ID MLFA_ASPLB Reviewed; 5068 AA.
AC A0A319A6V2;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 27-NOV-2024, entry version 32.
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=BO96DRAFT_457474;
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883;
RX PubMed=30349117; DOI=10.1038/s41588-018-0246-1;
RA Vesth T.C., Nybo J.L., Theobald S., Frisvad J.C., Larsen T.O.,
RA Nielsen K.F., Hoof J.B., Brandl J., Salamov A., Riley R., Gladden J.M.,
RA Phatale P., Nielsen M.T., Lyhne E.K., Kogle M.E., Strasser K.,
RA McDonnell E., Barry K., Clum A., Chen C., LaButti K., Haridas S., Nolan M.,
RA Sandor L., Kuo A., Lipzen A., Hainaut M., Drula E., Tsang A.,
RA Magnuson J.K., Henrissat B., Wiebenga A., Simmons B.A., Maekelae M.R.,
RA de Vries R.P., Grigoriev I.V., Mortensen U.H., Baker S.E., Andersen M.R.;
RT "Investigation of inter- and intraspecies variation through genome
RT sequencing of Aspergillus section Nigri.";
RL Nat. Genet. 50:1688-1695(2018).
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 additional 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; KZ821353; PYH55689.1; -; Genomic_DNA.
DR SMR; A0A319A6V2; -.
DR OrthoDB; 2787863at2759; -.
DR Proteomes; UP000247441; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043041; P:amino acid activation for nonribosomal peptide biosynthetic process; IEA:TreeGrafter.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:TreeGrafter.
DR CDD; cd05918; A_NRPS_SidN3_like; 4.
DR CDD; cd19542; CT_NRPS-like; 2.
DR CDD; cd19534; E_NRPS; 1.
DR CDD; cd19545; FUM14_C_NRPS-like; 1.
DR FunFam; 3.30.559.10:FF:000016; Nonribosomal peptide synthase Pes1; 1.
DR FunFam; 3.30.559.30:FF:000002; Nonribosomal peptide synthase Pes1; 1.
DR FunFam; 3.30.300.30:FF:000015; Nonribosomal peptide synthase SidD; 4.
DR FunFam; 3.30.559.30:FF:000003; Nonribosomal peptide synthase SidD; 1.
DR FunFam; 1.10.1200.10:FF:000005; Nonribosomal peptide synthetase 1; 1.
DR Gene3D; 3.30.300.30; -; 4.
DR Gene3D; 1.10.1200.10; ACP-like; 4.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 5.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 4.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 5.
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_com.
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 NCBIfam; TIGR01733; AA-adenyl-dom; 4.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 4.
DR Pfam; PF00668; Condensation; 5.
DR Pfam; PF00550; PP-binding; 4.
DR SMART; SM00823; PKS_PP; 3.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 4.
DR SUPFAM; SSF47336; ACP-like; 4.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 10.
