NPS2_GIBZE
ID NPS2_GIBZE Reviewed; 4841 AA.
AC I1RN14; A0A098DYP3; A0A1C3YK55;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 23-FEB-2022, entry version 64.
DE RecName: Full=Nonribosomal peptide synthetase 2 {ECO:0000303|PubMed:17043871};
DE Short=NPRS 2 {ECO:0000303|PubMed:17043871};
DE EC=6.3.2.- {ECO:0000305|PubMed:17043871};
DE AltName: Full=Ferricrocin synthetase {ECO:0000303|PubMed:17601875};
DE AltName: Full=Intracellular siderophore synthetase {ECO:0000303|PubMed:17601875};
GN Name=NPS2 {ECO:0000303|PubMed:17043871};
GN ORFNames=FG05372, FGRAMPH1_01T17751;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND PATHWAY.
RX PubMed=17056706; DOI=10.1105/tpc.106.045633;
RA Oide S., Moeder W., Krasnoff S., Gibson D., Haas H., Yoshioka K.,
RA Turgeon B.G.;
RT "NPS6, encoding a nonribosomal peptide synthetase involved in siderophore-
RT mediated iron metabolism, is a conserved virulence determinant of plant
RT pathogenic ascomycetes.";
RL Plant Cell 18:2836-2853(2006).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=17043871; DOI=10.1007/s00294-006-0103-0;
RA Tobiasen C., Aahman J., Ravnholt K.S., Bjerrum M.J., Grell M.N., Giese H.;
RT "Nonribosomal peptide synthetase (NPS) genes in Fusarium graminearum, F.
RT culmorum and F. pseudograminearium and identification of NPS2 as the
RT producer of ferricrocin.";
RL Curr. Genet. 51:43-58(2007).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=17601875; DOI=10.1128/ec.00111-07;
RA Oide S., Krasnoff S.B., Gibson D.M., Turgeon B.G.;
RT "Intracellular siderophores are essential for ascomycete sexual development
RT in heterothallic Cochliobolus heterostrophus and homothallic Gibberella
RT zeae.";
RL Eukaryot. Cell 6:1339-1353(2007).
RN [7]
RP FUNCTION.
RX PubMed=20507510; DOI=10.1111/j.1364-3703.2007.00401.x;
RA Greenshields D.L., Liu G., Feng J., Selvaraj G., Wei Y.;
RT "The siderophore biosynthetic gene SID1, but not the ferroxidase gene FET3,
RT is required for full Fusarium graminearum virulence.";
RL Mol. Plant Pathol. 8:411-421(2007).
CC -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC that mediates the biosynthesis of hydroxamate-containing siderophores
CC that play a critical role in virulence (PubMed:17043871,
CC PubMed:17601875). Gibberella zeae produces extracellular coprogen-type
CC siderophores as well as the intracellular siderophore ferricrocin
CC (PubMed:17056706). The role of extracellular siderophores is to supply
CC iron to the fungus during plant infection, and the intracellular
CC ferricrocin is required for intracellular iron distribution and storage
CC with a crucial role in ascus and ascospore development
CC (PubMed:17056706, PubMed:17043871, PubMed:17601875). SID1 catalyzes the
CC conversion of L-ornithine to N(5)-hydroxyornithine, the first step in
CC the biosynthesis of all hydroxamate-containing siderophores
CC (PubMed:20507510). The assembly of extracellular coprogen-type
CC siderophores is performed by the nonribosomal peptide synthetase (NRPS)
CC NPS6 whereas the intracellular siderophore ferricrocin is assembled by
CC NPS2 (PubMed:17056706, PubMed:17043871, PubMed:17601875).
CC {ECO:0000269|PubMed:17043871, ECO:0000269|PubMed:17056706,
CC ECO:0000269|PubMed:17601875, ECO:0000269|PubMed:20507510}.
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:17043871,
CC ECO:0000269|PubMed:17601875}.
