ID   SAN1_FUSV7              Reviewed;        5911 AA.
AC   C7ZBE4;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Nonribosomal peptide synthetase 30 {ECO:0000303|PubMed:26936154};
DE            EC=6.3.2.- {ECO:0000269|PubMed:26936154};
DE   AltName: Full=Sansalvamide biosynthesis cluster protein NRPS30 {ECO:0000303|PubMed:26936154};
GN   Name=NRPS30 {ECO:0000303|PubMed:26936154}; Synonyms=NPS5;
GN   ORFNames=NECHADRAFT_106280;
OS   Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS   45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex; Fusarium vanettenii.
OX   NCBI_TaxID=660122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4;
RX   PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA   Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA   Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA   Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M.,
RA   Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA   Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA   Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA   Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA   VanEtten H.D.;
RT   "The genome of Nectria haematococca: contribution of supernumerary
RT   chromosomes to gene expansion.";
RL   PLoS Genet. 5:E1000618-E1000618(2009).
RN   [2]
RP   FUNCTION, DOMAIN, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=26936154; DOI=10.1007/s00294-016-0584-4;
RA   Romans-Fuertes P., Sondergaard T.E., Sandmann M.I., Wollenberg R.D.,
RA   Nielsen K.F., Hansen F.T., Giese H., Brodersen D.E., Soerensen J.L.;
RT   "Identification of the non-ribosomal peptide synthetase responsible for
RT   biosynthesis of the potential anti-cancer drug sansalvamide in Fusarium
RT   solani.";
RL   Curr. Genet. 62:799-807(2016).
CC   -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC       that mediates the biosynthesis of sansalvamide, a cyclic
CC       pentadepsipeptide that shows promising results as potential anti-cancer
CC       drug (PubMed:26936154). The nonribosmal peptide synthetase NRPS30
CC       produces sansalvamide by incorporating successively one phenylalanine,
CC       one leucine, one alpha-hydroxyisocaproic acid (HICA), one valine and
CC       one leucine before sansalvamide is released from by cyclization by the
CC       terminal C domain of NRPS30 (PubMed:26936154). The HICA residue is
CC       probably provided by reduction of alpha-ketoisocaproate by the cluster-
CC       specific aldo-keto reductase (NECHADRAFT_45914) (Probable).
CC       {ECO:0000269|PubMed:26936154, ECO:0000305|PubMed:26936154}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:26936154}.
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. NRPS30 has the following
CC       pentamodular architecture: A1-T1-C1-A2-T2-C2-A3-T3-C3-A4-T4-C4-A5-T5-
CC       C5. {ECO:0000305|PubMed:26936154}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of sansalvamide.
CC       {ECO:0000269|PubMed:26936154}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR   EMBL; GG698914; EEU38841.1; -; Genomic_DNA.
DR   RefSeq; XP_003044554.1; XM_003044508.1.
DR   SMR; C7ZBE4; -.
DR   STRING; 140110.NechaP106280; -.
DR   EnsemblFungi; NechaT106280; NechaP106280; NechaG106280.
DR   GeneID; 9670748; -.
DR   KEGG; nhe:NECHADRAFT_106280; -.
DR   eggNOG; KOG1176; Eukaryota.
DR   eggNOG; KOG1178; Eukaryota.
DR   HOGENOM; CLU_223054_0_0_1; -.
DR   InParanoid; C7ZBE4; -.
DR   OMA; NRQHWNQ; -.
DR   OrthoDB; 4243at2759; -.
DR   Proteomes; UP000005206; Unassembled WGS sequence.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; -; 5.
DR   Gene3D; 3.30.300.30; -; 5.
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; IPR025110; AMP-bd_C.
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; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 5.
DR   Pfam; PF00550; PP-binding; 5.
DR   SMART; SM00823; PKS_PP; 5.
DR   SUPFAM; SSF47336; SSF47336; 5.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 5.
DR   PROSITE; PS00455; AMP_BINDING; 4.
DR   PROSITE; PS50075; CARRIER; 5.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 5.
PE   3: Inferred from homology;
KW   Isomerase; Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   Repeat; Virulence.
