LPSA2_CLAPU
ID LPSA2_CLAPU Reviewed; 3563 AA.
AC Q2PBY4;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 23-FEB-2022, entry version 69.
DE RecName: Full=D-lysergyl-peptide-synthetase subunit 1 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000305|PubMed:15904941};
DE AltName: Full=Ergot alkaloid synthesis protein ps4 {ECO:0000303|PubMed:15904941};
DE AltName: Full=Nonribosomal peptide synthetase 1 {ECO:0000303|PubMed:15904941};
GN Name=lpsA2 {ECO:0000303|PubMed:17720822};
GN Synonyms=cpps4 {ECO:0000303|PubMed:15904941};
OS Claviceps purpurea (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=5111;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION IN THE EAS CLUSTER,
RP FUNCTION, AND DOMAIN.
RC STRAIN=P1 / 1029/N5;
RX PubMed=15904941; DOI=10.1016/j.phytochem.2005.04.011;
RA Haarmann T., Machado C., Lubbe Y., Correia T., Schardl C.L.,
RA Panaccione D.G., Tudzynski P.;
RT "The ergot alkaloid gene cluster in Claviceps purpurea: extension of the
RT cluster sequence and intra species evolution.";
RL Phytochemistry 66:1312-1320(2005).
RN [2]
RP BIOTECHNOLOGY.
RC STRAIN=P1 / 1029/N5;
RX PubMed=11778866; DOI=10.1007/s002530100801;
RA Tudzynski P., Correia T., Keller U.;
RT "Biotechnology and genetics of ergot alkaloids.";
RL Appl. Microbiol. Biotechnol. 57:593-605(2001).
RN [3]
RP FUNCTION.
RX PubMed=14700635; DOI=10.1016/j.chembiol.2003.11.013;
RA Correia T., Grammel N., Ortel I., Keller U., Tudzynski P.;
RT "Molecular cloning and analysis of the ergopeptine assembly system in the
RT ergot fungus Claviceps purpurea.";
RL Chem. Biol. 10:1281-1292(2003).
RN [4]
RP FUNCTION.
RC STRAIN=ATCC 20102 / Farmitalia FI 32/17;
RX PubMed=14732265; DOI=10.1016/j.fgb.2003.10.002;
RA Wang J., Machado C., Panaccione D.G., Tsai H.-F., Schardl C.L.;
RT "The determinant step in ergot alkaloid biosynthesis by an endophyte of
RT perennial ryegrass.";
RL Fungal Genet. Biol. 41:189-198(2004).
RN [5]
RP FUNCTION.
RC STRAIN=P1 / 1029/N5;
RX PubMed=16538694; DOI=10.1002/cbic.200500487;
RA Haarmann T., Ortel I., Tudzynski P., Keller U.;
RT "Identification of the cytochrome P450 monooxygenase that bridges the
RT clavine and ergoline alkaloid pathways.";
RL ChemBioChem 7:645-652(2006).
RN [6]
RP FUNCTION.
RX PubMed=17308187; DOI=10.1128/aem.00257-07;
RA Fleetwood D.J., Scott B., Lane G.A., Tanaka A., Johnson R.D.;
RT "A complex ergovaline gene cluster in epichloe endophytes of grasses.";
RL Appl. Environ. Microbiol. 73:2571-2579(2007).
RN [7]
RP FUNCTION.
RX PubMed=17720822; DOI=10.1128/aem.01040-07;
RA Lorenz N., Wilson E.V., Machado C., Schardl C.L., Tudzynski P.;
RT "Comparison of ergot alkaloid biosynthesis gene clusters in Claviceps
RT species indicates loss of late pathway steps in evolution of C.
RT fusiformis.";
RL Appl. Environ. Microbiol. 73:7185-7191(2007).
RN [8]
RP FUNCTION.
RX PubMed=17560817; DOI=10.1016/j.fgb.2007.04.008;
RA Haarmann T., Lorenz N., Tudzynski P.;
RT "Use of a nonhomologous end joining deficient strain (Deltaku70) of the
RT ergot fungus Claviceps purpurea for identification of a nonribosomal
RT peptide synthetase gene involved in ergotamine biosynthesis.";
RL Fungal Genet. Biol. 45:35-44(2008).
RN [9]
RP FUNCTION, AND DOMAIN.
RX PubMed=19139103; DOI=10.1074/jbc.m807168200;
RA Ortel I., Keller U.;
RT "Combinatorial assembly of simple and complex D-lysergic acid alkaloid
RT peptide classes in the ergot fungus Claviceps purpurea.";
RL J. Biol. Chem. 284:6650-6660(2009).
