MLFA_ASPTC
ID MLFA_ASPTC Reviewed; 5073 AA.
AC A0A1L9NGU5;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Malformin synthetase mlfA {ECO:0000303|PubMed:30560908};
DE EC=6.3.2.- {ECO:0000269|PubMed:30560908};
DE AltName: Full=Malformin biosynthesis cluster protein A {ECO:0000303|PubMed:30560908};
DE AltName: Full=Nonribosomal peptide synthetase mlfA {ECO:0000303|PubMed:30560908};
GN Name=mlfA {ECO:0000303|PubMed:30560908}; ORFNames=ASPTUDRAFT_159361;
OS Aspergillus tubingensis (strain CBS 134.48).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767770;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 134.48;
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
RN [2]
RP BIOTECHNOLOGY.
RX PubMed=19876076; DOI=10.1038/ja.2009.100;
RA Kojima Y., Sunazuka T., Nagai K., Hirose T., Namatame M., Ishiyama A.,
RA Otoguro K., Omura S.;
RT "Solid-phase synthesis and biological activity of malformin C and its
RT derivatives.";
RL J. Antibiot. 62:681-686(2009).
RN [3]
RP BIOTECHNOLOGY.
RX PubMed=26540166; DOI=10.1371/journal.pone.0140069;
RA Wang J., Jiang Z., Lam W., Gullen E.A., Yu Z., Wei Y., Wang L., Zeiss C.,
RA Beck A., Cheng E.C., Wu C., Cheng Y.C., Zhang Y.;
RT "Study of malformin C, a fungal source cyclic pentapeptide, as an anti-
RT cancer drug.";
RL PLoS ONE 10:E0140069-E0140069(2015).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=26645406; DOI=10.1007/s00280-015-2915-4;
RA Liu Y., Wang M., Wang D., Li X., Wang W., Lou H., Yuan H.;
RT "Malformin A1 promotes cell death through induction of apoptosis, necrosis
RT and autophagy in prostate cancer cells.";
RL Cancer Chemother. Pharmacol. 77:63-75(2016).
RN [5]
RP BIOTECHNOLOGY.
RX PubMed=28713983; DOI=10.3892/ijo.2017.4070;
RA Park S.Y., Oh H.H., Park Y.L., Yu H.M., Myung D.S., Cho S.B., Lee W.S.,
RA Park D., Joo Y.E.;
RT "Malformin A1 treatment alters invasive and oncogenic phenotypes of human
RT colorectal cancer cells through stimulation of the p38 signaling pathway.";
RL Int. J. Oncol. 51:959-966(2017).
RN [6]
RP IDENTIFICATION, FUNCTION, AND PATHWAY.
RX PubMed=30560908; DOI=10.1038/s41598-018-36561-3;
RA Theobald S., Vesth T.C., Rendsvig J.K., Nielsen K.F., Riley R.,
RA de Abreu L.M., Salamov A., Frisvad J.C., Larsen T.O., Andersen M.R.,
RA Hoof J.B.;
RT "Uncovering secondary metabolite evolution and biosynthesis using gene
RT cluster networks and genetic dereplication.";
RL Sci. Rep. 8:17957-17957(2018).
CC -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC that mediates the biosynthesis of malformins, cyclic pentapeptides with
CC a disulfide bond between 2 consecutive cysteins, that show potential
CC anti-tumor as well as antimalarial and antitrypanosomal properties
CC (PubMed:30560908). The nonribosomal peptide synthetase mlfA is
CC responsible of the formation of the cyclic pentapeptide (Probable). The
CC malformin biosynthesis clusters in malformin-producing fungi also
CC contain enzymes involved in the formation of the disulfide bond between
CC the two consecutive cysteins within malformins, in addition to
CC additionnal tailoring enzymes such as methyltransferases or
CC oxidoreductases. They are also composed of up to 4 major facilitator
CC superfamily transporters, and transcription factors probably involved
CC in the regulation of the expression of those clusters (Probable).
