Family Of Pesticidal Proteins And Methods For Their Use

Abstract

Compositions and methods for conferring pesticidal activity to bacteria, plants, plant cells, tissues and seeds are provided. Compositions comprising a coding sequence for pesticidal polypeptides are provided. The coding sequences can be used in DNA constructs or expression cassettes for transformation and expression in plants and bacteria. Compositions also comprise transformed bacteria, plants, plant cells, tissues, and seeds. In particular, isolated pesticidal nucleic acid molecules are provided. Additionally, amino acid sequences corresponding to the polynucleotides are encompassed. In particular, the present invention provides for isolated nucleic acid molecules comprising nucleotide sequences encoding the amino acid sequence shown in SEQ ID NO: 2, 4, 6, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37 or 61, the nucleotide sequence set forth in SEQ ID NO: 1, 3, 5, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, or 60, or the nucleotide sequence deposited in a bacterial host as Accession No. B-30955, B-30956, B-30957, B-30958, B-30942, B-30939, B-30941, B-50047, B-30959, B-30960, B-30943, or B-50048, as well as variants and fragments thereof.

Description

CROSS REFERENCE TO RELATED APPLICATION

[0001] This application is a divisional of U.S. patent application Ser. No. 13/168,454, filed Jun. 24, 2011, which is a continuation of U.S. patent application Ser. No. 11/763,947, filed Jun. 15, 2007, which claims the benefit of U.S. Provisional Application Ser. Nos. 60/814,007, filed Jun. 15, 2006; 60/813,859, filed Jun. 15, 2006; 60/814,420, filed Jun. 16, 2006; 60/814,212, filed Jun. 16, 2006; and 60/814,989, filed Jun. 20, 2006, the contents of which are herein incorporated by reference in their entirety.

REFERENCE TO SEQUENCE LISTING SUBMITTED ELECTRONICALLY

[0002] The official copy of the sequence listing is submitted electronically via EFS-Web as an ASCII formatted sequence listing with a file named "APA039US01NDSEQLIST.txt", created on Aug. 5, 2014, and having a size of 305 kilobytes and is filed concurrently with the specification. The sequence listing contained in this ASCII formatted document is part of the specification and is herein incorporated by reference in its entirety.

FIELD OF THE INVENTION

[0003] This invention relates to the field of molecular biology. Provided are novel genes that encode pesticidal proteins. These proteins and the nucleic acid sequences that encode them are useful in preparing pesticidal formulations and in the production of transgenic pest-resistant plants.

BACKGROUND OF THE INVENTION

[0004] Bacillus thuringiensis is a Gram-positive spore forming soil bacterium characterized by its ability to produce crystalline inclusions that are specifically toxic to certain orders and species of insects, but are harmless to plants and other non-targeted organisms. For this reason, compositions including Bacillus thuringiensis strains or their insecticidal proteins can be used as environmentally-acceptable insecticides to control agricultural insect pests or insect vectors for a variety of human or animal diseases.

[0005] Crystal (Cry) proteins (delta-endotoxins) from Bacillus thuringiensis have potent insecticidal activity against predominantly Lepidopteran, Dipteran, and Coleopteran larvae. These proteins also have shown activity against Hymenoptera, Homoptera, Phthiraptera, Mallophaga, and Acari pest orders, as well as other invertebrate orders such as Nemathelminthes, Platyhelminthes, and Sarcomastigorphora (Feitelson (1993) The Bacillus Thuringiensis family tree. In Advanced Engineered Pesticides, Marcel Dekker, Inc., New York, N.Y.) These proteins were originally classified as CryI to CryV based primarily on their insecticidal activity. The major classes were Lepidoptera-specific (I), Lepidoptera- and Diptera-specific (II), Coleoptera-specific (III), Diptera-specific (IV), and nematode-specific (V) and (VI). The proteins were further classified into subfamilies; more highly related proteins within each family were assigned divisional letters such as Cry1A, Cry1B, Cry1C, etc. Even more closely related proteins within each division were given names such as Cry1C1, Cry1C2, etc.

[0006] A new nomenclature was recently described for the Cry genes based upon amino acid sequence homology rather than insect target specificity (Crickmore et al. (1998) Microbiol. Mol. Biol. Rev. 62:807-813). In the new classification, each toxin is assigned a unique name incorporating a primary rank (an Arabic number), a secondary rank (an uppercase letter), a tertiary rank (a lowercase letter), and a quaternary rank (another Arabic number). In the new classification, Roman numerals have been exchanged for Arabic numerals in the primary rank. Proteins with less than 45% sequence identity have different primary ranks, and the criteria for secondary and tertiary ranks are 78% and 95%, respectively.

[0007] The crystal protein does not exhibit insecticidal activity until it has been ingested and solubilized in the insect midgut. The ingested protoxin is hydrolyzed by proteases in the insect digestive tract to an active toxic molecule. (Hofte and Whiteley (1989) Microbiol. Rev. 53:242-255). This toxin binds to apical brush border receptors in the midgut of the target larvae and inserts into the apical membrane creating ion channels or pores, resulting in larval death.

[0008] Delta-endotoxins generally have five conserved sequence domains, and three conserved structural domains (see, for example, de Maagd et al. (2001) Trends Genetics 17:193-199). The first conserved structural domain consists of seven alpha helices and is involved in membrane insertion and pore formation. Domain II consists of three beta-sheets arranged in a Greek key configuration, and domain III consists of two antiparallel beta-sheets in "jelly-roll" formation (de Maagd et al., 2001, supra). Domains II and III are involved in receptor recognition and binding, and are therefore considered determinants of toxin specificity.

[0009] Because of the devastation that insects can confer, and the improvement in yield by controlling insect pests, there is a continual need to discover new forms of pesticidal toxins.

SUMMARY OF INVENTION

[0010] Compositions and methods for conferring pesticidal activity to bacteria, plants, plant cells, tissues and seeds are provided. Compositions include nucleic acid molecules encoding sequences for pesticidal and insectidal polypeptides, vectors comprising those nucleic acid molecules, and host cells comprising the vectors. Compositions also include the pesticidal polypeptide sequences and antibodies to those polypeptides. The nucleotide sequences can be used in DNA constructs or expression cassettes for transformation and expression in organisms, including microorganisms and plants. The nucleotide or amino acid sequences may be synthetic sequences that have been designed for expression in an organism including, but not limited to, a microorganism or a plant. Compositions also comprise transformed bacteria, plants, plant cells, tissues, and seeds.

[0011] In particular, isolated nucleic acid molecules are provided that encode a pesticidal protein. Additionally, amino acid sequences corresponding to the pesticidal protein are encompassed. In particular, the present invention provides for an isolated nucleic acid molecule comprising a nucleotide sequence encoding the amino acid sequence shown in SEQ ID NO:2, 4, 6, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37 or 61, a nucleotide sequence set forth in SEQ ID NO:1, 3, 5, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, or 60, or the delta-endotoxin nucleotide sequence of the DNA insert of the plasmid deposited in a bacterial host as Accession No. B-30955, B-30956, B-30957, B-30958, B-30942, B-30939, B-30941, B-50047, B-30959, B-30960, B-30943, or B-50048, as well as variants and fragments thereof. Nucleotide sequences that are complementary to a nucleotide sequence of the invention, or that hybridize to a sequence of the invention are also encompassed.

[0012] Methods are provided for producing the polypeptides of the invention, and for using those polypeptides for controlling or killing a lepidopteran, coleopteran, nematode, or dipteran pest. Methods and kits for detecting the nucleic acids and polypeptides of the invention in a sample are also included.

[0013] The compositions and methods of the invention are useful for the production of organisms with enhanced pest resistance or tolerance. These organisms and compositions comprising the organisms are desirable for agricultural purposes. The compositions of the invention are also useful for generating altered or improved proteins that have pesticidal activity, or for detecting the presence of pesticidal proteins or nucleic acids in products or organisms.

DESCRIPTION OF FIGURES

[0014] FIG. 1 shows an alignment of AXMI-022 with the Iota1b from Clostridium perfringens (SEQ ID NO:49), Isp1A from Brevibacillus laterosporus (SEQ ID NO:50), Isp1B from Brevibacillus laterosporus (SEQ ID NO:51), Vip1Ab from Bacillus thuringiensis (SEQ ID NO:52), and Vip1Ac from Bacillus thuringiensis (SEQ ID NO:53).

[0015] FIG. 2 shows an alignment of AXMI-022 with Vip1Ab (SEQ ID NO:52).

[0016] FIG. 3 shows an alignment of AXMI-022 with Cry 37Aa1 from Bacillus thuringiensis (SEQ ID NO:54).

[0017] FIG. 4 shows an alignment of AXMI-023 with the Vip2 pesticidal protein (SEQ ID NO:55), Isp2a from Brevibacillus laterosporus (SEQ ID NO:56) and Iota toxin component Ia from Clostridium perfringens (SEQ ID NO:57).

DETAILED DESCRIPTION

[0018] The present invention is drawn to compositions and methods for regulating pest resistance or tolerance in organisms, particularly plants or plant cells. By "resistance" is intended that the pest (e.g., insect) is killed upon ingestion or other contact with the polypeptides of the invention. By "tolerance" is intended an impairment or reduction in the movement, feeding, reproduction, or other functions of the pest. The methods involve transforming organisms with a nucleotide sequence encoding a pesticidal protein of the invention. In particular, the nucleotide sequences of the invention are useful for preparing plants and microorganisms that possess pesticidal activity. Thus, transformed bacteria, plants, plant cells, plant tissues and seeds are provided. Compositions are pesticidal nucleic acids and proteins of Bacillus or other species. The sequences find use in the construction of expression vectors for subsequent transformation into organisms of interest, as probes for the isolation of other homologous (or partially homologous) genes, and for the generation of altered pesticidal proteins by methods known in the art, such as domain swapping or DNA shuffling. The proteins find use in controlling or killing lepidopteran, coleopteran, dipteran, and nematode pest populations and for producing compositions with pesticidal activity.

[0019] Plasmids containing the nucleotide sequences of the invention were deposited in the permanent collection of the Agricultural Research Service Culture Collection, Northern Regional Research Laboratory (NRRL), 1815 North University Street, Peoria, Ill. 61604, United States of America, in accordance with Table 1. This deposit will be maintained under the terms of the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure. Access to these deposits will be available during the pendency of the application to the Commissioner of Patents and Trademarks and persons determined by the Commissioner to be entitled thereto upon request. Upon allowance of any claims in the application, the Applicants will make available to the public, pursuant to 37 C.F.R. .sctn.1.808, sample(s) of the deposit with the ATCC. This deposit was made merely as a convenience for those of skill in the art and is not an admission that a deposit is required under 35 U.S.C. .sctn.112.

TABLE-US-00001 TABLE 1 Microorganism Deposit NRRL Gene Strain Clone number Deposit Date axmi-011 ATX13008 pAX4600 B-30961 Jul. 21, 2006 axmi-012 ATX13026 pAX012 B-30955 Jul. 21, 2006 axmi-013 ATX13002 pAX013 B-30956 Jul. 21, 2006 axmi-015 ATX13026 pAX015 B-30957 Jul. 21, 2006 axmi-019 ATX14875 pAX019 B-30958 Jul. 21, 2006 axmi-044 ATX14759 pAX2599 B-30942 Jun. 15, 2006 axmi-037 ATX1489 pAX2558 B-30939 Jun. 15, 2006 axmi-043 ATX15398 pAX2597 B-30941 Jun. 15, 2006 axmi-033 ATX14833 pAX4341 B-50047 May 29, 2007 axmi-034 ATX14833 pAX4341 B-50047 May 29, 2007 axmi-022 ATX13045 pAX022 B-30959 Jul. 21, 2006 axmi-023 ATX13045 pAX023 B-30960 Jul. 21, 2006 axmi-041 ATX21738 pAX4310 B-30943 Jun. 15, 2006 axmi-063 ATX12972 pAX5036 B-50048 May 29, 2007 axmi-064 ATX12972 pAX5036 B-50048 May 29, 2007

[0020] By "pesticidal toxin" or "pesticidal protein" is intended a toxin that has toxic activity against one or more pests, including, but not limited to, members of the Lepidoptera, Diptera, and Coleoptera orders, or the Nematoda phylum, or a protein that has homology to such a protein. Pesticidal proteins have been isolated from organisms including, for example, Bacillus sp., Clostridium bifermentans and Paenibacillus popilliae. Pesticidal proteins include amino acid sequences deduced from the full-length nucleotide sequences disclosed herein, and amino acid sequences that are shorter than the full-length sequences, either due to the use of an alternate downstream start site, or due to processing that produces a shorter protein having pesticidal activity. Processing may occur in the organism the protein is expressed in, or in the pest after ingestion of the protein.

[0021] Pesticidal proteins encompass delta-endotoxins. Delta-endotoxins include proteins identified as cry1 through cry43, cyt1 and cyt2, and Cyt-like toxin. There are currently over 250 known species of delta-endotoxins with a wide range of specificities and toxicities. For an expansive list see Crickmore et al. (1998), Microbiol. Mol. Biol. Rev. 62:807-813, and for regular updates see Crickmore et al. (2003) "Bacillus thuringiensis toxin nomenclature," at www.biols.susx.ac.uk/Home/Neil_Crickmore/Bt/index.

[0022] Also provided herein are nucleotide sequences encoding polypeptides with homology to several other known classes of pesticidal protein toxins. For example, axmi-011, axmi-012, axmi-015, axmi-032, axmi-044, axmi-033, axmi-034, axmi-022, axmi-063, and axmi-064 demonstrate homology to pesticidal binary toxins such as VIP, Bin, and MTX toxins. The VIP1/VIP2 toxins (see, for example, U.S. Pat. No. 5,770,696, herein incorporated by reference in its entirety) are binary pesticidal toxins that exhibit strong activity on insects by a mechanism believed to involve receptor-mediated endocytosis followed by cellular toxification, similar to the mode of action of other binary ("A/B") toxins. A/B toxins such as VIP, C2, CDT, CST, or the B. anthracis edema and lethal toxins initially interact with target cells via a specific, receptor-mediated binding of "B" components as monomers. These monomers then form homoheptamers. The "B" heptamer-receptor complex then acts as a docking platform that subsequently binds and allows the translocation of an enzymatic "A" component(s) into the cytosol via receptor-mediated endocytosis. Once inside the cell's cytosol, "A" components inhibit normal cell function by, for example, ADP-ribosylation of G-actin, or increasing intracellular levels of cyclic AMP (cAMP). See Barth et al. (2004) Microbiol Mol Biol Rev 68:373-402, herein incorporated by reference in its entirety.

[0023] Aside from the A/B type binary toxins, other types of binary toxins that act as pesticidal proteins are known in the art. Cry34Ab1 and Cry35Ab1 comprise a binary toxin with pesticidal activity that was identified from strain PS149B1 (Ellis et al. (2002) Appl Environ Microbiol. 68:1137-45, herein incorporated by reference in its entirety). These toxins have molecular masses of approximately 14 and 44 kDa, respectively. Other binary toxins with similar organization and homology to Cry34Aa and Cry34Ab have been identified (Baum et al. (2004) Appl Environ Microbiol. 70:4889-98, herein incorporated by reference in its entirety).

[0024] BinA and BinB are proteins from Bacillus sphaericus that comprise a mosquitocidal binary toxin protein (Baumann et al. (1991) Micriobiol. Rev. 55:425-36). Cry35 exhibits amino acid similarity to these BinA and BinB proteins. Cry36 (ET69) and Cry38 (ET75) (International Patent Application No. WO/00/66742-B, herein incorporated by reference in its entirety) are independently isolated peptides that also exhibit amino acid similarity to BinA and BinB, and thus are likely to comprise binary toxins.

[0025] Cry23 (also known as cryET33; U.S. Pat. No. 6,063,756, herein incorporated by reference in its entirety) and Cry37 (also known as cryET34; U.S. Pat. No. 6,063,756, herein incorporated by reference in its entirety) also appear to be binary pesticidal toxins. Cry23 also exhibits homology to MTX2 and MTX3 toxins. The term "MTX" is used in the art to delineate a set of pesticidal proteins that are produced by Bacillus sphaericus. The first of these, often referred to in the art as MTX1, is synthesized as a parasporal crystal which is toxic to mosquitoes. The major components of the crystal are two proteins of 51 and 42 kDa, Since the presence of both proteins are required for toxicity, MTX1 is considered a "binary" toxin (Baumann et al. (1991) Microbiol. Rev. 55:425-436).

[0026] By analysis of different Bacillus sphaericus strains with differing toxicities, two new classes of MTX toxins have been identified. MTX2 and MTX3 represent separate, related classes of pesticidal toxins that exhibit pesticidal activity. See, for example, Baumann et al. (1991) Microbiol. Rev. 55:425-436, herein incorporated by reference in its entirety. MTX2 is a 100-kDa toxin. More recently MTX3 has been identified as a separate toxin, though the amino acid sequence of MTX3 from B. sphaericus is 38% identitical to the MTX2 toxin of B. sphaericus SSII-1 (Liu, et al. (1996) Appl. Environ. Microbiol. 62: 2174-2176).

[0027] Thus, provided herein are novel isolated nucleotide sequences that confer pesticidal activity. These isolated nucleotide sequences encode polypeptides with homology to known delta-endotoxins or binary toxins. Also provided are the amino acid sequences of the pesticidal proteins. The protein resulting from translation of this gene allows cells to control or kill pests that ingest it.

Isolated Nucleic Acid Molecules, and Variants and Fragments Thereof

[0028] One aspect of the invention pertains to isolated or recombinant nucleic acid molecules comprising nucleotide sequences encoding pesticidal proteins and polypeptides or biologically active portions thereof, as well as nucleic acid molecules sufficient for use as hybridization probes to identify nucleic acid molecules encoding proteins with regions of sequence homology. As used herein, the term "nucleic acid molecule" is intended to include DNA molecules (e.g., recombinant DNA, cDNA or genomic DNA) and RNA molecules (e.g., mRNA) and analogs of the DNA or RNA generated using nucleotide analogs. The nucleic acid molecule can be single-stranded or double-stranded, but preferably is double-stranded DNA.

[0029] An "isolated" or "purified" nucleic acid molecule or protein, or biologically active portion thereof, is substantially free of other cellular material, or culture medium when produced by recombinant techniques, or substantially free of chemical precursors or other chemicals when chemically synthesized. Preferably, an "isolated" nucleic acid is free of sequences (preferably protein encoding sequences) that naturally flank the nucleic acid (i.e., sequences located at the 5' and 3' ends of the nucleic acid) in the genomic DNA of the organism from which the nucleic acid is derived. For purposes of the invention, "isolated" when used to refer to nucleic acid molecules excludes isolated chromosomes. For example, in various embodiments, the isolated nucleic acid molecule encoding a pesticidal protein can contain less than about 5 kb, 4 kb, 3 kb, 2 kb, 1 kb, 0.5 kb, or 0.1 kb of nucleotide sequences that naturally flank the nucleic acid molecule in genomic DNA of the cell from which the nucleic acid is derived. A pesticidal protein that is substantially free of cellular material includes preparations of protein having less than about 30%, 20%, 10%, or 5% (by dry weight) of non-pesticidal protein (also referred to herein as a "contaminating protein").

[0030] Nucleotide sequences encoding the proteins of the present invention include the sequence set forth in SEQ ID NO:1, 3, 5, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, or 60, or the nucleotide sequence deposited in a bacterial host as Accession No. B-30955, B-30956, B-30957, B-30958, B-30942, B-30939, B-30941, B-50047, B-30959, B-30960, B-30943, or B-50048, and variants, fragments, and complements thereof. By "complement" is intended a nucleotide sequence that is sufficiently complementary to a given nucleotide sequence such that it can hybridize to the given nucleotide sequence to thereby form a stable duplex. The corresponding amino acid sequence for the pesticidal protein encoded by this nucleotide sequence are set forth in SEQ ID NO:2, 4, 6, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37 or 61.

[0031] Nucleic acid molecules that are fragments of these nucleotide sequences encoding pesticidal proteins are also encompassed by the present invention. By "fragment" is intended a portion of the nucleotide sequence encoding a pesticidal protein. A fragment of a nucleotide sequence may encode a biologically active portion of a pesticidal protein, or it may be a fragment that can be used as a hybridization probe or PCR primer using methods disclosed below. Nucleic acid molecules that are fragments of a nucleotide sequence encoding a pesticidal protein comprise at least about 50, 100, 200, 300, 400, 500, 600, 700, 800, 900, 1000, 1100, 1200, 1300, 1350, 1400 contiguous nucleotides, or up to the number of nucleotides present in a full-length nucleotide sequence encoding a pesticidal protein disclosed herein (for example, 957 nucleotides for SEQ ID NO: 1; 927 nucleotides for SEQ ID NO:3, 1017 nucleotides for SEQ ID NO:5; 1422 nucleotides for SEQ ID NO:8, 1053 nucleotides for SEQ ID NO:10; 1062 nucleotides for SEQ ID NO: 12, 942 nucleotides for SEQ ID NO: 14, etc.) depending upon the intended use. By "contiguous" nucleotides is intended nucleotide residues that are immediately adjacent to one another. Fragments of the nucleotide sequences of the present invention will encode protein fragments that retain the biological activity of the pesticidal protein and, hence, retain pesticidal activity. By "retains activity" is intended that the fragment will have at least about 30%, at least about 50%, at least about 70%, 80%, 90%, 95% or higher of the pesticidal activity of the pesticidal protein. Methods for measuring pesticidal activity are well known in the art. See, for example, Czapla and Lang (1990) J. Econ. Entomol. 83:2480-2485; Andrews et al. (1988) Biochem. J. 252:199-206; Marrone et al. (1985) J. of Economic Entomology 78:290-293; and U.S. Pat. No. 5,743,477, all of which are herein incorporated by reference in their entirety.

[0032] A fragment of a nucleotide sequence encoding a pesticidal protein that encodes a biologically active portion of a protein of the invention will encode at least about 15, 25, 30, 50, 75, 100, 125, 150, 175, 200, 250, 300, 350, 400, 450 contiguous amino acids, or up to the total number of amino acids present in a full-length pesticidal protein of the invention (for example, 318 amino acids for SEQ ID NO:2, 308 amino acids for SEQ ID NO:4, 338 amino acids for SEQ ID NO:6, 296 amino acids for SEQ ID NO:7, 473 amino acids for SEQ ID NO:9, 351 amino acids for SEQ ID NO:11, 353 amino acids for SEQ ID NO:13, and 314 amino acids for SEQ ID NO:15, etc.).

[0033] Preferred pesticidal proteins of the present invention are encoded by a nucleotide sequence sufficiently identical to the nucleotide sequence of SEQ ID NO: 1, 3, 5, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, or 60. By "sufficiently identical" is intended an amino acid or nucleotide sequence that has at least about 60% or 65% sequence identity, about 70% or 75% sequence identity, about 80% or 85% sequence identity, about 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or greater sequence identity compared to a reference sequence using one of the alignment programs described herein using standard parameters. One of skill in the art will recognize that these values can be appropriately adjusted to determine corresponding identity of proteins encoded by two nucleotide sequences by taking into account codon degeneracy, amino acid similarity, reading frame positioning, and the like.

[0034] To determine the percent identity of two amino acid sequences or of two nucleic acids, the sequences are aligned for optimal comparison purposes. The percent identity between the two sequences is a function of the number of identical positions shared by the sequences (i.e., percent identity=number of identical positions/total number of positions (e.g., overlapping positions).times.100). In one embodiment, the two sequences are the same length. The percent identity between two sequences can be determined using techniques similar to those described below, with or without allowing gaps. In calculating percent identity, typically exact matches are counted.

[0035] The determination of percent identity between two sequences can be accomplished using a mathematical algorithm. A nonlimiting example of a mathematical algorithm utilized for the comparison of two sequences is the algorithm of Karlin and Altschul (1990) Proc. Natl. Acad. Sci. USA 87:2264, modified as in Karlin and Altschul (1993) Proc. Natl. Acad. Sci. USA 90:5873-5877. Such an algorithm is incorporated into the BLASTN and BLASTX programs of Altschul et al. (1990) J. Mol. Biol. 215:403. BLAST nucleotide searches can be performed with the BLASTN program, score=100, wordlength=12, to obtain nucleotide sequences homologous to pesticidal-like nucleic acid molecules of the invention. BLAST protein searches can be performed with the BLASTX program, score=50, wordlength=3, to obtain amino acid sequences homologous to pesticidal protein molecules of the invention. To obtain gapped alignments for comparison purposes, Gapped BLAST (in BLAST 2.0) can be utilized as described in Altschul et al. (1997) Nucleic Acids Res. 25:3389. Alternatively, PSI-Blast can be used to perform an iterated search that detects distant relationships between molecules. See Altschul et al. (1997) supra. When utilizing BLAST, Gapped BLAST, and PSI-Blast programs, the default parameters of the respective programs (e.g., BLASTX and BLASTN) can be used. Alignment may also be performed manually by inspection.

[0036] Another non-limiting example of a mathematical algorithm utilized for the comparison of sequences is the ClustalW algorithm (Higgins et al. (1994) Nucleic Acids Res. 22:4673-4680). ClustalW compares sequences and aligns the entirety of the amino acid or DNA sequence, and thus can provide data about the sequence conservation of the entire amino acid sequence. The ClustalW algorithm is used in several commercially available DNA/amino acid analysis software packages, such as the ALIGNX module of the Vector NTI Program Suite (Invitrogen Corporation, Carlsbad, Calif.). After alignment of amino acid sequences with ClustalW, the percent amino acid identity can be assessed. A non-limiting example of a software program useful for analysis of ClustalW alignments is GENEDOC.TM.. GENEDOC.TM. (Karl Nicholas) allows assessment of amino acid (or DNA) similarity and identity between multiple proteins. Another non-limiting example of a mathematical algorithm utilized for the comparison of sequences is the algorithm of Myers and Miller (1988) CABIOS 4:11-17. Such an algorithm is incorporated into the ALIGN program (version 2.0), which is part of the GCG Wisconsin Genetics Software Package, Version 10 (available from Accelrys, Inc., 9685 Scranton Rd., San Diego, Calif., USA). When utilizing the ALIGN program for comparing amino acid sequences, a PAM 120 weight residue table, a gap length penalty of 12, and a gap penalty of 4 can be used.

[0037] Unless otherwise stated, GAP Version 10, which uses the algorithm of Needleman and Wunsch (1970) J. Mol. Biol. 48 (3):443-453, will be used to determine sequence identity or similarity using the following parameters: % identity and % similarity for a nucleotide sequence using GAP Weight of 50 and Length Weight of 3, and the nwsgapdna.cmp scoring matrix; % identity or % similarity for an amino acid sequence using GAP weight of 8 and length weight of 2, and the BLOSUM62 scoring program. Equivalent programs may also be used. By "equivalent program" is intended any sequence comparison program that, for any two sequences in question, generates an alignment having identical nucleotide residue matches and an identical percent sequence identity when compared to the corresponding alignment generated by GAP Version 10.

[0038] The invention also encompasses variant nucleic acid molecules. "Variants" of the pesticidal protein encoding nucleotide sequences include those sequences that encode the pesticidal proteins disclosed herein but that differ conservatively because of the degeneracy of the genetic code as well as those that are sufficiently identical as discussed above. Naturally occurring allelic variants can be identified with the use of well-known molecular biology techniques, such as polymerase chain reaction (PCR) and hybridization techniques as outlined below. Variant nucleotide sequences also include synthetically derived nucleotide sequences that have been generated, for example, by using site-directed mutagenesis but which still encode the pesticidal proteins disclosed in the present invention as discussed below. Variant proteins encompassed by the present invention are biologically active, that is they continue to possess the desired biological activity of the native protein, that is, pesticidal activity. By "retains activity" is intended that the variant will have at least about 30%, at least about 50%, at least about 70%, or at least about 80% of the pesticidal activity of the native protein. Methods for measuring pesticidal activity are well known in the art. See, for example, Czapla and Lang (1990) J. Econ. Entomol. 83: 2480-2485; Andrews et al. (1988) Biochem. J. 252:199-206; Marrone et al. (1985) J. of Economic Entomology 78:290-293; and U.S. Pat. No. 5,743,477, all of which are herein incorporated by reference in their entirety.

[0039] The skilled artisan will further appreciate that changes can be introduced by mutation of the nucleotide sequences of the invention thereby leading to changes in the amino acid sequence of the encoded pesticidal proteins, without altering the biological activity of the proteins. Thus, variant isolated nucleic acid molecules can be created by introducing one or more nucleotide substitutions, additions, or deletions into the corresponding nucleotide sequence disclosed herein, such that one or more amino acid substitutions, additions or deletions are introduced into the encoded protein. Mutations can be introduced by standard techniques, such as site-directed mutagenesis and PCR-mediated mutagenesis. Such variant nucleotide sequences are also encompassed by the present invention.

[0040] For example, conservative amino acid substitutions may be made at one or more, predicted, nonessential amino acid residues. A "nonessential" amino acid residue is a residue that can be altered from the wild-type sequence of a pesticidal protein without altering the biological activity, whereas an "essential" amino acid residue is required for biological activity. A "conservative amino acid substitution" is one in which the amino acid residue is replaced with an amino acid residue having a similar side chain. Families of amino acid residues having similar side chains have been defined in the art. These families include amino acids with basic side chains (e.g., lysine, arginine, histidine), acidic side chains (e.g., aspartic acid, glutamic acid), uncharged polar side chains (e.g., glycine, asparagine, glutamine, serine, threonine, tyrosine, cysteine), nonpolar side chains (e.g., alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan), beta-branched side chains (e.g., threonine, valine, isoleucine) and aromatic side chains (e.g., tyrosine, phenylalanine, tryptophan, histidine).

[0041] Delta-endotoxins generally have five conserved sequence domains, and three conserved structural domains (see, for example, de Maagd et al. (2001) Trends Genetics 17:193-199). The first conserved structural domain consists of seven alpha helices and is involved in membrane insertion and pore formation. Domain II consists of three beta-sheets arranged in a Greek key configuration, and domain III consists of two antiparallel beta-sheets in "jelly-roll" formation (de Maagd et al., 2001, supra). Domains II and III are involved in receptor recognition and binding, and are therefore considered determinants of toxin specificity.

[0042] Amino acid substitutions may be made in nonconserved regions that retain function. In general, such substitutions would not be made for conserved amino acid residues, or for amino acid residues residing within a conserved motif, where such residues are essential for protein activity. Examples of residues that are conserved and that may be essential for protein activity include, for example, residues that are identical between all proteins contained in an alignment of similar or related toxins to the sequences of the invention (e.g., residues that are identical between all proteins contained in the alignment in FIG. 1, 2, 3, or 4). Examples of residues that are conserved but that may allow conservative amino acid substitutions and still retain activity include, for example, residues that have only conservative substitutions between all proteins contained in an alignment of similar or related toxins to the sequences of the invention (e.g., residues that have only conservative substitutions between all proteins contained in the alignment in FIG. 1, 2, 3, or 4). However, one of skill in the art would understand that functional variants may have minor conserved or nonconserved alterations in the conserved residues.

[0043] Alternatively, variant nucleotide sequences can be made by introducing mutations randomly along all or part of the coding sequence, such as by saturation mutagenesis, and the resultant mutants can be screened for ability to confer pesticidal activity to identify mutants that retain activity. Following mutagenesis, the encoded protein can be expressed recombinantly, and the activity of the protein can be determined using standard assay techniques.

[0044] Using methods such as PCR, hybridization, and the like corresponding pesticidal sequences can be identified, such sequences having substantial identity to the sequences of the invention. See, for example, Sambrook and Russell (2001) Molecular Cloning: A Laboratory Manual. (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.) and Innis, et al. (1990) PCR Protocols: A Guide to Methods and Applications (Academic Press, NY).

[0045] In a hybridization method, all or part of the pesticidal nucleotide sequence can be used to screen cDNA or genomic libraries. Methods for construction of such cDNA and genomic libraries are generally known in the art and are disclosed in Sambrook and Russell, 2001, supra. The so-called hybridization probes may be genomic DNA fragments, cDNA fragments, RNA fragments, or other oligonucleotides, and may be labeled with a detectable group such as .sup.32P, or any other detectable marker, such as other radioisotopes, a fluorescent compound, an enzyme, or an enzyme co-factor. Probes for hybridization can be made by labeling synthetic oligonucleotides based on the known pesticidal protein-encoding nucleotide sequence disclosed herein. Degenerate primers designed on the basis of conserved nucleotides or amino acid residues in the nucleotide sequence or encoded amino acid sequence can additionally be used. The probe typically comprises a region of nucleotide sequence that hybridizes under stringent conditions to at least about 12, at least about 25, at least about 50, 75, 100, 125, 150, 175, or 200 consecutive nucleotides of nucleotide sequence encoding a pesticidal protein of the invention or a fragment or variant thereof. Methods for the preparation of probes for hybridization are generally known in the art and are disclosed in Sambrook and Russell, 2001, supra herein incorporated by reference.

[0046] For example, an entire pesticidal protein sequence disclosed herein, or one or more portions thereof, may be used as a probe capable of specifically hybridizing to corresponding pesticidal protein-like sequences and messenger RNAs. To achieve specific hybridization under a variety of conditions, such probes include sequences that are unique and are preferably at least about 10 nucleotides in length, or at least about 20 nucleotides in length. Such probes may be used to amplify corresponding pesticidal sequences from a chosen organism by PCR. This technique may be used to isolate additional coding sequences from a desired organism or as a diagnostic assay to determine the presence of coding sequences in an organism. Hybridization techniques include hybridization screening of plated DNA libraries (either plaques or colonies; see, for example, Sambrook et al. (1989) Molecular Cloning: A Laboratory Manual (2d ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.).

[0047] Hybridization of such sequences may be carried out under stringent conditions. By "stringent conditions" or "stringent hybridization conditions" is intended conditions under which a probe will hybridize to its target sequence to a detectably greater degree than to other sequences (e.g., at least 2-fold over background). Stringent conditions are sequence-dependent and will be different in different circumstances. By controlling the stringency of the hybridization and/or washing conditions, target sequences that are 100% complementary to the probe can be identified (homologous probing). Alternatively, stringency conditions can be adjusted to allow some mismatching in sequences so that lower degrees of similarity are detected (heterologous probing). Generally, a probe is less than about 1000 nucleotides in length, preferably less than 500 nucleotides in length.

[0048] Typically, stringent conditions will be those in which the salt concentration is less than about 1.5 M Na ion, typically about 0.01 to 1.0 M Na ion concentration (or other salts) at pH 7.0 to 8.3 and the temperature is at least about 30.degree. C. for short probes (e.g., 10 to 50 nucleotides) and at least about 60.degree. C. for long probes (e.g., greater than 50 nucleotides). Stringent conditions may also be achieved with the addition of destabilizing agents such as formamide. Exemplary low stringency conditions include hybridization with a buffer solution of 30 to 35% formamide, 1 M NaCl, 1% SDS (sodium dodecyl sulphate) at 37.degree. C., and a wash in 1.times. to 2.times.SSC (20.times.SSC=3.0 M NaCl/0.3 M trisodium citrate) at 50 to 55.degree. C. Exemplary moderate stringency conditions include hybridization in 40 to 45% formamide, 1.0 M NaCl, 1% SDS at 37.degree. C., and a wash in 0.5.times. to 1.times.SSC at 55 to 60.degree. C. Exemplary high stringency conditions include hybridization in 50% formamide, 1 M NaCl, 1% SDS at 37.degree. C., and a wash in 0.1.times.SSC at 60 to 65.degree. C. Optionally, wash buffers may comprise about 0.1% to about 1% SDS. Duration of hybridization is generally less than about 24 hours, usually about 4 to about 12 hours.

[0049] Specificity is typically the function of post-hybridization washes, the critical factors being the ionic strength and temperature of the final wash solution. For DNA-DNA hybrids, the T.sub.m can be approximated from the equation of Meinkoth and Wahl (1984) Anal. Biochem. 138:267-284: T.sub.m=81.5.degree. C.+16.6 (log M)+0.41 (% GC)-0.61 (% form)-500/L; where M is the molarity of monovalent cations, % GC is the percentage of guanosine and cytosine nucleotides in the DNA, % form is the percentage of formamide in the hybridization solution, and L is the length of the hybrid in base pairs. The T.sub.m is the temperature (under defined ionic strength and pH) at which 50% of a complementary target sequence hybridizes to a perfectly matched probe. T.sub.m is reduced by about 1.degree. C. for each 1% of mismatching; thus, T.sub.m, hybridization, and/or wash conditions can be adjusted to hybridize to sequences of the desired identity. For example, if sequences with .gtoreq.90% identity are sought, the T.sub.m can be decreased 10.degree. C. Generally, stringent conditions are selected to be about 5.degree. C. lower than the thermal melting point (T.sub.m) for the specific sequence and its complement at a defined ionic strength and pH. However, severely stringent conditions can utilize a hybridization and/or wash at 1, 2, 3, or 4.degree. C. lower than the thermal melting point (T.sub.m); moderately stringent conditions can utilize a hybridization and/or wash at 6, 7, 8, 9, or 10.degree. C. lower than the thermal melting point (T.sub.m); low stringency conditions can utilize a hybridization and/or wash at 11, 12, 13, 14, 15, or 20.degree. C. lower than the thermal melting point (T.sub.m). Using the equation, hybridization and wash compositions, and desired T.sub.m, those of ordinary skill will understand that variations in the stringency of hybridization and/or wash solutions are inherently described. If the desired degree of mismatching results in a T.sub.m of less than 45.degree. C. (aqueous solution) or 32.degree. C. (formamide solution), it is preferred to increase the SSC concentration so that a higher temperature can be used. An extensive guide to the hybridization of nucleic acids is found in Tijssen (1993) Laboratory Techniques in Biochemistry and Molecular Biology--Hybridization with Nucleic Acid Probes, Part I, Chapter 2 (Elsevier, New York); and Ausubel et al., eds. (1995) Current Protocols in Molecular Biology, Chapter 2 (Greene Publishing and Wiley-Interscience, New York). See Sambrook et al. (1989) Molecular Cloning: A Laboratory Manual (2d ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.).

Isolated Proteins and Variants and Fragments Thereof

[0050] Pesticidal proteins are also encompassed within the present invention. By "pesticidal protein" is intended a protein having the amino acid sequence set forth in SEQ ID NO:2, 4, 6, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37 or 61. Fragments, biologically active portions, and variants thereof are also provided, and may be used to practice the methods of the present invention.

[0051] "Fragments" or "biologically active portions" include polypeptide fragments comprising amino acid sequences sufficiently identical to the amino acid sequence set forth in SEQ ID NO:2, 4, 6, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37 or 61, and that exhibit pesticidal activity (for example, SEQ ID NO:7). A biologically active portion of a pesticidal protein can be a polypeptide that is, for example, 10, 25, 50, 100, 150, 200, 250 or more amino acids in length. Such biologically active portions can be prepared by recombinant techniques and evaluated for pesticidal activity. Methods for measuring pesticidal activity are well known in the art. See, for example, Czapla and Lang (1990) J. Econ. Entomol. 83:2480-2485; Andrews et al. (1988) Biochem. J. 252:199-206; Marrone et al. (1985) J. of Economic Entomology 78:290-293; and U.S. Pat. No. 5,743,477, all of which are herein incorporated by reference in their entirety. As used here, a fragment comprises at least 8 contiguous amino acids of SEQ ID NO:2, 4, 6, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37 or 61. The invention encompasses other fragments, however, such as any fragment in the protein greater than about 10, 20, 30, 50, 100, 150, 200, 250, or 300 amino acids.

[0052] By "variants" is intended proteins or polypeptides having an amino acid sequence that is at least about 60%, 65%, about 70%, 75%, about 80%, 85%, about 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the amino acid sequence of SEQ ID NO:2, 4, 6, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37 or 61. Variants also include polypeptides encoded by a nucleic acid molecule that hybridizes to the nucleic acid molecule of SEQ ID NO:1, 3, 5, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, or 60, or a complement thereof, under stringent conditions. Variants include polypeptides that differ in amino acid sequence due to mutagenesis. Variant proteins encompassed by the present invention are biologically active, that is they continue to possess the desired biological activity of the native protein, that is, retaining pesticidal activity. Methods for measuring pesticidal activity are well known in the art. See, for example, Czapla and Lang (1990) J. Econ. Entomol. 83:2480-2485; Andrews et al. (1988) Biochem. J. 252:199-206; Marrone et al. (1985) J. of Economic Entomology 78:290-293; and U.S. Pat. No. 5,743,477, all of which are herein incorporated by reference in their entirety.

[0053] Bacterial genes, such as the axmi genes of this invention, quite often possess multiple methionine initiation codons in proximity to the start of the open reading frame. Often, translation initiation at one or more of these start codons will lead to generation of a functional protein. These start codons can include ATG codons. However, bacteria such as Bacillus sp. also recognize the codon GTG as a start codon, and proteins that initiate translation at GTG codons contain a methionine at the first amino acid. Furthermore, it is not often determined a priori which of these codons are used naturally in the bacterium. Thus, it is understood that use of one of the alternate methionine codons may also lead to generation of pesticidal proteins. These pesticidal proteins are encompassed in the present invention and may be used in the methods of the present invention.

[0054] Antibodies to the polypeptides of the present invention, or to variants or fragments thereof, are also encompassed. Methods for producing antibodies are well known in the art (see, for example, Harlow and Lane (1988) Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.; U.S. Pat. No. 4,196,265).

Altered or Improved Variants

[0055] It is recognized that DNA sequences of a pesticidal protein may be altered by various methods, and that these alterations may result in DNA sequences encoding proteins with amino acid sequences different than that encoded by a pesticidal protein of the present invention. This protein may be altered in various ways including amino acid substitutions, deletions, truncations, and insertions of one or more amino acids of SEQ ID NO:2, 4, 6, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37 or 61, including up to about 2, about 3, about 4, about 5, about 6, about 7, about 8, about 9, about 10, about 15, about 20, about 25, 30, a 30, about 35, about 40, 45, a 45, about 50, about 55, about 60, about 65, about 70, about 75, about 80, about 85, about 90, about 100, about 105, about 110, about 115, about 120, about 125, about 130, about 135, about 140, about 145, about 150, about 155, or more amino acid substitutions, deletions or insertions. Methods for such manipulations are generally known in the art. For example, amino acid sequence variants of a pesticidal protein can be prepared by mutations in the DNA. This may also be accomplished by one of several forms of mutagenesis and/or in directed evolution. In some aspects, the changes encoded in the amino acid sequence will not substantially affect the function of the protein. Such variants will possess the desired pesticidal activity. However, it is understood that the ability of a pesticidal protein to confer pesticidal activity may be improved by the use of such techniques upon the compositions of this invention. For example, one may express a pesticidal protein in host cells that exhibit high rates of base misincorporation during DNA replication, such as XL-1 Red (Stratagene, La Jolla, Calif.). After propagation in such strains, one can isolate the DNA (for example by preparing plasmid DNA, or by amplifying by PCR and cloning the resulting PCR fragment into a vector), culture the pesticidal protein mutations in a non-mutagenic strain, and identify mutated genes with pesticidal activity, for example by performing an assay to test for pesticidal activity. Generally, the protein is mixed and used in feeding assays. See, for example Marrone et al. (1985) J. of Economic Entomology 78:290-293. Such assays can include contacting plants with one or more pests and determining the plant's ability to survive and/or cause the death of the pests. Examples of mutations that result in increased toxicity are found in Schnepf et al. (1998) Microbiol. Mol. Biol. Rev. 62:775-806.

[0056] Alternatively, alterations may be made to the protein sequence of many proteins at the amino or carboxy terminus without substantially affecting activity. This can include insertions, deletions, or alterations introduced by modern molecular methods, such as PCR, including PCR amplifications that alter or extend the protein coding sequence by virtue of inclusion of amino acid encoding sequences in the oligonucleotides utilized in the PCR amplification. Alternatively, the protein sequences added can include entire protein-coding sequences, such as those used commonly in the art to generate protein fusions. Such fusion proteins are often used to (1) increase expression of a protein of interest (2) introduce a binding domain, enzymatic activity, or epitope to facilitate either protein purification, protein detection, or other experimental uses known in the art (3) target secretion or translation of a protein to a subcellular organelle, such as the periplasmic space of Gram-negative bacteria, or the endoplasmic reticulum of eukaryotic cells, the latter of which often results in glycosylation of the protein.

[0057] Variant nucleotide and amino acid sequences of the present invention also encompass sequences derived from mutagenic and recombinogenic procedures such as DNA shuffling. With such a procedure, one or more different pesticidal protein coding regions can be used to create a new pesticidal protein possessing the desired properties. In this manner, libraries of recombinant polynucleotides are generated from a population of related sequence polynucleotides comprising sequence regions that have substantial sequence identity and can be homologously recombined in vitro or in vivo. For example, using this approach, sequence motifs encoding a domain of interest may be shuffled between a pesticidal gene of the invention and other known pesticidal genes to obtain a new gene coding for a protein with an improved property of interest, such as an increased insecticidal activity. Strategies for such DNA shuffling are known in the art. See, for example, Stemmer (1994) Proc. Natl. Acad. Sci. USA 91:10747-10751; Stemmer (1994) Nature 370:389-391; Crameri et al. (1997) Nature Biotech. 15:436-438; Moore et al. (1997) J. Mol. Biol. 272:336-347; Zhang et al. (1997) Proc. Natl. Acad. Sci. USA 94:4504-4509; Crameri et al. (1998) Nature 391:288-291; and U.S. Pat. Nos. 5,605,793 and 5,837,458.

[0058] Domain swapping or shuffling is another mechanism for generating altered pesticidal proteins. Domains may be swapped between pesticidal proteins, resulting in hybrid or chimeric toxins with improved pesticidal activity or target spectrum. Methods for generating recombinant proteins and testing them for pesticidal activity are well known in the art (see, for example, Naimov et al. (2001) Appl. Environ. Microbiol. 67:5328-5330; de Maagd et al. (1996) Appl. Environ. Microbiol. 62:1537-1543; Ge et al. (1991) J. Biol. Chem. 266:17954-17958; Schnepf et al. (1990) J. Biol. Chem. 265:20923-20930; Rang et al. 91999) Appl. Environ. Microbiol. 65:2918-2925).

Vectors

[0059] A pesticidal sequence of the invention may be provided in an expression cassette for expression in a plant of interest. By "plant expression cassette" is intended a DNA construct that is capable of resulting in the expression of a protein from an open reading frame in a plant cell. Typically these contain a promoter and a coding sequence. Often, such constructs will also contain a 3' untranslated region. Such constructs may contain a "signal sequence" or "leader sequence" to facilitate co-translational or post-translational transport of the peptide to certain intracellular structures such as the chloroplast (or other plastid), endoplasmic reticulum, or Golgi apparatus.

[0060] By "signal sequence" is intended a sequence that is known or suspected to result in cotranslational or post-translational peptide transport across the cell membrane. In eukaryotes, this typically involves secretion into the Golgi apparatus, with some resulting glycosylation. Insecticidal toxins of bacteria are often synthesized as protoxins, which are protolytically activated in the gut of the target pest (Chang (1987) Methods Enzymol. 153:507-516). In some embodiments of the present invention, the signal sequence is located in the native sequence, or may be derived from a sequence of the invention. By "leader sequence" is intended any sequence that when translated, results in an amino acid sequence sufficient to trigger co-translational transport of the peptide chain to a subcellular organelle. Thus, this includes leader sequences targeting transport and/or glycosylation by passage into the endoplasmic reticulum, passage to vacuoles, plastids including chloroplasts, mitochondria, and the like.

[0061] By "plant transformation vector" is intended a DNA molecule that is necessary for efficient transformation of a plant cell. Such a molecule may consist of one or more plant expression cassettes, and may be organized into more than one "vector" DNA molecule. For example, binary vectors are plant transformation vectors that utilize two non-contiguous DNA vectors to encode all requisite cis- and trans-acting functions for transformation of plant cells (Hellens and Mullineaux (2000) Trends in Plant Science 5:446-451). "Vector" refers to a nucleic acid construct designed for transfer between different host cells. "Expression vector" refers to a vector that has the ability to incorporate, integrate and express heterologous DNA sequences or fragments in a foreign cell. The cassette will include 5' and 3' regulatory sequences operably linked to a sequence of the invention. By "operably linked" is intended a functional linkage between a promoter and a second sequence, wherein the promoter sequence initiates and mediates transcription of the DNA sequence corresponding to the second sequence. Generally, operably linked means that the nucleic acid sequences being linked are contiguous and, where necessary to join two protein coding regions, contiguous and in the same reading frame. The cassette may additionally contain at least one additional gene to be cotransformed into the organism. Alternatively, the additional gene(s) can be provided on multiple expression cassettes.

[0062] "Promoter" refers to a nucleic acid sequence that functions to direct transcription of a downstream coding sequence. The promoter together with other transcriptional and translational regulatory nucleic acid sequences (also termed "control sequences") are necessary for the expression of a DNA sequence of interest.

[0063] Such an expression cassette is provided with a plurality of restriction sites for insertion of the pesticidal sequence to be under the transcriptional regulation of the regulatory regions.

[0064] The expression cassette will include in the 5'-3' direction of transcription, a transcriptional and translational initiation region (i.e., a promoter), a DNA sequence of the invention, and a translational and transcriptional termination region (i.e., termination region) functional in plants. The promoter may be native or analogous, or foreign or heterologous, to the plant host and/or to the DNA sequence of the invention. Additionally, the promoter may be the natural sequence or alternatively a synthetic sequence. Where the promoter is "native" or "homologous" to the plant host, it is intended that the promoter is found in the native plant into which the promoter is introduced. Where the promoter is "foreign" or "heterologous" to the DNA sequence of the invention, it is intended that the promoter is not the native or naturally occurring promoter for the operably linked DNA sequence of the invention.

[0065] The termination region may be native with the transcriptional initiation region, may be native with the operably linked DNA sequence of interest, may be native with the plant host, or may be derived from another source (i.e., foreign or heterologous to the promoter, the DNA sequence of interest, the plant host, or any combination thereof). Convenient termination regions are available from the Ti-plasmid of A. tumefaciens, such as the octopine synthase and nopaline synthase termination regions. See also Guerineau et al. (1991) Mol. Gen. Genet. 262:141-144; Proudfoot (1991) Cell 64:671-674; Sanfacon et al. (1991) Genes Dev. 5:141-149; Mogen et al. (1990) Plant Cell 2:1261-1272; Munroe et al. (1990) Gene 91:151-158; Ballas et al. (1989) Nucleic Acids Res. 17:7891-7903; and Joshi et al. (1987) Nucleic Acid Res. 15:9627-9639.

[0066] Where appropriate, the gene(s) may be optimized for increased expression in the transformed host cell. That is, the genes can be synthesized using host cell-preferred codons for improved expression, or may be synthesized using codons at a host-preferred codon usage frequency. Generally, the GC content of the gene will be increased. See, for example, Campbell and Gowri (1990) Plant Physiol. 92:1-11 for a discussion of host-preferred codon usage. Methods are available in the art for synthesizing plant-preferred genes. See, for example, U.S. Pat. Nos. 5,380,831, and 5,436,391, and Murray et al. (1989) Nucleic Acids Res. 17:477-498, herein incorporated by reference.

[0067] In one embodiment, the pesticidal protein is targeted to the chloroplast for expression. In this manner, where the pesticidal protein is not directly inserted into the chloroplast, the expression cassette will additionally contain a nucleic acid encoding a transit peptide to direct the pesticidal protein to the chloroplasts. Such transit peptides are known in the art. See, for example, Von Heijne et al. (1991) Plant Mol. Biol. Rep. 9:104-126; Clark et al. (1989) J. Biol. Chem. 264:17544-17550; Della-Cioppa et al. (1987) Plant Physiol. 84:965-968; Romer et al. (1993) Biochem. Biophys. Res. Commun. 196:1414-1421; and Shah et al. (1986) Science 233:478-481.

[0068] The pesticidal gene to be targeted to the chloroplast may be optimized for expression in the chloroplast to account for differences in codon usage between the plant nucleus and this organelle. In this manner, the nucleic acids of interest may be synthesized using chloroplast-preferred codons. See, for example, U.S. Pat. No. 5,380,831, herein incorporated by reference.

Plant Transformation

[0069] Methods of the invention involve introducing a nucleotide construct into a plant. By "introducing" is intended to present to the plant the nucleotide construct in such a manner that the construct gains access to the interior of a cell of the plant. The methods of the invention do not require that a particular method for introducing a nucleotide construct to a plant is used, only that the nucleotide construct gains access to the interior of at least one cell of the plant. Methods for introducing nucleotide constructs into plants are known in the art including, but not limited to, stable transformation methods, transient transformation methods, and virus-mediated methods.

[0070] By "plant" is intended whole plants, plant organs (e.g., leaves, stems, roots, etc.), seeds, plant cells, propagules, embryos and progeny of the same. Plant cells can be differentiated or undifferentiated (e.g. callus, suspension culture cells, protoplasts, leaf cells, root cells, phloem cells, pollen).

[0071] "Transgenic plants" or "transformed plants" or "stably transformed" plants or cells or tissues refers to plants that have incorporated or integrated exogenous nucleic acid sequences or DNA fragments into the plant cell. These nucleic acid sequences include those that are exogenous, or not present in the untransformed plant cell, as well as those that may be endogenous, or present in the untransformed plant cell.

[0072] "Heterologous" generally refers to the nucleic acid sequences that are not endogenous to the cell or part of the native genome in which they are present, and have been added to the cell by infection, transfection, microinjection, electroporation, microprojection, or the like.

[0073] Transformation of plant cells can be accomplished by one of several techniques known in the art. The pesticidal gene of the invention may be modified to obtain or enhance expression in plant cells. Typically a construct that expresses such a protein would contain a promoter to drive transcription of the gene, as well as a 3' untranslated region to allow transcription termination and polyadenylation. The organization of such constructs is well known in the art. In some instances, it may be useful to engineer the gene such that the resulting peptide is secreted, or otherwise targeted within the plant cell. For example, the gene can be engineered to contain a signal peptide to facilitate transfer of the peptide to the endoplasmic reticulum. It may also be preferable to engineer the plant expression cassette to contain an intron, such that mRNA processing of the intron is required for expression.

[0074] Typically this "plant expression cassette" will be inserted into a "plant transformation vector". This plant transformation vector may be comprised of one or more DNA vectors needed for achieving plant transformation. For example, it is a common practice in the art to utilize plant transformation vectors that are comprised of more than one contiguous DNA segment. These vectors are often referred to in the art as "binary vectors". Binary vectors as well as vectors with helper plasmids are most often used for Agrobacterium-mediated transformation, where the size and complexity of DNA segments needed to achieve efficient transformation is quite large, and it is advantageous to separate functions onto separate DNA molecules. Binary vectors typically contain a plasmid vector that contains the cis-acting sequences required for T-DNA transfer (such as left border and right border), a selectable marker that is engineered to be capable of expression in a plant cell, and a "gene of interest" (a gene engineered to be capable of expression in a plant cell for which generation of transgenic plants is desired). Also present on this plasmid vector are sequences required for bacterial replication. The cis-acting sequences are arranged in a fashion to allow efficient transfer into plant cells and expression therein. For example, the selectable marker gene and the pesticidal gene are located between the left and right borders. Often a second plasmid vector contains the trans-acting factors that mediate T-DNA transfer from Agrobacterium to plant cells. This plasmid often contains the virulence functions (Vir genes) that allow infection of plant cells by Agrobacterium, and transfer of DNA by cleavage at border sequences and vir-mediated DNA transfer, as is understood in the art (Hellens and Mullineaux (2000) Trends in Plant Science 5:446-451). Several types of Agrobacterium strains (e.g. LBA4404, GV3101, EHA101, EHA105, etc.) can be used for plant transformation. The second plasmid vector is not necessary for transforming the plants by other methods such as microprojection, microinjection, electroporation, polyethylene glycol, etc.

