Patent Publication Number: US-2003226175-A1

Title: DNA regulatory elements associated with fruit development

Description:
[0001] This application is a continuation-in-part of U.S. application Ser. No. 09/160,351, filed Sep. 25, 1998, which is a continuation of provisional Application 60/060,062, filed on Sep. 25, 1997. This application claims priority of these aforementioned applications under 35 U.S.C. §§ 119 and 120 and the entire content of both of these priority applications is hereby incorporated by reference. 
    
    
     
       BACKGROUND OF THE INVENTION  
       [0002] 1. Field of the Invention  
       [0003] The present invention relates to genes which are differentially expressed during banana fruit development, the protein products of these genes, and DNA regulatory elements which are differentially expressed during banana fruit development.  
       [0004] 2. Description of the Related Art  
       [0005] Bananas represent a crop of great importance to both the world economy and as a means of supplying subsistence to a large portion of the world&#39;s population. The global banana export market is about 10% of the world&#39;s production with a $4 billion dollar value. Banana fruit are the fourth most important food in the developing world (May, G D et al. (1995)  Biotechnology  13:486-492) with approximately 100 million people acquiring their main energy source from bananas. Bananas, like kiwifruit, papayas, and apples, are climacteric fruit, meaning they ripen in association with an ethylene signal. In the ripening process, starch degradation is associated with a respiratory climacteric in the fruit. Banana fruit ripening is characterized by a number of biochemical and physiological changes including fruit softening, changes in peel color and an increase in respiratory activity (Seymour, G B (1993) in: Seymour G B, et al. (eds)  Biochemistry of Fruit Ripening,  pp 83-106. Chapman &amp; Hall, London). Although ethylene is produced by the fruit, ripening can also be stimulated by the application of exogenous ethylene. Alternatively, endogenous ethylene production may be stimulated, e.g., by exposing fruit to acetylene.  
       [0006] More specifically, the post-harvest physiology of the banana ( Musa acuminata  cv. Grand Nain) is characterized by initial harvest, a green storage phase, followed by a burst in ethylene production that signals the beginning of the climacteric period. Associated with this respiratory climacteric is a massive conversion of starch to sugars in the pulp, during which the activities of enzymes involved in starch biosynthesis decrease while those involved in starch breakdown and mobilization increase rapidly (Wu et al. (1989)  Acta Phytophysiol. Sin.  15:145-152; Agravante et al. (1990)  J. Jpn. Soc. Food Sci. Technol.  37:911-915; Iyare et al. (1992)  J. Sci. Food Agric.  58: 173-176; Cordenunsi et al. (1995),  J. Agric. Food Chem.  43:347-351; Hill et al. (1995)  Planta  196:335-343 and 197:313-323). In addition, the rate of respiration rises sharply (Beaudry et al. (1987)  Plant Physiol.  8:277-282; Beaudry et al. (1989)  Plant Physiol.  91:1436-1444).  
       [0007] Other changes that occur during ripening include: fruit softening as a result of enzymatic degradation of structural carbohydrates (Agravante et al. (1991)  J. Jpn. Soc. Food Sci. Technol.  38:527-532; Kojima et al. (1994)  Physiol. Plant.  90:772-778); a decline in those polyphenol compounds responsible for the astringency of the green unripe fruit which are catalyzed by polyphenol oxidase and peroxidases (Mendoza et al. (1994) in I Uritani et al., eds., Postharvest Biochemistry of Plant Food-Materials in the Tropics. Japan Scientific Societies Press, Tokyo, pp 177-191); an increase in the activity of alcohol acetyltransferase, the enzyme that catalyzes the synthesis of isoamyl acetate—the major aroma compound of banana fruit (Harada et al. (1985)  Plant Cell Physiol.  26:1067-1074); and a de-greening of the peel as a result of chlorophyll breakdown by chlorophyllase (Thomas et al. (1992)  Int. J. Food Sci. Technol.  27:57-63). Stages of banana fruit ripening are scored by peel color index (PCI) numbers, on a scale from 1—very green, to 7—yellow-flecked with brown flecks (Color Preferences Chart, Customer Services Department, Chiquita Brands, Inc.,). PCI can be correlated with other biochemical and physiological parameters associated with fruit development and ripening such as ethylene biosynthesis and respiratory rate. The respiratory rate usually peaks at PCI 2 and PCI 4, respectively, in ethylene-treated bananas (Agravante et al. (1991) supra).  
