ID PYTA_ASPTE Reviewed; 3861 AA.
AC P9WEZ4; A0A5M3YSW6;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 1.
DT 27-NOV-2024, entry version 18.
DE RecName: Full=Hybrid PKS-NRPS synthetase pytA {ECO:0000303|PubMed:32077283};
DE EC=2.3.1.- {ECO:0000305|PubMed:32077283};
DE EC=6.3.2.- {ECO:0000305|PubMed:32077283};
DE AltName: Full=Pyranterreones biosynthesis cluster protein A {ECO:0000303|PubMed:32077283};
GN Name=pytA {ECO:0000303|PubMed:32077283};
GN ORFNames=ATEG_00913, ATETN484_0003083500;
OS Aspergillus terreus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=33178;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TN-484;
RA Kanamasa S., Takahashi H.;
RT "Aspergillus terreus TN-484 whole genome shotgun sequence.";
RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, DISRUPTION
RP PHENOTYPE, AND PATHWAY.
RC STRAIN=MEFC01;
RX PubMed=32077283; DOI=10.1021/acs.jnatprod.9b01140;
RA Tang S., Zhang W., Li Z., Li H., Geng C., Huang X., Lu X.;
RT "Discovery and characterization of a PKS-NRPS hybrid in Aspergillus terreus
RT by genome mining.";
RL J. Nat. Prod. 83:473-480(2020).
CC -!- FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that
CC mediates the biosynthesis of pyranterreones, a family of antioxidative
CC compounds (PubMed:32077283). The first step of pyranonigrins
CC biosynthesis is performed by the hybrid PKS-NRPS synthetase pytA that
CC condenses 4 malonyl-CoA units ato the acetyl starter unit by the
CC modular PKS of pytA (PubMed:32077283). The acyl chain is then connected
CC to an L-serine through the amide bond by the modular NRPS of pytA
CC (PubMed:32077283). A tetramic acid is formed and released from the PKS-
CC NRPS pytA to give pyranterreone 5 with the help of the thioesterase
CC pytI (PubMed:32077283). Pyranterreone 5 could be methylated by pytC to
CC afford pyranterreone 6 (Probable). Both pyranterreones 5 and 6 are
CC subsequently oxidized by the FAD-linked oxidoreductase pytB and the
CC cytochrome P450 monooxygenase pytD to form the fused gamma-pyrone core,
CC resulting in pyranterreones 7 and 11, respectively (PubMed:32077283).
CC The hydroxy group at C-8 of pyranterreones 7 and 11 are dehydrated by
CC the aspartyl protease pytH to form a delta-7 double bond to give
CC pyranterreones 3 and 1, 2 accordingly (PubMed:32077283). The exo-
CC methylene of pyranterreone 3 could be reduced into a pendant methyl by
CC reductase pytE to provide pyranterreone 4, also known as cordylactam
CC (Probable). Pyranterreone 4 can be reconverted to pyranterreone 3
CC through pytB-catalyzed dehydrogenation or further oxidized to
CC pyranterreones 9 and 10 (Probable). {ECO:0000269|PubMed:32077283,
CC ECO:0000305|PubMed:32077283}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:32077283}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor pytR. {ECO:0000269|PubMed:32077283}.
CC -!- DOMAIN: The N-terminal part acts as a polyketide synthase and includes
CC a ketosynthase (KS) domain that catalyzes repeated decarboxylative
CC condensation to elongate the polyketide backbone; a malonyl-CoA:ACP
CC transacylase (MAT) domain that selects and transfers the extender unit
CC malonyl-CoA; a dehydratase (DH) domain that reduces hydroxyl groups to
CC enoyl groups; an enoylreductase (ER) domain that reduces enoyl groups
CC to alkyl group; a ketoreductase (KR) domain that catalyzes beta-
CC ketoreduction steps; and an acyl-carrier protein (ACP) that serves as
CC the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm. {ECO:0000305|PubMed:32077283}.