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 (By similarity). Each module is responsible for the recognition
CC (via the A domain) and incorporation of a single amino acid into the
CC growing peptide product (By similarity). Thus, an NRP synthetase is
CC generally composed of one or more modules and can terminate in a
CC thioesterase domain (TE) that releases the newly synthesized peptide
CC from the enzyme (By similarity). Occasionally, methyltransferase
CC domains (responsible for amino acid methylation) are present within the
CC NRP synthetase (By similarity). NPS2 has the following architecture: A-
CC T-C-A-T-C-A-T-C-A-T-C-T-C-T-C (PubMed:17043871).
CC {ECO:0000250|UniProtKB:A0A144KPJ6, ECO:0000305|PubMed:17043871}.
CC -!- DISRUPTION PHENOTYPE: Leads to defective intracellular siderophore
CC (ferricrocin) biosynthesis and sexual development (PubMed:17601875).
CC {ECO:0000269|PubMed:17601875}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=SCB64745.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HG970334; SCB64745.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_011323896.1; XM_011325594.1.
DR SMR; I1RN14; -.
DR STRING; 5518.FGSG_05372P0; -.
DR GeneID; 23552557; -.
DR KEGG; fgr:FGSG_05372; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000092_2_0_1; -.
DR InParanoid; I1RN14; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 6.
DR Gene3D; 3.30.300.30; -; 3.
DR Gene3D; 3.30.559.10; -; 6.
DR Gene3D; 3.40.50.12780; -; 3.
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; 3.
DR Pfam; PF00668; Condensation; 6.
DR Pfam; PF00550; PP-binding; 6.
DR SMART; SM00823; PKS_PP; 5.
DR SUPFAM; SSF47336; SSF47336; 6.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 3.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 6.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 5.
PE 2: Evidence at transcript level;
KW Ligase; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..4841
FT /note="Nonribosomal peptide synthetase 2"
FT /id="PRO_0000444385"
FT DOMAIN 531..604
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1587..1665
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2139..2212
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3219..3293
FT /note="Carrier 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3759..3838
