPHGFYNK
NGETGGHSNV LHSYVLDEDI RAWDADFFKV SASEAAAIDP QQRLLMETVY EALEAGGQQI
HALRGSDTAV YVGLMGEEYS DIQGRELDMM PTYHATGTAR SIVSNRISYF FDWHGASMTI
DTACSSSLVA VHQCVQAIRS GYSRVAVAAG TNLCLGPEPY ISESTFHMLS PRGRSHMWDA
SADGYGRGEG VAAVILKKLS DAIADGDHIE CVIRETGVNQ DGRTNGITVP SPDAQVALIQ
DTYRRAGLDL ARPEDQPQFF EAHGTGTGAG DPLEAEAIYR AIGTRMAEGK RLYVGSIKTI
IGHTEGTAGI AGLMKASLAL QNRTIPPNML FNTLNPKIEP FIKKLQIPQE PRDWPDVPVK
RASVNSFGFG GTNAHAILER YEPDAYRQAE GGDAAFAGPY TFSAVSKTSL KQMLVNTLEF
LDDNPAVKPR DLAYTLNSRR STFTFRTSFA GRDVDALRKR ITASIESPDW ESQAVIRPAK
QPLKILGIFT GQGAQWPGMG KQLLDSSPSA QARIQELELA LATLQPGDRP CWSLKAELLA
EGSKSRLSQA EFAQPLCTAL QILLIDLLTA AGVQFSAVVG HSSGEIGAAY AAGVLSARDA
IVVAYYRGVH TKLARGDGDQ PGAMLAAGTT FEDAQDLVSL PELEGRIAIA ACNSPSSVTL
SGDADAIEAA VEMLSDEQKF ARTLRVDKAY HSHHMRPCSE PYVNSLRRAG VAARDPRPET
KWFSSVHAGR VLTSAAAEQL SDTYWALNMA QTVLFSAAVE EAVASEQYTA AIEVGPHGTL
KGPAIDTIKA AGRPVPTYLS CLARNMDSLD TFSTAIGQLW ATSPEGSLDL ERYSITAFGP
SQGANSPLKG FPSYPWDNKR RFWSESRRSR AFRLRPEPGH PLLGTLGADS TATDWSWHNV
LRLTSLPWVN GHQLQGQTVW PAAGYVALAV EAANQLAKGH GGLSHIIELE DLDIGKAIAF
ENDKAGVELL FSLHVNNITV VNGQKVLEAG FSSRSSVGEA STEAALNASG HIRLTITDFE
SPEPSPALPV QDSARIAMTE VDQNLFYNEL KVLGYNYTGP FRALHSLSRK LDHGRGRLAR
VSKSDMHDSE RGLLVHPGYL DAAFQAMFLA YAYPGDGQIW SLHVPVSIGR IRIDATQSRA
NADSYLTFDS ATNAVSQNNG QRGLAGDVNI FSADGQTGLV QVENIRLIPF AAASEANDAQ
VYYHNVWNTA TPDGLLASEA FKAGEGVAQE GLGQAAGILA HVVGQITHIN PHARLLQIGD
ESHEVAQRVL GKIGGAFSHY TLTSPSPDAV EEARDALHAK SRHLGFMELR PNEDFVAQGL
REQSFEVAIS ALAAHTVQDA EAYIKKIHQV LRPGGYLLML EPTLDSLRGS LSGKGKGTRG
IPTAEWHSLL LRAGFTGVET SASDSDRSGP PFNVLVSRAA NDHVNLLLEP STIPSPEARA
EHTLIVSGRS LASVRLAETM RRLLTPHTDR ISVVSTVGDL TSLDLSVRPV VLYLADLDEP
VFSHYTAEAH AGLQALWTTA QTVLWTTRGA QKHDPHSLQS IGFGRAMAVE HAHAKLNAQF
FDFAPGARVD PHALLDDLLR LQILGKRSSN TQGDFVWTKE PEIQVDELGR RWIPRLVPHS
DFNNGYNAAR RSIVADADPS RHVVEVVSSR NSDGSLQRSL LRLTVPRTAN VDSQEPLTKL
RVLYTAETPF HPPSSAQLYA SIGLDVTTSK PFVALSSTIS SIIEVPTSSL IEYNHRLAEG
PAHLHGITTS MLASLIIRTA KQDAATVLLE PSRELVSLLS KDAAAQDLKL AFVTASPATP
KSESIHLGAY STDSAIRRAL SFNIASVLDF TNRGSWSERI LKQLAPDVIV ESADSFRAHG
LAPAEIIEAF RSFIDAAPIA VQDHELVSAD DFVASQRSSP SILDWAGSST VSVSVQTPDS
