PKSN_BACSU
ID PKSN_BACSU Reviewed; 5488 AA.
AC O31782;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Polyketide synthase PksN;
DE EC=2.3.1.-;
GN Name=pksN; OrderedLocusNames=BSU17210;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP SEQUENCE REVISION TO 1128-1129 AND 1703.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [3]
RP FUNCTION AS AN ACYL CARRIER PROTEIN, AND PHOSPHOPANTETHEINYLATION AT
RP SER-1018.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=16460000; DOI=10.1021/bi052333k;
RA Dorrestein P.C., Blackhall J., Straight P.D., Fischbach M.A.,
RA Garneau-Tsodikova S., Edwards D.J., McLaughlin S., Lin M., Gerwick W.H.,
RA Kolter R., Walsh C.T., Kelleher N.L.;
RT "Activity screening of carrier domains within nonribosomal peptide
RT synthetases using complex substrate mixtures and large molecule mass
RT spectrometry.";
RL Biochemistry 45:1537-1546(2006).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17190806; DOI=10.1073/pnas.0609073103;
RA Straight P.D., Fischbach M.A., Walsh C.T., Rudner D.Z., Kolter R.;
RT "A singular enzymatic megacomplex from Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:305-310(2007).
RN [5]
RP FUNCTION IN BACILLAENE BIOSYNTHESIS.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17234808; DOI=10.1073/pnas.0610503104;
RA Butcher R.A., Schroeder F.C., Fischbach M.A., Straight P.D., Kolter R.,
RA Walsh C.T., Clardy J.;
RT "The identification of bacillaene, the product of the PksX megacomplex in
RT Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1506-1509(2007).
CC -!- FUNCTION: Involved in some intermediate steps for the synthesis of the
CC antibiotic polyketide bacillaene which is involved in secondary
CC metabolism. {ECO:0000269|PubMed:16460000, ECO:0000269|PubMed:17234808}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC Note=Binds 3 phosphopantetheines covalently. {ECO:0000305};
CC -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17190806}.
CC -!- MISCELLANEOUS: The acyl carrier 1 domain binds alanine.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB13604.3; -; Genomic_DNA.
DR RefSeq; NP_389602.3; NC_000964.3.
DR RefSeq; WP_010886514.1; NZ_CP053102.1.
DR SMR; O31782; -.
DR STRING; 224308.BSU17210; -.
DR PaxDb; O31782; -.
DR PRIDE; O31782; -.
DR EnsemblBacteria; CAB13604; CAB13604; BSU_17210.
DR GeneID; 940054; -.
DR KEGG; bsu:BSU17210; -.
DR PATRIC; fig|224308.43.peg.1817; -.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR eggNOG; COG4221; Bacteria.
DR InParanoid; O31782; -.
DR OMA; TYAWKAI; -.
DR PhylomeDB; O31782; -.
DR BioCyc; BSUB:BSU17210-MON; -.
DR UniPathway; UPA01003; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0071770; P:DIM/DIP cell wall layer assembly; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1200.10; -; 3.
DR Gene3D; 3.10.129.110; -; 3.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.40.47.10; -; 3.
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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 3.
DR Pfam; PF00109; ketoacyl-synt; 3.
DR Pfam; PF02801; Ketoacyl-synt_C; 3.
DR Pfam; PF08659; KR; 3.
DR Pfam; PF00550; PP-binding; 3.
DR Pfam; PF14765; PS-DH; 3.
DR SMART; SM00826; PKS_DH; 3.
DR SMART; SM00825; PKS_KS; 3.
DR SMART; SM00823; PKS_PP; 3.
DR SUPFAM; SSF47336; SSF47336; 3.
DR SUPFAM; SSF51735; SSF51735; 4.
DR SUPFAM; SSF53901; SSF53901; 3.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 2.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Coiled coil; Cytoplasm; Ligase; Multifunctional enzyme;
KW NADP; Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; WD repeat.
