LPSA1_CLAPU
ID LPSA1_CLAPU Reviewed; 3232 AA.
AC O94205;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=D-lysergyl-peptide-synthetase subunit 1 {ECO:0000303|PubMed:10071219};
DE Short=LPS1 {ECO:0000303|PubMed:10071219};
DE EC=2.3.1.- {ECO:0000269|PubMed:19139103};
DE AltName: Full=Ergot alkaloid synthesis protein ps1 {ECO:0000303|PubMed:10071219};
DE AltName: Full=Nonribosomal peptide synthetase 1 {ECO:0000303|PubMed:10071219};
GN Name=lpsA1 {ECO:0000303|PubMed:17720822};
GN Synonyms=cpps1 {ECO:0000303|PubMed:10071219};
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, AND
RP FUNCTION.
RC STRAIN=P1 / 1029/N5;
RX PubMed=10071219; DOI=10.1007/s004380050950;
RA Tudzynski P., Hoelter K., Correia T.H., Arntz C., Grammel N., Keller U.;
RT "Evidence for an ergot alkaloid gene cluster in Claviceps purpurea.";
RL Mol. Gen. Genet. 261:133-141(1999).
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, AND DOMAIN.
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 IDENTIFICATION IN THE EAS CLUSTER, FUNCTION, AND DOMAIN.
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 [6]
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 [7]
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 [8]
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 [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [10]
RP FUNCTION, DOMAIN, CATALYTIC ACTIVITY, AND PATHWAY.
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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:10071219, PubMed:14732265, PubMed:14700635, PubMed:15904941,
CC PubMed:17308187, PubMed:17720822). DmaW catalyzes the first step of
CC ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate
CC (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan
CC (PubMed:14732265). The second step is catalyzed by the
CC methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in
CC the presence of S-adenosyl-L-methionine, resulting in the formation of
CC 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the
CC FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-
CC abrine to chanoclavine-I which is further oxidized by easD in the
CC presence of NAD(+), resulting in the formation of chanoclavine-I
CC aldehyde (PubMed:20118373, PubMed:21409592). Agroclavine dehydrogenase
CC easG then mediates the conversion of chanoclavine-I aldehyde to
CC agroclavine via a non-enzymatic adduct reaction: the substrate is an
CC iminium intermediate that is formed spontaneously from chanoclavine-I
CC aldehyde in the presence of glutathione (PubMed:20735127,
CC PubMed:21494745). The presence of easA is not required to complete this
CC reaction (PubMed:21494745). Further conversion of agroclavine to
CC paspalic acid is a two-step process involving oxidation of agroclavine
CC to 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:10071219, ECO:0000269|PubMed:14700635,
CC ECO:0000269|PubMed:14732265, ECO:0000269|PubMed:15904941,
CC ECO:0000269|PubMed:16538694, ECO:0000269|PubMed:17560817,
CC ECO:0000269|PubMed:19139103, ECO:0000269|PubMed:20118373,
CC ECO:0000269|PubMed:20735127, ECO:0000269|PubMed:21409592,
CC ECO:0000269|PubMed:21494745, ECO:0000269|PubMed:24361048,
CC ECO:0000305|PubMed:17308187, ECO:0000305|PubMed:17720822}.
CC -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC {ECO:0000269|PubMed:19139103}.
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 (PubMed:10071219). 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 (PubMed:10071219). Thus, an NRP
CC synthetase is generally composed of one or more modules and can
CC terminate in a thioesterase domain (TE) or reductase domain (R) that
CC releases the newly synthesized peptide from the enzyme
CC (PubMed:10071219). LpsA1 has a domain arrangement (A-T-C-A-T-C-A-T-Cyc)
CC with 3 A and 3 peptidyl carrier (PCP/T) domains, 2 C-domains, and a
CC terminal domain called the Cyc domain (PubMed:19139103). The Cyc domain
CC has 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
CC (PubMed:19139103). LpsA1 misses an N-terminal C domain in the first
CC module, leading to the conclusion that this C domain is located on the
CC other subunit (lpsB or lpsC) containing the D-lysergic acid module
CC (PubMed:19139103). {ECO:0000269|PubMed:10071219,
CC ECO:0000269|PubMed:14700635, ECO:0000269|PubMed:19139103}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of ergotamine but is
CC still able to produce ergocryptine (PubMed:17560817).
CC {ECO:0000269|PubMed:17560817}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; AJ011964; CAB39315.1; -; Genomic_DNA.
DR SMR; O94205; -.
DR VEuPathDB; FungiDB:CPUR_04074; -.
