PYNA_ASPNC
ID PYNA_ASPNC Reviewed; 3902 AA.
AC A5ABG0;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Hybrid PKS-NRPS synthetase pynA {ECO:0000303|PubMed:24106156};
DE EC=2.3.1.- {ECO:0000269|PubMed:24106156};
DE EC=6.3.2.- {ECO:0000269|PubMed:24106156};
DE AltName: Full=Pyranonigrin biosynthesis cluster protein A {ECO:0000303|PubMed:24106156};
GN Name=pynA {ECO:0000303|PubMed:24106156}; ORFNames=An11g00250;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2]
RP FUNCTION, INDUCTION, CATALYTIC ACTIVITY, DOMAIN, AND PATHWAY.
RX PubMed=24106156; DOI=10.1002/cbic.201300430;
RA Awakawa T., Yang X.L., Wakimoto T., Abe I.;
RT "Pyranonigrin E: a PKS-NRPS hybrid metabolite from Aspergillus niger
RT identified by genome mining.";
RL ChemBioChem 14:2095-2099(2013).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=26414728; DOI=10.1021/acs.orglett.5b02435;
RA Yamamoto T., Tsunematsu Y., Noguchi H., Hotta K., Watanabe K.;
RT "Elucidation of pyranonigrin biosynthetic pathway reveals a mode of
RT tetramic acid, fused gamma-pyrone, and exo-methylene formation.";
RL Org. Lett. 17:4992-4995(2015).
CC -!- FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that
CC mediates the biosynthesis of pyranonigrins, a family of antioxidative
CC compounds (PubMed:24106156, PubMed:26414728). The first step of
CC pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS
CC synthetase that condenses 6 malonyl-CoA units to an acetyl starter
CC unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP
CC (PubMed:24106156). The enoyl reducrase (ER) domain of pynA is likely to
CC be functional during the first two rounds of polyketide chain
CC extension, to generate the saturated C-C bonds of the alkyl side chain
CC (Probable). PynA subsequently forms the amide bond between the acyl
CC chain and L-serine (PubMed:24106156, PubMed:26414728). Although pynA
CC has a terminal reductase domain, it appears to require the thioesterase
CC pynI for the release of the straight-chain intermediate from pynA via
CC the formation of a tetramic acid pyranonigrin J (PubMed:26414728). The
CC methyltransferase pynC then coverts pyranonigrin J to pyranonigrin I
CC via N-methylation (PubMed:26414728). The FAD-dependent monooxygenase
CC pynG catalyzes an epoxidation-mediated cyclization to form the dihydro-
CC gamma-pyrone moiety, followed by pynD-catalyzed oxidation of the
CC alcohol to the ketone and enolization to yield the characteristic
CC tetramic acid-fused gamma-pyrone core of pyranonigrin H
CC (PubMed:26414728). Pyranonigrin H is substrate of pynH for dehydration-
CC mediated exo-methylene formation from the serine side chain to produce
CC pyranonigrin E, before the oxidase pynE reduces the exo-methylene of
CC pyranonigrin E into a pendant methyl to form pyranonigrin G
CC (PubMed:26414728). The FAD-linked oxidoreductase pynB performs the
CC reverse reaction and converts pyranonigrin G back to pyranonigrin E
CC (PubMed:26414728). {ECO:0000269|PubMed:24106156,
CC ECO:0000269|PubMed:26414728, ECO:0000305|PubMed:24106156}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:24106156, ECO:0000269|PubMed:26414728}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor pynR. {ECO:0000269|PubMed:24106156}.
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:24106156}.
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 (Probable). Each module is
CC responsible for the recognition (via the A domain) and incorporation of
CC a single amino acid into the growing peptide product (Probable). PynA
CC contains one module and terminates in a thioesterase domain (TE) that
CC releases the newly synthesized peptide from the enzyme (Probable).
CC {ECO:0000305|PubMed:24106156}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of all pyranonigrins.
CC {ECO:0000269|PubMed:26414728}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000305}.
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DR EMBL; AM270218; CAK48258.1; -; Genomic_DNA.
DR SMR; A5ABG0; -.
DR PaxDb; A5ABG0; -.
DR EnsemblFungi; CAK48258; CAK48258; An11g00250.
DR VEuPathDB; FungiDB:An11g00250; -.
DR HOGENOM; CLU_000022_37_9_1; -.
DR Proteomes; UP000006706; Chromosome 7R.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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:0009058; P:biosynthetic process; IEA:UniProt.
DR GO; GO:0019748; P:secondary metabolic process; IGC:AspGD.
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 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; IPR011032; GroES-like_sf.
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; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
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; 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; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 4.
DR SUPFAM; SSF52151; SSF52151; 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; PS50075; CARRIER; 2.
