MLFA_ASPBC
ID MLFA_ASPBC Reviewed; 5112 AA.
AC A0A1L9U7P9;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 23-FEB-2022, entry version 22.
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=ASPBRDRAFT_34020;
OS Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767769;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101740 / IMI 381727 / IBT 21946;
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, DOMAIN, FUNCTION, DISRUPTION PHENOTYPE, 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. MlfA probably
CC acts iteratively on one amino acid and possesses multiple amino acid
CC specificities since it is involved in the biosynthesis of multiple
CC malformins, including malformin C and malformin A2. Malformin C
CC corresponds to a cyclo[D-Cys-D-Cys-Val-D-Leu-Val] pentapeptide whereas
CC malformin A2 corresponds to a cyclo[D-Cys-D-Cys-Val-D-Leu-Ile]
CC pentapeptide (PubMed:30560908). The malformin biosynthesis clusters in
CC malformin-producing fungi also contain enzymes involved in the
CC formation of the disulfide bond between the two consecutive cysteins
CC within malformins, in addition to additionnal tailoring enzymes such as
CC methyltransferases or oxidoreductases. They are also composed of up to
CC 4 major facilitator superfamily transporters, and transcription factors
CC probably involved in the regulation of the expression of those clusters
CC (Probable). {ECO:0000269|PubMed:30560908, ECO:0000305|PubMed:30560908}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|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 -!- DISRUPTION PHENOTYPE: Leads to a total abolishment of malformin A2 and
CC C production. {ECO:0000269|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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV878693; OJJ67652.1; -; Genomic_DNA.
DR SMR; A0A1L9U7P9; -.
DR STRING; 767769.A0A1L9U7P9; -.
DR EnsemblFungi; OJJ67652; OJJ67652; ASPBRDRAFT_34020.
DR VEuPathDB; FungiDB:ASPBRDRAFT_34020; -.
DR OrthoDB; 4243at2759; -.
DR Proteomes; UP000184499; 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; 3.
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; Reference proteome; Repeat.
FT CHAIN 1..5112
FT /note="Malformin synthetase mlfA"
FT /id="PRO_0000446429"
FT DOMAIN 757..830
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:30560908"
FT DOMAIN 1854..1931
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:30560908"
FT DOMAIN 3030..3106
