ID PKSJ_BACSU Reviewed; 5043 AA.
AC P40806; P40803;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 3.
DT 01-MAY-2013, entry version 106.
DE RecName: Full=Polyketide synthase PksJ;
DE Short=PKS;
GN Name=pksJ; Synonyms=pksK; OrderedLocusNames=BSU17180;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / PB1424;
RX PubMed=7704258;
RA Albertini A.M., Caramori T., Scoffone F., Scotti C., Galizzi A.;
RT "Sequence around the 159 degree region of the Bacillus subtilis
RT genome: the pksX locus spans 33.6 kb.";
RL Microbiology 141:299-309(1995).
RN [2]
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.,
RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA 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.,
RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA 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 [3]
RP SEQUENCE REVISION.
RX PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA Medigue C., Rose M., Viari A., Danchin A.;
RT "Detecting and analyzing DNA sequencing errors: toward a higher
RT quality of the Bacillus subtilis genome sequence.";
RL Genome Res. 9:1116-1127(1999).
RN [4]
RP SEQUENCE REVISION TO 87; 619 AND 4981.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
RA Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus
RT subtilis 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP FUNCTION AS AN ACYL CARRIER PROTEIN, AND PHOSPHOPANTETHEINE BINDING
RP SITE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC NCIMB 3610 / 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.,
RA Gerwick W.H., 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 [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC NCIMB 3610 / 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 [7]
RP FUNCTION IN BACILLAENE BIOSYNTHESIS.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC NCIMB 3610 / VKM B-501;
RX PubMed=17234808; DOI=10.1073/pnas.0610503104;
RA Butcher R.A., Schroeder F.C., Fischbach M.A., Straight P.D.,
RA Kolter R., Walsh C.T., Clardy J.;
RT "The identification of bacillaene, the product of the PksX megacomplex
RT in 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
CC the antibiotic polyketide bacillaene which is involved in
CC secondary metabolism.
CC -!- COFACTOR: Binds 5 phosphopantetheines covalently (Potential).
CC -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: The acyl carrier 2 domain binds glycine.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC family.
CC -!- SIMILARITY: Contains 5 acyl carrier domains.
CC -!- CAUTION: Was originally thought to be two separate ORFs named pksJ
CC and pksK.
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DR EMBL; U11039; AAA85143.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U11039; AAA85144.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL009126; CAB13589.3; -; Genomic_DNA.
DR PIR; A69679; A69679.
DR PIR; H69678; H69678.
DR RefSeq; NP_389598.3; NC_000964.3.
DR ProteinModelPortal; P40806; -.
DR SMR; P40806; 29-560, 586-1132, 1135-1645, 1650-1728, 1760-2658, 2736-3096, 3210-3287, 3339-3895, 4052-4419, 4461-4536, 4587-5035.
DR IntAct; P40806; 6.
DR STRING; 224308.BSU17180; -.
DR PaxDb; P40806; -.
DR EnsemblBacteria; CAB13589; CAB13589; BSU17180.
DR GeneID; 940043; -.
DR KEGG; bsu:BSU17180; -.
DR PATRIC; 18975245; VBIBacSub10457_1814.
DR GenoList; BSU17180; -.
DR eggNOG; COG0318; -.
DR HOGENOM; HOG000008928; -.
DR KO; K13611; -.
DR ProtClustDB; CLSK928133; -.
DR BioCyc; BSUB:BSU17180-MONOMER; -.
DR UniPathway; UPA01003; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 6.
DR Gene3D; 3.40.47.10; -; 6.
DR Gene3D; 3.40.50.720; -; 2.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR009081; Acyl_carrier_prot-like.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR020842; PKS/FAS_KR.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR006162; PPantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR016038; Thiolase-like_subgr.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00109; ketoacyl-synt; 3.
DR Pfam; PF02801; Ketoacyl-synt_C; 3.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF00550; PP-binding; 5.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 2.
DR SMART; SM00825; PKS_KS; 3.
DR SMART; SM00823; PKS_PP; 5.
DR SUPFAM; SSF47336; ACP_like; 5.
DR SUPFAM; SSF53901; Thiolase-like; 3.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS50075; ACP_DOMAIN; 5.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE 1: Evidence at protein level;
KW Acyltransferase; Antibiotic biosynthesis; Coiled coil;
KW Complete proteome; Cytoplasm; Ligase; Multifunctional enzyme; NADP;
KW Phosphopantetheine; Reference proteome; Repeat; Transferase.
FT CHAIN 1 5043 Polyketide synthase PksJ.
FT /FTId=PRO_0000193184.
FT DOMAIN 591 664 Acyl carrier 1.
FT DOMAIN 1659 1726 Acyl carrier 2.
FT DOMAIN 3112 3185 Acyl carrier 3.