RN [10]
RP FUNCTION.
RX PubMed=20118373; DOI=10.1128/aem.00737-09;
RA Lorenz N., Olsovska J., Sulc M., Tudzynski P.;
RT "Alkaloid cluster gene ccsA of the ergot fungus Claviceps purpurea encodes
RT chanoclavine I synthase, a flavin adenine dinucleotide-containing
RT oxidoreductase mediating the transformation of N-methyl-
RT dimethylallyltryptophan to chanoclavine I.";
RL Appl. Environ. Microbiol. 76:1822-1830(2010).
RN [11]
RP FUNCTION.
RC STRAIN=ATCC 20102 / Farmitalia FI 32/17;
RX PubMed=20735127; DOI=10.1021/ja105785p;
RA Cheng J.Z., Coyle C.M., Panaccione D.G., O'Connor S.E.;
RT "Controlling a structural branch point in ergot alkaloid biosynthesis.";
RL J. Am. Chem. Soc. 132:12835-12837(2010).
RN [12]
RP FUNCTION.
RX PubMed=21409592; DOI=10.1007/s00294-011-0336-4;
RA Goetz K.E., Coyle C.M., Cheng J.Z., O'Connor S.E., Panaccione D.G.;
RT "Ergot cluster-encoded catalase is required for synthesis of chanoclavine-I
RT in Aspergillus fumigatus.";
RL Curr. Genet. 57:201-211(2011).
RN [13]
RP FUNCTION.
RX PubMed=21494745; DOI=10.1039/c0ob01215g;
RA Matuschek M., Wallwey C., Xie X., Li S.M.;
RT "New insights into ergot alkaloid biosynthesis in Claviceps purpurea: an
RT agroclavine synthase EasG catalyses, via a non-enzymatic adduct with
RT reduced glutathione, the conversion of chanoclavine-I aldehyde to
RT agroclavine.";
RL Org. Biomol. Chem. 9:4328-4335(2011).
RN [14]
RP FUNCTION.
RX PubMed=24361048; DOI=10.1016/j.chembiol.2013.11.008;
RA Havemann J., Vogel D., Loll B., Keller U.;
RT "Cyclolization of D-lysergic acid alkaloid peptides.";
RL Chem. Biol. 21:146-155(2014).
CC -!- FUNCTION: D-lysergyl-peptide-synthetase subunit 1; part of the gene
CC cluster that mediates the biosynthesis of fungal ergot alkaloid
CC (PubMed:14732265, PubMed:14700635, PubMed:15904941, PubMed:17308187,
CC PubMed:17720822). DmaW catalyzes the first step of ergot alkaloid
CC biosynthesis by condensing dimethylallyl diphosphate (DMAP) and
CC tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:14732265). The
CC second step is catalyzed by the methyltransferase easF that methylates
CC 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-
CC methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By
CC similarity). The catalase easC and the FAD-dependent oxidoreductase
CC easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is
CC further oxidized by easD in the presence of NAD(+), resulting in the
CC formation of chanoclavine-I aldehyde (PubMed:20118373,
CC PubMed:21409592). Agroclavine dehydrogenase easG then mediates the
CC conversion of chanoclavine-I aldehyde to agroclavine via a non-
CC enzymatic adduct reaction: the substrate is an iminium intermediate
CC that is formed spontaneously from chanoclavine-I aldehyde in the
CC presence of glutathione (PubMed:20735127, PubMed:21494745). The
CC presence of easA is not required to complete this reaction
CC (PubMed:21494745). Further conversion of agroclavine to paspalic acid
CC is a two-step process involving oxidation of agroclavine to
CC elymoclavine and of elymoclavine to paspalic acid, the second step
CC being performed by the elymoclavine oxidase cloA (PubMed:16538694,
CC PubMed:17720822). Paspalic acid is then further converted to D-lysergic
CC acid (PubMed:15904941). Ergopeptines are assembled from D-lysergic acid
CC and three different amino acids by the D-lysergyl-peptide-synthetases
CC composed each of a monomudular and a trimodular nonribosomal peptide
CC synthetase subunit (PubMed:14700635, PubMed:15904941). LpsB and lpsC
