MLFA_ASPLC
ID MLFA_ASPLC Reviewed; 5082 AA.
AC A0A1M3T4K3;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 23-FEB-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=ASPFODRAFT_65064;
OS Aspergillus luchuensis (strain CBS 106.47).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1137211;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 106.47;
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; KV878250; OJZ81665.1; -; Genomic_DNA.
DR SMR; A0A1M3T4K3; -.
DR EnsemblFungi; OJZ81665; OJZ81665; ASPFODRAFT_65064.
DR VEuPathDB; FungiDB:ASPFODRAFT_65064; -.
DR OrthoDB; 4243at2759; -.
DR Proteomes; UP000184063; 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; Repeat.
FT CHAIN 1..5082
FT /note="Malformin synthetase mlfA"
FT /id="PRO_0000446434"
FT DOMAIN 749..822
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1846..1923
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3024..3100
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 4560..4636
FT /note="Carrier 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 225..616
FT /note="Adenylation 1"
FT /evidence="ECO:0000255"
FT REGION 860..1291
FT /note="Condensation 1"
FT /evidence="ECO:0000255"
FT REGION 1319..1708
FT /note="Adenylation 2"
FT /evidence="ECO:0000255"
FT REGION 1924..1953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1986..2012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2058..2473
FT /note="Condensation 2"
FT /evidence="ECO:0000255"
FT REGION 2496..2888
FT /note="Adenylation 3"
FT /evidence="ECO:0000255"
FT REGION 3117..3582
FT /note="Condensation 3"
FT /evidence="ECO:0000255"
FT REGION 3603..4022
FT /note="Condensation 4"
FT /evidence="ECO:0000255"
FT REGION 4047..4426
FT /note="Adenylation 4"
FT /evidence="ECO:0000255"
FT REGION 4673..5000
FT /note="Condensation 5"
FT /evidence="ECO:0000255"
FT COMPBIAS 1924..1947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1986..2008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 783
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1883
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3061
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 4597
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 5082 AA; 559619 MW; 9EDF479B8051EC4C CRC64;
MSRFSCIFPT LTDGYVPNPD HTRAAGRRTY RIDLSGWKAP GSETESLILA AWGLVLSSYV
GTDEVAFYVV PTTGPDTTAL AELKVEGDMP RQSLTYAAHQ LLHPGLVGAG QVSGETANTI
ITFANDIESL FVTQTEESFL SLHVYRDEQG HISLSLTYYL SLLTDAQAAN VGTAMAQALA
EVGTCDNDKL VKDLSLMSPA HLEHIWRFNA DVPGIWEECF HDVIERHAAN RPHSLAVDAW
DTKLTYTDLV REARLLAAYL QRRGVGPGSV VPISFERSGA ALVAMLAVSK AGGAFVSVPP
NLPAGRVDAI LEVIEAPFVV TWTKYESFWA ERLPTLPIDN YPKPAADATV EALGKPEDLF
