ID   APF1_GIBF5              Reviewed;        5084 AA.
AC   S0DLP2;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   28-JUN-2023, entry version 42.
DE   RecName: Full=Apicidin F synthase {ECO:0000305};
DE            EC=6.3.2.- {ECO:0000305|PubMed:25058475};
DE   AltName: Full=Apicidin F synthesis protein 1 {ECO:0000303|PubMed:25058475};
DE   AltName: Full=Non-ribosomal peptide synthetase apf1 {ECO:0000303|PubMed:25058475};
DE            Short=NRPS apf1 {ECO:0000303|PubMed:25058475};
GN   Name=apf1 {ECO:0000303|PubMed:25058475}; ORFNames=FFUJ_00003;
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
RN   [2]
RP   FUNCTION, AND BIOTECHNOLOGY.
RX   PubMed=24195442; DOI=10.1021/np4006053;
RA   von Bargen K.W., Niehaus E.M., Bergander K., Brun R., Tudzynski B.,
RA   Humpf H.U.;
RT   "Structure elucidation and antimalarial activity of apicidin F: an
RT   apicidin-like compound produced by Fusarium fujikuroi.";
RL   J. Nat. Prod. 76:2136-2140(2013).
RN   [3]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25058475; DOI=10.1371/journal.pone.0103336;
RA   Niehaus E.M., Janevska S., von Bargen K.W., Sieber C.M., Harrer H.,
RA   Humpf H.U., Tudzynski B.;
RT   "Apicidin F: characterization and genetic manipulation of a new secondary
RT   metabolite gene cluster in the rice pathogen Fusarium fujikuroi.";
RL   PLoS ONE 9:E103336-E103336(2014).
CC   -!- FUNCTION: Non-ribosomal peptide synthetase; part of the gene cluster
CC       that mediates the biosynthesis of the cyclic tetrapeptide apicidin F
CC       (APF) (PubMed:25058475). The non-ribosomal peptide synthetase apf1
CC       incorporates four different amino acids to produce apicidin F: L-
CC       phenylalanine, D-pipecolic acid (D-pip), N-methoxy-L-tryptophan and L-
CC       2-aminooctanedioic acid (PubMed:25058475). L-Phenylalanine is the only
CC       proteinogenic amino acid directly used by apf1 (PubMed:24195442,
CC       PubMed:25058475). The 3 other apf1 substrates are non-proteinogenic and
CC       have to be modified by other enzymes of the cluster (PubMed:25058475).
CC       Lysine is converted to delta-1-pyrroline-5-carboxylate (P5C) which is
CC       reduced to L-pipecolic acid (L-pip) by apf3 (PubMed:25058475). L-pip is
CC       epimerized to D-pip, probably by apf1 activity, prior to incorporation
CC       (PubMed:25058475). L-Tryptophan is N-oxidyzed by one of the cytochrome
CC       P450 monooxygenases (apf7 or apf8), and further methylated at the
CC       hydroxy group by the O-methyltransferase apf6 to yield N-methoxy-L-
CC       tryptophan (PubMed:25058475). The synthesis of the fourth apf1
CC       substrate is more complex (PubMed:25058475). The fatty acid synthase
CC       apf5 is involved in the synthesis of the octanoic acid backbone of L-2-
CC       aminooctanedioic acid by fixing one acetyl-CoA unit and three malonyl-
CC       CoA units (PubMed:25058475). Then one of the cytochrome P450
CC       monooxygenases (apf7 or apf8) may oxidize this backbone to 2-
CC       oxooctanoic acid (PubMed:25058475). The aminotransferase apf4 is
CC       predicted to catalyze the exchange of the keto group with an amino
CC       group (PubMed:25058475). The next step would be the oxidation of 2-
CC       aminooctanoic acid by one of the cytochrome P450 monooxygenases (apf7
CC       or apf8). The last step is the oxidation of 2-amino-8-hydroxyoctanoic
CC       acid to 2-aminooctanedioic acid is catalyzed by the FAD-dependent
CC       monooxygenase apf9 (PubMed:25058475). {ECO:0000269|PubMed:24195442,
CC       ECO:0000269|PubMed:25058475}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:25058475}.