FT DOMAIN 3214 3283 Acyl carrier 4.
FT DOMAIN 4464 4533 Acyl carrier 5.
FT REGION 141 481 Adenylation 1.
FT REGION 690 989 Condensation (By similarity).
FT REGION 1181 1578 Adenylation 2 (By similarity).
FT REGION 1763 2189 Beta-ketoacyl synthase 1 (By similarity).
FT REGION 3342 3782 Beta-ketoacyl synthase 2 (By similarity).
FT REGION 4591 4995 Beta-ketoacyl synthase 3 (By similarity).
FT COILED 3839 3872 Potential.
FT ACT_SITE 1932 1932 For beta-ketoacyl synthase 1 activity (By
FT similarity).
FT ACT_SITE 3511 3511 For beta-ketoacyl synthase 2 activity (By
FT similarity).
FT ACT_SITE 4743 4743 For beta-ketoacyl synthase 3 activity (By
FT similarity).
FT MOD_RES 627 627 O-(pantetheine 4'-phosphoryl)serine
FT (Potential).
FT MOD_RES 1689 1689 O-(pantetheine 4'-phosphoryl)serine
FT (Potential).
FT MOD_RES 3148 3148 O-(pantetheine 4'-phosphoryl)serine
FT (Potential).
FT MOD_RES 3246 3246 O-(pantetheine 4'-phosphoryl)serine
FT (Potential).
FT MOD_RES 4496 4496 O-(pantetheine 4'-phosphoryl)serine
FT (Potential).
FT CONFLICT 87 87 V -> W (in Ref. 1; AAA85143).
FT CONFLICT 619 619 N -> NAN (in Ref. 1; AAA85144).
FT CONFLICT 4981 4981 D -> G (in Ref. 1; AAA85144).
SQ SEQUENCE 5043 AA; 562814 MW; F6E8A8533D518DE4 CRC64;
MRNNDNIRIL TNPSVSHGEP LHISEKQPAT IPEVLYRTAT ELGDTKGIIY LQPDGTEVYQ
SYRRLWDDGL RIAKGLRQSG LKAKQSVILQ LGDNSQLLPA FWGCVLTGVV PAPLAVPPTY
AESSSGTQKL KDAWTLLDKP AVITDRGMHQ EMLDWAKEQG LEGFRAIIVE DLLSAEADTD
WHQSSPEDLA LLLLTSGSTG TPKAVMLNHR NIMSMVKGII QMQGFTREDI TFNWMPFDHV
GGIGMLHLRD VYLGCQEINV SSETILMEPL KWLDWIDHYR ASVTWAPNFA FGLVTDFAEE
IKDKKWDLSS MRYMLNGGEA MVAKVGRRIL ELLEPHGLPA DAIRPAWGMS ETSSGVIFSH
EFTRAGTSDD DHFVEIGSPI PGFSMRIVND HNELVEEGEI GRFQVSGLSV TSGYYQRPDL
NESVFTEDGW FETGDLGFLR NGRLTITGRT KDAIIINGIN YYSHAIESAV EELPEIETSY
TAACAVRLGQ NSTDQLAIFF VTSAKLNDEQ MSQLLRNIQS HVSQVIGVTP EYLLPVQKEE
IPKTAIGKIQ RTQLKTSFEN GEFDHLLHKP NRMNDAVQDE GIQQADQVKR VREEIQKHLL
TCLTEELHVS HDWVEPNANI QSLGVNSIKM MKLIRSIEKN YHIKLTAREI HQYPTIERLA
SYLSEHEDLS SLSADKKGTD TYKTEPERSQ ATFQPLSEVQ KGLWTLQKMS PEKSAYHVPL
CFKFSSGLHH ETFQQAFGLV LNQHPILKHV IQEKDGVPFL KNEPALSIEI KTENISSLKE
SDIPAFLRKK VKEPYVKENS PLVRVMSFSR SEQEHFLLVV IHHLIFDGVS SVTFIRSLFD
TYQLLLKGQQ PEKAVSPAIY HDFAAWEKNM LAGKDGVKHR TYWQKQLSGT LPNLQLPNVS
ASSVDSQFRE DTYTRRLSSG FMNQVRTFAK EHSVNVTTVF LSCYMMLLGR YTGQKEQIVG