[0075] In general, plant transformation methods involve transferring heterologous DNA into target plant cells (e.g. immature or mature embryos, suspension cultures, undifferentiated callus, protoplasts, etc.), followed by applying a maximum threshold level of appropriate selection (depending on the selectable marker gene) to recover the transformed plant cells from a group of untransformed cell mass. Explants are typically transferred to a fresh supply of the same medium and cultured routinely. Subsequently, the transformed cells are differentiated into shoots after placing on regeneration medium supplemented with a maximum threshold level of selecting agent. The shoots are then transferred to a selective rooting medium for recovering rooted shoot or plantlet. The transgenic plantlet then grows into a mature plant and produces fertile seeds (e.g. Hiei et al. (1994) The Plant Journal 6:271-282; Ishida et al. (1996) Nature Biotechnology 14:745-750). Explants are typically transferred to a fresh supply of the same medium and cultured routinely. A general description of the techniques and methods for generating transgenic plants are found in Ayres and Park (1994) Critical Reviews in Plant Science 13:219-239 and Bommineni and Jauhar (1997) Maydica 42:107-120. Since the transformed material contains many cells; both transformed and non-transformed cells are present in any piece of subjected target callus or tissue or group of cells. The ability to kill non-transformed cells and allow transformed cells to proliferate results in transformed plant cultures. Often, the ability to remove non-transformed cells is a limitation to rapid recovery of transformed plant cells and successful generation of transgenic plants.

[0076] Transformation protocols as well as protocols for introducing nucleotide sequences into plants may vary depending on the type of plant or plant cell, i.e., monocot or dicot, targeted for transformation. Generation of transgenic plants may be performed by one of several methods, including, but not limited to, microinjection, electroporation, direct gene transfer, introduction of heterologous DNA by Agrobacterium into plant cells (Agrobacterium-mediated transformation), bombardment of plant cells with heterologous foreign DNA adhered to particles, ballistic particle acceleration, aerosol beam transformation (U.S. Published Application No. 20010026941; U.S. Pat. No. 4,945,050; International Publication No. WO 91/00915; U.S. Published Application No. 2002015066), Lec1 transformation, and various other non-particle direct-mediated methods to transfer DNA.

[0077] Methods for transformation of chloroplasts are known in the art. See, for example, Svab et al. (1990) Proc. Natl. Acad. Sci. USA 87:8526-8530; Svab and Maliga (1993) Proc. Natl. Acad. Sci. USA 90:913-917; Svab and Maliga (1993) EMBO J. 12:601-606. The method relies on particle gun delivery of DNA containing a selectable marker and targeting of the DNA to the plastid genome through homologous recombination. Additionally, plastid transformation can be accomplished by transactivation of a silent plastid-borne transgene by tissue-preferred expression of a nuclear-encoded and plastid-directed RNA polymerase. Such a system has been reported in McBride et al. (1994) Proc. Natl. Acad. Sci. USA 91:7301-7305.

[0078] Following integration of heterologous foreign DNA into plant cells, one then applies a maximum threshold level of appropriate selection in the medium to kill the untransformed cells and separate and proliferate the putatively transformed cells that survive from this selection treatment by transferring regularly to a fresh medium. By continuous passage and challenge with appropriate selection, one identifies and proliferates the cells that are transformed with the plasmid vector. Molecular and biochemical methods can then be used to confirm the presence of the integrated heterologous gene of interest into the genome of the transgenic plant.

[0079] The cells that have been transformed may be grown into plants in accordance with conventional ways. See, for example, McCormick et al. (1986) Plant Cell Reports 5:81-84. These plants may then be grown, and either pollinated with the same transformed strain or different strains, and the resulting hybrid having constitutive expression of the desired phenotypic characteristic identified. Two or more generations may be grown to ensure that expression of the desired phenotypic characteristic is stably maintained and inherited and then seeds harvested to ensure expression of the desired phenotypic characteristic has been achieved. In this manner, the present invention provides transformed seed (also referred to as "transgenic seed") having a nucleotide construct of the invention, for example, an expression cassette of the invention, stably incorporated into their genome.

Evaluation of Plant Transformation

[0080] Following introduction of heterologous foreign DNA into plant cells, the transformation or integration of heterologous gene in the plant genome is confirmed by various methods such as analysis of nucleic acids, proteins and metabolites associated with the integrated gene.

[0081] PCR analysis is a rapid method to screen transformed cells, tissue or shoots for the presence of incorporated gene at the earlier stage before transplanting into the soil (Sambrook and Russell (2001) Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.). PCR is carried out using oligonucleotide primers specific to the gene of interest or Agrobacterium vector background, etc.

[0082] Plant transformation may be confirmed by Southern blot analysis of genomic DNA (Sambrook and Russell, 2001, supra). In general, total DNA is extracted from the transformant, digested with appropriate restriction enzymes, fractionated in an agarose gel and transferred to a nitrocellulose or nylon membrane. The membrane or "blot" is then probed with, for example, radiolabeled .sup.32P target DNA fragment to confirm the integration of introduced gene into the plant genome according to standard techniques (Sambrook and Russell, 2001, supra).

[0083] In Northern blot analysis, RNA is isolated from specific tissues of transformant, fractionated in a formaldehyde agarose gel, and blotted onto a nylon filter according to standard procedures that are routinely used in the art (Sambrook and Russell, 2001, supra). Expression of RNA encoded by the pesticidal gene is then tested by hybridizing the filter to a radioactive probe derived from a pesticidal gene, by methods known in the art (Sambrook and Russell, 2001, supra).

[0084] Western blot, biochemical assays and the like may be carried out on the transgenic plants to confirm the presence of protein encoded by the pesticidal gene by standard procedures (Sambrook and Russell, 2001, supra) using antibodies that bind to one or more epitopes present on the pesticidal protein.

Pesticidal Activity in Plants

[0085] In another aspect of the invention, one may generate transgenic plants expressing a pesticidal protein that has pesticidal activity. Methods described above by way of example may be utilized to generate transgenic plants, but the manner in which the transgenic plant cells are generated is not critical to this invention. Methods known or described in the art such as Agrobacterium-mediated transformation, biolistic transformation, and non-particle-mediated methods may be used at the discretion of the experimenter. Plants expressing a pesticidal protein may be isolated by common methods described in the art, for example by transformation of callus, selection of transformed callus, and regeneration of fertile plants from such transgenic callus. In such process, one may use any gene as a selectable marker so long as its expression in plant cells confers ability to identify or select for transformed cells.

[0086] A number of markers have been developed for use with plant cells, such as resistance to chloramphenicol, the aminoglycoside G418, hygromycin, or the like. Other genes that encode a product involved in chloroplast metabolism may also be used as selectable markers. For example, genes that provide resistance to plant herbicides such as glyphosate, bromoxynil, or imidazolinone may find particular use. Such genes have been reported (Stalker et al. (1985) J. Biol. Chem. 263:6310-6314 (bromoxynil resistance nitrilase gene); and Sathasivan et al. (1990) Nucl. Acids Res. 18:2188 (AHAS imidazolinone resistance gene). Additionally, the genes disclosed herein are useful as markers to assess transformation of bacterial or plant cells. Methods for detecting the presence of a transgene in a plant, plant organ (e.g., leaves, stems, roots, etc.), seed, plant cell, propagule, embryo or progeny of the same are well known in the art. In one embodiment, the presence of the transgene is detected by testing for pesticidal activity.

[0087] Fertile plants expressing a pesticidal protein may be tested for pesticidal activity, and the plants showing optimal activity selected for further breeding. Methods are available in the art to assay for pest activity. Generally, the protein is mixed and used in feeding assays. See, for example Marrone et al. (1985) J. of Economic Entomology 78:290-293.

[0088] The present invention may be used for transformation of any plant species, including, but not limited to, monocots and dicots. Examples of plants of interest include, but are not limited to, corn (maize), sorghum, wheat, sunflower, tomato, crucifers, peppers, potato, cotton, rice, soybean, sugarbeet, sugarcane, tobacco, barley, and oilseed rape, Brassica sp., alfalfa, rye, millet, safflower, peanuts, sweet potato, cassava, coffee, coconut, pineapple, citrus trees, cocoa, tea, banana, avocado, fig, guava, mango, olive, papaya, cashew, macadamia, almond, oats, vegetables, ornamentals, and conifers.

[0089] Vegetables include, but are not limited to, tomatoes, lettuce, green beans, lima beans, peas, and members of the genus Curcumis such as cucumber, cantaloupe, and musk melon. Ornamentals include, but are not limited to, azalea, hydrangea, hibiscus, roses, tulips, daffodils, petunias, carnation, poinsettia, and chrysanthemum. Preferably, plants of the present invention are crop plants (for example, maize, sorghum, wheat, sunflower, tomato, crucifers, peppers, potato, cotton, rice, soybean, sugarbeet, sugarcane, tobacco, barley, oilseed rape., etc.).

Use in Pesticidal Control

[0090] General methods for employing strains comprising a nucleotide sequence of the present invention, or a variant thereof, in pesticide control or in engineering other organisms as pesticidal agents are known in the art. See, for example U.S. Pat. No. 5,039,523 and EP 0480762A2.

[0091] The Bacillus strains containing a nucleotide sequence of the present invention, or a variant thereof, or the microorganisms that have been genetically altered to contain a pesticidal gene and protein may be used for protecting agricultural crops and products from pests. In one aspect of the invention, whole, i.e., unlysed, cells of a toxin (pesticide)-producing organism are treated with reagents that prolong the activity of the toxin produced in the cell when the cell is applied to the environment of target pest(s).

[0092] Alternatively, the pesticide is produced by introducing a pesticidal gene into a cellular host. Expression of the pesticidal gene results, directly or indirectly, in the intracellular production and maintenance of the pesticide. In one aspect of this invention, these cells are then treated under conditions that prolong the activity of the toxin produced in the cell when the cell is applied to the environment of target pest(s). The resulting product retains the toxicity of the toxin. These naturally encapsulated pesticides may then be formulated in accordance with conventional techniques for application to the environment hosting a target pest, e.g., soil, water, and foliage of plants. See, for example EPA 0192319, and the references cited therein. Alternatively, one may formulate the cells expressing a gene of this invention such as to allow application of the resulting material as a pesticide.

[0093] The active ingredients of the present invention are normally applied in the form of compositions and can be applied to the crop area or plant to be treated, simultaneously or in succession, with other compounds. These compounds can be fertilizers, weed killers, cryoprotectants, surfactants, detergents, pesticidal soaps, dormant oils, polymers, and/or time-release or biodegradable carrier formulations that permit long-term dosing of a target area following a single application of the formulation. They can also be selective herbicides, chemical insecticides, virucides, microbicides, amoebicides, pesticides, fungicides, bacteriocides, nematocides, molluscicides or mixtures of several of these preparations, if desired, together with further agriculturally acceptable carriers, surfactants or application-promoting adjuvants customarily employed in the art of formulation. Suitable carriers and adjuvants can be solid or liquid and correspond to the substances ordinarily employed in formulation technology, e.g. natural or regenerated mineral substances, solvents, dispersants, wetting agents, tackifiers, binders or fertilizers. Likewise the formulations may be prepared into edible "baits" or fashioned into pest "traps" to permit feeding or ingestion by a target pest of the pesticidal formulation.

[0094] Methods of applying an active ingredient of the present invention or an agrochemical composition of the present invention that contains at least one of the pesticidal proteins produced by the bacterial strains of the present invention include leaf application, seed coating and soil application. The number of applications and the rate of application depend on the intensity of infestation by the corresponding pest.

[0095] The composition may be formulated as a powder, dust, pellet, granule, spray, emulsion, colloid, solution, or such like, and may be prepared by such conventional means as desiccation, lyophilization, homogenation, extraction, filtration, centrifugation, sedimentation, or concentration of a culture of cells comprising the polypeptide. In all such compositions that contain at least one such pesticidal polypeptide, the polypeptide may be present in a concentration of from about 1% to about 99% by weight.

[0096] Lepidopteran, dipteran, or coleopteran pests may be killed or reduced in numbers in a given area by the methods of the invention, or may be prophylactically applied to an environmental area to prevent infestation by a susceptible pest. Preferably the pest ingests, or is contacted with, a pesticidally-effective amount of the polypeptide. By "pesticidally-effective amount" is intended an amount of the pesticide that is able to bring about death to at least one pest, or to noticeably reduce pest growth, feeding, or normal physiological development. This amount will vary depending on such factors as, for example, the specific target pests to be controlled, the specific environment, location, plant, crop, or agricultural site to be treated, the environmental conditions, and the method, rate, concentration, stability, and quantity of application of the pesticidally-effective polypeptide composition. The formulations may also vary with respect to climatic conditions, environmental considerations, and/or frequency of application and/or severity of pest infestation.

[0097] The pesticide compositions described may be made by formulating either the bacterial cell, crystal and/or spore suspension, or isolated protein component with the desired agriculturally-acceptable carrier. The compositions may be formulated prior to administration in an appropriate means such as lyophilized, freeze-dried, desiccated, or in an aqueous carrier, medium or suitable diluent, such as saline or other buffer. The formulated compositions may be in the form of a dust or granular material, or a suspension in oil (vegetable or mineral), or water or oil/water emulsions, or as a wettable powder, or in combination with any other carrier material suitable for agricultural application. Suitable agricultural carriers can be solid or liquid and are well known in the art. The term "agriculturally-acceptable carrier" covers all adjuvants, inert components, dispersants, surfactants, tackifiers, binders, etc. that are ordinarily used in pesticide formulation technology; these are well known to those skilled in pesticide formulation. The formulations may be mixed with one or more solid or liquid adjuvants and prepared by various means, e.g., by homogeneously mixing, blending and/or grinding the pesticidal composition with suitable adjuvants using conventional formulation techniques. Suitable formulations and application methods are described in U.S. Pat. No. 6,468,523, herein incorporated by reference.

[0098] "Pest" includes but is not limited to, insects, fungi, bacteria, nematodes, mites, ticks, and the like. Insect pests include insects selected from the orders Coleoptera, Diptera, Hymenoptera, Lepidoptera, Mallophaga, Homoptera, Hemiptera, Orthroptera, Thysanoptera, Dermaptera, Isoptera, Anoplura, Siphonaptera, Trichoptera, etc., particularly Coleoptera, Lepidoptera, and Diptera.

[0099] The order Coleoptera includes the suborders Adephaga and Polyphaga. Suborder Adephaga includes the superfamilies Caraboidea and Gyrinoidea, while suborder Polyphaga includes the superfamilies Hydrophiloidea, Staphylinoidea, Cantharoidea, Cleroidea, Elateroidea, Dascilloidea, Dryopoidea, Byrrhoidea, Cucujoidea, Meloidea, Mordelloidea, Tenebrionoidea, Bostrichoidea, Scarabaeoidea, Cerambycoidea, Chrysomeloidea, and Curculionoidea. Superfamily Caraboidea includes the families Cicindelidae, Carabidae, and Dytiscidae. Superfamily Gyrinoidea includes the family Gyrimidae. Superfamily Hydrophiloidea includes the family Hydrophilidae. Superfamily Staphylinoidea includes the families Silphidae and Staphylimidae. Superfamily Cantharoidea includes the families Cantharidae and Lampyridae. Superfamily Cleroidea includes the families Cleridae and Dermestidae. Superfamily Elateroidea includes the families Elateridae and Buprestidae. Superfamily Cucujoidea includes the family Coccinellidae. Superfamily Meloidea includes the family Meloidae. Superfamily Tenebrionoidea includes the family Tenebrionidae. Superfamily Scarabaeoidea includes the families Passalidae and Scarabaeidae. Superfamily Cerambycoidea includes the family Cerambycidae. Superfamily Chrysomeloidea includes the family Chrysomelidae. Superfamily Curculionoidea includes the families Curculionidae and Scolytidae.

[0100] The order Diptera includes the Suborders Nematocera, Brachycera, and Cyclorrhapha. Suborder Nematocera includes the families Tipulidae, Psychodidae, Culicidae, Ceratopogonidae, Chironomidae, Simuliidae, Bibionidae, and Cecidomyiidae. Suborder Brachycera includes the families Stratiomyidae, Tabanidae, Therevidae, Asilidae, Mydidae, Bombyliidae, and Dolichopodidae. Suborder Cyclorrhapha includes the Divisions Aschiza and Aschiza. Division Aschiza includes the families Phoridae, Syrphidae, and Conopidae. Division Aschiza includes the Sections Acalyptratae and Calyptratae. Section Acalyptratae includes the families Otitidae, Tephritidae, Agromyzidae, and Drosophilidae. Section Calyptratae includes the families Hippoboscidae, Oestridae, Tachimidae, Anthomyiidae, Muscidae, Calliphoridae, and Sarcophagidae.

[0101] The order Lepidoptera includes the families Papilionidae, Pieridae, Lycaenidae, Nymphalidae, Danaidae, Satyridae, Hesperiidae, Sphingidae, Saturniidae, Geometridae, Arctiidae, Noctuidae, Lymantriidae, Sesiidae, and Tineidae.

[0102] Insect pests of the invention for the major crops include: Maize: Ostrinia nubilalis, European corn borer; Agrotis ipsilon, black cutworm; Helicoverpa zea, corn earworm; Spodoptera frugiperda, fall armyworm; Diatraea grandiosella, southwestern corn borer; Elasmopalpus lignosellus, lesser cornstalk borer; Diatraea saccharalis, surgarcane borer; Diabrotica virgifera, western corn rootworm; Diabrotica longicornis barberi, northern corn rootworm; Diabrotica undecimpunctata howardi, southern corn rootworm; Melanotus spp., wireworms; Cyclocephala borealis, northern masked chafer (white grub); Cyclocephala immaculata, southern masked chafer (white grub); Popillia japonica, Japanese beetle; Chaetocnema pulicaria, corn flea beetle; Sphenophorus maidis, maize billbug; Rhopalosiphum maidis, corn leaf aphid; Anuraphis maidiradicis, corn root aphid; Blissus leucopterus leucopterus, chinch bug; Melanoplus femurrubrum, redlegged grasshopper; Melanoplus sanguinipes, migratory grasshopper; Hylemya platura, seedcorn maggot; Agromyza parvicornis, corn blot leafminer; Anaphothrips obscrurus, grass thrips; Solenopsis milesta, thief ant; Tetranychus urticae, twospotted spider mite; Sorghum: Chilo partellus, sorghum borer; Spodoptera frugiperda, fall armyworm; Helicoverpa zea, corn earworm; Elasmopalpus lignosellus, lesser cornstalk borer; Feltia subterranea, granulate cutworm; Phyllophaga crinita, white grub; Eleodes, Conoderus, and Aeolus spp., wireworms; Oulema melanopus, cereal leaf beetle; Chaetocnema pulicaria, corn flea beetle; Sphenophorus maidis, maize billbug; Rhopalosiphum maidis; corn leaf aphid; Sipha flava, yellow sugarcane aphid; Blissus leucopterus leucopterus, chinch bug; Contarinia sorghicola, sorghum midge; Tetranychus cinnabarinus, carmine spider mite; Tetranychus urticae, twospotted spider mite Wheat: Pseudaletia unipunctata, army worm; Spodoptera frugiperda, fall armyworm; Elasmopalpus lignosellus, lesser cornstalk borer; Agrotis orthogonia, western cutworm; Elasmopalpus lignosellus, lesser cornstalk borer; Oulema melanopus, cereal leaf beetle; Hypera punctata, clover leaf weevil; Diabrotica undecimpunctata howardi, southern corn rootworm; Russian wheat aphid; Schizaphis graminum, greenbug; Macrosiphum avenae, English grain aphid; Melanoplus femurrubrum, redlegged grasshopper; Melanoplus differentialis, differential grasshopper; Melanoplus sanguinipes, migratory grasshopper; Mayetiola destructor, Hessian fly; Sitodiplosis mosellana, wheat midge; Meromyza americana, wheat stem maggot; Hylemya coarctata, wheat bulb fly; Frankliniella fusca, tobacco thrips; Cephus cinctus, wheat stem sawfly; Aceria tulipae, wheat curl mite; Sunflower: Suleima helianthana, sunflower bud moth; Homoeosoma electellum, sunflower moth; zygogramma exclamationis, sunflower beetle; Bothyrus gibbosus, carrot beetle; Neolasioptera murtfeldtiana, sunflower seed midge; Cotton: Heliothis virescens, cotton budworm; Helicoverpa zea, cotton bollworm; Spodoptera exigua, beet armyworm; Pectinophora gossypiella, pink bollworm; Anthonomus grandis, boll weevil; Aphis gossypii, cotton aphid; Pseudatomoscelis seriatus, cotton fleahopper; Trialeurodes abutilonea, bandedwinged whitefly; Lygus lineolaris, tarnished plant bug; Melanoplus femurrubrum, redlegged grasshopper; Melanoplus differentialis, differential grasshopper; Thrips tabaci, onion thrips; Franklinkiella fusca, tobacco thrips; Tetranychus cinnabarinus, carmine spider mite; Tetranychus urticae, twospotted spider mite; Rice: Diatraea saccharalis, sugarcane borer; Spodoptera frugiperda, fall armyworm; Helicoverpa zea, corn earworm; Colaspis brunnea, grape colaspis; Lissorhoptrus oryzophilus, rice water weevil; Sitophilus oryzae, rice weevil; Nephotettix nigropictus, rice leafhopper; Blissus leucopterus leucopterus, chinch bug; Acrosternum hilare, green stink bug; Soybean: Pseudoplusia includens, soybean looper; Anticarsia gemmatalis, velvetbean caterpillar; Plathypena scabra, green cloverworm; Ostrinia nubilalis, European corn borer; Agrotis ipsilon, black cutworm; Spodoptera exigua, beet armyworm; Heliothis virescens, cotton budworm; Helicoverpa zea, cotton bollworm; Epilachna varivestis, Mexican bean beetle; Myzus persicae, green peach aphid; Empoasca fabae, potato leafhopper; Acrosternum hilare, green stink bug; Melanoplus femurrubrum, redlegged grasshopper; Melanoplus differentialis, differential grasshopper; Hylemya platura, seedcorn maggot; Sericothrips variabilis, soybean thrips; Thrips tabaci, onion thrips; Tetranychus turkestani, strawberry spider mite; Tetranychus urticae, twospotted spider mite; Barley: Ostrinia nubilalis, European corn borer; Agrotis ipsilon, black cutworm; Schizaphis graminum, greenbug; Blissus leucopterus leucopterus, chinch bug; Acrosternum hilare, green stink bug; Euschistus servus, brown stink bug; Delia platura, seedcorn maggot; Mayetiola destructor, Hessian fly; Petrobia latens, brown wheat mite; Oil Seed Rape: Brevicoryne brassicae, cabbage aphid; Phyllotreta cruciferae, Flea beetle; Mamestra configurata, Bertha armyworm; Plutella xylostella, Diamond-back moth; Delia ssp., Root maggots.

[0103] Nematodes include parasitic nematodes such as root-knot, cyst, and lesion nematodes, including Heterodera spp., Meloidogyne spp., and Globodera spp.; particularly members of the cyst nematodes, including, but not limited to, Heterodera glycines (soybean cyst nematode); Heterodera schachtii (beet cyst nematode); Heterodera avenae (cereal cyst nematode); and Globodera rostochiensis and Globodera pailida (potato cyst nematodes). Lesion nematodes include Pratylenchus spp.

Methods for Increasing Plant Yield

[0104] Methods for increasing plant yield are provided. The methods comprise introducing into a plant or plant cell a polynucleotide comprising a pesticidal sequence disclosed herein. As defined herein, the "yield" of the plant refers to the quality and/or quantity of biomass produced by the plant. By "biomass" is intended any measured plant product. An increase in biomass production is any improvement in the yield of the measured plant product. Increasing plant yield has several commercial applications. For example, increasing plant leaf biomass may increase the yield of leafy vegetables for human or animal consumption. Additionally, increasing leaf biomass can be used to increase production of plant-derived pharmaceutical or industrial products. An increase in yield can comprise any statistically significant increase including, but not limited to, at least a 1% increase, at least a 3% increase, at least a 5% increase, at least a 10% increase, at least a 20% increase, at least a 30%, at least a 50%, at least a 70%, at least a 100% or a greater increase in yield compared to a plant not expressing the pesticidal sequence.

[0105] The following examples are offered by way of illustration and not by way of limitation.

EXPERIMENTAL

Example 1

Extraction of Plasmid DNA

[0106] Strains ATX14759, ATX14875, ATX13008, ATX13002, ATX9387, ATX13045, ATX21738, ATX14833, ATX1489, ATX15398 and ATX12972 were selected for analysis. Pure cultures of each strain were grown in large quantities of rich media. The cultures were centrifuged to harvest the cell pellet. The cell pellet was then prepared by treatment with SDS by methods known in the art, resulting in breakage of the cell wall and release of DNA. Proteins and large genomic DNA were then precipitated by a high salt concentration. The plasmid DNA was then precipitated with ethanol. In several instances, the plasmid DNA was separated from any remaining chromosomal DNA by high-speed centrifugation through a cesium chloride gradient. Alternatively, the plasmid DNA was purified by binding to a resin, as known in the art. For each strain, the quality of the DNA was checked by visualization on an agarose gel by methods known in the art.

Example 2

Cloning of Genes

[0107] DNA libraries were prepared from the plasmid DNA or each strain. This may be achieved in many ways as known in the art. For, example, the purified plasmid DNA can be sheared into 5-10 kb sized fragments and the 5' and 3' single stranded overhangs repaired using T4 DNA polymerase and Klenow fragment in the presence of all four dNTPs, as known in the art. Phosphates can then be attached to the 5' ends by treatment with T4 polynucleotide kinase, as known in the art. The repaired DNA fragments can then be ligated overnight into a standard high copy vector (i.e. pBLUESCRIPT.TM. SK+), suitably prepared to accept the inserts as known in the art (for example by digestion with a restriction enzyme producing blunt ends).

[0108] The quality of the resulting DNA libraries was analyzed by digesting a subset of clones with a restriction enzyme known to have a cleavage site flanking the cloning site.

[0109] A high percentage of clones were determined to contain inserts, ideally with an average insert size of 5-6 kb.

Example 3

High Throughput Sequencing of Library Plates

[0110] Once the DNA library quality was checked and confirmed, colonies were grown in a rich broth in 2 ml 96-well blocks overnight at 37.degree. C., typically at a shaking speed of 350 rpm. The blocks were centrifuged to harvest the cells to the bottom of the block. The blocks were then prepared by standard alkaline lysis prep in a high throughput format.

[0111] The end sequences of clones from this library were then determined for a large number of clones from each block in the following manner: The DNA sequence of each clone chosen for analysis was determined using the fluorescent dye terminator sequencing technique (Applied Biosystems), by methods known in the art using an automated DNA sequencing machine, and standard oligonucleotide primers that anneal to the plasmid vector in the region flanking the insert.

Example 4

Assembly and Screening of Sequencing Data

[0112] DNA sequences obtained were compiled into an assembly project and aligned together to form contigs. This can be done efficiently using a computer program, such as Vector NTI, or alternatively by using the Phred/Phrap suite of DNA alignment and analysis programs. These contigs, along with any individual read that may not have been added to a contig, were compared to a compiled database of all classes of known pesticidal genes. Contigs or individual reads identified as having identity to a known endotoxin or pesticidal gene were analyzed further.

Example 5

Axmi-037

[0113] From strain ATX1489, clone pAX2558 was found to contain an open reading frame with homology to "cry" type delta-endotoxins. This open reading frame was designated as axmi-037 (SEQ ID NO: 16). Inspection of the axmi-037 open reading frame suggests that more than one start codon may be present. The two predicted start codons are the ATG codon beginning at nucleotide position 1 of SEQ ID NO: 16, and a downstream ATG codon (represented by SEQ ID NO: 18). The ATG at nucleotide 77 of SEQ ID NO:16 has a ribosome binding site sequence (5'-G-G-A-G-G-3'), located at nucleotide positions 63-67 of SEQ ID NO: 16. Based on the presence of this strong ribosome binding consensus sequence immediately upstream of this second start site, and the homology of the two predicted proteins to other endotoxins, the translation product of the downstream start site is herein designated AXMI-037 (SEQ ID NO: 19). The longer translation product, beginning at the ATG at nucleotide position 1 of SEQ ID NO: 16, is designated AXMI-37-2 (and set forth in SEQ ID NO:17). pAX2558 was deposited with the ARS Patent Strain Collection on Jun. 15, 2006, and assigned NRRL B-30939. AXMI-37-2 exhibits 60% amino acid identity to the Cry7Aa1 endotoxin.

Example 6

Axmi-019

[0114] From strain ATX14875, a clone was found to contain an open reading frame with homology to MTX family toxins. This open reading frame was designated as axmi-019 (SEQ ID NO:10), and the encoded protein was designated AXMI-019 (SEQ ID NO:11). By searching of public databases of protein sequences, such as the GenPept database, the C-terminal region of AXMI-019 (starting at approximately amino acid 123 of SEQ ID NO: 11) was found to have low homology to a class of toxins including Bacillus thuringiensis serovar darmstadiensis Cry14-4 toxin (SEQ ID NO:42; encoded by GENBANK.RTM. ID AAV70918.1), and the Bacillus sphaericus MTX2 protein (SEQ ID NO:16, GENBANK.RTM. ID AAC44124.1).

Example 7

Axmi-011, axmi-012 and axmi-015

[0115] From strain ATX13008, three individual clones were found to contain open reading frames with homology to MTX-like toxins. These open reading frames were designated axmi-011 (SEQ ID NO:1), axmi-012 (SEQ ID NO:3), and axmi-015 (SEQ ID NO:8), and the encoded proteins are designated AXMI-011 (SEQ ID NO:2), AXMI-012 (SEQ ID NO:4), and AXMI-015 (SEQ ID NO:9), respectively. By searching of public databases of protein sequences, AXMI-011 was found to have low homology to a class of toxins including MTX2 (SEQ ID NO: 16); AXMI-015 was found to have low homology (about 35% amino acid identify over 178 amino acids) to a mosquitocidal toxin from Bacillus thuringiensis israelensis RBTH.sub.--02046 (SEQ ID NO:41, GENBANK.RTM. ID gi|75761628:1-79; AXMI-012 was found to have homology (29% over 217 amino acids) to a class of toxins including the p42 binary toxin of Bacillus sphaericus (SEQ ID NO:39; GENBANK.RTM. ID CAA73761).

[0116] Inspection of the axmi-011 coding region reveals the existence of an alternate translational start site 12 nucleotides upstream of the ATG start of axmi-011. This open reading frame contains a 5' extension of the following twelve nucleotides

TABLE-US-00002 (SEQ ID NO: 59) 5'-G-T-G-A-T-G-A-A-A-A-A-A-3'

immediately upstream and adjacent to the axmi-11 open reading frame. This open reading frame is herein designated as axmi-011(long) (SEQ ID NO:60). Translation of axmi-011 utilizing the putative GTG start would result in a modified AXMI-011 protein that contains an N-terminal extension of four amino acids (amino acid residues 1 through 4 of SEQ ID NO:61).

[0117] Analysis of the DNA context surrounding the two potential start sites reveals a sequence with a good match to the consensus for a ribosome binding site 5' G-T-G-A-T-G-3' (SEQ ID NO:62) positioned from -10 to -6 nt relative to the ATG start codon of SEQ ID NO: 1. This is a proper position for a bacterial ribosome binding site. No obvious homology to the consensus ribosome start site is observed in the position 15 nt upstream of the putative GTG start site. Thus, the protein initiated from the ATG start codon is designated AXMI-011 (SEQ ID NO:2). The protein encoded by translation initiated at the GTG start codon is designated AXMI-011(LONG) (SEQ ID NO:61).

Example 8

Axmi-032

[0118] From strain ATX9387, a plasmid was found to contain an open reading frame with homology to pesticidal toxins. This open reading frame was designated as axmi-032 (SEQ ID NO: 12), and the encoded protein was designated AXMI-032 (SEQ ID NO: 13). By searching of public databases of protein sequences, such as the GenPept database, AXMI-032 was found to have homology to a class of toxins including a presumed binary toxin from Bacillus thuringiensis (SEQ ID NO:43; GENBANK.RTM. Accession No. CAD30104.1) which is a possible two-domain toxin from Bacillus thuringiensis serovar israelensis.

Example 9

Axmi-013

[0119] From strain ATX13002, a clone was found to contain an open reading frame with homology to "cry" type delta-endotoxins. This open reading frame was designated as axmi-013 (SEQ ID NO:5), and the encoded protein was designated AXMI-013 (SEQ ID NO:6). By searching of public databases of protein sequences, the C-terminal region of AXMI-013 was found to have 52% identity with the MTX3 toxin (SEQ ID NO:40: GENBANK.RTM. ID AAB36661).

Example 10

Expression of AXMI-013 in Bacillus

[0120] The insecticidal AXMI-013 gene is amplified by PCR and cloned into the Bacillus expression vector pAX916 by methods well known in the art. The resulting clone is assayed for expression of AXMI-013 protein after transformation into cells of a cry(-) Bacillus thuringiensis strain. A Bacillus strain containing the axmi-013 clone and expressing the AXMI-013 insecticidal protein is grown in, for example, CYS media (10 g/l Bacto-casitone; 3 g/l yeast extract; 6 g/l KH.sub.2PO.sub.4; 14 g/l K.sub.2HPO.sub.4; 0.5 mM MgSO.sub.4; 0.05 mM MnCl.sub.2; 0.05 mM FeSO.sub.4), until sporulation is evident by microscopic examination. Samples are prepared, and analyzed by polyacrylamide gel electrophoresis (PAGE). AXMI-013 is tested for insecticidal activity in bioassays against important insect pests.

[0121] Inspection of the predicted amino acid sequence of AXMI-013 (SEQ ID NO:6) suggested that the N-terminus of the full-length AXMI-013 protein may comprise a signal peptide for secretion. The predicted site of cleavage was estimated to be between the alanine at position 27 and lysine at position 28 of SEQ ID NO:6. Similarly, MTX3 (SEQ ID NO:40) is predicted to possess a secretion signal peptide at its N-terminus (Liu, et al. (1996) Appl. Environ. Microbiol. 62:2174-2176).

[0122] The expressed AXMI-013 protein was excised from a polyacrylamide gel and subjected to N-terminal sequence analysis as known in the art. The N-terminal sequence identified by this analysis corresponded to a N-terminal truncation of the AXMI-013 protein, resulting in a truncated peptide with an N-terminus corresponding to the glutamine (Q) at amino acid position 40 of SEQ ID NO:6. This truncated protein is referred to herein as AXMI-013(Q), and the amino acid sequence of this protein is provided in SEQ ID NO:7. As known in the art, prediction of the exact site of cleavage is somewhat difficult. Nonetheless, the cleavage at approximately amino acid position 40 of SEQ ID NO:6 suggests that either (1) AXMI-013 is further processed after initial cleavage at amino acid positions 27/28, or AXMI-013 has a novel secretion signal. In order to confirm this, one skilled in the art may make gene fusion constructs utilizing (1) a heterologous protein and (2) using increasing length portions of AXMI-013. One can then test for secretion of the marker protein and determine the processing sites by N-terminal sequencing. Other methods to determine the extent of the signal sequence are known in the art.

Example 11

Axmi-023 and axmi-041

[0123] From strain ATX13045, a plasmid clone was found to contain an open reading frame with homology to "cry" type delta-endotoxins. This open reading frame was designated as axmi-023 (SEQ ID NO:30), and the encoded protein was designated AXMI-023 (SEQ ID NO:31). BLAST search of the non-redundant `nr` database demonstrates that AXMI-023 has low amino acid identity (less than 30% amino acid identity) with the VIP2 protein toxin, as well as several other presumed or known toxins. (GENBANK.RTM. Accession No. AAO86513.1, SEQ ID NO:55)

[0124] From strain ATX21738, a plasmid clone was found to contain an open reading frame with homology to "cry" type delta-endotoxins. This open reading frame was designated as axmi-041 (SEQ ID NO:32), and the encoded protein was designated AXMI-041 (SEQ ID NO:33). pAX4310 was deposited with the ARS Patent Strain Collection on Jun. 15, 2006, and assigned NRRL B-30943. AXMI-041 is 21% identical to AXMI-023, and similarly exhibits low amino acid identity (less than 30% amino acid identity) with the VIP2 protein toxin, as well as several other presumed or known toxins. A search of DNA and protein databases with the DNA sequences and amino acid sequences of AXMI-023 and AXMI-041 revealed that they are homologous to known pesticidal proteins. FIG. 4 shows an alignment of AXMI-023 with the Vip2 pesticidal protein (SEQ ID NO:55), and several related toxins. AXMI-041 also shows homology with this class of toxins.

Example 12

AXMI-022 Defines a Novel Class of Pesticidal Proteins

[0125] From strain ATX13045, a plasmid clone was found to contain an open reading frame with homology to known insect toxins. This open reading frame was designated as axmi-022 (SEQ ID NO:28), and the encoded protein was designated AXMI-022 (SEQ ID NO:29).

[0126] The amino acid sequence of AXMI-022 is 64.9% identical to Vip1A(b) (SEQ ID NO:52; see also U.S. Pat. No. 5,770,696, herein incorporated by reference in its entirety) throughout the length of Vip1A(b), and has significant amino acid identity with several other binary protein toxins. Further analysis of AXMI-022 revealed the following features of this polypeptide:

[0127] AXMI-022 is significantly longer than other binary proteins to which it shares homology, and encodes a peptide of 1,003 amino acids. For example, the Vip1A(b) protein is 834 amino acids in length;

[0128] Inspection of the DNA region surrounding the axmi-022 open reading frame shows no evidence for a second ORF encoding a toxin domain. The genes encoding binary toxins are typically physically closely linked. Most often, both the toxin and the receptor protein are organized as adjacent open reading frames, and are often transcriptionally linked in an operon.

[0129] The receptor binding region of AXMI-022 (from about amino acid 640 to about amino acid 770 of SEQ ID NO:29) is different from other binary toxins. The region of AXMI-022 corresponding to the region of binary proteins involved in receptor binding is quite different in AXMI-022 compared to other binary proteins. This is suggestive that AXMI-022 binds to a different receptor than other binary proteins

[0130] The C-terminal 133 amino acids of AXMI-022 (starting about amino acid 870 of SEQ ID NO:29) show amino acid homology to the Cry37Aa binary protein (SEQ ID NO:54; GENBANK.RTM. Accession No. AAF76376; U.S. Pat. No. 6,063,756, herein incorporated by reference in its entirety). This region has homology to Cry37Aa at a sequence identity of about 36%. Cry37Aa is in a different class of binary toxins than the Vip1-type toxins. Cry37Aa belongs to the Cry34 family, which forms a binary toxin with the Cry35 family. Cry34Ab1 is principally responsible for forming pores in lipid membranes, while Cry35Ab1 enhances the formation of pores (Masson, et al. (2004) Biochemistry 43:12349-57).

[0131] Thus, AXMI-022 appears to be a novel type of "single peptide" binary toxin, having homology to multiple classes of binary proteins, with a receptor-binding component from one class of binary toxins directly fused to a toxin component from a different class of binary toxins. This organization of domains has not been previously predicted in the art.

Example 13

Axmi-043

[0132] From strain ATX15398, pAX2597 was found to contain an open reading frame with homology to "cry" type delta-endotoxins. This open reading frame was designated as axmi-043. pAX2597 was deposited with the ARS Patent Strain Collection on Jun. 15, 2006, and assigned NRRL B-30941. Inspection of the axmi-043 open reading frame suggests that more than one start codon may be present. The ATG at position 46 of SEQ ID NO:20 has a ribosome binding site (5' G-G-A-G-A-3') (SEQ ID NO:63) starting at nucleotide 33 of SEQ ID NO:20. Based on the presence of this strong ribosome binding consensus sequence immediately upstream of this second start site, and the homology of the two predicted proteins to other endotoxins, we herein designate the translation product of the internal start site (represented by SEQ ID NO:22) as AXMI-043 (SEQ ID NO:23), and the longer protein as AXMI-043-2 (SEQ ID NO:21). AXMI-043 exhibits 93% amino acid identity to the AXMI-028 endotoxin, and AXMI-43-2 is 90% identical to AXMI-028 (SEQ ID NO:45 of this application, see also U.S. patent application Ser. No. 11/416,261, herein incorporated by reference in its entirety). AXMI-043 appears to be a "full-length endotoxin," and contains a C-terminal region (after the aspartic residue at position 629 of the AXMI-043 amino acid sequence) often referred to in the art as a non-toxic domain or a "crystal domain." AXMI-043 exhibits 54% amino acid identity with the Cry7Aa1 endotoxin (SEQ ID NO:46) throughout the full length of the protein.

Example 14

Axmi-44

[0133] From strain ATX14759, pAX2599 was found to contain an open reading frame with homology to "cry" type delta-endotoxins. This open reading frame was designated as axmi-044 (SEQ ID NO: 14), and the encoded protein was designated AXMI-044 (SEQ ID NO: 15). pAX2599 was deposited with the ARS Patent Strain Collection on Jun. 15, 2006, and assigned Accession No. NRRL B-30942. By searching of public databases of protein sequences, such as the GenPept database maintained by the NCBI (National Center for Biotechnology Information) AXMI-044 was found to have low homology to the cry-15Aa/cry33 family of toxins (SEQ ID NO:44, GENBANK.RTM. ID 8928022), and to MTX2 (SEQ ID NO:38).

Example 15

Axmi-033 and axmi-034

[0134] From strain ATX14833, a plasmid clone was found to contain two open reading frames with homology to insect toxins. The first open reading frame was designated as axmi-033 (SEQ ID NO:24), and the encoded protein was designated AXMI-033 (SEQ ID NO:25). AXMI-33 exhibits 61% amino acid identity to the 326 amino acid CryC35 insect toxin (SEQ ID NO:47, encoded by GENBANK.RTM. reference CAA63374). The second open reading frame was designated as axmi-034 (SEQ ID NO:26), and the encoded protein was designated AXMI-034 (SEQ ID NO:27). AXMI-34 exhibits 45% amino acid identity with the CryC53 endotoxin. (SEQ ID NO:48, encoded by GENBANK.RTM. reference CAA67205).

[0135] axmi-033 and axmi-034 appear to comprise an operon. The ATG start of axmi-034 is immediately 3' to, and in close proximity of (15 nucleotides immediately downstream of), the TAA stop codon of axmi-033. This organization is well known in the art to suggest that two genes comprise an operon. Thus, the AXMI-033 and AXMI-034 proteins are likely to be co-expressed in their native strain. It is likely that the activities of the two proteins expressed together may be synergistic and superior to the activity of the proteins expressed separately. pAX4341, a clone containing both axmi-033 and axmi-034 open reading frames, was deposited with the ARS Patent Strain Collection on May 29, 2007, and assigned accession number NRRL B-50047.

Example 16

Axmi-063 and axmi-064

[0136] From strain ATX12972, a plasmid clone was found to contain two open reading frames with homology to insect toxins. The first open reading frame was designated as axmi-063 (SEQ ID NO:34), and the encoded protein was designated AXMI-063 (SEQ ID NO:35). AXMI-63 exhibits 53.1% amino acid identity to the CryC35 insect toxin (SEQ ID NO:47, encoded by GENBANK.RTM. reference CAA63374). The second open reading frame was designated as axmi-064 (SEQ ID NO:36), and the encoded protein was designated AXMI-064 (SEQ ID NO:37). AXMI-64 exhibits 44.3% amino acid identity with the CryC53 endotoxin (SEQ ID NO:48, encoded by GENBANK.RTM. reference CAA67205).

[0137] axmi-063 and axmi-064 appear to comprise an operon. The ATG start of axmi-064 is immediately 3' to, and in close proximity of, the TAA stop codon of axmi-063. This is an organization well known in the art to suggest that two genes comprise an operon. Thus, the AXMI-063 and AXMI-064 proteins are likely to be co-expressed in their native strain. It is likely that the activities of the two proteins expressed together may be synergistic and superior to the activity of the proteins expressed separately. pAX5036, a clone containing both axmi-063 and axmi-064 open reading frames, was deposited with the ARS Patent Strain Collection on May 29, 2007, and assigned NRRL B-50048.

[0138] AXMI-033/AXMI-034 are similar to AXMI-063/AXMI-064. Analysis of the amino acid sequence of AXMI-033, AXMI-043, AXMI-063, and AXMI-064 reveals that AXMI-033 and AXMI-063 share significant amino acid identity, and are 69% identical. Similarly AXMI-034 and AXMI-064 share significant amino acid similarity (52% identical).

Example 17

Homology of AXMI-011, AXMI-012, AXMI-013, AXMI-015, AXMI-032, and AXMI-044 to Known Pesticidal Protein Genes

[0139] A search of protein databases with the amino acid sequences of the proteins of the invention reveal that they are homologous to known pesticidal proteins. Comparison of the amino acid sequences of the proteins of the invention to the non-redundant (nr) database maintained by the NCBI using the BLAST algorithm revealed the following proteins as having the strongest block of amino acid identity to the sequences of the invention (Table 2). Thus, the proteins of the invention are "pesticidal proteins."

TABLE-US-00003 TABLE 2 Amino Acid Identity of AXMI-011, AXMI-012, AXMI-013, AXMI-015, AXMI-032, and AXMI-044 to mosquito toxins in public databases % Identity in PROTEIN Highest Blast Hit (nr) block AXMI-011 MTX2 28% AXMI-012 P42 component of binary toxin 29% AXMI-013 MTX3 52% AXMI-015 RBTH_02046 35% AXMI-019 Cry14-4, MTX2 35%, 30% AXMI-032 GENBANK .RTM. ID CAD30104.1 19% AXMI-044 cry15Aa, MTX2 30%, 30%

Example 18

Additional Assays for Pesticidal Activity

[0140] The ability of a pesticidal protein to act as a pesticide upon a pest is often assessed in a number of ways. One way well known in the art is to perform a feeding assay. In such a feeding assay, one exposes the pest to a sample containing either compounds to be tested, or control samples. Often this is performed by placing the material to be tested, or a suitable dilution of such material, onto a material that the pest will ingest, such as an artificial diet. The material to be tested may be composed of a liquid, solid, or slurry. The material to be tested may be placed upon the surface and then allowed to dry. Alternatively, the material to be tested may be mixed with a molten artificial diet, then dispensed into the assay chamber. The assay chamber may be, for example, a cup, a dish, or a well of a microtiter plate.

[0141] Assays for sucking pests (for example aphids) may involve separating the test material from the insect by a partition, ideally a portion that can be pierced by the sucking mouth parts of the sucking insect, to allow ingestion of the test material. Often the test material is mixed with a feeding stimulant, such as sucrose, to promote ingestion of the test compound.

[0142] Other types of assays can include microinjection of the test material into the mouth, or gut of the pest, as well as development of transgenic plants, followed by test of the ability of the pest to feed upon the transgenic plant. Plant testing may involve isolation of the plant parts normally consumed, for example, small cages attached to a leaf, or isolation of entire plants in cages containing insects.

[0143] Other methods and approaches to assay pests are known in the art, and can be found, for example in Robertson and Preisler, eds. (1992) Pesticide bioassays with arthropods, CRC, Boca Raton, Fla. Alternatively, assays are commonly described in the journals Arthropod Management Tests and Journal of Economic Entomology or by discussion with members of the Entomological Society of America (ESA).

Example 19

Vectoring of Axmi Genes for Plant Expression

[0144] The coding regions of the invention are connected with appropriate promoter and terminator sequences for expression in plants. Such sequences are well known in the art and may include the rice actin promoter or maize ubiquitin promoter for expression in monocots, the Arabidopsis UBQ3 promoter or CaMV 35S promoter for expression in dicots, and the nos or PinII terminators. Techniques for producing and confirming promoter--gene--terminator constructs also are well known in the art.

[0145] In one aspect of the invention, synthetic DNA sequences are designed and generated. These synthetic sequences have altered nucleotide sequence relative to the parent sequence, but encode proteins that are essentially identical to the parent AXMI protein.

[0146] In another aspect of the invention, modified versions of the synthetic genes are designed such that the resulting peptide is targeted to a plant organelle, such as the endoplasmic reticulum or the apoplast. Peptide sequences known to result in targeting of fusion proteins to plant organelles are known in the art. For example, the N-terminal region of the acid phosphatase gene from the White Lupin Lupinus albus (GENEBANK.RTM. ID GI:14276838, Miller et al. (2001) Plant Physiology 127: 594-606) is known in the art to result in endoplasmic reticulum targeting of heterologous proteins. If the resulting fusion protein also contains an endoplasmic reticulum retention sequence comprising the peptide N-terminus-lysine-aspartic acid-glutamic acid-leucine (i.e., the "KDEL" motif (SEQ ID NO:58)) at the C-terminus, the fusion protein will be targeted to the endoplasmic reticulum. If the fusion protein lacks an endoplasmic reticulum targeting sequence at the C-terminus, the protein will be targeted to the endoplasmic reticulum, but will ultimately be sequestered in the apoplast.

[0147] Thus, this gene encodes a fusion protein that contains the N-terminal thirty-one amino acids of the acid phosphatase gene from the White Lupin Lupinus albus (GENBANK.RTM. ID GI: 14276838, Miller et al., 2001, supra) fused to the N-terminus of the AXMI sequence, as well as the KDEL sequence at the C-terminus. Thus, the resulting protein is predicted to be targeted the plant endoplasmic reticulum upon expression in a plant cell.

[0148] The plant expression cassettes described above are combined with an appropriate plant selectable marker to aid in the selection of transformed cells and tissues, and ligated into plant transformation vectors. These may include binary vectors from Agrobacterium-mediated transformation or simple plasmid vectors for aerosol or biolistic transformation.

Example 20

Vectoring of Axmi Genes for Plant Expression

[0149] The coding region DNA of the axmi genes of the invention are operably connected with appropriate promoter and terminator sequences for expression in plants. Such sequences are well known in the art and may include the rice actin promoter or maize ubiquitin promoter for expression in monocots, the Arabidopsis UBQ3 promoter or CaMV 35S promoter for expression in dicots, and the nos or PinII terminators. Techniques for producing and confirming promoter--gene--terminator constructs also are well known in the art.

[0150] The plant expression cassettes described above are combined with an appropriate plant selectable marker to aid in the selections of transformed cells and tissues, and ligated into plant transformation vectors. These may include binary vectors from Agrobacterium-mediated transformation or simple plasmid vectors for aerosol or biolistic transformation.

Example 21

Transformation of Maize Cells with the Pesticidal Protein Genes Described Herein

[0151] Maize ears are best collected 8-12 days after pollination. Embryos are isolated from the ears, and those embryos 0.8-1.5 mm in size are preferred for use in transformation. Embryos are plated scutellum side-up on a suitable incubation media, such as DN62A5S media (3.98 g/L N6 Salts; 1 mL/L (of 1000.times. Stock) N6 Vitamins; 800 mg/L L-Asparagine; 100 mg/L Myo-inositol; 1.4 g/L L-Proline; 100 mg/L Casamino acids; 50 g/L sucrose; 1 mL/L (of 1 mg/mL Stock) 2,4-D). However, media and salts other than DN62A5S are suitable and are known in the art. Embryos are incubated overnight at 25.degree. C. in the dark. However, it is not necessary per se to incubate the embryos overnight.

[0152] The resulting explants are transferred to mesh squares (30-40 per plate), transferred onto osmotic media for about 30-45 minutes, then transferred to a beaming plate (see, for example, PCT Publication No. WO/0138514 and U.S. Pat. No. 5,240,842).

[0153] DNA constructs designed to the genes of the invention in plant cells are accelerated into plant tissue using an aerosol beam accelerator, using conditions essentially as described in PCT Publication No. WO/0138514. After beaming, embryos are incubated for about 30 min on osmotic media, and placed onto incubation media overnight at 25.degree. C. in the dark. To avoid unduly damaging beamed explants, they are incubated for at least 24 hours prior to transfer to recovery media. Embryos are then spread onto recovery period media, for about 5 days, 25.degree. C. in the dark, then transferred to a selection media. Explants are incubated in selection media for up to eight weeks, depending on the nature and characteristics of the particular selection utilized. After the selection period, the resulting callus is transferred to embryo maturation media, until the formation of mature somatic embryos is observed. The resulting mature somatic embryos are then placed under low light, and the process of regeneration is initiated by methods known in the art. The resulting shoots are allowed to root on rooting media, and the resulting plants are transferred to nursery pots and propagated as transgenic plants.

TABLE-US-00004 Materials DN62A5S Media Components Per Liter Source Chu's N6 Basal Salt Mixture 3.98 g/L Phytotechnology Labs (Prod. No. C 416) Chu's N6 Vitamin Solution 1 mL/L Phytotechnology Labs (Prod. No. C 149) (of 1000x Stock) L-Asparagine 800 mg/L Phytotechnology Labs Myo-inositol 100 mg/L Sigma L-Proline 1.4 g/L Phytotechnology Labs Casamino acids 100 mg/L Fisher Scientific Sucrose 50 g/L Phytotechnology Labs 2,4-D (Prod. No. D-7299) 1 mL/L Sigma (of 1 mg/mL Stock)

[0154] The pH of the solution is adjusted to pH 5.8 with 1N KOH/1N KCl, Gelrite (Sigma) is added at a concentration up to 3 g/L, and the media is autoclaved. After cooling to 50.degree. C., 2 ml/L of a 5 mg/ml stock solution of silver nitrate (Phytotechnology Labs) is added.

Example 22

Transformation of the Pesticidal Genes of the Invention in Plant Cells by Agrobacterium-Mediated Transformation

[0155] Ears are best collected 8-12 days after pollination. Embryos are isolated from the ears, and those embryos 0.8-1.5 mm in size are preferred for use in transformation. Embryos are plated scutellum side-up on a suitable incubation media, and incubated overnight at 25.degree. C. in the dark. However, it is not necessary per se to incubate the embryos overnight. Embryos are contacted with an Agrobacterium strain containing the appropriate vectors for Ti plasmid mediated transfer for about 5-10 min, and then plated onto co-cultivation media for about 3 days (25.degree. C. in the dark). After co-cultivation, explants are transferred to recovery period media for about five days (at 25.degree. C. in the dark). Explants are incubated in selection media for up to eight weeks, depending on the nature and characteristics of the particular selection utilized. After the selection period, the resulting callus is transferred to embryo maturation media, until the formation of mature somatic embryos is observed. The resulting mature somatic embryos are then placed under low light, and the process of regeneration is initiated as known in the art.

Example 23

Soil Infestation of Plants Expressing a Gene of the Invention with Western Corn Rootworm

[0156] Transgenic plants containing an axmi gene of the invention under the control of a plant promoter are tested for resistance to infestation by Western corn rootworm (WCRW). Plantlets are transplanted from tissue culture media to root trainer (clamshell) pots known in the art to be useful for growth of plantlets in soil. Plants are grown for about 2 weeks in a greenhouse. Transgenic plants, as well as untransformed controls, are infested with approximately 1,000 WCRW eggs. WCRW eggs are preincubated such that eggs are at the point of hatching when infested onto the plants. Plants are held for about four weeks, or until controls exhibited obvious damage due to the rootworms. At this stage, plants are pulled from pots, roots are washed, and damage evaluated. Several independent events are examined for reduced damage from WCRW infestation relative to non-transformed control plants.