CC   -!- INDUCTION: Expression is positively regulated by the apicidin F
CC       cluster-specific transcription factor apf2 that binds to the eight-
CC       base-pair motif 5'-TGACGTGA-3' called the 'Api-box' that is found in
CC       all promoters of the apicidin F cluster except in the promoter region
CC       of apf2 itself (PubMed:25058475). {ECO:0000269|PubMed:25058475}.
CC   -!- DISRUPTION PHENOTYPE: Leads to the loss of apicidin F production
CC       (PubMed:25058475). {ECO:0000269|PubMed:25058475}.
CC   -!- BIOTECHNOLOGY: Apicidin F, like the other known apicidins, is a cyclic
CC       tetrapeptides with anti-malarial properties via histone deacetylase
CC       inhibitory activity (PubMed:24195442). {ECO:0000269|PubMed:24195442}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR   EMBL; HF679023; CCT63360.1; -; Genomic_DNA.
DR   SMR; S0DLP2; -.
DR   STRING; 1279085.S0DLP2; -.
DR   EnsemblFungi; CCT63360; CCT63360; FFUJ_00003.
DR   VEuPathDB; FungiDB:FFUJ_00003; -.
DR   HOGENOM; CLU_000022_60_0_1; -.
DR   OrthoDB; 2787863at2759; -.
DR   BioCyc; MetaCyc:MON-19327; -.
DR   Proteomes; UP000016800; Chromosome 1.
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   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   CDD; cd05918; A_NRPS_SidN3_like; 4.
DR   CDD; cd19542; CT_NRPS-like; 1.
DR   CDD; cd19534; E_NRPS; 1.
DR   CDD; cd19545; FUM14_C_NRPS-like; 2.
DR   Gene3D; 3.30.300.30; -; 4.
DR   Gene3D; 1.10.1200.10; ACP-like; 4.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 5.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 4.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 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_com.
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   PANTHER; PTHR45527:SF7; HYDROXAMATE-TYPE FERRICHROME SIDEROPHORE PEPTIDE SYNTHETASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 4.
DR   Pfam; PF00668; Condensation; 5.
DR   Pfam; PF00550; PP-binding; 3.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 4.
DR   SUPFAM; SSF47336; ACP-like; 4.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 10.
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   Isomerase; Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   CHAIN           1..5084
FT                   /note="Apicidin F synthase"
FT                   /id="PRO_0000437156"
FT   DOMAIN          731..808
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          2341..2415
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          3463..3539
