ID   MLFA_ASPNA              Reviewed;        4870 AA.
AC   G3XUF0;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   23-FEB-2022, entry version 55.
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=ASPNIDRAFT_43807;
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL
RC   328 / USDA 3528.7;
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.I.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W.M., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N.M.E., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
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; ACJE01000005; EHA25778.1; -; Genomic_DNA.
DR   SMR; G3XUF0; -.
DR   EnsemblFungi; EHA25778; EHA25778; ASPNIDRAFT_43807.
DR   HOGENOM; CLU_000022_60_0_1; -.
DR   Proteomes; UP000009038; 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..4870
FT                   /note="Malformin synthetase mlfA"
FT                   /id="PRO_0000446435"
FT   DOMAIN          635..711
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1688..1765
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          2864..2940
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          4411..4487
FT                   /note="Carrier 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          106..497
FT                   /note="Adenylation 1"
FT                   /evidence="ECO:0000255"
FT   REGION          749..1133
FT                   /note="Condensation 1"
FT                   /evidence="ECO:0000255"
FT   REGION          1161..1550
FT                   /note="Adenylation 2"
FT                   /evidence="ECO:0000255"
FT   REGION          1764..1794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1829..1859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1898..2313
FT                   /note="Condensation 2"
FT                   /evidence="ECO:0000255"
FT   REGION          2336..2728
FT                   /note="Adenylation 3"
FT                   /evidence="ECO:0000255"
FT   REGION          2957..3422
FT                   /note="Condensation 3"
FT                   /evidence="ECO:0000255"
FT   REGION          3443..3862
FT                   /note="Condensation 4"
FT                   /evidence="ECO:0000255"
FT   REGION          3887..4277
FT                   /note="Adenylation 4"
FT                   /evidence="ECO:0000255"
FT   REGION          4524..4837
FT                   /note="Condensation 5"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1766..1789
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1829..1852
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         672
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1725
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         2901
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         4448
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   4870 AA;  535293 MW;  9BDDCA217490CA0C CRC64;