[0157] The resulting shoots are allowed to root on rooting media, and the resulting plants are transferred to nursery pots and propagated as transgenic plants.

[0158] All publications and patent applications mentioned in the specification are indicative of the level of skill of those skilled in the art to which this invention pertains. All publications and patent applications are herein incorporated by reference to the same extent as if each individual publication or patent application was specifically and individually indicated to be incorporated by reference.

[0159] Although the foregoing invention has been described in some detail by way of illustration and example for purposes of clarity of understanding, it will be obvious that certain changes and modifications may be practiced within the scope of the appended claims.

Sequence CWU 1

1

631957DNABacillus thuringiensisCDS(1)...(957) 1atg aat aaa aaa cct atg gta gcg ttg ata tta gcc act tcg att ggt 48Met Asn Lys Lys Pro Met Val Ala Leu Ile Leu Ala Thr Ser Ile Gly1 5 10 15ata cct tgt aca ttt aca cct gga agt gca tta gca gca gaa aat att 96Ile Pro Cys Thr Phe Thr Pro Gly Ser Ala Leu Ala Ala Glu Asn Ile 20 25 30cag act agt gtt aat gaa aat gta aaa gtt ggt att aca gat gtt caa 144Gln Thr Ser Val Asn Glu Asn Val Lys Val Gly Ile Thr Asp Val Gln 35 40 45tct gaa ttg aat aag ata gga gac tat tat tat agt aat aac tta gca 192Ser Glu Leu Asn Lys Ile Gly Asp Tyr Tyr Tyr Ser Asn Asn Leu Ala 50 55 60aat acg act ata aaa cct cct cat cat tgg gat tat aca ctt aaa aaa 240Asn Thr Thr Ile Lys Pro Pro His His Trp Asp Tyr Thr Leu Lys Lys65 70 75 80aat cct gat aaa gtt gga aca aat ttg gat ttt agt att act ggt act 288Asn Pro Asp Lys Val Gly Thr Asn Leu Asp Phe Ser Ile Thr Gly Thr 85 90 95gct agt aaa cta aat tat gat agt gta act cct ata tac att ggg cat 336Ala Ser Lys Leu Asn Tyr Asp Ser Val Thr Pro Ile Tyr Ile Gly His 100 105 110aat gaa ttt aat aat gat tca gat cag cct caa aaa ttt aca act tct 384Asn Glu Phe Asn Asn Asp Ser Asp Gln Pro Gln Lys Phe Thr Thr Ser 115 120 125aaa ttt act aaa gct gta aca gag gga aca aca agt acc gta aca aat 432Lys Phe Thr Lys Ala Val Thr Glu Gly Thr Thr Ser Thr Val Thr Asn 130 135 140gga ttt aga tta gga aat cca ggt tta aac tta ttt act att cca tta 480Gly Phe Arg Leu Gly Asn Pro Gly Leu Asn Leu Phe Thr Ile Pro Leu145 150 155 160att tta agt gat ggt atg aaa att aat gcg gaa ttt aac tct tct act 528Ile Leu Ser Asp Gly Met Lys Ile Asn Ala Glu Phe Asn Ser Ser Thr 165 170 175tca gaa tct caa caa aaa tcg gaa aca aaa aca ata gaa gca tca cct 576Ser Glu Ser Gln Gln Lys Ser Glu Thr Lys Thr Ile Glu Ala Ser Pro 180 185 190caa aac ata gaa gtt cca gca cat aaa aaa tat aaa gta gat gtt gta 624Gln Asn Ile Glu Val Pro Ala His Lys Lys Tyr Lys Val Asp Val Val 195 200 205ttg gaa caa aca agc tat tgg gca gat gtt aca ttt aca ggt gaa gga 672Leu Glu Gln Thr Ser Tyr Trp Ala Asp Val Thr Phe Thr Gly Glu Gly 210 215 220att aat ctt aat act act ata aat gca act gga ata cat act ggg cat 720Ile Asn Leu Asn Thr Thr Ile Asn Ala Thr Gly Ile His Thr Gly His225 230 235 240atg gga atg cag gag tca aga aaa ttt tct tgg aac aaa aat acc att 768Met Gly Met Gln Glu Ser Arg Lys Phe Ser Trp Asn Lys Asn Thr Ile 245 250 255gaa tta ttt aat gga cta aaa caa gag caa aaa aat aat ata cat ggg 816Glu Leu Phe Asn Gly Leu Lys Gln Glu Gln Lys Asn Asn Ile His Gly 260 265 270att aaa ttt agt aat ggg aaa atg aat gca aac gga aca ggt aaa gtt 864Ile Lys Phe Ser Asn Gly Lys Met Asn Ala Asn Gly Thr Gly Lys Val 275 280 285gaa ggt att ttt ggt agt aat cta gtt gta aag gta aat gat gtt aca 912Glu Gly Ile Phe Gly Ser Asn Leu Val Val Lys Val Asn Asp Val Thr 290 295 300gat cca tta aat cct atc cta gta atg act aaa agt tta aaa taa 957Asp Pro Leu Asn Pro Ile Leu Val Met Thr Lys Ser Leu Lys 305 310 3152318PRTBacillus thuringiensis 2Met Asn Lys Lys Pro Met Val Ala Leu Ile Leu Ala Thr Ser Ile Gly1 5 10 15 Ile Pro Cys Thr Phe Thr Pro Gly Ser Ala Leu Ala Ala Glu Asn Ile 20 25 30 Gln Thr Ser Val Asn Glu Asn Val Lys Val Gly Ile Thr Asp Val Gln 35 40 45 Ser Glu Leu Asn Lys Ile Gly Asp Tyr Tyr Tyr Ser Asn Asn Leu Ala 50 55 60 Asn Thr Thr Ile Lys Pro Pro His His Trp Asp Tyr Thr Leu Lys Lys65 70 75 80 Asn Pro Asp Lys Val Gly Thr Asn Leu Asp Phe Ser Ile Thr Gly Thr 85 90 95 Ala Ser Lys Leu Asn Tyr Asp Ser Val Thr Pro Ile Tyr Ile Gly His 100 105 110 Asn Glu Phe Asn Asn Asp Ser Asp Gln Pro Gln Lys Phe Thr Thr Ser 115 120 125 Lys Phe Thr Lys Ala Val Thr Glu Gly Thr Thr Ser Thr Val Thr Asn 130 135 140 Gly Phe Arg Leu Gly Asn Pro Gly Leu Asn Leu Phe Thr Ile Pro Leu145 150 155 160 Ile Leu Ser Asp Gly Met Lys Ile Asn Ala Glu Phe Asn Ser Ser Thr 165 170 175 Ser Glu Ser Gln Gln Lys Ser Glu Thr Lys Thr Ile Glu Ala Ser Pro 180 185 190 Gln Asn Ile Glu Val Pro Ala His Lys Lys Tyr Lys Val Asp Val Val 195 200 205 Leu Glu Gln Thr Ser Tyr Trp Ala Asp Val Thr Phe Thr Gly Glu Gly 210 215 220 Ile Asn Leu Asn Thr Thr Ile Asn Ala Thr Gly Ile His Thr Gly His225 230 235 240 Met Gly Met Gln Glu Ser Arg Lys Phe Ser Trp Asn Lys Asn Thr Ile 245 250 255 Glu Leu Phe Asn Gly Leu Lys Gln Glu Gln Lys Asn Asn Ile His Gly 260 265 270 Ile Lys Phe Ser Asn Gly Lys Met Asn Ala Asn Gly Thr Gly Lys Val 275 280 285 Glu Gly Ile Phe Gly Ser Asn Leu Val Val Lys Val Asn Asp Val Thr 290 295 300 Asp Pro Leu Asn Pro Ile Leu Val Met Thr Lys Ser Leu Lys305 310 315 3927DNABacillus thuringiensisCDS(1)...(927) 3atg att aat gta aac agt ggt aag gtt ata gat ata tca gga aat tca 48Met Ile Asn Val Asn Ser Gly Lys Val Ile Asp Ile Ser Gly Asn Ser1 5 10 15aca gca aat att caa caa tat gag tgg cgt ggt gat tta cca tct gaa 96Thr Ala Asn Ile Gln Gln Tyr Glu Trp Arg Gly Asp Leu Pro Ser Glu 20 25 30tat tgg tac ttt cat cgt gaa gcg gat ggg tat tat gtt att gaa tca 144Tyr Trp Tyr Phe His Arg Glu Ala Asp Gly Tyr Tyr Val Ile Glu Ser 35 40 45aaa ctt agt gga aag gta tta gac ata aaa gga aat tca aca gca aat 192Lys Leu Ser Gly Lys Val Leu Asp Ile Lys Gly Asn Ser Thr Ala Asn 50 55 60aat gca aat gtt cag caa tat caa ttt ata caa aat gca cct gct gaa 240Asn Ala Asn Val Gln Gln Tyr Gln Phe Ile Gln Asn Ala Pro Ala Glu65 70 75 80aga ttt gct gct gaa gaa gcg gga agc gtc tct ctc cca tca ata aat 288Arg Phe Ala Ala Glu Glu Ala Gly Ser Val Ser Leu Pro Ser Ile Asn 85 90 95acg aaa cca tta tca cca gta cca gaa tat aaa acg att aat gat caa 336Thr Lys Pro Leu Ser Pro Val Pro Glu Tyr Lys Thr Ile Asn Asp Gln 100 105 110ctt cca gaa gaa acg gaa cgt gta gta aca gct ttt aca ata gtt ccg 384Leu Pro Glu Glu Thr Glu Arg Val Val Thr Ala Phe Thr Ile Val Pro 115 120 125tgt atc tca gta aaa gat cca cat tat ggt gga gat act gct aaa caa 432Cys Ile Ser Val Lys Asp Pro His Tyr Gly Gly Asp Thr Ala Lys Gln 130 135 140ata aga gaa aat cct tat tac atg gtt gta aaa aaa caa tgg tgg aaa 480Ile Arg Glu Asn Pro Tyr Tyr Met Val Val Lys Lys Gln Trp Trp Lys145 150 155 160aaa caa gaa tct tat gtt tta gct cct agt gaa acg tat act ttt gaa 528Lys Gln Glu Ser Tyr Val Leu Ala Pro Ser Glu Thr Tyr Thr Phe Glu 165 170 175aca aaa act ggt ata aaa gta att gat caa gaa act gct aca agg aca 576Thr Lys Thr Gly Ile Lys Val Ile Asp Gln Glu Thr Ala Thr Arg Thr 180 185 190gta agt tgg agc att ggt gct gat atg gga ttt agt ttc aaa gga ttt 624Val Ser Trp Ser Ile Gly Ala Asp Met Gly Phe Ser Phe Lys Gly Phe 195 200 205tca tta gga atg tcc act caa tat tca aca caa tta cag act act ata 672Ser Leu Gly Met Ser Thr Gln Tyr Ser Thr Gln Leu Gln Thr Thr Ile 210 215 220agt cat aca act gaa caa tta aaa gaa gaa aca aac agg cac gaa ata 720Ser His Thr Thr Glu Gln Leu Lys Glu Glu Thr Asn Arg His Glu Ile225 230 235 240aag aat cca ttt tca gag aga atg gcg tat tct aga tat gta tta gcg 768Lys Asn Pro Phe Ser Glu Arg Met Ala Tyr Ser Arg Tyr Val Leu Ala 245 250 255aca gaa tat tct gtc caa aga aaa aat ggt aca atc gta aat tct cct 816Thr Glu Tyr Ser Val Gln Arg Lys Asn Gly Thr Ile Val Asn Ser Pro 260 265 270tgg act atg acc gat aag aca aaa gca cat gct gta act ttt cca aaa 864Trp Thr Met Thr Asp Lys Thr Lys Ala His Ala Val Thr Phe Pro Lys 275 280 285tcc aca gga aat gca tta gat gaa aat aca aag gaa cta tca aat agt 912Ser Thr Gly Asn Ala Leu Asp Glu Asn Thr Lys Glu Leu Ser Asn Ser 290 295 300gaa agt gta aac taa 927Glu Ser Val Asn 3054308PRTBacillus thuringiensis 4Met Ile Asn Val Asn Ser Gly Lys Val Ile Asp Ile Ser Gly Asn Ser1 5 10 15 Thr Ala Asn Ile Gln Gln Tyr Glu Trp Arg Gly Asp Leu Pro Ser Glu 20 25 30 Tyr Trp Tyr Phe His Arg Glu Ala Asp Gly Tyr Tyr Val Ile Glu Ser 35 40 45 Lys Leu Ser Gly Lys Val Leu Asp Ile Lys Gly Asn Ser Thr Ala Asn 50 55 60 Asn Ala Asn Val Gln Gln Tyr Gln Phe Ile Gln Asn Ala Pro Ala Glu65 70 75 80 Arg Phe Ala Ala Glu Glu Ala Gly Ser Val Ser Leu Pro Ser Ile Asn 85 90 95 Thr Lys Pro Leu Ser Pro Val Pro Glu Tyr Lys Thr Ile Asn Asp Gln 100 105 110 Leu Pro Glu Glu Thr Glu Arg Val Val Thr Ala Phe Thr Ile Val Pro 115 120 125 Cys Ile Ser Val Lys Asp Pro His Tyr Gly Gly Asp Thr Ala Lys Gln 130 135 140 Ile Arg Glu Asn Pro Tyr Tyr Met Val Val Lys Lys Gln Trp Trp Lys145 150 155 160 Lys Gln Glu Ser Tyr Val Leu Ala Pro Ser Glu Thr Tyr Thr Phe Glu 165 170 175 Thr Lys Thr Gly Ile Lys Val Ile Asp Gln Glu Thr Ala Thr Arg Thr 180 185 190 Val Ser Trp Ser Ile Gly Ala Asp Met Gly Phe Ser Phe Lys Gly Phe 195 200 205 Ser Leu Gly Met Ser Thr Gln Tyr Ser Thr Gln Leu Gln Thr Thr Ile 210 215 220 Ser His Thr Thr Glu Gln Leu Lys Glu Glu Thr Asn Arg His Glu Ile225 230 235 240 Lys Asn Pro Phe Ser Glu Arg Met Ala Tyr Ser Arg Tyr Val Leu Ala 245 250 255 Thr Glu Tyr Ser Val Gln Arg Lys Asn Gly Thr Ile Val Asn Ser Pro 260 265 270 Trp Thr Met Thr Asp Lys Thr Lys Ala His Ala Val Thr Phe Pro Lys 275 280 285 Ser Thr Gly Asn Ala Leu Asp Glu Asn Thr Lys Glu Leu Ser Asn Ser 290 295 300 Glu Ser Val Asn305 51017DNABacillus thuringiensisCDS(1)...(1017) 5atg gat aaa aaa ata aca aaa gca gcg tta agc atg ata atg ggt ata 48Met Asp Lys Lys Ile Thr Lys Ala Ala Leu Ser Met Ile Met Gly Ile1 5 10 15agt gtt tta tca tct cct tta gct gta gcc gca aaa aca gag aat aat 96Ser Val Leu Ser Ser Pro Leu Ala Val Ala Ala Lys Thr Glu Asn Asn 20 25 30aaa gaa caa cac gta att aca cag ttt aat cag aga gaa aat aag ttc 144Lys Glu Gln His Val Ile Thr Gln Phe Asn Gln Arg Glu Asn Lys Phe 35 40 45cct gat gta gga cag ggg att caa tgg tta tct caa ttt tat gga aaa 192Pro Asp Val Gly Gln Gly Ile Gln Trp Leu Ser Gln Phe Tyr Gly Lys 50 55 60tct tta agg aat aat ggt gaa gga tac tcc tta ggt cag gat gta atg 240Ser Leu Arg Asn Asn Gly Glu Gly Tyr Ser Leu Gly Gln Asp Val Met65 70 75 80agc tat ttt cta gaa gta aaa aat tct tat ggt caa ttg gca atg gaa 288Ser Tyr Phe Leu Glu Val Lys Asn Ser Tyr Gly Gln Leu Ala Met Glu 85 90 95cct caa gta ata agc act aca cct ctt tgg gct ggc caa agt gac ttg 336Pro Gln Val Ile Ser Thr Thr Pro Leu Trp Ala Gly Gln Ser Asp Leu 100 105 110gaa aat gca act gat gat gaa caa act tta aat tcc aca gaa ttt aaa 384Glu Asn Ala Thr Asp Asp Glu Gln Thr Leu Asn Ser Thr Glu Phe Lys 115 120 125aaa acg tat tct aat aca aca acc acc tct aca gaa aat gga ttt atg 432Lys Thr Tyr Ser Asn Thr Thr Thr Thr Ser Thr Glu Asn Gly Phe Met 130 135 140ata ggg cag gaa acc gaa ggg aaa gtt ggt ata ccc ttt gtc gca gaa 480Ile Gly Gln Glu Thr Glu Gly Lys Val Gly Ile Pro Phe Val Ala Glu145 150 155 160gga aaa gtc acc ata aaa act gaa tat aat ttt aat cat act aat ggg 528Gly Lys Val Thr Ile Lys Thr Glu Tyr Asn Phe Asn His Thr Asn Gly 165 170 175tat gaa aca tct gag agt gta gag tat att gct cct tct caa tct att 576Tyr Glu Thr Ser Glu Ser Val Glu Tyr Ile Ala Pro Ser Gln Ser Ile 180 185 190aag gta cca ccg cat act att gcc cga gtg aca gca tta tta gat gtg 624Lys Val Pro Pro His Thr Ile Ala Arg Val Thr Ala Leu Leu Asp Val 195 200 205aaa aaa att aaa ggg aag atg cat cta tat tca gaa att gga ctt aat 672Lys Lys Ile Lys Gly Lys Met His Leu Tyr Ser Glu Ile Gly Leu Asn 210 215 220aaa gat tat ggt tac gat atg gta cca ctt gtt tat aaa tat gga ggt 720Lys Asp Tyr Gly Tyr Asp Met Val Pro Leu Val Tyr Lys Tyr Gly Gly225 230 235 240cca ttt aaa tat gta acc tta ggt aca tta tat gac gag ggc tat aag 768Pro Phe Lys Tyr Val Thr Leu Gly Thr Leu Tyr Asp Glu Gly Tyr Lys 245 250 255cag gca aaa tta gat tat tct aat atg gga aat gtt ata ccg gaa gaa 816Gln Ala Lys Leu Asp Tyr Ser Asn Met Gly Asn Val Ile Pro Glu Glu 260 265 270att gag act gtt tcg aaa agt aac aat ccc aac cat tta tta gca agt 864Ile Glu Thr Val Ser Lys Ser Asn Asn Pro Asn His Leu Leu Ala Ser 275 280 285gga gta gga atc ttt gaa tca gaa tac gga agt gta ttt aat gtt aaa 912Gly Val Gly Ile Phe Glu Ser Glu Tyr Gly Ser Val Phe Asn Val Lys 290 295 300gtt gaa tat ata gat att aaa aat aaa aag att aaa aaa aca gag aat 960Val Glu Tyr Ile Asp Ile Lys Asn Lys Lys Ile Lys Lys Thr Glu Asn305 310 315 320ttc act atc gaa ccg aca ata gtc cct gtt gaa cag aag aat acg aat 1008Phe Thr Ile Glu Pro Thr Ile Val Pro Val Glu Gln Lys Asn Thr Asn 325 330 335aca aaa taa 1017Thr Lys 6338PRTBacillus thuringiensis 6Met Asp Lys Lys Ile Thr Lys Ala Ala Leu Ser Met Ile Met Gly Ile1 5 10 15 Ser Val Leu Ser Ser Pro Leu Ala Val Ala Ala Lys Thr Glu Asn Asn 20 25 30 Lys Glu Gln His Val Ile Thr Gln Phe Asn Gln Arg Glu Asn Lys Phe 35 40 45 Pro Asp Val Gly Gln Gly Ile Gln Trp Leu Ser Gln Phe Tyr Gly Lys 50 55 60 Ser Leu Arg Asn Asn Gly Glu Gly Tyr Ser Leu Gly Gln Asp Val Met65 70 75 80 Ser Tyr Phe Leu Glu Val Lys Asn Ser Tyr Gly Gln Leu Ala Met Glu 85 90 95 Pro Gln Val Ile Ser Thr Thr Pro Leu Trp Ala Gly Gln Ser Asp Leu 100 105 110 Glu Asn Ala Thr Asp Asp Glu Gln Thr Leu Asn Ser Thr Glu Phe Lys 115 120 125 Lys Thr Tyr Ser Asn Thr Thr Thr Thr Ser Thr Glu Asn Gly Phe Met 130 135 140 Ile Gly Gln Glu Thr Glu Gly Lys Val Gly Ile Pro Phe Val Ala Glu145 150 155 160 Gly Lys Val Thr Ile Lys Thr Glu Tyr Asn Phe Asn His Thr Asn Gly 165 170 175 Tyr Glu Thr Ser Glu Ser Val Glu Tyr Ile Ala Pro Ser Gln Ser Ile 180 185 190 Lys Val Pro Pro His Thr Ile Ala Arg

Val Thr Ala Leu Leu Asp Val 195 200 205 Lys Lys Ile Lys Gly Lys Met His Leu Tyr Ser Glu Ile Gly Leu Asn 210 215 220 Lys Asp Tyr Gly Tyr Asp Met Val Pro Leu Val Tyr Lys Tyr Gly Gly225 230 235 240 Pro Phe Lys Tyr Val Thr Leu Gly Thr Leu Tyr Asp Glu Gly Tyr Lys 245 250 255 Gln Ala Lys Leu Asp Tyr Ser Asn Met Gly Asn Val Ile Pro Glu Glu 260 265 270 Ile Glu Thr Val Ser Lys Ser Asn Asn Pro Asn His Leu Leu Ala Ser 275 280 285 Gly Val Gly Ile Phe Glu Ser Glu Tyr Gly Ser Val Phe Asn Val Lys 290 295 300 Val Glu Tyr Ile Asp Ile Lys Asn Lys Lys Ile Lys Lys Thr Glu Asn305 310 315 320 Phe Thr Ile Glu Pro Thr Ile Val Pro Val Glu Gln Lys Asn Thr Asn 325 330 335 Thr Lys7296PRTBacillus thuringiensis 7Gln Arg Glu Asn Lys Phe Pro Asp Val Gly Gln Gly Ile Gln Trp Leu1 5 10 15 Ser Gln Phe Tyr Gly Lys Ser Leu Arg Asn Asn Gly Glu Gly Tyr Ser 20 25 30 Leu Gly Gln Asp Val Met Ser Tyr Phe Leu Glu Val Lys Asn Ser Tyr 35 40 45 Gly Gln Leu Ala Met Glu Pro Gln Val Ile Ser Thr Thr Pro Leu Trp 50 55 60 Ala Gly Gln Ser Asp Leu Glu Asn Ala Thr Asp Asp Glu Gln Thr Leu65 70 75 80 Asn Ser Thr Glu Phe Lys Lys Thr Tyr Ser Asn Thr Thr Thr Thr Ser 85 90 95 Thr Glu Asn Gly Phe Met Ile Gly Gln Glu Thr Glu Gly Lys Val Gly 100 105 110 Ile Pro Phe Val Ala Glu Gly Lys Val Thr Ile Lys Thr Glu Tyr Asn 115 120 125 Phe Asn His Thr Asn Gly Tyr Glu Thr Ser Glu Ser Val Glu Tyr Ile 130 135 140 Ala Pro Ser Gln Ser Ile Lys Val Pro Pro His Thr Ile Ala Arg Val145 150 155 160 Thr Ala Leu Leu Asp Val Lys Lys Ile Lys Gly Lys Met His Leu Tyr 165 170 175 Ser Glu Ile Gly Leu Asn Lys Asp Tyr Gly Tyr Asp Met Val Pro Leu 180 185 190 Val Tyr Lys Tyr Gly Gly Pro Phe Lys Tyr Val Thr Leu Gly Thr Leu 195 200 205 Tyr Asp Glu Gly Tyr Lys Gln Ala Lys Leu Asp Tyr Ser Asn Met Gly 210 215 220 Asn Val Ile Pro Glu Glu Ile Glu Thr Val Ser Lys Ser Asn Asn Pro225 230 235 240 Asn His Leu Leu Ala Ser Gly Val Gly Ile Phe Glu Ser Glu Tyr Gly 245 250 255 Ser Val Phe Asn Val Lys Val Glu Tyr Ile Asp Ile Lys Asn Lys Lys 260 265 270 Ile Lys Lys Thr Glu Asn Phe Thr Ile Glu Pro Thr Ile Val Pro Val 275 280 285 Glu Gln Lys Asn Thr Asn Thr Lys 290 295 81422DNABacillus thuringiensisCDS(1)...(1422) 8atg gtt gat cgt aac ggc atg cca aca ata gat aga agc gga ttt act 48Met Val Asp Arg Asn Gly Met Pro Thr Ile Asp Arg Ser Gly Phe Thr1 5 10 15gtt aat cga act gtt aat tac aca aat aca aat tgg atg gct aat att 96Val Asn Arg Thr Val Asn Tyr Thr Asn Thr Asn Trp Met Ala Asn Ile 20 25 30gat aat tct cgt agg atc agt gaa tta tca att cca gga aca cat gga 144Asp Asn Ser Arg Arg Ile Ser Glu Leu Ser Ile Pro Gly Thr His Gly 35 40 45tca atg gca ctt cat ggt gga gtt gct gga act ata gga gat ata gct 192Ser Met Ala Leu His Gly Gly Val Ala Gly Thr Ile Gly Asp Ile Ala 50 55 60atc aat caa aca atg aac ctt gaa act caa tta aac tca gga atc cga 240Ile Asn Gln Thr Met Asn Leu Glu Thr Gln Leu Asn Ser Gly Ile Arg65 70 75 80tat att gat att cga tgt agg cat tat cat aat aat ttt gct atc cat 288Tyr Ile Asp Ile Arg Cys Arg His Tyr His Asn Asn Phe Ala Ile His 85 90 95cat gga cag ata tac cag cac gca ttt ttt ggt tct cat gtt tta gag 336His Gly Gln Ile Tyr Gln His Ala Phe Phe Gly Ser His Val Leu Glu 100 105 110ccc gtg ata aga ttt tta agg caa aat ccc agt gaa aca att tta atg 384Pro Val Ile Arg Phe Leu Arg Gln Asn Pro Ser Glu Thr Ile Leu Met 115 120 125cgt att caa caa gaa tac aat cca aca ggt aat aca aga act ttt gct 432Arg Ile Gln Gln Glu Tyr Asn Pro Thr Gly Asn Thr Arg Thr Phe Ala 130 135 140gaa act ttt gaa tcc ttc tgg act cca aat caa cgt tat ttt tgg tct 480Glu Thr Phe Glu Ser Phe Trp Thr Pro Asn Gln Arg Tyr Phe Trp Ser145 150 155 160cct act agt aat aat cca aca tta gga gac gtc cga gga aga att att 528Pro Thr Ser Asn Asn Pro Thr Leu Gly Asp Val Arg Gly Arg Ile Ile 165 170 175cta tta caa caa ttc ccc tct gat aga gga tgg ttt ggt att aat tgg 576Leu Leu Gln Gln Phe Pro Ser Asp Arg Gly Trp Phe Gly Ile Asn Trp 180 185 190ggc tcg tta gcc ata caa gat cag tgg gag gta gca ggt ctt aat ggc 624Gly Ser Leu Ala Ile Gln Asp Gln Trp Glu Val Ala Gly Leu Asn Gly 195 200 205ata tac aga aaa tgg ata gct att aaa aat cat ttt ttt aac aca ata 672Ile Tyr Arg Lys Trp Ile Ala Ile Lys Asn His Phe Phe Asn Thr Ile 210 215 220aat aat aga aat cga atc cat att aat cat tta agt gga act ggt ggt 720Asn Asn Arg Asn Arg Ile His Ile Asn His Leu Ser Gly Thr Gly Gly225 230 235 240ttc ggt gaa cca aga ccc tgg ttt tta gca agt ggc tat aat agt cga 768Phe Gly Glu Pro Arg Pro Trp Phe Leu Ala Ser Gly Tyr Asn Ser Arg 245 250 255aat gac aat agt atg tta agg tct gca tcg aga ggt cct agt gat gga 816Asn Asp Asn Ser Met Leu Arg Ser Ala Ser Arg Gly Pro Ser Asp Gly 260 265 270tgg cca gat ttc cca cgt cat agg ccc aca gga gat ata tat ttt gga 864Trp Pro Asp Phe Pro Arg His Arg Pro Thr Gly Asp Ile Tyr Phe Gly 275 280 285gga atg aat atc ctt gca act aga aga att cga gac cgt aga ttt act 912Gly Met Asn Ile Leu Ala Thr Arg Arg Ile Arg Asp Arg Arg Phe Thr 290 295 300cat aca gga att gtt gct gct gat ttc cct gga aga gga tta att gaa 960His Thr Gly Ile Val Ala Ala Asp Phe Pro Gly Arg Gly Leu Ile Glu305 310 315 320cgc aca att gcg tta aat ttc cct ata tca cca cct cac ttt cct ggt 1008Arg Thr Ile Ala Leu Asn Phe Pro Ile Ser Pro Pro His Phe Pro Gly 325 330 335tac tct caa att gtg aca gct tta aat agt agt agt gta att gat cta 1056Tyr Ser Gln Ile Val Thr Ala Leu Asn Ser Ser Ser Val Ile Asp Leu 340 345 350aat cct aat cgt aat gtc aca tta tgg tcg aat cat cga gga ctt aat 1104Asn Pro Asn Arg Asn Val Thr Leu Trp Ser Asn His Arg Gly Leu Asn 355 360 365caa agg tgg cgc att caa cat att tct gga aat tca tat tca ata ttg 1152Gln Arg Trp Arg Ile Gln His Ile Ser Gly Asn Ser Tyr Ser Ile Leu 370 375 380cca aat ctt cca gtt tta ggt tta cct tat gtt tta act ggg aat gtt 1200Pro Asn Leu Pro Val Leu Gly Leu Pro Tyr Val Leu Thr Gly Asn Val385 390 395 400tat aat ctt aat tct aat gta ttt ctt gct cga tct aac gga ttg cct 1248Tyr Asn Leu Asn Ser Asn Val Phe Leu Ala Arg Ser Asn Gly Leu Pro 405 410 415gag caa cag tgg ctt ctg gaa gaa ttt ttt gac ggt gac tat ata att 1296Glu Gln Gln Trp Leu Leu Glu Glu Phe Phe Asp Gly Asp Tyr Ile Ile 420 425 430aaa aat aga aga aat ccg aat ctg gtt tta gat gta tcc aga agc agc 1344Lys Asn Arg Arg Asn Pro Asn Leu Val Leu Asp Val Ser Arg Ser Ser 435 440 445act agt aat ggc tca ggt att att tta agt aca aga cac aat gga aat 1392Thr Ser Asn Gly Ser Gly Ile Ile Leu Ser Thr Arg His Asn Gly Asn 450 455 460aat caa aga ttt ttt atc aga cca ttt taa 1422Asn Gln Arg Phe Phe Ile Arg Pro Phe 465 4709473PRTBacillus thuringiensis 9Met Val Asp Arg Asn Gly Met Pro Thr Ile Asp Arg Ser Gly Phe Thr1 5 10 15 Val Asn Arg Thr Val Asn Tyr Thr Asn Thr Asn Trp Met Ala Asn Ile 20 25 30 Asp Asn Ser Arg Arg Ile Ser Glu Leu Ser Ile Pro Gly Thr His Gly 35 40 45 Ser Met Ala Leu His Gly Gly Val Ala Gly Thr Ile Gly Asp Ile Ala 50 55 60 Ile Asn Gln Thr Met Asn Leu Glu Thr Gln Leu Asn Ser Gly Ile Arg65 70 75 80 Tyr Ile Asp Ile Arg Cys Arg His Tyr His Asn Asn Phe Ala Ile His 85 90 95 His Gly Gln Ile Tyr Gln His Ala Phe Phe Gly Ser His Val Leu Glu 100 105 110 Pro Val Ile Arg Phe Leu Arg Gln Asn Pro Ser Glu Thr Ile Leu Met 115 120 125 Arg Ile Gln Gln Glu Tyr Asn Pro Thr Gly Asn Thr Arg Thr Phe Ala 130 135 140 Glu Thr Phe Glu Ser Phe Trp Thr Pro Asn Gln Arg Tyr Phe Trp Ser145 150 155 160 Pro Thr Ser Asn Asn Pro Thr Leu Gly Asp Val Arg Gly Arg Ile Ile 165 170 175 Leu Leu Gln Gln Phe Pro Ser Asp Arg Gly Trp Phe Gly Ile Asn Trp 180 185 190 Gly Ser Leu Ala Ile Gln Asp Gln Trp Glu Val Ala Gly Leu Asn Gly 195 200 205 Ile Tyr Arg Lys Trp Ile Ala Ile Lys Asn His Phe Phe Asn Thr Ile 210 215 220 Asn Asn Arg Asn Arg Ile His Ile Asn His Leu Ser Gly Thr Gly Gly225 230 235 240 Phe Gly Glu Pro Arg Pro Trp Phe Leu Ala Ser Gly Tyr Asn Ser Arg 245 250 255 Asn Asp Asn Ser Met Leu Arg Ser Ala Ser Arg Gly Pro Ser Asp Gly 260 265 270 Trp Pro Asp Phe Pro Arg His Arg Pro Thr Gly Asp Ile Tyr Phe Gly 275 280 285 Gly Met Asn Ile Leu Ala Thr Arg Arg Ile Arg Asp Arg Arg Phe Thr 290 295 300 His Thr Gly Ile Val Ala Ala Asp Phe Pro Gly Arg Gly Leu Ile Glu305 310 315 320 Arg Thr Ile Ala Leu Asn Phe Pro Ile Ser Pro Pro His Phe Pro Gly 325 330 335 Tyr Ser Gln Ile Val Thr Ala Leu Asn Ser Ser Ser Val Ile Asp Leu 340 345 350 Asn Pro Asn Arg Asn Val Thr Leu Trp Ser Asn His Arg Gly Leu Asn 355 360 365 Gln Arg Trp Arg Ile Gln His Ile Ser Gly Asn Ser Tyr Ser Ile Leu 370 375 380 Pro Asn Leu Pro Val Leu Gly Leu Pro Tyr Val Leu Thr Gly Asn Val385 390 395 400 Tyr Asn Leu Asn Ser Asn Val Phe Leu Ala Arg Ser Asn Gly Leu Pro 405 410 415 Glu Gln Gln Trp Leu Leu Glu Glu Phe Phe Asp Gly Asp Tyr Ile Ile 420 425 430 Lys Asn Arg Arg Asn Pro Asn Leu Val Leu Asp Val Ser Arg Ser Ser 435 440 445 Thr Ser Asn Gly Ser Gly Ile Ile Leu Ser Thr Arg His Asn Gly Asn 450 455 460 Asn Gln Arg Phe Phe Ile Arg Pro Phe465 470 101053DNABacillus thuringiensisCDS(1)...(1053) 10atg aaa tct tat aaa aaa ata tta cta gtt gcc cca tta gca tgt acc 48Met Lys Ser Tyr Lys Lys Ile Leu Leu Val Ala Pro Leu Ala Cys Thr1 5 10 15tta gca acg gga gtt ttt aca aca cct cat gca gca ttt gca gca tct 96Leu Ala Thr Gly Val Phe Thr Thr Pro His Ala Ala Phe Ala Ala Ser 20 25 30tca gtg ggc atg cag gcg aat gca aag gat act ctt gca ttt aat gat 144Ser Val Gly Met Gln Ala Asn Ala Lys Asp Thr Leu Ala Phe Asn Asp 35 40 45caa caa tta aaa aaa gat tta tca gat cga cta aca tct gcc gtg aga 192Gln Gln Leu Lys Lys Asp Leu Ser Asp Arg Leu Thr Ser Ala Val Arg 50 55 60aat agg cca gat tta ttt ggg ata acc aca cca gtc ctc gtt aat aac 240Asn Arg Pro Asp Leu Phe Gly Ile Thr Thr Pro Val Leu Val Asn Asn65 70 75 80att aaa aac atg aat ttc aaa tta aca gat atg aac gcg act tat ggg 288Ile Lys Asn Met Asn Phe Lys Leu Thr Asp Met Asn Ala Thr Tyr Gly 85 90 95tat aca aat aat gga aca att caa acg gat gcg aag gtg gat cat tat 336Tyr Thr Asn Asn Gly Thr Ile Gln Thr Asp Ala Lys Val Asp His Tyr 100 105 110ggt gat ggg gga caa gtg gag tta tta agc tat cgg aat gat acc tct 384Gly Asp Gly Gly Gln Val Glu Leu Leu Ser Tyr Arg Asn Asp Thr Ser 115 120 125gtg aat caa act ttc aat acc cca gaa aaa agc tta aaa aca tca gaa 432Val Asn Gln Thr Phe Asn Thr Pro Glu Lys Ser Leu Lys Thr Ser Glu 130 135 140agt ttt acc tat tca aat cag gaa ggg gta aaa ttg ggg gta gcc tcg 480Ser Phe Thr Tyr Ser Asn Gln Glu Gly Val Lys Leu Gly Val Ala Ser145 150 155 160gaa act aaa gtc ggt gta gat att ccc ttt ata ggt ggg gct gac gaa 528Glu Thr Lys Val Gly Val Asp Ile Pro Phe Ile Gly Gly Ala Asp Glu 165 170 175acg att aag att tcc agc gag ttt tct tat aac cat act agt tca aat 576Thr Ile Lys Ile Ser Ser Glu Phe Ser Tyr Asn His Thr Ser Ser Asn 180 185 190act agc aca aaa gaa gaa acg act aca ttt aaa tca caa ccg gtt att 624Thr Ser Thr Lys Glu Glu Thr Thr Thr Phe Lys Ser Gln Pro Val Ile 195 200 205tgt gta gca gga tat aca aca caa ttt tca gga agc gta caa aat gct 672Cys Val Ala Gly Tyr Thr Thr Gln Phe Ser Gly Ser Val Gln Asn Ala 210 215 220gtc ttt tct ggg tca ttt agt ggc act gca gaa gcg tca ggt gat gtg 720Val Phe Ser Gly Ser Phe Ser Gly Thr Ala Glu Ala Ser Gly Asp Val225 230 235 240aaa ttc caa gaa gtg aac gag ttg ttc cgt gta gat acg tct tta ggt 768Lys Phe Gln Glu Val Asn Glu Leu Phe Arg Val Asp Thr Ser Leu Gly 245 250 255gac aat cca aat att aaa gga cac gca tta tac aat gtc ttt aaa tat 816Asp Asn Pro Asn Ile Lys Gly His Ala Leu Tyr Asn Val Phe Lys Tyr 260 265 270tcg ggc atg cct gtt cca tca tat gta aaa tta gat gat acg aat aaa 864Ser Gly Met Pro Val Pro Ser Tyr Val Lys Leu Asp Asp Thr Asn Lys 275 280 285aga gct tta att gaa aat gtg aca tcc acg tat agt gga gtt ggt ggt 912Arg Ala Leu Ile Glu Asn Val Thr Ser Thr Tyr Ser Gly Val Gly Gly 290 295 300cat tat tca cgc gta gaa gtt aaa gtg ttc cca aat acg cgt agt aat 960His Tyr Ser Arg Val Glu Val Lys Val Phe Pro Asn Thr Arg Ser Asn305 310 315 320gaa gat gca atc aca ata cca tat gca aaa tat atg caa aaa gta aaa 1008Glu Asp Ala Ile Thr Ile Pro Tyr Ala Lys Tyr Met Gln Lys Val Lys 325 330 335gat ggt aca cta cag aaa gaa tta gaa cag cat tat aaa aaa gct 1053Asp Gly Thr Leu Gln Lys Glu Leu Glu Gln His Tyr Lys Lys Ala 340 345 35011351PRTBacillus thuringiensis 11Met Lys Ser Tyr Lys Lys Ile Leu Leu Val Ala Pro Leu Ala Cys Thr1 5 10 15 Leu Ala Thr Gly Val Phe Thr Thr Pro His Ala Ala Phe Ala Ala Ser 20 25 30 Ser Val Gly Met Gln Ala Asn Ala Lys Asp Thr Leu Ala Phe Asn Asp 35 40 45 Gln Gln Leu Lys Lys Asp Leu Ser Asp Arg Leu Thr Ser Ala Val Arg 50 55 60 Asn Arg Pro Asp Leu Phe Gly Ile Thr Thr Pro Val Leu Val Asn Asn65 70 75 80 Ile Lys Asn Met Asn Phe Lys Leu Thr Asp Met Asn Ala Thr Tyr Gly 85 90 95 Tyr Thr Asn Asn Gly Thr Ile Gln Thr Asp Ala Lys Val Asp His Tyr 100 105 110 Gly Asp Gly Gly Gln Val Glu Leu Leu Ser Tyr Arg Asn Asp Thr Ser 115 120 125 Val Asn Gln Thr Phe Asn Thr Pro Glu Lys Ser Leu Lys Thr

Ser Glu 130 135 140 Ser Phe Thr Tyr Ser Asn Gln Glu Gly Val Lys Leu Gly Val Ala Ser145 150 155 160 Glu Thr Lys Val Gly Val Asp Ile Pro Phe Ile Gly Gly Ala Asp Glu 165 170 175 Thr Ile Lys Ile Ser Ser Glu Phe Ser Tyr Asn His Thr Ser Ser Asn 180 185 190 Thr Ser Thr Lys Glu Glu Thr Thr Thr Phe Lys Ser Gln Pro Val Ile 195 200 205 Cys Val Ala Gly Tyr Thr Thr Gln Phe Ser Gly Ser Val Gln Asn Ala 210 215 220 Val Phe Ser Gly Ser Phe Ser Gly Thr Ala Glu Ala Ser Gly Asp Val225 230 235 240 Lys Phe Gln Glu Val Asn Glu Leu Phe Arg Val Asp Thr Ser Leu Gly 245 250 255 Asp Asn Pro Asn Ile Lys Gly His Ala Leu Tyr Asn Val Phe Lys Tyr 260 265 270 Ser Gly Met Pro Val Pro Ser Tyr Val Lys Leu Asp Asp Thr Asn Lys 275 280 285 Arg Ala Leu Ile Glu Asn Val Thr Ser Thr Tyr Ser Gly Val Gly Gly 290 295 300 His Tyr Ser Arg Val Glu Val Lys Val Phe Pro Asn Thr Arg Ser Asn305 310 315 320 Glu Asp Ala Ile Thr Ile Pro Tyr Ala Lys Tyr Met Gln Lys Val Lys 325 330 335 Asp Gly Thr Leu Gln Lys Glu Leu Glu Gln His Tyr Lys Lys Ala 340 345 350 121062DNAUnknownCDS(1)...(1062)Isolated from soil sample 12atg tca gga ttt gaa gaa tta ttt tac cca gat aat acc aac cgt aga 48Met Ser Gly Phe Glu Glu Leu Phe Tyr Pro Asp Asn Thr Asn Arg Arg1 5 10 15agc aga gta gaa caa tta atg gct caa tgt aca gat tta act aac caa 96Ser Arg Val Glu Gln Leu Met Ala Gln Cys Thr Asp Leu Thr Asn Gln 20 25 30att aag aat gat aga aaa gac att gat gac ctt ttt cga aat aat gat 144Ile Lys Asn Asp Arg Lys Asp Ile Asp Asp Leu Phe Arg Asn Asn Asp 35 40 45cca att atc aaa gaa aag ctt aaa ggt aag cta ata tta agc att cct 192Pro Ile Ile Lys Glu Lys Leu Lys Gly Lys Leu Ile Leu Ser Ile Pro 50 55 60aat aaa tat ttt gat ata tcc aaa aat tcc ata gat gat att tta aat 240Asn Lys Tyr Phe Asp Ile Ser Lys Asn Ser Ile Asp Asp Ile Leu Asn65 70 75 80tat gct tta ggt cca gtt cct gct gct att gta ggg gct gat aat aga 288Tyr Ala Leu Gly Pro Val Pro Ala Ala Ile Val Gly Ala Asp Asn Arg 85 90 95aca tta tat caa aaa ata att aaa gaa ttg gtg aaa att cgt att gag 336Thr Leu Tyr Gln Lys Ile Ile Lys Glu Leu Val Lys Ile Arg Ile Glu 100 105 110tta aag tat ata gaa tta aag act att tat gat aaa atg gtt att agt 384Leu Lys Tyr Ile Glu Leu Lys Thr Ile Tyr Asp Lys Met Val Ile Ser 115 120 125gcc gtt ata aaa gag att act cgg att aaa aaa aca gcc caa aaa cat 432Ala Val Ile Lys Glu Ile Thr Arg Ile Lys Lys Thr Ala Gln Lys His 130 135 140aac tgg act aat gaa ata cta gca gaa att act cag gaa atc att gaa 480Asn Trp Thr Asn Glu Ile Leu Ala Glu Ile Thr Gln Glu Ile Ile Glu145 150 155 160aac act att gaa acg ata gaa aca att aat gta gaa cct tct aga gaa 528Asn Thr Ile Glu Thr Ile Glu Thr Ile Asn Val Glu Pro Ser Arg Glu 165 170 175tta gct gta gat aaa tta caa gaa att gat gaa aat ctt gca gct tgg 576Leu Ala Val Asp Lys Leu Gln Glu Ile Asp Glu Asn Leu Ala Ala Trp 180 185 190atc aat gaa gat cca tct aat caa aaa att act atg gaa ttg aat gca 624Ile Asn Glu Asp Pro Ser Asn Gln Lys Ile Thr Met Glu Leu Asn Ala 195 200 205tta gat gaa gta tat aaa gtt att tcg cct tta aat aat aaa agc gtg 672Leu Asp Glu Val Tyr Lys Val Ile Ser Pro Leu Asn Asn Lys Ser Val 210 215 220tta gat ttt tct cgc tca aat aat aat gcg att tta tgg gat gac cat 720Leu Asp Phe Ser Arg Ser Asn Asn Asn Ala Ile Leu Trp Asp Asp His225 230 235 240gat ggt gaa aat caa aaa tgg aaa ttt gaa tac aat gca aag cac aca 768Asp Gly Glu Asn Gln Lys Trp Lys Phe Glu Tyr Asn Ala Lys His Thr 245 250 255gca tac caa att aaa agt ctg gta aat aaa gac ttt gtt tta gca tgg 816Ala Tyr Gln Ile Lys Ser Leu Val Asn Lys Asp Phe Val Leu Ala Trp 260 265 270gat gac ggt aat aaa tta aag aat gtg ttt gtt aca aaa aat caa tac 864Asp Asp Gly Asn Lys Leu Lys Asn Val Phe Val Thr Lys Asn Gln Tyr 275 280 285aaa gaa gaa cat ttt tgg att tta gaa aag aca gaa gat gac aat tat 912Lys Glu Glu His Phe Trp Ile Leu Glu Lys Thr Glu Asp Asp Asn Tyr 290 295 300att ata aaa aat aaa aaa tcc cta att tta ata tta gag gtc gat agg 960Ile Ile Lys Asn Lys Lys Ser Leu Ile Leu Ile Leu Glu Val Asp Arg305 310 315 320gct caa act aat aat gga gca aac att aaa tta aat gaa caa aac cgt 1008Ala Gln Thr Asn Asn Gly Ala Asn Ile Lys Leu Asn Glu Gln Asn Arg 325 330 335ata gat aaa cgg tta att aat gct caa aaa ttc aaa tta gca aag tgt 1056Ile Asp Lys Arg Leu Ile Asn Ala Gln Lys Phe Lys Leu Ala Lys Cys 340 345 350tat taa 1062Tyr 13353PRTUnknownIsolated from soil sample 13Met Ser Gly Phe Glu Glu Leu Phe Tyr Pro Asp Asn Thr Asn Arg Arg1 5 10 15 Ser Arg Val Glu Gln Leu Met Ala Gln Cys Thr Asp Leu Thr Asn Gln 20 25 30 Ile Lys Asn Asp Arg Lys Asp Ile Asp Asp Leu Phe Arg Asn Asn Asp 35 40 45 Pro Ile Ile Lys Glu Lys Leu Lys Gly Lys Leu Ile Leu Ser Ile Pro 50 55 60 Asn Lys Tyr Phe Asp Ile Ser Lys Asn Ser Ile Asp Asp Ile Leu Asn65 70 75 80 Tyr Ala Leu Gly Pro Val Pro Ala Ala Ile Val Gly Ala Asp Asn Arg 85 90 95 Thr Leu Tyr Gln Lys Ile Ile Lys Glu Leu Val Lys Ile Arg Ile Glu 100 105 110 Leu Lys Tyr Ile Glu Leu Lys Thr Ile Tyr Asp Lys Met Val Ile Ser 115 120 125 Ala Val Ile Lys Glu Ile Thr Arg Ile Lys Lys Thr Ala Gln Lys His 130 135 140 Asn Trp Thr Asn Glu Ile Leu Ala Glu Ile Thr Gln Glu Ile Ile Glu145 150 155 160 Asn Thr Ile Glu Thr Ile Glu Thr Ile Asn Val Glu Pro Ser Arg Glu 165 170 175 Leu Ala Val Asp Lys Leu Gln Glu Ile Asp Glu Asn Leu Ala Ala Trp 180 185 190 Ile Asn Glu Asp Pro Ser Asn Gln Lys Ile Thr Met Glu Leu Asn Ala 195 200 205 Leu Asp Glu Val Tyr Lys Val Ile Ser Pro Leu Asn Asn Lys Ser Val 210 215 220 Leu Asp Phe Ser Arg Ser Asn Asn Asn Ala Ile Leu Trp Asp Asp His225 230 235 240 Asp Gly Glu Asn Gln Lys Trp Lys Phe Glu Tyr Asn Ala Lys His Thr 245 250 255 Ala Tyr Gln Ile Lys Ser Leu Val Asn Lys Asp Phe Val Leu Ala Trp 260 265 270 Asp Asp Gly Asn Lys Leu Lys Asn Val Phe Val Thr Lys Asn Gln Tyr 275 280 285 Lys Glu Glu His Phe Trp Ile Leu Glu Lys Thr Glu Asp Asp Asn Tyr 290 295 300 Ile Ile Lys Asn Lys Lys Ser Leu Ile Leu Ile Leu Glu Val Asp Arg305 310 315 320 Ala Gln Thr Asn Asn Gly Ala Asn Ile Lys Leu Asn Glu Gln Asn Arg 325 330 335 Ile Asp Lys Arg Leu Ile Asn Ala Gln Lys Phe Lys Leu Ala Lys Cys 340 345 350 Tyr14942DNABacillus thuringiensisCDS(1)...(942) 14atg aaa aaa ata gga ttc gtt agt ggc atg aca tct tta gct att tta 48Met Lys Lys Ile Gly Phe Val Ser Gly Met Thr Ser Leu Ala Ile Leu1 5 10 15gct agt gct ttt gga gga gaa atc aaa cct gca tct gcg agc act tct 96Ala Ser Ala Phe Gly Gly Glu Ile Lys Pro Ala Ser Ala Ser Thr Ser 20 25 30gct tta tcc caa caa tct act ctt cat tct aca caa caa gct gtt cag 144Ala Leu Ser Gln Gln Ser Thr Leu His Ser Thr Gln Gln Ala Val Gln 35 40 45aaa cat aat ttt gat gca atc gtt aat gag atc att cat gca tgg att 192Lys His Asn Phe Asp Ala Ile Val Asn Glu Ile Ile His Ala Trp Ile 50 55 60aaa aaa aat aat cct ggt gga cat tat cca ttt att gat agt aaa aat 240Lys Lys Asn Asn Pro Gly Gly His Tyr Pro Phe Ile Asp Ser Lys Asn65 70 75 80atc tca caa att aaa gaa tcc cgt tta aac att ggt gct cct aaa cga 288Ile Ser Gln Ile Lys Glu Ser Arg Leu Asn Ile Gly Ala Pro Lys Arg 85 90 95att gga aat att gaa aat cga aca tta gtt aca act att cct tct aga 336Ile Gly Asn Ile Glu Asn Arg Thr Leu Val Thr Thr Ile Pro Ser Arg 100 105 110att tac aat aat aca aat gca tct gta tta aaa cca gca act tca acc 384Ile Tyr Asn Asn Thr Asn Ala Ser Val Leu Lys Pro Ala Thr Ser Thr 115 120 125gaa tta aaa aca agt cac agt agc tct ttt act aat tta aca gaa atc 432Glu Leu Lys Thr Ser His Ser Ser Ser Phe Thr Asn Leu Thr Glu Ile 130 135 140aca cat aca ggt ggc atc aca aca aaa gcg gaa gtg aaa ttt aaa cca 480Thr His Thr Gly Gly Ile Thr Thr Lys Ala Glu Val Lys Phe Lys Pro145 150 155 160aaa ggc ctt gtt gca gat ggt gaa gtt tct aca ggt cta gaa tta aaa 528Lys Gly Leu Val Ala Asp Gly Glu Val Ser Thr Gly Leu Glu Leu Lys 165 170 175tat gaa tat agt aat aca cag gga acc aat caa acc caa aca aca acc 576Tyr Glu Tyr Ser Asn Thr Gln Gly Thr Asn Gln Thr Gln Thr Thr Thr 180 185 190aat gaa tta agt ttt aaa gtc gat aca cct gtt gaa gtt cct cca cgg 624Asn Glu Leu Ser Phe Lys Val Asp Thr Pro Val Glu Val Pro Pro Arg 195 200 205tca tct ata gaa gta ata aca aat att tat aaa gac aaa gta aga tat 672Ser Ser Ile Glu Val Ile Thr Asn Ile Tyr Lys Asp Lys Val Arg Tyr 210 215 220gaa tat aca gga tat agt gaa ttc aca ggt gaa gtc aca ttc caa tat 720Glu Tyr Thr Gly Tyr Ser Glu Phe Thr Gly Glu Val Thr Phe Gln Tyr225 230 235 240aga ttg aat gca tct gac aca cca aaa aca gta aca aga gaa att ggt 768Arg Leu Asn Ala Ser Asp Thr Pro Lys Thr Val Thr Arg Glu Ile Gly 245 250 255acc atg atg tat gaa ata gat gat gaa acg tac aat aaa tta gct gac 816Thr Met Met Tyr Glu Ile Asp Asp Glu Thr Tyr Asn Lys Leu Ala Asp 260 265 270aga gga att aca gta aaa ggc gca gta gat tct cca gat gtc tta cgt 864Arg Gly Ile Thr Val Lys Gly Ala Val Asp Ser Pro Asp Val Leu Arg 275 280 285att aaa gga aca gct att ttg gat gta gat gag gca tat agc acg gaa 912Ile Lys Gly Thr Ala Ile Leu Asp Val Asp Glu Ala Tyr Ser Thr Glu 290 295 300gta att gca aga gat att gca cct att cag 942Val Ile Ala Arg Asp Ile Ala Pro Ile Gln305 31015314PRTBacillus thuringiensis 15Met Lys Lys Ile Gly Phe Val Ser Gly Met Thr Ser Leu Ala Ile Leu1 5 10 15 Ala Ser Ala Phe Gly Gly Glu Ile Lys Pro Ala Ser Ala Ser Thr Ser 20 25 30 Ala Leu Ser Gln Gln Ser Thr Leu His Ser Thr Gln Gln Ala Val Gln 35 40 45 Lys His Asn Phe Asp Ala Ile Val Asn Glu Ile Ile His Ala Trp Ile 50 55 60 Lys Lys Asn Asn Pro Gly Gly His Tyr Pro Phe Ile Asp Ser Lys Asn65 70 75 80 Ile Ser Gln Ile Lys Glu Ser Arg Leu Asn Ile Gly Ala Pro Lys Arg 85 90 95 Ile Gly Asn Ile Glu Asn Arg Thr Leu Val Thr Thr Ile Pro Ser Arg 100 105 110 Ile Tyr Asn Asn Thr Asn Ala Ser Val Leu Lys Pro Ala Thr Ser Thr 115 120 125 Glu Leu Lys Thr Ser His Ser Ser Ser Phe Thr Asn Leu Thr Glu Ile 130 135 140 Thr His Thr Gly Gly Ile Thr Thr Lys Ala Glu Val Lys Phe Lys Pro145 150 155 160 Lys Gly Leu Val Ala Asp Gly Glu Val Ser Thr Gly Leu Glu Leu Lys 165 170 175 Tyr Glu Tyr Ser Asn Thr Gln Gly Thr Asn Gln Thr Gln Thr Thr Thr 180 185 190 Asn Glu Leu Ser Phe Lys Val Asp Thr Pro Val Glu Val Pro Pro Arg 195 200 205 Ser Ser Ile Glu Val Ile Thr Asn Ile Tyr Lys Asp Lys Val Arg Tyr 210 215 220 Glu Tyr Thr Gly Tyr Ser Glu Phe Thr Gly Glu Val Thr Phe Gln Tyr225 230 235 240 Arg Leu Asn Ala Ser Asp Thr Pro Lys Thr Val Thr Arg Glu Ile Gly 245 250 255 Thr Met Met Tyr Glu Ile Asp Asp Glu Thr Tyr Asn Lys Leu Ala Asp 260 265 270 Arg Gly Ile Thr Val Lys Gly Ala Val Asp Ser Pro Asp Val Leu Arg 275 280 285 Ile Lys Gly Thr Ala Ile Leu Asp Val Asp Glu Ala Tyr Ser Thr Glu 290 295 300 Val Ile Ala Arg Asp Ile Ala Pro Ile Gln305 310 163552DNABacillus thuringiensisCDS(1)...(3552) 16atg tgt ttt cta tgt cat aga aga cac ata gga gat tgt tta ttc aat 48Met Cys Phe Leu Cys His Arg Arg His Ile Gly Asp Cys Leu Phe Asn1 5 10 15tta ata tac ttt ttg gag gta aat tat atg gat ata aga aat cag aag 96Leu Ile Tyr Phe Leu Glu Val Asn Tyr Met Asp Ile Arg Asn Gln Lys 20 25 30aaa tca gaa gaa ata cac ccc aca tta aat gaa tca tct tct aat aca 144Lys Ser Glu Glu Ile His Pro Thr Leu Asn Glu Ser Ser Ser Asn Thr 35 40 45aca tca aag tat cca ctt gca agt gat cta atc aaa caa tat caa aat 192Thr Ser Lys Tyr Pro Leu Ala Ser Asp Leu Ile Lys Gln Tyr Gln Asn 50 55 60atg aat tat aaa gat agt tta aat ata atc gag gag aat aat gta atc 240Met Asn Tyr Lys Asp Ser Leu Asn Ile Ile Glu Glu Asn Asn Val Ile65 70 75 80gat cct gta tct gga act gcc gct ttg gta act gca agg aaa att ggt 288Asp Pro Val Ser Gly Thr Ala Ala Leu Val Thr Ala Arg Lys Ile Gly 85 90 95ggt aag ata att aag aag tta gga gag gca gct ctg tct aaa att ttg 336Gly Lys Ile Ile Lys Lys Leu Gly Glu Ala Ala Leu Ser Lys Ile Leu 100 105 110aaa gag atc ttg ggt tat tta tgg ccg act tca gga gaa gac gat tca 384Lys Glu Ile Leu Gly Tyr Leu Trp Pro Thr Ser Gly Glu Asp Asp Ser 115 120 125tgg aca gat atg atg acg gca gta gaa gaa ctt att gat caa aaa ata 432Trp Thr Asp Met Met Thr Ala Val Glu Glu Leu Ile Asp Gln Lys Ile 130 135 140cag gaa cag gta gaa ttg gat gca ctt acg gag ttg gaa aaa ata ggt 480Gln Glu Gln Val Glu Leu Asp Ala Leu Thr Glu Leu Glu Lys Ile Gly145 150 155 160gaa gcc gtg gag gca tat tat atc gca tta gac gat tgg gaa cca gta 528Glu Ala Val Glu Ala Tyr Tyr Ile Ala Leu Asp Asp Trp Glu Pro Val 165 170 175cct gaa gat atg ttt agt cta agc gaa gta ata aaa cga tac gat ttt 576Pro Glu Asp Met Phe Ser Leu Ser Glu Val Ile Lys Arg Tyr Asp Phe 180 185 190gcg cag caa ctt gca aga gct tca atg cca gaa ttc aag aag aaa ggt 624Ala Gln Gln Leu Ala Arg Ala Ser Met Pro Glu Phe Lys Lys Lys Gly 195 200 205tat gaa att ccc ttg tta gca aca tat gca aat gct gca aat gtt cat 672Tyr Glu Ile Pro Leu Leu Ala Thr Tyr Ala Asn Ala Ala Asn Val His 210 215 220ttg ctt tta atg aga gat atg caa ata tac ggg gaa aga tgg gga ata 720Leu Leu Leu Met Arg Asp Met Gln Ile Tyr Gly Glu Arg Trp Gly Ile225 230 235 240cct aaa gaa gat ata gag ctc tac tta tct gaa caa gaa aat ttt acc 768Pro Lys Glu Asp Ile Glu Leu Tyr Leu Ser Glu Gln Glu Asn Phe Thr 245 250

