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Database: UniProt
Entry: STCK_EMENI
LinkDB: STCK_EMENI
Original site: STCK_EMENI 
ID   STCK_EMENI              Reviewed;        1914 AA.
AC   Q00706; C8VDT7; Q5AV66;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   24-JAN-2024, entry version 131.
DE   RecName: Full=Fatty acid synthase beta subunit stcK {ECO:0000303|PubMed:8643646};
DE            EC=2.3.1.86 {ECO:0000250|UniProtKB:Q8TGA1};
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase {ECO:0000250|UniProtKB:Q8TGA1};
DE              EC=4.2.1.59 {ECO:0000250|UniProtKB:Q8TGA1};
DE   Includes:
DE     RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000250|UniProtKB:Q8TGA1};
DE              EC=1.3.1.9 {ECO:0000250|UniProtKB:Q8TGA1};
DE   Includes:
DE     RecName: Full=[Acyl-carrier-protein] acetyltransferase {ECO:0000250|UniProtKB:Q8TGA1};
DE              EC=2.3.1.38 {ECO:0000250|UniProtKB:Q8TGA1};
DE   Includes:
DE     RecName: Full=[Acyl-carrier-protein] malonyltransferase {ECO:0000250|UniProtKB:Q8TGA1};
DE              EC=2.3.1.39 {ECO:0000250|UniProtKB:Q8TGA1};
DE     AltName: Full=S-acyl fatty acid synthase thioesterase {ECO:0000250|UniProtKB:Q8TGA1};
DE              EC=3.1.2.14 {ECO:0000250|UniProtKB:Q8TGA1};
DE     AltName: Full=Sterigmatocystin biosynthesis cluster protein K {ECO:0000303|PubMed:8643646};
GN   Name=stcK {ECO:0000303|PubMed:8643646}; ORFNames=AN7814;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, AND PATHWAY.
RC   STRAIN=FGSC 26;
RX   PubMed=8643646; DOI=10.1073/pnas.93.4.1418;
RA   Brown D.W., Yu J.-H., Kelkar H.S., Fernandes M., Nesbitt T.C., Keller N.P.,
RA   Adams T.H., Leonard T.J.;
RT   "Twenty-five coregulated transcripts define a sterigmatocystin gene cluster
RT   in Aspergillus nidulans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:1418-1422(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [4]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=8017929; DOI=10.1128/aem.60.5.1444-1450.1994;
RA   Keller N.P., Kantz N.J., Adams T.H.;
RT   "Aspergillus nidulans verA is required for production of the mycotoxin
RT   sterigmatocystin.";
RL   Appl. Environ. Microbiol. 60:1444-1450(1994).
RN   [5]
RP   FUNCTION.
RX   PubMed=7486998; DOI=10.1128/aem.61.10.3628-3632.1995;
RA   Keller N.P., Segner S., Bhatnagar D., Adams T.H.;
RT   "StcS, a putative P-450 monooxygenase, is required for the conversion of
RT   versicolorin A to sterigmatocystin in Aspergillus nidulans.";
RL   Appl. Environ. Microbiol. 61:3628-3632(1995).
RN   [6]
RP   FUNCTION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=7642507; DOI=10.1128/jb.177.16.4792-4800.1995;
RA   Yu J.-H., Leonard T.J.;
RT   "Sterigmatocystin biosynthesis in Aspergillus nidulans requires a novel
RT   type I polyketide synthase.";
RL   J. Bacteriol. 177:4792-4800(1995).
RN   [7]
RP   FUNCTION.
RX   PubMed=8900026; DOI=10.1128/aem.62.11.4296-4298.1996;
RA   Kelkar H.S., Keller N.P., Adams T.H.;
RT   "Aspergillus nidulans stcP encodes an O-methyltransferase that is required
RT   for sterigmatocystin biosynthesis.";
RL   Appl. Environ. Microbiol. 62:4296-4298(1996).
RN   [8]
RP   FUNCTION.
RX   PubMed=8962148; DOI=10.1073/pnas.93.25.14873;
RA   Brown D.W., Adams T.H., Keller N.P.;
RT   "Aspergillus has distinct fatty acid synthases for primary and secondary
RT   metabolism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:14873-14877(1996).
RN   [9]
RP   FUNCTION.
RX   PubMed=8999832; DOI=10.1074/jbc.272.3.1589;
RA   Kelkar H.S., Skloss T.W., Haw J.F., Keller N.P., Adams T.H.;
RT   "Aspergillus nidulans stcL encodes a putative cytochrome P-450
RT   monooxygenase required for bisfuran desaturation during
RT   aflatoxin/sterigmatocystin biosynthesis.";
RL   J. Biol. Chem. 272:1589-1594(1997).