MPAMVRPEER FDDAIGHFLN MLPIRSELNP ADTFSSFISK LQLTILDGLD HAAYPFPKMV
RDLNIPRSQA GSPVFQTAFF YQNFLQSGSY QSLLSRYADF FSVDFVEYIH QEGEYELVFE
LWETEEKMEL NIKYNTGLFD AASISAMFDH FVYVTEQAML NPSQPLKEYS LLPEAEKQMI
LKTWNATGKT YPYITFHELF EQQAKKTPDR AAVSYEGQTL TYRELDEKST QLAIYLQAHG
VGPDRLAGIY VDRSLDMLVG LLAILKAGGA YVPLDPSYPA ERLEYMLEDS EVFITLTTSE
LVNTLSWNGV TTALLDQDWD EIAQTASDRK VLTRTVTPEN LAYVIYTSGS TGKPKGVMIP
HKALTNFLVS MGETPGLTAE DKMLAVTTYC FDIAALELFL PLIKGAHCYI CQTEHTKDVE
KLKRDIRAIK PTVMQATPAT WKMLFYSGWE NEESVKILCG GEALPETLKR YFLDTGSEAW
NMFGPTETTI WSAVQRINVE CSHATIGRPI ANTQIYITDS QLAPVPAGVP GELCIAGDGV
AKGYYKKEEL TDSRFIDNPF EPGSKLYRTG DMARWLTGGR IEYIGRIDNQ VKIRGFRIEL
GDIESRLSEH PGILECVVVA DMDNLAAYYT AKHANASLTA RELRHFVKNA LPAYMVPSYF
IQLDHMPLTP NGKIDRNSLK NIDLSGEQLK QRQTSPKNIQ DTVFTIWQEV LKTSDIEWDD
GFFDVGGDSL LAVTVADRIK HELSCEFSVT DLFEYSTIKN ISQYITEQRM GDASDHIPTD
PAAHIEDQST EMSDLPDYYD DSVAIIGISC EFPGAKNHDE FWENLRDGKE SIAFFNKEEL
QRFGISKEIA ENADYVPAKA SIDGKDRFDP SFFQISPKDA EFMDPQLRML LTHSWKAIED
AGYAARQIPQ TSVFMSASNN SYRALLPSDT TESLETPDGY VSWVLAQSGT IPTMISHKLG
LRGPSYFVHA NCSSSLIGLH SAYKSLLSGE SDYALVGGAT LHTESNIGYV HQPGLNFSSD
GHIKAFDASA DGMIGGEGVA VVLLKKAADA VKDGDHIYAL LRGIGVNNDG ADKVGFYAPS
VKGQADVVQQ VMNQTKVQPE SICYVEAHGT GTKLGDPIEL AALTNVYRQY TNKTQFCGIG
SVKTNIGHLD TAAGLAGCIK VVMSLYHQEL APSVNYKEPN PNTDLASSPF YVVDQKKTLS
REIKTHRAAL SSFGLGGTNT HAIFEQFKRD SDKGKIDGTC IVPISAKNKE RLQEYAEDIL
AYLERRGFEN SQLPDFAYTL QVGREAMEHR VVFIADHVNE LKQRLTDFIN GNTAIEGCFQ
GSKHNAREVS WLTEDEDSAE LIRKWMAKGK VNKLAEMWSK GAHIDWMQLY KGERPNRMSL
PTYPFAKERY WPSQDDRKPV AQISGNQTGI GSIHPLLHQN TSDFSEQKFS SVFTGDEFFL
RDHVVRGKPV LPGVAYLEMA YAAINQAAGS EIGQDVRIRL NHTVWVQPVV VDRHSAQVDI
SLFPEEDGKI TFDIYSTQED GDDPVIHSQG SAELASAAET PVADLTEMSR RCGKGKMSPD
QFYEEGRSRG MFHGPAFQGI KNVNIGNREV LAQLQLPEIV SGTNEQFVLH PSIMDSALQT
ATICIMQELT DQKLILPFAL EELEVIKGCS SSMWAYARLS DSDHSGGVVQ KADIDVIDES
GTVCVRIKGF STRVLEGEVH TSKPSTRHER LMLEPVWEKQ NEEREDEDLS YTEHIIVLFE
TERSVTDSIA SHMKDARVIT LNEAVGHIAE RYQCYMQNIF ELLQSKVRKL SAGRIIIQAI
VPLEKEKQLF AGVSGLFKTA EIEFSKLTAQ VIEIEKPEEM IDLHLKLKDD SRRPFDKQIR
YEAGYRFVKG WREMVLPSAD TLHMPWRDEG VYLITGGAGS LGLLFAKEIA NRTGRSTIVL
TGRSVLSEDK ENELEALRSI GAEVVYREAD VSDQHAVRHL LEEIKERYGT LNGIIHGAGS
SKDRFIIHKT NEEFQEVLQP KVSGLLHVDE CSKDFPLDFF IFFSSVSGCL GNAGQADYAA