255tct gaa tat aca gat cat tgc gta aaa tat tat aat gag gga tta aat 816Ser Glu Tyr Thr Asp His Cys Val Lys Tyr Tyr Asn Glu Gly Leu Asn 260 265 270caa ttg aaa aat aaa agt ggc gta agt ggt tta gtt tgg gag aat tat 864Gln Leu Lys Asn Lys Ser Gly Val Ser Gly Leu Val Trp Glu Asn Tyr 275 280 285aac cgt ttc cgt aca gaa atg aca atc ctg gtg tta gat att gtg gct 912Asn Arg Phe Arg Thr Glu Met Thr Ile Leu Val Leu Asp Ile Val Ala 290 295 300gta ttt cca cgc tac aat gta atc gaa tat cct ata gat tca aca gta 960Val Phe Pro Arg Tyr Asn Val Ile Glu Tyr Pro Ile Asp Ser Thr Val305 310 315 320gaa tta aca aga aca att tat cta gat cca ctt ggt tac aca ggg aat 1008Glu Leu Thr Arg Thr Ile Tyr Leu Asp Pro Leu Gly Tyr Thr Gly Asn 325 330 335tcc aat gac gag cat ccc gaa tat tat gcg tct aca aaa tca ttt tca 1056Ser Asn Asp Glu His Pro Glu Tyr Tyr Ala Ser Thr Lys Ser Phe Ser 340 345 350tca ata gag agt aga gcc ata cct gca ccc aca tta ttc cag tgg atc 1104Ser Ile Glu Ser Arg Ala Ile Pro Ala Pro Thr Leu Phe Gln Trp Ile 355 360 365act gaa ctt caa gta tat tca gca aaa ggc tct cat ggt tct acc tat 1152Thr Glu Leu Gln Val Tyr Ser Ala Lys Gly Ser His Gly Ser Thr Tyr 370 375 380act aca tgg tgg act gga cat aaa gtg act gct aag cct act aat ggt 1200Thr Thr Trp Trp Thr Gly His Lys Val Thr Ala Lys Pro Thr Asn Gly385 390 395 400ggt ctt gaa agt aaa tat gat ttc gga agt tct tca ggt tct cag aac 1248Gly Leu Glu Ser Lys Tyr Asp Phe Gly Ser Ser Ser Gly Ser Gln Asn 405 410 415aag gat gtt ttt gct ctt gat ggc aag gat gta tat gat tca caa agt 1296Lys Asp Val Phe Ala Leu Asp Gly Lys Asp Val Tyr Asp Ser Gln Ser 420 425 430atg tta aca tcg att agt tat tcc ggt att aga tat ttt ggg tgt cct 1344Met Leu Thr Ser Ile Ser Tyr Ser Gly Ile Arg Tyr Phe Gly Cys Pro 435 440 445cag ttt aag tta aat tgg ata aat aag aat aat gag cta gca gaa cag 1392Gln Phe Lys Leu Asn Trp Ile Asn Lys Asn Asn Glu Leu Ala Glu Gln 450 455 460ata ttt aat tat tca agt aat gtt ggt tca tct ttc agt gag tat agg 1440Ile Phe Asn Tyr Ser Ser Asn Val Gly Ser Ser Phe Ser Glu Tyr Arg465 470 475 480tat agc aag gat gaa tta cca ata gaa ttg ttg gcg agc cct att tat 1488Tyr Ser Lys Asp Glu Leu Pro Ile Glu Leu Leu Ala Ser Pro Ile Tyr 485 490 495gga gat att gag gaa tac agt cat agg tta agt cac gtt tca gag gta 1536Gly Asp Ile Glu Glu Tyr Ser His Arg Leu Ser His Val Ser Glu Val 500 505 510att aaa gat tat ggg cag gga ata att cct gta tta ggt ttc aca cat 1584Ile Lys Asp Tyr Gly Gln Gly Ile Ile Pro Val Leu Gly Phe Thr His 515 520 525gta agt gta agt cgt gac aat aga att tat tca gat aag att acg caa 1632Val Ser Val Ser Arg Asp Asn Arg Ile Tyr Ser Asp Lys Ile Thr Gln 530 535 540att cca gct gtg aaa atg tat gaa tta gta agc cca gcc gtt gtt gta 1680Ile Pro Ala Val Lys Met Tyr Glu Leu Val Ser Pro Ala Val Val Val545 550 555 560aaa ggg cct gga tct aca ggt gga gat tta gtt aag aga ggg agt agt 1728Lys Gly Pro Gly Ser Thr Gly Gly Asp Leu Val Lys Arg Gly Ser Ser 565 570 575ggt aat ata gga tct atg aat gtt acc gta aac tca cca ctt tct caa 1776Gly Asn Ile Gly Ser Met Asn Val Thr Val Asn Ser Pro Leu Ser Gln 580 585 590aaa tat cgt gtc aga gtt cga tat gcc act aat gct tct ggc cag tta 1824Lys Tyr Arg Val Arg Val Arg Tyr Ala Thr Asn Ala Ser Gly Gln Leu 595 600 605aac gtg agt att aac gat aaa tta aca ctt caa aaa cct ttt gaa aga 1872Asn Val Ser Ile Asn Asp Lys Leu Thr Leu Gln Lys Pro Phe Glu Arg 610 615 620acc gga aca aca ata ggt gaa gga aca gat ttg tcc tat gat tca ttt 1920Thr Gly Thr Thr Ile Gly Glu Gly Thr Asp Leu Ser Tyr Asp Ser Phe625 630 635 640gga tat tta gaa tat tct acg acg att caa ttt ccg aat gag cac cca 1968Gly Tyr Leu Glu Tyr Ser Thr Thr Ile Gln Phe Pro Asn Glu His Pro 645 650 655aaa atc act ttt aat tta tcc cat tgg agc ggc agt gga gca ttt tat 2016Lys Ile Thr Phe Asn Leu Ser His Trp Ser Gly Ser Gly Ala Phe Tyr 660 665 670ata gat aaa atc gaa ttt atc cct gta gat gaa aat tac gat gaa aga 2064Ile Asp Lys Ile Glu Phe Ile Pro Val Asp Glu Asn Tyr Asp Glu Arg 675 680 685gta aca cta gaa aaa gca cag aaa gcc gtg aat gcc ttg ttt aca gcg 2112Val Thr Leu Glu Lys Ala Gln Lys Ala Val Asn Ala Leu Phe Thr Ala 690 695 700gga aga aat gca ctc caa aaa gat gtg aca gat ttt aaa gta gat cag 2160Gly Arg Asn Ala Leu Gln Lys Asp Val Thr Asp Phe Lys Val Asp Gln705 710 715 720gtt tcc att tta gtg gat tgt ata cca ggg gaa ttg tat cca aat gag 2208Val Ser Ile Leu Val Asp Cys Ile Pro Gly Glu Leu Tyr Pro Asn Glu 725 730 735aaa cgc gaa cta cta agt tta gtc aaa tac gca aaa cgg ttg agt tat 2256Lys Arg Glu Leu Leu Ser Leu Val Lys Tyr Ala Lys Arg Leu Ser Tyr 740 745 750tcc cgt aat tta ctc cta gac cca aca ttc gat tct atc aat tca cca 2304Ser Arg Asn Leu Leu Leu Asp Pro Thr Phe Asp Ser Ile Asn Ser Pro 755 760 765gat gag aat ggc tgg tac ggg agt aat ggt att gca att gga aat ggg 2352Asp Glu Asn Gly Trp Tyr Gly Ser Asn Gly Ile Ala Ile Gly Asn Gly 770 775 780aac ttt gta ttc aaa gga aac tat tta att ttc tca ggt acc aat gat 2400Asn Phe Val Phe Lys Gly Asn Tyr Leu Ile Phe Ser Gly Thr Asn Asp785 790 795 800aca caa tac cca acg tat ctc tat caa aaa att gat gaa tcc aag ctc 2448Thr Gln Tyr Pro Thr Tyr Leu Tyr Gln Lys Ile Asp Glu Ser Lys Leu 805 810 815aaa gaa tat aca cgc tat aaa ctg aga ggt ttt atc gag agt agt cag 2496Lys Glu Tyr Thr Arg Tyr Lys Leu Arg Gly Phe Ile Glu Ser Ser Gln 820 825 830gat tta gag gca tat gtg att cgc tat gat gca aaa cat gaa aca ttg 2544Asp Leu Glu Ala Tyr Val Ile Arg Tyr Asp Ala Lys His Glu Thr Leu 835 840 845gat gta tcc aat aat cta ttc cca gat att tct cct gtg aat gca tgc 2592Asp Val Ser Asn Asn Leu Phe Pro Asp Ile Ser Pro Val Asn Ala Cys 850 855 860gga gaa cca aat cgt tgt gcg gca cta caa tac ctg gat gaa aac cca 2640Gly Glu Pro Asn Arg Cys Ala Ala Leu Gln Tyr Leu Asp Glu Asn Pro865 870 875 880agg tta gaa tgt agt tcg ata caa gat ggc att tta tct gat tcg cat 2688Arg Leu Glu Cys Ser Ser Ile Gln Asp Gly Ile Leu Ser Asp Ser His 885 890 895tca ttt tct ctc aat ata gat aca ggt tct att gat tac gat gag aac 2736Ser Phe Ser Leu Asn Ile Asp Thr Gly Ser Ile Asp Tyr Asp Glu Asn 900 905 910gta ggt att tgg gtg ttg ttt aaa att tcc aca ccg gaa ggg tat gcg 2784Val Gly Ile Trp Val Leu Phe Lys Ile Ser Thr Pro Glu Gly Tyr Ala 915 920 925aaa ttt gga aac cta gaa gtg att gaa gat ggc cta gtc att gga gaa 2832Lys Phe Gly Asn Leu Glu Val Ile Glu Asp Gly Leu Val Ile Gly Glu 930 935 940gca tta gcc cgt gtg aaa cgt caa gaa acg aag tgg aga aac aag ttg 2880Ala Leu Ala Arg Val Lys Arg Gln Glu Thr Lys Trp Arg Asn Lys Leu945 950 955 960aca caa ctg cga acg gaa aca caa gcg att tat aca cga gca aaa caa 2928Thr Gln Leu Arg Thr Glu Thr Gln Ala Ile Tyr Thr Arg Ala Lys Gln 965 970 975gcc att gat aat tta ttc aca aat gca cag gac tct cac tta aaa ata 2976Ala Ile Asp Asn Leu Phe Thr Asn Ala Gln Asp Ser His Leu Lys Ile 980 985 990ggt gct aca ttc gcg tca att gtg gcc gcg cga aag att gtc caa tca 3024Gly Ala Thr Phe Ala Ser Ile Val Ala Ala Arg Lys Ile Val Gln Ser 995 1000 1005ata cgt gaa gcg tat atg tca tgg tta tct atc gtc cca agt gta aat 3072Ile Arg Glu Ala Tyr Met Ser Trp Leu Ser Ile Val Pro Ser Val Asn 1010 1015 1020tat cct att ttc aca gag ttg aat gaa aga gta cag cga gca ttt cga 3120Tyr Pro Ile Phe Thr Glu Leu Asn Glu Arg Val Gln Arg Ala Phe Arg1025 1030 1035 1040tta tat gat gta cga aat gtc gta cgt aat ggc cga ttc ttg agt gga 3168Leu Tyr Asp Val Arg Asn Val Val Arg Asn Gly Arg Phe Leu Ser Gly 1045 1050 1055gta tcg gat tgg att gtg aca tct gat gta aag gta caa gaa gaa aat 3216Val Ser Asp Trp Ile Val Thr Ser Asp Val Lys Val Gln Glu Glu Asn 1060 1065 1070ggg aac aac gta tta gtt ctt tcc aat tgg gat gca caa gta tta caa 3264Gly Asn Asn Val Leu Val Leu Ser Asn Trp Asp Ala Gln Val Leu Gln 1075 1080 1085tgt ctg aat ctc tac gaa gac cat ggg tat atc tta cgc gta aca gca 3312Cys Leu Asn Leu Tyr Glu Asp His Gly Tyr Ile Leu Arg Val Thr Ala 1090 1095 1100cgt aag gaa gga ctc gga gaa gga tat ata aca atc act gat gaa gaa 3360Arg Lys Glu Gly Leu Gly Glu Gly Tyr Ile Thr Ile Thr Asp Glu Glu1105 1110 1115 1120ggg cat aca gat caa ttg aca ttt ggt gga tgt gag gag ata gat tca 3408Gly His Thr Asp Gln Leu Thr Phe Gly Gly Cys Glu Glu Ile Asp Ser 1125 1130 1135tcc aat tct ttc gta tct aca ggt tat att aca aaa gag cta gaa ttc 3456Ser Asn Ser Phe Val Ser Thr Gly Tyr Ile Thr Lys Glu Leu Glu Phe 1140 1145 1150ttc cca gat aca gag aaa gtg cgc atc gaa att gga gaa aca gaa gga 3504Phe Pro Asp Thr Glu Lys Val Arg Ile Glu Ile Gly Glu Thr Glu Gly 1155 1160 1165aca ttc cag gta gaa agt gtg gaa tta ttt ttg atg gaa gac ata tgc 3552Thr Phe Gln Val Glu Ser Val Glu Leu Phe Leu Met Glu Asp Ile Cys 1170 1175 1180171184PRTBacillus thuringiensis 17Met Cys Phe Leu Cys His Arg Arg His Ile Gly Asp Cys Leu Phe Asn1 5 10 15 Leu Ile Tyr Phe Leu Glu Val Asn Tyr Met Asp Ile Arg Asn Gln Lys 20 25 30 Lys Ser Glu Glu Ile His Pro Thr Leu Asn Glu Ser Ser Ser Asn Thr 35 40 45 Thr Ser Lys Tyr Pro Leu Ala Ser Asp Leu Ile Lys Gln Tyr Gln Asn 50 55 60 Met Asn Tyr Lys Asp Ser Leu Asn Ile Ile Glu Glu Asn Asn Val Ile65 70 75 80 Asp Pro Val Ser Gly Thr Ala Ala Leu Val Thr Ala Arg Lys Ile Gly 85 90 95 Gly Lys Ile Ile Lys Lys Leu Gly Glu Ala Ala Leu Ser Lys Ile Leu 100 105 110 Lys Glu Ile Leu Gly Tyr Leu Trp Pro Thr Ser Gly Glu Asp Asp Ser 115 120 125 Trp Thr Asp Met Met Thr Ala Val Glu Glu Leu Ile Asp Gln Lys Ile 130 135 140 Gln Glu Gln Val Glu Leu Asp Ala Leu Thr Glu Leu Glu Lys Ile Gly145 150 155 160 Glu Ala Val Glu Ala Tyr Tyr Ile Ala Leu Asp Asp Trp Glu Pro Val 165 170 175 Pro Glu Asp Met Phe Ser Leu Ser Glu Val Ile Lys Arg Tyr Asp Phe 180 185 190 Ala Gln Gln Leu Ala Arg Ala Ser Met Pro Glu Phe Lys Lys Lys Gly 195 200 205 Tyr Glu Ile Pro Leu Leu Ala Thr Tyr Ala Asn Ala Ala Asn Val His 210 215 220 Leu Leu Leu Met Arg Asp Met Gln Ile Tyr Gly Glu Arg Trp Gly Ile225 230 235 240 Pro Lys Glu Asp Ile Glu Leu Tyr Leu Ser Glu Gln Glu Asn Phe Thr 245 250 255 Ser Glu Tyr Thr Asp His Cys Val Lys Tyr Tyr Asn Glu Gly Leu Asn 260 265 270 Gln Leu Lys Asn Lys Ser Gly Val Ser Gly Leu Val Trp Glu Asn Tyr 275 280 285 Asn Arg Phe Arg Thr Glu Met Thr Ile Leu Val Leu Asp Ile Val Ala 290 295 300 Val Phe Pro Arg Tyr Asn Val Ile Glu Tyr Pro Ile Asp Ser Thr Val305 310 315 320 Glu Leu Thr Arg Thr Ile Tyr Leu Asp Pro Leu Gly Tyr Thr Gly Asn 325 330 335 Ser Asn Asp Glu His Pro Glu Tyr Tyr Ala Ser Thr Lys Ser Phe Ser 340 345 350 Ser Ile Glu Ser Arg Ala Ile Pro Ala Pro Thr Leu Phe Gln Trp Ile 355 360 365 Thr Glu Leu Gln Val Tyr Ser Ala Lys Gly Ser His Gly Ser Thr Tyr 370 375 380 Thr Thr Trp Trp Thr Gly His Lys Val Thr Ala Lys Pro Thr Asn Gly385 390 395 400 Gly Leu Glu Ser Lys Tyr Asp Phe Gly Ser Ser Ser Gly Ser Gln Asn 405 410 415 Lys Asp Val Phe Ala Leu Asp Gly Lys Asp Val Tyr Asp Ser Gln Ser 420 425 430 Met Leu Thr Ser Ile Ser Tyr Ser Gly Ile Arg Tyr Phe Gly Cys Pro 435 440 445 Gln Phe Lys Leu Asn Trp Ile Asn Lys Asn Asn Glu Leu Ala Glu Gln 450 455 460 Ile Phe Asn Tyr Ser Ser Asn Val Gly Ser Ser Phe Ser Glu Tyr Arg465 470 475 480 Tyr Ser Lys Asp Glu Leu Pro Ile Glu Leu Leu Ala Ser Pro Ile Tyr 485 490 495 Gly Asp Ile Glu Glu Tyr Ser His Arg Leu Ser His Val Ser Glu Val 500 505 510 Ile Lys Asp Tyr Gly Gln Gly Ile Ile Pro Val Leu Gly Phe Thr His 515 520 525 Val Ser Val Ser Arg Asp Asn Arg Ile Tyr Ser Asp Lys Ile Thr Gln 530 535 540 Ile Pro Ala Val Lys Met Tyr Glu Leu Val Ser Pro Ala Val Val Val545 550 555 560 Lys Gly Pro Gly Ser Thr Gly Gly Asp Leu Val Lys Arg Gly Ser Ser 565 570 575 Gly Asn Ile Gly Ser Met Asn Val Thr Val Asn Ser Pro Leu Ser Gln 580 585 590 Lys Tyr Arg Val Arg Val Arg Tyr Ala Thr Asn Ala Ser Gly Gln Leu 595 600 605 Asn Val Ser Ile Asn Asp Lys Leu Thr Leu Gln Lys Pro Phe Glu Arg 610 615 620 Thr Gly Thr Thr Ile Gly Glu Gly Thr Asp Leu Ser Tyr Asp Ser Phe625 630 635 640 Gly Tyr Leu Glu Tyr Ser Thr Thr Ile Gln Phe Pro Asn Glu His Pro 645 650 655 Lys Ile Thr Phe Asn Leu Ser His Trp Ser Gly Ser Gly Ala Phe Tyr 660 665 670 Ile Asp Lys Ile Glu Phe Ile Pro Val Asp Glu Asn Tyr Asp Glu Arg 675 680 685 Val Thr Leu Glu Lys Ala Gln Lys Ala Val Asn Ala Leu Phe Thr Ala 690 695 700 Gly Arg Asn Ala Leu Gln Lys Asp Val Thr Asp Phe Lys Val Asp Gln705 710 715 720 Val Ser Ile Leu Val Asp Cys Ile Pro Gly Glu Leu Tyr Pro Asn Glu 725 730 735 Lys Arg Glu Leu Leu Ser Leu Val Lys Tyr Ala Lys Arg Leu Ser Tyr 740 745 750 Ser Arg Asn Leu Leu Leu Asp Pro Thr Phe Asp Ser Ile Asn Ser Pro 755 760 765 Asp Glu Asn Gly Trp Tyr Gly Ser Asn Gly Ile Ala Ile Gly Asn Gly 770 775 780 Asn Phe Val Phe Lys Gly Asn Tyr Leu Ile Phe Ser Gly Thr Asn Asp785 790 795 800 Thr Gln Tyr Pro Thr Tyr Leu Tyr Gln Lys Ile Asp Glu Ser Lys Leu 805 810 815 Lys Glu Tyr Thr Arg Tyr Lys Leu Arg Gly Phe Ile Glu Ser Ser Gln 820 825 830 Asp Leu Glu Ala Tyr Val Ile Arg Tyr Asp Ala Lys His Glu Thr Leu 835 840 845 Asp Val Ser Asn Asn Leu Phe Pro Asp Ile Ser Pro Val Asn Ala Cys 850 855 860 Gly Glu Pro Asn Arg Cys Ala Ala Leu Gln Tyr Leu Asp Glu Asn Pro865 870 875 880 Arg Leu Glu Cys Ser Ser Ile Gln Asp Gly Ile Leu Ser Asp Ser His 885 890 895 Ser Phe Ser Leu Asn Ile Asp Thr Gly Ser Ile Asp Tyr Asp Glu Asn 900 905 910 Val Gly Ile Trp Val Leu Phe Lys Ile

Ser Thr Pro Glu Gly Tyr Ala 915 920 925 Lys Phe Gly Asn Leu Glu Val Ile Glu Asp Gly Leu Val Ile Gly Glu 930 935 940 Ala Leu Ala Arg Val Lys Arg Gln Glu Thr Lys Trp Arg Asn Lys Leu945 950 955 960 Thr Gln Leu Arg Thr Glu Thr Gln Ala Ile Tyr Thr Arg Ala Lys Gln 965 970 975 Ala Ile Asp Asn Leu Phe Thr Asn Ala Gln Asp Ser His Leu Lys Ile 980 985 990 Gly Ala Thr Phe Ala Ser Ile Val Ala Ala Arg Lys Ile Val Gln Ser 995 1000 1005 Ile Arg Glu Ala Tyr Met Ser Trp Leu Ser Ile Val Pro Ser Val Asn 1010 1015 1020 Tyr Pro Ile Phe Thr Glu Leu Asn Glu Arg Val Gln Arg Ala Phe Arg1025 1030 1035 1040 Leu Tyr Asp Val Arg Asn Val Val Arg Asn Gly Arg Phe Leu Ser Gly 1045 1050 1055 Val Ser Asp Trp Ile Val Thr Ser Asp Val Lys Val Gln Glu Glu Asn 1060 1065 1070 Gly Asn Asn Val Leu Val Leu Ser Asn Trp Asp Ala Gln Val Leu Gln 1075 1080 1085 Cys Leu Asn Leu Tyr Glu Asp His Gly Tyr Ile Leu Arg Val Thr Ala 1090 1095 1100 Arg Lys Glu Gly Leu Gly Glu Gly Tyr Ile Thr Ile Thr Asp Glu Glu1105 1110 1115 1120 Gly His Thr Asp Gln Leu Thr Phe Gly Gly Cys Glu Glu Ile Asp Ser 1125 1130 1135 Ser Asn Ser Phe Val Ser Thr Gly Tyr Ile Thr Lys Glu Leu Glu Phe 1140 1145 1150 Phe Pro Asp Thr Glu Lys Val Arg Ile Glu Ile Gly Glu Thr Glu Gly 1155 1160 1165 Thr Phe Gln Val Glu Ser Val Glu Leu Phe Leu Met Glu Asp Ile Cys 1170 1175 1180 183477DNABacillus thuringiensisCDS(1)...(3477) 18atg gat ata aga aat cag aag aaa tca gaa gaa ata cac ccc aca tta 48Met Asp Ile Arg Asn Gln Lys Lys Ser Glu Glu Ile His Pro Thr Leu1 5 10 15aat gaa tca tct tct aat aca aca tca aag tat cca ctt gca agt gat 96Asn Glu Ser Ser Ser Asn Thr Thr Ser Lys Tyr Pro Leu Ala Ser Asp 20 25 30cta atc aaa caa tat caa aat atg aat tat aaa gat agt tta aat ata 144Leu Ile Lys Gln Tyr Gln Asn Met Asn Tyr Lys Asp Ser Leu Asn Ile 35 40 45atc gag gag aat aat gta atc gat cct gta tct gga act gcc gct ttg 192Ile Glu Glu Asn Asn Val Ile Asp Pro Val Ser Gly Thr Ala Ala Leu 50 55 60gta act gca agg aaa att ggt ggt aag ata att aag aag tta gga gag 240Val Thr Ala Arg Lys Ile Gly Gly Lys Ile Ile Lys Lys Leu Gly Glu65 70 75 80gca gct ctg tct aaa att ttg aaa gag atc ttg ggt tat tta tgg ccg 288Ala Ala Leu Ser Lys Ile Leu Lys Glu Ile Leu Gly Tyr Leu Trp Pro 85 90 95act tca gga gaa gac gat tca tgg aca gat atg atg acg gca gta gaa 336Thr Ser Gly Glu Asp Asp Ser Trp Thr Asp Met Met Thr Ala Val Glu 100 105 110gaa ctt att gat caa aaa ata cag gaa cag gta gaa ttg gat gca ctt 384Glu Leu Ile Asp Gln Lys Ile Gln Glu Gln Val Glu Leu Asp Ala Leu 115 120 125acg gag ttg gaa aaa ata ggt gaa gcc gtg gag gca tat tat atc gca 432Thr Glu Leu Glu Lys Ile Gly Glu Ala Val Glu Ala Tyr Tyr Ile Ala 130 135 140tta gac gat tgg gaa cca gta cct gaa gat atg ttt agt cta agc gaa 480Leu Asp Asp Trp Glu Pro Val Pro Glu Asp Met Phe Ser Leu Ser Glu145 150 155 160gta ata aaa cga tac gat ttt gcg cag caa ctt gca aga gct tca atg 528Val Ile Lys Arg Tyr Asp Phe Ala Gln Gln Leu Ala Arg Ala Ser Met 165 170 175cca gaa ttc aag aag aaa ggt tat gaa att ccc ttg tta gca aca tat 576Pro Glu Phe Lys Lys Lys Gly Tyr Glu Ile Pro Leu Leu Ala Thr Tyr 180 185 190gca aat gct gca aat gtt cat ttg ctt tta atg aga gat atg caa ata 624Ala Asn Ala Ala Asn Val His Leu Leu Leu Met Arg Asp Met Gln Ile 195 200 205tac ggg gaa aga tgg gga ata cct aaa gaa gat ata gag ctc tac tta 672Tyr Gly Glu Arg Trp Gly Ile Pro Lys Glu Asp Ile Glu Leu Tyr Leu 210 215 220tct gaa caa gaa aat ttt acc tct gaa tat aca gat cat tgc gta aaa 720Ser Glu Gln Glu Asn Phe Thr Ser Glu Tyr Thr Asp His Cys Val Lys225 230 235 240tat tat aat gag gga tta aat caa ttg aaa aat aaa agt ggc gta agt 768Tyr Tyr Asn Glu Gly Leu Asn Gln Leu Lys Asn Lys Ser Gly Val Ser 245 250 255ggt tta gtt tgg gag aat tat aac cgt ttc cgt aca gaa atg aca atc 816Gly Leu Val Trp Glu Asn Tyr Asn Arg Phe Arg Thr Glu Met Thr Ile 260 265 270ctg gtg tta gat att gtg gct gta ttt cca cgc tac aat gta atc gaa 864Leu Val Leu Asp Ile Val Ala Val Phe Pro Arg Tyr Asn Val Ile Glu 275 280 285tat cct ata gat tca aca gta gaa tta aca aga aca att tat cta gat 912Tyr Pro Ile Asp Ser Thr Val Glu Leu Thr Arg Thr Ile Tyr Leu Asp 290 295 300cca ctt ggt tac aca ggg aat tcc aat gac gag cat ccc gaa tat tat 960Pro Leu Gly Tyr Thr Gly Asn Ser Asn Asp Glu His Pro Glu Tyr Tyr305 310 315 320gcg tct aca aaa tca ttt tca tca ata gag agt aga gcc ata cct gca 1008Ala Ser Thr Lys Ser Phe Ser Ser Ile Glu Ser Arg Ala Ile Pro Ala 325 330 335ccc aca tta ttc cag tgg atc act gaa ctt caa gta tat tca gca aaa 1056Pro Thr Leu Phe Gln Trp Ile Thr Glu Leu Gln Val Tyr Ser Ala Lys 340 345 350ggc tct cat ggt tct acc tat act aca tgg tgg act gga cat aaa gtg 1104Gly Ser His Gly Ser Thr Tyr Thr Thr Trp Trp Thr Gly His Lys Val 355 360 365act gct aag cct act aat ggt ggt ctt gaa agt aaa tat gat ttc gga 1152Thr Ala Lys Pro Thr Asn Gly Gly Leu Glu Ser Lys Tyr Asp Phe Gly 370 375 380agt tct tca ggt tct cag aac aag gat gtt ttt gct ctt gat ggc aag 1200Ser Ser Ser Gly Ser Gln Asn Lys Asp Val Phe Ala Leu Asp Gly Lys385 390 395 400gat gta tat gat tca caa agt atg tta aca tcg att agt tat tcc ggt 1248Asp Val Tyr Asp Ser Gln Ser Met Leu Thr Ser Ile Ser Tyr Ser Gly 405 410 415att aga tat ttt ggg tgt cct cag ttt aag tta aat tgg ata aat aag 1296Ile Arg Tyr Phe Gly Cys Pro Gln Phe Lys Leu Asn Trp Ile Asn Lys 420 425 430aat aat gag cta gca gaa cag ata ttt aat tat tca agt aat gtt ggt 1344Asn Asn Glu Leu Ala Glu Gln Ile Phe Asn Tyr Ser Ser Asn Val Gly 435 440 445tca tct ttc agt gag tat agg tat agc aag gat gaa tta cca ata gaa 1392Ser Ser Phe Ser Glu Tyr Arg Tyr Ser Lys Asp Glu Leu Pro Ile Glu 450 455 460ttg ttg gcg agc cct att tat gga gat att gag gaa tac agt cat agg 1440Leu Leu Ala Ser Pro Ile Tyr Gly Asp Ile Glu Glu Tyr Ser His Arg465 470 475 480tta agt cac gtt tca gag gta att aaa gat tat ggg cag gga ata att 1488Leu Ser His Val Ser Glu Val Ile Lys Asp Tyr Gly Gln Gly Ile Ile 485 490 495cct gta tta ggt ttc aca cat gta agt gta agt cgt gac aat aga att 1536Pro Val Leu Gly Phe Thr His Val Ser Val Ser Arg Asp Asn Arg Ile 500 505 510tat tca gat aag att acg caa att cca gct gtg aaa atg tat gaa tta 1584Tyr Ser Asp Lys Ile Thr Gln Ile Pro Ala Val Lys Met Tyr Glu Leu 515 520 525gta agc cca gcc gtt gtt gta aaa ggg cct gga tct aca ggt gga gat 1632Val Ser Pro Ala Val Val Val Lys Gly Pro Gly Ser Thr Gly Gly Asp 530 535 540tta gtt aag aga ggg agt agt ggt aat ata gga tct atg aat gtt acc 1680Leu Val Lys Arg Gly Ser Ser Gly Asn Ile Gly Ser Met Asn Val Thr545 550 555 560gta aac tca cca ctt tct caa aaa tat cgt gtc aga gtt cga tat gcc 1728Val Asn Ser Pro Leu Ser Gln Lys Tyr Arg Val Arg Val Arg Tyr Ala 565 570 575act aat gct tct ggc cag tta aac gtg agt att aac gat aaa tta aca 1776Thr Asn Ala Ser Gly Gln Leu Asn Val Ser Ile Asn Asp Lys Leu Thr 580 585 590ctt caa aaa cct ttt gaa aga acc gga aca aca ata ggt gaa gga aca 1824Leu Gln Lys Pro Phe Glu Arg Thr Gly Thr Thr Ile Gly Glu Gly Thr 595 600 605gat ttg tcc tat gat tca ttt gga tat tta gaa tat tct acg acg att 1872Asp Leu Ser Tyr Asp Ser Phe Gly Tyr Leu Glu Tyr Ser Thr Thr Ile 610 615 620caa ttt ccg aat gag cac cca aaa atc act ttt aat tta tcc cat tgg 1920Gln Phe Pro Asn Glu His Pro Lys Ile Thr Phe Asn Leu Ser His Trp625 630 635 640agc ggc agt gga gca ttt tat ata gat aaa atc gaa ttt atc cct gta 1968Ser Gly Ser Gly Ala Phe Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val 645 650 655gat gaa aat tac gat gaa aga gta aca cta gaa aaa gca cag aaa gcc 2016Asp Glu Asn Tyr Asp Glu Arg Val Thr Leu Glu Lys Ala Gln Lys Ala 660 665 670gtg aat gcc ttg ttt aca gcg gga aga aat gca ctc caa aaa gat gtg 2064Val Asn Ala Leu Phe Thr Ala Gly Arg Asn Ala Leu Gln Lys Asp Val 675 680 685aca gat ttt aaa gta gat cag gtt tcc att tta gtg gat tgt ata cca 2112Thr Asp Phe Lys Val Asp Gln Val Ser Ile Leu Val Asp Cys Ile Pro 690 695 700ggg gaa ttg tat cca aat gag aaa cgc gaa cta cta agt tta gtc aaa 2160Gly Glu Leu Tyr Pro Asn Glu Lys Arg Glu Leu Leu Ser Leu Val Lys705 710 715 720tac gca aaa cgg ttg agt tat tcc cgt aat tta ctc cta gac cca aca 2208Tyr Ala Lys Arg Leu Ser Tyr Ser Arg Asn Leu Leu Leu Asp Pro Thr 725 730 735ttc gat tct atc aat tca cca gat gag aat ggc tgg tac ggg agt aat 2256Phe Asp Ser Ile Asn Ser Pro Asp Glu Asn Gly Trp Tyr Gly Ser Asn 740 745 750ggt att gca att gga aat ggg aac ttt gta ttc aaa gga aac tat tta 2304Gly Ile Ala Ile Gly Asn Gly Asn Phe Val Phe Lys Gly Asn Tyr Leu 755 760 765att ttc tca ggt acc aat gat aca caa tac cca acg tat ctc tat caa 2352Ile Phe Ser Gly Thr Asn Asp Thr Gln Tyr Pro Thr Tyr Leu Tyr Gln 770 775 780aaa att gat gaa tcc aag ctc aaa gaa tat aca cgc tat aaa ctg aga 2400Lys Ile Asp Glu Ser Lys Leu Lys Glu Tyr Thr Arg Tyr Lys Leu Arg785 790 795 800ggt ttt atc gag agt agt cag gat tta gag gca tat gtg att cgc tat 2448Gly Phe Ile Glu Ser Ser Gln Asp Leu Glu Ala Tyr Val Ile Arg Tyr 805 810 815gat gca aaa cat gaa aca ttg gat gta tcc aat aat cta ttc cca gat 2496Asp Ala Lys His Glu Thr Leu Asp Val Ser Asn Asn Leu Phe Pro Asp 820 825 830att tct cct gtg aat gca tgc gga gaa cca aat cgt tgt gcg gca cta 2544Ile Ser Pro Val Asn Ala Cys Gly Glu Pro Asn Arg Cys Ala Ala Leu 835 840 845caa tac ctg gat gaa aac cca agg tta gaa tgt agt tcg ata caa gat 2592Gln Tyr Leu Asp Glu Asn Pro Arg Leu Glu Cys Ser Ser Ile Gln Asp 850 855 860ggc att tta tct gat tcg cat tca ttt tct ctc aat ata gat aca ggt 2640Gly Ile Leu Ser Asp Ser His Ser Phe Ser Leu Asn Ile Asp Thr Gly865 870 875 880tct att gat tac gat gag aac gta ggt att tgg gtg ttg ttt aaa att 2688Ser Ile Asp Tyr Asp Glu Asn Val Gly Ile Trp Val Leu Phe Lys Ile 885 890 895tcc aca ccg gaa ggg tat gcg aaa ttt gga aac cta gaa gtg att gaa 2736Ser Thr Pro Glu Gly Tyr Ala Lys Phe Gly Asn Leu Glu Val Ile Glu 900 905 910gat ggc cta gtc att gga gaa gca tta gcc cgt gtg aaa cgt caa gaa 2784Asp Gly Leu Val Ile Gly Glu Ala Leu Ala Arg Val Lys Arg Gln Glu 915 920 925acg aag tgg aga aac aag ttg aca caa ctg cga acg gaa aca caa gcg 2832Thr Lys Trp Arg Asn Lys Leu Thr Gln Leu Arg Thr Glu Thr Gln Ala 930 935 940att tat aca cga gca aaa caa gcc att gat aat tta ttc aca aat gca 2880Ile Tyr Thr Arg Ala Lys Gln Ala Ile Asp Asn Leu Phe Thr Asn Ala945 950 955 960cag gac tct cac tta aaa ata ggt gct aca ttc gcg tca att gtg gcc 2928Gln Asp Ser His Leu Lys Ile Gly Ala Thr Phe Ala Ser Ile Val Ala 965 970 975gcg cga aag att gtc caa tca ata cgt gaa gcg tat atg tca tgg tta 2976Ala Arg Lys Ile Val Gln Ser Ile Arg Glu Ala Tyr Met Ser Trp Leu 980 985 990tct atc gtc cca agt gta aat tat cct att ttc aca gag ttg aat gaa 3024Ser Ile Val Pro Ser Val Asn Tyr Pro Ile Phe Thr Glu Leu Asn Glu 995 1000 1005aga gta cag cga gca ttt cga tta tat gat gta cga aat gtc gta cgt 3072Arg Val Gln Arg Ala Phe Arg Leu Tyr Asp Val Arg Asn Val Val Arg 1010 1015 1020aat ggc cga ttc ttg agt gga gta tcg gat tgg att gtg aca tct gat 3120Asn Gly Arg Phe Leu Ser Gly Val Ser Asp Trp Ile Val Thr Ser Asp1025 1030 1035 1040gta aag gta caa gaa gaa aat ggg aac aac gta tta gtt ctt tcc aat 3168Val Lys Val Gln Glu Glu Asn Gly Asn Asn Val Leu Val Leu Ser Asn 1045 1050 1055tgg gat gca caa gta tta caa tgt ctg aat ctc tac gaa gac cat ggg 3216Trp Asp Ala Gln Val Leu Gln Cys Leu Asn Leu Tyr Glu Asp His Gly 1060 1065 1070tat atc tta cgc gta aca gca cgt aag gaa gga ctc gga gaa gga tat 3264Tyr Ile Leu Arg Val Thr Ala Arg Lys Glu Gly Leu Gly Glu Gly Tyr 1075 1080 1085ata aca atc act gat gaa gaa ggg cat aca gat caa ttg aca ttt ggt 3312Ile Thr Ile Thr Asp Glu Glu Gly His Thr Asp Gln Leu Thr Phe Gly 1090 1095 1100gga tgt gag gag ata gat tca tcc aat tct ttc gta tct aca ggt tat 3360Gly Cys Glu Glu Ile Asp Ser Ser Asn Ser Phe Val Ser Thr Gly Tyr1105 1110 1115 1120att aca aaa gag cta gaa ttc ttc cca gat aca gag aaa gtg cgc atc 3408Ile Thr Lys Glu Leu Glu Phe Phe Pro Asp Thr Glu Lys Val Arg Ile 1125 1130 1135gaa att gga gaa aca gaa gga aca ttc cag gta gaa agt gtg gaa tta 3456Glu Ile Gly Glu Thr Glu Gly Thr Phe Gln Val Glu Ser Val Glu Leu 1140 1145 1150ttt ttg atg gaa gac ata tgc 3477Phe Leu Met Glu Asp Ile Cys 1155191159PRTBacillus thuringiensis 19Met Asp Ile Arg Asn Gln Lys Lys Ser Glu Glu Ile His Pro Thr Leu1 5 10 15 Asn Glu Ser Ser Ser Asn Thr Thr Ser Lys Tyr Pro Leu Ala Ser Asp 20 25 30 Leu Ile Lys Gln Tyr Gln Asn Met Asn Tyr Lys Asp Ser Leu Asn Ile 35 40 45 Ile Glu Glu Asn Asn Val Ile Asp Pro Val Ser Gly Thr Ala Ala Leu 50 55 60 Val Thr Ala Arg Lys Ile Gly Gly Lys Ile Ile Lys Lys Leu Gly Glu65 70 75 80 Ala Ala Leu Ser Lys Ile Leu Lys Glu Ile Leu Gly Tyr Leu Trp Pro 85 90 95 Thr Ser Gly Glu Asp Asp Ser Trp Thr Asp Met Met Thr Ala Val Glu 100 105 110 Glu Leu Ile Asp Gln Lys Ile Gln Glu Gln Val Glu Leu Asp Ala Leu 115 120 125 Thr Glu Leu Glu Lys Ile Gly Glu Ala Val Glu Ala Tyr Tyr Ile Ala 130 135 140 Leu Asp Asp Trp Glu Pro Val Pro Glu Asp Met Phe Ser Leu Ser Glu145 150 155 160 Val Ile Lys Arg Tyr Asp Phe Ala Gln Gln Leu Ala Arg Ala Ser Met 165 170 175 Pro Glu Phe Lys Lys Lys Gly Tyr Glu Ile Pro Leu Leu Ala Thr Tyr 180 185 190 Ala Asn Ala Ala Asn Val His Leu Leu Leu Met Arg Asp Met Gln Ile 195 200 205 Tyr Gly Glu Arg Trp Gly Ile Pro Lys Glu Asp Ile Glu Leu Tyr Leu 210 215 220 Ser Glu Gln Glu Asn Phe Thr Ser Glu Tyr Thr Asp His Cys Val Lys225 230 235 240 Tyr Tyr Asn Glu Gly Leu Asn Gln Leu Lys Asn Lys Ser Gly Val Ser 245 250 255 Gly Leu Val Trp Glu Asn Tyr Asn Arg Phe Arg Thr Glu Met Thr Ile 260 265 270 Leu Val Leu Asp Ile Val Ala Val Phe Pro Arg Tyr Asn Val Ile Glu 275 280 285 Tyr