PE 1: Evidence at protein level;
KW Ligase; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..3902
FT /note="Hybrid PKS-NRPS synthetase pynA"
FT /id="PRO_0000450056"
FT DOMAIN 2251..2328
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:24106156"
FT DOMAIN 3391..3467
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:24106156"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 32..444
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:24106156"
FT REGION 555..868
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:24106156"
FT REGION 945..1256
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:24106156"
FT REGION 1629..1945
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:24106156"
FT REGION 1971..2143
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:24106156"
FT REGION 2337..2364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2374..2816
FT /note="Condensation (C) domain 7"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:24106156"
FT REGION 2836..3248
FT /note="Adenylation (A) domain 8"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:24106156"
FT REGION 3515..3774
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:24106156"
FT COMPBIAS 2337..2351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 201
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 647
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 977
FT /note="For beta-hydroxyacyl dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2288
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3427
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 3902 AA; 429378 MW; 2158D82077AEF1AF CRC64;
MDTPLSSSEI SPRFSNTVPS SVSSMTPNAD PSVIVGLACR VPGATNPSQL WENIVAQKDL
QRKMPADRFN VDAFYHPDGT NKGTTNAKFG YFLDQDIGMF DAGFFRISGK EAEAMDPQQR
LLLEVVYEAL EDAGITLDEV NGSNTAVFCG SFTNDYNAMV TKDLEYYPKY TVTGTGNAIL
SNRISYFYNL HGPSVTIDTA CSSSLNESDI AIVVGSALHF DPNVFITMTD LGMLSSDGRC
RTFDSMGSGY VRGEGICAAV LKRRRDAVYN GDNIRAVVRA SGVNHDGIKQ GITLPNTNAQ
EKLIRRTYDL AGLDPNDTQY FEAHGTGTAR GDPIEARAIG AVFGSTRSEP LYVGSVKSNI
GHLEGASGLA GIIKATLALE ESQIPPNMHF KRPNPEIKFD EWKIQVPQDI ISWPASANGI
RRASINSFGY GGTNAHVILD AYKPEDSEAE LQAIPAISSS IPVDRPYLIP LSAHSTKAGA
LWEDKLTKYL SNEPIGRPAV SDLAVSLSTR RTMHGNRSFI IGKDMPTVLQ GLEQPPSPAA
AWTRPLKETP RLGFVFTGQG AQWFAMGRKL IQQSHLYRQT LERCDAVLQS LPDGPDWTVL
EELLRTEEAS RLKETRLSQP ICTAMQLATV CLLKQWGIEP SAVVGHSSGE VAAAYAAGIL
TFENAMIAAY YRGLYMSSGV DGSMTTDGAM MAVGLTEAEA KKEFETYTGQ ICVAAVNSAS
SLTLSGDKDA IVRLRDSLVE RKIFARLLQV AQAFHSHHML PLAPKYEEAL KNCAGFGTSP
ARVRMFSSVT ARLARPGEMG AGYWTANMTG TVRFSDALTG ILLNEEDEQN VDILVEIGPH
PALKGPSRQV MNALKLNLPY LASLTRGVND YESLLTLAGQ LFQYGFPVDL IAVNSDHFLQ
RETGMIQSEL HGKRLRDLPT YAWDHKRYWS ETRPIREHRL RKQRHSILGA RMPGIPERTP
HWRNYLRLKE IPWLADHVID GNAVFPAAGY FSMAIEAAVS MCAEDSVIKE IALRDLNVQS
ALLLSDSEEG TEVIMELRPA TQSAKSKSAL WYEFTIYSYG ESKILNEHCS GLVSVETNAL
TLPMRWESSK TFDDLAKESQ ESIPAETLYD HLTALGLQYG PSFQLLTGDV QTGPGFALAG
LDFQPSQFSV QAADLTIAHP TLLDASFHAI FPAIESALGR SLDEPLVPTF VRSFKVSGDF