CC {ECO:0000269|PubMed:30560908, ECO:0000305|PubMed:30560908}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30560908}.
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. MlfA has the following
CC architecture: A-T-C-A-T-C-A-T-C-C-A-T-C, with the functions of the five
CC condensation domains during malformin biosynthesis being DL-joining
CC (epimerizing subtype), LL-joining, epimerization, DL-joining and
CC cyclizing domain, respectively. {ECO:0000305|PubMed:30560908}.
CC -!- BIOTECHNOLOGY: Malformins show anti-tumor properties against human
CC colorectal and prostate cancer cells by the inhibition of proliferation
CC and induction of apoptosis through the activation of the p38 signaling
CC pathway (PubMed:26540166, PubMed:26645406, PubMed:28713983). Malformin
CC C has also been shown to exhibit potent antimalarial and
CC antitrypanosomal properties (PubMed:19876076).
CC {ECO:0000269|PubMed:19876076, ECO:0000269|PubMed:26540166,
CC ECO:0000269|PubMed:26645406, ECO:0000269|PubMed:28713983}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; KV878179; OJI88518.1; -; Genomic_DNA.
DR SMR; A0A1L9NGU5; -.
DR STRING; 767770.A0A1L9NGU5; -.
DR EnsemblFungi; OJI88518; OJI88518; ASPTUDRAFT_159361.
DR VEuPathDB; FungiDB:ASPTUDRAFT_159361; -.
DR OMA; YEWLMAF; -.
DR Proteomes; UP000184304; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR Gene3D; 1.10.1200.10; -; 4.
DR Gene3D; 3.30.300.30; -; 4.
DR Gene3D; 3.30.559.10; -; 5.
DR Gene3D; 3.40.50.12780; -; 4.
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; 4.
DR Pfam; PF00668; Condensation; 5.
DR Pfam; PF00550; PP-binding; 4.
DR SMART; SM00823; PKS_PP; 4.
DR SUPFAM; SSF47336; SSF47336; 4.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 4.
DR PROSITE; PS00455; AMP_BINDING; 3.
DR PROSITE; PS50075; CARRIER; 4.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Ligase; Phosphopantetheine; Phosphoprotein; Repeat.
FT CHAIN 1..5073
FT /note="Malformin synthetase mlfA"
FT /id="PRO_0000446439"
FT DOMAIN 726..799
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1823..1900
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2997..3073
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 4544..4620
FT /note="Carrier 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 194..585
