EASA_EMENI
ID EASA_EMENI Reviewed; 6919 AA.
AC C8VPS9; Q5BA85;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Nonribosomal peptide synthetase easA {ECO:0000303|PubMed:18559263};
DE EC=6.3.2.- {ECO:0000305|PubMed:18559263};
DE AltName: Full=Emericellamide biosynthesis protein A {ECO:0000303|PubMed:18559263};
GN Name=easA {ECO:0000303|PubMed:18559263}; ORFNames=AN2545;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=18559263; DOI=10.1016/j.chembiol.2008.05.010;
RA Chiang Y.M., Szewczyk E., Nayak T., Davidson A.D., Sanchez J.F., Lo H.C.,
RA Ho W.Y., Simityan H., Kuo E., Praseuth A., Watanabe K., Oakley B.R.,
RA Wang C.C.;
RT "Molecular genetic mining of the Aspergillus secondary metabolome:
RT discovery of the emericellamide biosynthetic pathway.";
RL Chem. Biol. 15:527-532(2008).
CC -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC that mediates the biosynthesis of emericellamides, secondary
CC metabolites acting as antibiotics (PubMed:18559263). The biosynthesis
CC of emericellamides initiates from the highly reducing polyketide
CC synthase easB which catalyzes the formation of the linear polyketide
CC chain (PubMed:18559263). EasB produces several polyketides that can be
CC further processed by the downstream enzymes (PubMed:18559263). The
CC polyketides are released from easB as linear polyketide carboxylic
CC acids, which are converted to CoA thioesters by the acyl-CoA ligase
CC easD (PubMed:18559263). The substrates are then loaded onto the
CC acyltransferase easC, which shuttles them to the first thiolation (T)
CC domain of the nonribosomal peptide synthetase easA (PubMed:18559263).
CC EasA then performs condensation of the polyketides with one glycine,
CC two alanine, one valine and one leucine residues (PubMed:18559263). A
CC last step of cyclization leads to the production of emericellamides
CC (PubMed:18559263). {ECO:0000269|PubMed:18559263}.
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:18559263}.
CC -!- DOMAIN: The NRPS easA is a multimodular enzymatic assembly that
CC contains 18 domains grouped into five modules corresponding to each of
CC the five amino acid monomers incorporated (PubMed:18559263). The second
CC to the fifth modules contain the three core domains, the condensation
CC (C) domain responsible for catalyzing peptide bond formation,
CC adenylation (A) domain responsible for selecting the amino acid monomer
CC substrate, and the thiolation (T) domain (PubMed:18559263). The first
CC module in the NRPS contains a unique T-E-C-A-T-E structure where (E)
CC domains are epimerization domains (PubMed:18559263). The NRPS does not
CC contain a TE domain at the end of module 5, presumably suggesting that
CC TE is not necessary for the cyclization of the emericellamides
CC (PubMed:18559263). {ECO:0000269|PubMed:18559263}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of emerecellamide A, C, D,
CC E and F (PubMed:18559263). {ECO:0000269|PubMed:18559263}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA64650.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000043; EAA64650.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001307; CBF87069.1; -; Genomic_DNA.
DR RefSeq; XP_660149.1; XM_655057.1.
DR SMR; C8VPS9; -.
DR STRING; 162425.CADANIAP00009275; -.
DR PRIDE; C8VPS9; -.
DR EnsemblFungi; CBF87069; CBF87069; ANIA_02545.
DR EnsemblFungi; EAA64650; EAA64650; AN2545.2.
DR GeneID; 2875600; -.
DR KEGG; ani:AN2545.2; -.
DR VEuPathDB; FungiDB:AN2545; -.
DR eggNOG; KOG1176; Eukaryota.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_60_0_1; -.
DR InParanoid; C8VPS9; -.
DR OMA; NEVRRWV; -.
DR OrthoDB; 4243at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:1900557; P:emericellamide biosynthetic process; IMP:AspGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
DR Gene3D; 1.10.1200.10; -; 6.
DR Gene3D; 3.30.300.30; -; 5.
DR Gene3D; 3.30.559.10; -; 8.
DR Gene3D; 3.40.50.12780; -; 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.
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; 5.
DR Pfam; PF00668; Condensation; 8.
DR Pfam; PF00550; PP-binding; 6.
DR SMART; SM00823; PKS_PP; 6.
DR SUPFAM; SSF47336; SSF47336; 6.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 5.
DR PROSITE; PS00455; AMP_BINDING; 5.