RN   [10]
RP   INDUCTION.
RX   PubMed=9680223; DOI=10.1046/j.1365-2958.1998.00907.x;
RA   Fernandes M., Keller N.P., Adams T.H.;
RT   "Sequence-specific binding by Aspergillus nidulans aflR, a C6 zinc cluster
RT   protein regulating mycotoxin biosynthesis.";
RL   Mol. Microbiol. 28:1355-1365(1998).
RN   [11]
RP   FUNCTION.
RX   PubMed=10618248; DOI=10.1128/aem.66.1.359-362.2000;
RA   Keller N.P., Watanabe C.M., Kelkar H.S., Adams T.H., Townsend C.A.;
RT   "Requirement of monooxygenase-mediated steps for sterigmatocystin
RT   biosynthesis by Aspergillus nidulans.";
RL   Appl. Environ. Microbiol. 66:359-362(2000).
RN   [12]
RP   REVIEW ON STERIGMATOCYSTIN BIOSYNTHESIS.
RX   PubMed=24957370; DOI=10.3390/metabo2010100;
RA   Klejnstrup M.L., Frandsen R.J., Holm D.K., Nielsen M.T., Mortensen U.H.,
RA   Larsen T.O., Nielsen J.B.;
RT   "Genetics of polyketide metabolism in Aspergillus nidulans.";
RL   Metabolites 2:100-133(2012).
CC   -!- FUNCTION: Fatty acid synthase beta subunit; part of the gene cluster
CC       that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-
CC       derived furanocoumarin which is part of the most toxic and carcinogenic
CC       compounds among the known mycotoxins (PubMed:8643646). The first step
CC       in the biosynthesis of sterigmatocystin is the production of hexanoate
CC       by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148).
CC       The polyketide backbone is assembled by the non-reducing polyketide
CC       synthase stcA by condensation of the starter hexanoyl-CoA and 7
CC       malonyl-CoA extender units followed by cyclization and release of
CC       norsolorinic acid (By similarity). Norsolorinic acid is the first
CC       stable intermediate in the biosynthesis of sterigmatocystin and is
CC       converted into averantin (AVN) by the ketoreductase stcE which reduces
CC       the hexanoate ketone to an alcohol (PubMed:8643646) (Probable).
CC       Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the
CC       cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-
CC       hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the
CC       5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step
CC       is the conversion of OAVN into averufin (AVF) which is catalyzed by a
CC       yet to be identified enzyme (PubMed:24957370). The cytochrome P450
CC       monoxygenase stcB and the flavin-binding monooxygenase stcW are both
CC       required for the conversion of averufin to 1-hydroxyversicolorone
CC       (PubMed:10618248). The esterase stcI probably catalyzes the formation
CC       of versiconal hemiacetal acetate from 1-hydroxyversicolorone
CC       (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the
CC       biosynthetic step from versiconal to versicolorin B (VERB)
CC       (PubMed:24957370). The next step is performed by the versicolorin B
CC       desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The
CC       ketoreductase stcU and the cytochrome P450 monooxygenase stcS are
CC       involved in the conversion of versicolorin A to
CC       demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas
CC       stcQ and the reductase stcR might be involved in the biosynthetic step
CC       from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The
CC       final step in the biosynthesis of sterigmatocystin is the methylation
CC       of demethylsterigmatocystin catalyzed by the methyltransferase stcP
CC       (PubMed:8900026). {ECO:0000250|UniProtKB:Q12053,
CC       ECO:0000269|PubMed:10618248, ECO:0000269|PubMed:7486998,
CC       ECO:0000269|PubMed:8643646, ECO:0000269|PubMed:8900026,
CC       ECO:0000269|PubMed:8962148, ECO:0000269|PubMed:8999832,
CC       ECO:0000303|PubMed:24957370, ECO:0000305|PubMed:8643646}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain
CC         fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+);
CC         Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:83139; EC=2.3.1.86;
CC         Evidence={ECO:0000250|UniProtKB:Q8TGA1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA;
CC         Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78446; EC=2.3.1.38;
CC         Evidence={ECO:0000250|UniProtKB:Q8TGA1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC         Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449; EC=2.3.1.39;
CC         Evidence={ECO:0000250|UniProtKB:Q8TGA1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC         Evidence={ECO:0000250|UniProtKB:Q8TGA1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC         H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC         COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC         Evidence={ECO:0000250|UniProtKB:Q8TGA1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) +
CC         holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC         COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14;
CC         Evidence={ECO:0000250|UniProtKB:Q8TGA1};
CC   -!- PATHWAY: Mycotoxin biosynthesis; sterigmatocystin biosynthesis.