       [0008] Associated with the respiratory climacteric is a large increase in the rate of protein synthesis (Mugugaiyan (1993)  Geobios,  20:18-21), as well as differential protein accumulation (Dominguez-Puigjaner et al. (1992)  Plant Physiol.  98:157-162). Poly-galacturonase (PG) has been identified as a protein that increases in banana pulp during ripening, as determined by 2-D gel electrophoresis and immuno-hybridization (id.). Many of the changes that occur during ripening require de novo protein synthesis (Areas et al. (1988)  J. Food Biochem.  12:51-60); therefore, a secondary approach to investigate changes that occur during ripening is to isolate transcripts encoding proteins associated with the ripening process. Analogous studies of differential gene expression have been successfully employed in other plant species.  
       [0009] Other enzymes associated with developing and ripening of fruit include proteinase inhibitors and chitinases (Dopico et al. (1993)  Plant Molec. Bio.  21:437), stress-related enzymes (Ledger et al. (1994)  Plant Molec. Biol.  25:877), β-oxidation pathway enzymes (Bojorquez et al. (1995),  Plant Molec. Biol.  28:811), and metabolite-detoxifying enzymes (Picton et al. (1993)  Plant Molec. Biol.  23:193). Chitinases are abundant proteins found in a wide variety of plants. Although chitinases are produced by a diversity of plant species, the presence of chitin has not been reported in higher plants. Since chitin is the major structural component of fungal cell walls, it has been proposed that chitinases serve as defense proteins with antifungal activity. Chitinases are reported to be induced in higher plants by a number of different types of stress (Linthorst (1991)  Crit. Rev. Plant Sci.  10: 123; Punja et al. (1993)  J. Nematol.  25:526; Collinge et al. (1993)  Plant J.  3:31). Many plant chitinases are expressed constitutively, although at a low level.  
       [0010] As noted above, in ripening climacteric fruit, starch degradation is associated with a respiratory climacteric in the fruit. Reactive oxygen species (ROS) are byproducts of cellular respiration, especially under conditions which result in high levels of NADH. ROS generation during respiration may be at the site of ubiquinones in the electron transport chain. Both yeast and mammalian metallothioniens may play a direct role in the cellular defense against oxidative stress by functioning as antioxidants (Dalton et al. (1994)  Nucl. Acids Res.  22:5016-5203; Tamai et al. (1993)  Proc Nat Acad Sci  (USA) 90:8013-8017; Bauman et al. (1991)  Toxicol. Appl. Pharmacol.  110:347-354). MT may play an additional role in supplying metal ions to Cu- and Zn-superoxide dismutase (SOD), an enzyme that catalyzes the disproportionation of superoxide anion to hydrogen peroxide and dioxygen and is thought to play an important role in protecting cells from oxygen toxicity.  
