ID MLFA_ASPEC Reviewed; 5044 AA.
AC A0A317VEE1;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 27-NOV-2024, entry version 21.
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=BO83DRAFT_417906;
OS Aspergillus eucalypticola (strain CBS 122712 / IBT 29274).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1448314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 122712 / IBT 29274;
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; MSFU01000015; PWY71312.1; -; Genomic_DNA.
DR SMR; A0A317VEE1; -.
DR VEuPathDB; FungiDB:BO83DRAFT_417906; -.
DR OrthoDB; 2787863at2759; -.
DR Proteomes; UP000246171; 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 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; 4.
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; 4.
DR PROSITE; PS50075; CARRIER; 4.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Ligase; Phosphopantetheine; Phosphoprotein; Repeat.
FT CHAIN 1..5044
FT /note="Malformin synthetase mlfA"
FT /id="PRO_0000446430"
FT DOMAIN 710..786
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1810..1887
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2984..3060
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 4522..4598
FT /note="Carrier 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 181..572
FT /note="Adenylation 1"
FT /evidence="ECO:0000255"
FT REGION 824..1255
FT /note="Condensation 1"
FT /evidence="ECO:0000255"
FT REGION 1283..1672
FT /note="Adenylation 2"
FT /evidence="ECO:0000255"
FT REGION 1887..1916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2018..2433
FT /note="Condensation 2"
FT /evidence="ECO:0000255"
FT REGION 2456..2848
FT /note="Adenylation 3"
FT /evidence="ECO:0000255"
FT REGION 3077..3533
FT /note="Condensation 3"
FT /evidence="ECO:0000255"
FT REGION 3554..3973
FT /note="Condensation 4"
FT /evidence="ECO:0000255"
FT REGION 3998..4388
FT /note="Adenylation 4"
FT /evidence="ECO:0000255"
FT REGION 4591..4615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4635..4962
FT /note="Condensation 5"
FT /evidence="ECO:0000255"
FT COMPBIAS 1888..1911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4595..4612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 747
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1847
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3021
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 4559
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 5044 AA; 555887 MW; 97278B6BC3E2FB0A CRC64;
MSRFSCIFPT LTDGYLGTDQ VAFYVVPTTG PDTTALAELK VEGDMSRQSL NYAANHLLHP
GLVGAGQVSG ETANTIVTFA DDIESLFVTQ TEESFLSLHV YRDEQGHISL SLTYYLSLLT
DAQATNVGTA LVQALAEVGT CDNDRLIKDL NLMSPAHLEH IWRFNADVPG IWEECFHDVI