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          4554..4631
FT                   /note="Carrier 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          209..606
FT                   /note="Adenylation 1"
FT                   /evidence="ECO:0000255"
FT   REGION          822..1124
FT                   /note="Condensation 1"
FT                   /evidence="ECO:0000255"
FT   REGION          1309..1609
FT                   /note="Condensation 2"
FT                   /evidence="ECO:0000255"
FT   REGION          1788..2192
FT                   /note="Adenylation 2"
FT                   /evidence="ECO:0000255"
FT   REGION          2415..2441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2478..2755
FT                   /note="Condensation 3"
FT                   /evidence="ECO:0000255"
FT   REGION          2935..3328
FT                   /note="Adenylation 3"
FT                   /evidence="ECO:0000255"
FT   REGION          3581..3866
FT                   /note="Condensation 4"
FT                   /evidence="ECO:0000255"
FT   REGION          4029..4426
FT                   /note="Adenylation 4"
FT                   /evidence="ECO:0000255"
FT   REGION          4669..4948
FT                   /note="Condensation 5"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        2416..2441
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         768
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         2376
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3500
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         4592
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   5084 AA;  562186 MW;  DBCE0E79CE257757 CRC64;
     MAIKMIDKQV LACNLDAFAG RVTNSTDINE QAIEWLSPTP SAVTLEAAWC VTLRLYTGLD
     HLSFGSLTQD GIVATKLCNL GPHDTLEDVC SHVQLYDYSD DTVCHYNTAV IFKLDENEGK
     KLSELIPRGI DVALMVTGSN LGVLARASFM DADEARNLCQ NFRHVLNCFQ EPNQAVRGIT
     LSDNDVNQIL SWNKSQLTRT ESLIHDQFAR ILQRQPDKSA IESWDGNMTY RELDAASSSL
     AESLSRANIG PGSWVLFCFN KSRWAIVSML AILKAGGACV PLDPRHPKSR VVQILQATGA
     QHILVGDADN DIKNRLCNEF PSVKVIGVPH HEVCESQDID TISLSFDSPA IGLFTSGSTG
     TPKGIVATHA TICTGASSYA HHIGADDKTR VLQFASYTFD VCMVDVFTAL LHGGTLCIPS
     EEERMTGLQE YISRTQPNWA ALTPTVARVL DPALSSKSIR KILLVGEMVR ESDIAEWLDS
     GVQVYNVYGP AENNLITTAA KAIRGRASNV GTGINTHTWV ADVENERLVP IGAVGELICS
     GPHLTPGYLN DPERTASSFF EDLSWIPNMM DNKPFSRRFY RSGDLVRYCA DGSLQCVGRL
     DSQVKLGGQR VELSEIESYI KSHNAAVLVP KAGSMKNKLI AVLEGAGSSG QSLGISSCDP
     GVAQQVEQVL RKNLPSYMCP SIWISVPHLP LSSSGKLDRK VLMNKLETLS HEEYLGLILD
     HAQDEDDQDG HETDNCQRLL REACSQVLNI PVERIAMSRA FAGHGGDSIT AMQVSSLIKR