       [0011] Transcripts encoding MT or MT-like proteins have been isolated from many different plants (recently reviewed in Robinson et al. (1993)  Biochem J.  295: 1-10). There is accumulating evidence that the plant MT mRNAs are translated, and the protein may have a function in the plant tissues from which transcripts have been isolated. A seed-associated polypeptide (E c  protein) has been purified from wheat and sequenced (Kawashima et al. 1992), and more recently, MT was reported to have been isolated from Arabidopsis (meeting abstract). Based on deduced amino acid sequences, plant MT proteins are approximately 70 aa and have characteristic cysteine-rich regions at the N and C termini, separated by a variable spacer region. Based on the number and distribution of the cysteine residues, plant MTs have been classified into two distinct types (Robinson et al. (1993), supra). Type 1 MTs have 6 N-terminal and 6 C-terminal cysteine residues, whereas type 2 have 8 cysteine residues in the N-terminal domain and 6 at the C-terminus. Although there are no strict patterns of MT expression, in general type 1 transcript abundance is high in roots, and is often metal-inducible, whereas type 2 is expressed primarily in leaves. Other transcripts have been isolated that encode proteins with homology to plant MTs but cannot be classified as either type 1 or type 2, and these include seed-specific proteins or transcripts from barley and wheat (see, Robinson et al. (1993), supra). In  Arabidopsis thaliana,  MT proteins are encoded by a gene family containing five members, two copies encoding a type 2 MT and 3 encoding a MT with homology to type 1 (Zhou et al. (1995)  Mol. Gen. Genet.  248:318-328).  
       [0012] In plants transcripts encoding metallothionein-like proteins have often been isolated by differential screening. Type 2 MT have recently been isolated from plants expressed in association with senescence, leaf abcission (Coupe et al. (1995)  Planta  197:442-447), and fruit ripening (Ledger et al. (1994)  Plant Molec. Biol.  25:877-886). Using differential screening, Ledger and Gardner (id.) found transcripts encoding MT-like proteins in developing kiwifruit. One, pKIWI503, was specifically upregulated late in fruit development, during ripening of the mature fruit.  
       [0013] A major component of the export market is the level of ripening control which is exerted by modern banana shipping systems. Bananas for export must be shipped under refrigeration at 12-14° C., often under controlled atmosphere (CA) conditions (i.e., low oxygen combined with CO 2 ), which reduces the effects of ethylene produced by the fruit. Exposure to ethylene for 24 hours at concentrations of 100-1000 μl per liter is used to trigger the ripening climacteric. This “gassing” step is typically done near the final point in the distribution system. Although this system is entirely functional, resulting in marketability of high quality fruit with minimal losses, there remains a role for engineered ethylene control in the banana export market. Bananas for export are harvested green at approximately 75% of full size. This is done to ensure, even with the use of low temperature and CA, that few if any of the bananas start ripening during shipment. Allowing the bananas to remain on the plant longer would result in more carbohydrate accumulation to the fruit and a direct, zero cost increase in yield. If engineered ethylene control were implemented in banana, this increased yield would come at no increased risk of premature ripening during shipment.  
       [0014] Moreover, linking exogenous genes to isolated gene promoters that are differentially expressed during banana ripening, and in response to ethylene, would allow for the production of exogenous protein in banana tied to the ripening process, and in other plants, controlled by ripening or exposure to ethylene.  
       SUMMARY OF THE INVENTION  
       [0015] Accordingly, a major object of the present invention is to provide isolated and purified genes which are differentially expressed during banana fruit development, and to provide the protein products of these genes.  
       [0016] A further object of the present invention is to provide DNA regulatory elements which are differentially expressed during banana fruit development, and chimeric genes comprising these DNA regulatory elements operably linked to heterologous DNA molecules, and plants transformed with said chimeric genes, providing for controlled expression of said heterologous DNA molecules during the development of the fruit of said plants, or in response to exogenous development signals, such as ethylene signals in said plants.  
       [0017] A still further object of the present invention is to provide a method for expression of a heterologous protein in fruit comprising transforming fruiting plants with one or more chimeric genes according to the present invention, exposing said fruit to the appropriate natural or exogenous development signal, such as an ethylene signal, and harvesting fruit containing said heterologous protein. The method of the present invention may further comprise isolating the proteins produced by said method from the harvested fruit. In a particularly preferred embodiment, the heterologous protein is a therapeutic protein, which may be isolated from the harvested fruit, or consumed directly in the transformed fruit by a patient in need of said therapeutic protein.  
       [0018] With the foregoing and other objects, advantages and features of the invention that will become hereinafter apparent, the nature of the invention may be more clearly understood by reference to the following detailed description of the preferred embodiments of the invention and to the appended claims. 