CC -!- DOMAIN: The C-terminal part acts as an NRP synthetase composed of
CC discrete domains (adenylation (A), thiolation (T) or peptidyl carrier
CC protein (PCP) and condensation (C) domains) which when grouped together
CC are referred to as a single module. Each module is responsible for the
CC recognition (via the A domain) and incorporation of a single amino acid
CC into the growing peptide product. PytA contains one module and
CC terminates in a thioesterase domain (TE) that releases the newly
CC synthesized peptide from the enzyme. {ECO:0000305|PubMed:32077283}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of pyranterreones.
CC {ECO:0000269|PubMed:32077283}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000305}.
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DR EMBL; BKZM02000003; GES59609.1; -; Genomic_DNA.
DR EMBL; MN699959; QIH14017.1; -; Genomic_DNA.
DR SMR; P9WEZ4; -.
DR VEuPathDB; FungiDB:ATEG_00282; -.
DR VEuPathDB; FungiDB:ATEG_04975; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
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:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd20483; C_PKS-NRPS; 1.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR FunFam; 3.40.50.720:FF:000209; Polyketide synthase Pks12; 1.
DR FunFam; 3.40.366.10:FF:000002; Probable polyketide synthase 2; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 4.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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_dom.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR013120; Far_NAD-bd.
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; 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; IPR020843; PKS_ER.
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; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; PF07993; NAD_binding_4; 1.
DR Pfam; PF21089; PKS_DH_N; 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; SM00829; PKS_ER; 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; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 4.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
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 2: Evidence at transcript level;
KW Ligase; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Repeat;
KW Transferase.
FT CHAIN 1..3861
FT /note="Hybrid PKS-NRPS synthetase pytA"
FT /id="PRO_0000450465"
FT DOMAIN 1..391
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348,
FT ECO:0000305|PubMed:32077283"
FT DOMAIN 898..1208
FT /note="PKS/mFAS DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT DOMAIN 2212..2289
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3355..3433
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 506..821
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:32077283"