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..5068
FT /note="Malformin synthetase mlfA"
FT /id="PRO_0000446433"
FT DOMAIN 723..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 2999..3075
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 4546..4622
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 1899..1929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1964..1994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2033..2448
FT /note="Condensation 2"
FT /evidence="ECO:0000255"
FT REGION 2471..2863
FT /note="Adenylation 3"
FT /evidence="ECO:0000255"
FT REGION 3092..3557
FT /note="Condensation 3"
FT /evidence="ECO:0000255"
FT REGION 3578..3997
FT /note="Condensation 4"
FT /evidence="ECO:0000255"
FT REGION 4022..4412
FT /note="Adenylation 4"
FT /evidence="ECO:0000255"
FT REGION 4659..4986
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 1964..1987
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 3036
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 4583
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 5068 AA; 557199 MW; 93C1A4E9E6D76FCD CRC64;
MSRFSCIFPT LTDGYVPNLD QTRAAGRRTY TIDRRGWTAP SSQTESHILA AWGLVLSSYV
GTDEVAFYIV PTTGPDTTAL AELKVEGDMS RRSLINAAEQ LLHPGPVGAG QVSGESANTI
ITFEKDIESL FVTQAEAANV GTAMAQALAE VGADDHNRLI KNLNLMSPTH LESIWQFNAN
VPGMWEECFH DVIERRAANR PHSLAVDAWD MKLTYADLVR EARLLAAYLQ HRGVRPGSVV
PISFERSGAA LVAMLAVSKA GGAFVSVPPT LPAGRLDAIL EVIEAPFVVT WSKYEPFWAE
RLPTLPIDSY PKPSADATVK TLGKPEDLFY VIFTSGSTGR PKGCMLSHSN WLNGALRNAP
SWKYGPESRV LQMLSHTFDM SLLEICTSLG SGACVCVPRT EEIETSVSDA INRWQVNHVI
MTPSLARSLR RDDVPGLKTM CLGGEAFPRE IVTMWSERIN LWQFYGPSEC SINSSSRPIT
RPDADPLNIG PPNSAACWVV DTQDYNKLVP VGAIGELLVS GPIVGMGYLK NPIKTAEAFL
DEVGFVAKDD PQFGGFRFYR TGDLVRWNSD GTITFCGRAD TQVKLNGQRL ELAEVEYQLG
LEAGVQYAIA MAPQSGRCKN NLIAVLTVKC GGASNQGNAD DEIPLLDRHD PIVQQTVKKL
RSQLQHALPR YMVPTIWAFV GRMPMSPSGK IDRVQLRNWV QEMSQETFDA ITGRSFEAED
HVLGLSQLEQ EIQLAWAEAL GLSAAEVGLQ QPFVALGGDS IKALDAVARC RARQIKISMV
HILSCEGVRE ASSLAEVQET PAHQVAEIAV DYSDLWTRLS TEYDISKLGV TQVEEVEDVF
PCTTMQEGMF LGQIRRPGAY HMRFFHRVQL KGGSLPTVER IQQAWASLVE RHPSLRTVFV
DDLSSEAIYH SVVLRSVPME LTMREVPRDL NPESALAMFT EELVPFRPNA PLHRMLLLTC
RGRVPYLMLE ISHVIMDGYA LSVFRREFIR ACSSTASLPR GPDYRMFANY HRTRQTDESA