LACCRESREQ KFQVTCFTRL PGPRVALSDL TVCSKESNKP LLQFNGLEVT ALGSDKTDNS
AGRSLFFRTR WQPAFTFLGP DHPAVAQKNI SEILDIFAHQ FPDTRILHVS DTVDGTRDVL
KYLGGRSNER RRFHSITPVF QTQIALEEID ALSQEWPGLV EISEPEPNAY GLVVLSSDAA
DLDSRQFVKE GGFVLALGPH PQPEGLHDVF FTKDLAVWQK STDNAQKPKQ LSLILPSCPS
QRTLDIADGM EMQHGSSVFV TRTSLAALSN EALQAEDIVV LANLDEDVLF EHSSSDQSTF
LGIKRLLTAG GKNIVWVLEG GSMDAPKPEH AMIIGLARVA RSENDQLRFV TLDLPRASTQ
ETVVRHVWRL LDRSITEDEV AVRDNCIFIP RVEADDQLNS KLRNGTNSQP REEPLGAGRP
LALKIGRVGL LETLVFEDDE QILDTQLADD EIEIEVKASA INFRDIAASM GIIDDYKLGD
ECAGIVTRIG AQVNPQDFQV GDRVAAWRPG QGAHKTIVRN PASLSYKLGD MSFVDAASLP
CILTTAYYSL VHVAHLQPGE TVLIHSAAGG VGQMAIQVAQ YVGARVIATV GSQAKRSLLK
SRYGLADDMI FNSRDDSFVR DVLDTTGGRG VDVILNSLAG KLLHATWSCV APFGRFIEIG
KRDIHENSKI DMDPFRRNVA FASVDLVTIF EKNKPLGARL LKECGTLVHK GHITPPETVT
ELPYSDAVKA FRLLQMGKHT GKVVLVPHAG DRVPVLPSTY RNQPLFKHEK TYLLVGGLGG
LGRTLAEWMV RKNARRLAFL SRSGADKEEA KRTVEWLRER GVSVTVFKGD VSRYEDVERA
VKAIDNLGGI FQAAMVLQDA PLENMSYQQW QICVEPKVKG TYNLHQATLG KQLDFFICFS
SASGSIGSKG QANYSSANCY LDALMRHRRE MGLAGTTMNC GMIVGIGAVA ANQALLKVMM
RSGYDGVNKE ELLYQIEEAV LSDNNKKVSR RGVDLHQTIT GINMTKADFY WCQKPLYRNL
YNNHEFLGQT AIKQGTKSLA SQLQGTKSVE ERTTLVLSAF IEKVADVLSV SVDSIESANP
LSAYGLDSII AVEFRKWFSR SVGVEIALFD VLGAPSIFAL VTKASGLITI TTSNDDKAEN
VDNEGAKGNE DQEVETQQGQ LNQPIPPAAA VGPVPMSSFQ QRLWFIHNFG DDKTFLNLSI
TSYLEGNPDA TILEKALNEL VNRNAILRTG YTEGDEFAEQ TVLDMPSISL ERIDVSSKPS
PTVSLQDVIQ RRRAIELEIE EGEVVRPMLV RLSDDQHALV LICHHIAIDR GSAKSSLNQL
TGIYDAIRQG RDLDMVPRPG VSYADFAVWH NRLLSSPSLQ ADLTFWKENL SGMPKTCKLL
PFAKSERPLH DDLQRTVVSG ILKKSLLNRM KRICSQSGAT PFQFLLAAFR AFIFRYTEDS
DLGILMIDGD RPHPDLEDVL GFFVNMTPIR CQDSCEGAFD QLLEATKTRT LEAMSHSKAP
FDSIVDVVKA KKTTSHFPLA QIALNYQIHG TFPVYRTQDF NVHDVQSVDV PTACDMQLEA
LEHPERGLDL RLEYSSTLYG SGDMNRFFDN FVTFMSSLIR DHRQPIAEVN LCGALEIAHL
EKNFWNTQFT QNPWGSVGVC QRIMENAAKQ PEAVAIAASD GAAITYSELV ERAQRVAASL
KASGVTERQK ICVLVDPGVD AVIALLAVLL TRSCYVALDS SFAVDRLAFM ASDCGAGVLL
FGPELQGLAE TVASKSKSGL RLLDTKKAAL CEDRFVGDLP SVNEDPFFII YTSGSTGKPK
GVVLSHANTQ QMLASVGEYF RFTSDDRFLQ QSSLCFDLSV VQIFSALTAG ARVCVAKHDI
RKDPAALAAF MHETGVTITY FTPTHFALLL EHSWETLHQC SQYRAALFAG ERLPVRIARA
FYDLQTPAVV YNTWSPSELV VQTTIHKVDK PDDDVFDIPI GRPLPNCRHY VVDAVLNPLP
AGFVGEICVG GAQVGLEYLN RPLANATSFV RDLNSTPEDQ ARGWKKMFRT GDKGSFLPNG
LLTFKGRIAG DKQIKLRGFR IDLGEVEQVL YKNASTPDGQ GIVDISVIAR DSEKSDATSP
LTDERRLIAF VIPKKPLQST QERDEYANYL HRMAQGSLNE YMCPNGYQFL ERLPMTIGGK
VDRRSLLTMK LDLAQHTTTC TDSRPVTEVA GDDAEILQGV TGQVCSLLGI DRSIAPNDNF
FELGGQSILL LRLQSRLKKK FKVTLKLQEL IHAPTPLAIA GMIQKQLKGP AGVQNENASK
SIDWSEEISL PASLMNTDYS QLSRFPRTDV SSILLTGIDT FIGLHMLATI LSNNHNATVY
VIGIHDELTA DHLVEGLTKY KLLDAHLSTE DVLSRTCAVP GKMTSPRFGL AEEAFRNLAD
KVRVIFNIAA DVSLLKTYVD LKTVNTSAIL TLIELATSSH GHLLEIHHLS TWSVPHLQTW
KKTSRTRAFA SNREEDPSHF TPPTADEYGY FKSRWAAEMY LTQAAARGVP VSIYRASSVS
GSRATNVPVP EMDFISNMIM HMIQHRAIPE INSSSLIDEA GDFVVDFLPV DALTSSMYTL
ASEESAAAPG LQVYHLGSSQ PLPLQALVDV IPSLDQSGAA GKCRVVPMQE WLRLVSEGAS
EEEQLHWMVV KKYFQHGHSM FALDKSHTVA ALKKAGKEVE FPAIDVDYLK RLLDERGPGL
KR