FT   CHAIN           1..5911
FT                   /note="Nonribosomal peptide synthetase 30"
FT                   /id="PRO_0000450716"
FT   DOMAIN          891..968
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:26936154"
FT   DOMAIN          2001..2077
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:26936154"
FT   DOMAIN          3110..3186
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:26936154"
FT   DOMAIN          4248..4325
FT                   /note="Carrier 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:26936154"
FT   DOMAIN          5360..5436
FT                   /note="Carrier 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:26936154"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..754
FT                   /note="Adenylation 1"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:26936154"
FT   REGION          1007..1422
FT                   /note="Condensation 1"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:26936154"
FT   REGION          1467..1865
FT                   /note="Adenylation 2"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:26936154"
FT   REGION          2121..2538
FT                   /note="Condensation 2"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:26936154"
FT   REGION          2568..2977
FT                   /note="Adenylation 3"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:26936154"
FT   REGION          3227..3652
FT                   /note="Condensation 3"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:26936154"
FT   REGION          3701..4108
FT                   /note="Adenylation 4"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:26936154"
FT   REGION          4326..4347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          4353..4793
FT                   /note="Condensation 4"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:26936154"
FT   REGION          4819..5231
FT                   /note="Adenylation 5"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:26936154"
FT   REGION          5474..5828
FT                   /note="Condensation 5"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:26936154"
FT   COMPBIAS        4329..4344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         928
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         2038
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3147