FT /note="Adenylation 1"
FT /evidence="ECO:0000255"
FT REGION 837..1268
FT /note="Condensation 1"
FT /evidence="ECO:0000255"
FT REGION 1296..1685
FT /note="Adenylation 2"
FT /evidence="ECO:0000255"
FT REGION 1901..1930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1963..1984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2031..2446
FT /note="Condensation 2"
FT /evidence="ECO:0000255"
FT REGION 2469..2861
FT /note="Adenylation 3"
FT /evidence="ECO:0000255"
FT REGION 3090..3555
FT /note="Condensation 3"
FT /evidence="ECO:0000255"
FT REGION 3576..3995
FT /note="Condensation 4"
FT /evidence="ECO:0000255"
FT REGION 4020..4410
FT /note="Adenylation 4"
FT /evidence="ECO:0000255"
FT REGION 4611..4633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4657..4991
FT /note="Condensation 5"
FT /evidence="ECO:0000255"
FT COMPBIAS 1901..1924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4617..4633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 760
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1860
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3034
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 4581
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 5073 AA; 558190 MW; 5CD50B70CBC7DC03 CRC64;
MSRFSCIFPT LTDGYIPKPD HTCAAGRRTY TIDLSGWKAP GSETESHILA AWGLVLSSYV
GTDEVAFYVV PTTGPDTTAL ADLKVEGDMS RQSLTYAAMQ LLHPALVGAG QVSGETANTI
ITFAKDIESL FVTQTEAANV GTAMAQALAE VGTCDNDRII KDLNLMSPAH LEHIWRFNAN
VPGIWEECFH DVIERHATNR PHSLAVDAWD TKLTYADLVR EARLLAAYLQ QRGVGPGSVV
PISFERSGAA LVAMLAVSKA GSAFVSVPPN LPAGRLDAIL DVIEAPFVVT WTKYESFWAE
RLPTLPIDNY PKPAADATVE ALGKPEDLFY VIFTSGSTGR PKGCMLSHSN WLNGALRNAP
SWKYGPESRV LQMLSHTFDM SLLEICTSLG SGACVCVPRT EEIETSISDA INRWQVNHVI
MTPSLARALR PDDVPGLKTM CLGGEAFPKE IVTMWSERIN LWQFYGPSEC SINSSSRPIT
RPDADPLNIG PPNSAACWVT DVHDYNKLVP VGAIGELLVS GPIVGMGYLK NPVKTAEAFL
EEVGFVAKDD PQFGGFRFYR TGDLVRWNSD GTITFCGRAD TQVKLNGQRL ELAEVEYQLG
LESGVQYAIA MAPQAGLCKN NLIAILTVKG TSTGNQDTAA DEIPLLDRRD PIVQETVKRL
RSQLQHALPR YMVPTIWAFV GRMPMSASGK IDRVQLRDWV QKMSQETFDA ITGRSLEAED
HVLGLSRLEQ EVQLAWAEAL GLSAAEVGLQ QPFVALGGDS IMALDAVARC RARQIKISMV
HILSCEGVRE AASLAEVQET PAQQVAEMAV DYSNLWTRLS DDYDLDKLGV TQLEEVEDVF
PCTTMQEGMF LGQIRRPGAY HMRFFHRVQL KGGCLPTVER IQQAWASLVE RHPSLRTVFV
DDLSPEAIYH SIVLRSVPME LRMREVPRDL RAEAALAMFT EELVPFRANA PLHRMLLLTC