     
    
    
     BRIEF DESCRIPTION OF THE DRAWINGS  
     [0019] The patent or application file contains at least one drawing executed in color. Copies of this patent or patent application publication with color drawing(s) will be provided by the Office upon request and payment of the necessary fee.  
     [0020]FIG. 1. Relative abundance of ripening-associated transcripts in banana pulp at PCI 1, 3 and 5. Plasmids containing the indicated cDNA were affixed to nylon membrane and hybridized with pulp radio-labeled first-strand cDNAs. Relative transcript abundance is expressed in arbitrary units (AU).  
     [0021]FIG. 2. Northern analyses of total RNA from pulp and peel (at PCI 3), root, corm, and leaf tissues hybridized with cDNA probes representing each of the eleven classes of differentially expressed transcripts. Putative identities of each transcript are indicated to the left of the panel.  
     [0022]FIG. 3. Total banana pulp protein extract at different stages of ripening, separated by SDS-PAGE and stained with Coomassie blue. Protein profiles during ripening show the presence of an abundant protein of 31 kDa that decreases in relative abundance during ripening.  
     [0023]FIG. 4. Western blot analysis of total soluble protein extracted from different banana tissues and hybridized with polyclonal antiserum against purified P31. The antiserum detects a 31 kDa protein in pulp which is not present in peel, meristem, leaf, corm, or root tissue.  
     [0024]FIG. 5. Expression of P31 (top panel) and pBAN3-30 (bottom panel) in banana pulp during ripening. Total protein and RNA were isolated from banana pulp at each of seven stages of banana fruit ripening (PCI 1 through 7, numbered at top of figure). Pulp proteins were separated by SDS-PAGE and hybridized with the P31 antiserum. Total RNA (10 μg per lane) was separated by agarose gel electrophoresis and transferred to nylon membrane, and hybridized with a  32 P-labeled banana chitinase cDNA probe (pBAN3-30). Both the P31 protein and the corresponding chitinase transcript at 1.2 kilobases are abundant in pulp during the early stages of ripening but decrease as ripening progresses.  
     [0025]FIG. 6. Western blot analysis of the translation products of four banana chitinase cDNA clones homologous to pBAN3-30 expressed as fusion proteins with β-galactosidase in pBluescript and hybridized with P31 antiserum. The polyclonal antiserum recognizes a 35 kDa polypeptide in bacterial cultures containing in-frame cDNA inserts (pBAN3-36 and pBAN3-45) that is not present in bacterial cells containing either the pBluescript cloning vector without an insert (no insert) or chitinase cDNA inserts that are not in-frame with the β-galactosidase gene (pBAN3-30 and pBAN3-31).  
     [0026]FIG. 7. SEQ ID NO: 1-2 Complete nucleotide sequence of the cDNA clone pBAN3-30 and deduced amino acid sequence of the pBAN3-30 translation product. The N-terminal amino acid sequence obtained from purified P31 is aligned with the translation product and underlined, and is identical to the deduced amino acid sequence of pBAN3-30 at 17 of 20 residues. The translation initiation codon ATG starting at position 55 of pBAN3-30 is underlined as well as the in-frame stop codon at position 1024. Other features of the cDNA sequence include several putative polyadenylation signals between positions 1136 and 1148 (underlined).  
     [0027]FIG. 8. SEQ ID NO: 3-8 Amino acid alignments of A) amino- and B)-carboxy-terminal regions of banana P31 with class III acidic chitinase sequences from chickpea ( Cicer arietinum,  16), grape ( Vitis vinifera,  Busam et al. unpublished),  Arabidopsis thaliana  (17), tobacco ( Nicotiana tabacum,  18), sugar beet ( Beta vulgaris,  19). Dots indicate the amino acid residues identical to the banana P31 amino acid sequence on the top line. Dashes indicate gaps introduced to aid the alignment. A) Amino-terminal alignment illustrates the lack of sequence homology of the signal-peptide sequence of plant chitinases. B) The carboxy-terminal region indicates the 18 residue C-terminal extension unique to the banana P31 sequence.  