FT REGION 898..1206
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:32077283"
FT REGION 898..1031
FT /note="N-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1051..1208
FT /note="C-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1581..1898
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:32077283"
FT REGION 1924..2100
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:32077283"
FT REGION 2340..2783
FT /note="Condensation (C) domain 7"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:32077283"
FT REGION 2803..3211
FT /note="Adenylation (A) domain 8"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:32077283"
FT REGION 3478..3735
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:32077283"
FT ACT_SITE 138
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 273
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 311
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 599
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 930
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 1115
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT MOD_RES 2249
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3393
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 3861 AA; 424040 MW; DE1169DC4B9C2E17 CRC64;
MPQDRFNVDA FYHPDGTHKG TTNAKYGYFL DQDLGLFDAS FFNISGKEAE AMDPQQRLLL
EVVYEALEDA GITLDEIQGS LTSVYCGCFT NDYNAMTAKD LEYYPKYTVT GTGNSILANR
ISYFYNLHGP SATVDTACSS SLVCFHLGAQ SLRDAEADIS IVVGSALHFD PNIFITMTDL
GMLSTDGRCR HGDAAGSGYV RGEGIAAMVL KRQDRAQADG DHIRAVVRGT GVNHDGRKQG
ITLPSARAQA DLITSTYERA GLEPAETTYV ECHGTGTKAG DPRELRAVHE VFCRHRPDTL
HVGSVKTNIG HLEGASGIAG LMKATMALEK KIIPPNMHFS TPNPEVDFEN WKLEIPTKPK
VWEMGRRTIP RRASINSFGY GGTNAHAILE EYSSSGSTTT ACQQPIVSLP PDLAAMVERR
PYLVPLTSHS ERAGELWAGR LAQYLAKNEP SVADVALSLS TRRTMHRFRS FAVSADMEMV
IERIRDPPPS AAWKSKLDTI PRIGFVFTGQ GAQWFGMARS LLEQCPLFLQ TIRKCDRILQ
ALPSHRPTWS VEAELQKSQE DTMLGRTEYS QPICTAVQLA LVDVLAHWGV KPSGVVGHSS
GELAATYAAG LLSFENALVA AYYRGVHMGS GAAAPGSVPG AMMAVGMTEA EVTAELEPYR
GRIAIAAMNS PSSFTVSGDE DAIVELQQAL TDRKVFARRL QVAQAFHSHH MFPLAPGYKE
ALSAYPGFKA NKEASAIMVS SVTGRYAGPE TLGPDYLAAN MTGMVKFSDA LTELVLDEED
QQRIDVLLEI GPHPALKGPS NQTLDPLKLK LPYFGTLDRK QDAYESLLAT TGQLFSLGYP
VDLRKVNKNQ FLDTTAQVVS VGAQARRLEL PSYAWDHHDR YWAETRHIRE HRLRPSRHSI
LGARVPGSLE TRPRWRNYLR VSEVPWLPDH SIDGKTIFPA AGYINMVIEA AATMVDGSIR
EFELVDVSVK SALVVSDKDV GTETIVELAP ALESAETSSS LWKQFVVLSV DEAGNQREHC
TGMIRTESGS PKAIQNSSNY SSVDAFRRRS FRSTECMQYY HRLHSMGLQY GPTFQLVAGN
VESGDGIAIA PISWKPTMYP REDTDLSILH PALLDACLHP VFSSIEGKLG NNLSAPYVPT
FIRSLRVSGL LDAWKRSEAG FEAEVLVETD ALGPRTATND LRLHLSDGEL LFDIKGLRLT
SLGSNAADDT KRSLFFGTQW KPMFTGLEWA PKEEYNLTTL VELYVHQHPN SKILHVTPSL
SSTESILPAF KGIADSERRN ISGLVILPAG AAATDFGALV DRGNGLVSVV EDTEDAFDLV
IVSTDIDMSA IRGRVADNGF LVTLNPTKTP LDTHAFHILY ASSVLKIWHN KHSPNNGSVG