DR PROSITE; PS50075; CARRIER; 6.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE 3: Inferred from homology;
KW Isomerase; Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..6919
FT /note="Nonribosomal peptide synthetase easA"
FT /id="PRO_0000438969"
FT DOMAIN 17..93
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:18559263"
FT DOMAIN 1531..1608
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:18559263"
FT DOMAIN 3067..3143
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:18559263"
FT DOMAIN 4151..4228
FT /note="Carrier 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:18559263"
FT DOMAIN 5260..5337
FT /note="Carrier 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:18559263"
FT DOMAIN 6344..6421
FT /note="Carrier 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:18559263"
FT REGION 123..427
FT /note="Epimerization 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT REGION 294..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..981
FT /note="Condensation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT REGION 1003..1394
FT /note="Adenylation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT REGION 1617..2031
FT /note="Epimerization 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT REGION 2072..2509
FT /note="Condensation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT REGION 2541..2930
FT /note="Adenylation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT REGION 3188..3599
FT /note="Condensation 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT REGION 3620..4018
FT /note="Adenylation 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT REGION 4282..4708
FT /note="Condensation 4"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT REGION 4732..5133
FT /note="Adenylation 4"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT REGION 5380..5775
FT /note="Condensation 5"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT REGION 5824..6216
FT /note="Adenylation 5"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT COMPBIAS 300..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1569
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3104
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 4188
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 5296
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 6381
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 6919 AA; 764631 MW; 001A0679156709E6 CRC64;
MEQSTFATAG SPNRTVTNNE VVEKDIREIC AEVLRRPVGK IKLDKSFIAQ GGDSLLAIKL