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:30560908"
FT DOMAIN 4593..4669
FT /note="Carrier 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:30560908"
FT REGION 225..616
FT /note="Adenylation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30560908"
FT REGION 868..1299
FT /note="Condensation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30560908"
FT REGION 1327..1716
FT /note="Adenylation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30560908"
FT REGION 1926..1961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1994..2034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2064..2479
FT /note="Condensation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30560908"
FT REGION 2502..2894
FT /note="Adenylation 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30560908"
FT REGION 3122..3586
FT /note="Condensation 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30560908"
FT REGION 3607..4044
FT /note="Condensation 4"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30560908"
FT REGION 4069..4459
FT /note="Adenylation 4"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30560908"
FT REGION 4724..5106
FT /note="Condensation 5"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30560908"
FT COMPBIAS 1928..1955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1994..2018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 791
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1891
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3067
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 4630
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 5112 AA; 563090 MW; 60BC6ED30CA7BC27 CRC64;
MSRFSCIFPT LTDGYVPNPD HTRAAGRRTY TIDLSGWNGS SGQAESYILA AWGLVLSSYV
GTDEVAFYVV PTTGPDTTAL AELKVEGDMS RLSLTDAAEQ LLHPKHVGAG QISGETANTI
ITFANDIESL FVTQTEESFL LLHVHRDEKG HISLTLTYYL SLLTDAQAAN VCTAMSQALA
VVTTDHPERL IKDLNLMSPT HIDHIWKFNA NVPGPWEECF HDVVERHAAN RPHSLAVDAW
DMKLTYAELV REAHLLAAYL QQRGVRPGSV VPISFERSGA ALVAMLAVSK AGGAFVSVPP
NLPAGRLDAI LEVIEAPFVV TWSKYEAFWS ERLSTLPIDN YPKPSGDATV ESLGKPDDLF
YVIFTSGSTG RPKGCMLSHS NWLNGALRNA PSWKYGPESR VLQMLSHTFD MSLLEICTSL
GSGACVCVPC TEEIETSVSD AINRWQVNHV IMTPSLARAL KPDDVPGLKT MCLGGEAFPK
EIVTMWSERI NLWQFYGPSE CSINSSSRPI TRPDADPLNI GPPNSAACWV VDAQDYNKLV
PVGAIGELLV SGPIVGMGYL KNPVKTAEAF LDQVGFVSKD DPQFGGFRFY RTGDHVRWNS
DGTITFCGRA DTQVKLNGQR LELAEVEYQL GLEDGVQYAI AMSPQTGRCK NNLIAILTVK
GTNCSNQRNA ADEIPLLDRR DPIIQQTVKK LRSQLQHALP RYMVPTIWAF VGRMPMSASG