DR BioCyc; MetaCyc:MON-15623; -.
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; -; 3.
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; 3.
DR SMART; SM00823; PKS_PP; 3.
DR SUPFAM; SSF47336; SSF47336; 3.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 1: Evidence at protein level;
KW Ligase; Phosphopantetheine; Phosphoprotein; Repeat; Transferase.
FT CHAIN 1..3232
FT /note="D-lysergyl-peptide-synthetase subunit 1"
FT /id="PRO_0000439105"
FT DOMAIN 617..686
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:19139103"
FT DOMAIN 1717..1785
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:19139103"
FT DOMAIN 2810..2878
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:19139103"
FT REGION 90..474
FT /note="Adenylation (A) domain 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:19139103"
FT REGION 731..1122
FT /note="Condensation (C) domain 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:19139103"
FT REGION 1165..1572
FT /note="Adenylation (A) domain 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:19139103"
FT REGION 1835..2252
FT /note="Condensation (C) domain 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:19139103"
FT REGION 2276..2675
FT /note="Adenylation (A) domain 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:19139103"
FT REGION 2943..3218
FT /note="Cyclization (Cyc) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:19139103"
FT MOD_RES 649
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1749
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2842
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 3232 AA; 355443 MW; 76FEEF2D0051063F CRC64;
MRCMLSYRDQ FMSESQARHL AATMRVVLSS IASAPQQSLA DVDMCSSLDY QTLSRWNLKS
PVMMEVCVHD LVQQNCCSRP TCQAVASWDG CLTYDEMSIL SSHLAQRLRA AGVKPGVFVA
LCLDRCKWAV IGILAVLKAG GAFCALDSSY PVSRLQDMCR DLEITIVLTV KTNIQHASPL
ADTVILLDDD LYSESALSSA QKCASRSSLS PHDPVYAVFT SGSTGKPKGI IMEHASFSAC
ALSSMEPLHI GPQDRVLHFA SYAFDLSLFE ILAPLIAGAT VVIPSEKARL ENLPCAMTDL
GATWAFLTPT VARLYRPTQM PTLKTLCLGG EAVNASDIKS WSSKNLISGY NPAECCPLGI
SGLLNDHMPR ALGSTFPSQM AWIVDPEDHE KLLPVGAIGE LAIEGPVVAR GYVHDLKSSD
SSTPFVVKTP TWLCRFRSNI NRSNRIYLTG DLARQDCDDG SVHYLGRKDD QVKIHGQRVE
LAEIEQHIEQ HFSSLATKAV VMLLRPISGR TVLTALVMPH QRLENGEKTS NSLLMELADI
NQDFRATLAL AASKLRLALP SHMVPSVYLP IRHFPTTKGG KIDRGHLQSL LLSLPPEYLY
GSEEATTHQG EEPKSDREKL LQGCFAQALD LPRTRIDLDS NFFQLGGDSL SAMKLLALAL
EEGISSIAYQ DIFSHPTLRE IVIVSTSATS REPLSSETVE TPPFSLIKDP EMLIQIASEQ
CGSGVGKADI EDIYPCTHLQ QSLMASTAHN PNAYVAILAF KLKSGVDRTR LERAWHIACS
GHTILRTRLV QTDTGDCYQV VVKQPPHWTE TNEVSDDGST DSLLRTSFGL GRPLIQSHLS
TDQLFVAMHH ALYDGWSLPM LIGELDLAYR ELSVRRLPCL KNYVKYTMDS ADAAASFWQA