     TQTLVVTVKD LLTCHSLAEA ASSMREVVTS IQVPTAHPGK LYPLSPIQRL FMATAPTSVT
     WNHYNQSVLL RIRERRSSDH VKESLGGVVR RHAMLRGRFQ RVSSSEWMQR ILPDDQGNLF
     FEYFPDASDY KQREALMLKA RESLDIESGP LLRAQLFDGQ VEQGMLLFIV SHHLVVDLVS
     WRVILEELEV SLAQPYGNTT DANDISALLL PQESVPFPVW SELQHEAAKN MDPDRVIPQQ
     YAVPAPDFSY WGISSARNVY RDVIEKSISL GDMTTKNVLY ECHEALQTEP VDIFLSAILL
     SFKRAFPERP IPPIFNEGHG REPWTSDLDI SRTVGWFTTM FPIYVPNISA GDVVDTVRRV
     KDFRKGCAEN GFQYFSTKYL HEQGRKTFKD HIPAEIMFNY EGRYQSLEKE KSLLMAEAWE
     AGEALSDSAP ELQRFCLFEL SAAVLTDGEI HFTMAWNSRA RYQERISLWL TRLLPAVIDE
     IVTYLMLEKR QYTLSDLSQA RLSDYSDLET LMASVSTIPG IDSIEGVEEI YCGSPMQDSL
     ALSQSRISGG VYEIDLTWEV TDGRQGNYQV DVNRLVLAWN DVVARHAALR TVFLEAASSS
     NDVMLHQVVL RKYRPSTILM HTRDSSQALK QLSSCASYKK RGILIDKRPP HALAICSTDE
     GRTFVRFQVN HILFDGTSIA PLLRDLSRAY RNSHEVRREW TWNPFANFIR YIRDEKRRSD
     DLAYWKSYLA TARPCQFPTL KHEESIEAPG TEQQRGAVQV CMSDKPSSLR NFLADMGVTV
     PTLVQLVWAL VLRMYTSDSQ VAFGYLASGR DAPVVDIEQA VGPFISILVH FLDFDNEGQL
     PIADMLQRIQ DRSARSISHQ SRSLAEIQDA IGLTGSSLLF NTGISFMPKW TKDMQLRNGS
     GLIFDQIAAN DPTEFDISLI VETGDDGVDG MCIYVDYRTS TVGRMHAINI AASFDHILSQ
     IIQDPSVPLN DVSGISTRDF DQISNWNRLL SPPKDKCLHD LFIEKVIEDP TREAVFSWDG
     SMSYGELHDL SARLANYLVH LGVGPEQMIP ICFEKSVWTV VTILAVLKAG GCFVLLDPTH
     PASRLWNIVG EIEASILLCS PLTNRSKKLD ASPDMNARKA AIIEIHPSFV NNLKSVSRES
     QHTPLCPSLS PDNAAYVVFT SGSTGIPKGV VVTHRAVVTG LDELGRAAGM TAMGSGTRTL
     QFASYSFDAS IADIFCALQL GGCVCVMSDE GRSPADITDF IQRSRATYAG ITPSFASLLD
     PRLVPSLRVL CFSGEALPAS QIEAWSGYVK MVNMYGPTEA SIACIANSEV TRTTDASNIG
     RAFRGSTWIV DENDHNQLRA IGSSGELLIE GPILAREYLK RPEQTAQAFI SNPPWLQNIR
     PNSRLYKTGD MVRYNTNGTI SYIGRKDNQI KINGQRVEVS EIEETLRASI EPEAGLITVE
     LLDRKALGEA DVLTAFVYIA GHDPSSTRDD KADNKKPFTI PDNPLLLEYF RSMLPRLESS
     SSKMPRYMVP QAYIPIDSLP LTTSGKVDRR ALRHAAAQLN RNQLFSFASS LDMVHEPSVD
     VVKDDPVSEL AHLWESVLNV RVSGTQSNFF RLGGNSMAAM NLRSQARKAG FQLSVADILA
     NPTLSDMAKG MAPLSLTAPE STSSSSPQSF STSTSTTIIE NDPDTSPFSL LRTRGIALNE
     GLWQQMFDNA DILWSEVEDI FPCTPMQEGL MVLSAHREGH GAYALHAPYK LPSDLDLAKL
     QFAWEQTTMV HAILRSRIVT HSQGALIVLQ KSPVVVQQST CSTLDDHLEE QRRLIFGYGV
     PLFRMTMVFD QIAQCHYFVM SIHHALFDGW SFSRMWDTAL AIYQGRQLSR DIPSFQSFVQ
     HLGAAPLSAS KEYWKSHLVE QDRDGFQFPA VPSTHKPIAT ASASFEFAFQ STIAMSAGVT
     PSTMVHAAWA ILLSQYTASS TVNFGVTLSG RDFPMPGLDQ VVGATIVTLP RQLNINLNQN
     VIEFLEYVQQ EAANVIPHQY LGIHEIRALG LEAQQACNFS TLILVNHNTV DLDSPLSVFG
     ITQVPVDSVD FHPYPLAVEF TVQPESLVVN VCYDPVCIGG SMVESVMQQY DHVLQSLSEG
     LMCSSGLSGT NLASIMTGIA PAHLQKMLDW NKDGHRYGAS RQTHLVLDHI GLNTRNNPRA