RGRVPYFMLE ISHVIMDGYA LSVFRREFIR ACSSSAPLPR GPDYRMFANY HRTRQTDDSA
RYWTNYLADC VPCHIPTHAV SAPSDGPPEW PRTLQRRDFG FDNSAAFLQR CKERQVTLAC
AIRAAWALVL RAYTQSQDVC FGYVSSGRNV PVPEVETIFG LCLSMQVCRA RLSEASTIAS
IAKKIQEDYV ASLPFQHYPL AEAQRGLKQT HGQGLFNTAI SMEWVPPSAE DEDALLDLEE
IREQDDPTEY DIAISVDVHE GHIKLGFLYW PNLTDFEITH LAEALQGAMN CFVFQPDEAL
NTLSLLQASD VCSALADGPT LLPLEAVRGN VVSMIDRWVT RHPEGAAIDG WDGSLTYKEL
HEQSSWVARN LLHQGVQLGD RILVCADRSS RTVATVLGIV RAGCVLVLSN PTDPAKRLQW
LAKRCNAALI VADPTYEERF ATADARVLST TSVCAPAAWD YEFPALDEHD LISILFTSGS
TGTPKGILME HGALATSVLL GHGRTLRFSR HTRMLHFASL TFDAALAEIF TTLAHGGCIC
VPCEEDRLSD VPGCISRFAV NMAMLTPSVG RLLEPGALPT LKSLIMVGEP MSRLDVERFA
PVLDLYNGAG PTETSIMVTI AGPMKPTDEP VDLGYAVAGV RLWVTEAENP NRLAPLGAVG
ELVVEGRLVT RGYLDDPART HEAFLPSLPW LPSQHALYRT GDLVRYADDG SLRYMGRKDT
QVKLRGQRIE LQEVEYHLRK SLQQAQIVVE MVVPAGKMRA QASLVAFVSG LTAADVESSS
ACNLEGMIPI SQIVLPKSAF KALEEALPRH MIPSVYYALD TIPLSVNGKA DRRRLREMGS
LLLASSAAHK NTIEGMSKSV KWTPASELER TLLELMAATL GLEAETMHGD DSFFELGGDS
VSAMKLVATA RDKYKLSLSV PQMFRYPTIC QLAAEVGEPA GQSASSASST TEEGFTFSTP
DDSSTNDGVD DDFLQLATAQ LAQLAQEKGK KVDIAALLKQ LQGGSSSNKT PSVSSSSSSS
SSSKRKKKAA LAEAAAPISV QFSLLDGGAD VLDKVRAQAV EHCKIPHEDI EDIYPATALQ
EGMIALTART PGVYTTTLTC DLSEQVDLAR LHYAWGKAAE AHPILRTRII LTDNNTAVQV
VQRAKGLPWD TYSLREGDVL PDLTSNMTSG SPLLRLAVVH RQNQPRMLLV AIHHALYDGW
SMPLLKEAVE DAYHGRDLRP QPFTPFIKHL IAGKVAAQAF WTTHLDSFAG GVFPNLPGVD
HQVQPKERRT RSLTMPTATP RAQYTMATKI QAAWAVTVSR YAEDNDVVFG SVSTGRSAPV
PAIDRMVGPT ITTVPVRISL GDQAERLTSL LQRVQDDSWE RMDHEHLGLQ HIRRLGESAA
AACGFQTLLV IQPREQPNNK YRSTLLSSLQ DVAELEGVDT YPLMLVCEPD GARLHLSAVF
DPVVLDGVTL ERMLANWELV LTQLWNEPDM AVLELDAVSC SDTETLIRWN TGETIADGCA
HDAVCEWSSR TPHAPAVCAW DGEWTYEELE RCSSLVASQI LAHDVSSGDF IALYHEKSRW
AAAGILAVFK AGAILITLDP AHPTDRIKNI LDQARPRLIL TSQSLLDVAR NLETPALSVQ
FAASQPLPEG WSSLPTISST QAAYAPFTSG STGRPKGIPL DHRGLAASTA SIAHSCLLRP
ASRVLHFASF AFDASMMEHL IAWRAGGCLC IPDETARQTD LAKCIRDFNV TWAFLTPSCL
RLITPDDVPS LQALGLGGES MTSEDIAIWS PRLRQIVQLY GPAECCIVAA LTEVTKPSEN
RLIGRPNACR CWVVDLQNPD RLAPIGAVGE LLIEGITVGR GYINDPDRTT PVFIRPPKWL
QTLYPDDQEP KRLYRTGDLV RYADVDGKLA FIGRRDGQLK LHGQRIELAD IEAHLRPLIP
ATQKMAVEML HSADNQNLIL AAFLEEMSTS QKPTEREVKL LHPSQSQCAL NVMAIDSALS
RKVPQYMIPS MYLHISRLPL SASGKLDRRH LREMIAELPR QRLNEYAAGS GLRVPDRPKT