KIDRVQLRNW VQEMSQETFD AITGRSFEAE DHVLGLSRLE QEIQLAWAEA LGLSAAEVGL
QQPFVALGGD SIKALDAVAR CRTRQIKISM VHILSCEGVR EAASLAEVQE TPAQQVAEMA
VDYSDLWTRL STEYDLGKLG VTQVEDVEDV FPCTTMQEGM FLGQIRRPGA YHMRFFHRVQ
LKGGCLPTVD RIQQAWASLI ERHPSLRTIF VDDLSPDAIY HSVVLRSVPL ELTMREVPRD
LSPEDALAMF TDELVPFRPN APLHRMLLLT CRGRVPYFML EISHVIMDGY ALSVFRREFI
QACSSTGPLP RGPDYRMFAN YHRTRQTDDS AKYWTNYLSD CVPCHIPTHA VIAPTDAPPE
WPRNLQRRDF SFNNSAAFLQ RCKERQVTLA CAIRAAWALV LRAYTQSQDV CFGYVSSGRN
VPVPEVETIF GLCLSMQVCR ARLSESSTIA SLARKIQEDY VASLPFQHYP LAEAQRGLKQ
THGQGLFNTA ISMEWVPPTA EDGDALLDLE EIREQDDPTE YDVAISVDIH EGHIKLGFLY
WPNLTEFEIA HLAEALQGAM NCFAYQPDDA LDSLTLLQAS DVCSTLADGP TLLPLEAVRV
NMLSMIDRRV TRQPDTPAIE GWDGSLSYKQ LHEQSCWVAR NLLHQGLQLG DRVLVCADRS
SRTVATILGL VRAGCVLVLS NPTDPDKRLH WLAEKCNAAL IIADPAYEKR FATAGSRVLL
TTAVCSPAAW DYEFPALDEH DLISILFTSG STGTPKGILM DHGALATSVL LGHGRTLRFS
RQTRMLHFAS LTFDAALAEI FTTLAHGGCI CVPTEEDRLS DVPGCISRFA VNTAMLTPSV
GRLLDPTALP MLKSLIMVGE PMSRLDVERF APVLDLYNGA GPTETSIMVT IAGPMTPTDE
PTNLGHSVAG VRLWVTEAED PNRLAPLGAV GELIVEGRLV TRGYLDDGER TQQAFLPSLP
WLPSQHALYR TGDLVRYADD GSLRYMGRKD TQVKLRGQRI ELQEVEYHLR KSLQQAQVVV
EMVIPEGKTR AQASLVAFVS GLTAADVESS SACNSEESMT ISQVVLPKST IQTLEEALPR
HMIPSVYYAL ETIPLSVNGK ADRRRLREMG ASLLASSAAN KSTADGKKEP AKWTAASELE
RTLLELWATT LGLEVEAIHG DDSFFELGGD SVSAMKLVAT ARDKFKLSLS VPQMFRYPTI
RQLAAELGES PRSSTSSASS STEDEFTIST PDDSSTNDGV DDDFLQLATA QLAQLAQEKG
KKVDIAALLK QLQGGSSSSK TPSVSSSSSS SSSRKKKSSK AAFPVEAPGP VPEPFSLLNG
DADVVEQVRA HAAEQCKIPH EDIEDIYPAT ALQEGMMALM ARTPGVYTTA LTCELSSQID
LARLHSAWDK AAEAHPILRT RIIMTDDNTA VQVVQRAKGL PWDRYTLQDG ESIPNLTSDM
TLGSPLLRLA EIHRHSKPPM LLVAIHHALY DGWSMPLLKQ AVEDAYHGQT LQPQPFTPFI
NYLKEGKRAA QDFWTAHLDG FAGGVFPNLP SIDHHIQPSE RRSRSLTIPT AVSRNQYTMA
TKIQAAWAVT VSRYAEDEDI VFGTVSTGRS APVPAIDRMV GPTITTVPVR ISLGDQAQRV
SPLLQRVQED GWNRMDHEHL GLQYIGRLSE SAAAACRLQT LLVIQPREES HANSGATLLS
GLQDSAELEG VDTYPLMLVC EPDGASLHLT AVFDPLVLDR TILERMLAHW ELVLTQLWTE
PDMAVVDLDA VSYSDKQTLV QWNVGEKIAD GCAHDAVHEW SIRTPHAPAV CAWDGEWTYE
ELDKCSSLLA SQILEHGVTS GDFVALYHEK SRWVAAGILA VFKAGGILVT LDPAHPKDRI
RDILDQTQPR LILTSQSLLG EARELDTPVL CLQFAASQPV PERCSSPPTV SPTQAAYAPF
TSGSTGRPKG VPLEHRGLAA STASVSRACL LRPASRVLHF ASFAFDASIM EPLVAWHAGG
CLCIPDETAR QTDLARCIRD FDVTWAFLTP SCLRLITPDD VQCLEALALG GESMTPEDIS
IWCPRLNQMV QLYGPAECCF VAALTEVTKP SENRLIGRPN ACRCWVVNPK SPERLAPLGA
IGELMVEGIT VGQGYINNPE RTTQSFIQPP TWLQALYPDE EQPRHLYRTG DLVRYAGEDG