CC       {ECO:0000269|PubMed:8643646}.
CC   -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC       (alpha and beta). {ECO:0000250|UniProtKB:P19097}.
CC   -!- INDUCTION: The genes forming the sterigmatocystin biosynthesis cluster
CC       are co-regulated and induced on oatmeal porridge or the fungal isolates
CC       were grown either on oatmeal porridge or in YEC medium (0.2% yeast
CC       extract, 5.0% corn steep liquor) (PubMed:8643646, PubMed:8017929).
CC       Expression is positively regulated by the cluster-specific
CC       transcription factor aflR that binds the palindromic sequence 5'-
CC       TCG(N5)CGA-3'found in the promoter (PubMed:9680223).
CC       {ECO:0000269|PubMed:8017929, ECO:0000269|PubMed:8643646,
CC       ECO:0000269|PubMed:9680223}.
CC   -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC49199.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U34740; AAC49199.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AACD01000132; EAA61602.1; -; Genomic_DNA.
DR   EMBL; BN001304; CBF80162.1; -; Genomic_DNA.
DR   RefSeq; XP_681083.1; XM_675991.1.
DR   AlphaFoldDB; Q00706; -.
DR   SMR; Q00706; -.
DR   STRING; 227321.Q00706; -.
DR   EnsemblFungi; CBF80162; CBF80162; ANIA_07814.
DR   GeneID; 2869366; -.
DR   KEGG; ani:AN7814.2; -.
DR   VEuPathDB; FungiDB:AN7814; -.
DR   eggNOG; ENOG502SKWI; Eukaryota.
DR   HOGENOM; CLU_000114_5_0_1; -.
DR   InParanoid; Q00706; -.
DR   OMA; VCAGHFR; -.
DR   OrthoDB; 2238313at2759; -.
DR   UniPathway; UPA00377; -.
DR   Proteomes; UP000000560; Chromosome IV.
DR   GO; GO:0005835; C:fatty acid synthase complex; IBA:GO_Central.
DR   GO; GO:0004317; F:(3R)-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:InterPro.
DR   GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:InterPro.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:InterPro.
DR   GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0045461; P:sterigmatocystin biosynthetic process; IMP:AspGD.
DR   CDD; cd03447; FAS_MaoC; 1.
DR   Gene3D; 1.20.930.70; -; 1.
DR   Gene3D; 3.30.1120.100; -; 1.
DR   Gene3D; 3.30.70.3320; -; 1.
DR   Gene3D; 3.30.70.3330; -; 1.
DR   Gene3D; 6.10.60.10; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 2.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 3.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR016452; Fas1/AflB-like.
DR   InterPro; IPR013565; Fas1/AflB-like_central.
DR   InterPro; IPR040883; FAS_meander.
DR   InterPro; IPR003965; Fatty_acid_synthase.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR039569; MaoC-like_dehydrat_N.
DR   InterPro; IPR002539; MaoC-like_dom.
DR   InterPro; IPR032088; SAT.
DR   PANTHER; PTHR10982:SF21; FATTY ACID SYNTHASE SUBUNIT BETA; 1.
DR   PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08354; Fas1-AflB-like_hel; 1.
DR   Pfam; PF17951; FAS_meander; 1.
DR   Pfam; PF13452; MaoC_dehydrat_N; 1.
DR   Pfam; PF01575; MaoC_dehydratas; 1.
DR   Pfam; PF16073; SAT; 1.
DR   PIRSF; PIRSF005562; FAS_yeast_beta; 1.