     [0028]FIG. 9. SEQ ID NO: 9-10 cDNA sequences of MT F-1 and F-3.  
     [0029]FIG. 10. A) SEQ ID NO: 11-15 Alignment of deduced amino acid sequences of banana and kiwifruit, apple and papaya fruit-associated metallothionein-like proteins. Alignment was performed using Clustal (default settings). Amino acid alignment of fruit-associated MTs. Asterisks above the sequence indicate the pattern of conserved cysteine residues. A dash denotes a gap inserted in the sequence to aid in alignment. A dot indicates that the amino acid in that position is identical to the banana F1 sequence on the top line. (The total number of amino acids is indicated in parentheses at the end of the sequence.) B) Phylogenetic tree of plant MT sequences indicating that the fruit-associated MT are distinct from MT1 and MT2. GenBank Accession numbers for sequences: banana F1; banana F3; kiwifruit (1-2781 1); papaya (EMBL Y08322); apple (U61974); white spruce (L47746);  Vicia faba  MT1b (X91078); chickpea MT1 ( Cicer arietinum ) (X95708);  P. sativum  MT (Z23097);  Oryza sativa  MT-2 (D89931); banana MT2;  L. esculentum  MT-2 (Z68138);  Arabidopsis thaliana  MT2b (U1 1256);  Arabidopsis thaliana  MT1b (U1 1254);  Arabidopsis thaliana  MT1a (U1 1253).  
     [0030]FIG. 11. Northern blot analysis of MT transcript distribution in banana. Total RNA (5 μg/lane) from different banana tissues was separated in a formaldehyde-containing 2% agarose gel, transferred to nylon membrane, and hybridized with an F1 or F3 cDNA probe. The large transcript hybridizes more strongly to the F1 probe, and is approximately 540 bases. The smaller transcript hybridizes more strongly to the F3 cDNA probe, and is approximately 370 bases. Lane labels: Pu=pulp; Pe=perl; R=root; C=corm; L=leaf.  
     [0031]FIG. 12. Restriction maps of MT genomic clones. The maps represent the coding region and at least 1 kb of flanking DNA. The approximate scale is indicated by a dark bar.  
     [0032]FIG. 13. SEQ ID NO: 16 Nucleotide sequence of MT F3 genomic clone, from the 5′ Hindll site to the 3′ Sall site. A 10-base 5′ sequence motif beginning at −313 from the translation start site (in capital letters) shares homology with an antioxidant response element. The putative TATA box (starting at position −96 from the translation start site) is underlined, and the three exons (beginning from the translation start site) are depicted in capital letters. At the 3′ end of the sequence, the stop codon is underlined, as well as a potential polyadenylation signal (TAAATAAA).  
     [0033]FIG. 14. Relative MT transcript abundance in banana pulp-derived protoplasts increases in the presence of hydrogen peroxide but not metal ions, as compared to the untreated control. RNA dot-blots were hybridized to the F3 cDNA probe and hybridization signal intensity, expressed in arbitrary units (AU), was normalized to 18S rRNA as a measure of total RNA loaded.  
     [0034] FIGS.  15 A-E. SEQ ID NO: 17-21 Gluc. DNA and amino acid sequence.  
     [0035] FIGS.  16 A-I. SEQ ID NO: 22-26 Endo. DNA and amino acid sequence.  
     [0036] FIGS.  17 A-G. SEQ ID NO: 27-31 Chitinase DNA and amino acid sequence.  
     [0037] FIGS.  18 A-C. SEQ ID NO: 32-36 MT/F1 DNA and amino acid sequence.  
     [0038] FIGS.  19 A-C. SEQ ID NO: 37-41 F1/MT#2 DNA and amino acid sequence.  