Pro Ile Asp Ser Thr Val Glu Leu Thr Arg Thr Ile Tyr Leu Asp 290 295 300 Pro Leu Gly Tyr Thr Gly Asn Ser Asn Asp Glu His Pro Glu Tyr Tyr305 310 315 320 Ala Ser Thr Lys Ser Phe Ser Ser Ile Glu Ser Arg Ala Ile Pro Ala 325 330 335 Pro Thr Leu Phe Gln Trp Ile Thr Glu Leu Gln Val Tyr Ser Ala Lys 340 345 350 Gly Ser His Gly Ser Thr Tyr Thr Thr Trp Trp Thr Gly His Lys Val 355 360 365 Thr Ala Lys Pro Thr Asn Gly Gly Leu Glu Ser Lys Tyr Asp Phe Gly 370 375 380 Ser Ser Ser Gly Ser Gln Asn Lys Asp Val Phe Ala Leu Asp Gly Lys385 390 395 400 Asp Val Tyr Asp Ser Gln Ser Met Leu Thr Ser Ile Ser Tyr Ser Gly 405 410 415 Ile Arg Tyr Phe Gly Cys Pro Gln Phe Lys Leu Asn Trp Ile Asn Lys 420 425 430 Asn Asn Glu Leu Ala Glu Gln Ile Phe Asn Tyr Ser Ser Asn Val Gly 435 440 445 Ser Ser Phe Ser Glu Tyr Arg Tyr Ser Lys Asp Glu Leu Pro Ile Glu 450 455 460 Leu Leu Ala Ser Pro Ile Tyr Gly Asp Ile Glu Glu Tyr Ser His Arg465 470 475 480 Leu Ser His Val Ser Glu Val Ile Lys Asp Tyr Gly Gln Gly Ile Ile 485 490 495 Pro Val Leu Gly Phe Thr His Val Ser Val Ser Arg Asp Asn Arg Ile 500 505 510 Tyr Ser Asp Lys Ile Thr Gln Ile Pro Ala Val Lys Met Tyr Glu Leu 515 520 525 Val Ser Pro Ala Val Val Val Lys Gly Pro Gly Ser Thr Gly Gly Asp 530 535 540 Leu Val Lys Arg Gly Ser Ser Gly Asn Ile Gly Ser Met Asn Val Thr545 550 555 560 Val Asn Ser Pro Leu Ser Gln Lys Tyr Arg Val Arg Val Arg Tyr Ala 565 570 575 Thr Asn Ala Ser Gly Gln Leu Asn Val Ser Ile Asn Asp Lys Leu Thr 580 585 590 Leu Gln Lys Pro Phe Glu Arg Thr Gly Thr Thr Ile Gly Glu Gly Thr 595 600 605 Asp Leu Ser Tyr Asp Ser Phe Gly Tyr Leu Glu Tyr Ser Thr Thr Ile 610 615 620 Gln Phe Pro Asn Glu His Pro Lys Ile Thr Phe Asn Leu Ser His Trp625 630 635 640 Ser Gly Ser Gly Ala Phe Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val 645 650 655 Asp Glu Asn Tyr Asp Glu Arg Val Thr Leu Glu Lys Ala Gln Lys Ala 660 665 670 Val Asn Ala Leu Phe Thr Ala Gly Arg Asn Ala Leu Gln Lys Asp Val 675 680 685 Thr Asp Phe Lys Val Asp Gln Val Ser Ile Leu Val Asp Cys Ile Pro 690 695 700 Gly Glu Leu Tyr Pro Asn Glu Lys Arg Glu Leu Leu Ser Leu Val Lys705 710 715 720 Tyr Ala Lys Arg Leu Ser Tyr Ser Arg Asn Leu Leu Leu Asp Pro Thr 725 730 735 Phe Asp Ser Ile Asn Ser Pro Asp Glu Asn Gly Trp Tyr Gly Ser Asn 740 745 750 Gly Ile Ala Ile Gly Asn Gly Asn Phe Val Phe Lys Gly Asn Tyr Leu 755 760 765 Ile Phe Ser Gly Thr Asn Asp Thr Gln Tyr Pro Thr Tyr Leu Tyr Gln 770 775 780 Lys Ile Asp Glu Ser Lys Leu Lys Glu Tyr Thr Arg Tyr Lys Leu Arg785 790 795 800 Gly Phe Ile Glu Ser Ser Gln Asp Leu Glu Ala Tyr Val Ile Arg Tyr 805 810 815 Asp Ala Lys His Glu Thr Leu Asp Val Ser Asn Asn Leu Phe Pro Asp 820 825 830 Ile Ser Pro Val Asn Ala Cys Gly Glu Pro Asn Arg Cys Ala Ala Leu 835 840 845 Gln Tyr Leu Asp Glu Asn Pro Arg Leu Glu Cys Ser Ser Ile Gln Asp 850 855 860 Gly Ile Leu Ser Asp Ser His Ser Phe Ser Leu Asn Ile Asp Thr Gly865 870 875 880 Ser Ile Asp Tyr Asp Glu Asn Val Gly Ile Trp Val Leu Phe Lys Ile 885 890 895 Ser Thr Pro Glu Gly Tyr Ala Lys Phe Gly Asn Leu Glu Val Ile Glu 900 905 910 Asp Gly Leu Val Ile Gly Glu Ala Leu Ala Arg Val Lys Arg Gln Glu 915 920 925 Thr Lys Trp Arg Asn Lys Leu Thr Gln Leu Arg Thr Glu Thr Gln Ala 930 935 940 Ile Tyr Thr Arg Ala Lys Gln Ala Ile Asp Asn Leu Phe Thr Asn Ala945 950 955 960 Gln Asp Ser His Leu Lys Ile Gly Ala Thr Phe Ala Ser Ile Val Ala 965 970 975 Ala Arg Lys Ile Val Gln Ser Ile Arg Glu Ala Tyr Met Ser Trp Leu 980 985 990 Ser Ile Val Pro Ser Val Asn Tyr Pro Ile Phe Thr Glu Leu Asn Glu 995 1000 1005 Arg Val Gln Arg Ala Phe Arg Leu Tyr Asp Val Arg Asn Val Val Arg 1010 1015 1020 Asn Gly Arg Phe Leu Ser Gly Val Ser Asp Trp Ile Val Thr Ser Asp1025 1030 1035 1040 Val Lys Val Gln Glu Glu Asn Gly Asn Asn Val Leu Val Leu Ser Asn 1045 1050 1055 Trp Asp Ala Gln Val Leu Gln Cys Leu Asn Leu Tyr Glu Asp His Gly 1060 1065 1070 Tyr Ile Leu Arg Val Thr Ala Arg Lys Glu Gly Leu Gly Glu Gly Tyr 1075 1080 1085 Ile Thr Ile Thr Asp Glu Glu Gly His Thr Asp Gln Leu Thr Phe Gly 1090 1095 1100 Gly Cys Glu Glu Ile Asp Ser Ser Asn Ser Phe Val Ser Thr Gly Tyr1105 1110 1115 1120 Ile Thr Lys Glu Leu Glu Phe Phe Pro Asp Thr Glu Lys Val Arg Ile 1125 1130 1135 Glu Ile Gly Glu Thr Glu Gly Thr Phe Gln Val Glu Ser Val Glu Leu 1140 1145 1150 Phe Leu Met Glu Asp Ile Cys 1155 203438DNABacillus thuringiensisCDS(1)...(3438) 20atg aaa aaa att aag ttt aaa tat tgt ata caa gga gac ttg aat atg 48Met Lys Lys Ile Lys Phe Lys Tyr Cys Ile Gln Gly Asp Leu Asn Met1 5 10 15aat caa aaa aac tat gat att ata ggt gct tcg aca aac ggt aca aac 96Asn Gln Lys Asn Tyr Asp Ile Ile Gly Ala Ser Thr Asn Gly Thr Asn 20 25 30aaa tta ctt gaa ggt tat aac att ata atc agt ccc tac gaa gct cca 144Lys Leu Leu Glu Gly Tyr Asn Ile Ile Ile Ser Pro Tyr Glu Ala Pro 35 40 45aca tcc gtt act aca act att gaa att act gga acc ata cta agc gat 192Thr Ser Val Thr Thr Thr Ile Glu Ile Thr Gly Thr Ile Leu Ser Asp 50 55 60tta ggt gtt cca gga gca tca tca gtt agt tta ctt ttg aat aaa ctt 240Leu Gly Val Pro Gly Ala Ser Ser Val Ser Leu Leu Leu Asn Lys Leu65 70 75 80ata aat cta tta tgg cca aat gat acc aat act gtg tgg ggg aca ttc 288Ile Asn Leu Leu Trp Pro Asn Asp Thr Asn Thr Val Trp Gly Thr Phe 85 90 95gga aaa gaa acc gct gat ctt cta aat gaa gtg tta tct cca aat gat 336Gly Lys Glu Thr Ala Asp Leu Leu Asn Glu Val Leu Ser Pro Asn Asp 100 105 110cca gta gta aca gat gca aat act aat tta gca gga cta aat gac tcc 384Pro Val Val Thr Asp Ala Asn Thr Asn Leu Ala Gly Leu Asn Asp Ser 115 120 125ctt aac tta tat tta aat gaa ctt gaa ata tgg aaa aaa gac ccc aac 432Leu Asn Leu Tyr Leu Asn Glu Leu Glu Ile Trp Lys Lys Asp Pro Asn 130 135 140aac gca act acc caa agg aat gtc aca caa tac ttt gtt agt ttg aat 480Asn Ala Thr Thr Gln Arg Asn Val Thr Gln Tyr Phe Val Ser Leu Asn145 150 155 160ttg gat ttt aca cat gat atg cct tca ttt gct gta cct gga tat gaa 528Leu Asp Phe Thr His Asp Met Pro Ser Phe Ala Val Pro Gly Tyr Glu 165 170 175acg aag tta tta aca att tat gca caa gct gca aat ctt cat tta ctt 576Thr Lys Leu Leu Thr Ile Tyr Ala Gln Ala Ala Asn Leu His Leu Leu 180 185 190tta tta aga gat gct tct agg ttt gga gaa ggt tgg gga ctg act caa 624Leu Leu Arg Asp Ala Ser Arg Phe Gly Glu Gly Trp Gly Leu Thr Gln 195 200 205gaa atc ata gat tct aac tat aat aat caa tta aaa ttg aca gaa aaa 672Glu Ile Ile Asp Ser Asn Tyr Asn Asn Gln Leu Lys Leu Thr Glu Lys 210 215 220tac acg gac cat tgt gta aag tgg tac aac gca gga tta gaa aaa tta 720Tyr Thr Asp His Cys Val Lys Trp Tyr Asn Ala Gly Leu Glu Lys Leu225 230 235 240aaa gga aat tta act ggg gaa aat tgg tac act tat aat aga ttt cgt 768Lys Gly Asn Leu Thr Gly Glu Asn Trp Tyr Thr Tyr Asn Arg Phe Arg 245 250 255aga gaa atg acg tta atg gtg tta gac gta gtt gca tta ttt cca aac 816Arg Glu Met Thr Leu Met Val Leu Asp Val Val Ala Leu Phe Pro Asn 260 265 270tat gat aca cga atg tac ccg atc gca acg tca tca gaa ctt aca aga 864Tyr Asp Thr Arg Met Tyr Pro Ile Ala Thr Ser Ser Glu Leu Thr Arg 275 280 285atg att tat aca gat cca atc gct tat aca caa agc gat cca tgg tac 912Met Ile Tyr Thr Asp Pro Ile Ala Tyr Thr Gln Ser Asp Pro Trp Tyr 290 295 300aag ata aca tct ctt tct ttt tca aat att gaa aac agc gcg att cca 960Lys Ile Thr Ser Leu Ser Phe Ser Asn Ile Glu Asn Ser Ala Ile Pro305 310 315 320agt cct tct ttc ttc aag tgg cta aga tcc gtt tca att aat agc cag 1008Ser Pro Ser Phe Phe Lys Trp Leu Arg Ser Val Ser Ile Asn Ser Gln 325 330 335tgg tgg ggc agt ggt cct aat caa acc tac tat tgg gtt gga cat gaa 1056Trp Trp Gly Ser Gly Pro Asn Gln Thr Tyr Tyr Trp Val Gly His Glu 340 345 350tta gta tat tct aat tca aat tct aat caa tca ctt aag gtt aaa tat 1104Leu Val Tyr Ser Asn Ser Asn Ser Asn Gln Ser Leu Lys Val Lys Tyr 355 360 365gga gac cct aat tct tat att gag ccc cct gat tct ttc agt ttt tct 1152Gly Asp Pro Asn Ser Tyr Ile Glu Pro Pro Asp Ser Phe Ser Phe Ser 370 375 380tct acg gat gtt tac aga acc att tct gtt gtt aga aat tca gta agt 1200Ser Thr Asp Val Tyr Arg Thr Ile Ser Val Val Arg Asn Ser Val Ser385 390 395 400aat tat ata gta agt gaa gtt caa ttc aat tca att agt aat aca aat 1248Asn Tyr Ile Val Ser Glu Val Gln Phe Asn Ser Ile Ser Asn Thr Asn 405 410 415caa att agt gaa gaa att tat aaa cat caa tca aat tgg agt aga aaa 1296Gln Ile Ser Glu Glu Ile Tyr Lys His Gln Ser Asn Trp Ser Arg Lys 420 425 430gaa acc aaa gat tca att aca gaa cta tcc tta gct gct aat ccc cca 1344Glu Thr Lys Asp Ser Ile Thr Glu Leu Ser Leu Ala Ala Asn Pro Pro 435 440 445aca aca ttt gga aat gta gca gaa tac agt cat aga tta gca tat att 1392Thr Thr Phe Gly Asn Val Ala Glu Tyr Ser His Arg Leu Ala Tyr Ile 450 455 460tca gag gca tac caa agt caa aac cca tca aaa tac cca acc tac att 1440Ser Glu Ala Tyr Gln Ser Gln Asn Pro Ser Lys Tyr Pro Thr Tyr Ile465 470 475 480cct gta ttc ggt tgg acg cat aca agc gta cgt tac gat aat aaa att 1488Pro Val Phe Gly Trp Thr His Thr Ser Val Arg Tyr Asp Asn Lys Ile 485 490 495ttc ccg gac aaa atc act caa att cca gct gtt aaa agc tct tca gct 1536Phe Pro Asp Lys Ile Thr Gln Ile Pro Ala Val Lys Ser Ser Ser Ala 500 505 510caa ggt gga tca tgg aaa aat ata gtg aaa ggt ccc ggg ttt act gga 1584Gln Gly Gly Ser Trp Lys Asn Ile Val Lys Gly Pro Gly Phe Thr Gly 515 520 525gga gat gtg aca act gca gtt tcg cca gca act tta acc gac ata ata 1632Gly Asp Val Thr Thr Ala Val Ser Pro Ala Thr Leu Thr Asp Ile Ile 530 535 540aaa ata caa gtt act cta gat cca aat tca ctt tca caa aaa tat cgt 1680Lys Ile Gln Val Thr Leu Asp Pro Asn Ser Leu Ser Gln Lys Tyr Arg545 550 555 560gca cga ctt cgc tat gct tcc aat gca ttt gta gca gct act ttg tat 1728Ala Arg Leu Arg Tyr Ala Ser Asn Ala Phe Val Ala Ala Thr Leu Tyr 565 570 575aca aat aca agt agt aat tat aat ttt gaa ctt aca aaa ggt aca act 1776Thr Asn Thr Ser Ser Asn Tyr Asn Phe Glu Leu Thr Lys Gly Thr Thr 580 585 590gaa cag ttt aca aca tat aat tca tac cag tat gta gat atc cca ggt 1824Glu Gln Phe Thr Thr Tyr Asn Ser Tyr Gln Tyr Val Asp Ile Pro Gly 595 600 605tca ata caa ttt aat aat act tct gat aca gtg tct gtt tat ttg cat 1872Ser Ile Gln Phe Asn Asn Thr Ser Asp Thr Val Ser Val Tyr Leu His 610 615 620atg gat tca aca act aat gca aac gtt cat gta gat aga att gaa ttc 1920Met Asp Ser Thr Thr Asn Ala Asn Val His Val Asp Arg Ile Glu Phe625 630 635 640att cca gta gat gaa cag tac gat gaa aga gta aca cta gaa aaa gca 1968Ile Pro Val Asp Glu Gln Tyr Asp Glu Arg Val Thr Leu Glu Lys Ala 645 650 655cag aaa gcc gtg aat gcc ttg ttt aca gcg gga aga cat gca ctc caa 2016Gln Lys Ala Val Asn Ala Leu Phe Thr Ala Gly Arg His Ala Leu Gln 660 665 670aca gat gtg aca gat tac aaa gtg gat caa gtg tca att tta gtg gat 2064Thr Asp Val Thr Asp Tyr Lys Val Asp Gln Val Ser Ile Leu Val Asp 675 680 685tgt gta tca ggg gag tta tat cca aat gag aaa cgc gaa cta ctc agt 2112Cys Val Ser Gly Glu Leu Tyr Pro Asn Glu Lys Arg Glu Leu Leu Ser 690 695 700tta gtc aaa tac gca aaa cgt ttg agc tat tct cgt aat tta ctc cta 2160Leu Val Lys Tyr Ala Lys Arg Leu Ser Tyr Ser Arg Asn Leu Leu Leu705 710 715 720gat cca aca ttc gat tct atc aat tca tca gat aag aat ggc tgg tac 2208Asp Pro Thr Phe Asp Ser Ile Asn Ser Ser Asp Lys Asn Gly Trp Tyr 725 730 735ggg agt aat ggt att gca att agc agt ggg aat ttt gta ttc aaa ggg 2256Gly Ser Asn Gly Ile Ala Ile Ser Ser Gly Asn Phe Val Phe Lys Gly 740 745 750aac tat tta atc ttc tca ggt aca aat gat gaa caa tat cca acc tat 2304Asn Tyr Leu Ile Phe Ser Gly Thr Asn Asp Glu Gln Tyr Pro Thr Tyr 755 760 765ctc tat caa aaa ata gac gaa tct aag tta aaa gaa tat aca cgt tat 2352Leu Tyr Gln Lys Ile Asp Glu Ser Lys Leu Lys Glu Tyr Thr Arg Tyr 770 775 780aaa ctg aga ggc ttt ata gaa aat agt caa gat tta gaa gca tat gtc 2400Lys Leu Arg Gly Phe Ile Glu Asn Ser Gln Asp Leu Glu Ala Tyr Val785 790 795 800att cgc tat gat gcc aaa cat gaa aca ttg gat gta tcc aat aat cta 2448Ile Arg Tyr Asp Ala Lys His Glu Thr Leu Asp Val Ser Asn Asn Leu 805 810 815tta ccg gat att tct cct gta aat gca tgt gga gaa cca aat cgt tgt 2496Leu Pro Asp Ile Ser Pro Val Asn Ala Cys Gly Glu Pro Asn Arg Cys 820 825 830gtg gca tta caa tac ctg gat gaa aac cca aga tta gaa tgt agt tcg 2544Val Ala Leu Gln Tyr Leu Asp Glu Asn Pro Arg Leu Glu Cys Ser Ser 835 840 845gtt caa gat ggt att tta tct gat tcg cat tca ttt tct ctc aat ata 2592Val Gln Asp Gly Ile Leu Ser Asp Ser His Ser Phe Ser Leu Asn Ile 850 855 860gat aca ggt tct att gat ttc aat gag agc gta gga att tgg gtg ttg 2640Asp Thr Gly Ser Ile Asp Phe Asn Glu Ser Val Gly Ile Trp Val Leu865 870 875 880ttt aaa att tcc aca ccg gaa ggg tat gcg aaa ttt gga aac cta gaa 2688Phe Lys Ile Ser Thr Pro Glu Gly Tyr Ala Lys Phe Gly Asn Leu Glu 885 890 895gtg att gaa aat ggc cca gtc atc gga gaa gca tta gcc cgt gtg aaa 2736Val Ile Glu Asn Gly Pro Val Ile Gly Glu Ala Leu Ala Arg Val Lys 900 905 910cgc caa gaa aca aag tgg aga aac cag ttg aca caa ctg aga acg gaa 2784Arg Gln Glu Thr Lys Trp Arg Asn Gln Leu Thr Gln Leu Arg Thr Glu 915 920 925aca caa gcg att tat aca cga gca aaa caa gcg ctg gat aat ctt ttt 2832Thr Gln Ala Ile Tyr Thr Arg Ala Lys Gln Ala Leu Asp Asn Leu Phe 930 935 940gcg aat gca caa gac tct cac tta aaa ata ggt acg aca ttt gcg gca 2880Ala Asn Ala Gln Asp Ser His Leu Lys Ile Gly Thr Thr Phe Ala Ala945 950 955

960att gtg gct gcg cga aag att gtc caa tcc ata cgc gaa gcg tat atg 2928Ile Val Ala Ala Arg Lys Ile Val Gln Ser Ile Arg Glu Ala Tyr Met 965 970 975tca tgg tta tct gtt gtt cca ggt gta aat tat cct atc ttt aca gag 2976Ser Trp Leu Ser Val Val Pro Gly Val Asn Tyr Pro Ile Phe Thr Glu 980 985 990ttg act gag aga gta cag caa gca ttt caa tta tat gat gta cga aat 3024Leu Thr Glu Arg Val Gln Gln Ala Phe Gln Leu Tyr Asp Val Arg Asn 995 1000 1005gtc gtg cgt aat ggc caa ttc ctt agt ggc tta tcc gat tgg att gta 3072Val Val Arg Asn Gly Gln Phe Leu Ser Gly Leu Ser Asp Trp Ile Val 1010 1015 1020aca cct gac gtc aag gta caa gaa gac aat ggg aat aac gta ttg gtt 3120Thr Pro Asp Val Lys Val Gln Glu Asp Asn Gly Asn Asn Val Leu Val1025 1030 1035 1040ctt tct aat tgg gat gcg caa gta tta caa tgt ctg aag ctc tat caa 3168Leu Ser Asn Trp Asp Ala Gln Val Leu Gln Cys Leu Lys Leu Tyr Gln 1045 1050 1055gat cgc ggg tat atc tta cgt gta acg gca cgt aag gaa gga ttg gga 3216Asp Arg Gly Tyr Ile Leu Arg Val Thr Ala Arg Lys Glu Gly Leu Gly 1060 1065 1070gaa gga tac gta aca att acg gat gaa gaa ggg aat aca gat caa ttg 3264Glu Gly Tyr Val Thr Ile Thr Asp Glu Glu Gly Asn Thr Asp Gln Leu 1075 1080 1085acg ttt ggt gca tgt gag gag ata gat gca tct aat gcg ttc att tcc 3312Thr Phe Gly Ala Cys Glu Glu Ile Asp Ala Ser Asn Ala Phe Ile Ser 1090 1095 1100aca ggt tat att aca aaa gaa ctg gaa ttc ttc cca gat aca gag aaa 3360Thr Gly Tyr Ile Thr Lys Glu Leu Glu Phe Phe Pro Asp Thr Glu Lys1105 1110 1115 1120gtg cgt ata gaa att gga gaa aca gaa gga aca ttc cag gtg gaa agt 3408Val Arg Ile Glu Ile Gly Glu Thr Glu Gly Thr Phe Gln Val Glu Ser 1125 1130 1135gta gaa tta ttc ttg atg gaa gat cta tgt 3438Val Glu Leu Phe Leu Met Glu Asp Leu Cys 1140 1145211146PRTBacillus thuringiensis 21Met Lys Lys Ile Lys Phe Lys Tyr Cys Ile Gln Gly Asp Leu Asn Met1 5 10 15 Asn Gln Lys Asn Tyr Asp Ile Ile Gly Ala Ser Thr Asn Gly Thr Asn 20 25 30 Lys Leu Leu Glu Gly Tyr Asn Ile Ile Ile Ser Pro Tyr Glu Ala Pro 35 40 45 Thr Ser Val Thr Thr Thr Ile Glu Ile Thr Gly Thr Ile Leu Ser Asp 50 55 60 Leu Gly Val Pro Gly Ala Ser Ser Val Ser Leu Leu Leu Asn Lys Leu65 70 75 80 Ile Asn Leu Leu Trp Pro Asn Asp Thr Asn Thr Val Trp Gly Thr Phe 85 90 95 Gly Lys Glu Thr Ala Asp Leu Leu Asn Glu Val Leu Ser Pro Asn Asp 100 105 110 Pro Val Val Thr Asp Ala Asn Thr Asn Leu Ala Gly Leu Asn Asp Ser 115 120 125 Leu Asn Leu Tyr Leu Asn Glu Leu Glu Ile Trp Lys Lys Asp Pro Asn 130 135 140 Asn Ala Thr Thr Gln Arg Asn Val Thr Gln Tyr Phe Val Ser Leu Asn145 150 155 160 Leu Asp Phe Thr His Asp Met Pro Ser Phe Ala Val Pro Gly Tyr Glu 165 170 175 Thr Lys Leu Leu Thr Ile Tyr Ala Gln Ala Ala Asn Leu His Leu Leu 180 185 190 Leu Leu Arg Asp Ala Ser Arg Phe Gly Glu Gly Trp Gly Leu Thr Gln 195 200 205 Glu Ile Ile Asp Ser Asn Tyr Asn Asn Gln Leu Lys Leu Thr Glu Lys 210 215 220 Tyr Thr Asp His Cys Val Lys Trp Tyr Asn Ala Gly Leu Glu Lys Leu225 230 235 240 Lys Gly Asn Leu Thr Gly Glu Asn Trp Tyr Thr Tyr Asn Arg Phe Arg 245 250 255 Arg Glu Met Thr Leu Met Val Leu Asp Val Val Ala Leu Phe Pro Asn 260 265 270 Tyr Asp Thr Arg Met Tyr Pro Ile Ala Thr Ser Ser Glu Leu Thr Arg 275 280 285 Met Ile Tyr Thr Asp Pro Ile Ala Tyr Thr Gln Ser Asp Pro Trp Tyr 290 295 300 Lys Ile Thr Ser Leu Ser Phe Ser Asn Ile Glu Asn Ser Ala Ile Pro305 310 315 320 Ser Pro Ser Phe Phe Lys Trp Leu Arg Ser Val Ser Ile Asn Ser Gln 325 330 335 Trp Trp Gly Ser Gly Pro Asn Gln Thr Tyr Tyr Trp Val Gly His Glu 340 345 350 Leu Val Tyr Ser Asn Ser Asn Ser Asn Gln Ser Leu Lys Val Lys Tyr 355 360 365 Gly Asp Pro Asn Ser Tyr Ile Glu Pro Pro Asp Ser Phe Ser Phe Ser 370 375 380 Ser Thr Asp Val Tyr Arg Thr Ile Ser Val Val Arg Asn Ser Val Ser385 390 395 400 Asn Tyr Ile Val Ser Glu Val Gln Phe Asn Ser Ile Ser Asn Thr Asn 405 410 415 Gln Ile Ser Glu Glu Ile Tyr Lys His Gln Ser Asn Trp Ser Arg Lys 420 425 430 Glu Thr Lys Asp Ser Ile Thr Glu Leu Ser Leu Ala Ala Asn Pro Pro 435 440 445 Thr Thr Phe Gly Asn Val Ala Glu Tyr Ser His Arg Leu Ala Tyr Ile 450 455 460 Ser Glu Ala Tyr Gln Ser Gln Asn Pro Ser Lys Tyr Pro Thr Tyr Ile465 470 475 480 Pro Val Phe Gly Trp Thr His Thr Ser Val Arg Tyr Asp Asn Lys Ile 485 490 495 Phe Pro Asp Lys Ile Thr Gln Ile Pro Ala Val Lys Ser Ser Ser Ala 500 505 510 Gln Gly Gly Ser Trp Lys Asn Ile Val Lys Gly Pro Gly Phe Thr Gly 515 520 525 Gly Asp Val Thr Thr Ala Val Ser Pro Ala Thr Leu Thr Asp Ile Ile 530 535 540 Lys Ile Gln Val Thr Leu Asp Pro Asn Ser Leu Ser Gln Lys Tyr Arg545 550 555 560 Ala Arg Leu Arg Tyr Ala Ser Asn Ala Phe Val Ala Ala Thr Leu Tyr 565 570 575 Thr Asn Thr Ser Ser Asn Tyr Asn Phe Glu Leu Thr Lys Gly Thr Thr 580 585 590 Glu Gln Phe Thr Thr Tyr Asn Ser Tyr Gln Tyr Val Asp Ile Pro Gly 595 600 605 Ser Ile Gln Phe Asn Asn Thr Ser Asp Thr Val Ser Val Tyr Leu His 610 615 620 Met Asp Ser Thr Thr Asn Ala Asn Val His Val Asp Arg Ile Glu Phe625 630 635 640 Ile Pro Val Asp Glu Gln Tyr Asp Glu Arg Val Thr Leu Glu Lys Ala 645 650 655 Gln Lys Ala Val Asn Ala Leu Phe Thr Ala Gly Arg His Ala Leu Gln 660 665 670 Thr Asp Val Thr Asp Tyr Lys Val Asp Gln Val Ser Ile Leu Val Asp 675 680 685 Cys Val Ser Gly Glu Leu Tyr Pro Asn Glu Lys Arg Glu Leu Leu Ser 690 695 700 Leu Val Lys Tyr Ala Lys Arg Leu Ser Tyr Ser Arg Asn Leu Leu Leu705 710 715 720 Asp Pro Thr Phe Asp Ser Ile Asn Ser Ser Asp Lys Asn Gly Trp Tyr 725 730 735 Gly Ser Asn Gly Ile Ala Ile Ser Ser Gly Asn Phe Val Phe Lys Gly 740 745 750 Asn Tyr Leu Ile Phe Ser Gly Thr Asn Asp Glu Gln Tyr Pro Thr Tyr 755 760 765 Leu Tyr Gln Lys Ile Asp Glu Ser Lys Leu Lys Glu Tyr Thr Arg Tyr 770 775 780 Lys Leu Arg Gly Phe Ile Glu Asn Ser Gln Asp Leu Glu Ala Tyr Val785 790 795 800 Ile Arg Tyr Asp Ala Lys His Glu Thr Leu Asp Val Ser Asn Asn Leu 805 810 815 Leu Pro Asp Ile Ser Pro Val Asn Ala Cys Gly Glu Pro Asn Arg Cys 820 825 830 Val Ala Leu Gln Tyr Leu Asp Glu Asn Pro Arg Leu Glu Cys Ser Ser 835 840 845 Val Gln Asp Gly Ile Leu Ser Asp Ser His Ser Phe Ser Leu Asn Ile 850 855 860 Asp Thr Gly Ser Ile Asp Phe Asn Glu Ser Val Gly Ile Trp Val Leu865 870 875 880 Phe Lys Ile Ser Thr Pro Glu Gly Tyr Ala Lys Phe Gly Asn Leu Glu 885 890 895 Val Ile Glu Asn Gly Pro Val Ile Gly Glu Ala Leu Ala Arg Val Lys 900 905 910 Arg Gln Glu Thr Lys Trp Arg Asn Gln Leu Thr Gln Leu Arg Thr Glu 915 920 925 Thr Gln Ala Ile Tyr Thr Arg Ala Lys Gln Ala Leu Asp Asn Leu Phe 930 935 940 Ala Asn Ala Gln Asp Ser His Leu Lys Ile Gly Thr Thr Phe Ala Ala945 950 955 960 Ile Val Ala Ala Arg Lys Ile Val Gln Ser Ile Arg Glu Ala Tyr Met 965 970 975 Ser Trp Leu Ser Val Val Pro Gly Val Asn Tyr Pro Ile Phe Thr Glu 980 985 990 Leu Thr Glu Arg Val Gln Gln Ala Phe Gln Leu Tyr Asp Val Arg Asn 995 1000 1005 Val Val Arg Asn Gly Gln Phe Leu Ser Gly Leu Ser Asp Trp Ile Val 1010 1015 1020 Thr Pro Asp Val Lys Val Gln Glu Asp Asn Gly Asn Asn Val Leu Val1025 1030 1035 1040 Leu Ser Asn Trp Asp Ala Gln Val Leu Gln Cys Leu Lys Leu Tyr Gln 1045 1050 1055 Asp Arg Gly Tyr Ile Leu Arg Val Thr Ala Arg Lys Glu Gly Leu Gly 1060 1065 1070 Glu Gly Tyr Val Thr Ile Thr Asp Glu Glu Gly Asn Thr Asp Gln Leu 1075 1080 1085 Thr Phe Gly Ala Cys Glu Glu Ile Asp Ala Ser Asn Ala Phe Ile Ser 1090 1095 1100 Thr Gly Tyr Ile Thr Lys Glu Leu Glu Phe Phe Pro Asp Thr Glu Lys1105 1110 1115 1120 Val Arg Ile Glu Ile Gly Glu Thr Glu Gly Thr Phe Gln Val Glu Ser 1125 1130 1135 Val Glu Leu Phe Leu Met Glu Asp Leu Cys 1140 1145 223393DNABacillus thuringiensisCDS(1)...(3393) 22atg aat caa aaa aac tat gat att ata ggt gct tcg aca aac ggt aca 48Met Asn Gln Lys Asn Tyr Asp Ile Ile Gly Ala Ser Thr Asn Gly Thr1 5 10 15aac aaa tta ctt gaa ggt tat aac att ata atc agt ccc tac gaa gct 96Asn Lys Leu Leu Glu Gly Tyr Asn Ile Ile Ile Ser Pro Tyr Glu Ala 20 25 30cca aca tcc gtt act aca act att gaa att act gga acc ata cta agc 144Pro Thr Ser Val Thr Thr Thr Ile Glu Ile Thr Gly Thr Ile Leu Ser 35 40 45gat tta ggt gtt cca gga gca tca tca gtt agt tta ctt ttg aat aaa 192Asp Leu Gly Val Pro Gly Ala Ser Ser Val Ser Leu Leu Leu Asn Lys 50 55 60ctt ata aat cta tta tgg cca aat gat acc aat act gtg tgg ggg aca 240Leu Ile Asn Leu Leu Trp Pro Asn Asp Thr Asn Thr Val Trp Gly Thr65 70 75 80ttc gga aaa gaa acc gct gat ctt cta aat gaa gtg tta tct cca aat 288Phe Gly Lys Glu Thr Ala Asp Leu Leu Asn Glu Val Leu Ser Pro Asn 85 90 95gat cca gta gta aca gat gca aat act aat tta gca gga cta aat gac 336Asp Pro Val Val Thr Asp Ala Asn Thr Asn Leu Ala Gly Leu Asn Asp 100 105 110tcc ctt aac tta tat tta aat gaa ctt gaa ata tgg aaa aaa gac ccc 384Ser Leu Asn Leu Tyr Leu Asn Glu Leu Glu Ile Trp Lys Lys Asp Pro 115 120 125aac aac gca act acc caa agg aat gtc aca caa tac ttt gtt agt ttg 432Asn Asn Ala Thr Thr Gln Arg Asn Val Thr Gln Tyr Phe Val Ser Leu 130 135 140aat ttg gat ttt aca cat gat atg cct tca ttt gct gta cct gga tat 480Asn Leu Asp Phe Thr His Asp Met Pro Ser Phe Ala Val Pro Gly Tyr145 150 155 160gaa acg aag tta tta aca att tat gca caa gct gca aat ctt cat tta 528Glu Thr Lys Leu Leu Thr Ile Tyr Ala Gln Ala Ala Asn Leu His Leu 165 170 175ctt tta tta aga gat gct tct agg ttt gga gaa ggt tgg gga ctg act 576Leu Leu Leu Arg Asp Ala Ser Arg Phe Gly Glu Gly Trp Gly Leu Thr 180 185 190caa gaa atc ata gat tct aac tat aat aat caa tta aaa ttg aca gaa 624Gln Glu Ile Ile Asp Ser Asn Tyr Asn Asn Gln Leu Lys Leu Thr Glu 195 200 205aaa tac acg gac cat tgt gta aag tgg tac aac gca gga tta gaa aaa 672Lys Tyr Thr Asp His Cys Val Lys Trp Tyr Asn Ala Gly Leu Glu Lys 210 215 220tta aaa gga aat tta act ggg gaa aat tgg tac act tat aat aga ttt 720Leu Lys Gly Asn Leu Thr Gly Glu Asn Trp Tyr Thr Tyr Asn Arg Phe225 230 235 240cgt aga gaa atg acg tta atg gtg tta gac gta gtt gca tta ttt cca 768Arg Arg Glu Met Thr Leu Met Val Leu Asp Val Val Ala Leu Phe Pro 245 250 255aac tat gat aca cga atg tac ccg atc gca acg tca tca gaa ctt aca 816Asn Tyr Asp Thr Arg Met Tyr Pro Ile Ala Thr Ser Ser Glu Leu Thr 260 265 270aga atg att tat aca gat cca atc gct tat aca caa agc gat cca tgg 864Arg Met Ile Tyr Thr Asp Pro Ile Ala Tyr Thr Gln Ser Asp Pro Trp 275 280 285tac aag ata aca tct ctt tct ttt tca aat att gaa aac agc gcg att 912Tyr Lys Ile Thr Ser Leu Ser Phe Ser Asn Ile Glu Asn Ser Ala Ile 290 295 300cca agt cct tct ttc ttc aag tgg cta aga tcc gtt tca att aat agc 960Pro Ser Pro Ser Phe Phe Lys Trp Leu Arg Ser Val Ser Ile Asn Ser305 310 315 320cag tgg tgg ggc agt ggt cct aat caa acc tac tat tgg gtt gga cat 1008Gln Trp Trp Gly Ser Gly Pro Asn Gln Thr Tyr Tyr Trp Val Gly His 325 330 335gaa tta gta tat tct aat tca aat tct aat caa tca ctt aag gtt aaa 1056Glu Leu Val Tyr Ser Asn Ser Asn Ser Asn Gln Ser Leu Lys Val Lys 340 345 350tat gga gac cct aat tct tat att gag ccc cct gat tct ttc agt ttt 1104Tyr Gly Asp Pro Asn Ser Tyr Ile Glu Pro Pro Asp Ser Phe Ser Phe 355 360 365tct tct acg gat gtt tac aga acc att tct gtt gtt aga aat tca gta 1152Ser Ser Thr Asp Val Tyr Arg Thr Ile Ser Val Val Arg Asn Ser Val 370 375 380agt aat tat ata gta agt gaa gtt caa ttc aat tca att agt aat aca 1200Ser Asn Tyr Ile Val Ser Glu Val Gln Phe Asn Ser Ile Ser Asn Thr385 390 395 400aat caa att agt gaa gaa att tat aaa cat caa tca aat tgg agt aga 1248Asn Gln Ile Ser Glu Glu Ile Tyr Lys His Gln Ser Asn Trp Ser Arg 405 410 415aaa gaa acc aaa gat tca att aca gaa cta tcc tta gct gct aat ccc 1296Lys Glu Thr Lys Asp Ser Ile Thr Glu Leu Ser Leu Ala Ala Asn Pro 420 425 430cca aca aca ttt gga aat gta gca gaa tac agt cat aga tta gca tat 1344Pro Thr Thr Phe Gly Asn Val Ala Glu Tyr Ser His Arg Leu Ala Tyr 435 440 445att tca gag gca tac caa agt caa aac cca tca aaa tac cca acc tac 1392Ile Ser Glu Ala Tyr Gln Ser Gln Asn Pro Ser Lys Tyr Pro Thr Tyr 450 455 460att cct gta ttc ggt tgg acg cat aca agc gta cgt tac gat aat aaa 1440Ile Pro Val Phe Gly Trp Thr His Thr Ser Val Arg Tyr Asp Asn Lys465 470 475 480att ttc ccg gac aaa atc act caa att cca gct gtt aaa agc tct tca 1488Ile Phe Pro Asp Lys Ile Thr Gln Ile Pro Ala Val Lys Ser Ser Ser 485 490 495gct caa ggt gga tca tgg aaa aat ata gtg aaa ggt ccc ggg ttt act 1536Ala Gln Gly Gly Ser Trp Lys Asn Ile Val Lys Gly Pro Gly Phe Thr 500 505 510gga gga gat gtg aca act gca gtt tcg cca gca act tta acc gac ata 1584Gly Gly Asp Val Thr Thr Ala Val Ser Pro Ala Thr Leu Thr Asp Ile 515 520 525ata aaa ata caa gtt act cta gat cca aat tca ctt tca caa aaa tat 1632Ile Lys Ile Gln Val Thr Leu Asp Pro Asn Ser Leu Ser Gln Lys Tyr 530 535 540cgt gca cga ctt cgc tat gct tcc aat gca ttt gta gca gct act ttg 1680Arg Ala Arg Leu Arg Tyr Ala Ser Asn Ala Phe Val Ala Ala Thr Leu545 550 555 560tat aca aat aca agt agt aat tat aat ttt gaa ctt aca aaa ggt aca 1728Tyr Thr Asn Thr Ser Ser Asn Tyr Asn Phe Glu Leu Thr Lys Gly Thr 565 570 575act gaa cag ttt aca aca tat aat tca tac

cag tat gta gat atc cca 1776Thr Glu Gln Phe Thr Thr Tyr Asn Ser Tyr Gln Tyr Val Asp Ile Pro 580 585 590ggt tca ata caa ttt aat aat act tct gat aca gtg tct gtt tat ttg 1824Gly Ser Ile Gln Phe Asn Asn Thr Ser Asp Thr Val Ser Val Tyr Leu 595 600 605cat atg gat tca aca act aat gca aac gtt cat gta gat aga att gaa 1872His Met Asp Ser Thr Thr Asn Ala Asn Val His Val Asp Arg Ile Glu 610 615 620ttc att cca gta gat gaa cag tac gat gaa aga gta aca cta gaa aaa 1920Phe Ile Pro Val Asp Glu Gln Tyr Asp Glu Arg Val Thr Leu Glu Lys625 630 635 640gca cag aaa gcc gtg aat gcc ttg ttt aca gcg gga aga cat gca ctc 1968Ala Gln Lys Ala Val Asn Ala Leu Phe Thr Ala Gly Arg His Ala Leu 645 650 655caa aca gat gtg aca gat tac aaa gtg gat caa gtg tca att tta gtg 2016Gln Thr Asp Val Thr Asp Tyr Lys Val Asp Gln Val Ser Ile Leu Val 660 665 670gat tgt gta tca ggg gag tta tat cca aat gag aaa cgc gaa cta ctc 2064Asp Cys Val Ser Gly Glu Leu Tyr Pro Asn Glu Lys Arg Glu Leu Leu 675 680 685agt tta gtc aaa tac gca aaa cgt ttg agc tat tct cgt aat tta ctc 2112Ser Leu Val Lys Tyr Ala Lys Arg Leu Ser Tyr Ser Arg Asn Leu Leu 690 695 700cta gat cca aca ttc gat tct atc aat tca tca gat aag aat ggc tgg 2160Leu Asp Pro Thr Phe Asp Ser Ile Asn Ser Ser Asp Lys Asn Gly Trp705 710 715 720tac ggg agt aat ggt att gca att agc agt ggg aat ttt gta ttc aaa 2208Tyr Gly Ser Asn Gly Ile Ala Ile Ser Ser Gly Asn Phe Val Phe Lys 725 730 735ggg aac tat tta atc ttc tca ggt aca aat gat gaa caa tat cca acc 2256Gly Asn Tyr Leu Ile Phe Ser Gly Thr Asn Asp Glu Gln Tyr Pro Thr 740 745 750tat ctc tat caa aaa ata gac gaa tct aag tta aaa gaa tat aca cgt 2304Tyr Leu Tyr Gln Lys Ile Asp Glu Ser Lys Leu Lys Glu Tyr Thr Arg 755 760 765tat aaa ctg aga ggc ttt ata gaa aat agt caa gat tta gaa gca tat 2352Tyr Lys Leu Arg Gly Phe Ile Glu Asn Ser Gln Asp Leu Glu Ala Tyr 770 775 780gtc att cgc tat gat gcc aaa cat gaa aca ttg gat gta tcc aat aat 2400Val Ile Arg Tyr Asp Ala Lys His Glu Thr Leu Asp Val Ser Asn Asn785 790 795 800cta tta ccg gat att tct cct gta aat gca tgt gga gaa cca aat cgt 2448Leu Leu Pro Asp Ile Ser Pro Val Asn Ala Cys Gly Glu Pro Asn Arg 805 810 815tgt gtg gca tta caa tac ctg gat gaa aac cca aga tta gaa tgt agt 2496Cys Val Ala Leu Gln Tyr Leu Asp Glu Asn Pro Arg Leu Glu Cys Ser 820 825 830tcg gtt caa gat ggt att tta tct gat tcg cat tca ttt tct ctc aat 2544Ser Val Gln Asp Gly Ile Leu Ser Asp Ser His Ser Phe Ser Leu Asn 835 840 845ata gat aca ggt tct att gat ttc aat gag agc gta gga att tgg gtg 2592Ile Asp Thr Gly Ser Ile Asp Phe Asn Glu Ser Val Gly Ile Trp Val 850 855 860ttg ttt aaa att tcc aca ccg gaa ggg tat gcg aaa ttt gga aac cta 2640Leu Phe Lys Ile Ser Thr Pro Glu Gly Tyr Ala Lys Phe Gly Asn Leu865 870 875 880gaa gtg att gaa aat ggc cca gtc atc gga gaa gca tta gcc cgt gtg 2688Glu Val Ile Glu Asn Gly Pro Val Ile Gly Glu Ala Leu Ala Arg Val 885 890 895aaa cgc caa gaa aca aag tgg aga aac cag ttg aca caa ctg aga acg 2736Lys Arg Gln Glu Thr Lys Trp Arg Asn Gln Leu Thr Gln Leu Arg Thr 900 905 910gaa aca caa gcg att tat aca cga gca aaa caa gcg ctg gat aat ctt 2784Glu Thr Gln Ala Ile Tyr Thr Arg Ala Lys Gln Ala Leu Asp Asn Leu 915 920 925ttt gcg aat gca caa gac tct cac tta aaa ata ggt acg aca ttt gcg 2832Phe Ala Asn Ala Gln Asp Ser His Leu Lys Ile Gly Thr Thr Phe Ala 930 935 940gca att gtg gct gcg cga aag att gtc caa tcc ata cgc gaa gcg tat 2880Ala Ile Val Ala Ala Arg Lys Ile Val Gln Ser Ile Arg Glu Ala Tyr945 950 955 960atg tca tgg tta tct gtt gtt cca ggt gta aat tat cct atc ttt aca 2928Met Ser Trp Leu Ser Val Val Pro Gly Val Asn Tyr Pro Ile Phe Thr 965 970 975gag ttg act gag aga gta cag caa gca ttt caa tta tat gat gta cga 2976Glu Leu Thr Glu Arg Val Gln Gln Ala Phe Gln Leu Tyr Asp Val Arg 980 985 990aat gtc gtg cgt aat ggc caa ttc ctt agt ggc tta tcc gat tgg att 3024Asn Val Val Arg Asn Gly Gln Phe Leu Ser Gly Leu Ser Asp Trp Ile 995 1000 1005gta aca cct gac gtc aag gta caa gaa gac aat ggg aat aac gta ttg 3072Val Thr Pro Asp Val Lys Val Gln Glu Asp Asn Gly Asn Asn Val Leu 1010 1015 1020gtt ctt tct aat tgg gat gcg caa gta tta caa tgt ctg aag ctc tat 3120Val Leu Ser Asn Trp Asp Ala Gln Val Leu Gln Cys Leu Lys Leu Tyr1025 1030 1035 1040caa gat cgc ggg tat atc tta cgt gta acg gca cgt aag gaa gga ttg 3168Gln Asp Arg Gly Tyr Ile Leu Arg Val Thr Ala Arg Lys Glu Gly Leu 1045 1050 1055gga gaa gga tac gta aca att acg gat gaa gaa ggg aat aca gat caa 3216Gly Glu Gly Tyr Val Thr Ile Thr Asp Glu Glu Gly Asn Thr Asp Gln 1060 1065 1070ttg acg ttt ggt gca tgt gag gag ata gat gca tct aat gcg ttc att 3264Leu Thr Phe Gly Ala Cys Glu Glu Ile Asp Ala Ser Asn Ala Phe Ile 1075 1080 1085tcc aca ggt tat att aca aaa gaa ctg gaa ttc ttc cca gat aca gag 3312Ser Thr Gly Tyr Ile Thr Lys Glu Leu Glu Phe Phe Pro Asp Thr Glu 1090 1095 1100aaa gtg cgt ata gaa att gga gaa aca gaa gga aca ttc cag gtg gaa 3360Lys Val Arg Ile Glu Ile Gly Glu Thr Glu Gly Thr Phe Gln Val Glu1105 1110 1115 1120agt gta gaa tta ttc ttg atg gaa gat cta tgt 3393Ser Val Glu Leu Phe Leu Met Glu Asp Leu Cys 1125 1130231131PRTBacillus thuringiensis 23Met Asn Gln Lys Asn Tyr Asp Ile Ile Gly Ala Ser Thr Asn Gly Thr1 5 10 15 Asn Lys Leu Leu Glu Gly Tyr Asn Ile Ile Ile Ser Pro Tyr Glu Ala 20 25 30 Pro Thr Ser Val Thr Thr Thr Ile Glu Ile Thr Gly Thr Ile Leu Ser 35 40 45 Asp Leu Gly Val Pro Gly Ala Ser Ser Val Ser Leu Leu Leu Asn Lys 50 55 60 Leu Ile Asn Leu Leu Trp Pro Asn Asp Thr Asn Thr Val Trp Gly Thr65 70 75 80 Phe Gly Lys Glu Thr Ala Asp Leu Leu Asn Glu Val Leu Ser Pro Asn 85 90 95 Asp Pro Val Val Thr Asp Ala Asn Thr Asn Leu Ala Gly Leu Asn Asp 100 105 110 Ser Leu Asn Leu Tyr Leu Asn Glu Leu Glu Ile Trp Lys Lys Asp Pro 115 120 125 Asn Asn Ala Thr Thr Gln Arg Asn Val Thr Gln Tyr Phe Val Ser Leu 130 135 140 Asn Leu Asp Phe Thr His Asp Met Pro Ser Phe Ala Val Pro Gly Tyr145 150 155 160 Glu Thr Lys Leu Leu Thr Ile Tyr Ala Gln Ala Ala Asn Leu His Leu 165 170 175 Leu Leu Leu Arg Asp Ala Ser Arg Phe Gly Glu Gly Trp Gly Leu Thr 180 185 190 Gln Glu Ile Ile Asp Ser Asn Tyr Asn Asn Gln Leu Lys Leu Thr Glu 195 200 205 Lys Tyr Thr Asp His Cys Val Lys Trp Tyr Asn Ala Gly Leu Glu Lys 210 215 220 Leu Lys Gly Asn Leu Thr Gly Glu Asn Trp Tyr Thr Tyr Asn Arg Phe225 230 235 240 Arg Arg Glu Met Thr Leu Met Val Leu Asp Val Val Ala Leu Phe Pro 245 250 255 Asn Tyr Asp Thr Arg Met Tyr Pro Ile Ala Thr Ser Ser Glu Leu Thr 260 265 270 Arg Met Ile Tyr Thr Asp Pro Ile Ala Tyr Thr Gln Ser Asp Pro Trp 275 280 285 Tyr Lys Ile Thr Ser Leu Ser Phe Ser Asn Ile Glu Asn Ser Ala Ile 290 295 300 Pro Ser Pro Ser Phe Phe Lys Trp Leu Arg Ser Val Ser Ile Asn Ser305 310 315 320 Gln Trp Trp Gly Ser Gly Pro Asn Gln Thr Tyr Tyr Trp Val Gly His 325 330 335 Glu Leu Val Tyr Ser Asn Ser Asn Ser Asn Gln Ser Leu Lys Val Lys 340 345 350 Tyr Gly Asp Pro Asn Ser Tyr Ile Glu Pro Pro Asp Ser Phe Ser Phe 355 360 365 Ser Ser Thr Asp Val Tyr Arg Thr Ile Ser Val Val Arg Asn Ser Val 370 375 380 Ser Asn Tyr Ile Val Ser Glu Val Gln Phe Asn Ser Ile Ser Asn Thr385 390 395 400 Asn Gln Ile Ser Glu Glu Ile Tyr Lys His Gln Ser Asn Trp Ser Arg 405 410 415 Lys Glu Thr Lys Asp Ser Ile Thr Glu Leu Ser Leu Ala Ala Asn Pro 420 425 430 Pro Thr Thr Phe Gly Asn Val Ala Glu Tyr Ser His Arg Leu Ala Tyr 435 440 445 Ile Ser Glu Ala Tyr Gln Ser Gln Asn Pro Ser Lys Tyr Pro Thr Tyr 450 455 460 Ile Pro Val Phe Gly Trp Thr His Thr Ser Val Arg Tyr Asp Asn Lys465 470 475 480 Ile Phe Pro Asp Lys Ile Thr Gln Ile Pro Ala Val Lys Ser Ser Ser 485 490 495 Ala Gln Gly Gly Ser Trp Lys Asn Ile Val Lys Gly Pro Gly Phe Thr 500 505 510 Gly Gly Asp Val Thr Thr Ala Val Ser Pro Ala Thr Leu Thr Asp Ile 515 520 525 Ile Lys Ile Gln Val Thr Leu Asp Pro Asn Ser Leu Ser Gln Lys Tyr 530 535 540 Arg Ala Arg Leu Arg Tyr Ala Ser Asn Ala Phe Val Ala Ala Thr Leu545 550 555 560 Tyr Thr Asn Thr Ser Ser Asn Tyr Asn Phe Glu Leu Thr Lys Gly Thr 565 570 575 Thr Glu Gln Phe Thr Thr Tyr Asn Ser Tyr Gln Tyr Val Asp Ile Pro 580 585 590 Gly Ser Ile Gln Phe Asn Asn Thr Ser Asp Thr Val Ser Val Tyr Leu 595 600 605 His Met Asp Ser Thr Thr Asn Ala Asn Val His Val Asp Arg Ile Glu 610 615 620 Phe Ile Pro Val Asp Glu Gln Tyr Asp Glu Arg Val Thr Leu Glu Lys625 630 635 640 Ala Gln Lys Ala Val Asn Ala Leu Phe Thr Ala Gly Arg His Ala Leu 645 650 655 Gln Thr Asp Val Thr Asp Tyr Lys Val Asp Gln Val Ser Ile Leu Val 660 665 670 Asp Cys Val Ser Gly Glu Leu Tyr Pro Asn Glu Lys Arg Glu Leu Leu 675 680 685 Ser Leu Val Lys Tyr Ala Lys Arg Leu Ser Tyr Ser Arg Asn Leu Leu 690 695 700 Leu Asp Pro Thr Phe Asp Ser Ile Asn Ser Ser Asp Lys Asn Gly Trp705 710 715 720 Tyr Gly Ser Asn Gly Ile Ala Ile Ser Ser Gly Asn Phe Val Phe Lys 725 730 735 Gly Asn Tyr Leu Ile Phe Ser Gly Thr Asn Asp Glu Gln Tyr Pro Thr 740 745 750 Tyr Leu Tyr Gln Lys Ile Asp Glu Ser Lys Leu Lys Glu Tyr Thr Arg 755 760 765 Tyr Lys Leu Arg Gly Phe Ile Glu Asn Ser Gln Asp Leu Glu Ala Tyr 770 775 780 Val Ile Arg Tyr Asp Ala Lys His Glu Thr Leu Asp Val Ser Asn Asn785 790 795 800 Leu Leu Pro Asp Ile Ser Pro Val Asn Ala Cys Gly Glu Pro Asn Arg 805 810 815 Cys Val Ala Leu Gln Tyr Leu Asp Glu Asn Pro Arg Leu Glu Cys Ser 820 825 830 Ser Val Gln Asp Gly Ile Leu Ser Asp Ser His Ser Phe Ser Leu Asn 835 840 845 Ile Asp Thr Gly Ser Ile Asp Phe Asn Glu Ser Val Gly Ile Trp Val 850 855 860 Leu Phe Lys Ile Ser Thr Pro Glu Gly Tyr Ala Lys Phe Gly Asn Leu865 870 875 880 Glu Val Ile Glu Asn Gly Pro Val Ile Gly Glu Ala Leu Ala Arg Val 885 890 895 Lys Arg Gln Glu Thr Lys Trp Arg Asn Gln Leu Thr Gln Leu Arg Thr 900 905 910 Glu Thr Gln Ala Ile Tyr Thr Arg Ala Lys Gln Ala Leu Asp Asn Leu 915 920 925 Phe Ala Asn Ala Gln Asp Ser His Leu Lys Ile Gly Thr Thr Phe Ala 930 935 940 Ala Ile Val Ala Ala Arg Lys Ile Val Gln Ser Ile Arg Glu Ala Tyr945 950 955 960 Met Ser Trp Leu Ser Val Val Pro Gly Val Asn Tyr Pro Ile Phe Thr 965 970 975 Glu Leu Thr Glu Arg Val Gln Gln Ala Phe Gln Leu Tyr Asp Val Arg 980 985 990 Asn Val Val Arg Asn Gly Gln Phe Leu Ser Gly Leu Ser Asp Trp Ile 995 1000 1005 Val Thr Pro Asp Val Lys Val Gln Glu Asp Asn Gly Asn Asn Val Leu 1010 1015 1020 Val Leu Ser Asn Trp Asp Ala Gln Val Leu Gln Cys Leu Lys Leu Tyr1025 1030 1035 1040 Gln Asp Arg Gly Tyr Ile Leu Arg Val Thr Ala Arg Lys Glu Gly Leu 1045 1050 1055 Gly Glu Gly Tyr Val Thr Ile Thr Asp Glu Glu Gly Asn Thr Asp Gln 1060 1065 1070 Leu Thr Phe Gly Ala Cys Glu Glu Ile Asp Ala Ser Asn Ala Phe Ile 1075 1080 1085 Ser Thr Gly Tyr Ile Thr Lys Glu Leu Glu Phe Phe Pro Asp Thr Glu 1090 1095 1100 Lys Val Arg Ile Glu Ile Gly Glu Thr Glu Gly Thr Phe Gln Val Glu1105 1110 1115 1120 Ser Val Glu Leu Phe Leu Met Glu Asp Leu Cys 1125 1130 241002DNABacillus thuringiensisCDS(1)...(1002) 24atg gtg aga gtc tat cca gac ttt gat gag atg ata agg gaa gct gct 48Met Val Arg Val Tyr Pro Asp Phe Asp Glu Met Ile Arg Glu Ala Ala1 5 10 15cga aaa tgg tca gaa gca aat gga ttg cta ttt caa aag gtg tcg tat 96Arg Lys Trp Ser Glu Ala Asn Gly Leu Leu Phe Gln Lys Val Ser Tyr 20 25 30gcg gat cct tta acc aat gcg gat aca atc agt cta agt gtc aaa ttc 144Ala Asp Pro Leu Thr Asn Ala Asp Thr Ile Ser Leu Ser Val Lys Phe 35 40 45aaa gat atc gga tgc cta gaa gaa tgc gtc gaa gta gaa aaa ata agc 192Lys Asp Ile Gly Cys Leu Glu Glu Cys Val Glu Val Glu Lys Ile Ser 50 55 60att cca caa aat ttt acg aat aat acg gat caa aaa caa aaa gaa aca 240Ile Pro Gln Asn Phe Thr Asn Asn Thr Asp Gln Lys Gln Lys Glu Thr65 70 75 80ttg gaa act ata aca tat gta gaa aat ctg ttg act tgg gaa aat gac 288Leu Glu Thr Ile Thr Tyr Val Glu Asn Leu Leu Thr Trp Glu Asn Asp 85 90 95ttt cat ttt gtg ctt cca gga caa aac ttt ctt acg ata cca cgt gtt 336Phe His Phe Val Leu Pro Gly Gln Asn Phe Leu Thr Ile Pro Arg Val 100 105 110cct cgt tca gtt cat atg gat att aat cca ggt ttc ctt gtg aat ttt 384Pro Arg Ser Val His Met Asp Ile Asn Pro Gly Phe Leu Val Asn Phe 115 120 125ttt ggt aga aat caa cta ttc cat acc aaa ata aga gaa cca cgt ccc 432Phe Gly Arg Asn Gln Leu Phe His Thr Lys Ile Arg Glu Pro Arg Pro 130 135 140att cgg gcg gaa gtg ttt tta gaa cca tct agc agt gca tcg att caa 480Ile Arg Ala Glu Val Phe Leu Glu Pro Ser Ser Ser Ala Ser Ile Gln145 150 155 160ctg caa gtg gaa aaa caa cat gtt tct caa ccg tat caa atg gaa tta 528Leu Gln Val Glu Lys Gln His Val Ser Gln Pro Tyr Gln Met Glu Leu 165 170 175tca atg cta gga agt att att gtg acg gca caa gat aga gga cag gaa 576Ser Met Leu Gly Ser Ile Ile Val Thr Ala Gln Asp Arg Gly Gln Glu 180 185 190caa ggt acg gat cgc tat gtt gag tta aca gat ctc ata cca ttc ctc 624Gln Gly Thr Asp Arg Tyr Val Glu Leu Thr Asp Leu Ile Pro Phe Leu 195 200 205tgc ccg cat aaa aac ttt tct tct aaa ggg cgg gca ttg ata ttc ctt 672Cys Pro His Lys Asn Phe Ser Ser Lys Gly Arg Ala Leu Ile Phe Leu 210 215 220gaa cag gga acg ttc aag gga ata ttg agt cga