     MSRRSLINAA EQLLHPGPVG AGQVSGESAN TIITFEKDIE SLFVTQAEAA NVGTAMAQAL
     AEVGADDHNR LIKNLNLMSP THLESIWQFN ANVPGMWEEC FHDVIERRAA NRPHSLAVDA
     WDMKLTYADL VREARLLAAY LQHRGVRPGS VVPISFERSG AALVAMLAVS KAGGAFVSVP
     PTLPAGRLDA ILEVIEAPFV VTWSKYEPFW AERLPTLPID SYPKPSADAT VKTLGKPEDL
     FYVIFTSGST GRPKGCMLSH SNWLNGALRN APSWKYGPES RVLQMLSHTF DMSLLEICTS
     LGSGACVCVP RTEEIETSVS DAINRWQVNH VIMTPSLARS LRRDDVPGLK TMCLGGEAFP
     REIVTMWSER INLWQFYGPS ECSINSSSRP ITRPDADPLN IGPPNSAACW VVDTQDYNKL
     VPVGAIGELL VSGPIVGMGY LKNPIKTAEA FLDEVGFVAK DDPQFGGFRF YRTGDLVRWN
     SDGTITFCGR ADTQVKLNGQ RLELAEVEYQ LGLEAGVQYA IAMAPQSGRC KNNLIAVLTV
     KCGGASNQGN ADDEIPLLDR HDPIVQQTVK KLRSQLQHAL PRYMVPTIWA FVGRMPMSPS
     GKIDRVQLRN WVQEMSQETF DAITGRSFEA EDHVLGLSQL EQEIQLAWAE ALGLSAAEVG
     LQQPFVALGG DSIKALDAVA RCRARQIKIS MVHILSCEGV REASSLAEVQ ETPAHQVAEI
     AVDYSDLWTR LSTEYDISKL GVTQVEEVED VFPCTTMQEG MFLGQIRRPG AYHMRFFHRV
     QLKGGSLPTV ERIQQAWASL VERHPSLRTV FVDDLSSEAI YHSVVLRSVP MELTMREVPR
     DLNPESALAM FTEELVPFRP NAPLHRMLLL TCRGRVPYLM LEISHVIMDG YALSVFRREF
     IRACSSTASL PRGPDYRMFA NYHRTRQTDE SAKYWTNYLA DCVPCHIPTD PLSVPTDASP
     EWPRTLQRRD FGFDNSVAFL QRCKERQVTL ACAIRAAWAL VLRAYTQSRD VCFGYVSSGR
     NVPVPEVETI FGLCLSMQGL FNTAISMEWV PPTAEDEDAL LDLEEIREQD DPTEYDIAIS
     VDIHEGHIKL GFLYWPNLSD FQITHLAEAL QGAMNCFAFQ PDVALNTLTL LQASDLCSTL
     TNGPTLLPLE AVRGNVISMI DRWVTRQPES PAIDGWDGSL TYKQLHEQSS WVARNLLHQG
     VKLGDRILVC ADRSSRTVVT ILGVVRAGCV LVLSNPTDPE KRLQWLAHKC NATLVVVDPA
     YEERFATSGA RVFSTTSVCA PAAWDYEFSA LDDQDLVSIL FTSGSTGTPK GILMDHGALA
     TSVLLGHGRT LRFSRHTRML HFASLTFDAA LAEIFTTLAH GGCICVPCEE DRLSDVSGCI
     SRFAVNTAML TPSVGRLLDP EALPTLKALA MIGEPMSRLD VERFAPVLDL YNGAGPTETS
     IMVTIAGPMK PTDEPVNLGY AVAGVRLWVT EAENPNRLAP LGAVGELIVE GRLVTRGYLD
     DPARTRESFL PNLPWLPSQH ALYRTGDLVR YAEDGSLRYM GRKDTQVKLR GQRIELQEVE
     YHLRKSLQQA QVVVEMVIPE GKIRAQASLV AFVSGLTAAD VESSSARNFD QSMPMSQIAL
     PGSTIQALEE ALPRYMIPSV YFALDTIPLS VNGKADRRRL REIGAALLVS STAHKNTVDG
     KSEPVKWTAS SKLELTLLEL WTTTLGLEAE TIYGDDSFFE LGGDSVSAMK LVATARDRFK
     LSLSVPQMFR HPTIHQLAAI LGEATGQPES SASSTTEEGF TFSTPDDSST NDGVDDDFLR
     LATAQLAQLA QEKGKKVDIA ALLKQLQGGS SSCKTPSVSS SSSSSSSRKK KSAKVVSPVE
     APAPVPVPFS LLDGGADVVE KIRAQAVEQC KILPGDIEDI YPATALQEGM MALMARTPGV
     YTTTLTCELP ERVNLARLHS AWDKAAEAHP ILRTRIILTE NNTAVQVVQR AKELPWDAYS
     LQDGDPLPDL TSNMTLGSTL LRLAEIHRQN QPRMLLVAIH HALYDGWSMP LLKQAVEDVY
     HGQELWPQPF TPFINYLNEG KPAAQGYWTA HLDGFAGSVF PNLPSINHHI QPTERRTRSL
     AVPTAPPGSQ YTMATKIQAA WAVTVSRYAE AEDIVFGTVS TGRSAPVPSI DRMVGPTITT
     VPVRISLGNQ AERLTSLLQR VQEDGWNRMD HEHLGLQHIR RLGESAAAAC NLQTLLVIQP
     REEPRAKSIS TLLSGLQDVA ELKGVDTYPL MLVCEPDGVS LHLTAVFDPA VLDAVMLDRM
     LAHWELVLNQ IWSEPDMAVM GLDGVSYRDK QTLVRWNAGE KIADGCAHDA VYEWSVRTPH
     APAVFAWDGK WTYEELEKCS SLIASQVLVH GVSSGDFVAL YHEKSRWAAA AILAVFKAGG
     ILVTLDPAHP KDRIKDILDQ ARPRLVLTSQ SLLDEARELE TPVMVVQFAA SQPMPGECFP