QPIFRGDRTY ILFGLAGAGG LGLPLAEYMA SLGARYIVLT SRNPEVDQDL VAEYASRGVH
LRFMANDITN ENQVSNLVSE IRASWPPIAG VANGANVLND MQFKDMTHDD MVKVLRPKVE
GSKTLDRLFF DDPLEFFIGF SSISIVFGRS GQSNYDAANI FMLGLASQRR ARGLNASVID
IGPISGVGLM ARDVSENVMG LLVNHGYRKM SGRDFLQLFL NGITCGRVES GEPEELITGL
TVHPKNGDFK PTWTDNARFS HLFLNTDDSS GSSADGTGQM ESIQDLLLRS STKNDVARVL
RHAILNKMQN VLSLSDESVL DSESLLQRDT SSLGLDSLLA VELRTWMLGE LEVDLPVLKI
LSDTPIQGLV DFAVDNLPPA LAPSVTPEGK DSITEEDLTA PKAKTDAPAA APTPASATAP
GSKSDGNVSS IARSADQSPS HKDTLPQPTA ILTNATAGTK PVSPSLSVTG STSSAAGDDE
TPTSSQAASL ESSQVIDSRP VIDYKPVIEK TLPMSYGQSR FWVMNQIVQD PTAFNITCDI
EISSEVDKAV LSRAVDIIGA RHEALRTCFL NDENHEPIQA VMNTSTLRLE VVSDDQSQVD
SYFEQVKKTV YDLSNGYLMR ALLVSTSKTS HHLIVGYHHV NMDSTSFVVF MSDLLKIYAG
QTLSPPKVQY PDFAQYQLQR LRNGQWASHI NYWTREFAKL PDPLPLLSIS PKASRPRPYL
TNYQNIDAET RVSATVARQI QSTSRRLKVT PFHVYTTVLQ IVLARLSGTD DVCIGMADAN
RTDIGAIDSI GNFLNLLPLR LTTDAKQSFE TLVKVTKNKI LHALSHSAVP FDVILEKVGV
QRSPTHSPLF QAFIDYRHVT EKLPFGTGFL EGKRYAVSET PYDIMVEMID TPTGEASLKI
LVQEALYTSE DAQTIMDCYI NLLDAVTKDD RQAVGKPQIF NSSKVQKALE LGQGETLNLQ
HATILPELDD IAAVQPTLTA LQDSIGGSLS WSEMKAKSIA IGRNLDQLRL APQSRVGVFQ
APEVDWVCSM LGVWRSGHIY VPLETTQGIK RLSDVAQQAR LDAILLHDPT VSLFSQLSLP
NPLPTINVSA VPFAHLTDQR HFSTLKPDDQ AMIVYTSGST GVPKGITIAH RVVVNAVRSF
LHRWPMTPQT VLQQTALSFD VSWWATVVGL ATKGSVVVAG SDSRRDPRAL TDLIVSKDIT
FTFAVPSESV SWLESGNADA LRASSWAYHC SGGEPYSLNL IDKLKTLNKP DLTAINIYGP
TETMIPNAHV VEYRTLTADD LPVPIGTTMP NYLARVVDLE GHPVPAGVPG ELIFVGPGIA
SGYVDNAALT AERFPKDSLA GPEYVKNGWD VAHNSGDHGY LDGKTGEFVL QARIKGDTQV
KLRGLRIDMQ DVEANILTAS NRQITDAIVH VRKPELNNPS ADFLLAHVVL SREARLRYPT
PADQSAFFRD IVRDLRVPDY MRPALVVALD SLPLTHHGKA DRRAIANLPL DQIASQLQKE
PVPLTNKGGL KETPVARPTR YQNDPIPRQV LSSSPFSSLD QVKDLWLDIL GTAVNAHTLD
PESDFFLVGG NSLLLIRIQG ELRKRAGLDV PLTQLFQNST LGQMASLLDG KDRAKQQGAS
GIDWVSEIKI QPNLARLRAN RAPLPQDGLV MALTGATGFL GLELTRRLID LPNVRTVHAL
SVRDSRKLSQ LQSPKLVVHS GDLSRPSLGM DSGVLAQIFK TSHVVIHNGA DVSFLKSYGS
VRATNLESTK EIAKLALQHN NVRALHYVST AGIATMLSHD LYEESIGSFP PSSSPEGYVL
TKWAAELYLE RVAAVTNLPV TIHRPTAIVG ENAPHLDVMS NILHYSQKLN TVPSMTALEG
TFQFVPVEDV ANGLVGRVVA GHSSTLSAVE YQNHNGAIED TVDVHGLAPY LSNKHGRSVT
VTPDAEWIAL ASRAGMADEV VQYMGGVNMS DRKGEKWRFP RALNGSKP
//