KLTFIGRRDG QVKLHGQRIE LADVEAHLRP LIPAKHNIVV EMISSVDNQH PLLAAFVEEP
SPSQGPQEQH IGLIHPSEAQ YALNVKTIDG ALSRTVPQHM IPSMYLHISR LPLSSSGKLN
RRQLREMVAQ LPRQKLNEYA AGSCEMASQR PTTAKECEMQ AIWARVLAAD PDTIGLNDDF
FRIGGDSISG MQIATKCNAA GMHITSADLF RHRTIAQLLF HLRNAKKRGD AISLPAEPVE
EWVDLAPIQQ LFFEIAPEGS SHFNQSLLLR TSRHISVEEL TAGLDILVKR HSMLRASFRR
SESGHWSQQV RSLDSPAGTF YRLATHNGIT RESLPSVFTT SQTSLSIQEG PLLAIDLVEL
TDGSQLLYLV AHHLVIDLVS WRILHGELEQ YLQTGSLEPV TESVPFLTWS RAQAEYSAKH
LTPVSALPRF QEAHDEFDGA RYWGIPPESN TFGQTSTFRF TLDQTATDTL FGTGNNVLGT
RPVEILQAAL WYSFTQSLTD RPYPSIYVEG HGREPWADSI DISGTVGWFT TMSPLVFAPW
DSLSRTSMED FLDALSYIKD QRRRVPANGW AYFTSRYLND EGKVAYGRMK PVVEILFNYM
GQYQEMTRED AILQLAGDDI QSGTGAADIA DDVPRFSLID VGAFTANGCL SFEFIFPECI
QRDARLKLWV ENCERMLLSA AKLLSNEGPR KTLSDFPLMP ELTYEQLSQC FEHTLPSMGL
SASDVVNIYP CSSVQQGMLL AQLRDPQAYQ QRFKFHVKSD ERRLTLEQVK DAWREVINRH
DILRTLLLPV SDHGHLDQVV MAPGSLQHLV RIDATDVNLT QGIPHSINIT RDSSGTVVCE
WNVSHVLVDA MSVAVIQLEV SQSLDGLLGQ HEKPGQYADY IQWVSRRDKT ETQAYWQRYL
EGVEPCLFPK LTSTSDNVKP EGTISAVRAT WDRDARMDEL CQKHGITLTN LFHIVWALVL
GAYVGTDDVC FGYTTLGRDV PVDGVEMMVG PLVNVLATTV QLRDEDSILD ALRTHQAHLT
NSLQHQHHAL ADVYASIGLV GSQLFNTIVS LQDVSHFDAP DEQSTRLEVQ PANDASEVCH
YLLVYKCFIF FDVNFRKYDV ALNIGVGSSS IQLVCSYRTL SLSAEHADTL LRTASHVLSE
ILRDPTQRIQ EIEIISPECK EQLVKWNPTV PAPSDEYIHE KIQGQCRLHS SRQAVCAWDG
IFTYAELDDL SSRLAVRLTR MGATSEHIIP IYSPRSRWTV IAILGVLKTG AAFTLLEVSH
PMNRLQEVCK QIDASVIIAP ASHATSAASL APILVVLDNI TSMTPGQSES SPAVRMPPAS
EALAYLIFTS GSTGNPKGVM VTHQNLCSNA SIMTTSVNMT ADSRVLQFAS YAFDASLWEM
LGALFAGACL VIPSESESKE DLAGCIDRMA VTWAFLTPSV ARILKPERVP QLRVLALGGE
PIAVSDLDTW RTHAQVVCAY GPSETAILAS TTSPSTIPTV GKDIGMPTTC SLWIVDKRDY
QKLAPLGATG ELLIEGPNVS KGYLGDPEKT NEAFPVAPRW LSQLRQSPTR VYRTGDLVRF
DQSTGTLRFV GRKDNQIKFH GQRIELGDIE NHAQQALPNA STVIVDLISP GESQQSYLVA
FVYQPDTSTQ TADAIDPILL PPSESFRTDA LAAQKHMHDR LPHYMVPTAF LPLNCLPLSN
TGKADRKRLR HCALALSGSE LNAYRATATA KRMPSTEAEC IMQQLIATVL GRDASEIGMD
DSFFHLGGDS VQAMRLVSEG RQQGLTLSLR TIFDSPRLDD LARHNSLVQD DQPAAASPAT
MHDTFSLIDK LVSTYPIDKA AVVDILPTTS FQRHWLDAQL KSYIVVDIPG RISRDRLFTA
MQRVVDAHPI LRTSFVPHDN TAVQVILRTA FAITDADLST TTVEDLCRQD ANAAIAPGAP
YLRVILATGE FGYKLIMRLS HAQYDAVSLS LLMNDLGHAY ENDTHELPSS YSPSFTDYIT
YQQRQKVDST ATTFWRHLLQ DVPLTSLDLQ PSKPSTSNGT PITRTRDINI ATFPQLPNGI
TLATAVKAAW SIVLAQKTNS PAVIFGQVVH GRGIPLPGVE GIVGPCANIT PVVARLSPQT
TGLELLQALQ DQHRSGLSYE AVDLDDALAY TKGWQAGSPR VQTIVQHQNN VMTDGMGLSL
GEVKCGVDVR AVDHVPREVW VYSSVDENKP GMLEVKIMSS TLVLSEEVAE ELMDLVVEKV
VALLRDPRGV CV