CC encode the monomodular subunits responsible for D-lysergic acid
CC activation and incorporation into the ergopeptine backbone
CC (PubMed:14700635). LpsA1 and A2 subunits encode the trimodular
CC nonribosomal peptide synthetase assembling the tripeptide portion of
CC ergopeptines (PubMed:14700635). LpsA1 is responsible for formation of
CC the major ergopeptine, ergotamine, and lpsA2 for alpha-ergocryptine,
CC the minor ergopeptine of the total alkaloid mixture elaborated by
CC C.purpurea (PubMed:17560817, PubMed:19139103). D-lysergyl-tripeptides
CC are assembled by the nonribosomal peptide synthetases and released as
CC N-(D-lysergyl-aminoacyl)-lactams (PubMed:24361048). Cyclolization of
CC the D-lysergyl-tripeptides is performed by the Fe(2+)/2-ketoglutarate-
CC dependent dioxygenase easH which introduces a hydroxyl group into N-(D-
CC lysergyl-aminoacyl)-lactam at alpha-C of the aminoacyl residue followed
CC by spontaneous condensation with the terminal lactam carbonyl group
CC (PubMed:24361048). {ECO:0000250|UniProtKB:Q50EL0,
CC ECO:0000269|PubMed:14700635, ECO:0000269|PubMed:14732265,
CC ECO:0000269|PubMed:15904941, ECO:0000269|PubMed:16538694,
CC ECO:0000269|PubMed:17560817, ECO:0000269|PubMed:19139103,
CC ECO:0000269|PubMed:20118373, ECO:0000269|PubMed:20735127,
CC ECO:0000269|PubMed:21409592, ECO:0000269|PubMed:21494745,
CC ECO:0000269|PubMed:24361048, ECO:0000305|PubMed:17308187,
CC ECO:0000305|PubMed:17720822}.
CC -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC {ECO:0000305|PubMed:15904941}.
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 (By similarity). Each module is responsible for the recognition
CC (via the A domain) and incorporation of a single amino acid into the
CC growing peptide product (By similarity). Thus, an NRP synthetase is
CC generally composed of one or more modules and can terminate in a
CC thioesterase domain (TE) or reductase domain (R) that releases the
CC newly synthesized peptide from the enzyme (By similarity). LpsA2 has a
CC domain arrangement (A-T-C-A-T-C-A-T-Cyc) with 3 A and 3 peptidyl
CC carrier (PCP/T) domains, 2 C-domains, and a terminal domain called the
CC Cyc domain (PubMed:15904941, PubMed:19139103). The Cyc domain has
CC limited similarity to both C and Cy domains of NRPS but is most
CC different in the so-called C3 and Cy3 motif of the latter domains,
CC suggesting a special mechanism in acyl diketopiperazine formation,
CC which is the final step of D-lysergyl peptide lactam synthesis (By
CC similarity). LpsA2 misses an N-terminal C domain in the first module,
CC leading to the conclusion that this C domain is located on the other
CC subunit (lpsB or lpsC) containing the D-lysergic acid module (By
CC similarity). {ECO:0000250|UniProtKB:O94205,
CC ECO:0000269|PubMed:15904941, ECO:0000269|PubMed:19139103}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI59268.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ884678; CAI59268.1; ALT_FRAME; Genomic_DNA.
DR SMR; Q2PBY4; -.
DR VEuPathDB; FungiDB:CPUR_04074; -.
DR UniPathway; UPA00327; -.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0035835; P:indole alkaloid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.30.300.30; -; 3.
DR Gene3D; 3.30.559.10; -; 3.
DR Gene3D; 3.40.50.12780; -; 3.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR Pfam; PF00501; AMP-binding; 3.
DR Pfam; PF00668; Condensation; 3.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 2.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Ligase; Phosphopantetheine; Phosphoprotein; Repeat; Transferase.