aag ata cgt gca tat 720Glu Gln Gly Thr Phe Lys Gly Ile Leu Ser Arg Lys Ile Arg Ala Tyr225 230 235 240gcc aca caa atg ctt cat tgc gac gga aaa aca cta gaa tat gaa att 768Ala Thr Gln Met Leu His Cys Asp Gly Lys Thr Leu Glu Tyr Glu Ile 245 250 255cct tta aat aat cca tta cct gaa tct gcc cta cga cct aaa cct atg 816Pro Leu Asn Asn Pro Leu Pro Glu Ser Ala Leu Arg Pro Lys Pro Met 260 265 270acg att aac gct aca tca tgt gga tgt tct tct gat aga cca tca gtc 864Thr Ile Asn Ala Thr Ser Cys Gly Cys Ser Ser Asp Arg Pro Ser Val 275 280 285gta tct act tcc tct cat cca tcg aat cct aca acc tat tcc cag caa 912Val Ser Thr Ser Ser His Pro Ser Asn Pro Thr Thr Tyr Ser Gln Gln 290 295 300cct aaa cct atg acg act aac gct aca tca tgt gga tgt tct gcc tgt 960Pro Lys Pro Met Thr Thr Asn Ala Thr Ser Cys Gly Cys Ser Ala Cys305 310 315 320atg tct gca aca tca aat aaa aat cta tat aca gaa caa taa 1002Met Ser Ala Thr Ser Asn Lys Asn Leu Tyr Thr Glu Gln 325 33025333PRTBacillus thuringiensis 25Met Val Arg Val Tyr Pro Asp Phe Asp Glu Met Ile Arg Glu Ala Ala1 5 10 15 Arg Lys Trp Ser Glu Ala Asn Gly Leu Leu Phe Gln Lys Val Ser Tyr 20 25 30 Ala Asp Pro Leu Thr Asn Ala Asp Thr Ile Ser Leu Ser Val Lys Phe 35 40 45 Lys Asp Ile Gly Cys Leu Glu Glu Cys Val Glu Val Glu Lys Ile Ser 50 55 60 Ile Pro Gln Asn Phe Thr Asn Asn Thr Asp Gln Lys Gln Lys Glu Thr65 70 75 80 Leu Glu Thr Ile Thr Tyr Val Glu Asn Leu Leu Thr Trp Glu Asn Asp 85 90 95 Phe His Phe Val Leu Pro Gly Gln Asn Phe Leu Thr Ile Pro Arg Val 100 105 110 Pro Arg Ser Val His Met Asp Ile Asn Pro Gly Phe Leu Val Asn Phe 115 120 125 Phe Gly Arg Asn Gln Leu Phe His Thr Lys Ile Arg Glu Pro Arg Pro 130 135 140 Ile Arg Ala Glu Val Phe Leu Glu Pro Ser Ser Ser Ala Ser Ile Gln145 150 155 160 Leu Gln Val Glu Lys Gln His Val Ser Gln Pro Tyr Gln Met Glu Leu 165 170 175 Ser Met Leu Gly Ser Ile Ile Val Thr Ala Gln Asp Arg Gly Gln Glu 180 185 190 Gln Gly Thr Asp Arg Tyr Val Glu Leu Thr Asp Leu Ile Pro Phe Leu 195 200 205 Cys Pro His Lys Asn Phe Ser Ser Lys Gly Arg Ala Leu Ile Phe Leu 210 215 220 Glu Gln Gly Thr Phe Lys Gly Ile Leu Ser Arg Lys Ile Arg Ala Tyr225 230 235 240 Ala Thr Gln Met Leu His Cys Asp Gly Lys Thr Leu Glu Tyr Glu Ile 245 250 255 Pro Leu Asn Asn Pro Leu Pro Glu Ser Ala Leu Arg Pro Lys Pro Met 260 265 270 Thr Ile Asn Ala Thr Ser Cys Gly Cys Ser Ser Asp Arg Pro Ser Val 275 280 285 Val Ser Thr Ser Ser His Pro Ser Asn Pro Thr Thr Tyr Ser Gln Gln 290 295 300 Pro Lys Pro Met Thr Thr Asn Ala Thr Ser Cys Gly Cys Ser Ala Cys305 310 315 320 Met Ser Ala Thr Ser Asn Lys Asn Leu Tyr Thr Glu Gln 325 330 261026DNABacillus thuringiensisCDS(1)...(1026) 26atg aaa aag tct tgt aat cca aat gaa gtg aat cca agt gca tat act 48Met Lys Lys Ser Cys Asn Pro Asn Glu Val Asn Pro Ser Ala Tyr Thr1 5 10 15tta tac aac ttt gat gag tat gta att ggc aat ttt ttc aat gca gtg 96Leu Tyr Asn Phe Asp Glu Tyr Val Ile Gly Asn Phe Phe Asn Ala Val 20 25 30caa cac cct ata aat ctt tcc ttc aga gaa gat gaa tgg aat ttt gat 144Gln His Pro Ile Asn Leu Ser Phe Arg Glu Asp Glu Trp Asn Phe Asp 35 40 45tca gac tat att cct acc cca act tct gac caa cta act agc cct tgt 192Ser Asp Tyr Ile Pro Thr Pro Thr Ser Asp Gln Leu Thr Ser Pro Cys 50 55 60aaa tct gtt cca acc agc gca ccg tgt aaa tat ggt cca atc gat cct 240Lys Ser Val Pro Thr Ser Ala Pro Cys Lys Tyr Gly Pro Ile Asp Pro65 70 75 80tat gag tgg ata gaa tgg cta gac ctc gta gca gaa ggg aca gat tta 288Tyr Glu Trp Ile Glu Trp Leu Asp Leu Val Ala Glu Gly Thr Asp Leu 85 90 95tat gaa gaa atc caa aat gca aat aca aaa acc ccg ttt att aat gat 336Tyr Glu Glu Ile Gln Asn Ala Asn Thr Lys Thr Pro Phe Ile Asn Asp 100 105 110gaa tat tac ttt aat aat aca tca tct gaa aca caa cca tat cag acc 384Glu Tyr Tyr Phe Asn Asn Thr Ser Ser Glu Thr Gln Pro Tyr Gln Thr 115 120 125att tct cat tca gaa aca ttg acc aca acc acg aca aac aca aca aca 432Ile Ser His Ser Glu Thr Leu Thr Thr Thr Thr Thr Asn Thr Thr Thr 130 135 140caa gga tgt aaa ata aat cca aaa gtc agt tat tcg aga aaa acg aaa 480Gln Gly Cys Lys Ile Asn Pro Lys Val Ser Tyr Ser Arg Lys Thr Lys145 150 155 160gtt aaa gtc aaa att gtt gat gta gaa aag gga ttt aac acg gaa ata 528Val Lys Val Lys Ile Val Asp Val Glu Lys Gly Phe Asn Thr Glu Ile 165 170 175ggg gca gaa tat aac ttt agc gat aca aac aca tac aca gaa aca gca 576Gly Ala Glu Tyr Asn Phe Ser Asp Thr Asn Thr Tyr Thr Glu Thr Ala 180 185 190act cgg act gtg aca gtt cca tca atg acg aca tat gtt cca ccc tat 624Thr Arg Thr Val Thr Val Pro Ser Met Thr Thr Tyr Val Pro Pro Tyr 195 200 205acc tct gcg tat gtg acg gtc gta tta gaa aga gga tat tat gaa gct 672Thr Ser Ala Tyr Val Thr Val Val Leu Glu Arg Gly Tyr Tyr Glu Ala 210 215 220tat aat att cca atc gac acg aat tta tat gga aga ttt gaa ctc atc 720Tyr Asn Ile Pro Ile Asp Thr Asn Leu Tyr Gly Arg Phe Glu Leu Ile225 230 235 240tac acc aac ctc gat ggc agc aac cct cga tcg gcg ggt gtt ctg gat 768Tyr Thr Asn Leu Asp Gly Ser Asn Pro Arg Ser Ala Gly Val Leu Asp 245 250 255cta tat cct ttc gta gaa tta att aca aca tgt tgt caa aat tgt agt 816Leu Tyr Pro Phe Val Glu Leu Ile Thr Thr Cys Cys Gln Asn Cys Ser 260 265 270cag tgt gtg cca gac atg att cag cct gat cgt gac aat caa aca gtt 864Gln Cys Val Pro Asp Met Ile Gln Pro Asp Arg Asp Asn Gln Thr Val 275 280 285cgt ttt act gga aga ggg gat ctt ata tcg gat ttt gca gcg aat act 912Arg Phe Thr Gly Arg Gly Asp Leu Ile Ser Asp Phe Ala Ala Asn Thr 290 295 300tta acc gta acg act aca ttt gtt gac aat gca aca gga gca acc gtt 960Leu Thr Val Thr Thr Thr Phe Val Asp Asn Ala Thr Gly Ala Thr Val305 310 315 320tcg caa cac gta gaa tcc gta cca gtt cag tat gga ccc gct acc aca 1008Ser Gln His Val Glu Ser Val Pro Val Gln Tyr Gly Pro Ala Thr Thr 325 330 335gta gta aac aca tct aaa 1026Val Val Asn Thr Ser Lys 34027342PRTBacillus thuringiensis 27Met Lys Lys Ser Cys Asn Pro Asn Glu Val Asn Pro Ser Ala Tyr Thr1 5 10 15 Leu Tyr Asn Phe Asp Glu Tyr Val Ile Gly Asn Phe Phe Asn Ala Val 20 25 30 Gln His Pro Ile Asn Leu Ser Phe Arg Glu Asp Glu Trp Asn Phe Asp 35 40 45 Ser Asp Tyr Ile Pro Thr Pro Thr Ser Asp Gln Leu Thr Ser Pro Cys 50 55 60 Lys Ser Val Pro Thr Ser Ala Pro Cys Lys Tyr Gly Pro Ile Asp Pro65 70 75 80 Tyr Glu Trp Ile Glu Trp Leu Asp Leu Val Ala Glu Gly Thr Asp Leu 85 90 95 Tyr Glu Glu Ile Gln Asn Ala Asn Thr Lys Thr Pro Phe Ile Asn Asp 100 105 110 Glu Tyr Tyr Phe Asn Asn Thr Ser Ser Glu Thr Gln Pro Tyr Gln Thr 115 120 125 Ile Ser His Ser Glu Thr Leu Thr Thr Thr Thr Thr Asn Thr Thr Thr 130 135 140 Gln Gly Cys Lys Ile Asn Pro Lys Val Ser Tyr Ser Arg Lys Thr Lys145 150 155 160 Val Lys Val Lys Ile Val Asp Val Glu Lys Gly Phe Asn Thr Glu Ile 165 170 175 Gly Ala Glu Tyr Asn Phe Ser Asp Thr Asn Thr Tyr Thr Glu Thr Ala 180 185 190 Thr Arg Thr Val Thr Val Pro Ser Met Thr Thr Tyr Val Pro Pro Tyr 195 200 205 Thr Ser Ala Tyr Val Thr Val Val Leu Glu Arg Gly Tyr Tyr Glu Ala 210 215 220 Tyr Asn Ile Pro Ile Asp Thr Asn Leu Tyr Gly Arg Phe Glu Leu Ile225 230 235 240 Tyr Thr Asn Leu Asp Gly Ser Asn Pro Arg Ser Ala Gly Val Leu Asp 245 250 255 Leu Tyr Pro Phe Val Glu Leu Ile Thr Thr Cys Cys Gln Asn Cys Ser 260 265 270 Gln Cys Val Pro Asp Met Ile Gln Pro Asp Arg Asp Asn Gln Thr Val 275 280 285 Arg Phe Thr Gly Arg Gly Asp Leu Ile Ser Asp Phe Ala Ala Asn Thr 290 295 300 Leu Thr Val Thr Thr Thr Phe Val Asp Asn Ala Thr Gly Ala Thr Val305 310 315 320 Ser Gln His Val Glu Ser Val Pro Val Gln Tyr Gly Pro Ala Thr Thr 325 330 335 Val Val Asn Thr Ser Lys 340 283009DNABacillus thuringiensisCDS(1)...(3009) 28atg aaa agg atg aag aaa aag cta gca agt gtt gta acc tgt aca tta 48Met Lys Arg Met Lys Lys Lys Leu Ala Ser Val Val Thr Cys Thr Leu1 5 10 15tta gct cct atg ttt ttg aat ggg aac gta gac act gta ttt gca gat 96Leu Ala Pro Met Phe Leu Asn Gly Asn Val Asp Thr Val Phe Ala Asp 20 25 30agt aaa aca aat caa att tct tca aca cag gaa aac caa aag aat gag 144Ser Lys Thr Asn Gln Ile Ser Ser Thr Gln Glu Asn Gln Lys Asn Glu 35 40 45atg gat cga aaa gga cta ctt ggt tat tat ttt aaa gga aaa gat ttt 192Met Asp Arg Lys Gly Leu Leu Gly Tyr Tyr Phe Lys Gly Lys Asp Phe 50 55 60aat aat ctt act ata ttt gct cca aca cgt gag aat act ctt att tat 240Asn Asn Leu Thr Ile Phe Ala Pro Thr Arg Glu Asn Thr Leu Ile Tyr65 70 75 80gat tta gaa aca gcg aat tct tta tta gat aag caa caa caa acc tat 288Asp Leu Glu Thr Ala Asn Ser Leu Leu Asp Lys Gln Gln Gln Thr Tyr 85 90 95caa tct att cgt tgg atc ggt tta ata aaa agc aaa aaa gct gga gat 336Gln Ser Ile Arg Trp Ile Gly Leu Ile Lys Ser Lys Lys Ala Gly Asp 100 105 110ttt acc ttt caa tta tcg gat gat gag cat gct att ata gaa atc gat 384Phe Thr Phe Gln Leu Ser Asp Asp Glu His Ala Ile Ile Glu Ile Asp 115 120 125ggg aaa gtt att tcg caa aaa ggc caa aag aaa caa gtt gtt cat tta 432Gly Lys Val Ile Ser Gln Lys Gly Gln Lys Lys Gln Val Val His Leu 130 135 140gaa aaa gat aaa tta gtt ccc atc aaa att gaa tat caa tct gat aaa 480Glu Lys Asp Lys Leu Val Pro Ile Lys Ile Glu Tyr Gln Ser Asp Lys145 150 155 160gcg tta aac cca gat agt caa atg ttt aaa gaa ttg aaa tta ttt aaa 528Ala Leu Asn Pro Asp Ser Gln Met Phe Lys Glu Leu Lys Leu Phe Lys 165 170 175ata aat agt caa aaa caa tct cag caa gtg caa caa gac gaa ttg aga 576Ile Asn Ser Gln Lys Gln Ser Gln Gln Val Gln Gln Asp Glu Leu Arg 180 185 190aat cct gaa ttt ggt aaa gaa aaa act caa aca tat tta aag aaa gca 624Asn Pro Glu Phe Gly Lys Glu Lys Thr Gln Thr Tyr Leu Lys Lys Ala 195 200 205tcg aaa agc agc ttg ttt agc aat aaa agt aaa cga gat ata gat gaa 672Ser Lys Ser Ser Leu Phe Ser Asn Lys Ser Lys Arg Asp Ile Asp Glu 210 215 220gat ata gat gag gat aca gat aca gat gga gat gcc att cct gat gta 720Asp Ile Asp Glu Asp Thr Asp Thr Asp Gly Asp Ala Ile Pro Asp Val225 230 235 240tgg gaa gaa aat ggg tat acc atc aaa gga aga gta gct gtt aaa tgg 768Trp Glu Glu Asn Gly Tyr Thr Ile Lys Gly Arg Val Ala Val Lys Trp 245 250 255gac gaa gga tta gct gat aag gga tat aaa aag ttt gtt tcc aat cct 816Asp Glu Gly Leu Ala Asp Lys Gly Tyr Lys Lys Phe Val Ser Asn Pro 260 265 270ttt aga cag cac act gct ggt gac ccc tat agt gac tat gaa aag gca 864Phe Arg Gln His Thr Ala Gly Asp Pro Tyr Ser Asp Tyr Glu Lys Ala 275 280 285tca aaa gat ttg gat tta tct aat gca aaa gaa aca ttt aat cca ttg 912Ser Lys Asp Leu Asp Leu Ser Asn Ala Lys Glu Thr Phe Asn Pro Leu 290 295 300gtg gct gct ttt cca agt gtc aat gtt agc ttg gaa aat gtc acc ata 960Val Ala Ala Phe Pro Ser Val Asn Val Ser Leu Glu Asn Val Thr Ile305 310 315 320tca aaa gat gaa aat aaa act gct gaa att gcg tct act tca tcg aat 1008Ser Lys Asp Glu Asn Lys Thr Ala Glu Ile Ala Ser Thr Ser Ser Asn 325 330 335aat tgg tcc tat aca aat aca gag ggg gca tct att gaa gct gga att 1056Asn Trp Ser Tyr Thr Asn Thr Glu Gly Ala Ser Ile Glu Ala Gly Ile 340 345 350gga cca gaa ggt ttg ttg tct ttt gga gta agt gcc aat tat caa cat 1104Gly Pro Glu Gly Leu Leu Ser Phe Gly Val Ser Ala Asn Tyr Gln His 355 360 365tct gaa aca gtg gcc aaa gag tgg ggt aca act aag gga gac gca aca 1152Ser Glu Thr Val Ala Lys Glu Trp Gly Thr Thr Lys Gly Asp Ala Thr 370 375 380caa tat aat aca gct tca gca gga tat cta aat gcc aat gtt cga tat 1200Gln Tyr Asn Thr Ala Ser Ala Gly Tyr Leu Asn Ala Asn Val Arg Tyr385 390 395 400aat aat gta ggg acg gca gcc att tat gat gtg aaa cct aca acg aat 1248Asn Asn Val Gly Thr Ala Ala Ile Tyr Asp Val Lys Pro Thr Thr Asn 405 410 415ttt gta tta gat aag act aca ctc gcg acg att aag gca aaa gaa aat 1296Phe Val Leu Asp Lys Thr Thr Leu Ala Thr Ile Lys Ala Lys Glu Asn 420 425 430gcc acg gct gat cat ata ata cca ggg aat agt tac ccg gaa aaa ggg 1344Ala Thr Ala Asp His Ile Ile Pro Gly Asn Ser Tyr Pro Glu Lys Gly 435 440 445aaa aat gga att gcg ata act act atg gat gat ttt aac tct cat cct 1392Lys Asn Gly Ile Ala Ile Thr Thr Met Asp Asp Phe Asn Ser His Pro 450 455 460att act cta aat aaa caa caa cta gat aag ttg tta tat aat gtt aca 1440Ile Thr Leu Asn Lys Gln Gln Leu Asp Lys Leu Leu Tyr Asn Val Thr465 470 475 480cca ctt atg ttg gaa act acc caa gtt gag ggt acg tat aag aaa aaa 1488Pro Leu Met Leu Glu Thr Thr Gln Val Glu Gly Thr Tyr Lys Lys Lys 485 490 495gat gta gat ggt aat atc att act gga ggg aca tgg agt gga gtg aca 1536Asp Val Asp Gly Asn Ile Ile Thr Gly Gly Thr Trp Ser Gly Val Thr 500 505 510caa caa att gag gcg caa act gct tct att att gtt gat act gga gag 1584Gln Gln Ile Glu Ala Gln Thr Ala Ser Ile Ile Val Asp Thr Gly Glu 515 520 525ggt gtt tcg gaa aaa cgt att gca gca aaa gat tat gat gac ccc gaa 1632Gly Val Ser Glu Lys Arg Ile Ala Ala Lys Asp Tyr Asp Asp Pro Glu 530 535 540gat aaa aca ccg tct tta act cta aaa gat gcc ctg aaa att gga tat 1680Asp Lys Thr Pro Ser Leu Thr Leu Lys Asp Ala Leu Lys Ile Gly Tyr545 550 555 560cca gaa gaa att gaa gaa aaa aat gat tta tta tat tat aaa gga aaa 1728Pro Glu Glu Ile Glu Glu Lys Asn Asp Leu Leu Tyr Tyr Lys Gly Lys 565 570 575ata ata tct gaa tca agt gtg atg act ttt ctt gat aat gga acc tcc 1776Ile Ile Ser Glu Ser Ser Val Met Thr Phe Leu Asp Asn Gly Thr Ser 580 585 590gaa aaa gtt aaa aaa caa atc gag gat aaa act gga aaa ttt aaa gac 1824Glu Lys Val Lys Lys Gln Ile Glu Asp Lys Thr Gly Lys Phe Lys Asp 595 600 605gta caa cat ttg tat gat gtg aaa cta aca cct gga atg aat ttt act 1872Val Gln His Leu Tyr Asp Val Lys Leu Thr Pro Gly Met Asn Phe Thr 610 615 620att aaa tta gct tca

ata tac gat agt gtc gat aat ttt agt ggc agt 1920Ile Lys Leu Ala Ser Ile Tyr Asp Ser Val Asp Asn Phe Ser Gly Ser625 630 635 640caa tca tta ggg gca tta aat agt ata agt aag gtt gct gga gga aat 1968Gln Ser Leu Gly Ala Leu Asn Ser Ile Ser Lys Val Ala Gly Gly Asn 645 650 655aca ggg aaa aat caa tat caa tca tca tct tct aat gcg tat att tct 2016Thr Gly Lys Asn Gln Tyr Gln Ser Ser Ser Ser Asn Ala Tyr Ile Ser 660 665 670tta tct tcg agt aca aaa gga gag ttg aat aaa aat act acg tac tat 2064Leu Ser Ser Ser Thr Lys Gly Glu Leu Asn Lys Asn Thr Thr Tyr Tyr 675 680 685ctt agc atg tat atg aga gca gat gct gat aca gaa cct acc ata gaa 2112Leu Ser Met Tyr Met Arg Ala Asp Ala Asp Thr Glu Pro Thr Ile Glu 690 695 700cta aaa gga gaa aaa tcc aca ata aaa agc caa aaa gtt aaa cta aac 2160Leu Lys Gly Glu Lys Ser Thr Ile Lys Ser Gln Lys Val Lys Leu Asn705 710 715 720aat aag gga tat cag agg gta gat att tta gta gaa aat act gag tcg 2208Asn Lys Gly Tyr Gln Arg Val Asp Ile Leu Val Glu Asn Thr Glu Ser 725 730 735aat cca att cat caa att tat gta cac ggt aac aat aag aca aat gtc 2256Asn Pro Ile His Gln Ile Tyr Val His Gly Asn Asn Lys Thr Asn Val 740 745 750tat tgg gac gat gtg tct ctt aca gag gta tct gct ata aaa caa gaa 2304Tyr Trp Asp Asp Val Ser Leu Thr Glu Val Ser Ala Ile Lys Gln Glu 755 760 765tta ccc gat ata tca gat aaa gag ata caa agg gct cat aca ttt aag 2352Leu Pro Asp Ile Ser Asp Lys Glu Ile Gln Arg Ala His Thr Phe Lys 770 775 780aaa gaa cag tta agt tta gat ggt aag tat atg aat gaa ttg aca tta 2400Lys Glu Gln Leu Ser Leu Asp Gly Lys Tyr Met Asn Glu Leu Thr Leu785 790 795 800cac gtt gat tcg tta aaa gac aag aac aat aag ccg gtt cag ttc agt 2448His Val Asp Ser Leu Lys Asp Lys Asn Asn Lys Pro Val Gln Phe Ser 805 810 815tat aaa gtg aaa gat ggt gaa aaa gat tta gga act aaa tcc tat aca 2496Tyr Lys Val Lys Asp Gly Glu Lys Asp Leu Gly Thr Lys Ser Tyr Thr 820 825 830cct gat aag cag gga aat ata aac att aac ttt cta gat tac aat cgt 2544Pro Asp Lys Gln Gly Asn Ile Asn Ile Asn Phe Leu Asp Tyr Asn Arg 835 840 845gga ttt gga att tct aag gat cat aaa att caa att tat gcg gta cgt 2592Gly Phe Gly Ile Ser Lys Asp His Lys Ile Gln Ile Tyr Ala Val Arg 850 855 860aaa gac caa gag gtg aaa gta gca gaa cta aaa aac tat aat atg agt 2640Lys Asp Gln Glu Val Lys Val Ala Glu Leu Lys Asn Tyr Asn Met Ser865 870 875 880gga act atc aga ttt agc aat gat gga gaa agt ggc ctt cca gag ata 2688Gly Thr Ile Arg Phe Ser Asn Asp Gly Glu Ser Gly Leu Pro Glu Ile 885 890 895tat gga tat att ttc atg act cca gaa ggt caa tat cct gtt tct cct 2736Tyr Gly Tyr Ile Phe Met Thr Pro Glu Gly Gln Tyr Pro Val Ser Pro 900 905 910gta gga ggt ata cac caa ata tgg tca aga tat tat aca agc act tac 2784Val Gly Gly Ile His Gln Ile Trp Ser Arg Tyr Tyr Thr Ser Thr Tyr 915 920 925aag tgg agt act caa tat agt tat gat ttt gca tcc ttt aat agt gat 2832Lys Trp Ser Thr Gln Tyr Ser Tyr Asp Phe Ala Ser Phe Asn Ser Asp 930 935 940ata aaa aca gtt cat ttt aat gga tat gta aag gaa ctg gat gat acg 2880Ile Lys Thr Val His Phe Asn Gly Tyr Val Lys Glu Leu Asp Asp Thr945 950 955 960aat ggc gac gac ata ctg gct tat ctt gaa aat aaa tat gaa tct cat 2928Asn Gly Asp Asp Ile Leu Ala Tyr Leu Glu Asn Lys Tyr Glu Ser His 965 970 975ggt tta gag ggg agt gta gtg tta gaa gga gat gaa agg ggc agt aat 2976Gly Leu Glu Gly Ser Val Val Leu Glu Gly Asp Glu Arg Gly Ser Asn 980 985 990gtg act gtt gaa tat cat ata aaa ttg aaa taa 3009Val Thr Val Glu Tyr His Ile Lys Leu Lys 995 1000291002PRTBacillus thuringiensis 29Met Lys Arg Met Lys Lys Lys Leu Ala Ser Val Val Thr Cys Thr Leu1 5 10 15 Leu Ala Pro Met Phe Leu Asn Gly Asn Val Asp Thr Val Phe Ala Asp 20 25 30 Ser Lys Thr Asn Gln Ile Ser Ser Thr Gln Glu Asn Gln Lys Asn Glu 35 40 45 Met Asp Arg Lys Gly Leu Leu Gly Tyr Tyr Phe Lys Gly Lys Asp Phe 50 55 60 Asn Asn Leu Thr Ile Phe Ala Pro Thr Arg Glu Asn Thr Leu Ile Tyr65 70 75 80 Asp Leu Glu Thr Ala Asn Ser Leu Leu Asp Lys Gln Gln Gln Thr Tyr 85 90 95 Gln Ser Ile Arg Trp Ile Gly Leu Ile Lys Ser Lys Lys Ala Gly Asp 100 105 110 Phe Thr Phe Gln Leu Ser Asp Asp Glu His Ala Ile Ile Glu Ile Asp 115 120 125 Gly Lys Val Ile Ser Gln Lys Gly Gln Lys Lys Gln Val Val His Leu 130 135 140 Glu Lys Asp Lys Leu Val Pro Ile Lys Ile Glu Tyr Gln Ser Asp Lys145 150 155 160 Ala Leu Asn Pro Asp Ser Gln Met Phe Lys Glu Leu Lys Leu Phe Lys 165 170 175 Ile Asn Ser Gln Lys Gln Ser Gln Gln Val Gln Gln Asp Glu Leu Arg 180 185 190 Asn Pro Glu Phe Gly Lys Glu Lys Thr Gln Thr Tyr Leu Lys Lys Ala 195 200 205 Ser Lys Ser Ser Leu Phe Ser Asn Lys Ser Lys Arg Asp Ile Asp Glu 210 215 220 Asp Ile Asp Glu Asp Thr Asp Thr Asp Gly Asp Ala Ile Pro Asp Val225 230 235 240 Trp Glu Glu Asn Gly Tyr Thr Ile Lys Gly Arg Val Ala Val Lys Trp 245 250 255 Asp Glu Gly Leu Ala Asp Lys Gly Tyr Lys Lys Phe Val Ser Asn Pro 260 265 270 Phe Arg Gln His Thr Ala Gly Asp Pro Tyr Ser Asp Tyr Glu Lys Ala 275 280 285 Ser Lys Asp Leu Asp Leu Ser Asn Ala Lys Glu Thr Phe Asn Pro Leu 290 295 300 Val Ala Ala Phe Pro Ser Val Asn Val Ser Leu Glu Asn Val Thr Ile305 310 315 320 Ser Lys Asp Glu Asn Lys Thr Ala Glu Ile Ala Ser Thr Ser Ser Asn 325 330 335 Asn Trp Ser Tyr Thr Asn Thr Glu Gly Ala Ser Ile Glu Ala Gly Ile 340 345 350 Gly Pro Glu Gly Leu Leu Ser Phe Gly Val Ser Ala Asn Tyr Gln His 355 360 365 Ser Glu Thr Val Ala Lys Glu Trp Gly Thr Thr Lys Gly Asp Ala Thr 370 375 380 Gln Tyr Asn Thr Ala Ser Ala Gly Tyr Leu Asn Ala Asn Val Arg Tyr385 390 395 400 Asn Asn Val Gly Thr Ala Ala Ile Tyr Asp Val Lys Pro Thr Thr Asn 405 410 415 Phe Val Leu Asp Lys Thr Thr Leu Ala Thr Ile Lys Ala Lys Glu Asn 420 425 430 Ala Thr Ala Asp His Ile Ile Pro Gly Asn Ser Tyr Pro Glu Lys Gly 435 440 445 Lys Asn Gly Ile Ala Ile Thr Thr Met Asp Asp Phe Asn Ser His Pro 450 455 460 Ile Thr Leu Asn Lys Gln Gln Leu Asp Lys Leu Leu Tyr Asn Val Thr465 470 475 480 Pro Leu Met Leu Glu Thr Thr Gln Val Glu Gly Thr Tyr Lys Lys Lys 485 490 495 Asp Val Asp Gly Asn Ile Ile Thr Gly Gly Thr Trp Ser Gly Val Thr 500 505 510 Gln Gln Ile Glu Ala Gln Thr Ala Ser Ile Ile Val Asp Thr Gly Glu 515 520 525 Gly Val Ser Glu Lys Arg Ile Ala Ala Lys Asp Tyr Asp Asp Pro Glu 530 535 540 Asp Lys Thr Pro Ser Leu Thr Leu Lys Asp Ala Leu Lys Ile Gly Tyr545 550 555 560 Pro Glu Glu Ile Glu Glu Lys Asn Asp Leu Leu Tyr Tyr Lys Gly Lys 565 570 575 Ile Ile Ser Glu Ser Ser Val Met Thr Phe Leu Asp Asn Gly Thr Ser 580 585 590 Glu Lys Val Lys Lys Gln Ile Glu Asp Lys Thr Gly Lys Phe Lys Asp 595 600 605 Val Gln His Leu Tyr Asp Val Lys Leu Thr Pro Gly Met Asn Phe Thr 610 615 620 Ile Lys Leu Ala Ser Ile Tyr Asp Ser Val Asp Asn Phe Ser Gly Ser625 630 635 640 Gln Ser Leu Gly Ala Leu Asn Ser Ile Ser Lys Val Ala Gly Gly Asn 645 650 655 Thr Gly Lys Asn Gln Tyr Gln Ser Ser Ser Ser Asn Ala Tyr Ile Ser 660 665 670 Leu Ser Ser Ser Thr Lys Gly Glu Leu Asn Lys Asn Thr Thr Tyr Tyr 675 680 685 Leu Ser Met Tyr Met Arg Ala Asp Ala Asp Thr Glu Pro Thr Ile Glu 690 695 700 Leu Lys Gly Glu Lys Ser Thr Ile Lys Ser Gln Lys Val Lys Leu Asn705 710 715 720 Asn Lys Gly Tyr Gln Arg Val Asp Ile Leu Val Glu Asn Thr Glu Ser 725 730 735 Asn Pro Ile His Gln Ile Tyr Val His Gly Asn Asn Lys Thr Asn Val 740 745 750 Tyr Trp Asp Asp Val Ser Leu Thr Glu Val Ser Ala Ile Lys Gln Glu 755 760 765 Leu Pro Asp Ile Ser Asp Lys Glu Ile Gln Arg Ala His Thr Phe Lys 770 775 780 Lys Glu Gln Leu Ser Leu Asp Gly Lys Tyr Met Asn Glu Leu Thr Leu785 790 795 800 His Val Asp Ser Leu Lys Asp Lys Asn Asn Lys Pro Val Gln Phe Ser 805 810 815 Tyr Lys Val Lys Asp Gly Glu Lys Asp Leu Gly Thr Lys Ser Tyr Thr 820 825 830 Pro Asp Lys Gln Gly Asn Ile Asn Ile Asn Phe Leu Asp Tyr Asn Arg 835 840 845 Gly Phe Gly Ile Ser Lys Asp His Lys Ile Gln Ile Tyr Ala Val Arg 850 855 860 Lys Asp Gln Glu Val Lys Val Ala Glu Leu Lys Asn Tyr Asn Met Ser865 870 875 880 Gly Thr Ile Arg Phe Ser Asn Asp Gly Glu Ser Gly Leu Pro Glu Ile 885 890 895 Tyr Gly Tyr Ile Phe Met Thr Pro Glu Gly Gln Tyr Pro Val Ser Pro 900 905 910 Val Gly Gly Ile His Gln Ile Trp Ser Arg Tyr Tyr Thr Ser Thr Tyr 915 920 925 Lys Trp Ser Thr Gln Tyr Ser Tyr Asp Phe Ala Ser Phe Asn Ser Asp 930 935 940 Ile Lys Thr Val His Phe Asn Gly Tyr Val Lys Glu Leu Asp Asp Thr945 950 955 960 Asn Gly Asp Asp Ile Leu Ala Tyr Leu Glu Asn Lys Tyr Glu Ser His 965 970 975 Gly Leu Glu Gly Ser Val Val Leu Glu Gly Asp Glu Arg Gly Ser Asn 980 985 990 Val Thr Val Glu Tyr His Ile Lys Leu Lys 995 1000 301347DNABacillus thuringiensisCDS(1)...(1347) 30atg cat aaa caa aca ata aaa aat tta tct att tgc ata gca act gta 48Met His Lys Gln Thr Ile Lys Asn Leu Ser Ile Cys Ile Ala Thr Val1 5 10 15tca cta tta gga caa tac ttt ata tcc tct act acg gta tac gct gct 96Ser Leu Leu Gly Gln Tyr Phe Ile Ser Ser Thr Thr Val Tyr Ala Ala 20 25 30gaa aat caa att aac tca tta aat cta aaa gta gag caa att cta gat 144Glu Asn Gln Ile Asn Ser Leu Asn Leu Lys Val Glu Gln Ile Leu Asp 35 40 45ttt gga aga gat aaa gag aaa gca aaa gaa tgg gcc gat act tac ttt 192Phe Gly Arg Asp Lys Glu Lys Ala Lys Glu Trp Ala Asp Thr Tyr Phe 50 55 60aaa gat tgg aag aaa aca att aat aat gaa caa aaa aaa ctt tta aat 240Lys Asp Trp Lys Lys Thr Ile Asn Asn Glu Gln Lys Lys Leu Leu Asn65 70 75 80gat att aaa cgc tta aca caa tta aat gaa aaa ata ggt aaa ttc gat 288Asp Ile Lys Arg Leu Thr Gln Leu Asn Glu Lys Ile Gly Lys Phe Asp 85 90 95caa aat tca gag atg ttt tct aaa aaa gat aaa gag gat ata gat aaa 336Gln Asn Ser Glu Met Phe Ser Lys Lys Asp Lys Glu Asp Ile Asp Lys 100 105 110ata gac aaa gct ttg aat aat aaa aat gca aaa tta acc aaa tct ttg 384Ile Asp Lys Ala Leu Asn Asn Lys Asn Ala Lys Leu Thr Lys Ser Leu 115 120 125aat gtg tat aaa aat ttg aat ggc aaa gat tta gga tat gta gaa ggt 432Asn Val Tyr Lys Asn Leu Asn Gly Lys Asp Leu Gly Tyr Val Glu Gly 130 135 140tat ttt aat gta ccg aat tcc cca aat aaa ata gat aga aca aaa tat 480Tyr Phe Asn Val Pro Asn Ser Pro Asn Lys Ile Asp Arg Thr Lys Tyr145 150 155 160aat aaa tta gtt aat gag ttt aag tat ggg gct atc aat aca ttc atg 528Asn Lys Leu Val Asn Glu Phe Lys Tyr Gly Ala Ile Asn Thr Phe Met 165 170 175aat aca gac tta aca caa gat act aca aat aaa tca aca cct att ttg 576Asn Thr Asp Leu Thr Gln Asp Thr Thr Asn Lys Ser Thr Pro Ile Leu 180 185 190ctt tca ttg aag cta cca aaa gga aca aaa ata gga caa tta aat gaa 624Leu Ser Leu Lys Leu Pro Lys Gly Thr Lys Ile Gly Gln Leu Asn Glu 195 200 205gaa cat ata ata aca gac aga aac tta gga att gaa ata aaa aaa aca 672Glu His Ile Ile Thr Asp Arg Asn Leu Gly Ile Glu Ile Lys Lys Thr 210 215 220agt att att gtt gaa aaa gga aga gaa gtt att aaa cta gaa gga gac 720Ser Ile Ile Val Glu Lys Gly Arg Glu Val Ile Lys Leu Glu Gly Asp225 230 235 240gta gta cca aaa act aaa att caa gaa aaa gta aaa aaa gca gaa agt 768Val Val Pro Lys Thr Lys Ile Gln Glu Lys Val Lys Lys Ala Glu Ser 245 250 255gat ttg aat caa aaa ttt aaa gaa ata acg ggt tta aaa caa aac tta 816Asp Leu Asn Gln Lys Phe Lys Glu Ile Thr Gly Leu Lys Gln Asn Leu 260 265 270cta agt ctg aaa ata gat aat cta tat aca tca gct agc att gac aga 864Leu Ser Leu Lys Ile Asp Asn Leu Tyr Thr Ser Ala Ser Ile Asp Arg 275 280 285acg gaa aca gtt ata aaa caa tta gtc agc aat gta cca aac aat tta 912Thr Glu Thr Val Ile Lys Gln Leu Val Ser Asn Val Pro Asn Asn Leu 290 295 300ttg tta aat ata atg aaa aat atg aat aat aaa aca tta ttt act att 960Leu Leu Asn Ile Met Lys Asn Met Asn Asn Lys Thr Leu Phe Thr Ile305 310 315 320aca gat aaa att cta ata ccc ggc aag gaa ggt gta tta ggt tat tat 1008Thr Asp Lys Ile Leu Ile Pro Gly Lys Glu Gly Val Leu Gly Tyr Tyr 325 330 335gat acc att tct aaa aca tta ttt ata caa att gat cat ttg ggg cat 1056Asp Thr Ile Ser Lys Thr Leu Phe Ile Gln Ile Asp His Leu Gly His 340 345 350aaa aac aat gaa gga aat gac act aat act ctt ctt cat gaa ttt ggt 1104Lys Asn Asn Glu Gly Asn Asp Thr Asn Thr Leu Leu His Glu Phe Gly 355 360 365cat gct gta gat cat ttg gca aaa ggg gag ata caa tca aaa tct agt 1152His Ala Val Asp His Leu Ala Lys Gly Glu Ile Gln Ser Lys Ser Ser 370 375 380aag ttc att gaa ata ttt aat cga gag aga ggt aat att aca ata gaa 1200Lys Phe Ile Glu Ile Phe Asn Arg Glu Arg Gly Asn Ile Thr Ile Glu385 390 395 400cca tat att aaa caa gat gca gcg gaa ttt ttt gca ggt gtt ttt aat 1248Pro Tyr Ile Lys Gln Asp Ala Ala Glu Phe Phe Ala Gly Val Phe Asn 405 410 415tac tta tat tca cct aaa ata tca gat aga gaa caa att caa aaa gaa 1296Tyr Leu Tyr Ser Pro Lys Ile Ser Asp Arg Glu Gln Ile Gln Lys Glu 420 425 430gca cct gat gct tgt aaa ttt atc cga aat tta ata cat ggt cta cat 1344Ala Pro Asp Ala Cys Lys Phe Ile Arg Asn Leu Ile His Gly Leu His 435 440 445tga 134731448PRTBacillus thuringiensis 31Met His Lys Gln Thr Ile Lys Asn Leu Ser Ile Cys Ile Ala Thr Val1 5 10 15 Ser Leu Leu Gly Gln Tyr Phe Ile Ser Ser Thr Thr Val Tyr Ala Ala 20 25 30 Glu Asn Gln Ile Asn Ser Leu Asn Leu Lys Val Glu Gln Ile Leu Asp 35 40

45 Phe Gly Arg Asp Lys Glu Lys Ala Lys Glu Trp Ala Asp Thr Tyr Phe 50 55 60 Lys Asp Trp Lys Lys Thr Ile Asn Asn Glu Gln Lys Lys Leu Leu Asn65 70 75 80 Asp Ile Lys Arg Leu Thr Gln Leu Asn Glu Lys Ile Gly Lys Phe Asp 85 90 95 Gln Asn Ser Glu Met Phe Ser Lys Lys Asp Lys Glu Asp Ile Asp Lys 100 105 110 Ile Asp Lys Ala Leu Asn Asn Lys Asn Ala Lys Leu Thr Lys Ser Leu 115 120 125 Asn Val Tyr Lys Asn Leu Asn Gly Lys Asp Leu Gly Tyr Val Glu Gly 130 135 140 Tyr Phe Asn Val Pro Asn Ser Pro Asn Lys Ile Asp Arg Thr Lys Tyr145 150 155 160 Asn Lys Leu Val Asn Glu Phe Lys Tyr Gly Ala Ile Asn Thr Phe Met 165 170 175 Asn Thr Asp Leu Thr Gln Asp Thr Thr Asn Lys Ser Thr Pro Ile Leu 180 185 190 Leu Ser Leu Lys Leu Pro Lys Gly Thr Lys Ile Gly Gln Leu Asn Glu 195 200 205 Glu His Ile Ile Thr Asp Arg Asn Leu Gly Ile Glu Ile Lys Lys Thr 210 215 220 Ser Ile Ile Val Glu Lys Gly Arg Glu Val Ile Lys Leu Glu Gly Asp225 230 235 240 Val Val Pro Lys Thr Lys Ile Gln Glu Lys Val Lys Lys Ala Glu Ser 245 250 255 Asp Leu Asn Gln Lys Phe Lys Glu Ile Thr Gly Leu Lys Gln Asn Leu 260 265 270 Leu Ser Leu Lys Ile Asp Asn Leu Tyr Thr Ser Ala Ser Ile Asp Arg 275 280 285 Thr Glu Thr Val Ile Lys Gln Leu Val Ser Asn Val Pro Asn Asn Leu 290 295 300 Leu Leu Asn Ile Met Lys Asn Met Asn Asn Lys Thr Leu Phe Thr Ile305 310 315 320 Thr Asp Lys Ile Leu Ile Pro Gly Lys Glu Gly Val Leu Gly Tyr Tyr 325 330 335 Asp Thr Ile Ser Lys Thr Leu Phe Ile Gln Ile Asp His Leu Gly His 340 345 350 Lys Asn Asn Glu Gly Asn Asp Thr Asn Thr Leu Leu His Glu Phe Gly 355 360 365 His Ala Val Asp His Leu Ala Lys Gly Glu Ile Gln Ser Lys Ser Ser 370 375 380 Lys Phe Ile Glu Ile Phe Asn Arg Glu Arg Gly Asn Ile Thr Ile Glu385 390 395 400 Pro Tyr Ile Lys Gln Asp Ala Ala Glu Phe Phe Ala Gly Val Phe Asn 405 410 415 Tyr Leu Tyr Ser Pro Lys Ile Ser Asp Arg Glu Gln Ile Gln Lys Glu 420 425 430 Ala Pro Asp Ala Cys Lys Phe Ile Arg Asn Leu Ile His Gly Leu His 435 440 445 321113DNAPaenibacillus popilliaeCDS(1)...(1113) 32atg aat aaa tta att aaa gta gaa gaa aat aaa aca cct caa acc caa 48Met Asn Lys Leu Ile Lys Val Glu Glu Asn Lys Thr Pro Gln Thr Gln1 5 10 15act ata tac act agt ttt aac gca acc gat att ggt ttt gca tcg aat 96Thr Ile Tyr Thr Ser Phe Asn Ala Thr Asp Ile Gly Phe Ala Ser Asn 20 25 30tca gat ata aaa gat gga ttt cta aat ttt gat gag caa aaa ata aat 144Ser Asp Ile Lys Asp Gly Phe Leu Asn Phe Asp Glu Gln Lys Ile Asn 35 40 45aca att ata aaa tat tta aaa atg gga aat ttc cca gat ttt cga gtg 192Thr Ile Ile Lys Tyr Leu Lys Met Gly Asn Phe Pro Asp Phe Arg Val 50 55 60ggg aat ttg tta cca tcc gaa cca cat tcc aca gta aat gct ttc ttt 240Gly Asn Leu Leu Pro Ser Glu Pro His Ser Thr Val Asn Ala Phe Phe65 70 75 80aca caa agg cga att tta ata gag tta gag gtt ccg gct ggt act tat 288Thr Gln Arg Arg Ile Leu Ile Glu Leu Glu Val Pro Ala Gly Thr Tyr 85 90 95ctt gcg cat tta gga aac ggt caa acc att ttc cct tta gat tat gga 336Leu Ala His Leu Gly Asn Gly Gln Thr Ile Phe Pro Leu Asp Tyr Gly 100 105 110atg aag tta act gat cag gcg gga acg att att gga aag caa gta cta 384Met Lys Leu Thr Asp Gln Ala Gly Thr Ile Ile Gly Lys Gln Val Leu 115 120 125aaa ttg aaa gca ctt gtt gtc ccg aag gat gat att ctg aaa gaa act 432Lys Leu Lys Ala Leu Val Val Pro Lys Asp Asp Ile Leu Lys Glu Thr 130 135 140aat gtg cag atg ttc att tta tac aaa tca ata tcc aat ata ttg cgt 480Asn Val Gln Met Phe Ile Leu Tyr Lys Ser Ile Ser Asn Ile Leu Arg145 150 155 160tct aag gga ttt gat gaa aag gat ata gaa agc ctg aaa gct cag tgc 528Ser Lys Gly Phe Asp Glu Lys Asp Ile Glu Ser Leu Lys Ala Gln Cys 165 170 175atg ttt ata ttt tca ggc cct aat gta ttg ttg gca ata gaa aat tct 576Met Phe Ile Phe Ser Gly Pro Asn Val Leu Leu Ala Ile Glu Asn Ser 180 185 190caa agt gca atg ctt gat tta cta act aat gag tat ata cca aat aat 624Gln Ser Ala Met Leu Asp Leu Leu Thr Asn Glu Tyr Ile Pro Asn Asn 195 200 205tta tta aga gat aca ttg tta aaa tta aaa caa cac gcg ggg att gct 672Leu Leu Arg Asp Thr Leu Leu Lys Leu Lys Gln His Ala Gly Ile Ala 210 215 220ttt cta agt gtg cct att tgt atg gat aaa gcg att gcc ggg agt aca 720Phe Leu Ser Val Pro Ile Cys Met Asp Lys Ala Ile Ala Gly Ser Thr225 230 235 240tca ttt cct aaa aat ggc gat aaa cct aat atg agt ata atc cca acc 768Ser Phe Pro Lys Asn Gly Asp Lys Pro Asn Met Ser Ile Ile Pro Thr 245 250 255cat caa tct tta ctg agc cag ttg gat gaa cat ata agt aca tca cgt 816His Gln Ser Leu Leu Ser Gln Leu Asp Glu His Ile Ser Thr Ser Arg 260 265 270aca tta cat cat gaa ttt ggt cat gta ata gat cga gaa att cta aat 864Thr Leu His His Glu Phe Gly His Val Ile Asp Arg Glu Ile Leu Asn 275 280 285ggg att tct tcc act cca gag ttt aaa gcg ctg ttt gaa aaa gaa aaa 912Gly Ile Ser Ser Thr Pro Glu Phe Lys Ala Leu Phe Glu Lys Glu Lys 290 295 300aat aat att aca gaa ata aat acg tat gcc aac tat gca aaa acg aat 960Asn Asn Ile Thr Glu Ile Asn Thr Tyr Ala Asn Tyr Ala Lys Thr Asn305 310 315 320tca caa gaa ttt ttt gca gag gtt ttt aaa tct atg gtt tcc atg ggg 1008Ser Gln Glu Phe Phe Ala Glu Val Phe Lys Ser Met Val Ser Met Gly 325 330 335aat gag aaa tat cca tca agt tat tat cgt gat tct att gag aaa gaa 1056Asn Glu Lys Tyr Pro Ser Ser Tyr Tyr Arg Asp Ser Ile Glu Lys Glu 340 345 350gct cct gag act gtg aga ttt ata aaa gat aaa ttg aaa gag aaa gga 1104Ala Pro Glu Thr Val Arg Phe Ile Lys Asp Lys Leu Lys Glu Lys Gly 355 360 365tat gta ctt 1113Tyr Val Leu 37033371PRTPaenibacillus popilliae 33Met Asn Lys Leu Ile Lys Val Glu Glu Asn Lys Thr Pro Gln Thr Gln1 5 10 15 Thr Ile Tyr Thr Ser Phe Asn Ala Thr Asp Ile Gly Phe Ala Ser Asn 20 25 30 Ser Asp Ile Lys Asp Gly Phe Leu Asn Phe Asp Glu Gln Lys Ile Asn 35 40 45 Thr Ile Ile Lys Tyr Leu Lys Met Gly Asn Phe Pro Asp Phe Arg Val 50 55 60 Gly Asn Leu Leu Pro Ser Glu Pro His Ser Thr Val Asn Ala Phe Phe65 70 75 80 Thr Gln Arg Arg Ile Leu Ile Glu Leu Glu Val Pro Ala Gly Thr Tyr 85 90 95 Leu Ala His Leu Gly Asn Gly Gln Thr Ile Phe Pro Leu Asp Tyr Gly 100 105 110 Met Lys Leu Thr Asp Gln Ala Gly Thr Ile Ile Gly Lys Gln Val Leu 115 120 125 Lys Leu Lys Ala Leu Val Val Pro Lys Asp Asp Ile Leu Lys Glu Thr 130 135 140 Asn Val Gln Met Phe Ile Leu Tyr Lys Ser Ile Ser Asn Ile Leu Arg145 150 155 160 Ser Lys Gly Phe Asp Glu Lys Asp Ile Glu Ser Leu Lys Ala Gln Cys 165 170 175 Met Phe Ile Phe Ser Gly Pro Asn Val Leu Leu Ala Ile Glu Asn Ser 180 185 190 Gln Ser Ala Met Leu Asp Leu Leu Thr Asn Glu Tyr Ile Pro Asn Asn 195 200 205 Leu Leu Arg Asp Thr Leu Leu Lys Leu Lys Gln His Ala Gly Ile Ala 210 215 220 Phe Leu Ser Val Pro Ile Cys Met Asp Lys Ala Ile Ala Gly Ser Thr225 230 235 240 Ser Phe Pro Lys Asn Gly Asp Lys Pro Asn Met Ser Ile Ile Pro Thr 245 250 255 His Gln Ser Leu Leu Ser Gln Leu Asp Glu His Ile Ser Thr Ser Arg 260 265 270 Thr Leu His His Glu Phe Gly His Val Ile Asp Arg Glu Ile Leu Asn 275 280 285 Gly Ile Ser Ser Thr Pro Glu Phe Lys Ala Leu Phe Glu Lys Glu Lys 290 295 300 Asn Asn Ile Thr Glu Ile Asn Thr Tyr Ala Asn Tyr Ala Lys Thr Asn305 310 315 320 Ser Gln Glu Phe Phe Ala Glu Val Phe Lys Ser Met Val Ser Met Gly 325 330 335 Asn Glu Lys Tyr Pro Ser Ser Tyr Tyr Arg Asp Ser Ile Glu Lys Glu 340 345 350 Ala Pro Glu Thr Val Arg Phe Ile Lys Asp Lys Leu Lys Glu Lys Gly 355 360 365 Tyr Val Leu 370 34987DNABacillus thuringiensisCDS(1)...(987) 34atg gtg aga gac tat cct gat ttt gat ggg atg ata aga aaa gcc gct 48Met Val Arg Asp Tyr Pro Asp Phe Asp Gly Met Ile Arg Lys Ala Ala1 5 10 15cga aag tgg gca gaa gca aac aga ttg aca ttc caa gat att tcg tat 96Arg Lys Trp Ala Glu Ala Asn Arg Leu Thr Phe Gln Asp Ile Ser Tyr 20 25 30gca gat cct tta acc aat tca gat aca atc agt cta aat gcc aaa ttc 144Ala Asp Pro Leu Thr Asn Ser Asp Thr Ile Ser Leu Asn Ala Lys Phe 35 40 45aaa gat atc gga tgc ccc gaa gaa tgt gtc gaa tta gaa aaa ata agc 192Lys Asp Ile Gly Cys Pro Glu Glu Cys Val Glu Leu Glu Lys Ile Ser 50 55 60gtc gca caa gct ttt acg aat aat acg ggg caa caa caa aaa gaa aca 240Val Ala Gln Ala Phe Thr Asn Asn Thr Gly Gln Gln Gln Lys Glu Thr65 70 75 80ttt aca acc gca aca ttt gta gaa gat gag tat act tgg gag aat gac 288Phe Thr Thr Ala Thr Phe Val Glu Asp Glu Tyr Thr Trp Glu Asn Asp 85 90 95tat cat ttt gtg ctt cca gga caa aac ttc ctt ata atg ccc cgt ctt 336Tyr His Phe Val Leu Pro Gly Gln Asn Phe Leu Ile Met Pro Arg Leu 100 105 110cct cgg tca gct cat agg gat att aat cca ggt ttc ctt gtg aat ttc 384Pro Arg Ser Ala His Arg Asp Ile Asn Pro Gly Phe Leu Val Asn Phe 115 120 125ttt ggt caa aat caa caa ttt cat act aaa atg aga gat cta cgt cca 432Phe Gly Gln Asn Gln Gln Phe His Thr Lys Met Arg Asp Leu Arg Pro 130 135 140att aac ggg gaa gta ttt tta gaa cca tct agc agt gca aca att caa 480Ile Asn Gly Glu Val Phe Leu Glu Pro Ser Ser Ser Ala Thr Ile Gln145 150 155 160ctg caa gtg gaa aaa caa tat att tct caa ccg tat gaa att gaa tta 528Leu Gln Val Glu Lys Gln Tyr Ile Ser Gln Pro Tyr Glu Ile Glu Leu 165 170 175tcg ata cta gga agt att att gtg ata gca cga gat ggg cag aac cga 576Ser Ile Leu Gly Ser Ile Ile Val Ile Ala Arg Asp Gly Gln Asn Arg 180 185 190agc agt gag aac tat gtt caa tta aca gat ctc atg cca ctt ctc tgc 624Ser Ser Glu Asn Tyr Val Gln Leu Thr Asp Leu Met Pro Leu Leu Cys 195 200 205cct tgt aaa aac ttt ttt tgt aga ggg cga gcg ttg gta ttc gtt gaa 672Pro Cys Lys Asn Phe Phe Cys Arg Gly Arg Ala Leu Val Phe Val Glu 210 215 220cag gga acg ttc aag gga gta ttg agc cga gcg ata cgt gca tac gtc 720Gln Gly Thr Phe Lys Gly Val Leu Ser Arg Ala Ile Arg Ala Tyr Val225 230 235 240aca caa acg ctt cac aaa gac gga aaa acg cta gaa tat gaa att cct 768Thr Gln Thr Leu His Lys Asp Gly Lys Thr Leu Glu Tyr Glu Ile Pro 245 250 255tta aac gca tca cct gac agg gaa agc gaa ttc tcc cca caa cct ttg 816Leu Asn Ala Ser Pro Asp Arg Glu Ser Glu Phe Ser Pro Gln Pro Leu 260 265 270gca gca aga tgt atc tca gac gaa gaa tcg aat ggg aac cct tcg att 864Ala Ala Arg Cys Ile Ser Asp Glu Glu Ser Asn Gly Asn Pro Ser Ile 275 280 285ttg tca tcg aga cca tcg aat cct aca gcc tat tcc cag caa cct atg 912Leu Ser Ser Arg Pro Ser Asn Pro Thr Ala Tyr Ser Gln Gln Pro Met 290 295 300aca act gac tct aca tcc tgt gga tgt tct tct tgt atg tct gaa aaa 960Thr Thr Asp Ser Thr Ser Cys Gly Cys Ser Ser Cys Met Ser Glu Lys305 310 315 320tca aat aac aat cta tat ata aat cag 987Ser Asn Asn Asn Leu Tyr Ile Asn Gln 32535329PRTBacillus thuringiensis 35Met Val Arg Asp Tyr Pro Asp Phe Asp Gly Met Ile Arg Lys Ala Ala1 5 10 15 Arg Lys Trp Ala Glu Ala Asn Arg Leu Thr Phe Gln Asp Ile Ser Tyr 20 25 30 Ala Asp Pro Leu Thr Asn Ser Asp Thr Ile Ser Leu Asn Ala Lys Phe 35 40 45 Lys Asp Ile Gly Cys Pro Glu Glu Cys Val Glu Leu Glu Lys Ile Ser 50 55 60 Val Ala Gln Ala Phe Thr Asn Asn Thr Gly Gln Gln Gln Lys Glu Thr65 70 75 80 Phe Thr Thr Ala Thr Phe Val Glu Asp Glu Tyr Thr Trp Glu Asn Asp 85 90 95 Tyr His Phe Val Leu Pro Gly Gln Asn Phe Leu Ile Met Pro Arg Leu 100 105 110 Pro Arg Ser Ala His Arg Asp Ile Asn Pro Gly Phe Leu Val Asn Phe 115 120 125 Phe Gly Gln Asn Gln Gln Phe His Thr Lys Met Arg Asp Leu Arg Pro 130 135 140 Ile Asn Gly Glu Val Phe Leu Glu Pro Ser Ser Ser Ala Thr Ile Gln145 150 155 160 Leu Gln Val Glu Lys Gln Tyr Ile Ser Gln Pro Tyr Glu Ile Glu Leu 165 170 175 Ser Ile Leu Gly Ser Ile Ile Val Ile Ala Arg Asp Gly Gln Asn Arg 180 185 190 Ser Ser Glu Asn Tyr Val Gln Leu Thr Asp Leu Met Pro Leu Leu Cys 195 200 205 Pro Cys Lys Asn Phe Phe Cys Arg Gly Arg Ala Leu Val Phe Val Glu 210 215 220 Gln Gly Thr Phe Lys Gly Val Leu Ser Arg Ala Ile Arg Ala Tyr Val225 230 235 240 Thr Gln Thr Leu His Lys Asp Gly Lys Thr Leu Glu Tyr Glu Ile Pro 245 250 255 Leu Asn Ala Ser Pro Asp Arg Glu Ser Glu Phe Ser Pro Gln Pro Leu 260 265 270 Ala Ala Arg Cys Ile Ser Asp Glu Glu Ser Asn Gly Asn Pro Ser Ile 275 280 285 Leu Ser Ser Arg Pro Ser Asn Pro Thr Ala Tyr Ser Gln Gln Pro Met 290 295 300 Thr Thr Asp Ser Thr Ser Cys Gly Cys Ser Ser Cys Met Ser Glu Lys305 310 315 320 Ser Asn Asn Asn Leu Tyr Ile Asn Gln 325 361071DNABacillus thuringiensisCDS(1)...(1071) 36atg aaa aag tct tgt aat ccc aag aaa gta aat cct aac gaa gtg aat 48Met Lys Lys Ser Cys Asn Pro Lys Lys Val Asn Pro Asn Glu Val Asn1 5 10 15cca aca gaa ttt att tta tac gac ttg gat aac tat tta aat cat att 96Pro Thr Glu Phe Ile Leu Tyr Asp Leu Asp Asn Tyr Leu Asn His Ile 20 25 30ttg cat aat gta cag tac gac cct gtg aat ctg tcc agt atg tac gac 144Leu His Asn Val Gln Tyr Asp Pro Val Asn Leu Ser Ser Met Tyr Asp 35 40 45ggt tat aag cca tca ggt ggt tgg aat ttt gat gga aaa ttc tat cct 192Gly Tyr Lys Pro Ser Gly Gly Trp Asn Phe Asp Gly Lys Phe Tyr Pro 50 55 60acc cca act tct agc caa ata cct aac gct tgc gta cca tac ggt aca 240Thr Pro Thr Ser Ser Gln Ile Pro Asn Ala Cys Val Pro Tyr Gly Thr65 70 75