ANSFMDAFAE YRRSLAASKK RFGSTISFNW PLWEEGGMQV GAEDEKRMLK TTGMVPMPTD
SGLKAFYQGI VSDKPQVFVM EGQLQKMKQK LLSAGSKAKR NDQRKADQDQ GQTRKLEAAL
IQMVGAILKV NTDDIDVNTE LSEYGFDSVT FTVFTNKINE KFQLELTPTI FFEYGSVQSL
AEYVVAAYQG EWNQDATAKG KDERTNLVHS LSSLEASLSN MVSAILKVNS EDIDVNTELS
EYGFDSVTFT VFTNKINEEF QLELTPTIFF EYGSLHSLAE YLTVEHGDTL VQEREKPEGQ
EELQTKSSEA PKITSRRKRR FTQPIIAKAE RNKKQAADFE PVAIVGISGR FPGAMDIDEF
WKNLEEGKDS ITEVPKDRWD WREHYGNPDT DVNKTDIKWG GFIDGVAEFD PLFFGISPRE
ADYVDPQQRL LMTYVWKALE DAGCSPQSLS GTGTGIFIGT GNTGYKDLFH RANLPIEGHA
ATGHMIPSVG PNRMSYFLNI HGPSEPVETA CSSSLVAIHR AVTAMQNGDC EMAIAGGVNT
ILTEEAHISY SKAGMLSTDG RCKTFSADAN GYVRGEGVGM VMLKKLEDAE RDGNHIYGVI
RGTAENHGGR ANTLTSPNPK AQADLLVRAY RQADIDPSTV TYIEAHGTGT ELGDPIEING
LKAAFKELSN MRGESQPDVP DHRCGIGSVK SNIGHLELAA GISGLIKVLL QMKHKTLVKS
LHCETLNPYL QLTDSPFYIV QEKQEWKSVT DRDGNELPRR AGISSFGIGG VNAHIVIEEY
MPKANSEHTA TEQPNVIVLS AKNKSRLIDR ASQLLEVIRN KKYTDQDLHR IAYTLQVGRE
EMDERLACVA GTMQELEEKL QAFVDGKEET DEFFRGQSHR NKETQTIFTA DEDMALALDA
WIRKRKYAKL ADLWVKGVSI QWNTLYGETK PRLISLPSYP FAKDHYWVPA KEHSERDKKE
LVNAIEDRAA CFLTKQWSLS PIGSAVPGTR TVAILCCQET ADLAAEVSSY FPNHLLIDVS
RIENDQSDID WKEFDGLVDV IGCGWDDEGR LDWIEWVQRL VEFGHKEGLR LLCVTKGLES
FQNTSVRMAG ASRAGLYRML QCEYSHLISR HMDAEEVTDH RRLAKLIADE FYSDSYDAEV
CYRDGLRYQA FLKAHPETGK ATEQSAVFPK DHVLLITGGT RGIGLLCARH FAECYGVKKL
VLTGREQLPP REEWARFKTS NTSLAEKIQA VRELEAKGVQ VEMLSLTLSD DAQVEQTLQH
IKRTLGPIGG VIHCAGLTDM DTLAFIRKTS DDIQRVLEPK VSGLTTLYRH VCNEPLQFFV
LFSSVSAIIP ELSAGQADYA MANSYMDYFA EAHQKHAPII SVQWPNWKET GMGEVTNQAY
RDSGLLSITN SEGLRFLDQI VSKKFGPVVL PAMANQTNWE PELLMKRRKP HEGGLQEAAL
QSPPARDIEE ADEVSKCDGL LSETQSWLID LFTEELRIDR EDFEIDGLFQ DYGVDSIILA
QVLQRINRKL EAALDPSILY EYPTIQRFAD WLIGSYSERL SALFGGRISD ASAPLENKIE
AEASVPGKDR ALTPQIQAPA ILSPDSHAEG IAVVGLSCRF PGAETLESYW SLLSEGRSSI
GPIPAERWGC KTPYYAGVID GVSYFDPDFF LLHEEDVRAM DPQALLVLEE CLKLLYHAGY
TPEEIKGKPV GVYIGGRSQH KPDEDSLDHA KNPIVTVGQN YLAANLSQFF DVRGPSVVVD
TACSSALVGM NMAIQALRGG DIQSAIVGGV SLLSSDASHR LFDRRGILSK HSSFHVFDER
ADGVVLGEGV GMVMLKTVKQ ALEDGDIIYA VVKAASVNND GRTAGPATPN LEAQKEVMKD
ALFKSGKKPE DISYLEANGS GSIVTDLLEL KAIQSVYRSG HSSPLSLGSI KPNIGHPLCA
EGIASFIKVV LMLKERRFVP FLSGEKEMAH FDQQKANITF SRALEKWTDS QPTAAINCFA
DGGTNAHVIV EAWEKDEKHA IKRSPISPPQ LKKRMLSPGE PKLEAETSKM TAANIWDTYE
VEV
//
