PSOA_ASPFU
ID PSOA_ASPFU Reviewed; 4007 AA.
AC Q4WAZ9;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=PKS-NRPS hybrid synthetase psoA {ECO:0000303|PubMed:17722120};
DE EC=2.3.1.- {ECO:0000305|PubMed:17722120, ECO:0000305|PubMed:24082142};
DE EC=6.3.2.- {ECO:0000305|PubMed:17722120, ECO:0000305|PubMed:24082142};
DE AltName: Full=Nonribosomal peptide synthetase 14 {ECO:0000303|PubMed:16962256};
DE Short=NRPS14 {ECO:0000303|PubMed:16962256};
DE AltName: Full=Pseurotin biosynthesis protein A {ECO:0000303|PubMed:17722120};
GN Name=NRPS14 {ECO:0000303|PubMed:16962256};
GN Synonyms=pesO {ECO:0000303|PubMed:17464044}; ORFNames=AFUA_8G00540;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP INDUCTION.
RX PubMed=16207816; DOI=10.1091/mbc.e05-07-0617;
RA Sheppard D.C., Doedt T., Chiang L.Y., Kim H.S., Chen D., Nierman W.C.,
RA Filler S.G.;
RT "The Aspergillus fumigatus StuA protein governs the up-regulation of a
RT discrete transcriptional program during the acquisition of developmental
RT competence.";
RL Mol. Biol. Cell 16:5866-5879(2005).
RN [3]
RP NOMENCLATURE.
RX PubMed=16962256; DOI=10.1016/j.gene.2006.07.008;
RA Cramer R.A. Jr., Stajich J.E., Yamanaka Y., Dietrich F.S., Steinbach W.J.,
RA Perfect J.R.;
RT "Phylogenomic analysis of non-ribosomal peptide synthetases in the genus
RT Aspergillus.";
RL Gene 383:24-32(2006).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17722120; DOI=10.1002/cbic.200700202;
RA Maiya S., Grundmann A., Li X., Li S.M., Turner G.;
RT "Identification of a hybrid PKS/NRPS required for pseurotin A biosynthesis
RT in the human pathogen Aspergillus fumigatus.";
RL ChemBioChem 8:1736-1743(2007).
RN [5]
RP REVIEW ON FUNCTION, AND DOMAIN.
RX PubMed=17464044; DOI=10.1099/mic.0.2006/006908-0;
RA Stack D., Neville C., Doyle S.;
RT "Nonribosomal peptide synthesis in Aspergillus fumigatus and other fungi.";
RL Microbiology 153:1297-1306(2007).
RN [6]
RP INDUCTION.
RX PubMed=21388144; DOI=10.1021/pr1012812;
RA Voedisch M., Scherlach K., Winkler R., Hertweck C., Braun H.P., Roth M.,
RA Haas H., Werner E.R., Brakhage A.A., Kniemeyer O.;
RT "Analysis of the Aspergillus fumigatus proteome reveals metabolic changes
RT and the activation of the pseurotin A biosynthesis gene cluster in response
RT to hypoxia.";
RL J. Proteome Res. 10:2508-2524(2011).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24082142; DOI=10.1073/pnas.1313258110;
RA Wiemann P., Guo C.J., Palmer J.M., Sekonyela R., Wang C.C., Keller N.P.;
RT "Prototype of an intertwined secondary-metabolite supercluster.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:17065-17070(2013).
RN [8]
RP FUNCTION.
RX PubMed=24939566; DOI=10.1002/anie.201404804;
RA Tsunematsu Y., Fukutomi M., Saruwatari T., Noguchi H., Hotta K., Tang Y.,
RA Watanabe K.;
RT "Elucidation of pseurotin biosynthetic pathway points to trans-acting C-
RT methyltransferase: generation of chemical diversity.";
RL Angew. Chem. Int. Ed. 53:8475-8479(2014).
CC -!- FUNCTION: PKS-NRPS hybrid synthetase; part of the gene cluster that
CC mediates the biosynthesis of pseurotin A, a competitive inhibitor of
CC chitin synthase and an inducer of nerve-cell proliferation
CC (PubMed:17722120, PubMed:17464044, PubMed:24082142, PubMed:24939566).