     RAVVADDSTL SYAELNRLAR VVSHRITQLD ISGEFIAVCF DKSAAAIVSM LAVLQTGFAF
     MPISASQPPA RLENLLTAAN VQVVLTSPAH TDLLSGLSSH RRIVPVDLKD IDQHEQMQLN
     RSGSAVDKSR AAYLLYTSGT TGQPKGVVVQ HGAWSKAIAS QIDFFGFTRD TKMLQFSNYT
     FDASIFEIFI TLCSGGCLFV PSEHSRVNDL EGFIRTNELN TITLTPTVAR VIRPGQLPCV
     RQCLFGGESL TQSDIFAWAQ QGRRVTNCYG PTEACVFSCG RDIRLDATDT KVTNIGRPVG
     INAWIISSMS GSISPIGAPG ELCLEGQMLA RGYLNDPERT QLSFSNHLPN NIPGKKNSRT
     YRTGDMVCHE ADGTLNFLGR RDGQIKLRGH RIDVGEIEHH IQHAMADDST YHSSTVQVYW
     KDTRNKSDAE LAALLRMDIQ HKECVMGVPC SLLSMPGRAD ESPTASQLKF KLRRILPEHM
     TPNTFIAVQH FPTTASGKLD RSFAQRCVEY FVPYTQKEVN KNETWSSSEA IVREWWCSIL
     GVNTDLICRH DNFFGLGGNS IYAIRLVGLA RSNGHHLQYE DVFSSPVLAD MASRLSRPED
     SRVQSETRQP PEPFQLISES DLKSVMDDIL PLYNINKDEV EDIYPCTPLQ ATLMAETARH
     RGVYILAESI QVPSSQMTLF QDAWLLMFKS YEILRTRIVL SHDQSHGEWQ VVMKYQPLTW
     TEFPDAKSFI EFVYNTHDYG KPLVHLAILG GNGGRIKDTD HSVKVGLCVH HAAYDGWSLS
     NIWRTITKKL TSSSSYSVGP YTPFNTYIRH LTEQDPEKAK SYWKERFSGL SSASLIPRPQ
     DPGHQSSATD TIQRNLDLPT LSDHLLGKTA IVAQAAWAIT ISHYTANSDT LCGTILSGRE
     YAAASVPGVE TIVGPTIATV PSRTTINYDS CVLDLITAVQ KDNLNAVRFS HMGLEQISRL
     NLDCRQACKF DNLFWVQPDL DETPANSIIR DIINVRGFSS SPMVLEIQLP AEGQKVVVNM
     SFDRVAVSNQ QAELIVDTYI TIMDNLLHAP LDTRLRSIAA LSPAHISQIS RVSSSPVEAV
     QACVHDLVRK QVELSPSHTA IDAWDGSMAY AALDALSTSL AEKLSGLGIG PESPVCILFE
     KSKWAIVAML GVVKTGGCFV PLNPQSPIKR LQHLVESVDA SIILVSPQYE ELSISLSLHH
     VKILVISQDT IPSPISALKP SRAFPSSVGP QNAAYILFTS GSTGLPKGVV IEHQALCSSL
     TVLSSRVGLN SNSRVFQFNA YWFDVMLLDV FGTLISGGTI CAPSESDCMD DLAGSINKFN
     ANTIAALSTS VSRLIEPSSI PCLNTLGLGG EPVLSSDRDR WAPHVRLFSM YGPTETCIVS
     LMTDMTSTTP ASLLGHPVGC RVWIVNPLKN DELAPLGGIG ELFIEGPGLA RYYLVDEDKT
     AAAFLSNQSW TIQDPSFQGS RRFYKTGDLV RINTDGTVSW IGRKDHSQVK IRGQRVELAE
     IEETIRQHIP SALTVAVDIL IDGERRILAA VFGTNLMLPG LSDTEVEVYM EKLIKGLLPK
     LNGSLPKHMV PTAFIPLPFL PFLSTGKLDR KALHRLALPL AVELTKRTST NRQALKTPKE
     RLLSALWSEV LSTSKGEPAG PADNFFNAGG DSMMAMKLVA MARHRGLTLS VVDIFKNPIL
     SDMADLLGPL RHEEEPSKED STHMLPIDTS SKLKDSLYEV LTVPPDRIEQ IYPCTAYQEM
     FLSGTEVWPG AHVTQFIFSI DKGTDMHRLE KAMGRCTAEF PTLRTRIVRH GESGQLLQVV
     LHKGHEAPWS IHLTDDLDSA LDQEKKDHWM HSGLSEPLHR LSLVMNNSGC THLIWSLNHA
     AYDAWSFGMM LRSLGQDRAN STRHSRTCLP FNGLIRHISK LRDASSESRR FWRSYIADIG
     SQVLLFRYPS IADPRQDRLA VHQVSFPKHG GRSSTSLITA AWIMLLARLS HRKDITIAYL
     VTGRTLPLGG IDTCPGPLIS KLPLRIQLLD EPRGLVDVAD LVRIETVRVM PHEHTGLDAI
     KDLASQDDDD IHPHAASLLG RFPLDLAIHP AGHTDVDAAR SIGITHIGQK VVVPPPGTFS
     AECSIISEDN YIAVSLAVIW DNRAMDEDDV NRVVEIWKDI IVRG
//