80tac aaa cct tat tgt aaa tat gaa cca tat caa agt ggt act tgg gtt 288Tyr Lys Pro Tyr Cys Lys Tyr Glu Pro Tyr Gln Ser Gly Thr Trp Val 85 90 95gta gat aca tcc gct tta atc gca gaa ggg aca gat ata tat gaa gaa 336Val Asp Thr Ser Ala Leu Ile Ala Glu Gly Thr Asp Ile Tyr Glu Glu 100 105 110atc gaa tcc atg gct cta gaa acc cct att att gcg gat aga cat gaa 384Ile Glu Ser Met Ala Leu Glu Thr Pro Ile Ile Ala Asp Arg His Glu 115 120 125tat aat aat aac tca tct tta gaa caa tcc tat gtg acc cct gcc tat 432Tyr Asn Asn Asn Ser Ser Leu Glu Gln Ser Tyr Val Thr Pro Ala Tyr 130 135 140tca gaa aca acg act aca act acg aca aat aca aca aca cac gga tgt 480Ser Glu Thr Thr Thr Thr Thr Thr Thr Asn Thr Thr Thr His Gly Cys145 150 155 160aaa gta aat cca aaa atc agt tat tcg cgt aaa tcg aaa tat aaa gtt 528Lys Val Asn Pro Lys Ile Ser Tyr Ser Arg Lys Ser Lys Tyr Lys Val 165 170 175ggt att aag gat aca gaa aat gga ttt aac ctg gaa tta ggg gca gaa 576Gly Ile Lys Asp Thr Glu Asn Gly Phe Asn Leu Glu Leu Gly Ala Glu 180 185 190tat aac ttc agc aat aca aac tca aac acg gct acg aca act cgg act 624Tyr Asn Phe Ser Asn Thr Asn Ser Asn Thr Ala Thr Thr Thr Arg Thr 195 200 205gtg aca ttt cca tca ttt acg aca aaa gtg cca ccc tat acc act acg 672Val Thr Phe Pro Ser Phe Thr Thr Lys Val Pro Pro Tyr Thr Thr Thr 210 215 220att gtg acg gtc ata tta aac aaa gga aca tat gcc aat tat aat gtt 720Ile Val Thr Val Ile Leu Asn Lys Gly Thr Tyr Ala Asn Tyr Asn Val225 230 235 240cca gtc caa acg aat tta ttt ggg aga ttt ctc act cat cac ggc caa 768Pro Val Gln Thr Asn Leu Phe Gly Arg Phe Leu Thr His His Gly Gln 245 250 255ggc atg gat cca aac gac tcg cgt acg tac aat tat ttt gac cta tat 816Gly Met Asp Pro Asn Asp Ser Arg Thr Tyr Asn Tyr Phe Asp Leu Tyr 260 265 270cct tgc gta gaa tta aat caa aca tgc tgt gca gca tca tct tgt agc 864Pro Cys Val Glu Leu Asn Gln Thr Cys Cys Ala Ala Ser Ser Cys Ser 275 280 285gaa tgt gta aca gac atg gtg caa gct ctt cct gac aat ctt acg gtt 912Glu Cys Val Thr Asp Met Val Gln Ala Leu Pro Asp Asn Leu Thr Val 290 295 300cgt ttt aat gga aca ggg tca ttt ata gcg gat gtt gca tcg aat aac 960Arg Phe Asn Gly Thr Gly Ser Phe Ile Ala Asp Val Ala Ser Asn Asn305 310 315 320ttt gtc att act act gaa gag gtt gac aat gca aca gga gta acc att 1008Phe Val Ile Thr Thr Glu Glu Val Asp Asn Ala Thr Gly Val Thr Ile 325 330 335tcg aaa aaa aca gaa tac gta ccc gct att tac gga ccc ccg acc aca 1056Ser Lys Lys Thr Glu Tyr Val Pro Ala Ile Tyr Gly Pro Pro Thr Thr 340 345 350aca gta acc aca tct 1071Thr Val Thr Thr Ser 35537357PRTBacillus thuringiensis 37Met Lys Lys Ser Cys Asn Pro Lys Lys Val Asn Pro Asn Glu Val Asn1 5 10 15 Pro Thr Glu Phe Ile Leu Tyr Asp Leu Asp Asn Tyr Leu Asn His Ile 20 25 30 Leu His Asn Val Gln Tyr Asp Pro Val Asn Leu Ser Ser Met Tyr Asp 35 40 45 Gly Tyr Lys Pro Ser Gly Gly Trp Asn Phe Asp Gly Lys Phe Tyr Pro 50 55 60 Thr Pro Thr Ser Ser Gln Ile Pro Asn Ala Cys Val Pro Tyr Gly Thr65 70 75 80 Tyr Lys Pro Tyr Cys Lys Tyr Glu Pro Tyr Gln Ser Gly Thr Trp Val 85 90 95 Val Asp Thr Ser Ala Leu Ile Ala Glu Gly Thr Asp Ile Tyr Glu Glu 100 105 110 Ile Glu Ser Met Ala Leu Glu Thr Pro Ile Ile Ala Asp Arg His Glu 115 120 125 Tyr Asn Asn Asn Ser Ser Leu Glu Gln Ser Tyr Val Thr Pro Ala Tyr 130 135 140 Ser Glu Thr Thr Thr Thr Thr Thr Thr Asn Thr Thr Thr His Gly Cys145 150 155 160 Lys Val Asn Pro Lys Ile Ser Tyr Ser Arg Lys Ser Lys Tyr Lys Val 165 170 175 Gly Ile Lys Asp Thr Glu Asn Gly Phe Asn Leu Glu Leu Gly Ala Glu 180 185 190 Tyr Asn Phe Ser Asn Thr Asn Ser Asn Thr Ala Thr Thr Thr Arg Thr 195 200 205 Val Thr Phe Pro Ser Phe Thr Thr Lys Val Pro Pro Tyr Thr Thr Thr 210 215 220 Ile Val Thr Val Ile Leu Asn Lys Gly Thr Tyr Ala Asn Tyr Asn Val225 230 235 240 Pro Val Gln Thr Asn Leu Phe Gly Arg Phe Leu Thr His His Gly Gln 245 250 255 Gly Met Asp Pro Asn Asp Ser Arg Thr Tyr Asn Tyr Phe Asp Leu Tyr 260 265 270 Pro Cys Val Glu Leu Asn Gln Thr Cys Cys Ala Ala Ser Ser Cys Ser 275 280 285 Glu Cys Val Thr Asp Met Val Gln Ala Leu Pro Asp Asn Leu Thr Val 290 295 300 Arg Phe Asn Gly Thr Gly Ser Phe Ile Ala Asp Val Ala Ser Asn Asn305 310 315 320 Phe Val Ile Thr Thr Glu Glu Val Asp Asn Ala Thr Gly Val Thr Ile 325 330 335 Ser Lys Lys Thr Glu Tyr Val Pro Ala Ile Tyr Gly Pro Pro Thr Thr 340 345 350 Thr Val Thr Thr Ser 355 38292PRTBacillus sphaericus 38Met Lys Arg Thr Lys Leu Leu Phe Tyr Ile Met Ile Ala Ser Phe Leu1 5 10 15 Phe Val Asn Gly Ser Ile Tyr Thr Ala Lys Ala Thr Thr Ile Asp Glu 20 25 30 Asn Asn Leu Asp Ile Ile Lys Gln Gln Gly Val Ser Ile Glu Asp Ile 35 40 45 Asp Arg Lys Ile Asp Asn Met Ile Ala Ser Ile Pro Pro Leu Phe Gly 50 55 60 Phe Leu Pro Tyr Ser Arg Phe Pro Tyr Ile Phe Gly Glu Ser Val Asp65 70 75 80 Val Ser Gly Ile Asn Ile Glu Asn Thr Asn Val Thr Ser Val Val Pro 85 90 95 Leu Phe Ile Gly Ser Asn Thr Phe Glu Asn Thr Thr Asp Arg Thr Met 100 105 110 Thr Phe Asn Thr Val Ser Phe Ser Lys Ser Ile Thr Asp Ser Thr Thr 115 120 125 Thr Gln Thr Leu Asn Gly Phe Lys Thr Ala Phe Glu Ala Ser Gly Lys 130 135 140 Val Gly Ile Pro Leu Val Ala Glu Gly Gln Ile Lys Thr Thr Leu Glu145 150 155 160 Tyr Asn Phe Ser His Thr Asn Ser Asn Thr Thr Ser Val Thr Thr Thr 165 170 175 Tyr Thr Val Pro Pro Gln Pro Ile Pro Val Pro Pro His Thr Lys Thr 180 185 190 Arg Thr Asp Val Tyr Leu Asn Gln Val Ser Ile Ser Gly Asn Val Glu 195 200 205 Ile Tyr Ala Asp Ala Ile Thr Gly Ile Lys Ala Glu Ser Ser Gly Thr 210 215 220 Val Ile Ser Ile Gly Asp Gly Leu Asn Leu Ala Ser Asn Thr Tyr Gly225 230 235 240 Leu Ile Arg Ser Pro Gln Asp Pro Asp Arg Val Arg Ala Ile Gly Ser 245 250 255 Gly Lys Phe Asn Leu Ile His Gly Ala Asp Phe Thr Ala Ile Thr Tyr 260 265 270 Asp Ile Thr Ser Gly Glu Ala Ser Ala Arg Ile Ile Asp Val Lys Glu 275 280 285 Ile Ser Phe Lys 290 39362PRTBacillus sphaericus 39Ser Phe Ile Pro Thr Glu Gly Lys Tyr Ile Arg Val Met Asp Phe Tyr1 5 10 15 Asn Ser Glu Tyr Pro Phe Cys Ile His Ala Pro Ser Ala Pro Asn Gly 20 25 30 Asp Ile Met Thr Glu Ile Cys Ser Arg Glu Asn Asn Gln Tyr Phe Ile 35 40 45 Phe Phe Pro Thr Asp Asp Gly Arg Val Ile Ile Ala Asn Arg His Asn 50 55 60 Gly Ser Val Phe Thr Gly Glu Ala Thr Ser Val Val Ser Asp Ile Tyr65 70 75 80 Thr Gly Ser Pro Ser Gln Phe Phe Arg Glu Val Lys Arg Thr Met Ser 85 90 95 Thr Tyr Tyr Leu Ala Ile Gln Asn Pro Glu Ser Ala Thr Asp Val Arg 100 105 110 Ala Leu Glu Pro Asn Ser His Glu Leu Pro Ser Arg Leu Tyr Phe Thr 115 120 125 Asn Asn Ile Glu Asn Asn Ser Asn Ile Leu Ile Ser Asn Lys Glu Gln 130 135 140 Ile Tyr Leu Thr Leu Pro Ser Leu Pro Glu Asn Glu Gln Tyr Pro Lys145 150 155 160 Thr Pro Val Leu Ser Gly Ile Asp Asp Ile Gly Pro Asn Gln Ser Glu 165 170 175 Lys Ser Ile Ile Gly Ser Thr Leu Ile Pro Cys Ile Met Val Ser Asp 180 185 190 Phe Ile Ser Leu Gly Glu Arg Met Lys Thr Thr Pro Tyr Tyr Tyr Val 195 200 205 Lys His Thr Gln Tyr Trp Gln Ser Met Trp Ser Ala Leu Phe Pro Pro 210 215 220 Gly Ser Lys Glu Thr Lys Thr Glu Lys Ser Gly Ile Thr Asp Thr Ser225 230 235 240 Gln Ile Ser Met Thr Asp Gly Ile Asn Val Ser Ile Gly Ala Asp Phe 245 250 255 Gly Leu Lys Phe Gly Asn Lys Thr Phe Gly Ile Lys Gly Gly Phe Thr 260 265 270 Tyr Asp Thr Lys Thr Gln Ile Thr Asn Thr Ser Gln Leu Leu Ile Glu 275 280 285 Thr Thr Tyr Thr Arg Glu Tyr Thr Asn Thr Glu Asn Phe Pro Val Arg 290 295 300 Tyr Thr Gly Tyr Val Leu Ala Ser Glu Phe Thr Leu His Arg Ser Asp305 310 315 320 Gly Thr Gln Val Asn Thr Ile Pro Trp Val Ala Leu Asn Asp Asn Tyr 325 330 335 Thr Thr Ile Ala Arg Tyr Pro His Phe Ala Ser Glu Pro Leu Leu Gly 340 345 350 Asn Thr Lys Ile Ile Thr Asp Asp Gln Asn 355 360 40327PRTBacillus sphaericus 40Met Met Lys Asn Lys Ala Lys Val Ile Leu Met Gly Ala Thr Ile Gly1 5 10 15 Leu Ser Leu Leu Ser Ser Pro Ile Ala Met Ala Ala Asn Gly Asp Ser 20 25 30 Asn Val Lys Glu Asn Gln Ser Ile Ala Asn Phe Ser Pro Val Lys Asn 35 40 45 Ser Phe Pro Asp Ala Ala Asn Gly Ser Arg Phe Leu Val Asn Tyr Tyr 50 55 60 Gly Arg Tyr Leu Thr Ser Asn Gly Leu Gly Ser Ile Gly Lys His Pro65 70 75 80 Glu Asn Ile Asp Phe Glu Val Lys Asn Thr Tyr Gly Lys Leu Ser Met 85 90 95 Glu Pro Gln Val Ile Ser Gln Asn Pro Leu Trp Ala Gly Gln Ser Asp 100 105 110 Leu Arg Asn Asp Thr Asp Arg Asp Gln Thr Leu Ser Ser Gln Glu Phe 115 120 125 Arg Lys Ser Phe Ser Asn Thr Thr Thr Ala Thr Thr Glu His Gly Phe 130 135 140 Met Phe Gly Thr Glu Thr Ser Leu Ala Thr Gly Ile Pro Phe Leu Ala145 150 155 160 Glu Gly Lys Ile Thr Leu Lys Ala Glu Tyr Asn Phe Ser Ser Ser Gln 165 170 175 Ala Asn Glu Thr Ser Glu Thr Val Glu Tyr Val Ala Pro Ser Gln Ser 180 185 190 Ile Val Val Pro Pro His Thr Ile Ala Arg Val Val Ala Val Leu Glu 195 200 205 Ile Lys Lys Ile Lys Gly Glu Met Asp Ile Tyr Ala Glu Val Gly Leu 210 215 220 Asn Lys Glu Lys Phe Gly Tyr Glu Glu Leu Pro Ile Ser Ser Met Gly225 230 235 240 Gly Leu Lys Trp Val Ser Leu Gly Ser Ile Tyr Glu Glu Ala Tyr Asn 245 250 255 Gln Ala Lys Leu Ser Gly Thr His Glu Phe Pro Asp Ile Lys Ile Ile 260 265 270 Ser Arg Ser Val Asn Asn Pro Asp Tyr Phe Leu Ala Ser Gly Lys Gly 275 280 285 Arg Phe Glu Ser Glu Tyr Gly Ser Leu Phe Asn Val Gln Val Glu Tyr 290 295 300 Ile Ser Thr Lys Ser Asn Glu Val Ile Lys Thr Glu Asn Leu Met Val305 310 315 320 Ser Pro Thr Ile Ile Ser Glu 325 4179PRTBacillus thuringiensis 41Met Ser Ala Asp Gly Thr Thr Ser Phe Ser Gln Asn Phe Glu Leu Pro1 5 10 15 Lys Asp Thr Val Pro Ala Thr Pro Lys Gly Asp Ala Lys Thr Val Glu 20 25 30 Arg Thr Glu Gly Thr Gly Thr Asp Ser Gly Glu Gly Lys Met Val Glu 35 40 45 Thr Lys Val Gly Ser Pro Leu Asn Asn Glu Lys Val Gln Lys Leu Leu 50 55 60 Lys Glu Gln Lys Val Gln Val Gln Ile Leu Gly Lys Glu Lys Trp65 70 75 42316PRTBacillus thuringiensis 42Met Tyr Met Ala Glu Ile Lys Arg Leu Asp Tyr Tyr Leu Gly Ala Leu1 5 10 15 Pro Phe Gly Asn Phe Tyr Val Asp Asp Cys Asp Thr Leu Lys Asn Phe 20 25 30 Ile Asp Ser Leu Leu Asp Gly Lys Pro Ser Thr Met Asn Asn Thr Pro 35 40 45 Leu Thr Gly Asn Val Asn Val Thr Asn Gln Ser Val Thr Ile Leu Asp 50 55 60 Asp Leu Asp Ser Ile Ala Thr Leu Thr Pro Glu Tyr Val Tyr Asp Asn65 70 75 80 Tyr Phe Ser Asn Asp Thr Ser Thr Glu Lys Thr Tyr Gln Thr Leu Ser 85 90 95 Phe Glu Lys Asp Val Gln Thr Thr Val Ser Thr Thr Val Thr His Gly 100 105 110 Phe Gln Ile Gly Gly Lys Leu Gly Ala Glu Val Lys Gly Ser Val Ser 115 120 125 Ile Pro Phe Val Ala Asp Gly Gly Val Thr Val Ser Ala Glu Ile Ser 130 135 140 Gly Gln Tyr Asn Phe Ser Ser Ala Asp Thr Glu Thr Thr Thr Thr Ser145 150 155 160 Gln Lys Leu Ile Ile Pro Ser Gln Ser Gly Asn Ile Arg Pro Gly Tyr 165 170 175 Thr Thr Arg Val Gln Ile Met Leu Ala Lys Ile Asn Ile Pro Gln Thr 180 185 190 Ala Val His Phe Ser Gly Ser Met Ser Gly Thr Val His Arg Asp Pro 195 200 205 Ile Pro Ser Ser Val Ile Gly Leu Val Asp Tyr Asp Leu Tyr Asp Glu 210 215 220 Val Arg Ser Leu Glu Asn Asn Cys Ser Asn Ser Thr Val Gly Arg Asp225 230 235 240 Thr Gly Leu Val Leu Asn Asn Ala Asn Gln Ser Val Asp Phe Ser Gly 245 250 255 Ser Gly Phe Phe Thr Gly Ser Ile Thr Ala Phe Asn Phe Tyr Val Lys 260 265 270 Ile Thr Glu Tyr Pro Ile Asn Asn Ser Ser Gln Glu Asn Ile Arg Trp 275 280 285 Tyr Ser Ile Glu Pro Lys Val Leu Asn Gln Ser Ile Ile Arg His Arg 290 295 300 Phe Pro Ser Asn Ser Ser Val Asn Thr Cys Asn Cys305 310 315 43525PRTBacillus thuringiensis 43Met Ala Gln Ser Glu Phe Asn Gln Asn Leu Arg Glu Gln Gly Gln Ser1 5 10 15 Arg Ala Arg Val Ile Ile Leu Arg Val Asn Asn Pro Gly Tyr Asn Thr 20 25 30 Asn Thr Leu Asp Ile Ala Asp Ile Glu Asp Ile Ile His Leu Pro Gln 35 40 45 Ala Ile Glu Leu Ala Asn Ala Phe Gln Ser Ala Leu Val Pro Thr Thr 50 55 60 Ser Asn Phe Gly Glu Asp Thr Leu Arg Phe Asp Val Glu Arg Gly Leu65 70 75 80 Gly Ile Ala Thr His Val Tyr Pro Arg Ala Ile Asn Val Asn Tyr Val 85 90 95 Thr Arg Thr Leu Ser Gln Thr Asn Asn Gln Val Gln Ser Met Ile Asn 100 105 110 Lys Val Ile Glu Glu Leu Lys Ser Leu Leu Gly Ile Asn Leu Ala Asn 115 120 125 Ser Val Leu Gln Gln Leu Thr Thr

Val Ile Thr Glu Thr Phe Thr Asn 130 135 140 Leu Tyr Val Gln Gln Gln Ser Ala Trp Leu Phe Trp Gly Arg Gln Thr145 150 155 160 Ser Ser Gln Thr Asn Tyr Thr Tyr Asn Ile Val Phe Ala Ile Gln Asn 165 170 175 Ala Gln Thr Gly Ser Phe Met Lys Ala Ile Pro Ile Gly Phe Glu Ile 180 185 190 Ser Ala Tyr Ile Ala Arg Glu Arg Leu Leu Phe Phe Asn Ile Gln Asp 195 200 205 Tyr Ala Ser Tyr Ser Val Lys Ile His Ala Ile Gln Val Met Gln Pro 210 215 220 Leu Ile His Glu Ser Phe Gln Pro Leu Arg Gly Ile Phe Asn Ile Ile225 230 235 240 Thr Ser Val Asn Asn Arg Ser Ala Ile Gln Ile Thr Glu Tyr Tyr Asp 245 250 255 Glu Asn Thr His Asp Tyr Pro Val Lys Leu Trp Asp Tyr Asn Asn Ile 260 265 270 Ile Asn Gln Lys Trp Ile Leu Val Phe Asn Gln Thr Thr Arg Ala Tyr 275 280 285 Ser Ile Gln Asn Leu Ile Ala Arg Tyr Leu Val Leu Thr Trp Asp Ser 290 295 300 Thr Pro Gly Ser Asn Lys Val Phe Ala Ser Thr Asn Arg Trp Asn Asp305 310 315 320 Ser Gln Phe Trp Ile Leu Glu Ser Thr Ala Asp Gly Ser Ile Phe Leu 325 330 335 Thr Asn Met Lys Asp Thr Gln Phe Val Leu Glu Ile Glu Asn Ser Ser 340 345 350 Thr Thr Asn Gly Thr Asn Val Ile Val Asn Arg Lys Asn Asn Asn Ala 355 360 365 Gln Gln Lys Phe Tyr Leu Asn Lys Val Asn Gln Glu Phe Gln Asp Gly 370 375 380 Val Tyr Lys Ile Lys Thr Ala Leu Asn Asn Ser Ser Val Leu Gln Met385 390 395 400 Ser Glu Asp Tyr Phe Gly Tyr Thr Ser Asp Tyr Phe Val Lys Leu Trp 405 410 415 Thr Asn Asn Asn Asn Asp Ile Asn Gln Lys Trp Ile Phe Glu Phe Asp 420 425 430 Ser Thr Lys Ser Ala Tyr Gln Ile Lys Ser Gln Arg Asp Pro Ser Leu 435 440 445 Val Leu Ala Trp Thr Trp Ser Val Pro Thr Val Lys Leu Pro Ile Pro 450 455 460 Asn Asn Asp Asp His Leu Trp Phe Leu Gln Asn Ala Gly Ser Gly Thr465 470 475 480 Tyr Tyr Phe Val Asn Met Thr Asp Thr Arg Tyr Val Leu Glu Val Ala 485 490 495 Ser Ser Ser Thr Thr Asn Gly Thr Ile Leu Thr Ile Asn Lys Arg Asn 500 505 510 Gly Asn Leu Asn Gln Lys Phe Leu Leu Asp Met Ile Asn 515 520 525 44340PRTBacillus cereus 44Met Ala Ile Met Asn Asp Ile Ala Gln Asp Ala Ala Arg Ala Trp Asp1 5 10 15 Ile Ile Ala Gly Pro Phe Ile Arg Pro Gly Thr Thr Pro Thr Asn Arg 20 25 30 Gln Leu Phe Asn Tyr Gln Ile Gly Asn Ile Glu Val Glu Pro Gly Asn 35 40 45 Leu Asn Phe Ser Val Val Pro Glu Leu Asp Phe Ser Val Ser Gln Asp 50 55 60 Leu Phe Asn Asn Thr Ser Val Gln Gln Ser Gln Thr Ala Ser Phe Asn65 70 75 80 Glu Ser Arg Thr Glu Thr Thr Ser Thr Ala Val Thr His Gly Val Lys 85 90 95 Ser Gly Val Thr Val Ser Ala Ser Ala Lys Phe Asn Ala Lys Ile Leu 100 105 110 Val Lys Ser Ile Glu Gln Thr Ile Thr Thr Thr Val Ser Thr Glu Tyr 115 120 125 Asn Phe Ser Ser Thr Thr Thr Arg Thr Asn Thr Val Thr Arg Gly Trp 130 135 140 Ser Ile Ala Gln Pro Val Leu Val Pro Pro His Ser Arg Val Thr Ala145 150 155 160 Thr Leu Gln Ile Tyr Lys Gly Asp Phe Thr Val Pro Val Leu Leu Ser 165 170 175 Leu Arg Val Tyr Gly Gln Thr Gly Thr Leu Ala Gly Asn Pro Ser Phe 180 185 190 Pro Ser Leu Tyr Ala Ala Thr Tyr Glu Asn Thr Leu Leu Gly Arg Ile 195 200 205 Arg Glu His Ile Ala Pro Pro Ala Leu Phe Arg Ala Ser Asn Ala Tyr 210 215 220 Ile Ser Asn Gly Val Gln Ala Ile Trp Arg Gly Thr Ala Thr Thr Arg225 230 235 240 Val Ser Gln Gly Leu Tyr Ser Val Val Arg Ile Asp Glu Arg Pro Leu 245 250 255 Ala Gly Tyr Ser Gly Glu Thr Arg Thr Tyr Tyr Leu Pro Val Thr Leu 260 265 270 Ser Asn Ser Ser Gln Ile Leu Thr Pro Gly Ser Leu Gly Ser Glu Ile 275 280 285 Pro Ile Ile Asn Pro Val Pro Asn Ala Ser Cys Lys Lys Glu Asn Ser 290 295 300 Pro Ile Ile Ile His His Asp Arg Glu Lys His Arg Glu Arg Asp Tyr305 310 315 320 Asp Lys Glu His Ile Cys His Asp Gln Ala Glu Lys Tyr Glu Arg Asp 325 330 335 Tyr Asp Lys Glu 340 451131PRTBacillus thuringiensis 45Met Asn Gln Lys Asn Tyr Glu Ile Ile Gly Ala Ser Thr Asn Gly Thr1 5 10 15 Ile Glu Leu Pro Glu Asp Tyr Asn Thr Ile Val Ser Pro Tyr Asp Ala 20 25 30 Pro Ala Ser Val Thr Thr Thr Ile Glu Ile Thr Gly Thr Ile Leu Ser 35 40 45 Asp Leu Gly Val Pro Gly Ala Ser Ser Val Ser Leu Leu Leu Asn Lys 50 55 60 Leu Ile Asn Leu Leu Trp Pro Asn Asp Thr Asn Thr Val Trp Gly Thr65 70 75 80 Phe Gly Lys Glu Thr Ala Asp Leu Leu Asn Glu Val Leu Ser Pro Asp 85 90 95 Asp Pro Val Val Lys Asp Ala Asn Thr Ile Leu Lys Gly Ile Asn Gly 100 105 110 Ser Leu Asn Leu Tyr Leu Asn Ala Leu Glu Ile Trp Lys Lys Asp Pro 115 120 125 Asn Asn Leu Thr Thr Ile Glu Asn Val Thr Asp Tyr Phe Arg Ser Leu 130 135 140 Asn Val Val Phe Thr His Asp Met Pro Ser Phe Ala Val Pro Gly Tyr145 150 155 160 Glu Thr Lys Leu Leu Thr Ile Tyr Ala Gln Ala Ala Asn Leu His Leu 165 170 175 Leu Leu Leu Arg Asp Ala Ser Arg Phe Gly Glu Gly Trp Gly Leu Thr 180 185 190 Gln Glu Ile Ile Asn Thr Asn Tyr Asn Asp Gln Leu Arg Leu Thr Ala 195 200 205 Glu Tyr Thr Asp His Cys Val Lys Trp Tyr Asn Ala Gly Leu Glu Lys 210 215 220 Leu Lys Gly Asn Leu Thr Gly Glu Asn Trp Tyr Thr Tyr Asn Arg Phe225 230 235 240 Arg Arg Glu Met Thr Leu Met Val Leu Asp Val Val Ala Leu Phe Pro 245 250 255 Asn Tyr Asp Thr Arg Met Tyr Pro Ile Gly Thr Ser Ser Glu Leu Thr 260 265 270 Arg Met Ile Tyr Thr Asp Pro Ile Ala Tyr Thr Gln Ser Asp Pro Trp 275 280 285 Tyr Lys Ile Thr Ser Leu Ser Phe Ser Asn Ile Glu Asn Ser Ala Ile 290 295 300 Pro Ser Pro Ser Phe Phe Arg Trp Leu Lys Ser Val Ser Ile Asn Ser305 310 315 320 Gln Trp Trp Gly Ser Gly Pro Ser Gln Thr Tyr Tyr Trp Val Gly His 325 330 335 Glu Leu Val Tyr Ser Asn Ser Asn Ser Asn Gln Ser Leu Lys Val Lys 340 345 350 Tyr Gly Asp Pro Asn Ser Phe Ile Glu Pro Pro Asp Ser Phe Ser Phe 355 360 365 Ser Ser Thr Asp Val Tyr Arg Thr Ile Ser Val Val Arg Asn Ser Val 370 375 380 Ser Asn Tyr Ile Val Ser Glu Val Arg Phe Asn Ser Ile Ser Ser Thr385 390 395 400 Asn Gln Ile Ser Glu Glu Ile Tyr Lys His Gln Ser Asn Trp Ser Arg 405 410 415 Gln Glu Thr Lys Asp Ser Ile Thr Glu Leu Ser Leu Ala Ala Asn Pro 420 425 430 Pro Thr Thr Phe Gly Asn Val Ala Glu Tyr Ser His Arg Leu Ala Tyr 435 440 445 Ile Ser Glu Ala Tyr Gln Ser His Asn Pro Ser Lys Tyr Pro Thr Tyr 450 455 460 Ile Pro Val Phe Gly Trp Thr His Thr Ser Val Arg Tyr Asp Asn Lys465 470 475 480 Ile Phe Pro Asp Lys Ile Thr Gln Ile Pro Ala Val Lys Ser Ser Ser 485 490 495 Ala Gln Gly Gly Ser Trp Lys Asn Ile Val Lys Gly Pro Gly Phe Thr 500 505 510 Gly Gly Asp Val Thr Thr Ala Val Ser Pro Ala Thr Val Thr Asp Ile 515 520 525 Ile Lys Ile Gln Val Thr Leu Asp Pro Asn Ser Leu Ser Gln Lys Tyr 530 535 540 Arg Ala Arg Leu Arg Tyr Ala Ser Asn Ala Phe Val Pro Ala Thr Leu545 550 555 560 Tyr Thr Asn Thr Ser Ser Asn Tyr Asn Phe Glu Leu Lys Lys Gly Thr 565 570 575 Thr Glu Gln Phe Thr Thr Tyr Asn Ser Tyr Gln Tyr Val Asp Ile Pro 580 585 590 Gly Ser Ile Gln Phe Asn Asn Thr Ser Asp Thr Val Ser Val Tyr Leu 595 600 605 His Met Asp Ser Thr Ser Asn Val Asn Val His Val Asp Arg Ile Glu 610 615 620 Phe Ile Pro Ile Asp Glu Asn Tyr Asp Glu Arg Phe Gln Leu Glu Lys625 630 635 640 Ala Gln Lys Ala Val Asn Ala Leu Phe Thr Ala Gly Arg Asn Ala Leu 645 650 655 Gln Thr Asp Val Thr Asp Tyr Lys Val Asp Gln Val Ser Ile Leu Val 660 665 670 Asp Cys Val Ser Gly Glu Leu Tyr Pro Asn Glu Lys Arg Glu Leu Leu 675 680 685 Ser Leu Val Lys Tyr Ala Lys Arg Leu Ser Tyr Ser Arg Asn Leu Leu 690 695 700 Leu Asp Pro Thr Phe Asp Ser Ile Asn Ser Pro Glu Glu Asn Gly Trp705 710 715 720 Tyr Gly Ser Asn Gly Ile Ala Ile Gly Ser Gly Asn Ile Val Phe Lys 725 730 735 Gly Asn Tyr Leu Ile Phe Ser Gly Thr Asn Asp Glu Gln Tyr Pro Thr 740 745 750 Tyr Leu Tyr Gln Lys Ile Asp Glu Thr Lys Leu Lys Glu Tyr Thr Arg 755 760 765 Tyr Lys Leu Arg Gly Phe Ile Glu Ser Ser Gln Asp Leu Glu Ala Tyr 770 775 780 Val Ile Arg Tyr Asp Ala Lys His Gln Thr Met Asp Val Ser Asn Asn785 790 795 800 Leu Phe Ser Asp Ile Thr Pro Val Asn Ala Cys Gly Glu Pro Asn Arg 805 810 815 Cys Ala Ala Leu Pro Tyr Leu Asp Glu Asn Pro Arg Leu Glu Cys Ser 820 825 830 Ser Ile Gln Asp Gly Ile Leu Ser Asp Ser His Ser Phe Ser Leu His 835 840 845 Ile Asp Thr Gly Ser Ile Asp Phe Asn Glu Asn Val Gly Ile Trp Val 850 855 860 Leu Phe Lys Ile Ser Thr Pro Glu Gly Tyr Ala Arg Phe Gly Asn Leu865 870 875 880 Glu Val Ile Glu Asp Gly Pro Val Ile Gly Glu Ala Leu Ala Arg Val 885 890 895 Lys Arg Gln Glu Thr Lys Trp Arg Asn Lys Leu Thr Gln Leu Arg Thr 900 905 910 Glu Thr Gln Ala Ile Tyr Thr Arg Ala Lys Gln Ala Ile Asp Asn Leu 915 920 925 Phe Thr Asn Ala Gln Asp Ser His Leu Lys Ile Gly Ala Thr Phe Ala 930 935 940 Ser Ile Val Ala Ala Arg Lys Ile Val Gln Ser Ile Arg Glu Ala Tyr945 950 955 960 Met Ser Trp Leu Ser Ile Val Pro Gly Val Asn Tyr Pro Ile Val Thr 965 970 975 Glu Leu Asn Glu Arg Ile Gln Gln Ala Phe Gln Leu Tyr Asp Val Arg 980 985 990 Asn Val Val Arg Asn Gly Arg Phe Gln Ser Gly Thr Ser Asp Trp Ile 995 1000 1005 Val Thr Ser Asp Val Arg Val Gln Glu Glu Asn Gly Asn Asn Val Leu 1010 1015 1020 Val Leu Ser Asn Trp Asp Ala Gln Val Leu Gln Cys Met Thr Leu Tyr1025 1030 1035 1040 Gln Asp Arg Gly Tyr Ile Leu Arg Val Thr Ala Arg Lys Glu Gly Leu 1045 1050 1055 Gly Glu Gly Tyr Val Thr Ile Thr Asp Glu Glu Gly Asn Thr Asp Gln 1060 1065 1070 Leu Arg Phe Gly Gly Cys Glu Glu Ile Asp Ala Ser Asn Ser Phe Val 1075 1080 1085 Ser Thr Gly Tyr Met Thr Lys Glu Leu Glu Phe Phe Pro Asp Thr Glu 1090 1095 1100 Lys Val Arg Ile Glu Ile Gly Glu Thr Glu Gly Thr Phe Gln Val Glu1105 1110 1115 1120 Ser Val Glu Leu Phe Leu Met Glu Asp Leu Cys 1125 1130 461138PRTBacillus thuringiensis 46Met Asn Leu Asn Asn Leu Asp Gly Tyr Glu Asp Ser Asn Arg Thr Leu1 5 10 15 Asn Asn Ser Leu Asn Tyr Pro Thr Gln Lys Ala Leu Ser Pro Ser Leu 20 25 30 Lys Asn Met Asn Tyr Gln Asp Phe Leu Ser Ile Thr Glu Arg Glu Gln 35 40 45 Pro Glu Ala Leu Ala Ser Gly Asn Thr Ala Ile Asn Thr Val Val Ser 50 55 60 Val Thr Gly Ala Thr Leu Ser Ala Leu Gly Val Pro Gly Ala Ser Phe65 70 75 80 Ile Thr Asn Phe Tyr Leu Lys Ile Ala Gly Leu Leu Trp Pro Glu Asn 85 90 95 Gly Lys Ile Trp Asp Glu Phe Met Thr Glu Val Glu Ala Leu Ile Asp 100 105 110 Gln Lys Ile Glu Glu Tyr Val Arg Asn Lys Ala Ile Ala Glu Leu Asp 115 120 125 Gly Leu Gly Ser Ala Leu Asp Lys Tyr Gln Lys Ala Leu Ala Asp Trp 130 135 140 Leu Gly Lys Gln Asp Asp Pro Glu Ala Ile Leu Ser Val Ala Thr Glu145 150 155 160 Phe Arg Ile Ile Asp Ser Leu Phe Glu Phe Ser Met Pro Ser Phe Lys 165 170 175 Val Thr Gly Tyr Glu Ile Pro Leu Leu Thr Val Tyr Ala Gln Ala Ala 180 185 190 Asn Leu His Leu Ala Leu Leu Arg Asp Ser Thr Leu Tyr Gly Asp Lys 195 200 205 Trp Gly Phe Thr Gln Asn Asn Ile Glu Glu Asn Tyr Asn Arg Gln Lys 210 215 220 Lys Arg Ile Ser Glu Tyr Ser Asp His Cys Thr Lys Trp Tyr Asn Ser225 230 235 240 Gly Leu Ser Arg Leu Asn Gly Ser Thr Tyr Glu Gln Trp Ile Asn Tyr 245 250 255 Asn Arg Phe Arg Arg Glu Met Ile Leu Met Ala Leu Asp Leu Val Ala 260 265 270 Val Phe Pro Phe His Asp Pro Arg Arg Tyr Ser Met Glu Thr Ser Thr 275 280 285 Gln Leu Thr Arg Glu Val Tyr Thr Asp Pro Val Ser Leu Ser Ile Ser 290 295 300 Asn Pro Asp Ile Gly Pro Ser Phe Ser Gln Met Glu Asn Thr Ala Ile305 310 315 320 Arg Thr Pro His Leu Val Asp Tyr Leu Asp Glu Leu Tyr Ile Tyr Thr 325 330 335 Ser Lys Tyr Lys Ala Phe Ser His Glu Ile Gln Pro Asp Leu Phe Tyr 340 345 350 Trp Ser Ala His Lys Val Ser Phe Lys Lys Ser Glu Gln Ser Asn Leu 355 360 365 Tyr Thr Thr Gly Ile Tyr Gly Lys Thr Ser Gly Tyr Ile Ser Ser Gly 370 375 380 Ala Tyr Ser Phe His Gly Asn Asp Ile Tyr Arg Thr Leu Ala Ala Pro385 390 395 400 Ser Val Val Val Tyr Pro Tyr Thr Gln Asn Tyr Gly Val Glu Gln Val 405 410 415 Glu Phe Tyr Gly Val Lys Gly His Val His Tyr Arg Gly Asp Asn Lys 420 425 430 Tyr Asp Leu Thr Tyr Asp Ser Ile Asp Gln Leu Pro Pro Asp Gly

Glu 435 440 445 Pro Ile His Glu Lys Tyr Thr His Arg Leu Cys His Ala Thr Ala Ile 450 455 460 Phe Lys Ser Thr Pro Asp Tyr Asp Asn Ala Thr Ile Pro Ile Phe Ser465 470 475 480 Trp Thr His Arg Ser Ala Glu Tyr Tyr Asn Arg Ile Tyr Pro Asn Lys 485 490 495 Ile Thr Lys Ile Pro Ala Val Lys Met Tyr Lys Leu Asp Asp Pro Ser 500 505 510 Thr Val Val Lys Gly Pro Gly Phe Thr Gly Gly Asp Leu Val Lys Arg 515 520 525 Gly Ser Thr Gly Tyr Ile Gly Asp Ile Lys Ala Thr Val Asn Ser Pro 530 535 540 Leu Ser Gln Lys Tyr Arg Val Arg Val Arg Tyr Ala Thr Asn Val Ser545 550 555 560 Gly Gln Phe Asn Val Tyr Ile Asn Asp Lys Ile Thr Leu Gln Thr Lys 565 570 575 Phe Gln Asn Thr Val Glu Thr Ile Gly Glu Gly Lys Asp Leu Thr Tyr 580 585 590 Gly Ser Phe Gly Tyr Ile Glu Tyr Ser Thr Thr Ile Gln Phe Pro Asp 595 600 605 Glu His Pro Lys Ile Thr Leu His Leu Ser Asp Leu Ser Asn Asn Ser 610 615 620 Ser Phe Tyr Val Asp Ser Ile Glu Phe Ile Pro Val Asp Val Asn Tyr625 630 635 640 Ala Glu Lys Glu Lys Leu Glu Lys Ala Gln Lys Ala Val Asn Thr Leu 645 650 655 Phe Thr Glu Gly Arg Asn Ala Leu Gln Lys Asp Val Thr Asp Tyr Lys 660 665 670 Val Asp Gln Val Ser Ile Leu Val Asp Cys Ile Ser Gly Asp Leu Tyr 675 680 685 Pro Asn Glu Lys Arg Glu Leu Gln Asn Leu Val Lys Tyr Ala Lys Arg 690 695 700 Leu Ser Tyr Ser Arg Asn Leu Leu Leu Asp Pro Thr Phe Asp Ser Ile705 710 715 720 Asn Ser Ser Glu Glu Asn Gly Trp Tyr Gly Ser Asn Gly Ile Val Ile 725 730 735 Gly Asn Gly Asp Phe Val Phe Lys Gly Asn Tyr Leu Ile Phe Ser Gly 740 745 750 Thr Asn Asp Thr Gln Tyr Pro Thr Tyr Leu Tyr Gln Lys Ile Asp Glu 755 760 765 Ser Lys Leu Lys Glu Tyr Thr Arg Tyr Lys Leu Lys Gly Phe Ile Glu 770 775 780 Ser Ser Gln Asp Leu Glu Ala Tyr Val Ile Arg Tyr Asp Ala Lys His785 790 795 800 Arg Thr Leu Asp Val Ser Asp Asn Leu Leu Pro Asp Ile Leu Pro Glu 805 810 815 Asn Thr Cys Gly Glu Pro Asn Arg Cys Ala Ala Gln Gln Tyr Leu Asp 820 825 830 Glu Asn Pro Ser Pro Glu Cys Ser Ser Met Gln Asp Gly Ile Leu Ser 835 840 845 Asp Ser His Ser Phe Ser Leu Asn Ile Asp Thr Gly Ser Ile Asn His 850 855 860 Asn Glu Asn Leu Gly Ile Trp Val Leu Phe Lys Ile Ser Thr Leu Glu865 870 875 880 Gly Tyr Ala Lys Phe Gly Asn Leu Glu Val Ile Glu Asp Gly Pro Val 885 890 895 Ile Gly Glu Ala Leu Ala Arg Val Lys Arg Gln Glu Thr Lys Trp Arg 900 905 910 Asn Lys Leu Ala Gln Leu Thr Thr Glu Thr Gln Ala Ile Tyr Thr Arg 915 920 925 Ala Lys Gln Ala Leu Asp Asn Leu Phe Ala Asn Ala Gln Asp Ser His 930 935 940 Leu Lys Arg Asp Val Thr Phe Ala Glu Ile Ala Ala Ala Arg Lys Ile945 950 955 960 Val Gln Ser Ile Arg Glu Ala Tyr Met Ser Trp Leu Ser Val Val Pro 965 970 975 Gly Val Asn His Pro Ile Phe Thr Glu Leu Ser Gly Arg Val Gln Arg 980 985 990 Ala Phe Gln Leu Tyr Asp Val Arg Asn Val Val Arg Asn Gly Arg Phe 995 1000 1005 Leu Asn Gly Leu Ser Asp Trp Ile Val Thr Ser Asp Val Lys Val Gln 1010 1015 1020 Glu Glu Asn Gly Asn Asn Val Leu Val Leu Asn Asn Trp Asp Ala Gln1025 1030 1035 1040 Val Leu Gln Asn Val Lys Leu Tyr Gln Asp Arg Gly Tyr Ile Leu His 1045 1050 1055 Val Thr Ala Arg Lys Ile Gly Ile Gly Glu Gly Tyr Ile Thr Ile Thr 1060 1065 1070 Asp Glu Glu Gly His Thr Asp Gln Leu Arg Phe Thr Ala Cys Glu Glu 1075 1080 1085 Ile Asp Ala Ser Asn Ala Phe Ile Ser Gly Tyr Ile Thr Lys Glu Leu 1090 1095 1100 Glu Phe Phe Pro Asp Thr Glu Lys Val His Ile Glu Ile Gly Glu Thr1105 1110 1115 1120 Glu Gly Ile Phe Leu Val Glu Ser Ile Glu Leu Phe Leu Met Glu Glu 1125 1130 1135 Leu Cys 47326PRTBacillus thuringiensis 47Met Val Arg Glu Tyr Pro Asp Leu Asp Ser Met Ile Arg Glu Ala Ala1 5 10 15 Gln Lys Trp Ser Glu Asp Asn Gly Leu Gln Phe Gln Lys Val Ser Phe 20 25 30 Lys Asp Pro Phe Thr Asn Arg Asp Thr Ile Arg Met Ser Val Lys Phe 35 40 45 Lys Asp Ile Gly Cys Pro Glu Glu Cys Leu Glu Thr Glu Thr Val Lys 50 55 60 Leu Ser Gln Ala Phe Thr Asn Asn Thr Gly Gln Pro Lys Lys Glu Thr65 70 75 80 Val Asn Thr Val Thr Tyr Val Glu Asn Gln Leu Thr Trp Glu Asn Asp 85 90 95 Phe His Phe Lys Leu Pro Gly Gln Asn Phe Leu Ile Leu Pro Arg Ile 100 105 110 Pro Gln Ser Val Arg Met Asp Ile Asn Pro Gly Phe Leu Val Asn Phe 115 120 125 Phe Gly Asp Asn Glu Leu Phe Ser Thr Asn Met Arg Asp Arg Arg Pro 130 135 140 Ile Gln Ala Asp Val Phe Val Glu Pro Gly Ser Ser Ala Ala Ile Gln145 150 155 160 Leu Lys Val Glu Lys Leu His Val Thr Gln Pro Tyr Glu Ile Glu Leu 165 170 175 Ser Ile Leu Gly Ser Ile Ile Val Thr Ala Gln Gly Ala Glu Arg Tyr 180 185 190 Val Asp Val Thr Asp Leu Leu Pro Phe Leu Cys Leu Ser Lys Asn Leu 195 200 205 Ser Ser Arg Gly Arg Ala Leu Ile Phe Leu Glu Gln Gly Thr Phe Lys 210 215 220 Gly Ile Leu Asn Arg Lys Ile Arg Gly Tyr Ala Leu Gln Thr Arg His225 230 235 240 Cys Asp Gly Lys Thr Ile Glu Tyr Glu Ile Pro Leu Asn Asn Arg Pro 245 250 255 Pro Val Ser Ala Arg Pro Leu Asn Pro Ala Thr Thr Ala Gln Gln Ser 260 265 270 Arg Lys Thr Asn Asp Ser Ser Cys Gly Cys Ser Ser Asp Arg Pro Pro 275 280 285 Val Gly Ile Tyr Leu Leu Ser Thr Ile Glu Ser Asn Asn Leu Phe Ser 290 295 300 Ala Thr Glu Ala Asp Glu Gly Cys Arg Phe Ile Met Trp Met Cys Cys305 310 315 320 Leu Phe Val Cys Ile Lys 325 48335PRTBacillus thuringiensis 48Met Lys Lys Ser Cys Asp Pro Asn Pro Val Asn Gln Ser Thr Thr Thr1 5 10 15 Thr Phe Asp Leu Asp Asp Phe Leu Leu Asn Asn Met Phe Asn Val Thr 20 25 30 Leu Gln Pro Ala Asn Ile Trp Tyr Tyr Gln Asp Glu Trp Pro Tyr Glu 35 40 45 Ser Pro Tyr Val Pro Thr Pro Thr Ser Asp Asp Leu Ser Lys Gly Cys 50 55 60 Trp Phe Asp Ala Tyr Val Pro Thr Cys Arg Tyr Asp His Ala Pro Gly65 70 75 80 Tyr Thr Ala Asn Thr Ser Gly Leu Met Ala Glu Gly Thr Asp Leu Thr 85 90 95 Glu Glu Ile Asp Ser Val Ala Tyr Ala Thr Pro Tyr Ile Ala Asp Ser 100 105 110 Tyr Thr Phe Thr Asn Asp Gly Pro Ile Thr Gln Glu Tyr Gln Thr Leu 115 120 125 Ala Tyr Glu Gln Ala Val Glu Thr Ser Thr Ser Asn Thr Thr Thr His 130 135 140 Gly Cys Arg Val Gly Ser Thr Phe Gly Tyr Ser Arg Asn Ser Thr Phe145 150 155 160 Thr Ala Lys Ile Arg Asp Thr Glu Lys Gly Phe His Leu Asp Val Gly 165 170 175 Ala Glu Tyr Asp Phe Thr Asn Thr Asn Thr Phe Thr Thr Ser Thr Thr 180 185 190 Thr Asn Val Leu Val Pro Ser Gln Val Ile Thr Val Pro Ser Tyr Cys 195 200 205 Thr Ala Tyr Val Thr Met Val Leu Asn Lys Ala Thr Tyr Ala Lys Ala 210 215 220 Asp Val Pro Leu Ile Thr Thr Leu Ser Gly Arg Phe Phe Ile Asp Glu225 230 235 240 Thr Asp Asn Ser Asp Glu Tyr Phe Asp Ile Tyr Pro Tyr Val Glu Leu 245 250 255 Val Thr Thr Cys Cys Thr Gly Asn Cys Ser Gln Cys Val Thr Asp Gln 260 265 270 Leu Gln Leu Asp Ala Val Asn Arg Thr Val Ile Phe Asp Gly Leu Gly 275 280 285 Ser Phe Glu Ala Asn Ile Ala Ser Asn Glu Leu Ile Val Arg Thr Lys 290 295 300 Leu Val Asp Asn Val Thr Gly Ala Thr Ile Ser Glu Gln Ala Gly Arg305 310 315 320 Val Pro Val Val Tyr Gly Pro Ser Thr Thr Lys Val Thr Thr Ser 325 330 335 49875PRTClostridium perfringens 49Met Asn Ile Gln Ile Lys Asn Val Phe Ser Phe Leu Thr Leu Thr Ala1 5 10 15 Met Ile Ser Gln Thr Leu Ser Tyr Asn Val Tyr Ala Gln Thr Thr Thr 20 25 30 Gln Asn Asp Thr Asn Gln Lys Glu Glu Ile Thr Asn Glu Asn Thr Leu 35 40 45 Ser Ser Asn Gly Leu Met Gly Tyr Tyr Phe Ala Asp Glu His Phe Lys 50 55 60 Asp Leu Glu Leu Met Ala Pro Ile Lys Asn Gly Asp Leu Lys Phe Glu65 70 75 80 Glu Lys Lys Val Asp Lys Leu Leu Thr Glu Asp Asn Ser Ser Ile Lys 85 90 95 Ser Ile Arg Trp Thr Gly Arg Ile Ile Pro Ser Glu Asp Gly Glu Tyr 100 105 110 Ile Leu Ser Thr Asp Arg Asn Asp Val Leu Met Gln Ile Asn Ala Lys 115 120 125 Gly Asp Ile Ala Lys Thr Leu Lys Val Asn Met Lys Lys Gly Gln Ala 130 135 140 Tyr Asn Ile Arg Ile Glu Ile Gln Asp Lys Asn Leu Gly Ser Ile Asp145 150 155 160 Asn Leu Ser Val Pro Lys Leu Tyr Trp Glu Leu Asn Gly Asn Lys Thr 165 170 175 Val Ile Pro Glu Glu Asn Leu Phe Phe Arg Asp Tyr Ser Lys Ile Asp 180 185 190 Glu Asn Asp Pro Phe Ile Pro Asn Asn Asn Phe Phe Asp Val Arg Phe 195 200 205 Phe Ser Ala Ala Trp Glu Asp Glu Asp Leu Asp Thr Asp Asn Asp Asn 210 215 220 Ile Pro Asp Ala Tyr Glu Lys Asn Gly Tyr Thr Ile Lys Asp Ser Ile225 230 235 240 Ala Val Lys Trp Asn Asp Ser Phe Ala Glu Gln Gly Tyr Lys Lys Tyr 245 250 255 Val Ser Ser Tyr Leu Glu Ser Asn Thr Ala Gly Asp Pro Tyr Thr Asp 260 265 270 Tyr Gln Lys Ala Ser Gly Ser Ile Asp Lys Ala Ile Lys Leu Glu Ala 275 280 285 Arg Asp Pro Leu Val Ala Ala Tyr Pro Val Val Gly Val Gly Met Glu 290 295 300 Asn Leu Ile Ile Ser Thr Asn Glu His Ala Ser Ser Asp Gln Gly Lys305 310 315 320 Thr Val Ser Arg Ala Thr Thr Asn Ser Lys Thr Asp Ala Asn Thr Val 325 330 335 Gly Val Ser Ile Ser Ala Gly Tyr Gln Asn Gly Phe Thr Gly Asn Ile 340 345 350 Thr Thr Ser Tyr Ser His Thr Thr Asp Asn Ser Thr Ala Val Gln Asp 355 360 365 Ser Asn Gly Glu Ser Trp Asn Thr Gly Leu Ser Ile Asn Lys Gly Glu 370 375 380 Ser Ala Tyr Ile Asn Ala Asn Val Arg Tyr Tyr Asn Thr Gly Thr Ala385 390 395 400 Pro Met Tyr Lys Val Thr Pro Thr Thr Asn Leu Val Leu Asp Gly Glu 405 410 415 Thr Leu Ala Thr Ile Lys Ala Gln Asp Asn Gln Ile Gly Asn Asn Leu 420 425 430 Ser Pro Asn Glu Thr Tyr Pro Lys Lys Gly Leu Ser Pro Leu Ala Leu 435 440 445 Asn Thr Met Asp Gln Phe Asn Ala Arg Leu Ile Pro Ile Asn Tyr Asp 450 455 460 Gln Leu Lys Lys Leu Asp Ser Gly Lys Gln Ile Lys Leu Glu Thr Thr465 470 475 480 Gln Val Ser Gly Asn Tyr Gly Thr Lys Asn Ser Gln Gly Gln Ile Ile 485 490 495 Thr Glu Gly Asn Ser Trp Ser Asn Tyr Ile Ser Gln Ile Asp Ser Val 500 505 510 Ser Ala Ser Ile Ile Leu Asp Thr Gly Ser Gln Thr Phe Glu Arg Arg 515 520 525 Val Ala Ala Lys Glu Gln Gly Asn Pro Glu Asp Lys Thr Pro Glu Ile 530 535 540 Thr Ile Gly Glu Ala Ile Lys Lys Ala Phe Ser Ala Thr Lys Asn Gly545 550 555 560 Glu Leu Leu Tyr Phe Asn Gly Ile Pro Ile Asp Glu Ser Cys Val Glu 565 570 575 Leu Ile Phe Asp Asp Asn Thr Ser Glu Ile Ile Lys Glu Gln Leu Lys 580 585 590 Tyr Leu Asp Asp Lys Lys Ile Tyr Asn Val Lys Leu Glu Arg Gly Met 595 600 605 Asn Ile Leu Ile Lys Val Pro Ser Tyr Phe Thr Asn Phe Asp Glu Tyr 610 615 620 Asn Asn Phe Pro Ala Ser Trp Ser Asn Ile Asp Thr Lys Asn Gln Asp625 630 635 640 Gly Leu Gln Ser Val Ala Asn Lys Leu Ser Gly Glu Thr Lys Ile Ile 645 650 655 Ile Pro Met Ser Lys Leu Lys Pro Tyr Lys Arg Tyr Val Phe Ser Gly 660 665 670 Tyr Ser Lys Asp Pro Ser Thr Ser Asn Ser Ile Thr Val Asn Ile Lys 675 680 685 Ser Lys Glu Gln Lys Thr Asp Tyr Leu Val Pro Glu Lys Asp Tyr Thr 690 695 700 Lys Phe Ser Tyr Glu Phe Glu Thr Thr Gly Lys Asp Ser Ser Asp Ile705 710 715 720 Glu Ile Thr Leu Thr Ser Ser Gly Val Ile Phe Leu Asp Asn Leu Ser 725 730 735 Ile Thr Glu Leu Asn Ser Thr Pro Glu Ile Leu Lys Glu Pro Glu Ile 740 745 750 Lys Val Pro Ser Asp Gln Glu Ile Leu Asp Ala His Asn Lys Tyr Tyr 755 760 765 Ala Asp Ile Lys Leu Asp Thr Asn Thr Gly Asn Thr Tyr Ile Asp Gly 770 775 780 Ile Tyr Phe Glu Pro Thr Gln Thr Asn Lys Glu Ala Leu Asp Tyr Ile785 790 795 800 Gln Lys Tyr Arg Val Glu Ala Thr Leu Gln Tyr Ser Gly Phe Lys Asp 805 810 815 Ile Gly Thr Lys Asp Lys Glu Ile Arg Asn Tyr Leu Gly Asp Gln Asn 820 825 830 Gln Pro Lys Thr Asn Tyr Ile Asn Phe Arg Ser Tyr Phe Thr Ser Gly 835 840 845 Glu Asn Val Met Thr Tyr Lys Lys Leu Arg Ile Tyr Ala Val Thr Pro 850 855 860 Asp Asn Arg Glu Leu Leu Val Leu Ser Val Asn865 870 875 50871PRTBrevibacillus laterosporus 50Met Lys Tyr Met Lys Lys Gly Leu Ser Ser Val Val Ile Gly Thr Leu1 5 10 15 Phe Ala Ser Met Phe Leu Asn Gly Asn Val Asn Ala Val Tyr Ala Asn 20 25 30 Ser Lys Thr Asn Gln Ile Ala Thr Thr Thr Gln Ala Ser Lys Asp Asn 35 40 45 Gln Ile Asp Arg Glu Gly Leu Leu Gly Tyr Tyr Phe Lys Gly Lys Asp 50 55 60