YVIFTSGSTG RPKGCMLSHT NWLNGALRNA PSWKYGPESR VLQMLSHTFD MSLLEICTSL
GSGSCVCVPR PEEIETSISD AINRWQVNHV IMTPSLARAL RPDDVPGLKT MCLGGEAFPK
EIVTMWSERI NLWQFYGPSE CSINSSSWPI TRPDADPLNI GPPNSAACWV VDVHDYNKLV
PVGAIGELLV SGPIVGMGYL KNPVKTAEAF LEEVGFVAKD DPQFGGFRFY RTGDLVRWNS
DGTITFCGRA DTQVKLNGQR LELAEVEYQL GLEAGVQYAI AMAPQAGLCK NNLIAILTVK
GTSTGTQDTA ADEIPLLDRR DPIVQETVKK LRSQLQHALP RYMVPTIWAF VGRMPMSASG
KIDRRMSQET FDAITGRSLE AEEHAFGLSR LEQKIQLAWA EALGLSAAEV GLQQPFVALG
GDSIKALDAV ARCRARQIKI SMVHILSCEG VREAASLAEV QETPAQQVAE MAVDYSNLWT
RLSNDYDLDK LGVTQVEEVE NVFPCTTMQE GMFLGQIRRP GAYHMRFFHR VQLKGGCLPT
VERIQQAWAS LVERHPSLRT VFVDDLSPEA IYHSIVLRSV PMEVRMREVP RDLSAEAALA
IFTEELVPFR ANAPLHRMLL LTCRGRVPYL MLEISHVIMD GYALSVFRRE FIRACSSSAP
LPRGPDYRMF ANYHRTRQTD DSARYWTDYL ADCVPCHIPT HAVSAPSDGP PEWPRTLQRR
DFGFENSAAF LQRCKERQVT LACAIRAAWA LVLRAYTQSE DVCFGYVSSG RNVPVPEVET
IFGLCLSMQV CRARLSEAST IASLARKIQE DYVASLPFQH YPLAEAQRGL KQTHGQGLFN
TAISMEWVPP SAEDEDALLD LEEIREQDDP TEYDIAISVD VHEGHIKLGF LYWPDLTDFE
INHLAEALHG AMNCFASHPD EALNTLSLLQ ASDVCSALSD GPTLLPLEAV RGNVVSMIDR
WVTRQPEGAA IDGWDGSMSY KELHEQSSWV ARNLLHQGVR LGDRVLVCAD RSSRTVATIL
GIVRAGCVLV LSNPTDPEKR LQWLAKKCNA SLVVADPTYE ERLATADAHV LSTTSVCAPA
AWDYEFPALD EHDLISILFT SGSTGTPKGI LMEHGALATS VFLGHGRTLR FSRHTRMLHF
ASLTFDAALA EIFTTLAHGG CICVPCEEDR LSDVPGCISR FAVNTAMLTP SVGRLLDPGA
LPTLQTLIMV GEPMSRLDVE RFAPVLDLYN GAGPTETSIM VTIAGPMKPT DEPVNLGYAV
AGVRLWVTEA ENPNRLAPLG AVGELIVEGR LVTSGYLDDQ ARTQEAFLPT LPWLPSQHAL
YRTGDLVRYV DDGSLRYMGR KDTQVKLRGQ RIELQEVEYH LRKSLQQAQI VVEMVVPAGK
MRAQASLVAF VSGLTAADVE SSSACNLEGT IPISQIVLPK SAFQALEEVL PRHMIPSVYY
ALDTIPLSVN GKADRRRLRE MGSLLLASSA AHKNNIEGMS KSVKWTPTLE LERTLLGLWA
ATLGLEAETI HGDDSFFELG GDSVSAMKLV ATARDKYKLS LSVPQMFRYP TVCQLAAEVG
EPAGQSASSA SSTTEEGFTF STPDDSSTND GVDDDFLQLA TAQLAQLAQE KGKKVDIAAL
LKQLQGGSSS NKTPSVSSSS SSSSSSKRKK NAAKAESLAE AAAPIPVQFS LLDGGADALD
KVRAQAVEHC KITHEDIEDI YPATALQEGM MALTARTPGV YTTTLTGDLS EQVDIARLQY
AWGKAAEAHP ILRTRIILTD NNTAVQVVQR AKGLPWDTYS LREDNVLPDL TSNMTSGSPL
LRLAVVHRQS QPRMLLVAIH HALYDGWSMP LLKQAVEDAY HGRDLRPQPF TPFIKHLIAG
KPAAQDFWTT HLDNFVGGVF PKLPSIYHQI QPTERRTRSM TLPTAAPKAQ YTMATKIQAA
WAVTVSRYVE ANDIVFGTVS TGRSAPVPAI DRMVGPTVTT VPVRISLGGQ ADRVLSLLQR
VQEDSWNKLD HEHLGLQHIR RLGESAAAAC NFQTLLVIQP REQPDTKYRS TLLSGLQDVA
ELEGVDTYPL MLVCEPDGAS LNLTAVFDRA VLDGATLDRM LAHWELVLTQ MWNEPNMAVI
DIDAVSCSDK ETLMRWNTGE TITEGCAHNA VCEWSRRTPH APAVCAWDGE WTYKELERYS
SLIASQISAH GLSSGDFVAL YHEKSRWTAA GILAVFKAGA ILITLDPAHP TDRIKDILDQ
ARPRLILTSQ SLLDVARNLD TPVLSVQFAA SQPLPEEWSS LPTICPTLAA YAPFTSGSTG
RPKGIPLDHR GLAASTASIA RSCLLRPASR VLHFASFAFD ASMMEHLIAW HAGGCLCIPD