FT CHAIN 1..5488
FT /note="Polyketide synthase PksN"
FT /id="PRO_0000379566"
FT REPEAT 165..205
FT /note="WD 1"
FT REPEAT 965..1006
FT /note="WD 2"
FT DOMAIN 983..1058
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REPEAT 2165..2204
FT /note="WD 3"
FT DOMAIN 2448..2525
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REPEAT 3666..3705
FT /note="WD 4"
FT DOMAIN 3952..4026
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REPEAT 5206..5244
FT /note="WD 5"
FT REGION 3..301
FT /note="Condensation"
FT REGION 493..903
FT /note="Adenylation"
FT REGION 1092..1518
FT /note="Beta-ketoacyl synthase 1"
FT REGION 2579..3015
FT /note="Beta-ketoacyl synthase 2"
FT REGION 4079..4514
FT /note="Beta-ketoacyl synthase 3"
FT COILED 3038..3109
FT /evidence="ECO:0000255"
FT COILED 3626..3655
FT /evidence="ECO:0000255"
FT COILED 5275..5303
FT /evidence="ECO:0000255"
FT ACT_SITE 1261
FT /note="For beta-ketoacyl synthase 1 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 2747
FT /note="For beta-ketoacyl synthase 2 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 4245
FT /note="For beta-ketoacyl synthase 3 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1018
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000269|PubMed:16460000"
FT MOD_RES 2485
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3986
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 5488 AA; 609593 MW; 1EA0D0F91C78FDDD CRC64;
MKRQLKSPLS EGQKGLWMLQ KMSPGMSAYN IPLCFRFSKP IHAETFKKAL LFVQRQYPVL
ASVIQEENGI PFQSVQLSKD LYFVEEDISA MKSADIMPFL KEKAKEPFQL EAGPLWRTHL
FHRLEECIVL ITIHHIIFDG VSMLTLISAL FEAYQQLLNG IEPLQQPSTA DYYDFVDWEN
RMLTGREGEE HLAYWKEQLS GSLPVLDLPA DRPRSSARKF KGQAYKSLLP HHLRNQIKSF
ARTNHVNESV VFLSIYKVLL HHYTKQKDII VGVPTMGRQE DRFETLIGYF INMMAVRSKN
IGSQPLTAFI RELQLTVAVG LDHAAFPFPA LVRELNVDRS AADSPVFQTA FLYQNFFQAT
GLQKVLEPYQ TLGIEYIEDI RQEGEFELAL EIYEQENETV LHLLYNPDLY ELSSIESMME
NYMKLAQHMM EDPSLPLEAY SLQLNQEQTS LLEQWNATGT NIANDKCIHE VFEEKAKQTP
DAVAVMFEDR SLTYKEVDEK STSVAVYLQH QGVRPEQPVG ICAERSFDMI IGILGILKAG
GAYVPLDPSF PQERLKYMLK DSQASIVLTQ PNVHDRISGL TGSHVKAINI ELACRNGYTD
QQSSGLKREV KPEHLAYIIY TSGSTGEPKG VMVEHRSIMN TLNFLESHYP VTAEDAYLLK
TNYVFDVSIS ELFGWFIGDG RLVILPPNGE KSPQLCMDYI ETYKVTHINF VPAMLHVFLE
MAKDNKRFTE DGPLKYMMVA GEAFPKVLVK KAVSLFTNCR VENIYGPTEA SIYAAYFGCG
KGDIASHHTP IGKPVSNTKI YIVDQHLKPV PIGKPGELCI AGAGLARGYF KKPGLTAEKF
IDNPFESGTK LYKSGDSARW LPDGNIEYLG RIDSQVKIRG FRVELGAIET KLGEFPGILD
QAVVVKQLEG HQQLAAYYTE ESGHASANPK DLRLHLKSSL PEYMIPSHFI RLDELPLSPS