ERHAANRPHS LAVDAWDTKL TYTDLVREAR LLAAYLQQRG VGPGSVVPIS FERSGAALVA
MLAVSKAGGA FVSVPPNLPA GRLDAILEVI EAPFVVTWTK YESFWAERLP TLPIDNYPKP
AADATVEALG KPEDLFYVIF TSGSTGRPKG CMLSHTNWLN GALRSAPNWK YGPESRVLQM
LSHTFDMSLL EICTSLGSGS CVCVPRAEEI ETSISDAINR WQVNHVIMTP SLARALRPDD
VPGLKTMCLG GEAFPKEIVT MWSERINLWQ FYGPSECSIN SSSRPITRPD ADPLNIGPPN
SAACWVVDVH DYNKLVPVGA IGELLVSGPI VGMGYLKNPV KTAEAFLDEV GFVAKDDPQF
GGLRFYRTGD LVRWNSDGTI TFCGRADTQV KLNGQRLELA EVEYQLGLEA GVQYAIAMAP
QAGLCKNNLI AILTVKGTST GNQDTAADEI PLLDRRDPVV QETVKKLRSQ LQHALPRYMV
PTIWAFVGRM PMSASGKIDR VQLRDWVQKM SQETFDAITG RSLEAEDHVL GLSRLERDIQ
LAWAEALGLS AAEVGLQQPF VALGGDSIKA LDAVARCRAR QIKISMVHIL SCEGVREAAS
LAEVQITPPQ QVAEMAVDYS NLWTRLSYDY DLDKLGVTQV EEVEDVFPCT TMQEGMFLGQ
IRRPGAYHMR FFHRVQLKGG CLPTVERIQQ AWASLVERHP SLRTVFVDDL SPEAIYHSIV
LRSVPMELRM REVPRDLSAE AALAMFTEEL VPFPANAPLH RMLLLTCRGR VLYFMLEISH
VIMDGYALSV FRREFIRACS SSTPLPRGPD YRMFVNYNRT RQTDDSARYW TNYLADCVPC
HIPTHAVSAP SDDPPEWPRT LQRRDFGFDN SAAFLQRCKE RQVTLACAIR AAWALVLRAY
TQSEDVCFGY VSSGRNVPVP EVETIFGLCL SMQVCRARLS EASTIASLAR KIQEDYVASL
PFQHYPLAEA QRGLKQAHGQ GLFNTAISME WVPPSVEDED ALLDLEEIRE QDDPTEYDIA
ISVDVHEGHI KLGFLYWPNL TDFDIAHLAE ALRGAMNRFA FQPDEALNTL SLLQASDVCS
ALAGGPTLLP LEAVRGNVVS MIDRWVTRQP EGAAIDGWDG SLSYKGLHEQ SSWVARNLLH
QGVQLGDRVL VCADRSSRTV ATVLGIVRAG CVLVLSNPTD PEKRLQWLAN KCNAALIVAD
PTYEERFATA GARVLSTTSV CAPAAWDYEF PSLDEHDLVS ILFTSGSTGT PKGILMEHGA
LATSVLLGHG RTLRFSRHTR MLHFASLTFD AALAEMFTTL AHGGCICVPY EEDRLSDVPG
CISRFAVNTA MLTPSVGRLL DPGALPTLKT LIMVGEPMSR LDVERFAPVL DLYNGAGPTE
TSIMVTIAGP MKPTDEPVNL GYAVAGVRLW VTEAENPNRL APLGAVGELI VEGRLVTRGY
LDDPARTQKA FLPSLPWLPS QHALYRTGDL VRYADDGSLR YMGRKDTQVK LRGQRIELQE
VEYHLRKSLQ QAQIVVEMVV PAGKMRAQAS LVAFVSGLTA ADVESSSACN LEGTIPISQI
VLPKSAFQAL EEVLPRHMIP SVYYALDTIP LSVNGKVDRR RLREMGTLLL ASSAAHKNII
EGMSKSVKWT PASELERTLL ELWAATPGLE ADTIHGDDSF LELGGDSVSA MKLVATARDK
YKLSLSVPQM FRYPTICQLA AEVGGPAGQS ASSASSTTEE GFTFSTPDDS STNDGVDDDF
LQLAAAQLAQ LAQDKGKKVD IAALLKQLQG GSSSNKTLSV SFSSSSSSSS KRKKKAALAE
AAAPIPVQFS LLDGGADVLD KVRAQAVEHC KIPHEDIEDI YPATALQEGM MALTARTPGV
YTTTLTCDLS EQVNLARLHY AWGKAAEAHP ILRTRIILTD NNMAVQVVQR AKGLPWDTYS
LREGDVLPDL TSNMTSGSPL LRLAVVHRQS QPRMFLVAIH HALYDGWSMP LLKQAVEDAY
HGRDLRPQLF TLFIKHLIAG KPAAQDFWTT HLDSFAGGVF PNLPSVDHQV QPKERRARSL
TLPTATPRSQ YSMATKIQAA WALTVSRYAE ANDIVFGTVS TGRSAPVPAI DRMVGPTITT
VPVRISLGDQ TERVISILQR VQENSWNIMD HEHLGLQHIR RLGESAAAAC SFQTLLVIQP
REQTDTKYRY TLLSGLQDVA EFEGVDTYPL MLVCEPDGAR LHLTAVFDPA VLDGATLDRM
LAHWELVLTQ LWNESDMAVI ELDTVSCTDK ETLMRWNTGQ TIPNACAHDA VYEWSVHTPH
APAVCAWDGE WTYEEVERCS SLIAGHILAH GVSCGDSVAL YHEKSRWGAA GILAVFKAGA
ILIALDPTHP TDRIKDILDQ ARPRLILTSQ FLLDEARNLE TSVLSVQFAA SQPLPEGCSP
LPKINSTQAA YIPFTSGSTG RPKGIPLDHR GLAASTASIA RSCLLSPASR VLHFASFAFD