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         4285
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         5397
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   5911 AA;  652233 MW;  8619CF4392122630 CRC64;
     MVPEKPTAQS KSGIGEPFRA GDAAGLHIPT SEINSTYLDD TFPSLFSTMH QFRENDAVKA
     YPSGGIEKFG DIRATVQPVS SGSSDTSSSD DSQQLQHAVE YWKDILADGK FVSYPSPPAS
     TQQRSSLSGL APHAVEQLQL PLPKHSKVPP ATLMRAAWAL VAGRMTDSES IVFGTNVLDE
     PILSAVPFRA HIHGHTVSSF IESVQKQEEE VMASPHQLTL LFSGMEQAST LFQTLLLIPS
     DEEYSNSPQD SGCRTPEPCG FGLVLEIAHT QDRASLKVTA RYRSDTLQAF EVKRLLHRFA
     SVMAQLDTVK PDQSVDEIDF MTEQDFQDIW AWNSKAPAAI NGFIHDIVKE KALIQPSSTA
     VYAWDGEFTY AEIDRHSNRL AVTLITGYGV QPGTPIALCF EKSKWMAVSM LGVLKAGAYF
     VMLDAASAPE QRLRTMVEQV QARLVISSPL NQALSSRICA AVVTLDSQTL RECKYNDDEI
     DRLLHQQLLT SSSNALAHVI FTSGSTGTPK AIPTTHQSIR SALHHQVAAI HLNTKSRVYD
     FSSYSFDAAI FNIWATFYAG GCLCVPSEAD RKDDLVGSFQ RLGANHVIMT PSAAQLLASA
     PEKVPQLETI MLVGERLTIQ DVLPWWNRVC LINSYGPCEC TPLGTSNLNP SSPTDLLDIG
     VGLGQVTWIV DPDDHNRLVP PGLIGELVLE GPSVSQGYLN DPERTAAAFV KDPAWLVERG
     RHGKVYKTGD LVQYSNEQGR LKYIGRKDAQ VKIRGQRVEL GEVEHRVQQC MPDVSQVVVE
     MITPKSGNNL SSAMLAAFLV PSRGSGKEVS EPRMAQSIPQ IYAVSEEVQS ALSKALPSYM
     VPSVFFSVRD LPKAASSGKL DRKKIREMGS SFSVKQLADL RTNAQGPKRQ PRPFSVEYSL
     QGIWASVLNM ERSDIGLNDS FFQLGGDSIS AMKVVRDARE QLEVELSVAD ILQHPRLSEA
     AAIVARGTKL FKSDEVPAAF SLLPGNNARE AIDPALKSHG VQSLSVEDAF PCTPLQEGLV
     FLSLKSPGDY IMQTTLDLST SSYSNAHKFR QAWEHVVAEH PALRTRFVHS DGETGLAQVV
     LRPEAFAWNE VANSSLNEYL ETDRRQPMSL GQAFARCALV HDKGAPRWFV WTMHHALYDG
     WSIRLIMNAF QRAYRSLEAG SNLVTGTTNA SYPAFIKYIL SQSVSADGSM AKYWKKTLSD
     CEAAQFPAVP LHVQNQAPDH DKINTLFQDL PSMTKKQGIS NATPSTLIRA AWALVVRSMT
     NSDDVVFGVT VSGRSAPVAA IDEVPGPTMA TVPFRSILAK NMLVGDYLRS VQQQAIDMIP
     FEQIGLPRIA KLSADCEHAC RFQTLLVVQP EETADILSEF DDEHGGPERW FNNTYALLLE
     VQLGDKKANS SGAVKARFDS RIIQANTVKS LLERLIFVID QLSGADNMAR VLSDIDVVTP
     VDLEQIWQWN KTVPATIDRN VHDMILERAL SQPDRPVVLA WDGELTYGEL TRLSSTLARR
     LIDQYGVRPG DIVGLCFEKS KWTSVAILAV LQAGAGFAML DPFLPETRLQ TIVDQVNALV
     VVSSPKQRDL SLQLGCDQVL HLASDLFSEP ETALVNVKTD PSSPVYIIFT SGSTGTPKGS
     IISHRSLASS LVHQREGCGF SQSSRVYDFS SYGFDAPLFL AFQTFSAGGC LCVPSDEDRK
     SRLAESLREL KATFALIPPS ASQLVSPEQV PDLKTLIVGG EASTVKDLER WSSADLMLIN
     AYGPCECTAV SMINPTHTSN MSVRKALAIG KGLGQVTWVV DPQDHSRLVS PGAVGELLLE
     GPYIGQGYLN NEEKTREAYV KDPAWLLQGT GKVPGRRGRL YKTGDLVQYS EDGDGSLMFV