MARCGEAGYT ITINDMLQAT SIRELCQSVK LAEGSSAPGK LSSGPVLDGP AQPAEIRTKP
LTEAQKLYAS TKAWDAKVFK LEGGIAESTL YAALKLLVSH HPILRANFTT LENNDLGLTY
NDTIDAFAHR RIEIPTISTQ AEQGYLTVGW EADGKREDGL FAATVFVQKD RDHGTCLARY
LRLDFHRAII DVSSWDILQR DLDHAVLGKP LARGYPETSF DSWASTHNLS DFTFRRSTPV
ESTNDERNTN ERQHNRHQND GKIELADVVI LETDAAGLAK LEDESIHSVL RTQPEDFIVA
ALHIALKGVT RSEETLSFGI ISNGRHSGGP KLSATVGCFD NIIRRSVERA EEDGGLGFLR
KVKDTRMGFF NVSRISGVED RSRYVLLHMG QLGRTTAPIA DTLHELFHQD DFSILPHGCL
AFVEPFLEQQ QLKLRLRSRS AELGREKLGQ LAGLFRAALK ELIAECEMSE VQGTLSDFPF
LKLTYSELDN LVSSRLKAVT GDPFRDVEAV FPCGPRQEAF LVAQAVYPDL YQCSFVIKLS
SEDLNVELDC GRLRDAWVRL VARHPALRTV FIESPNRQGH FDQVVMKQGI SSITFLENEG
EEAARRLACR RPVTFKSYGQ THQVTFCRIS PSSVYLRLDM SHAVVDGLSA LVLMRDLFQL
YSKQKLASRV MAYQDFVNYQ SRLPMQESMT YWSNYLAGAQ PSHFPLYGDQ LSREDLRTVR
SNIQLGSDVL GEFCAWALVL RSYTGLEDVC FSYATSGRDV PLKGINNTVG AFLNAVVCRI
KLPPTATVPQ ALVKARNDFV ESLSHQYYLA LDDAQSGDFA RFKSNTLMSC QRKAATELAG
SGLAFELVDA ANPNEYDMSI NIQVGHEGLE VMIDYWNSRI GQRTVESVAQ SFRQALLNIV
KEEDAVLGEI DISTTQEINQ LREWAKEIPP KADYRIHDKV YEQRLRRPDA WAVQGWDGDL
TYQQLDDTAN QLASYLIRLG VQPETKIPIC FEKSKWAVIS QLAILKAGGC VVPLGTTQPA
SRTRLILKDL QATIILTSGK FASRFMDLVT HTVVIDEAFM AELPPSEMVP CLATVDNAAF
IIYTSGSTGV PKGVVLPHAS LCTSLEHMGA RFKLSPDTRT VQFSAYTFDI SIQDIYTTWH
YGGCLIILSE EDRISNLAPE MVKYQVNCAG LTSTVAGTIF PQDVPTLKKL VLLGEAVKQA
VVDQWIGHVE VYNAYGPSEC SMQASINRLT PGCNALNIGW AFAGALWVVD PNDYNRLVPI
GAPGELLIEG PLQARGYLNS PEKTAAAFVV DAAWMIKNGF GSGRRLYRTG DLVQQNPDGS
ITYIGRRDTQ IKVRGQRVEV GEIEHHLLQQ DAVLDAAIIY PKQGPCKDRL VGLLTLRDFF
CGKRPGQDII PIPSGKLSHT KSQLAAASEE LSNHVPEHMV PKIWIPLESM MPQNDSSKLD
RKKLGVWLEA IDTAFLEALT KSSDAGSESR EPETLLERQV QQAWADVLRL PPTQIPIEHK
SFLSVGGDSI TAMHVVSWLR VRGITVAVRD VLESKSVAQL AQTAEVKDEK TEGHQSLLSP
MQKWYFESIA DPELPLKSSG AHRYNSNICL VPRKLFEYSE LAQAVGALVD RHPILRSRFQ
RHNVAGWQQS LHSDGDQPFA LRHYTVSTSE EAEALIVEAQ GSLDLEQGPV FFVEYIQVED
ARNTDLLFMT AHRLVVDEVS WDIIRRDISV LLEGQQFPTS NPLSFQTWIK LQAQRSQNLE
GIVFRSDLPP ADFKYWGLND GNTYEDETVE EVIFNSHDTN AYFRDANRAL RTERVEILLA
ALLKSFQKTF PNRRLPAVFE INDGRNVGDS GLDFSNTVGN FECMTPIHIF LDEPHNGLDI
VRQTKDARRS AFGRVLSDGQ QAFTDRWVEV LFQYSEGLAS ETIFETVDLT GPGTSPVGKS
TRRGCVFNVN VIAYPDKLRI RFKFNRNMKY QEKIRDWADS YANAISALGT ELSGASPTLT
VTDFPLLHLT SESLRVLQDE ILPDAGLNCS DVEDIYPCSP IQQGILISQV KSPSEYYIQQ
SFEIIPTTSS GKLDHTRLLA AWQVLINRHP MLRTRFVRSA SGSSERLFDQ VVLKSCKAEA
EHVECTDDDL FRNLAVKATL DERHIDKRIG HKLTIYSTSS NRTFGNIIIS HALVDASSLM
IIQAELAQAY DGKLAPDTIG AAYSEYISHL QKIPADQALD YWAKRLADAE PCYLRGMTED
GMQPATADDS TPRRPMQTVS IDINCIEKLH SFTETYGVTI ANVFQLVWAM VLAQYTGSPN