FT /note="Carrier 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 4318..4394
FT /note="Carrier 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 26..429
FT /note="Adenylation 1"
FT /evidence="ECO:0000250|UniProtKB:Q5D6D7, ECO:0000255"
FT REGION 640..1042
FT /note="Condensation 1"
FT /evidence="ECO:0000250|UniProtKB:Q5D6D7, ECO:0000255"
FT REGION 1072..1463
FT /note="Adenylation 2"
FT /evidence="ECO:0000250|UniProtKB:Q5D6D7, ECO:0000255"
FT REGION 1702..2043
FT /note="Condensation 2"
FT /evidence="ECO:0000250|UniProtKB:Q5D6D7, ECO:0000255"
FT REGION 2248..2663
FT /note="Condensation 3"
FT /evidence="ECO:0000250|UniProtKB:Q5D6D7, ECO:0000255"
FT REGION 2695..3090
FT /note="Adenylation 3"
FT /evidence="ECO:0000250|UniProtKB:Q5D6D7, ECO:0000255"
FT REGION 3333..3735
FT /note="Condensation 4"
FT /evidence="ECO:0000250|UniProtKB:Q5D6D7, ECO:0000255"
FT REGION 3873..4242
FT /note="Condensation 5"
FT /evidence="ECO:0000250|UniProtKB:Q5D6D7, ECO:0000255"
FT REGION 4430..4726
FT /note="Condensation 6"
FT /evidence="ECO:0000250|UniProtKB:Q5D6D7, ECO:0000255"
FT MOD_RES 565
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1625
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2173
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3253
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3799
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 4355
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 4841 AA; 536040 MW; 390CA4A642790FDB CRC64;
MDITGLSIMN AQASRQPGPH LLHQLVKPPN QNVALDYMGS NQRVNITYHQ LHEAATSLAS
RITKTSGSAQ GQFVVPLLIH QSPSLYISLL AILKAGGAFC PLNIDAPPER VKFILDDVAA
TVVLVSKELA SAIPNGISAA VIIVDEEEDQ SSTLQSLSTE VSSRVPGPED LAYVMYTSGS
TGTPKGVGIS HDAATQALIA HDRHIPSFSR FLQFAAPTFD VSVFEIFFPF FRGATLVSVR
RIEMLDDLPG VLRTMEVDAC ELTPTVAGSL LRTRSNAPEL KVLLTIGEML NAPVVEEFGG
DENRPSMLWA MYGPTEATIH CTLQAEFSSD SSTGNIGVPL DTVSCFIIEV PDSDSEQSEI
RVLPQGEVGE LAVGGCQLAT GYINRPEQTN SVFIDSPFGR IYRTGDKARL LPNGKLECFG
RLSDGQVKLR GQRLELGEVE QAVLRTSGCH SAVAAVARSI LVVFCAVDAG VTEDAVLKHC
GDWLPQYMVP GEVVLMSEFP RLPSGKVDRK RLKAEYEEHK EAMLEDIADS EPVDEFESSL
LVVVSRVMNF KVNKSTSLAA IGMDSLSAIK LASSLRNAGY SIDTTDLLTA KTVFDIIFAA
RRQIQNQTVS SLPFSTNLSL DFGQILQQNA TLADMSGLIE EIIPCTPLQA AMLAETSHNS
TAYCNQVELA IPLSYSAYQI SESFAQLSQK NPILRTGFAI VDRRFVTLVY GELRPEQIKV