CC The PKS-NRPS hybrid synthetase psoA is responsible for the biosynthesis
CC of azaspirene, one of the first intermediates having the 1-oxa-7-
CC azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin, via condensation
CC of one acetyl-CoA, 4 malonyl-CoA, and a L-phenylalanine molecule
CC (PubMed:24082142, PubMed:24939566). The dual-functional
CC monooxygenase/methyltransferase psoF seems to be involved in the
CC addition of the C3 methyl group onto the pseurotin scaffold
CC (PubMed:24939566). Azaspirene is then converted to synerazol through 4
CC steps including oxidation of C17 by the cytochrome P450 monooxygenase
CC psoD, O-methylation of the hydroxy group of C8 by the methyltransferase
CC psoC, and the trans-to-cis isomerization of the C13 olefin by the
CC glutathione S-transferase psoE (PubMed:24939566). The fourth step of
CC synerazol production is performed by the dual-functional
CC monooxygenase/methyltransferase psoF which seems to catalyze the
CC epoxidation of the intermediate deepoxy-synerazol (PubMed:24939566).
CC Synerazol can be attacked by a water molecule nonenzymatically at two
CC different positions to yield two diol products, pseurotin A and
CC pseurotin D (PubMed:24939566). {ECO:0000269|PubMed:17464044,
CC ECO:0000269|PubMed:17722120, ECO:0000269|PubMed:24082142,
CC ECO:0000269|PubMed:24939566}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:24082142, ECO:0000269|PubMed:24939566}.
CC -!- INDUCTION: Expression is under the control of StuA, which is
CC responsible for transcriptional activation during acquisition of
CC developmental competence (PubMed:16207816). Expression is also induced
CC under hypoxic conditions (PubMed:21388144).
CC {ECO:0000269|PubMed:16207816, ECO:0000269|PubMed:21388144}.
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 (PubMed:17464044). Each module is responsible for the
CC recognition (via the A domain) and incorporation of a single amino acid
CC into the growing peptide product (PubMed:17464044). Thus, an NRP
CC synthetase is generally composed of one or more modules and can
CC terminate in a thioesterase domain (TE) that releases the newly
CC synthesized peptide from the enzyme. Occasionally, epimerase (E)
CC domains (responsible for l- to d- amino acid conversion) are present
CC within the NRP synthetase (PubMed:17464044). NRPS14 contains also a
CC ketoacyl synthase domain (KS), an acyl transferase domain (AT), a
CC dehydratase domain (DH), and 2 ketoreductase domains (KR)
CC (PubMed:17464044). NRPS14 has the following architecture: KS-AT-DH-KR-
CC T-C-A-T-KR (PubMed:17464044). {ECO:0000269|PubMed:17464044}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of pseurotin
CC (PubMed:17722120, PubMed:24082142). {ECO:0000269|PubMed:17722120,
CC ECO:0000269|PubMed:24082142}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000305}.
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DR EMBL; AAHF01000014; EAL85113.2; -; Genomic_DNA.
DR RefSeq; XP_747151.2; XM_742058.2.
DR SMR; Q4WAZ9; -.
DR STRING; 746128.CADAFUBP00008381; -.
DR PRIDE; Q4WAZ9; -.
DR EnsemblFungi; EAL85113; EAL85113; AFUA_8G00540.
DR GeneID; 3504510; -.
DR KEGG; afm:AFUA_8G00540; -.
DR VEuPathDB; FungiDB:Afu8g00540; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_37_0_1; -.
DR InParanoid; Q4WAZ9; -.
DR OMA; GYPPISE; -.
DR OrthoDB; 19161at2759; -.
DR Proteomes; UP000002530; Chromosome 8.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0019184; P:nonribosomal peptide biosynthetic process; ISM:AspGD.
DR GO; GO:1900790; P:pseurotin A biosynthetic process; IMP:AspGD.
DR GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:AspGD.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
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; IPR013120; Far_NAD-bd.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF51735; SSF51735; 3.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 2.