VSFGYLSSGR DVPVKDVETM VGPLINMMVT HIKLDMEASA QNTLKQIQEN FFESFNYQRA
PLVEIWHALQ LQGRSLFNTA LSYRHIVSAE KHQLSLALEQ ITGEDPTEYD VTVSVFASPE
KISASLQYSP DFLSYDSANR LLGCVRQGIQ SLVTNGDTHV GQLNTVTPKD ILQVRAWNDK
IPAVDGYCLI HDLFNEQRLL RPNATAVCAW DGDLTYQQLD EMSNALAHHL VTLGIGPEVM
VALCLDKSKF AIIAQLSVLK AAGVVVSINP KHPTQRLELV LKDINAKVML TSHQYSSQFR
NLVPHILHMD ETLFSALSSQ PQPPSTNVTP NNAAFIIYTS GSTGMPKGVI LTHLSLCSSF
RAHGKIYEMS PSTRSLQFAA YTFDASISDI WGTMSHGGCV CVISEEERMN NLQGVIEAYG
ATHAQVTPTV ASLLDIANIK CLTTLILGGE AVREAMIEEH AKAAGRVKVL NGYGPSECSI
YTTCSAALVQ KKQALNIGRP LVGSVWVIAN GESICPIGAV GELWVEGPLL ARGYHNDPKK
TKAAFVTNPK WAKAIRLEGH RFYNTGDLVR QSPNGDLIYQ ARKDSQVKVR GQRVEIGEIE
YRVKKLLPAV KSLVASLITP GGNSPNIMIS VAMELSDDFL QRHLLSAPFH EIFLPNAPHL
RDAFSQLHAS LLEVLPSYMV PRLFVPVVHL PQTTSSKLDR RTIKQMLENL PGDVLFQYSL
STSLSVAPST FMEKKLQSLW ATVLNVDQDH VGVQDHFLHC GGDSFTAMRL VSLANAKDIP
ISVADVFRYP KLQEMAAHLE AQMGRRRDVQ DIPRFGLWKE AQQTEASVSE RELLRVAKLC
DVAVHDIEDV YPCTPLQEGL MAITTQQPGS YIGRWVFRIQ EAVDTNAFKR AWSSLTQKAP
ILRTRIAPSQ SGGLQVVVRE SVAWGGDLNL KQYLDKDLQQ SFGYGQPLVR QALIYSGNKR
YFVLTAHHSV YDGYSLRKLF DAVALLYDGK ELAPTPAFSR FISYIGQQDL KAAKSFWQSQ
IKRKVGAPFP SLHKLSYRPQ PTQKLSSSVE IRPVGGPNTL ASSLRAAWAL AISAYGGNDV
LFGVALSGRS APVPGILDMA APTITTVPVH VHINPEQTIN QYLTMVHKQS VDMIPFEHTG
LQNIRRFVGQ IDLPHLFAVQ PAQERESSVH GKLLAYEHGH VPELNLDGYA LTVECVTSDI
SDIPVTIEAH FDERMISASQ TNDLLSRFSH IVTQLVTNGR DQTQLKYLDL LSKDEARRLF
QFNQGIPPVK QALVHELVSQ HVSTNPYAPA VCAWDGDLTR EELDRLANKL ALYLTTLGVI
PETMVALCFE KSKWALVANL AVLKAGGAVV PIRADPIQRV QNILQQTGIT TILASEGFAS
ALEGLVPNVI TIGDDLIQSL PSPVTQPIST VTPSNAAFVI FTSGSTGNPK GVVVEHGAMS
TSMQAHGKKF GMNSETRAFN FAHFTFDISL HDIISTLQFG GCVCMPSERE RVNNMADAMN
RMGVNYSFLP PRVIHTIKPS DVPGLKTLVV GGEAVQPEYL EPWLNGVRVF NAYGPAECSI
AATCNEVANK ADVPNIGRAI AGGLWVVDEN NYNRLLPLGA VGELLIEGPL LARGYLNDPI
KTANAFICNP AWISRYSEHD HCSQRRERRM YRTGDLVRQM EDGSLIYVGR RDGQVKIRGQ
RVEIGEIEHH VTEHPSVVEN VIVYPHCGPA QLQLVGILTL HGFISSDADE GIQTTPLDQL
PHALQQASSV RDHLHSCIPE YMVPNSWISL AAMPHNSSDK IDRRRLTQWL ETMEVEHFKI
LTQSYTEGTT TPSTSEEKNI QAVWADVLHA SIGKVPMSRP FLAVGGDSVT AMQVVSKCRS
QYSIYVTVRD VLQCESISQL AKKAVIKTTS PNTDTQLSTS SIDQAPAATS APTAFDINAS
DLSKLETDVL PRTGVENLSA IESIYYCSPI QQGILMSQIK DHTTYQVRQA GEIRAADSSP
VDMNRLLRAW QLVVQRHAIL RTFFVPSPSG RELFYQVVLK RYTPTIPVLQ SCSSDDFLAQ
FEGLERPEYA PGQPPYQLTL AQASTGQVYA QVDVNHVLMD ASSMDLILND LILAYDNMLP
DSPAPSYGIY VSFLQQTFAF DSLNYWTNHL AGAEPSCLPA SSNLDSGKRS LRTVSLEVDN
IKPLQDFRDT HGVTIANITQ LAWATVLSRY LGSRDVSFGY ISNGRDAPID GIHEMCGPMI
NLMVSRVQLA HPGTTVAEAA KQVQHNFLDA FNHQRTSLSD IQHALHLSER GLFNTTMIYK