VDQVQGDFSL SSPEDFCSPM RLQIQRDSVD EKSRVLLQIH HSLYDGWSMD VLLSDWSKLL
LQEPVSEHSS FREVVKFYQQ LQTSDDARMF WTENLAGWKQ TPLPKLRDKL VHSGEVLSFR
RPMSLSRRRV TAEVQRNGFS PQVLFQASLA LLWTSVTGAR DITIGSVTSG RTIPVIDIEQ
IIGPCIAALP VRIDFDKISI GLELLKNLHS SNRKIMQYCT VSLSEVKKLV GLQLGESLYD
VLFVYQESLA SSERTQCMVK EATHLDRLET PILFEVEPTE DGFTLQVTYH EAIVPPATVQ
HMVDQFEALA HSILERPTQE IKCALREIKC TPSVDNINAS PPQRVPDLAR LFEDVVRKHP
EENALLFYHS LKVANNVVWS FRELNNEANQ IAHYLQSCGI QVGQVVAVIM EKSPALYASI
LAIIKCGCGY LPILPSTPLA RTREILLQAE IKYCLVDSSP DQLASMLELS TITVNTNLFN
EFSTANLDNE VDGSRLAYVI YTSGTTGTPK GVAVQQQSIV ANIEHLEATY PKPSSSQGRL
LQACSQAFDV SVFEIFYTWC AGMCLCAGTN DTILEDIERS IRDLEITHLS MTPTVAALVE
PSNVPSVQFL VTAGEPMTQA VHNKWCHQLW QGYGPSETTN ICTVKKMATD DHIEHLGHVF
PNTSAVVLSP ATLDTVPLNW VGEFCFGGAQ VAQGYLNMPE LTAQKFIHHP QYGKLYRSGD
MGRMLPDGSL VILGRIDDQV KLRGQRIEIG EINSTVTMAG FATSAATVLV EHEESTIKQL
ALFFVPQHDP TEFRVLEIDN EVQQSLAAHM QSRLPGYMVP SYLVPISSMP MTSSGKVDKR
RLHDCFDKLD RHYLEKVSRS SGDNPDEGDW SRMDLVISEV IKESVAASAG GFGRWTPFTV
LGVDSISAID LARALNAKLG ARVAVSDILR NPTIAQLAKH LEGKPLYEET AFEGTQREFF
PAAFTAAIKE VFLGESKAIK DILPCTPLQE AMLSRGQRGY YNKVLLRLKA EPGAIRSYWE
VMSKRHDILR TCFATTTDSK HAIAQVVLED WEIPWRTFDI SEPSFDGAIE EHLKSLPDPV
DSRTPPVSLA LLRYRGSAFL SFICHHALYD GVAMERLLKE VEALAGGEDL LPPVSYKEFL
EISTNLPNDT EEFWQQHLRG YKALSIFTQS SSSEIDQSTC TTSLDMPLAN LQGRLRDFGT
TLLSVCQASW ATVLAMTYRQ PDVCFGNVMS GRTLDIDGLE RLVAPCFNTI PIRVALPTTS
SNIDMVKHLQ KLNTEMLTYQ FTPLRLIQRS INRTGKHIFD TLLLLQKPLQ DIDQTVWELE
ADSGDMDIPL VCEVVPCPGL NSLVINLHRD MSIVTEDVAS AMADAFKVIL KAILTAPHST
PMTAEDLPDS LRSILQQLKP QYDKKDNTGN MPDGEEEWSE VELDVRQVLA KLSGVSEQQI
KRRTTIFQLG LDSINAVQVA SILRQRGFIV SASDVIECPS CSKIAAKLLE NRSRTKSEDL
KRYDIGRFSH QVYSEIAGRL PQTATIEAVL PCTPLQSAML ASFIQSGGEN YLNAMEYIVT
DEISLESLTK AWQLLHERHP MLRTGFVPVQ HPDATFAMVR YAPGSMKTPV SIAESEGDEV
SDLLNLKGNT SERVLTALHQ PPWTVVLAQT PQQTSMKFVA HHVLYDAHAL QMMLYDLSRL
VKSERLPPVS RIEPAVSAIL INSLDEQGSE KAFWEAKASS TVVNKFPLMT PLRVESRCML
ADTTVASLSF TKLKRATQAS NVTIQAVIQA AWTRVLASYL GENSVVFGVA LSGRTTDETK
DAPFPCLNTV PVVGNNVTSN AELVSYMMEY NQRLHKHQFS PLGKVQRWLG HPTGPVFDTL
IAYQKMADAG SSSLPWKLVK DEARVEYSVS LEIEPTENDH VRLCITYYND ILPREQAHLL
MKQFDSSLNH IACNHLATED EAFNLSPDLY SVLPPSHPVL DAPVQFLHQF VELGAAVHPN
KLALEFVSAF DGDTCLKKQW DYRQLNIMGN RVANMLQEKL TPGSIVAIHF DKCPEAYFSI