GKVNRKELEK REIVFNRRKP NHLQLTEIED QVLRIWEETL KVSGFGPEDG FFDAGGDSLL
AVAVAERIKK EFDCEFHVTE LFEYSTIRAI SEYILEMKNS DLAGTQNEDD HDDKKDGKYP
KQKIPPYFDD SVAIVGISCQ FPGAKNHHDF WNHIKEGKES IRFFSEEELR ANGVPEELIQ
HPDYVPVQSV IEGKDLFDPG FFQISPKDAE YMDPQLRLLL LHSWKAIEDA GYVAKEIPAT
SVYMSASSNS YRTLLPKETT EGHESPDGYV SWVLAQSGTI PTMISHKLGL KGPSYFVHSN
CSSSLVGLYQ AYKSLTSGES QYALVGGATL HAQSAIGYVH QNGLNFSSDG HVKAFDASAD
GMAGGEGVAV ILLKKAVDAV KDGDHIYAIM RGIGINNDGA EKAGFYAPSV KGQTEVIQHV
LDTTKIHPET VSYIEAHGTG TKLGDPIEMS ALNKVYKQYT DKTQFCGIGS VKTNIGHLDT
AAGLAGCIKV AMSLYHNELA PTINCTEPNP DIKFESSPFY VVRERKSLEK HAGVHRAALS
SFGLGGTNAH AIFEQYENIS DAGAENEGNQ PYIIPISAKN SERLQVYAKE MLSYISQDEQ
RHFSLRDIAY TFQVGREAMD NRIVFIVNDL EEWKHQLEAF VTGKPLAEGC IQGEKTRMTS
AEQLLGNAEA DDMASSRISK EELRKLAEMW ANGFHVEWRR LYPNIKPRRI SLPTYPFAEE
RYWPESSTGA ITTIEPSRLH PLVHHNTSVL SEQRFSSIFT GQEYFIAEHI IKGMAILPAA
VTLEMARAAI EQGIGGLEDH ETGIRLKNVV WVRPVVAGSE PVQVNIGLYD EDGGHIAYRM
YGDPESADAE PVVYNQGKAE LIQLKREKAL DLSKIKKQCD QSKMDAASFY EGMIGADYGP
GYKSVEAVYK GDGQLLAKLS LPESVAHTLG DYVLHPSVMD GALQAAEYLQ NVVRAELSDT
EDFKAALPFA LEELEVFRQC VSDMWVYVQF NSKNKPGDLI QKVDIHLCDE HGMICVRLKG
FSTRVMEADI QTEPSKINAE TLLLQPVWQE QKAANSLAAK KYAEHLVFLC EYDHETRKQI
EAAIEDVHVY SLEARPSSVD GRFHSYTEQV FKKVQEIIRT KPKDGILVQI VTSAEGEQQL
FSGLTGLLKT ACQENAKLTG QMIEVSSEES GESIAGKLLE NQMSSDSYVK YQNGTRYIAD
WREIKQAKGD GSKPWKDNGV YLISGGAGGL GHIFAKEIAE QTKNATVILA GRSPLSESKS
KKLKELHSKG ADITYRQTDV TNKIEVYQLI DDIQKRYGRL NGILHSAGII KDSYLVNKQA
KDLHDVLAPK VKGLVYLDEA SKDLPLDFFI LFSSLSGSLG SIGQSDYAAA NVFMDMYAGY
RNRLADLSQR HGQTLSVNWP LWRDGGMQVD QETEKRLVQL AGIVPMRAEK GIQALYQALH
SEANQVMVIE GDVQKIKQNM LAKNASAPME KKEAEHMTEQ INSIDADSLL DKVKAMLKRE
IAKLLKVKLE TIDDHAEMTV YGFDSISMTE FTNHINRAYQ LELTPTVFFD HPTIHAFGKH
LSEEYQSVFA KTFAVRAVSA QLQPAAKQEQ AVRAKAKRRR KQQVMLPNAI QSDAGPEPIA
IVGISGIFPM AKDVEAYWNI LKEGKDCMTE IPKDRWDWRE YEGDPAKEVN KTNVKWGGFI
DGIADFDPLF FGISPREAEQ MEPQQRLLLT YAWKAIEDAG YSAKRLSGTK TGVFIGTGNT
GYSSLLSKAN SAIEGSAAAN TSPSVGPNRV SYFLNLHGPS EPVDTACSSS LVAIHHAISS
IEEGTCDMAL AGGVNTIILP EVYISFDKAG ALSKEGKCKT FSNQADGFAH GEGAGILFLK
KLKAAEEAGD HIYGVIKGSA INHGGRAASL TTPNPKAQAD VIQSAYQKAG IDPKTVTYIE
AHGTGTELGD PVEINGLKSA FKALGVNEGD TSANPYCGLG SVKTNIGHLS LAAGAAGVIK
ILLQLKHKTL VKSLHCENVN PYIQLKNSPF YIVRETEEWK ALKNEQGEEL PRRAGVSSFG
IGGVNAHVII EEYIPEASDE NIPSIAPEHP GIFVLSAKNE ARLKEHAQQL ADALDKQTYS
DVNLARIAYT LQAGRDAMEE RLGIISGSIE DLQKKLKDFA AEKSGVEDVF KGRIDKGTLQ
MLTEDEEIQE AVEKWMERGK YAKLLELWVK GLDVDWTKLY GENLPKRISL PTYPFAKDRY
WISDHIEKSG SIDANQAASR LGGAVLHPLM HQNTSNLSEQ RFSSIYTGEE FFLADHVVKG