Phe Asn Asp Leu Thr Leu Phe Ala Pro Thr Arg Asp Asn Thr Leu Ile65 70 75 80 Tyr Asp Gln Gln Thr Ala Asn Thr Leu Val Asp Gln Lys His Gln Glu 85 90 95 Tyr His Ser Ile Arg Trp Ile Gly Leu Ile Gln Ser Ser Ala Thr Gly 100 105 110 Asp Phe Thr Phe Lys Leu Ser Asp Asp Glu Asn Ala Ile Ile Glu Leu 115 120 125 Asp Gly Lys Val Ile Ser Glu Lys Gly Asn Asn Lys Gln Ser Val His 130 135 140 Leu Glu Lys Gly Gln Leu Val Gln Ile Lys Ile Glu Tyr Gln Ser Asp145 150 155 160 Asp Ala Leu His Ile Asp Asn Lys Ile Phe Lys Glu Leu Lys Leu Phe 165 170 175 Lys Ile Asp Ser Gln Asn His Ser Gln Gln Val Gln Gln Asp Glu Leu 180 185 190 Arg Asn Pro Glu Phe Asn Lys Lys Glu Thr Gln Val Phe Leu Lys Lys 195 200 205 Ala Ser Lys Thr Asn Leu Phe Thr Gln Lys Thr Lys Arg Asp Ile Asp 210 215 220 Glu Asp Thr Asp Thr Asp Gly Asp Ser Ile Pro Asp Val Trp Glu Glu225 230 235 240 Asn Gly Tyr Thr Ile Gln Asn Lys Val Ala Val Lys Trp Asp Asp Ser 245 250 255 Leu Ala Ser Lys Gly Tyr Gln Lys Phe Thr Ser Asn Pro Leu Glu Ala 260 265 270 His Thr Val Gly Asp Pro Tyr Ser Asp Tyr Glu Lys Ala Ala Arg Asp 275 280 285 Met Pro Leu Ser Asn Ala Lys Glu Thr Phe Asn Pro Leu Val Ala Ala 290 295 300 Phe Pro Ser Val Asn Val Ser Leu Glu Lys Val Ile Leu Ser Lys Asn305 310 315 320 Glu Asp Leu Ser His Ser Val Glu Ser Ser Gln Ser Thr Asn Trp Ser 325 330 335 Tyr Thr Asn Thr Glu Gly Val Asn Val Asn Ala Gly Trp Ser Gly Leu 340 345 350 Gly Pro Ser Phe Gly Val Ser Val Asn Tyr Gln His Ser Glu Thr Val 355 360 365 Ala Asn Glu Trp Gly Ser Ala Thr Asn Asp Gly Thr His Ile Asn Gly 370 375 380 Ala Glu Ser Ala Tyr Leu Asn Ala Asn Val Arg Tyr Asn Asn Val Gly385 390 395 400 Thr Gly Ala Ile Tyr Glu Thr Lys Pro Thr Thr Ser Phe Ile Leu Asp 405 410 415 Gly Thr Thr Ile Gly Thr Ile Lys Ala Lys Glu Asn Thr Thr Ala Leu 420 425 430 Thr Ile Leu Pro Asp Gln Ser Tyr Pro Glu Lys Gly Lys Asn Gly Ile 435 440 445 Ala Ile Asn Thr Met Asp Asp Phe Asn Ser Arg Pro Ile Pro Leu Asn 450 455 460 Lys Glu Gln Leu Asn Thr Tyr Leu Ser Asn Lys Lys Pro Ile Leu Leu465 470 475 480 Glu Thr Asp Gln Val Glu Gly Lys Tyr Ala Ile Lys Asp Thr Asn Gly 485 490 495 Asn Ile Thr Ile Ala Gly Asp Trp Asn Gly Ile Thr Asp Glu Ile Ser 500 505 510 Ala Lys Thr Ala Ser Ile Ile Val Asp Asn Gly Asn Gln Met Ser Glu 515 520 525 Lys Arg Val Ala Ala Lys Asp Tyr Thr Asn Pro Glu Asp Lys Thr Pro 530 535 540 Asn Leu Ser Val Lys Glu Ala Leu Lys Leu Ala Tyr Pro Asp Glu Ile545 550 555 560 Glu Glu Lys Asp Gly Leu Leu Phe Tyr Asn Asp Gln Pro Ile Phe Glu 565 570 575 Ala Ser Val Gln Ser Tyr Val Asp Glu Tyr Thr Ala Lys Gln Ile Arg 580 585 590 Lys Gln Leu Asn Asp Ser Thr Gly Ser Phe Lys Asp Val Lys Asn Leu 595 600 605 Tyr Asp Val Lys Leu Glu Pro Lys Met Asn Phe Thr Ile Lys Thr Ser 610 615 620 Thr Leu Tyr Asp Gly Gly Glu Ser Asp Asn Thr Lys Ile Gly Asn Trp625 630 635 640 Tyr Tyr Thr Tyr Val Val Asn Gly Gly Asn Thr Gly Lys Lys Gln Tyr 645 650 655 Arg Ser Ala Asn Lys Gly Ala Phe Thr Glu Leu Ser Thr Glu Ser Lys 660 665 670 Asn Lys Leu Lys Lys Asn Ile Asp Tyr Tyr Val Ser Leu Tyr Met Lys 675 680 685 Ala Asp Ser Lys Val Ser Val Asp Ile Glu Ile Asp Gly Lys Gln Glu 690 695 700 Ser Ile Val Thr Asp Asn Ile Thr Leu Asp His Val Gly Tyr Gln Arg705 710 715 720 Ile Asn Ile Leu Val Pro Asn Leu Glu Gly Asn Glu Ile Asn Thr Ile 725 730 735 Ser Ile Lys Gly Asp Gly Gln Thr Asn Val Tyr Trp Asp Asp Val Ser 740 745 750 Phe Val Glu Val Gly Ala Glu Glu Ile Glu Tyr Lys Asp Pro Val Pro 755 760 765 Gln Phe Asp Ile Ile Glu Gly Asp Phe Asp Phe Phe Gly Asp Pro Leu 770 775 780 Ala Val Lys Tyr His Asp Ala Thr Tyr Phe Ile Asp Ser Pro Leu Ile785 790 795 800 Thr Gln Thr Pro Gly Thr Phe Ser Phe Thr Tyr Lys Val Ile Gly Glu 805 810 815 Gln Thr Lys Thr Val Leu Asp Ser Gly Ser Gly Lys Asn Ala Asn Arg 820 825 830 Ile Asn Leu Asp Phe Lys Asn Val Lys Ser Asp Arg Ser Phe Leu Tyr 835 840 845 Thr Leu Ser Cys Lys Asp Asp Leu Trp Gly Ser Thr Arg Thr Ala Val 850 855 860 Val Arg Ile Phe Ala Val Asp865 870 51785PRTBrevibacillus laterosporus 51Met Thr Tyr Met Lys Lys Lys Leu Val Ser Val Val Thr Cys Ala Leu1 5 10 15 Leu Ala Pro Met Phe Leu Asn Gly Asn Val Asn Pro Val Tyr Ala Asp 20 25 30 Asn Gln Thr Asn Gln Leu Ser Thr Ala Gln Glu Asn Gln Glu Lys Glu 35 40 45 Val Asp Arg Lys Gly Leu Leu Gly Tyr Tyr Phe Lys Gly Lys Glu Phe 50 55 60 Asn His Leu Thr Leu Phe Ala Pro Thr Arg Asp Asn Thr Leu Ile Tyr65 70 75 80 Asp Gln Gln Thr Val Asp Phe Leu Leu Asp Lys Lys Gln Gln Glu Tyr 85 90 95 Gln Ser Ile Arg Trp Ile Gly Leu Ile Gln Ser Lys Glu Thr Gly Asp 100 105 110 Phe Thr Phe Asn Leu Ser Asp Asp Lys Asn Ala Ile Ile Glu Ile Asp 115 120 125 Gly Lys Thr Ile Ser His Lys Gly Gln Asn Lys Gln Val Val His Leu 130 135 140 Glu Lys Gly Lys Leu Val Pro Ile Lys Ile Glu Tyr Gln Ser Asp Gln145 150 155 160 Ile Val Asn Arg Asp Ser Lys Ile Phe Lys Glu Phe Lys Leu Phe Lys 165 170 175 Val Asp Ser Gln Gln Gln Ser His Gln Val Gln Leu Asp Glu Leu Arg 180 185 190 Asn Pro Glu Phe Asn Lys Lys Glu Thr Gln Gln Phe Leu Glu Lys Ala 195 200 205 Ser Lys Thr Asn Ile Phe Thr Gln Asn Met Lys Arg Asp Glu Asp Ala 210 215 220 Thr Asp Thr Asp Gly Asp Ser Ile Pro Asp Leu Trp Glu Glu Asn Gly225 230 235 240 Tyr Thr Ile Gln Asn Lys Val Ala Val Lys Trp Asp Asp Ser Phe Ala 245 250 255 Ala Lys Gly Tyr Thr Lys Phe Val Ser Asn Pro Phe Asp Ser His Thr 260 265 270 Val Gly Asp Pro Tyr Thr Asp Tyr Glu Lys Ala Ala Arg Asp Leu Asp 275 280 285 Leu Ala Asn Ala Lys Glu Thr Phe Asn Pro Leu Val Ala Ala Phe Pro 290 295 300 Ser Val Asn Val Asn Leu Glu Lys Val Ile Leu Ser Pro Asn Glu Asp305 310 315 320 Leu Ser Asn Ser Val Glu Ser His Ser Ser Thr Asn Trp Ser Tyr Thr 325 330 335 Asn Thr Glu Gly Ala Ser Ile Glu Ala Gly Ser Gly Pro Leu Gly Ile 340 345 350 Ser Tyr Gly Val Ser Ala Asn Tyr Gln His Ser Glu Thr Val Ala Lys 355 360 365 Glu Trp Gly Thr Ser Thr Gly Asn Thr Ser Gln Phe Asn Thr Ala Ser 370 375 380 Ala Gly Tyr Leu Asn Ala Asn Val Arg Tyr Asn Asn Val Gly Thr Gly385 390 395 400 Ala Ile Tyr Glu Val Lys Pro Thr Thr Gly Phe Val Leu Asp Asn Asp 405 410 415 Thr Val Ala Thr Ile Thr Ala Lys Ser Asn Ser Thr Ala Leu Ser Ile 420 425 430 Ser Pro Gly Glu Ser Tyr Pro Lys Lys Gly Gln Asn Gly Ile Ala Ile 435 440 445 Asn Thr Met Asp Asp Phe Asn Ser His Pro Ile Thr Leu Asn Lys Gln 450 455 460 Gln Leu Asp Gln Ile Phe Asn Asn Lys Pro Leu Met Leu Glu Thr Asn465 470 475 480 Gln Ala Asp Gly Val Tyr Lys Ile Lys Asp Thr Ser Gly Asn Ile Val 485 490 495 Thr Gly Gly Glu Trp Asn Gly Val Ile Gln Gln Ile Gln Ala Lys Thr 500 505 510 Ala Ser Ile Ile Val Asp Thr Gly Glu Gly Val Ser Glu Lys Arg Val 515 520 525 Ala Ala Lys Asp Tyr Asp Asn Pro Glu Asp Lys Thr Pro Ser Leu Ser 530 535 540 Leu Lys Glu Ala Leu Lys Leu Gly Tyr Pro Glu Glu Ile Lys Glu Lys545 550 555 560 Asp Gly Leu Leu Tyr Tyr Asn Asp Lys Pro Ile Tyr Glu Ser Ser Val 565 570 575 Met Thr Tyr Leu Asp Glu Asn Thr Ala Lys Glu Val Lys Glu Gln Leu 580 585 590 Asn Asp Ile Thr Gly Lys Phe Lys Asp Val Lys Gln Leu Phe Asp Val 595 600 605 Lys Leu Thr Pro Lys Met Asn Phe Thr Ile Lys Leu Ala Thr Leu Tyr 610 615 620 Asp Gly Ala Glu Asp Gly Ser Ser Pro Thr Asp Val Gly Ile Ser Ser625 630 635 640 Pro Leu Gly Glu Trp Ala Phe Lys Pro Asp Ile Asn Asn Val Glu Gly 645 650 655 Gly Asn Thr Gly Lys Arg Gln Tyr Gln Leu Ser Lys Asn Lys Asp Gly 660 665 670 Tyr Tyr Tyr Gly Met Leu Ala Leu Ser Pro Glu Val Ser Asn Lys Leu 675 680 685 Lys Lys Asn Tyr Gln Tyr Tyr Ile Ser Met Ser Ile Lys Ala Asp Ala 690 695 700 Gly Val Glu Pro Thr Val Thr Val Met Asp Asn Leu Leu Asn Gly Ile705 710 715 720 Val Asp Lys Lys Leu Lys Leu Ser Ser Asn Gly Tyr Gln Arg Phe Asp 725 730 735 Ile Leu Val Asp Asn Ser Glu Ser His Pro Ile Asn Val Met Val Ile 740 745 750 Asp Leu Gly Val Ser Ser Gln Asp Tyr Asn Asn Tyr Ser Lys Asn Ile 755 760 765 Tyr Ile Asp Asp Ile Thr Ile Thr Glu Val Ser Ala Met Lys Val Lys 770 775 780 Asn785 52462PRTBacillus cereus 52Met Lys Arg Met Glu Gly Lys Leu Phe Met Val Ser Lys Lys Leu Gln1 5 10 15 Val Val Thr Lys Thr Val Leu Leu Ser Thr Val Phe Ser Ile Ser Leu 20 25 30 Leu Asn Asn Glu Val Ile Lys Ala Glu Gln Leu Asn Ile Asn Ser Gln 35 40 45 Ser Lys Tyr Thr Asn Leu Gln Asn Leu Lys Ile Thr Asp Lys Val Glu 50 55 60 Asp Phe Lys Glu Asp Lys Glu Lys Ala Lys Glu Trp Gly Lys Glu Lys65 70 75 80 Glu Lys Glu Trp Lys Leu Thr Ala Thr Glu Lys Gly Lys Met Asn Asn 85 90 95 Phe Leu Asp Asn Lys Asn Asp Ile Lys Thr Asn Tyr Lys Glu Ile Thr 100 105 110 Phe Ser Met Ala Gly Ser Phe Glu Asp Glu Ile Lys Asp Leu Lys Glu 115 120 125 Ile Asp Lys Met Phe Asp Lys Thr Asn Leu Ser Asn Ser Ile Ile Thr 130 135 140 Tyr Lys Asn Val Glu Pro Thr Thr Ile Gly Phe Asn Lys Ser Leu Thr145 150 155 160 Glu Gly Asn Thr Ile Asn Ser Asp Ala Met Ala Gln Phe Lys Glu Gln 165 170 175 Phe Leu Asp Arg Asp Ile Lys Phe Asp Ser Tyr Leu Asp Thr His Leu 180 185 190 Thr Ala Gln Gln Val Ser Ser Lys Glu Arg Val Ile Leu Lys Val Thr 195 200 205 Val Pro Ser Gly Lys Gly Ser Thr Thr Pro Thr Lys Ala Gly Val Ile 210 215 220 Leu Asn Asn Ser Glu Tyr Lys Met Leu Ile Asp Asn Gly Tyr Met Val225 230 235 240 His Val Asp Lys Val Ser Lys Val Val Lys Lys Gly Val Glu Cys Leu 245 250 255 Gln Ile Glu Gly Thr Leu Lys Lys Ser Leu Asp Phe Lys Asn Asp Ile 260 265 270 Asn Ala Glu Ala His Ser Trp Gly Met Lys Asn Tyr Glu Glu Trp Ala 275 280 285 Lys Asp Leu Thr Asp Ser Gln Arg Glu Ala Leu Asp Gly Tyr Ala Arg 290 295 300 Gln Asp Tyr Lys Glu Ile Asn Asn Tyr Leu Arg Asn Gln Gly Gly Ser305 310 315 320 Gly Asn Glu Lys Leu Asp Ala Gln Ile Lys Asn Ile Ser Asp Ala Leu 325 330 335 Gly Lys Lys Pro Ile Pro Glu Asn Ile Thr Val Tyr Arg Trp Cys Gly 340 345 350 Met Pro Glu Phe Gly Tyr Gln Ile Ser Asp Pro Leu Pro Ser Leu Lys 355 360 365 Asp Phe Glu Glu Gln Phe Leu Asn Thr Ile Lys Glu Asp Lys Gly Tyr 370 375 380 Met Ser Thr Ser Leu Ser Ser Glu Arg Leu Ala Ala Phe Gly Ser Arg385 390 395 400 Lys Ile Ile Leu Arg Leu Gln Val Pro Lys Gly Ser Thr Gly Ala Tyr 405 410 415 Leu Ser Ala Ile Gly Gly Phe Ala Ser Glu Lys Glu Ile Leu Leu Asp 420 425 430 Lys Asp Ser Lys Tyr His Ile Asp Lys Val Thr Glu Val Ile Ile Lys 435 440 445 Gly Val Lys Arg Tyr Val Val Asp Ala Thr Leu Leu Thr Asn 450 455 460 53775PRTBacillus thuringiensis 53Met Lys Asn Met Lys Lys Lys Leu Ala Ser Val Val Thr Cys Thr Leu1 5 10 15 Leu Ala Pro Met Phe Leu Asn Gly Asn Val Asn Ala Val Tyr Ala Asp 20 25 30 Ser Lys Thr Asn Gln Ile Ser Thr Thr Gln Lys Asn Gln Gln Lys Glu 35 40 45 Met Asp Arg Lys Gly Leu Leu Gly Tyr Tyr Phe Lys Gly Lys Asp Phe 50 55 60 Ser Asn Leu Thr Met Phe Ala Pro Thr Arg Asp Asn Thr Leu Ile Tyr65 70 75 80 Asp Gln Gln Thr Ala Asn Lys Leu Leu Asp Lys Lys Gln Gln Gln Tyr 85 90 95 Gln Ser Ile Arg Trp Ile Gly Leu Ile Gln Ser Lys Glu Lys Gly Asp 100 105 110 Phe Thr Phe Asn Leu Ser Glu Asp Glu Gln Ala Ile Ile Glu Ile Asp 115 120 125 Gly Lys Ile Ile Ser Asn Lys Gly Lys Glu Lys Gln Val Val His Leu 130 135 140 Glu Lys Glu Lys Leu Val Pro Ile Lys Ile Glu Tyr Gln Ser Asp Thr145 150 155 160 Lys Phe Asn Ile Asp Ser Lys Thr Phe Lys Glu Phe Lys Leu Phe Lys 165 170 175 Ile Asp Ser Gln Asn Gln Ser Gln Gln Val Lys Arg Asp Glu Leu Arg 180 185 190 Asn Pro Glu Phe Asn Lys Lys Glu Ser Arg Glu Phe Leu Ala Lys Ala 195 200 205 Ser Lys Thr Asn Phe Phe Met Gln Lys Met Lys Arg Asp Ile Asp Glu 210 215 220 Asp Thr Asp Thr Asp Gly Asp Ser Ile Pro Asp Leu Trp Glu Glu Asn225 230 235 240 Gly Tyr Thr Ile Gln Asn Lys Val Ala Val Lys Trp Asp Asp Lys Phe

245 250 255 Ala Gln Gln Gly Tyr Val Lys Tyr Leu Ser Ser Pro Tyr Gln Ala His 260 265 270 Thr Val Gly Asp Pro Tyr Thr Asp Trp Glu Lys Ala Ala Gly Asp Ile 275 280 285 Pro Lys Ser Asn Ala Ala Ala Thr Arg Asn Pro Leu Val Ala Ala Phe 290 295 300 Pro Ser Ile Asn Val Asp Met Arg Lys Met Ile Leu Ser Lys Asp Ser305 310 315 320 Asn Leu Ser Asn Ser Ala Glu Ala His Ser Asn Asn Ser Tyr Thr Tyr 325 330 335 Ala Asn Ser Glu Gly Ala Ser Ile Glu Ala Gly Phe Gly Pro Lys Gly 340 345 350 Phe Ser Phe Gly Val Ser Ala Asn Tyr Gln His Thr Glu Thr Val Gly 355 360 365 Ser Asp Trp Gly Asn Ser Lys Ser Asn Thr Glu Gln Phe Asn Ser Ala 370 375 380 Ser Ala Gly Tyr Leu Asn Ala Asn Val His Tyr Asn Asn Val Gly Thr385 390 395 400 Gly Gly Ile Tyr Asp Ala Gln Pro Thr Thr Ser Phe Ile Leu Gln Asp 405 410 415 Ser Thr Ile Ala Thr Ile Thr Ala Lys Ser Asn Ala Thr Ala Leu Ser 420 425 430 Ile Pro Ser Gly Asp Arg Tyr Pro Ala Ser Lys Glu Gly Ile Ser Leu 435 440 445 Lys Thr Met Asp Asp Phe Asn Ser His Pro Ile Thr Leu Asn Lys Pro 450 455 460 Gln Leu Asp Ala Val Leu Asn Asn Glu Val Ile Lys Ile Asn Thr Asp465 470 475 480 Gln Thr Asp Gly Arg Tyr Gly Ile Ile Gly Val Asp Gly Lys Ala Glu 485 490 495 Ile Gly Asp Arg Trp Ser Pro Ile Ile Asp Glu Ile Lys Gly Arg Thr 500 505 510 Ala Ser Ile Ile Ile Asp Pro Ala Asp Gly Lys Ala Leu Glu Thr Arg 515 520 525 Ile Ala Ala Lys Asp Tyr Lys Asn Pro Glu Asp Lys Thr Pro Ser Leu 530 535 540 Thr Ile Lys Glu Gly Leu Lys Ile Ala Tyr Pro Glu Ser Ile Ser Glu545 550 555 560 Asp Lys Asp Gly Ile Leu Phe Tyr Glu Tyr Lys Asn Asp Glu Gly Lys 565 570 575 Val Thr Lys Lys Gln Leu Ser Glu Glu Asn Ile Met Pro Tyr Leu Asp 580 585 590 Glu Asp Thr Ser Lys Glu Phe Glu Arg Gln Leu Ser Asp Gly Ser Ala 595 600 605 Lys Gly Leu Tyr Asp Ile Lys Leu Thr Pro Lys Met Asn Ile Thr Ile 610 615 620 Arg Leu Ala Thr Val Thr Leu Gly Phe Asp Asp Gln Phe Ser Ala Tyr625 630 635 640 Pro Trp Glu Asn Ala Thr Trp Ser Asp Lys Phe Gly Asn Leu Arg Leu 645 650 655 Gly Ser Leu Ala Ile Pro Gln Glu Ser Lys Tyr Thr Ile Pro Lys Asp 660 665 670 Lys Val Lys Pro Asn Tyr Asp Tyr Leu Ile Thr Gly Tyr Ile Lys His 675 680 685 Asp Phe Thr Thr Asp Asn Glu Ser Leu Gly Ile Val Ala Phe Thr Lys 690 695 700 Lys Asp Asn Phe Glu Met Trp Asn Met Gly Thr Ser Ile Phe Ser Gln705 710 715 720 Asn Ser Gly Gly Glu Phe Lys Lys Phe Thr Ile Lys Thr Gln Asn Ile 725 730 735 Ser Gly Asp Tyr Ile Leu Asp Ser Ile Gln Leu Met Lys Arg Asn Asn 740 745 750 Asp Val Asn Lys Ile Asp Ser Tyr Leu Asp Asp Ile Ser Ile Ile Pro 755 760 765 Ile Gly Pro Asn Lys Ser Arg 770 775 54126PRTBacillus thuringiensis 54Met Thr Val Tyr Asn Ala Thr Phe Thr Ile Asn Phe Tyr Asn Glu Gly1 5 10 15 Glu Trp Gly Gly Pro Glu Pro Tyr Gly Tyr Ile Lys Ala Tyr Leu Thr 20 25 30 Asn Pro Asp His Asp Phe Glu Ile Trp Lys Gln Asp Asp Trp Gly Lys 35 40 45 Ser Thr Pro Glu Arg Ser Thr Tyr Thr Gln Thr Ile Lys Ile Ser Ser 50 55 60 Asp Thr Gly Ser Pro Ile Asn Gln Met Cys Phe Tyr Gly Asp Val Lys65 70 75 80 Glu Tyr Asp Val Gly Asn Ala Asp Asp Ile Leu Ala Tyr Pro Ser Gln 85 90 95 Lys Val Cys Ser Thr Pro Gly Val Thr Val Arg Leu Asp Gly Asp Glu 100 105 110 Lys Gly Ser Tyr Val Thr Ile Lys Tyr Ser Leu Thr Pro Ala 115 120 125 55462PRTBacillus cereus 55Met Lys Arg Met Glu Gly Lys Leu Phe Met Val Ser Lys Lys Leu Gln1 5 10 15 Val Val Thr Lys Thr Val Leu Leu Ser Thr Val Phe Ser Ile Ser Leu 20 25 30 Leu Asn Asn Glu Val Ile Lys Ala Glu Gln Leu Asn Ile Asn Ser Gln 35 40 45 Ser Lys Tyr Thr Asn Leu Gln Asn Leu Lys Ile Thr Asp Lys Val Glu 50 55 60 Asp Phe Lys Glu Asp Lys Glu Lys Ala Lys Glu Trp Gly Lys Glu Lys65 70 75 80 Glu Lys Glu Trp Lys Leu Thr Ala Thr Glu Lys Gly Lys Met Asn Asn 85 90 95 Phe Leu Asp Asn Lys Asn Asp Ile Lys Thr Asn Tyr Lys Glu Ile Thr 100 105 110 Phe Ser Met Ala Gly Ser Phe Glu Asp Glu Ile Lys Asp Leu Lys Glu 115 120 125 Ile Asp Lys Met Phe Asp Lys Thr Asn Leu Ser Asn Ser Ile Ile Thr 130 135 140 Tyr Lys Asn Val Glu Pro Thr Thr Ile Gly Phe Asn Lys Ser Leu Thr145 150 155 160 Glu Gly Asn Thr Ile Asn Ser Asp Ala Met Ala Gln Phe Lys Glu Gln 165 170 175 Phe Leu Asp Arg Asp Ile Lys Phe Asp Ser Tyr Leu Asp Thr His Leu 180 185 190 Thr Ala Gln Gln Val Ser Ser Lys Glu Arg Val Ile Leu Lys Val Thr 195 200 205 Val Pro Ser Gly Lys Gly Ser Thr Thr Pro Thr Lys Ala Gly Val Ile 210 215 220 Leu Asn Asn Ser Glu Tyr Lys Met Leu Ile Asp Asn Gly Tyr Met Val225 230 235 240 His Val Asp Lys Val Ser Lys Val Val Lys Lys Gly Val Glu Cys Leu 245 250 255 Gln Ile Glu Gly Thr Leu Lys Lys Ser Leu Asp Phe Lys Asn Asp Ile 260 265 270 Asn Ala Glu Ala His Ser Trp Gly Met Lys Asn Tyr Glu Glu Trp Ala 275 280 285 Lys Asp Leu Thr Asp Ser Gln Arg Glu Ala Leu Asp Gly Tyr Ala Arg 290 295 300 Gln Asp Tyr Lys Glu Ile Asn Asn Tyr Leu Arg Asn Gln Gly Gly Ser305 310 315 320 Gly Asn Glu Lys Leu Asp Ala Gln Ile Lys Asn Ile Ser Asp Ala Leu 325 330 335 Gly Lys Lys Pro Ile Pro Glu Asn Ile Thr Val Tyr Arg Trp Cys Gly 340 345 350 Met Pro Glu Phe Gly Tyr Gln Ile Ser Asp Pro Leu Pro Ser Leu Lys 355 360 365 Asp Phe Glu Glu Gln Phe Leu Asn Thr Ile Lys Glu Asp Lys Gly Tyr 370 375 380 Met Ser Thr Ser Leu Ser Ser Glu Arg Leu Ala Ala Phe Gly Ser Arg385 390 395 400 Lys Ile Ile Leu Arg Leu Gln Val Pro Lys Gly Ser Thr Gly Ala Tyr 405 410 415 Leu Ser Ala Ile Gly Gly Phe Ala Ser Glu Lys Glu Ile Leu Leu Asp 420 425 430 Lys Asp Ser Lys Tyr His Ile Asp Lys Val Thr Glu Val Ile Ile Lys 435 440 445 Gly Val Lys Arg Tyr Val Val Asp Ala Thr Leu Leu Thr Asn 450 455 460 56457PRTBrevibacillus laterosporus 56Met Ile Val Ile Ile Phe Thr Asn Val Lys Gly Gly Asn Glu Leu Lys1 5 10 15 Lys Asn Phe Tyr Lys Asn Leu Ile Cys Met Ser Ala Leu Leu Leu Ala 20 25 30 Met Pro Ile Ser Ser Asn Val Thr Tyr Ala Tyr Gly Ser Glu Lys Val 35 40 45 Asp Tyr Leu Val Lys Thr Thr Asn Asn Thr Glu Asp Phe Lys Glu Asp 50 55 60 Lys Glu Lys Ala Lys Glu Trp Gly Lys Glu Lys Glu Lys Glu Trp Lys65 70 75 80 Leu Thr Val Thr Glu Lys Thr Arg Met Asn Asn Phe Leu Asp Asn Lys 85 90 95 Asn Asp Ile Lys Lys Asn Tyr Lys Glu Ile Thr Phe Ser Met Ala Gly 100 105 110 Ser Phe Glu Asp Glu Ile Lys Asp Leu Lys Glu Ile Asp Lys Met Phe 115 120 125 Asp Lys Ala Asn Leu Ser Ser Ser Ile Val Thr Tyr Lys Asn Val Glu 130 135 140 Pro Ser Thr Ile Gly Phe Asn Lys Pro Leu Thr Glu Gly Asn Thr Ile145 150 155 160 Asn Thr Asp Val Gln Ala Gln Phe Lys Glu Gln Phe Leu Gly Lys Asp 165 170 175 Ile Lys Phe Asp Ser Tyr Leu Asp Thr His Leu Thr Ala Gln Asn Val 180 185 190 Ser Ser Lys Glu Arg Ile Ile Leu Gln Val Thr Val Pro Ser Gly Lys 195 200 205 Gly Ser Thr Ile Pro Thr Lys Ala Gly Val Ile Leu Asn Asn Asn Glu 210 215 220 Tyr Lys Met Leu Ile Asp Asn Gly Tyr Val Leu His Val Asp Asn Ile225 230 235 240 Ser Lys Val Val Lys Lys Gly Tyr Glu Cys Leu Gln Ile Gln Gly Thr 245 250 255 Leu Lys Lys Ser Leu Asp Phe Lys Asn Asp Ile Asn Ala Glu Ala His 260 265 270 Arg Trp Gly Met Lys Asn Tyr Glu Gly Trp Ala Lys Asn Leu Thr Asp 275 280 285 Pro Gln Arg Glu Ala Leu Asp Gly Tyr Ala Arg Gln Asp Tyr Lys Gln 290 295 300 Ile Asn Asp Tyr Leu Arg Asn Gln Gly Gly Ser Gly Asn Glu Lys Leu305 310 315 320 Asp Thr Gln Ile Lys Asn Ile Ser Glu Ala Leu Glu Lys Gln Pro Ile 325 330 335 Pro Glu Asn Ile Thr Val Tyr Arg Trp Cys Gly Met Ala Glu Phe Gly 340 345 350 Tyr Gln Ile Ser Asp Pro Leu Pro Ser Leu Lys Glu Met Glu Glu Lys 355 360 365 Phe Leu Asn Thr Met Lys Glu Asp Lys Gly Tyr Met Ser Thr Ser Leu 370 375 380 Ser Ser Glu Arg Leu Ser Ala Phe Gly Ser Arg Lys Phe Ile Leu Arg385 390 395 400 Leu Gln Val Pro Lys Gly Ser Thr Gly Ala Tyr Leu Ser Ala Ile Gly 405 410 415 Gly Phe Ala Ser Glu Lys Glu Ile Leu Ile Asp Lys Asp Ser Asn Tyr 420 425 430 His Ile Asp Lys Ile Thr Glu Val Val Ile Lys Gly Val Lys Arg Tyr 435 440 445 Val Val Asp Ala Thr Leu Leu Thr Lys 450 455 57454PRTClostridium perfringens 57Met Lys Lys Val Asn Lys Ser Ile Ser Val Phe Leu Ile Leu Tyr Leu1 5 10 15 Ile Leu Thr Ser Ser Phe Pro Ser Tyr Thr Tyr Ala Gln Asp Leu Gln 20 25 30 Ile Ala Ser Asn Tyr Ile Thr Asp Arg Ala Phe Ile Glu Arg Pro Glu 35 40 45 Asp Phe Leu Lys Asp Lys Glu Asn Ala Ile Gln Trp Glu Lys Lys Glu 50 55 60 Ala Glu Arg Val Glu Lys Asn Leu Asp Thr Leu Glu Lys Glu Ala Leu65 70 75 80 Glu Leu Tyr Lys Lys Asp Ser Glu Gln Ile Ser Asn Tyr Ser Gln Thr 85 90 95 Arg Gln Tyr Phe Tyr Asp Tyr Gln Ile Glu Ser Asn Pro Arg Glu Lys 100 105 110 Glu Tyr Lys Asn Leu Arg Asn Ala Ile Ser Lys Asn Lys Ile Asp Lys 115 120 125 Pro Ile Asn Val Tyr Tyr Phe Glu Ser Pro Glu Lys Phe Ala Phe Asn 130 135 140 Lys Glu Ile Arg Thr Glu Asn Gln Asn Glu Ile Ser Leu Glu Lys Phe145 150 155 160 Asn Glu Leu Lys Glu Thr Ile Gln Asp Lys Leu Phe Lys Gln Asp Gly 165 170 175 Phe Lys Asp Val Ser Leu Tyr Glu Pro Gly Asn Gly Asp Glu Lys Pro 180 185 190 Thr Pro Leu Leu Ile His Leu Lys Leu Pro Lys Asn Thr Gly Met Leu 195 200 205 Pro Tyr Ile Asn Ser Asn Asp Val Lys Thr Leu Ile Glu Gln Asp Tyr 210 215 220 Ser Ile Lys Ile Asp Lys Ile Val Arg Ile Val Ile Glu Gly Lys Gln225 230 235 240 Tyr Ile Lys Ala Glu Ala Ser Ile Val Asn Ser Leu Asp Phe Lys Asp 245 250 255 Asp Val Ser Lys Gly Asp Leu Trp Gly Lys Glu Asn Tyr Ser Asp Trp 260 265 270 Ser Asn Lys Leu Thr Pro Asn Glu Leu Ala Asp Val Asn Asp Tyr Met 275 280 285 Arg Gly Gly Tyr Thr Ala Ile Asn Asn Tyr Leu Ile Ser Asn Gly Pro 290 295 300 Leu Asn Asn Pro Asn Pro Glu Leu Asp Ser Lys Val Asn Asn Ile Glu305 310 315 320 Asn Ala Leu Lys Leu Thr Pro Ile Pro Ser Asn Leu Ile Val Tyr Arg 325 330 335 Arg Ser Gly Pro Gln Glu Phe Gly Leu Thr Leu Thr Ser Pro Glu Tyr 340 345 350 Asp Phe Asn Lys Ile Glu Asn Ile Asp Ala Phe Lys Glu Lys Trp Glu 355 360 365 Gly Lys Val Ile Thr Tyr Pro Asn Phe Ile Ser Thr Ser Ile Gly Ser 370 375 380 Val Asn Met Ser Ala Phe Ala Lys Arg Lys Ile Ile Leu Arg Ile Asn385 390 395 400 Ile Pro Lys Asp Ser Pro Gly Ala Tyr Leu Ser Ala Ile Pro Gly Tyr 405 410 415 Ala Gly Glu Tyr Glu Val Leu Leu Asn His Gly Ser Lys Phe Lys Ile 420 425 430 Asn Lys Val Asp Ser Tyr Lys Asp Gly Thr Val Thr Lys Leu Ile Leu 435 440 445 Asp Ala Thr Leu Ile Asn 450 584PRTArtificial Sequenceendoplasmic reticulum retention sequence 58Lys Asp Glu Leu1 5912DNAArtificial Sequencenucleotide sequence upstream of the ATG start site of axmi-011 59gtgatgaaaa aa 1260969DNABacillus thuringiensisCDS(1)...(969) 60gtg atg aaa aaa atg aat aaa aaa cct atg gta gcg ttg ata tta gcc 48Met Met Lys Lys Met Asn Lys Lys Pro Met Val Ala Leu Ile Leu Ala1 5 10 15act tcg att ggt ata cct tgt aca ttt aca cct gga agt gca tta gca 96Thr Ser Ile Gly Ile Pro Cys Thr Phe Thr Pro Gly Ser Ala Leu Ala 20 25 30gca gaa aat att cag act agt gtt aat gaa aat gta aaa gtt ggt att 144Ala Glu Asn Ile Gln Thr Ser Val Asn Glu Asn Val Lys Val Gly Ile 35 40 45aca gat gtt caa tct gaa ttg aat aag ata gga gac tat tat tat agt 192Thr Asp Val Gln Ser Glu Leu Asn Lys Ile Gly Asp Tyr Tyr Tyr Ser 50 55 60aat aac tta gca aat acg act ata aaa cct cct cat cat tgg gat tat 240Asn Asn Leu Ala Asn Thr Thr Ile Lys Pro Pro His His Trp Asp Tyr65 70 75 80aca ctt aaa aaa aat cct gat aaa gtt gga aca aat ttg gat ttt agt 288Thr Leu Lys Lys Asn Pro Asp Lys Val Gly Thr Asn Leu Asp Phe Ser 85 90 95att act ggt act gct agt aaa cta aat tat gat agt gta act cct ata 336Ile Thr Gly Thr Ala Ser Lys Leu Asn Tyr Asp Ser Val Thr Pro Ile 100 105 110tac att ggg cat aat gaa ttt aat aat gat tca gat cag cct caa aaa 384Tyr Ile Gly His Asn Glu Phe Asn Asn Asp Ser Asp Gln Pro Gln Lys 115 120 125ttt aca act tct aaa ttt act aaa gct gta aca gag gga aca aca agt 432Phe Thr Thr Ser Lys Phe Thr Lys Ala Val Thr Glu Gly Thr Thr Ser 130 135 140acc gta aca aat gga ttt aga tta gga aat cca ggt tta aac tta ttt 480Thr Val Thr Asn Gly Phe Arg Leu Gly Asn Pro Gly Leu Asn Leu Phe145

150 155 160act att cca tta att tta agt gat ggt atg aaa att aat gcg gaa ttt 528Thr Ile Pro Leu Ile Leu Ser Asp Gly Met Lys Ile Asn Ala Glu Phe 165 170 175aac tct tct act tca gaa tct caa caa aaa tcg gaa aca aaa aca ata 576Asn Ser Ser Thr Ser Glu Ser Gln Gln Lys Ser Glu Thr Lys Thr Ile 180 185 190gaa gca tca cct caa aac ata gaa gtt cca gca cat aaa aaa tat aaa 624Glu Ala Ser Pro Gln Asn Ile Glu Val Pro Ala His Lys Lys Tyr Lys 195 200 205gta gat gtt gta ttg gaa caa aca agc tat tgg gca gat gtt aca ttt 672Val Asp Val Val Leu Glu Gln Thr Ser Tyr Trp Ala Asp Val Thr Phe 210 215 220aca ggt gaa gga att aat ctt aat act act ata aat gca act gga ata 720Thr Gly Glu Gly Ile Asn Leu Asn Thr Thr Ile Asn Ala Thr Gly Ile225 230 235 240cat act ggg cat atg gga atg cag gag tca aga aaa ttt tct tgg aac 768His Thr Gly His Met Gly Met Gln Glu Ser Arg Lys Phe Ser Trp Asn 245 250 255aaa aat acc att gaa tta ttt aat gga cta aaa caa gag caa aaa aat 816Lys Asn Thr Ile Glu Leu Phe Asn Gly Leu Lys Gln Glu Gln Lys Asn 260 265 270aat ata cat ggg att aaa ttt agt aat ggg aaa atg aat gca aac gga 864Asn Ile His Gly Ile Lys Phe Ser Asn Gly Lys Met Asn Ala Asn Gly 275 280 285aca ggt aaa gtt gaa ggt att ttt ggt agt aat cta gtt gta aag gta 912Thr Gly Lys Val Glu Gly Ile Phe Gly Ser Asn Leu Val Val Lys Val 290 295 300aat gat gtt aca gat cca tta aat cct atc cta gta atg act aaa agt 960Asn Asp Val Thr Asp Pro Leu Asn Pro Ile Leu Val Met Thr Lys Ser305 310 315 320tta aaa taa 969Leu Lys 61322PRTBacillus thuringiensis 61Met Met Lys Lys Met Asn Lys Lys Pro Met Val Ala Leu Ile Leu Ala1 5 10 15 Thr Ser Ile Gly Ile Pro Cys Thr Phe Thr Pro Gly Ser Ala Leu Ala 20 25 30 Ala Glu Asn Ile Gln Thr Ser Val Asn Glu Asn Val Lys Val Gly Ile 35 40 45 Thr Asp Val Gln Ser Glu Leu Asn Lys Ile Gly Asp Tyr Tyr Tyr Ser 50 55 60 Asn Asn Leu Ala Asn Thr Thr Ile Lys Pro Pro His His Trp Asp Tyr65 70 75 80 Thr Leu Lys Lys Asn Pro Asp Lys Val Gly Thr Asn Leu Asp Phe Ser 85 90 95 Ile Thr Gly Thr Ala Ser Lys Leu Asn Tyr Asp Ser Val Thr Pro Ile 100 105 110 Tyr Ile Gly His Asn Glu Phe Asn Asn Asp Ser Asp Gln Pro Gln Lys 115 120 125 Phe Thr Thr Ser Lys Phe Thr Lys Ala Val Thr Glu Gly Thr Thr Ser 130 135 140 Thr Val Thr Asn Gly Phe Arg Leu Gly Asn Pro Gly Leu Asn Leu Phe145 150 155 160 Thr Ile Pro Leu Ile Leu Ser Asp Gly Met Lys Ile Asn Ala Glu Phe 165 170 175 Asn Ser Ser Thr Ser Glu Ser Gln Gln Lys Ser Glu Thr Lys Thr Ile 180 185 190 Glu Ala Ser Pro Gln Asn Ile Glu Val Pro Ala His Lys Lys Tyr Lys 195 200 205 Val Asp Val Val Leu Glu Gln Thr Ser Tyr Trp Ala Asp Val Thr Phe 210 215 220 Thr Gly Glu Gly Ile Asn Leu Asn Thr Thr Ile Asn Ala Thr Gly Ile225 230 235 240 His Thr Gly His Met Gly Met Gln Glu Ser Arg Lys Phe Ser Trp Asn 245 250 255 Lys Asn Thr Ile Glu Leu Phe Asn Gly Leu Lys Gln Glu Gln Lys Asn 260 265 270 Asn Ile His Gly Ile Lys Phe Ser Asn Gly Lys Met Asn Ala Asn Gly 275 280 285 Thr Gly Lys Val Glu Gly Ile Phe Gly Ser Asn Leu Val Val Lys Val 290 295 300 Asn Asp Val Thr Asp Pro Leu Asn Pro Ile Leu Val Met Thr Lys Ser305 310 315 320 Leu Lys626DNAArtificial Sequenceribosomal binding sequence 62gtgatg 6635DNAArtificial Sequenceribosomal binding sequence 63ggaga 5

Claims

1. An isolated or recombinant nucleic acid molecule comprising a nucleotide sequence selected from the group consisting of: a) the nucleotide sequence of SEQ ID NO:18, 3, 5, 8, 10, 12, 14, 16, 20, 22, 24, 26, 28, 30, 32, 34, or 36, or a complement thereof; b) a nucleotide sequence that encodes a polypeptide comprising the amino acid sequence of SEQ ID NO:19, 4, 6, 7, 9, 11, 13, 15, 17, 21, 23, 25, 27, 29, 31, 33, 35, or 37; c) a nucleotide sequence that encodes a polypeptide comprising an amino acid sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:19, 4, 6, 7, 9, 11, 13, 15, 17, 21, 23, 25, 27, 29, 31, 33, 35, or 37; and d) the nucleotide sequence of the DNA insert of the plasmid deposited as Accession No. B-30955, B-30956, B-30957, B-30958, B-30942, B-30939, B-30941, B-50047, B-30959, B-30960, B-30943, or B-50048, or a complement thereof.

2. The isolated or recombinant nucleic acid molecule of claim 1, wherein said nucleotide sequence is operably linked to a promoter capable of directing expression of the nucleotide sequence in a plant cell.

3. The isolated or recombinant nucleic acid molecule of claim 1, wherein said nucleotide sequence is a synthetic sequence that has been designed for expression in a plant.

4. A vector comprising the nucleic acid molecule of claim 1.

5. The vector of claim 4, further comprising a nucleic acid molecule encoding a heterologous polypeptide.

6. A host cell that contains the recombinant nucleic acid of claim 1.

7. The host cell of claim 6 that is a bacterial host cell.

8. The host cell of claim 6 that is a plant cell.

9. A transgenic plant comprising the host cell of claim 8.

10. The transgenic plant of claim 9, wherein said plant is selected from the group consisting of maize, sorghum, wheat, cabbage, sunflower, tomato, crucifers, peppers, potato, cotton, rice, soybean, sugarbeet, sugarcane, tobacco, barley, and oilseed rape.

11. A transgenic seed comprising the nucleic acid molecule of claim 1.

12. An isolated polypeptide with pesticidal activity, selected from the group consisting of: a) a polypeptide comprising the amino acid sequence of SEQ ID NO:19, 4, 6, 7, 9, 11, 13, 15, 17, 21, 23, 25, 27, 29, 31, 33, 35, or 37; b) a polypeptide comprising an amino acid sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 19, 4, 6, 7, 9, 11, 13, 15, 17, 21, 23, 25, 27, 29, 31, 33, 35, or 37; c) a polypeptide that is encoded by the nucleotide sequence of SEQ ID NO:18, 3, 5, 8, 10, 12, 14, 16, 20, 22, 24, 26, 28, 30, 32, 34, or 36; d) a polypeptide encoded by the nucleotide sequence of the DNA insert of the plasmid deposited as Accession No. B-30955, B-30956, B-30957, B-30958, B-30942, B-30939, B-30941, B-50047, B-30959, B-30960, B-30943, or B-50048.

13. The polypeptide of claim 12 further comprising heterologous amino acid sequences.

14. A composition comprising the polypeptide of claim 12.

15. The composition of claim 14, wherein said composition is selected from the group consisting of a powder, dust, pellet, granule, spray, emulsion, colloid, and solution.

16. The composition of claim 14, wherein said composition is prepared by desiccation, lyophilization, homogenization, extraction, filtration, centrifugation, sedimentation, or concentration of a culture of bacterial cells.

17. The composition of claim 14, comprising from about 1% to about 99% by weight of said polypeptide.

18. A method for killing or controlling a lepidopteran, coleopteran, nematode, or dipteran pest population comprising contacting said population with a pesticidally-effective amount of a polypeptide of claim 12.

19. A method for producing a polypeptide with pesticidal activity, comprising culturing the host cell of claim 6 under conditions in which the nucleic acid molecule encoding the polypeptide is expressed.

20. A plant having stably incorporated into its genome a DNA construct comprising a nucleotide sequence that encodes a protein having pesticidal activity, wherein said nucleotide sequence is selected from the group consisting of: a) the nucleotide sequence of SEQ ID NO:18, 3, 5, 8, 10, 12, 14, 16, 20, 22, 24, 26, 28, 30, 32, 34, or 36; b) a nucleotide sequence that encodes a polypeptide comprising the amino acid sequence of SEQ ID NO:19, 4, 6, 7, 9, 11, 13, 15, 17, 21, 23, 25, 27, 29, 31, 33, 35, or 37; c) a nucleotide sequence that encodes a polypeptide comprising an amino acid sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:19, 4, 6, 7, 9, 11, 13, 15, 17, 21, 23, 25, 27, 29, 31, 33, 35, or 37; and d) the nucleotide sequence of the DNA insert of the plasmid deposited as Accession No. B-30955, B-30956, B-30957, B-30958, B-30942, B-30939, B-30941, B-50047, B-30959, B-30960, B-30943, or B-50048; wherein said nucleotide sequence is operably linked to a promoter that drives expression of a coding sequence in a plant cell.

21. The plant of claim 20, wherein said plant is a plant cell.

22. A method for protecting a plant from a pest, comprising introducing into said plant or cell thereof at least one expression vector comprising a nucleotide sequence that encodes a pesticidal polypeptide, wherein said nucleotide sequence is selected from the group consisting of: a) the nucleotide sequence of SEQ ID NO:18, 3, 5, 8, 10, 12, 14, 16, 20, 22, 24, 26, 28, 30, 32, 34, or 36; b) a nucleotide sequence that encodes a polypeptide comprising the amino acid sequence of SEQ ID NO:19, 4, 6, 7, 9, 11, 13, 15, 17, 21, 23, 25, 27, 29, 31, 33, 35, or 37; c) a nucleotide sequence that encodes a polypeptide comprising an amino acid sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:19, 4, 6, 7, 9, 11, 13, 15, 17, 21, 23, 25, 27, 29, 31, 33, 35, or 37; and d) the nucleotide sequence of the DNA insert of the plasmid deposited as Accession No. B-30955, B-30956, B-30957, B-30958, B-30942, B-30939, B-30941, B-50047, B-30959, B-30960, B-30943, or B-50048.

23. The method of claim 22, wherein said plant produces a pesticidal polypeptide having pesticidal activity against a lepidopteran, coleopteran, nematode, or dipteran pest.