LGILKAGCSF VALDPSAPKA RKQFIVEDSR APCLLTRSLE DLDFEAKTAI LEVKVESLSV
LEEEELIFQP AISPSDTCYC LYTSGTTGTP KGCEITHDNA VQAMMAFQEL FKGHWDADSR
WLQFAALHFD VSVLEQYWSW SVGMAVVAAP KDLILDDLTA SINKLEITHI DLTPSLARLT
HPDEIPSLCR GVFITGGEQL KQEILDVWGP KAVIYNAYGP TEATIGVTMF QRVPVNGRPS
NIGKQFPNVG SFIFKQNTNT PVLRGAVGEL CVSGRLVGKG YLNRPQLTEE RFPTLEEFGE
RVYRTGDLVR VLHDGCFDFL GRADDQVKLR GQRLEIAEIN HIIRTDVTEV HDAATIVARH
GTSGKDVLVS FIVSEHLTTG PLRVVSDDEG LATKAKEACR AKLPGYMVPT YILLLPYIPL
SSNNKAEIKD LKKLFSELAP EQLMELSHAA TAPVSRGAQD ILVLLYDALA QFSNISKDDI
SPTTSIFDVG VDSITALKLA SLLKSRGLHA VSPAMLLKNP VIGDLANCLA KAASSQRQKL
AREIKQSIQA YAHRHRGLVY SSLNIGPADI EYIAPCSPLQ EGIISRSLTS TKPGAYFNTF
QLKLHQSTTT TKFQQAWKDL VFSESILRTV FVPSTDGFLQ VALRNPLFPW ESTAFGSNEL
AEYYFAEQKE NWIQRNKSSI TQPLLLTYVE TPTSRLFTVH IFHALYDGNS FDLMMDRVAA
NYAGTSVQKA PSFFEALTSG PLTRHDNCKG FWEKHLEGWV PSSITAHERS THGSVVVAER
DMPISNFEAM RSSHNVTLQA VIMALWTSVL QNLVESQITI GVVVSGRAVD LPGVENTIGP
LFNTVPFFRQ AVQHEDWKSL VRRCHDFNAS VLDFQHVPLK NIQKWCSHNK ALFDTLFTYQ
IDEAKTDDNE LPFEIQNSEV TPDYPLALEA VYTKTGKLRF TLVAQGHVVS QSILDNLLNE
IERFADLAAE SPQSEVPVPQ FKIPIVDDFH SGNAEKDSQN SFEWTSEAQA IQNEISVLVG
INPAEIAQDV SILELGLDSI DVIKLAAKLK RKSINLAPSQ IMRQQTIAKM ITELASITND
SSCPPRDNFL SRIGYRLREH LEASEVDISN VESVLPPTHL QESMVAGMIH SGFEAYFNHD
VLRVSDHVDT TQLIQAWKDL IHQTPVLRTG FYQVESQDFD MTFCQVVSKS IDIDFEATRV
EDLSELHQIT DAAKSAAKNG RGQKKLFQLK LVVIGQERYM VLSIAHALYD GWSLSLLFQD
LQALLEGRLI TRPPVEQFIA RVMESTTSKA KDFWMQYLQD APSSTILTKV QLPTVEEKVQ
RFESVSKVSL LEIDAACKRL SVSLQVLCQA CWAVTLARQI RSTDVTFGTV LSGRDFDGAD
SLVFPTMNTV ALRCILHGSA AEFLRYLEEN MTDIRDFQHY PLRKAQSAAK VDGQDLFNTL
FILQRSPVSS DPADRPLLTS VEASSSTEYP LCVEAEAVSD SLVWRLALQP QCSWNGGPQS
LLETLDNVMS FLLKSKDPEI LSFSERGVSI CGTPPVALPE SIIHEDASDN YSSRDEKIEW
NQNEIGIREV LFQVSNVPIL SIKLSDNLYH LGLDSISAIK VSSLLRKAGI NLRPQDLIKS
SSISEMAQKA DTKLKKPLQT LETVEDWLPP ADIDVNKLLA DNGINKDEAE VLPALPMQVY
MLTAWENSDG SVFFPEFPCR IKTSASLGEI DQAWGKLVSE TPLLRTCFAS TQSSTIPFIQ
IILKELGIPL SSLQPGERSN CCIRPLVEVN IEQEDKDTWL LRLKLHHALY DGVSLPALLQ
RLSELLNGSG TMENKGLSQW KQFTMRHTTD EARIARREFW TSYLKGSSSS PIIANSDTDV
KMRTSHLNRS AISDISSIQA LATQSGVSFQ SLFLSAYARA LAKQNNVSDT VFGLYLANRA
AGENLPQTYP TLNLVPLRVS SPINRPLAAV AADIQRDIHL ITSESRAEVG LWEIAQWTGI
RITSFVNFLT LPGDTDPTGN SITVLPETNT GVVVKDNLPD RPRTPYLESI FRNDIPMAID
IEASVDGKNL AIGVFGSLQQ ISSEEALTLV ANIAEILDGG I