KYWTNYLADC VPCHIPTDPL SVPTDASPEW PRTLQRRDFG FDNSVAFLQR CKERQVTLAC
AIRAAWALVL RAYTQSRDVC FGYVSSGRNV PVPEVETIFG LCLSMQVCRA KLSEASTIAS
LARKIQEDYV ASLPFQHYPL AEAQRGLKQT HGQGLFNTAI SMEWVPPTAE DEDALLDLEE
IREQDDPTEY DIAISVDIHE GHIKLGFLYW PNLSDFQITH LAEALQGAMN CFAFQPDVAL
NTLTLLQASD LCSTLTNGPT LLPLEAVRGN VISMIDRWVT RQPESPAIDG WDGSLTYKQL
HEQSSWVARN LLHQGVKLGD RILVCADRSS RTVVTILGVV RAGCVLVLSN PTDPEKRLQW
LAHKCNATLV VADPAYEERF ATSGARVFST TSVCAPAAWD YEFSALDDQD LVSILFTSGS
TGTPKGILMD HGALATSVLL GHGRTLRFSR HTRMLHFASL TFDAALAEIF TTLAHGGCIC
VPCEEDRLSD VSGCISRFAV NTAMLTPSVG RLLDPEALPT LKALAMIGEP MSRLDVERFA
PVLDLYNGAG PTETSIMVTI AGPMKPTDEP VNLGYAVAGV RLWVTEAENP NRLAPLGAVG
ELIVEGRLVT RGYLDDPART RESFLPNLPW LPSQHALYRT GDLVRYAEDG SLRYMGRKDT
QVKLRGQRIE LQEVEYHLRK SLQQAQVVVE MVIPEGKIRA QASLVAFVSG LTAADVESSS
ARNFDQSMPM SQIALPGSTI QALEEALPRY MIPSVYFALD TIPLSVNGKA DRRRLREIGA
ALLVSSTAHK NTVDGKSEPV KWTASSKLEL TLLELWTTTL GLEAETIYGD DSFFELGGDS
VSAMKLVATA RDRFKLSLSV PQMFRHPTIH QLAAILGEAT GQPESSASST TEEGFTFSTP
DDSSTNDGVD DDFLRLATAQ LAQLAQEKGK KVDIAALLKQ LQGGSSSCKT PSVSSSSSSS
SSRKKKSAKV VSPVEAPAPV PVPFSLLDGG ADVVEKIRAQ AVEQCKILPG DIEDIYPATA
LQEGMMALMA RTPGVYTTTL TCELPERVNL ARLHSAWDKA AEAHPILRTR IILTENNTAV
QVVQRAKELP WDAYSLQDGD PLPDLTSNMT LGSTLLRLAE IHRQNQPRML LVAIHHALYD
GWSMPLLKQA VEDVYHGQEL WPQPFTPFIN YLNEGKPAAQ GYWTAHLDGF AGSVFPNLPS
INHHIQPTER RTRSLAVPTA PPGSQYTMAT KIQAAWAVTV SRYAEAEDIV FGTVSTGRSA
PVPSIDRMVG PTITTVPVRI SLGNQAERLT SLLQRVQEDG WNRMDHEHLG LQHIRRLGES
AAAACNLQTL LVIQPREEPR AKSISTLLSG LQDVAELKGV DTYPLMLVCE PDGVSLHLTA
VFDPAVLDAV MLDRMLAHWE LVLNQIWSEP DMAVMGLDGV SYRDKQTLVR WNAGEKIADG
CAHDAVYEWS VRTPHAPAVF AWDGKWTYEE LEKCSSLIAS QVLVHGVSSG DFVALYHEKS
RWAAAAILAV FKAGGILVTL DPAHPKDRIK DILDQARPRL VLTSQSLLDE ARELETPVMV
VQFAASQPMP GECFPLPTVS PTQAAYAPFT SGSTGRPKGI PLEHRGLAAS TASVARACLL
RPASRVLHFA SFAFDASMME HLIAWHAGSC LCIPVETVRQ TDLARCIRDF EVTWAFLTPS
CLRLISPDDV QSLEALGLGG ESMTPEDIFI WGPRLRQIVQ LYGPAECSIV AALTEVTKPS
ENRLIGRPNA CRCWVVDPHS PDRLAPLGAV GELVIEGITV GRGYIDDPER TTQAFIPPPT
WIQTLYPNEQ QPSRLYRTGD LVRYAGTDGK LTFIGRRDGQ LKLHGQRIEL ADVEAHLRPL
IPGTQKVVVE MVHSVGNHHP LLAAFVEEIL TSQDQVEQVV NLLHPSQTQC ALNVKAIDSA
LSQTVPQYMI PSMYLHISRL PLSASGKLNR RHLRRLVAEF PRQRLSEYAA GSGLAVPNRP
ATAQEREMQA IWARVLSVDP DTIGVNEDFF RIGGDSISGM QVATRCNAAG MHITSADLFQ