DR   PRINTS; PR01483; FASYNTHASE.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR   SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
PE   2: Evidence at transcript level;
KW   Hydrolase; Lyase; Multifunctional enzyme; NAD; NADP; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..1914
FT                   /note="Fatty acid synthase beta subunit stcK"
FT                   /id="PRO_0000180290"
FT   DOMAIN          1398..1532
FT                   /note="MaoC-like"
FT                   /evidence="ECO:0000255"
FT   REGION          17..395
FT                   /note="Acetyltransferase (AT) domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TGA1, ECO:0000255"
FT   REGION          446..692
FT                   /note="Enoyl reductase (ER) domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TGA1, ECO:0000255"
FT   REGION          1009..1509
FT                   /note="Dehydratase (DH) domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TGA1, ECO:0000255"
FT   REGION          1548..1900
FT                   /note="Malonyl/palmitoyl transferase (MT/PT) domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TGA1, ECO:0000255"
FT   CONFLICT        525
FT                   /note="I -> T (in Ref. 1; AAC49199)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1914 AA;  211238 MW;  EE42E46F43442BD6 CRC64;
     MTPSPFLDAV DAGLSRLYAC FGGQGPSNWA GLDELVHLSH AYADCAPIQD LLDSSARRLE
     SLAAIPHRSS FFAGRGFQLQ AWLNDAAASA PLPEDLALSP YSFPINTLLS LLHYAITAYS
     LQLDPGQLRQ KLQGAIGHSQ GVFVAAAIAI SHTDHGWPSF YRAADLALQL SFWVGLESHH
     ASPRSILCAN EVIDCLENGE GAPSHLLSVT GLDINHLERL VRKLNDQGGD SLYISLINGH
     NKFVLAGAPH ALRGVCIALR SVKASPELDQ SRVPFPLRRS VVDVQFLPVS APYHSSLLSS
     VELRVTDAIG GLRLRGNDLA IPVYCQANGS LRNLQDYGTH DILLTLIQSV TVERVNWPAL
     CWAMNDATHV LSFGPGAVGS LVQDVLEGTG MNVVNLSGQS MASNLSLLNL SAFALPLGKD
     WGRKYRPRLR KAAEGSAHAS IETKMTRLLG TPHVMVAGMT PTTCSPELVA AIIQADYHVE
     FACGGYYNRA TLETALRQLS RSIPPHRSIT CNVIYASPKA LSWQIQVLRR LIMEEGLPID
     GITVGAGIPS PEVVKEWIDM LAISHIWFKP GSVDAIDRVL TIARQYPTLP VGIQWTGGRA
     GGHHSCEDFH LPILDCYARI RNCENVILVA GSGFGGAEDT WPYMNGSWSC KLGYAPMPFD
     GILLGSRMMV AREAKTSFAV KQLIVEAPGV KDDGNDNGAW AKCEHDAVGG VISVTSEMGQ
     PIHVLATRAM RLWKEFDDRF FSIRDPKRLK AALKQHRVEI INRLNNDFAR PWFAQTDSSK
     PTEIEELSYR QVLRRLCQLT YVQHQARWID SSYLSLVHDF LRLAQGRLGS GSEAELRFLS
     CNTPIELEAS FDAAYGVQGD QILYPEDVSL LINLFRRQGQ KPVPFIPRLD ADFQTWFKKD
     SLWQSEDVDA VVDQDAQRVC IIQGPVAVRH SRVCDEPVKD ILDGITEAHL KMMLKEAASD
     NGYTWANQRD EKGNRLPGIE TSQEGSLCRY YLVGPTLPST EAIVEHLVGE CAWGYAALSQ
     KKVVFGQNRA PNPIRDAFKP DIGDVIEAKY MDGCLREITL YHSLRRQGDP RAIRAALGLI
     HLDGNKVSVT LLTRSKGKRP ALEFKMELLG GTMGPLILKM HRTDYLDSVR RLYTDLWIGR
     DLPSPTSVGL NSEFTGDRVT ITAEDVNTFL AIVGQAGPAR CRAWGTRGPV VPIDYAVVIA
     WTALTKPILL EALDADPLRL LHQSASTRFV PGIRPLHVGD TVTTSSRITE RTITTIGQRV
     EISAELLREG KPVVRLQTTF IIQRRPEESV SQQQFRCVEE PDMVIRVDSH TKLRVLMSRK
     WFLLDGPCSD LIGKILIFQL HSQTVFDAAG APASLQVSGS VSLAPSDTSV VCVSSVGTRI
     GRVYMEEEGF GANPVMDFLN RHGAPRVQRQ PLPRAGWTGD DAASISFTAP AQSEGYAMVS
     GDTNPIHVCP LFSRFAGLGQ PVVHGLHLSA TVRRILEWII GDNERTRFCS WAPSFDGLVR
     ANDRLRMEIQ HFAMADGCMV VHVRVLKEST GEQVMHAEAV LEQAQTTYVF TGQGTQERGM
     GMALYDTNAA ARAVWDRAER HFRSQYGISL LHIVRENPTS LTVNFGSRRG RQIRDIYLSM
     SDSDPSMLPG LTRDSRSYTF NYPSGLLMST QFAQPALAVM EIAEYAHLQA QGVVQTQAIF
     AGHSLGEYSS LGACTTIMPF ESLLSLILYR GLKMQNTLPR NANGRTDYGM VAADPSRIRS
     DFTEDRLIEL VRLVSQATGV LLEVVNYNVH SRQYVCAGHV RSLWVLSHAC DDLSRSTSPN
     SPQTMSECIA HHIPSSCSVT NETELSRGRA TIPLAGVDIP FHSQMLRGHI DGYRQYLRHH
     LRVSDIKPEE LVGRWIPNVT GKPFALDAPY IRLVQGVTQS RPLLELLRRV EENR
//
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