TLTIVMPPQP TPGTRKLADI IKSQRQGPTS ECDFLSLIQS SNELHGDVVV LASLDSNLYF
GSALSRAEDF QAAQALLTQE RQGNVIWLTR GGLMNVASPE QALILGLARS ARSENPELRL
VVFDIDPTAD ESQTAQLTSH LMDDSIREDE IAERGGRLYI PRVVASDDLN SRIPNGVRSE
PTIQPLYQKD RPLALRIGRP GLLDTLMFSD DTDLTSRQLQ PDDLEIEVKA SALNFRDIAA
SMGIIDDFKL GDECAGVVLR VGSNVSSTDF AVGDRVVAWR PGQGAHRTIL RNPACLCYRL
QGQMPFSVAS SIPLVLTTAY YSLVDTARLQ RGETILIHSA AGGVGQMAIQ ISQNIGATII
ATVGSAEKRA FLIDKYGLED SHILSSRDDS FVEGIRRLTN GRGVDVVLNS LAGPLLLSTW
ASVAPFGRFV EIGKRDIHQN SRIPMDPFRR NVSFASVDMI TVYERNQPLG ARVFQESCAL
VHEGKIKPPQ PITEVPYADV QRAFRMLQTG TTSGKIVLIP GPDDRVLVEQ PRFHRRQLFD
AHKTYLLVGG LGGLGRRLSE WLFQRGARHL AFLSRSGKSR PEARETVEWL EARGVEVKVF
SGDATDSTAV NTAVSQVDGS SHRLAGVFQA AMVLQDAPLG QMTFAQWQRC MAPKIQGAYN
LHNATASLPL DFFVCFSSVS AILGSKAQAN YSAANSYLDA LCAYRRSIGL VGTTMNVGMV
VGVGAVSEDA QLQTVMERIG YDAVNEEELF AQIGAAVCPV GSQDKLALVD SQGRDAHQII
TGVNLRRPTY FWANEPRFRN LYANHDFAGS SEGKNKKQDV MSQLREAPDE AARVSILTLR
FLEKIASVLS VDQSTLQPNR SLGDYGLDSI VAIEIRQWFF KAVGVELAMF DILSSRSIQA
LIEKVASLIV LKNEAESSTA ANADVQKNAK RAANRTADST ISLLPPIDGA SIVEMPIMEV
PMSSYQRRLW FMHNLSADPS FLNLPIIFRL RGQPHGPLIR RVLEELKRRN EILRTAYSEG
EEFSQQVVMD DCTTELPAVD FSTDGDTESS LSNYVKALQQ EQMDIEDGVV MKAALAKLSE
DRHALVLIFH HICIDRGSSQ SFLEQFTSLY DAMRKERNLA SVARPAVSYG EFSVWHNTLL
RSTDMQPSLA FWKSVYEDRP ATAMQLLPFA KGDRPETNDY RRHVHKTTLK KTLLQRMKRI
CSRLGVTPAQ FLMAGLRAFL YRHTEEEDLT IHLVDGNRPH PAVNDTLGFF VNVVPVRCRI
DHSGSFEDVL RQIKDLVISA LQHSQFPFDA IIDAVGAART TSHFPLGQVI LNYQVHGTMP
VYSAGDFDIT EVQGDDIPTA CEIGLEALED PAEGLKLRLE YSSTLYGEDD MARFLDNFVA
FLASTIHDYR QPVSEVNMVG SKELEFLKAN MFNLNFVPNT WGGMSVPERI LAMAREYPQE
VAVESSEGVN NLTYASLVTQ ASDIARAIID SGIQPASKVG LFALPGPTAV ASMVGVLFAG
CGYVALDPDF AKERLAFMIT DSGAKLVLAG DGLEDSACAL STVPVLASER IQHSGKMIDS
PVPTEGNFPF YTIYTSGSTG TPKGVVLSQS NTQQMLSTLH HDYRFSPADR FLHHSSISFD
LSVVQVFSAL TTGARVCVAG AEIRKDPLAL ATYMAAAQVS ITYFTPTQFA MLIESAGSIL
EGMTNYRIAY FAGERLPVRL VKAFYDLKTP AKLYNTWSPS ELVVQTTIQS VAYPADDALN
IPIGFPMANT RHYILDSKAK PLPMGVVGEI VVGGAQVGLG YINRPEINER AFLPDPFCSE
EDHRRGWGRM FRTGDKGRFL PGGNLEFHGR IAGDKQVKLR GYRVDLSEVE HRIFVESNKG
STDVAVVDLA VVAREIAGET SQGNGTDDRQ LIAFVVPRQA PPRERLSMFA FQLNQMAGKY
LNPYMLPAAY QFVERLPTTI GGKVDLQRLL NCPLNLVFPV EENVNPQSPA GETSDDQDVV
LKAVIQGFRQ ILKLPSTRAV GPGDSFFALG GNSLLLMRLQ ARLKRALKLP LPLNMMFKTP
TPAAITQLMT GRISSSATPT VQTPATDAVD WEVETRLGDD VKPSPVNIGR SQVNSVLVTG
VDSFIGVHML ATLLEDQSID NIYVLGSQKQ IQVTDIYQSF DHYHLSGLLP SREELDLRIR
SVPGNLASPQ FGLSAAAFRQ LARNIQSIYH LGGYVSLLRS YDALQDSNVR PIHDIIHLAT
LGRVNTAIHH LSTWSVPHLQ TWSTTTHQRG KGQPSITATE VSASHFIPES SGRLGYFKSR
WAAEMILEKA AERGFAVAIY RASAVTADRR TGIPEPKDDF IRTMILSMLQ TKAVPRLPAR
ERPFVVDFVP VDYITRGMHA LAMHETLNEE TTEKAPIYHL SNPQPLPLEE LPAIMEAIGG
ERGQSLPVDE WLEAVARLDT APEAQVRWGA LKEYFGLGHL MFGLDTAKTQ RALKALDIGS
CSPVDVEYLR TMLARESQRV G
//