QRILPGVAHL ELARAAVEQA AEVQGVPRIM KLKNAVWVRP IVVEDQPQQV HIRLLPGENG
EISYEIYGHS DVTGEQSIVY SQGSAVLNPA ENLPAVDLQS LREQCQESHF SVNEVYDTYR
MIGFEYGPAY RGVKKIYTAE QFVLAKLSLH PSAADTLSQY KMHPGLMDSA LQASSILTGA
GDNQLTLPFA VQELEVFGAC SSEMWVYARY SQGSKATDKV QKRDMDILDE SGNVCVRMKG
LSFRAAEGGS GSAESDQTLA TLMFEEKWVP KDFKKESPEP HYERHIVMLC DMNGLSKDRI
ESRMTGAECI VLESFREGLA ERFQDYAEQA LETVQGLLKS RPQGNVLIQL LTSAQRKQYS
FSGLSALLKT AGLENKKLIG QTIEIDSHEN VESVIEKLKE NKRHTEDQHI KYEKGKRYIN
DLDEMQIDDR EISMPWRDKG VYLITGGAGG LGFIFAKEIA RQAEQPVLIL TGRSALNADQ
QAELNELQQL GARAEYRQVD VTQTEAASEL ITSITSDYED LNGVIHSAGL IKDNYLMSKT
NEELTQVLAP KVKGLVNVDE ATEHLALDFF ILFSSISSVA GSAGQADYAM ANAFMDSYAA
YRNALVTAMY RHGQTLSINW PLWKEGGMRA NKEIENMTLK NTGVTPMRTE TGIQALYKGL
AFGKDQVIVM EGFKDMMREK LTQKPSSDDV PMKTVQVRVT SEARMDQGNM FDHIQEVLKQ
TISQLLKIKP EEIDPDMEFN QYGFDSITLT EFANTLNEKC KLDLTPTVFF EHATVYAFAG
YLSEEYPNAF TAQTPAKAEV LMQPVEQNIK NMTFSTENRF VKPSVTPMQK EADHKPEPIA
IVGMSGVFPK AKDVEEYWKN LSSGADCITE VPKDRWDWQE YYGDPLKEAN KTNVKWGGFI
DEVADFDPLF FGISPLEAEQ MEPQQRLLMT YAWKAVEEAG HSARSLAGTK TGIFIGTGNT
GYSSLLSNVD IEGSAAANMS PSAGPNRVSY FLNIHGPSEP IDTACSSSLV AIHHAVCAIE
NGNCEMAIAG GVNTVVTPQG HIAYDKAGAL SKEGRCKTFS DKADGFAVSE GAGILFLKKL
TAAERDGDHI YGVIKGSAVN HGGRANSLTT PNPKAQADVV KTAYEKAGID PRTVTYIEAH
GTGTELGDPV EINGLKAAFK ELYEKTGDPA VHGSHCGLGS AKTNIGHLSL AAGVAGVIKV
LLQLKHKTLV KSLYSETVNP YIRLDDSPFY IVQESREWQA LRDEAGRELP RRAGISSFGI
GGVNAHVVIE EYIPKETTHP ATAPAVTAQH PGIFILSAKD EDRLKDQARQ LADFISKRSI
TARDLTDIAY TLQEGRDAME ERLGIIAVST GDLLEKLNLF IEGGTNAKYM YRGRAEKGIA
QTLRSDDEVQ KTLNNSWEPH IYERLLDLWV KGMEIGWSKL YDGKQPKRIS LPTYPFAKER
YWITDTKEEA AAHQTALKTV ESAALHPLIH VNTSDLSEQR FSSAFTGAEF FFADHKVKGK
PVMPGVAYLE MVHAAVTRAV RRTEDQQSVI HIKNVVWVQP IVADGQPVQV DISLNPQQDG
EIAFNVYTEA AHNDRKIHCQ GSASIRGAGD IPVQDISALQ DQCSLSTLSH DQCYELFKAI
GIDYGPGFQG IDRLYIGRNQ ALAELSLPAG VTHTLNEFVL HPSMADSALQ ASIGLKLNSG
DEQLSLPFAL QELEIFSPCT NKMWVSVTSR PNEDKIQRLD IDLCDEQGRV CVRIKGITSR
LLEEGIQPPD GPTSLGNSKA TLNGALLMAP IWDRVQLEKR SISPADERVV ILGGDDNSRK
AVQREFPFAK ELYIEPNASI HRITGQLEAL GSFDHIVWMS PSRVTECEVG DEMIEAQDQG
VIQMYRLIKA MLSLGYGQKE ISWTIVTVNT QYVDQHDIVD PVDAGVHGLI GSMSKEYPNW
QTKLIDVKKY EDLPLSQLLS LPADQEGNTW AYRNKIWHKL RLIPVHNNQP VHTKYKHGGV
YVVIGGAGGI GEAWSEYMIR TYQAQIVWIG RRKKDAAIQS KLDRFARLGR APYYIQADAA
NREELERAYE TMKQTHREIN GIIHSAIVLQ DRSLMNMSEE CFRNVLAAKV DVSVRMAQVF
RHEPLDFVLF FSSVQSFARA SGQSNYAAGC SFKDAFAQRL SQVWPCTVAV MNWSYWGSIG
VVSSPDYQKR MAQAGIGSIE APEAMEALEL LLGGPLKQLV MMKMANETND EAEQTEETIE
VYPETHGSAI QKLRSYHPGD NTKIQQLL
