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Database: UniProt
Entry: P40806
LinkDB: P40806
Original site: P40806 
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   16-APR-2014, entry version 113.
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 PHOSPHOPANTETHEINYLATION AT
RP   SER-1689.
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   PDB; 4NA1; X-ray; 1.95 A; A/B=3336-3951.
DR   PDB; 4NA2; X-ray; 2.30 A; A/B=3336-3951.
DR   PDB; 4NA3; X-ray; 2.89 A; A/B=3336-3951.
DR   PDBsum; 4NA1; -.
DR   PDBsum; 4NA2; -.
DR   PDBsum; 4NA3; -.
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; 7.
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   OrthoDB; EOG6QP0WP; -.
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: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; IPR025110; AMP-bd_C.
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; PF13193; AMP-binding_C; 1.
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; SSF47336; 7.
DR   SUPFAM; SSF53901; SSF53901; 7.
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   3D-structure; Acyltransferase; Antibiotic biosynthesis; Coiled coil;
KW   Complete proteome; Cytoplasm; Ligase; Multifunctional enzyme; NADP;
KW   Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW   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   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
//
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