     [0039]FIG. 20. Structural map of pKS-31G. The banana p31 promoter is located between the BamHI (609) and NcoI sites, and the GUS coding sequence is located between the NcoI and BamHI (4657) sites. The polyadenylation signal present in the CaMV 35S 3′ end is located between the XbaI (4663) and the PstI sites.  
     [0040]FIG. 21. Structural map of pGPT-31G. The expression cassette “p31-GUS-35S” from pKS-31G was placed in the T-DNA vector pGPTV-KAN. The T-DNA right and left borders delineate the DNA that is integrated into the plant nuclear genome during transformation mediated by Agrobacterium.  
     [0041] Selection of transformed plants is facilitated by expression of the NptII gene, which confers resistance to kanamycin, adjacent to the left T-DNA border.  
     [0042]FIG. 22. GUS staining of nontransgenic TA234 and transgenic pGPT-31G tomato fruits. Fruits from fully red-ripe (upper) or pink/red fruit (lower) were stained with X-gluc as described (Jefferson, R. A. (1987),  Plant Mol. Biol. Rep.  5:387-405; Jefferson et al. (1987),  EMBO J.  13:3901-3907). No staining is seen in control fruits, while staining in transgenic fruits is seen mostly in the vascular and placental tissues. 
    
    
     DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENTS OF THE INVENTION  
     [0043] The present invention provides isolated and purified banana proteins which are differentially produced in banana fruit during ripening. In a preferred embodiment, said proteins are selected from the group consisting of starch synthases, granule-bound starch synthases, chitinases, endochitinases, β-1,3 glucanases, thaumatin-like proteins, ascorbate peroxidases, metallothioneins, lectins, and other senescence-related genes.  
     [0044] The proteins of the present invention may be isolated from ripening fruit using protein purification methods well known in the art. In particular, fruit containing the protein of the present invention may be subjected to chromatographic techniques which separate proteins present in the extract according to size, affinity and charge. Fractions obtained from each chromatographic step are analyzed for the desired enzymatic activity and subjected to further purification steps. A particularly preferable method for obtaining purified proteins according to the present invention is high performance liquid chromatography (HPLC).  
     [0045] After a protein according to the present invention has been purified, its amino acid sequence can be determined using amino acid sequencing methods well known in the art. A particularly preferable method is Edman degradation. Having obtained sequence information on the protein of the present invention, one can design oligonucleotide probes for isolating the DNA encoding the protein of the present invention, using conventional screening methods, or amplification methods such as polymerase chain reaction (PCR). It is particularly preferable to design such oligonucleotides in a completely degenerate manner, such that oligonucleotides containing each codon encoding a particular amino acid are present in the oligonucleotide mix. Alternatively, inosine can be used at positions in the codon where degeneracies are known to be present. In a particularly preferred embodiment, the proteins of the present invention are encoded by a DNA molecule selected from the group consisting of clones pBAN 3-33, pBAN 3-18, pBAN 3-30, pBAN 3-24, pBAN 1-3, pBAN 3-28, pBAN 3-25, pBAN 3-6, pBAN 3-23, pBAN 3-32, and pBAN 3-46.  
     [0046] The present invention thus further provides an isolated and purified banana DNA molecule which is differentially expressed in fruit during ripening. More specifically, the present invention provides a DNA molecule which is differentially expressed in fruit during ripening, wherein said DNA molecule encodes a protein selected from the group consisting of a starch synthase, a granule-bound starch synthase, a chitinase, an endochitinase, a β-1,3-glucanase, a thaumatin-like protein, an ascorbate peroxidase, a metallothionein, a lectin, or another senescence-related gene. In a particularly preferred embodiment, these DNA molecules are the clones pBAN 3-33, pBAN 3-18, pBAN 3-30, pBAN 3-24, pBAN 1-3, pBAN 3-28, pBAN 3-25, pBAN 3-6, pBAN 3-23, pBAN 3-32, and pBAN 3-46. In another preferred embodiment, the DNA molecule of the present invention has a nucleotide sequence selected from the group consisting of SEQ ID NO: 1; SEQ ID NO: 2; and SEQ ID NO: 3.  