ETARQTDLAK CIRDFNVTWA FLTPSCLRLI TPDDVPSLQA LGLGGESMTS EDITIWSPRL
RQIVQLYGPA ECCIVAALTE VTKPSENRLI GRPNACRCWV VDPQNPDRLA PIGAVGELLI
EGITVGRGYI NDPDRTTPAF IRPPKWLQTL YPDDQEPKRL YRTGDLVRYA GVDGKLAFIG
RRDGQLKLHG QRIELADVEA HLRSLIPGMQ KMVVEMVHSA DNQNPFLAAF LEEISTSQKP
KEREIGLLHP SQSQCALDVK AIDSALSRTV PQYMIPSMYL HISRLPLSAS GKLDRRHLRE
MVAELPRQSL NEYAAGSGLG VPDRPVTSQE HEMQAIWARV LSLDPNTFGV NDDFFRIGGD
SISGMQVSTK CNAAGIHITS ADLFRHRTIE QLICHLNTIR TTDSASVLLP TEPVNEWVAL
APIQHLFFEV APEGPNHFNQ SLLLRTSRRV SVEELAGGLD VLIGRHSMLR ARFCRKDSGQ
WFQQVKSLDS EPASAFYRLA AHNHITRESL RTLFTAAQMA LSIEDGPLLT VDLVELEDGS
QLVYLAAHHL IIDLVSWRIL HGDLEEYLQT GSLSSATGSV PFLTWTQLQA EYSAEHLTPA
RALPGFQEAN DDFDFMRYWG ISSESNTFGQ TSTSRFALDR TVTDILFGSA NKVMDTRPVE
ILEAALWYSC NQALPDHPGP SIYVEGHGRE PWTDSIDVSG TVGWFTIMSP LVSTPWHHLS
RKSMRDFVDV LSYIKDQRRR IPANGWAYFT SRYLNDEGRV AYGRTKPVME VLFNYMGQYQ
EMKREDAILQ LAGDDIQSGT GASDIAGNVP RFSLIDVTAF TANGCLTFEF TFPQLIQQDA
RLEQCIKECE HTLVAAASSL SAEGPRKTLT DFPLMSALTY DQLSQCLNHT LPSMGLRAQD
VWNIYPCSPV QRGMLLAQLR DRQAYQQRFK FQVMSRGPTE QLSLEKVKDA WTEVINRHDI
LRTLLLPVSD HSHFDQVVMV PGSLQHLVRG DAMDANPTEG LPHTINITSD STGAIICEWN
VSHALVDAMS IAFIQREVNQ ALEGSLGQHQ NLPQYVEYIK WLTLQDNTEA QAYWQNHLNG
VEPCLFPKLT SSPDKVNPEA TISAIRATWS RDVRMDELCH KHAITLTNLF HIVWAIVLGA
YVGTDEVCFG YTALGRDVPV HRVETLVGPL VNVLATTVRH QEDETILNAL LTHQAHLTNS
LQHQHYALAD VYASLGLVGS QLFNTIVSLQ DTSHFDAPDE QRTRLEMLPA NDVSEYDVAL
NIGVDKSTIQ LVCSYQTVSL SAEQADALLR TAFHVLDEIL RDPTQRFCEL EVISPKCKEH
LVKWNAGMLA PTHEYIHEKI QGQCRIHNSR QAVFDDLSSR LAARLIRMGV TSEDIIPIYS
PKSRWMVIAI LGVLKAGAAF TLLEISHPMA RLRVICNQIK APMLIAPASH AVPAANLAPI
LVVLDNITSL AEERPVSLPA VDIPPAREAL AYLIFTSGST GNPKGVMVTH QNLCSNASII
TTSVNMTSDS RVLQFASHAF DGCLWEILGA LLAGACLIIP SESENKEDLT GCIERMGVTW
AFLTPSVARI LKPETLPSLC NLVLGGEPIA ASDLEMWRGH VQVVCAYGPT ETTILASTTS
PSTFPRDGKD IGTPTSSSLW IVDTRNYQTL VPLGATGELL IEGPNVSQGY LGDPEKTNDA
FPDAPRWLSQ LRKSPTRLYR TGDLVRFDTS TGTIRFVGRK DNQIKFHGQR IELGEIEYHA
QFAFSSASTV IVDLITPEQP RQPYIVAFVH QLDAANETTD TNDTLLLPSS EVFRADALAA
QNKMHKRLPH YMVPAVFLPL HRLPLSVTGK ADRKRLRQCA LALSSPELSA YRATASTKRM
PSTAAERKMQ ELVATVLGRD PTEIGMDDSF FYLGGDSVQA MRLVAEGRQQ GLTLSLRAIF
DSPCLGDLSD QAKSLIEDNQ RASTASRGNL RYDCDRIDKI VVTNSLNKAD VVDVLPTTSF
QRHWLDAQLK SYIVVDIPGP IDPARLLRAM HRVVEAHPIL RVSFVPYETT TVQVILRTAV
AITNVDLSTA TVEELCRRDV DAQMAPGVPY LRVIIATQDK AGHKLIMRLS HAQYDAVSLS
LLMNDLSHAY ANDTHPLPSS HFPRFNDYIT YQQAQRADLT ATTFWRHLLQ DVPLTHLNLQ
PAESSASNGT PITLSRDIDI AVFPSLPSDI TIATMVKAAW SLALAQKTNS LAVIFGQVVH
GRAIALPGVE GIVGPCANIT PVVARLGLET TGLELMQALQ DQHHSAMSYE SVDLDDALAY
ANDSQAGRKG LQTIVQHQNN VMVDDMELSL GEVKCGVDFR AVDHLPKEVW VYSSVDEKRP
GMLEVKIMSS TLVLGEEFAE ELMGLLVEKI VGLLRHPESV CV