ELQDADPVHF PAPSSLDYKP QPCAAMTVSV PLVNSPRRNV TLATEIQFAW AMTVYTYTGC
KDVIFGLISS GRAAPVAQIE SILGPTFACT PLRVSIDPQG KLGEALDDLQ YTIVEQSMFV
HFGAQAIRQL GPNAAAACNF QTVLAVEADG PETGEEEGSW FTRYDFLSDV ASFSSYALTL
RCKLSTRGVE INAVYDKLMV DERQMGRILA QFEHILTQIH SNETVHDDIG GLDKLSVSDW
RQLQAWNIDL PPAHPKGLGA HQAIQAKCQA QPDATAIDAW DGCVTYGELE RRAEKLAGLV
RSHVSKPDQV VVLYFSKSWL TVVAQLAVLK AGAAFITLEI SQPVHYLQRV ISALGPVLVL
TSEDLFSAAE DLQENAVPVM AVDKDDLSDA TARTSQASSS ACTVECDLMY IIATSGTTGM
PKIVMTDHQA FMTNASPLMN GLGITSDSRV FQFCGYSFDL LIVEHFLTLL AGGCICIPSL
HNRNNRFAAS IVELEANWVG SPSSVLQLLD PQTVPTVKTI MQAGERLQQG LVDRWASHVR
LINAYGPAEC SVGALARDTV RPDTDDVQNL GFATGSVCWI VNAETSEKLL PVPIGAEGEL
IIEGHTLSRG YLGDADKTNA SFLRLPNWLR DFRADRGQSQ GHRVYLTGDI VRQNSDGSMS
FVRRKDAQVK IRGQRVELTD VEHQVERCFI GAHQVVTDIV QIPNSQSSIL VALVLTKDAM
TNHKQQESLL DQKSAGGLSI LAPTSSFTAN ANAAETALQD RMPAYMVPDL FVPVSDLPRE
ASGKIGRKAI KQYLASLTQQ DWSRYSSTRK VPPSNATEHE ISAIWARVLQ IEPHTFGVHD
SFFRLGGDSI SGMQVAAACG VAGISVTVKD MFEYRTIRKL ALARGETQQL TVGTTSTVSN
ASGIRQKKAL HPFYPEGRLE VYMERMQSRL GQAIERIYPC SPIQQGILMS HARNPHHYDE
VIQWKVAGDV SCDISRMQRA WREVVSRHGI LRTLFLQVSE DSFLDQVVLK NYSPDISVCT
NEEDVEPYRP FEDSVPMHHL LVFQRSADDV TVHLRIHHAL VDGLSLHIIR RDLELAYQER
LDELAQPPGY HEYISYLQEK RSRKSLQEYW SSYLQGATGS LFPAVQDEPA SDGQYFGAVE
IELGSIAKLT QFCEEHKLGV TVVLHVVWAV IVQRYAATDE VCFGYMTSGR HVPVTNVENV
VGPLFNMLIG RVKLAYHLSV LSTMYAYQEN FINSLDHQHQ SLVETLHSIG SSAGDLFNTL
ITVVNDQPED HVSQSALRLV GDSVQSRSEY PITLNILNHA DKIKMQLSYH TSLLSGVSAN
TIAKAFRFVL QRTLEQPHEL LRALPVLDED QMNIVFAQNR CMPPQVDDFI HDTIHQQCLR
CPDSPSVCAW DGNFTYRQLD DLSSALSEEI VRKGAGPEVT IPIVLEKTRW TPVAILAVLK
SGSSFVLMDS THPAARVGSI VQAIGPPVII VSAQTRSKVA TFSTDVVEVG DWLAREVPFE
KQQGTRQTGL LKATNAAYLV FTSGSTGKPK GAIVEHASLS TAAKYMASRL HIDSASRVLQ
FSSHAWDIPV TEVLVTLRMG GCVCVPSEEE RTGNLAKASE RMKVNWALWT PTVARLFKPE
EFPHLKTLVF AGEALSATDL ETWCDRVRLV QGYGPAECSL ISTVTDPLTR SDNPRCIGLP
SGCVAWVVNR DNHELLAPPG ATGELVLEGP IVGRGYLGDP GRAASAFISP PAWLMRLRGS
GSSNRLYKTG DLVRQHVSSG LLTFVGRNDD QVKVRGQRVE PGEVEGQVAQ VFPGSQVIVL
VVKKSAGAVL AALVLQNGED RSSAGETANL FPPPSLAFAA LAKAAFSKLR ETMPTYMIPS
IMLPISYLPK AATGKADRNL LRDRVASLSD GEIEAYVAAS VSHRPASTAM EAELQRLVGQ
VLQRPLHSIS LDEDLFRLGM DSLTAMTLAS AARRRGWEVS VPIIFQHSRV SDLARIVEQG
QHGISSRAQL EEDRVVLNKR LVSLLPEICT KWDLREDQIT HIAPTTYYQH MALASDHEAF
FGLYFSKPVA SEALKAAASR VVKLHSILRT AFVPLEDTYV QLTLCDFDLP SQEIQTNEAE
VSAAMELFCR DAADKTAGFG VPVTKLILML DRQGDCLSLL LRLQRAQFDG VSVMRIMADW
RSALEHASCS WEPAPSLDYA DFALARVAQN TPDVFGMWRD VLQGSSMTYL VPQQEYISMT
DRGHAERLVT SSCDIPLPEP APGYTMATVA KAAWAICLAR ETESEDLLFL QLVRNRHLAL
DGIDKMVGCS LNYVPVRVPL RRDWKISDLL HWLHQQHIRT MAGDTATGRC RG