ASMMEHLIAW HAGGCLCIPD ETARQTDLAK CIRDFNVTWA FLTPSCLRLI TPDDVPSLQA
LGLGGESMTS EDIIIWGPRL RQIIQLYGPA ECCFVAALNE VTKPSENRLI GRPNACRCWV
VDPRSPDRLA PIGAVGELII EGITVGRGYI NSPDRTTRAF IRPPNWLQTL YPDDHEPKRL
YRTGDLVRYA GVDGKLAFIG RRDSQLKLHG QRIELADVEA HLRPLIHGTQ KMVVEMVHSA
DNQNPILAAF LEEMSTSQNS AEREVGLLHP SQSQCALDVM AIHSALSRTV PHYMIPSMYL
HISRLPLSAS GKLNRRHLRE MVAELPRQRL NEYAAGSSLS VPDRPKTSQE QEMQAIWARV
LSLDPNTIGV NEDFFRIGGD SISGMQVATK CNAAGIHITS ADIFRYRTIE QLICHLNFIR
ITDCASVLLP AEPVDEWVAL APIQQLFFEV APEGPNHFNQ SLLLRTSRRV SVGELAGGLD
ILVGRHSMLR ARFCRKDSGQ WFQQVRSLDS EPASAFYRLA AHNQITRESL PTLFTAAQMA
LSIEDGPLLT VDLVELEDGN QLVYLAAHHL IIDFVSWRIL HGDLEEYFQT GSLSSATGSV
PFLTWTQLQA EYSAEHLPPL NDDFDVMRYW GISSESNTFG QTSISRFTLD RTVTDILFGS
ANNVIDTRPV EILQAALWYS CNQALTDHPG PSIYVESHGR EPWTNSINVS GTVGWFTTMS
PLVSTPWDHL SRKSMRDFVD VLSYIKDQRR RIPANGWAYF TSRYLNDEGR VAYGRTKPVV
EVLFNYMGQY QEMKRDDAML QLAGDDIQSG TGASDIADNV PRFSLIDVTA FTANGCLTFE
FTFPQLMQQD ARLEQCIKEC ERTLVAAASS LPAEGPRKTL TDFPLMSALT YDQLSQCLNY
TLPSMGLRAQ DVWNIYPCCP VQQGMLLAQL RDRQAYQQRF RFQVMSRGPT DQLPLEKVKD
AWTEVINRHE ILRTLLRPVS DHSHFDQVVM VPGSLQHLVR INAMNDNPTE GLPHTINITS
DSTGTTICEW NVSHALVDAM SIAVIQREVN QVFEGALGQH RDVPQYVDYI QWLSLQDNTE
AQAYWQNYLN GVEPCLFPKL TSSPDKVDSE GTISAIRATW SRDARMDELC LRHAITLTNL
FHIVWAIVLG AYVGTDEVCF GYTALGRDVP VNRVETMVGP LVNVLATTVR HQEDETILNA
LLVHQAHLTN SLQHQHYALA DVYASLGLVG SQLFNTIVSL QDTSHFDAPD EQRARLEMLP
ANDVSEYDVA LNIGVDKSSI QLVCSYQSVS LSAEQADALL RTAFHVLGEI LRDPTQRFCE
LEVISPKCKE QLVRWNAGML APTDEYIHEK IQGQCRIHNS RQAVCAWDGM FTYAEVDDLS
SRLAARLIRI GVTFEDIIPI YSPKSRWTVI AILGVLKAGA AFTLLETSHP MARLHVICDQ
IKAPMIIAPA SHAVPAANLI PILVVLDNIT SLTQEKSDLL PAVGIPPAGE ALAYLIFTSG
STGNPKGVMV THQNLCSNAS IITTSVNMTS DSRVLQFASH AFDGCILELL GALIAGSCLI
IPSESENKED LAGCIERMDV TWALLTPSVA RILEPETLPR LRNLVLGGEP IAASDLDMWR
GHVQVVCAYG PTETTIIAST TSPSTFPTDG KDIGLPNGSS IWVVSRQNYQ KLAPLGATGE
LLIEGPNVSL GYLGDPEKTK EAFPDSPRWL SQLRKSPPRV YRTGDLVRFD TTTGTIRFVG
RKDNQIKFHG QRIELGEIEH HAQLAFPSAS MVIVDLITPE QPQQPYIVAF VHQSDATNET
TDTTDSLLLP PSEAFRADAL AAQNKMHERL PHYMVPAVFL PLHRLPLSVT GKADRKHLRQ
CALALSSPEL NTYRATASTK HTPSTAEERK MQELVATVLG RDPTEIGMDD SFFYLGGDSV
QAMRLVAEGR QQGLALSLRA IFDSPRLRDL ADQARSPNAD NQRVSTASSA GPRDDCDQID
RIVATNSLNK ADVADVLPTT SFQRHWLEAQ LKSYIVVDIS GPVDPARLLR AMHRVVEAHP
ILRVSFVPYE TTTLQVILRT AVAITNADLS TTTVEEFCRR DVDAQMAPGV PYLRVILATQ
DKADHKLIMR LSHAQYDAVS LSLLMNDLSH AYANEIHPLP STHFPRFNDY ITYQQAQRAD
PTATTFWRHL LQDVSLTYLN LQPAESSASN GTPIILSRDI NIAAFPSLPS DITIATTIKA
AWSLVLAQKT DFLAVIFGQV VHGRAIALPG VEGIVGPCAN VTPVVARLGL QTTGMELMQT
LQDQHRSAMP YETVDLDDAL AYAKDSQAGR KGLQTIVQHQ NNVMVDDVEL SLGEVKCGVD
ARAVDHLPKE VWVYSSVDEN RPGMLEVKIM SSTLVMGEEV AKELMGLLVE KIVGLLRHPE
IVCV
//