     GRKADDAQVK IRGQRAELGE IELRVQQALK YDKTVQEVVV DVIVPHGEGS RPMLVAFLKT
     TDVKDTSATP DLYRVSSAFE DELAQSLPSY MIPEAFFKLA GIPQTATGKL HRMRLRAMGA
     SYSLRQLADL RTEATQGPKP QPTSELEAEM QQIWARVLSF EPERIGLDDS FFRLGGDSIA
     AMKAVGEATK ASIRVTVADF FEHRTLRNIC SHSYYCSEMA AESLSIAVES FSLLAPDSIE
     TREKLVQGLA AQLRTTTSRI QDAYPCTPLQ EGLVSLASKR TGDYIMQQVL ELSPDMLNNI
     DTFKDAWQKA VHAVPVLRTR IVQHEKLGLL QVLLNHQDEG IEWTEAMGLD WYLKSDRQKP
     MGLGQPLARY ALVRDRTGRP KWFVWTVHHA LYDGLSLPMI LEEVDRTMQG QSVEQARPQA
     QAFIKYIQQH DSNELKSYWQ ATLGDSGECV SYPSLPSGLE RPIMSNNLIE HQIPRAWVSS
     SSNETTVSTM LRAAWGLVTS QMTGSDDVVF GATVSGRNAP VVGVESMAFP TIATVPLRLK
     LNRKDQRVVD YLDQVQRQAT EMIPYEQAGL QRIAQLVSPG ARQACAFQTL LVVQPKSKTE
     STKTSQLGEW TTPDQTEWFT TYPLTIEATV SLSQIDVDAR FDSRVVEPWM VKGLLERLDF
     VMQQLGQAGP DINMSDIGIM TPGGLQQIWK WNEKVPDPVD RSIHSVIEEQ ARLRPEAAAI
     CAWDGNLTYA ELNSFSSRLA FYLIALTGGK SLKETFVPLC FDKSMWTPVA MLGVLKTGAG
     FVLLDSALPE QRLRHIVEKV GAGQLMLSSD SCSSLSGRIS QGVVTINSDF FKLAAQTIAR
     LPVASADSAA YVIFTSGSTG TPKGVVITHR NLASALPYHV KRLGYTPDSR VYEFASYSFG
     ASLNNMFTAL TTGSCLCIPS DHERRSQLDR SLVSMNATHV LLTPSVAESL APRSVSGLKS
     IIFGGEAVRS QDVGPWWEAG IKVCTAYGSS ECTTISTIND TASTPDEATR IGWGVGLVPW
     VVDPSDHEKL LPPGCIGELL LEGPAVGRGY LSDPEKTAEV FIQSPSWLTR GIPAANNDNH
     SQKGRSGRLY KTGDLVRYNE DGSLSFFGRK DSQVKIRGQR VELGEVEHRV KERVSEAAQV
     VVEAIIPTGS DSAHQTLAAF LVMKEETERP ASDDDKPTII PISAGVEDML SQNLPVYMVP
     TVFFSMKKLP MTATGKMNRR VLRQIGSSFS AKQFAAARKT REQGTPSQEQ PSTNAQRELQ
     QIWSRILDLP TDLIGLDDGF FSLGGDSVSA MKVVGEARKA GIELAVADIF THRTLRLIAD
     NSKSIKREGD QTVANIIPPF SLIGNEVDIE ALRQNISTQC DIDTSKVQDA YPCTPLQEGL
     ISLASKRPGD YVMQAVLELS SEVSITKFQA AWEETTKTID VLRTRIVHCQ GYEKLGLLQV
     ILDSSVNWIN ATGLESYLQA DRKQVMGLND PLARYALVYD GQTDRPRWFV WTVHHAIYDG
     WSLPLVLDTV AKAYQGETNA GSQSLTGASG FQPFIKYLEE QQRNPEGVKK TEDYWKRYFD
     SCEATQFPTL PSPSYEPTSN KTTLYRMKVN SPSSSTSLNL TPSTIIRAAW ALVVGQMTNT
     SDVVFGTTVS GRNAPVQTIE MMPAPTLATV PLRVKWTSGQ AILGYLETVQ REATEMIAFE
     QTGLHRIAKM SSDARQACQF QTLLVIQSQG HDEDESTGSL VQNELGSSPF GEWVNQDQNE
     WFNPYALMIE AQPGSQGDSF TLTANYDEKT IQEWIVLKLL KRLELVIQAF MAESYGQGQM
     VSKTIDELGG SIMTEDDLEQ IWTWNQSTPE AVDKYVHEMV EERVREQPNA PAVHAWDGRL
     TYKELDQLAE KMAAQLLSSI DTGARLSSPR VIPLCFTKSM WTSVAMYGVL KAGGAFVLLD
     PMVPEQRLKT IVEQVGADVV LSSESEADLA KRLCPHVIQV GLSLSTGPSP TTQRLKGSQR
     HLSPHAPMFA VFTSGSTGVP KGVLLSHRNF ASEIKHHSHL LGFHKNSRVF DFASHAFDAA