SQEQEMQAIW ARVLSLDPNT IGVNDDFFRI GGDSISGMQV ATKCNAAGIH ITSADLFRHR
TIEQLICHLN SIRTTDCASV SLPAEPVDEW VALAPIQQLF FEVAPEGPNH FNQSLLLRTS
RRVSVEELAG GLDILVGRHS MLRARFCRKD SGQWFQQVKS LGSEPASNFY RLAAHNQITR
ESLPTLFTTA QMALSIQDGP LLTVDLVELE DGRQLVYLAA HHLIIDLVSW RILHGELEEY
LQTDSLSSAT GSVPFITWSQ LQAEYSAEHL TPARAFPGFQ EANDDFDVMR YWGISSESNT
FGQTSISRFT LDRTVTDILF GSANKVMDTR PVEILQAALW YSCNQALTDR PGPSIYVEGH
GREPWTDAIN VSGTVGWFTT MSPLVSTPWD HLSRTSMRDF VDALSYIKDQ RRRIPANGWA
YFTSRYLNDE GRVAYGRTKP VVEVLFNYMG QYQEMNREGA MLQLAGNDIQ SGTGASDIAD
NVPRFSLIDV SAFTANGCLT FEFTFPQLMQ QDARLEQCIK ECERTLVAAA SSLSAEGPRK
TLTDFPLMSA LTYDQLSQFL DHTLPSLGLR AQDVLDIYPC SPVQQGMLLA QLRDRQAYQQ
RFRFQVMSRV PTDQLPLEKV KGAWTEVINR HDILRTLLLP VSDHSHFDQV VMVPGSLQHL
VRLNAMDTNP ADGLPHTINI TSDSADTIIC EWKVSHALVD AMSIAVIQRE VNQAFEGSLG
QYRDVPQYVD YIKWLSLQDN TEAQAYWQNH LKEVEPCLFP QLTSSPNPIN PEGTISAIRA
TWTRDARMDD LCHKHAITLT NLFQIVWAVV LGAYVGTDEV CFGYTTLGRD VPVDGVETMV
GPLVNVLAAT VQLKQDESIL NALLTHQNRL TSSLQHQHYA LADVYACLGL AGSQLFNTIV
SLQDISHFDV PDERGTRLEM LPANDVSEYN VALNIGVDKS SIQLVCSYQT VSLSAEQADA
LLRTVFHVLG EILRDPTQRF CELEVISPKC KEQLVKWNAG MLAPTDEYIH EKIQGQCRIH
ASRQAVCAWD GMFTYAEVDD LSSRLAARLI RMGVTSEDII PIYSPKSRWT VIAILGVLKA
GAAFTLLETS HPMARLHMIC NQIKAPMIIA PASHAVPAAN LAPILVVLDN ITSLAQEKLD
PFPGIGIPPA GEALAYLIFT SGSTGNPKGV MVTHQNLCSN ASIITTSVNM TSDSRVLQFA
SHAFDGCLWE ILGALLAGAC LIIPSESENK EDLTGCIERM DVTWAFLTPS VARILKPETL
PSLCNLVLGG EPIAASDLDM WRGHVQVVCA YGPTETTILA STTSPSTFPT DGKDIGTPTG
SSLWIVDTRN YQTMVPLGAT GELLIEGPNV SQGYLGDPEK TNDAFPDAPR WLSQLRKSPT
RVYRTGDLVR FDTTAGTIRF VGRKDNQIKF HGQRIELGEI EHHAQLAFSS ASTVIVDLIT
PEQPQQPYIV AFVHLPDATP ETTETMDTIL LPPSESFRAD ALAAQKKMHK RLPHYMVPAA
FLPLHRFPLS ATGKADRKRL RQCALGLSSP DLSAYRATAS TKRMPSTAAE RKMQLLVASV
LGRDPTEIGM DDSFFYLGGD SVQAMRLVAE GRQQGLSLSL RAIFDSPRLR DLGDQARSPN
ADNQRVSTAS SAGLRDNRDQ IDKVVATNSL KKADVADVLP TTSFQRHWLD AQLKSYIVVD
IPGPIDPARL LRAMHRVVEA HPILRVSFVP YETTTLQIIL RTAAAMTNVD VSTTTVDFST
TTVEDICRQD AGAQLPPGVP YLRVILATQD KADHKLIMRL SHAQYDAVSL SLLMNDLSHA
YATETHALPS SHFPRFNDYI TYQQAQRADP TATTFWRLLL QNVSLTYLNL QPAESSASNG
TPITLSRDIN IATFPSLPNG ITIATMVKAA WSLVLAQKTD SHAVIFGQVV HGRTIALPGV
EGIVGPCANI TPVVARLGLQ TTGFELMQTL QDQHRSAMPY EALDLDDALA YTKNSPVGRR
GLQTIVQHQN NVMVDDMELL LGEVKCGVDV RAVDHVPKEV WVYSSVDEKR PDMLEVKIMS
STLALGEEVA EELMGLLVEK IVGLLRHPER VCV