FT CHAIN 1..3563
FT /note="D-lysergyl-peptide-synthetase subunit 1"
FT /id="PRO_0000439108"
FT DOMAIN 844..921
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:15904941, ECO:0000305|PubMed:19139103"
FT DOMAIN 1944..2020
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:15904941, ECO:0000305|PubMed:19139103"
FT DOMAIN 3025..3104
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:19139103"
FT REGION 307..706
FT /note="Adenylation (A) domain 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:15904941,
FT ECO:0000305|PubMed:19139103"
FT REGION 963..1354
FT /note="Condensation (C) domain 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:15904941,
FT ECO:0000305|PubMed:19139103"
FT REGION 1397..1804
FT /note="Adenylation (A) domain 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:15904941,
FT ECO:0000305|PubMed:19139103"
FT REGION 2067..2486
FT /note="Condensation (C) domain 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:15904941,
FT ECO:0000305|PubMed:19139103"
FT REGION 2511..2909
FT /note="Adenylation (A) domain 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:15904941,
FT ECO:0000305|PubMed:19139103"
FT REGION 3166..3451
FT /note="Cyclization (Cyc) domain"
FT /evidence="ECO:0000250|UniProtKB:M1W5Z4, ECO:0000255"
FT MOD_RES 881
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1981
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3064
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 3563 AA; 391166 MW; 92EE652A037621ED CRC64;
MSISVPEKLQ DLTAVKSPSA FGNSIESING DKNKSERHTA SSSAVSTYEI GHPCLLTNFK
LAVACSGPAI TKVATVNDKD SGAKLKNVIN GKDISASEVF KGAWAVVLGT YLAKSHVSLD
YGVMKPKGLG PETSCNARVP SENSEMSTSS FLLRANDTLL DIIRQNSMCA HTELRQKSSL
DDVESPKRCN TCVIYWPEIS CSEQLQIDAW MTILEENDQL TQYDCMIHFA SDMRCMLSYR
DQFMSESQAR HLAATMRVVL SSIASAPQQS LADVDVCSSL DYRTLSRWNF KAPIVSEVCV
HDLIEKSCSP RPNPQAVVSW DGCLTYNEMD RLSSHLAQRL RDAGVEPGVF VALCLDRCKW
AVIGIVAVMK AGGAFCALDP SYPVSRLKEM CRDLGITIVL TVKSNIQHAS PLASKVFALD
DDVYFESALS SAHESASWVN VSPHDPVYAV FTSGSTGKPK GIIMEHASFS ACALSSVKPL
QIADQDRVLH FASYAFDASV IEILAPLIAG ATVAIPSERA RLEDLPRAMT DLKATWAFLT
PTVARLYRPE QMPTLKTLCL GGEAVNASDT RSWSSKNLIS GYNPAECCPL GISGPLNDRM
PRSLGSTFAS QTAWIVDPKD HEKLLPAGAI GELAIEGPVV ARGYIHDVTC SDPSTPFVVK
PPPWLRRFRA TANRGNRIYL TGDLARLDCD DGSVHYLGRK DDQVKIHGQR VELAEIEHHL
EQHFVSLATK VVVMLLRPIS GRTVLAALIM PHQRLQHGDK SLESLLMEPG DVSQDFRANL
ASAASKLRLA LPSHMVPSVY LPIRHFPTTK GGKIDRGHLQ SLLLSLPPEC LYGSEEATTR
RGEEPKSDRE KLLQALFAQS LDLPRTRIDL DSNFFQLGGD SLSAMKLLAL ALEEGISSIA
YQDIFSHPTL REIVIVSTSA TSREPLSSET VETPPFSLIK DPEMLIQIAS EQCGSGVGKA
DIEDIYPCTH LQQSLMASTA HNPNAYVAIL AFKLKSGVDR TRLERAWHIA CSGHTILRTR
LVQTDTGDCY QVVVKQPPHW TETNEVSDDG STDSLLRTSF GLGRPLIQSH LSTDQLFVAM