PE 2: Evidence at transcript level;
KW Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..4007
FT /note="PKS-NRPS hybrid synthetase psoA"
FT /id="PRO_0000416555"
FT DOMAIN 2418..2495
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3576..3652
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..389
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 575..897
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 969..1147
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 2131..2305
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255"
FT REGION 2513..2550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2589..2885
FT /note="Condensation (C) domain"
FT /evidence="ECO:0000255"
FT REGION 3076..3478
FT /note="Adenylation (A) domain"
FT /evidence="ECO:0000255"
FT REGION 3696..3920
FT /note="Reductase (R) domain"
FT /evidence="ECO:0000255"
FT ACT_SITE 182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2455
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3612
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 4007 AA; 435726 MW; D3E04435030E5CAD CRC64;
MVYTHSPKEP IAIIGTGCRF PGGSTSPSKL WDLLYSPRDL TREVPAESRF NPKGFYNVDG
EHHGASNATN AYFIEEDPRY FDAGFFSIAP REAESIDPQQ RLLLETVYEA MENAGLTLNG
MRGSATSAYM GAMSADYTDT QLRDIENVSK YMITGTSRAL LANRLSYFFD WKGPSISVDT
ACSSSLAAVH LGVQALRAGE CTISCVGGSN IILNPDCYLA ATSLHLLSPT GRSQMWDQAA
DGYARGEGVC VFFMKTLSQA LRDGDRIDAL LRETCVNSDG RTQGIALPSA EAQVSLMRTA
YKNAGLDLSK AEDRPQYIEA HGTGTQAGDP REAYAIATTF FPPGEDHSHR PKLVVGSVKT
IIGHTEGCAG IAGILKAVLA MRHKTIPPNQ HFHNLNPSVK PSFKHLSIAT SPQPWPVVPP
DTPLRASVNG FGSGGTNCHA IVESYVPEIH DNGPWGKPKE MTQVPNGVAA PETDFSPIPL
IFSASSGTAL RAMLERYQEY LERTEVSLLR LAMTLNSHRS TLPVRVSIPG TSKADVLAAI
RTQLAKVGSN PGAEIGTRSS VPEFDHVRRP KILGVFTGQG AQWAGMGQGL MAKSALFRQV
IEVMEEAMAQ LPDGPEWSLK EEIMKPPKTS RLGEAEISLP VCAALQVGLV KVLRSAGITF
SMVVGHSGGE IGSAYAAGKI SEVDAIKIAY YRGVYTKLAI GKDGKKGGMI AVGFGYEDGL
NFCAMEQFAD RLTVAASNSP KSVTLSGDLD AVHEAKELLD AEGVFNRVLR LDTAYHSPHM
YPCAAPYLAA IERCGLVAGK SNGTAWASSV YDDNRMMTSA QDKDLEAAYW KDNLIGRVLF
SQAVERALDE GNGDFDLALE IGPHPSLKGP TLETIRHKIG SEIPYSGVLD RKADDILALS
TALGFSWLTL GSGVVDFAGY VSGFDPSNAS ILNAPALPDL PTYPWDHKKV LYRESRLNKN
VRHRVDPPHP LLGSRTPDDT DYEPRWRNFL IMEELPWLRD HCVQGQIIVP AATYSVMALE
AAKVLCRGKH VQSIELSDVA ILRPIVLDEA SDGTETLFSV RSDLDSNKKH EDEIHAQFTL
SAGAMDDRHL RTAATGHIRI TLAAEAPSSF PNGPRPTELD LLPTSVDRFY ASMDEIGLSY
SGPFRAMTSM KRRLNVASAT VAVDRDLAGT IPVHPTWLDA CFQTFLAAFA APRDGSLWTA
FMPTAIGRMV FSPSSTSQVP GRSVTVDAHI TDFAPGYQVS LPTLTGDMSI FNSETNQLQI
QIEDFVMSSF LPASEKDDRR FYLQNVWGQE MLSGALCAAA ERCVAPTESE SKIIDTCEKA
VHYYLSKLKA AGLLDQWADK NPGLRSLMNE IEARVTSIPE QSDLVSMLGE VGEHIDLVLV
RTIGESLLNS PSEGLGPITP SPMGALISRW HHEGLGFAQL QRHFVSAAKQ ISHQHANLRI
LQVGPSSPGL VRSVCQELGR SLERYTLVDD SEQTIEEMKS ALAADQLRVD FTTASVENGI