HRTIEQLMRH LSANGKTGSA SISLPPEPVD EWVPLAPIQQ LFFEIAPQGP DHFNQSLLLR
TSRRVSAEKL AGGLDILVGR HSMLRARFCR DDSGQWSQQV RSRGPYPASA FYRLTTHNHI
APELLSSLLA ASQMALSIQE GPLLAVDLVN LTDDTQLVYL VAHHLIIDLV SWRILHAELE
EYLQTGSFAS TTGSVPFLTW SRAQAEYSAN HLTPTLPLPG FQEANDGFDA SRYWGISCES
NTFGQTSTST FTLDQTVTDQ LFGPANNVLD TRPAEILQAA LWYSFTQSLT DRPGPSIYVE
GHGREPWTGS IDLSGTVGWF TTMSPLVSAP WDSLSQTSMR DFLDALSYIK DQRRRIPANG
WAYFTSRYLN DEGKVAYGRM KPVVEILFNY MGQYQEMNRE DAILQLAGDG IQSGTGAADV
ADNVPRFSLI DVSAFISNGC LTFQFILPKS LQQDSRLQGC FQEYERTLVA AANSLSTEGP
RKTLADFPLM PALTYDQLSQ CLDHTLPSMG LCARDVVDIY PCSPVQQGML LAQLRDRQAY
QQRFRFQVKS RGSTDRLTLE KLKDAWTEVI NRHDILRTLL LPVSDYSHLD QVVMAPGSLQ
HLVRINAMDT NPTQGLPHSI NITSDSTGTV ICEWNVSHAL VDAMSIAVIQ QEVNEALEGS
LGQHQKTPRY ADYIQWLSLQ DNTETQAYWK KYLEGVEPCL FPKLASSTDK VNPEGTISAI
RATWTRDSRL DKLCHTHGIT LTNLFHIVWS LLLSAYLGTD KVCFGYTTLG RDVPVDGVEK
MVGPLVNVIA TTIQLQEDDS ILDALLTHQT HLSNSLQHQH YALADVYASL GLVGSQLFNT
IVSLQDISHF DANDERPTRV EMLPANDVSE YDVALNIGVD QSSIQVVCSY RTLSLSVEQA
DALLRTTSHV LDEILRDPKQ PLRDLEVISP QCKEQLVKWN AAMPAPTDEY IHEKIQDQCR
LHSSREAACA WDGIFTFAEV DDLSSRLAAR LIRMGVTSGH IIPIYSPKSR WTVIAILGVL
KTGAAFTLLE TSHPTARLRV ICNEIKADII IAPASHAVPA ATLAPILVVL DSITSMSPQE
SDLLPAVGMP PAAEALAYLI FTSGSTGNPK GVMVTHQNLC SNASIMTTSV NMTSDSRVLH
FASHAFDACL WEIFGALFAG ACLIIPSESE TKEDLAGCIE RMVVTWAFLT PSVARILKPE
ALPSLRNLVL GGEPIAASDL DMWRGHVQVV CAYGPTETAI LASTTSPSTF PSDGKDIGVP
TGSSLWIVDK QNYNKLAPHG ATGELLIEGP NVSQGYLGDP EKTNEAFPVA PRWLSQLRKS
PTRVYRTGDL VRFNTSTGTI HFVGRKDNQI KFHGQRIELG DIEHHAQQAF SNASMVIVDL
ITPEQPQQPY IVAFVHQADT RTGTADPIDT ILLPPSESFR ADAIGAQNHM HKRLPHYMVP
TAFLPLHRLP LSGTGKADRK RLRQCALSLS SLELNAYRAT ASAKRMPFTA AECKMQELVA
TVLGRDMSEI GMDDSFFYLG GDSIQAMRLV SEGRQQGLTL SLQAIFDAPR LGDLAYRTAN
LVRVSEPAPP TLPATSSDDC DHKETIVAAL PIKKTDVAEV LPTTSFQRTW LDSQLKSYIV
VDIPGPIDLA RLRTAIQRVV KAHPILRASF VPYETTTMQV ILRTAVVITE ADLSTTTVEG
ICRKDANAPM APGTPYLRVI LATQGEVDRK LIMRLSHAQY DGISLSLLMN DLSHAYASES
RPLPSSHLPA FNDYITYQQT QGADPTATTF WHRLLKDVPI TYLDLQPAET PTSNGSLITR
TRDINIAAFP SLPNGITTAT AVKAAWSLVL AQKTGSLAVI FGQVVHGRGI ALTGVEGIVG
PCANITPVVA RLGPQTTRME LMQTLQDQHR SAMPYETVSL DDALAYTKDS QAGRKELQTI
VQHQNNVMAD DMELSLGEAR CRVDLRAVDH VPQEVWVYSS IDGGRPGMLE VKIMSSTLVL
SEEVAEELMD LLVEMMKRLF SDPEGVCV
//