     LPTVSPTQAA YAPFTSGSTG RPKGIPLEHR GLAASTASVA RACLLRPASR VLHFASFAFD
     ASMMEHLIAW HAGSCLCIPV ETVRQTDLAR CIRDFEVTWA FLTPSCLRLI SPDDVQSLEA
     LGLGGESMTP EDIFIWGPRL RQIVQLYGPA ECSIVAALTE VTKPSENRLI GRPNACRCWV
     VDPHSPDRLA PLGAVGELVI EGITVGRGYI DDPERTTQAF IPPPTWIQTL YPNEQQPSRL
     YRTGDLVRYA GTDGKLTFIG RRDGQLKLHG QRIELADVEA HLRPLIPGTQ KVVVEMVHSV
     GNHHPLLAAF VEEILTSQDQ VEQVVNLLHP SQTQCALNVK AIDSALSQTV PQYMIPSMYL
     HISRLPLSAS GKLNRRHLRR LVAEFPRQRL SEYAAGSGLA VPNRPATAQE REMQAIWARV
     LSVDPDTIGV NEDFFRIGGD SISGMQVATR CNAAGMHITS ADLFQHRTIE QLMRHLSANG
     KTGSASISLP PEPVDEWVPL APIQQLFFEI APQGPDHFNQ SLLLRTSRRV SAEKLAGGLD
     ILVGRHSMLR ARFCRDDSGQ WSQQVRSRGP YPASAFYRLT THNHIAPELL SSLLAASQMA
     LSIQEGPLLA VDLVNLTDDT QLVYLVAHHL IIDLVSWRIL HAELEEYLQT GSFASTTGSV
     PFLTWSRAQA EYSANHLTPT LPLPGFQEAN DGFDASRYWG ISCESNTFGQ TSTSTFTLDQ
     TVTDQLFGPA NNVLDTRPAE ILQAALWYSF TQSLTDRPGP SIYVEGHGRE PWTGSIDLSG
     TVGWFTTMSP LVSAPWDSLS QTSMRDFLDA LSYIKDQRRR IPANGWAYFT SRYLNDEGKV
     AYGRMKPVVE ILFNYMGQYQ EMNREDAILQ LAGDGIQSGT GAADVADNVP RFSLIDVSAF
     ISNGCLTFQF ILPKSLQQDS RLQGCFQEYE RTLVAAANSL STEGPRKTLA DFPLMPALTY
     DQLSQCLDHT LPSMGLCARD VVDIYPCSPV QQGMLLAQLR DRQAYQQRFR FQVKSRGSTD
     RLTLEKLKDA WTEVINRHDI LRTLLLPVSD YSHLDQVVMA PGSLQHLVRI NAMDTNPTQG
     LPHSINITSD STGTVICEWN VSHALVDAMS IAVIQQEVNE ALEGSLGQHQ KTPRYADYIQ
     WLSLQDNTET QAYWKKYLEG VEPCLFPKLA SSTDKVNPEG TISAIRATWT RDSRLDKLCH
     THGITLTNLF HIVWSLLLSA YLGTDKVCFG YTTLGRDVPV DGVEKMVGPL VNVIATTIQL
     QEDDSILDAL LTHQTHLSNS LQHQHYALAD VYASLGLVGS QLFNTIVSLQ DISHFDANDE
     RPTRVEMLPA NDVSEYDVAL NIGVDQSSIQ VVCSYRTLSL SVEQADALLR TTSHVLDEIL
     RDPKQPLRDL EVISPQCKEQ LVKWNAAMPA PTDEYIHEKI QDQCRLHSSR EAACAWDGIF
     TFAEVDDLSS RLAARLIRMG VTSGHIIPIY SPKSRWTVIA ILGVLKTGAA FTLLETSHPT
     ARLRVICNEI KADIIIAPAS HAVPAATLAP ILVVLDSITS MSPQESDLLP AVGMPPAAEA
     LAYLIFTSGS TGNPKGVMVT HQNLCSNASI MTTSVNMTSD SRVLHFASHA FDACLWEIFG
     ALFAGACLII PSESETKEDL AGCIERMVVT WAFLTPSVAR ILKPEALPSL RNLVLGGEPI
     AASDLDMWRG HVQVVCAYGP TETAILASTT SPSTFPSDGK DIGVPTGSSL WIVDKQNYNK
     LAPHGATGEL LIEGPNVSQG YLGDPEKTNE AFPVAPRWLS QLRKSPTRVY RTGDLVRFNT
     STGTIHFVGR KDNQIKFHGQ RIELGDIEHH AQQAFSNASM VIVDLITPEQ PQQPYIVAFV
     HQADTRTGTA DPIDTILLPP SESFRADAIG AQNHMHKRLP HYMVPTAFLP LHRLPLSGTG
     KADRKRLRQC ALSLSSLELN AYRATASAKR MPFTAAECKM QELVATVLGR DMSEIGMDDS
     FFYLGGDSIQ AMRLVSEGRQ QGLTLSLQAI FDAPRLGDLA YRTANLVRVS EPAPPTLPAT
     SSDDCDHKET IVAALPIKKT DVAEVLPTTS FQRTWLDSQL KSYIVVDIPG PIDLARLRTA
     IQRVVKAHPI LRASFVPYET TTMQVILRTA VVITEADLST TTVEGICRKD ANAPMAPGTP
     YLRVILATQG EVDRKLIMRL SHAQYDGISL SLLMNDLSHA YASESRPLPS SHLPAFNDYI
     TYQQTQGADP TATTFWHRLL KDVPITYLDL QPAETPTSNG SLITRTRDIN IAAFPSLPNG
     ITTATAVKAA WSLVLAQKTG SLAVIFGQVV HGRGIALTGV EGIVGPCANI TPVVARLGPQ
     TTRMELMQTL QDQHRSAMPY ETAGRKELQT IVQHQNNVMA DDMELSLGEA RWGKTGYVGG
     EDHVVDVGVE