PKPMMDTHEK RSLVIESLAG EDPTEYDVQV KIVSDDKSLS LDLEYATTFI DEPSARRLLG
SFGRALSSIA ANPDANIDEI DVIPTGDVEV LHIWNSTVGE TVPGSIHDKI HEQALSQPGA
QAVCGWDGEL TYAELTGMSD RLAHHLRNLG VREEVMVGLC FDKSMWTIVS MIAVLKSGGV
IVPLGVQMPV QRLQHILNEI TAPVVLTMDK HASKLRDITS ANVLTIDGGF IATLPNPCHP
PSESSLTSES AAVVIYTSGS TGTPKGVVLT HGTICTSIES HGPKLQMGPN TRALQYSAYV
FDLSLLDILS TLRFGGCVCV VSEEDRVDTN SLTTKMEAMA VNFAVLTPTV ASLIDPRTVP
TLSTLVLAGE VVPHSAVETW ASHVTLFNGY GPAESTILAT TNGPIIEKEQ ASSVGTALAG
AIWVVDTQDH NRLVPLGVVG ELLISGPLVA RGYLNDTERT SQSFITDPAF VSKYGFHSWA
GKRIYKTGDL VRQDPTDGSI MFVGRADGQI KIRGQRVEVG EIEYWLRQHF DTQTVAVDVI
GASTGDVALV AAIELRKDRS SNECVFLDVN HQLRESFLQL QAALLKALPS YMVPSKYIPI
KNMPNTASGK LDRRALRTLI GGLKEEQLAQ YSLADGGNVA LSTETERRLA RVWVAALNTS
KEFGANAHFF RVGGDSVTAM RLVALARTAQ PPILLSVSDV FKHPVLSDMA NTIANSESTE
NCQYDNDVPP FLLLPYPQHE RQARLQEIAS QCKVEVDVIE DAYPCTPLQQ GLMAITAQHP
QAYISRWVFR LEDTIDESRF CQAWRTLVEL NPILRTRIIQ DPKAGGMQVV LQQQITWNNV
LSELPSYIAE DSAKPMGFGD PLVRLAVVTS RQARFFVWTA HHSTYDGWTA RKLMEAAFAL
YSNNPAPSFH PFTRFVQYLQ SNSAEETRDY WKSQLEGGIG PSFPGSPKNG SPRKLRIQSC
RIPANNSNDF TLSTLLRATW ALILSQETGS QIVGFPTALS GRTAPVDGIL DVLGPTITTV
PIRVSVDPAQ SLSAYLASIQ QQATEMLPFE HAGLHNISRM TSLPLNFQHL FVVQPAVDRL
DQANSGFQGL TPVPFETYGF HNYPLVIECS TNMTDTDSAV DLQLQFDPAV LSVEKATTIL
ERFTHVFGQL QSAANEATCE VLVSDVIFMT PEDLGRIQKW NHFDERMTMA DGCIHDLVHH
QLLSCPDAQA VHAFDGHLTY RELHRLATRL AYHLEGLGVG PQVPVATIFE KTKWVVVTYL
AVLKAGGTIV PVNHQHPKQR MQALVQSIGT RVILTSQDPG RLQGLVTGPV LKVDQDFFTQ
LPDSDNPHPV VQATDSAFII FTSGSTGTSK AVVLQHGAIV SSMVQGHGSL YASPDTRAIQ
FSALNFDISI AEIFTTLSFG GCVCVISEDD RVSRLAEAME EAAVNFAILT PTVASLLKPE
QVPSLRRLLL VGEALRPEVA EPWSSSHVEL HNAYGPAESS ILTTFSQRIR DPVQAPNIGF
PLAHSNLFVV DPSNYHNLLP VGMVGELLIE GPLLAREYLG DAKKTAEAFV TDPAWLQQYD
LGPVSGRRFY RTGDLVQQKL DGSFIYIGRR DTQVKIHGQR VEIGEIEFWV KNKLPDVREV
VAGLFKPIYE EDEPLLAVAM EVPSSSVESS GLLSLSDELR EAFGELRRNL LTVVPSYMVP
QLYLPFAKLP LTDSGKLNRR ATWEMIHSCG SWSQYFLVDD IKAEPATVTE RLLQSLWATV
LKVPASSIGA KDDFFRSGGD SISAMRLVAS AREDAHISLK VADVFRHPIL SDMATLIDRK
TTVTKPAYCP FSTMTDDYAI RDSIKPLLSV PSEIIDVAPT TDLQSLSIAT SLRPSRDLMA
YVSIDGIGSP NFARWRASCL EVVKKHDILR TAYVVYKNQL LQVVLRDYAP AVTHYQTDQS
IEEFTKEFIA HDMHRPPQLG YPFLEFAIIC SPVANRHRVL FRLSHAEYDA ISLSYFVNSL
REIYQRQSTT EYVGFPQYIS SLANQDTWSS REYWRSLLKG CTMPAISSSS QPRRLPSRQV
YHDSRRVSFK TLPAGITLST IVRSAWALTL GQHVGNPDVL FGEVVSGRNG DPIAERAAGC
CANLVPVRAT IHPAWTTHDL LRSVQQQLVS RLPHESLGFR DLMRNCTDMP VGTVFTSLLN
HLDQASEWTL DLDDGKYNVS VAKTEGAGDV SDVSVTSTAS TDYVEIAMAY LEDGVTVEVA
EKLLSQLCET VDAFMNGALD AELPTVDCVS ELNAQGVNEA PKFEGDLVDA SLVAFELQKR
GHEVTVDEVV DRGLSLSGV