HHALYDGWSL PMLIGELDLA YRELSVRRLP CLKNYVKYTM DSADAAASFW QAELQDADPV
HFPAPSSLDY KPQPCAAMTV SVPLVNSPRR NVTLATEIQF AWAMTVYTYT GCKDVIFGLI
SSGRAAPVAQ IESMLGPTFA STPLRVSIDP QGKLGEALDD LQYTIVEQSM FVHFGAQAIR
QLGPNAAAAC NFQTVLAVET AGPDTGVEEG SWFTGYDFLS DLASFSSHAL TLRCKLSAKG
VEINAVYDKA VVDERQMGRI LAQFEHILTE IHSNETIHDD IGSLDKLSRS DWRELQAWNS
DLPPPHPKGL GAHQVIQEKC QAQPDATAID AWDGSVTYDE LERRAEKLAG LVRSYVSKPD
QVVVLYFSKS RLTVVTQLAI LKAGAAFITL DITQPPHHLR RIIAALGPAL ILVLTSDELL
SAAEELQEGA AVMAVDKDHL SNGIIASQTS SSACAVECEL MYVVATSGTT GVPKIIMTNH
QSFMTNASPL MNRMGITAES RVFQFCGYSF DLMIAEHFLT LLAGGCICIP SLHNRNNRFA
ASIVEFKANW IGAPSSVLQL LDPQTVPTVK TIMQGGERLQ QGLVDRWAPS ARLINAYGPA
ECSVAALVSD TVRPDTENVQ NLGFATGSVC WIVNADTEGK LLPVPIGAEG ELLIEGHTLS
RGYLGDLDKT NAVFLALPDW LRDFRADCNQ GQGHRAYLTG DIVRQNSDGS ISFVRRKDAQ
VKIRGQRVEL ADVEHQVERC FAGSHQVVTD IVQISDSQSS ILVALVLTKD VMTNYKQQES
LLDQKSAGGL SILAPTSSFT ANANAAETAL QDRIPAYMVP DLFVPVSDFP REASGKVGRR
TIKQYLASLT QQDWSRYSLT RKVPPSNATE HEILAIWARV LRIEPHTFGV HDSFFRLGGD
SISSMRVAAA CGVAGISVTV KDMFEYRTIR KLALARGVTQ QMDVATTSTE ANASVVSQKK
APHIFYPEGR LEIYMERMQS RLGQAIERIY PCSPIQQGIL MSHARNAHHY DEVIQWRVAG
DVWCDISRMQ RAWREVVSRH GILRTLFLQV SEDSFLDQVV LKNYSPHISV YTDGEDWEAY
RPFEDSVPMH QLLVIQRSAD DVTVSLRIHH ALVDGLSLHI IRRDLEHAYQ GCLDDLVEPP
AYHEYISYLQ EKRLQESPKE YWKSYLQGAT GALFPAVQDE PAEDGQYFGV VEIELGPSAK
LTQFCEEHKL GMTVVLHVVW AIIVQRYTAT DEVCFGFMTS GRHVPVANVE NMVGPLFNML
IGRVKLAYNL SLLSTMYEYQ ENFINSLDHQ QQSLVESLHS IGSSAGDLFN TLITVFNDQP
EGHASQQQST LRLVGDIVQS RSEYPITLNI VSCADKIKMQ LSYHAILLNS VSANAIAEAF
RFVLQRTLER PHELLRALPV LDEDQMNSVF EKNSSVPPQV EELIHDTIHQ QCIRCPDSPS
VCAWDGNFTY RQLDELSSAL SREIVRKGAG PEVTIPIVLE KTRWTPVAML AVLKSGSSFV
LMDSTHPAVR VGSIVQAIGP PVIIVSAQTR SKVATFSTDV VEVGDWLARE ILVAKQHVTR
QNGLLQATNA AYLVFTSGST GKPKGAIVEH ASLSTAAKYM ASRLHIDSAS RVLQFSSHAW
DIPVTEVLVT LRMGGCVCVP SEEERTGNLA KASERMKVNW ALWTPTVARL FKPEEFPHLK
TLVFAGEALS ATDLETWCDR VRLVQGYGPA ECSLISTVTD PLTRSDNPRC IGLPSGCVAW
VVNRDNHELL APPGATGELV LEGPIVGRGY LGDPGRAASA FISPPAWLMR LRGSGSSNRL
YKTGDLVRQH VSSGLLTFVG RNDDQVKVRG QRVEPGEVEG QVAQVFPGSQ VIVLVVKKSA
GAVLAALVLQ NGEDRSSAGE TANLFPPPSL AFAALAKAAF SKLREDHAYA ATGKADRNLL
RDRVASLSAE EDRGICGGPV CRPGPPRTAL EAELPRLVGQ VLPKASSFPF PLDEDPIPDL
GMDSPPGPDP LASSCAPTWV GGFRSNHFPA LATVRFGSYR RAGAARNQFT ESARRSSCYI
NKRLVSLLPE ICTKWDLRED QITHIAPTTY YQHMALASDH EAFFGLYFSK PMASEALKAA
ASRVVNLHSI LRTAFVPLED TYVQLTLCDF DLPSQEIQTN EAEVSAAMEL FCRDAADKTA
GFGVPVTKLI LMLDRQGDCL SLLLRLQRAQ FDGVSVMRIM ADWRSALEHA SCSWEPAPSL
DYADFALARV AQNTPDVFGM WRDQEYISMT DRGHAERLVT SSCDIPLPEP APGYTMATVA
KAAWAICLAR ETESEDLLFL QLVRNRHLAL DGIDKMVGCS LNYVPVRVPL RRDWKISDLL
HWLHQQHIRT MAGDTADWPD VVAKSTTWSS DTEFGSVIHY LSAPAAPVYH FPGDTVAQFQ
LYDEKMTHTC PLVTCIEFPG PTEQSGRQMK ILVTSAVGGQ DMVDRLLAVF RSLLCEANAQ
LDQSVSNILQ GLRDGDDAMG KAR