     VHNVFATFAN GACLCVPSEK DRKNNIGGVM ASMRVTVADL TPTVARLLDP TTLPDIETMI
     LAGEAVSAED AARWWRDSTR VVNGYGPSEC TVMSTINAYP TSPEDASSIG LGAGHTTWVV
     DPNNHNILVA PGCIGELLLE GPLVGQGYLN DPAKTAASFI EDPTWLLKGS STRPGRRGRL
     YKSGDLVKYR EDGRFWFMGR KDSQVKIRGQ RIELEEVERQ VQASWSGDDI SQIAAEVIKP
     QGQGSKPMLA AFIVSKDHQL SDDGPPEKAV KPVPVDPEIE ARLAERLPAA MVPSVFFFYM
     RSHLPQTATG KTHRKLLREI GSSFSFQHLA EVANQVQDDE NETKARRPPT TPLECQMQAI
     WVRILGISPD RISLDDSFIR LGGDSIAAMK VVGEARKHGS LDITVADLLR RPKLCDIIAT
     MTKNKATGAS RRLPRDDDEP IPHTKYAGPV DQSYAQGRLW FLDRLYPGLT WCLMPFTARF
     RGILRLDALH IALQAVENRH EALRTTFMSR DNVDLQEIHP FIPRELKLVE LPRGAKGEES
     LQRALFKERT TPLDLSTETG WRVTVYRLGP EEENHHVLSI LMHHIISDGW SLNVLRRELD
     IFYAAAVNSL DPLSQIDPLP IQYRDYASWQ KQRFHQDEYQ RQLDYWVSQL QTSRPAEFLC
     DKPRPDTLSG GAGVHEFTIA NTMYDRLQKF CAEAEVTPFV VLLAAFRATH FRLTGVDDAT
     IGTANANRDR WEVKELIGFF VNLQCLRIKM EQGVSFEDLV QQVQETAAAS FDNQHVPFEK
     IVSQLNTPRD LSRHPLVQVI FALHSRGTSG PVKLGDDLES EMLDPIPTSQ FDLEFHVFDD
     GDCLTANVVY SQDLFETETI NSMVSVFNNL LDRALSEPKT AISSLPLLTE DGRLKLETWG
     LTKIDRTNYP RDSSIVDLFK EQVSRHPNRV AVKGNSSSQL TYAELDRKSD TLARWLLKQQ
     PEFAPESMIG VMAHRSCEEI IALFGILKAN MAHLPLNHNT PTGRVETILS AIQGPKRLLL
     LGQDVAPPAV NLDNIEMVRI ADTLEEEAPR SWWKRAVVQA LPRPKPTSLA YVLFTSGSTG
     KPKGVMVEHR GVSRLCRDNN IIRHLPSSGG FGHFLNISFD GSSLEVYFAI LNGLTLVCVD
     EITILDAIAL QGVFERENVR AVLFTPALLK QILRVNPTTL GTLDLLCVGG DRLDPADCVK
     AYKHTAQGAK VLNLYGPTEN SVVSTVFCYE GQDEGFATGT APIGEPISNS GALVMDSQQR
     LVPLGVIGEI VVTGDGVARG YTDPSRDVDR FIRLDGGKGE RAYRTGDYAR WRPVDGKIEF
     MGRMDVQVKI RGHRVELGEI EHAIRGHEAV HDVVVLAYRD EKDGGEPRLV GFVTLHDTSK
     EDVEVKEVEH KDGEGETKQH VHQELEARLR ANLPTYMIPQ TITILERMPL NASGKVDRVA
     LSLTITPKTK ARAAGVALRK PTTDMEVALR KIWAQVLDLD PETIGLDDNF FDIGGHSILA
     MRAVSEARKV DIELTVADIF RSKCLEALAR RQEEIVGGPN TEEEEEVELI DSNTKAALLK
     DLDSLKATIH STQVEDMLPL TSMQEHYVTT GVASGEYAHY FYLDLGANPD VSRIEKACRL
     TLAKIPILRA SFMRLLGQHW QVIPRDVPAR LQTVNTIHVN GDLDRAADDF CLRNWDNISA
     AEPPALFTLL KHRTQGTRLV IRLSHAQYDG VCFPPIVRAI IEGYTTGDVT PLPSFTKFLS
     GAARQRPQSL EYWSRLLRGS SLTTILPRLR LSNSSRALTP PRPIAAELDV ALPQRLPSSI
     TPAIVASAAW SILLSQISGK QDVVFGHVVA GRNSSISRID EIVGPCLNLV PVRATLTESL
     TATELLQSLQ TQFFTMGSAD SVGFKDIMHE SSNWPSNSDF ESVLHHANVD EHPEFDFDGI
     KMKLHFFTNP RLIVSRLALA SYPTKGGECL QFRLTASTDK LSDVQAKMLL DALCKIIRGF
     GESANVPVLS WIGQVGLRLS FTLMDYSSFP L