DAVNHLTSAG GFDLVIVHKA FTKQVTALKT VRNLLRPGGF MLMMAATGAQ LRFPFMLMST
LPSLDDERLA QTKFINATRA ETHDLLRQIG FSGVDSIALD NVPDKHTFSV VVSQALDDHI
AFLRSPLTSP SPVPLSGNLL VVGGFSADIA KLATAIQSLV STVWHGDIIN VRTLAELDDE
ASTVEAVLSL TDLDRPVLED VRAPTFRGLQ RLFSEAKTVL WITHRAKADN PYHNATIGLG
RSFQSENPQK VLQFLDVDTL DGVESAIAET FLKLIGGVNM RNSNPADPTR LWTIEPEVSL
ENGKYLVPRL FPDTERNDRL NALRRKVQTQ VSVETQPISL SRSAQSDQVA YTAEAVHFHR
DLADGATDPV TIQVELCSTE PVIPNIDNED LFCFVGRTSE GARLVGLSTS NSSVVKVPRE
WTIPVDKHTS HDQGAFVLEL RNEIQSLVIA KSIPPGSTTL IYEPDPHLAA SLQRPGRPAT
SSVSFRARST WSIPGSHILI DPHASRKDIQ AKVPPKTRML IHMEQGPETC EFLALRQALP
PYATVVAFND LAADDVNPRE LLAEALSIIR GDSQSTKVPF DPSSVVKASA LVAGGTREHA
NAAVVDWTGA QSITLSPRPV DTRNLFSPNK TYLLVGLTGH IGQSICRWMV QGGARHIVVT
SRHPEKQGQL WREELLRQGV NIVIEAADVT KEHDLLDLRA RIVSSMPPVG GIANGAMVLD
DKLFIDMPFE SFQAAMKPKV QGSIYLEEVF SADNLDFFLF FSSISVMTGQ RTQANYVAAN
NFMVAMAERR RARGLPASVI DIGMVVGIGV IQRSQNDKGV SAMENSIRQM DYMPVSETDL
HHLLAEAILV GQRDESPELI TGLETYKPVE GEAPFWHHNV RFSHLITDPD AAQAGADSAG
SAQKSLKEML LSSGGPEEAR KVMENALLQY LASSLKLSRE TIYTDVPIID LGIDSLVAVQ
IRNWTWAEAG YDLPVLKILG GSSVTQICDE VVASLSFDKS SIAAAKVDSQ AAPAHKLRPW
DKPSADTKRT DSIAPVPRSQ IAANGPNGLP NGALKKASKL AVKVRPLWTT QAGGKDTKKG
PRPAPIRIQP LSLGQSRLYF LSQYMDDDRV LNCTISYALS GKLDVSKLEQ SLIQVVQRHE
ALRTSFYTDE KDGKPMQGLL EKSPFRLRVV PGVSASSDVE TEFNLIRYRP YDLEQADTFA
ATLLSHSPDS HTLICGYHHI IMDGVSWQIF QKDLAMFYNN SGIADSAKHL PAQYSEFTRK
QQEDLSCGAY AERLRFFQDQ FREPVESLPL FPFAKVGTRK VVKQYAVQEA TTHLNAKVVS
AIKQASQTSR TTPFHFYLSA FQVLLHRLLE TDKMCIGVVD ANRSDQNFVN TIGFFLETIP
LWFKVNSEQR FVELLKETRT KAYAALAQTG VPTEEILRAC GVASSTTETP LFQVCFNYRM
GAGRTAALQG VEMKFLDYVD AQNPFDLVAT VDDLDDGTAM ITLYLQDYLY DQEGAQLLAT
MYANVLQVLA ENPERLVGSV SISNATLEDE GVKLGTGPIL DLVAPSTPTL SKIFHTWVDK
DPHALAVKDT TGKSKTYVQL AERANAIAAS LLNAGAAPSI PIGVLLDPGV DTIATILAIL
RIGAAYVPLD TRSSDAVLSD ILQESQPGIV IHHSATAPRS QILLKASAKT KLVTLNAVPQ
KTIRKIQDVS VPEGLAMILY TSGSTGSPKG IPLTNANIRT PILGVSERVP LGREVVLQQS
GQGFDAAVYQ IFIALANGGT LIMVDNRDDP AKVAALMAQE SVTCTTHIVS EMQALLKYGY
DELRNCSSWR IAMVAGEAFT VHLLDQFRAL NRPDLKVINA YGPTEASICS SLGEVSFNRI
SSSETSIPIG KAIPNYGTYI VDQHCKPVPL GWPGEVAIAG PGVASGYLNL GELTQAKFRS
AATLGEVFGS DCLYLTGDRG RMLSDGSIVL SGRVDGDDQV KIRGHRVQLG DVARALVQAS
RGVFADAAVI LKGDDTSNPQ LVAYVVFSRT SNIQDQQTYL RQLNQDLPVP AYMRPAITIP
LDTLPVTDRG KLDSKKLASL PLPSISVDYE EDEQLTPTEA RLRDVWKNVL GDIASSIPIR
RSSDFFSVGG NSLILLALKA EIAQVFGVGL SVSELFQAST LELLAARLDG TSLLAQINWE
EETAPDETQF TLPPPINGIN GHGSSNGHAQ GISVLLTGAT GFLGGHILRQ LVQLPSVEHV
HCVAIRPNKV DVRRQLSVES PKIIRYSGDL ALPNMGMSES EFSDLFKSID VIVHNGAEVS
HMKNYRSLRA ANFLSTVGLA RAAVSRGIPI HYISTGGVAR LSVADEQPEA SLAAFHPPID
GSDGYVASKW ASEVFLEKVQ RRFQGQVWIH RPSSITGDDV PDNDIAHSLL KFSRELGAVP
ELTGSGFFDF INVETVSNNI AASVVRSSEK SGGGLIYLHQ SGEQVIPVGD LQKYVEELEG
RPLQVLPLKE WVDLSIRKGL DEVLGSYMLA SKGVIRAPLL QRGPHVE