     [0047] In general, the procedures for isolating the DNA encoding a protein according to the present invention, subjecting it to partial digestion, isolating DNA fragments, ligating the fragments into a cloning vector, and transforming a host are well known in recombinant DNA technology. Accordingly, one of ordinary skill in the art can use or adapt the detailed protocols for such procedures as found in Sambrook et al. (1989),  Molecular Cloning: A Laboratory Manual,  2nd. Ed., Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y., 3 volumes, or in any other manual on recombinant DNA technology.  
     [0048] Once the gene encoding a protein of the present invention has been obtained from one species, it can serve as a hybridization probe to isolate corresponding genes from the other species by cross-hybridization under low to moderate stringency conditions. Such conditions are usually found empirically by determining the conditions wherein the probe specifically cross-hybridizes to its counterpart gene with a minimum of background hybridization. Nucleic acid hybridization is a well known technique and thoroughly detailed in Sambrook et al.  
     [0049] As noted above, the DNA encoding the proteins of the present invention can be originally isolated using PCR. Corresponding DNAs from other species can also be isolated using PCR, and oligonucleotides for performing these subsequent PCR reactions can be optimized using the sequence information obtained from DNA cloned from the first species.  
     [0050] Moreover, peptides and fragments as well as chemically modified derivatives of the proteins of the present invention are also contemplated by the present invention. Briefly, any peptide fragment, derivative or analog which retains substantially the same biological activity of the protein of the present invention, and is differentially produced during fruit ripening, is contemplated. An analog may be defined herein as a peptide or fragment which exhibits the biological activity of the protein of the present invention, and which is differentially expressed during fruit ripening, but which has an amino acid substitution, insertion or deletion in comparison to the wild-type protein. Such an analog can be prepared by the “conservative” substitution of an amino acid having similar chemical properties. One of ordinary skill in the art can readily identify suitable substitions.  
     [0051] Thus, it should also be appreciated that also within the scope of the present invention are DNA sequences encoding a protein according to the present invention having the same amino acid sequence as the wild-type protein, but also those DNA sequences which are degenerate to the wild-type sequence. By “degenerate to” is meant that a different three-letter codon is used to specify a particular amino acid. It is well known in the art that the following codons can be used interchangeably to code for each specific amino acid:  
                                           Amino                   Acid   Abbrev.   Codons                  Phenyla-   (Phe or   UUU, UUC           lanine   F)               Leucine   (Leu or   UUA, UUG, CUU, CUC,           L)   CUA, CUG               Isoleu-   (Ile or   AUU, AUC, AUA       cine   I)               Methio-   (Met or   AUG       nine   M)               Valine   (Val or   GUU, GUC, GUA, GUG           V)               Serine   (Ser or   UCU, UCC, UCA, UCG,           S)   AGU, AGC               Proline   (Pro or   CCU, CCC, CCA, CCG           P)               Threonine   (Thr or   ACU, ACC, ACA, ACG           T)               Alanine   (Ala or   GCU, GCG, GCA, GCG           A)               Tyrosine   (Tyr or   UAU, UAC           Y)               Histidine   (His or   CAU, CAC           H)               Glutamine   (Gln or   CAA, CAG           Q)               Aspara-   (Asn or   AAU, AAC       gine   N)               Lysine   (Lys or   AAA, AAG           K)               Aspartic   (Asp or   GAU or GAC       Acid   D)               Glutamic   (Glu or   GAA or GAG       Acid   E)               Cysteine   (Cys or   UGU or UGC           C)               Arginine   (Arg or   CGU, CGC, CGA, CGG,           R)   AGA, AGG               Glycine   (Gly or   GGU, GGC, GGA, GGG           G)               Stop       UAA (ochre), UAG       codon   (amber), UGA (opal)                  
 
     [0052] It should be understood that the codons specified above are for RNA sequences. The corresponding codons for DNA have T substituted for U.  
     [0053] Mutations can be made in the wild-type sequence such that a particular codon is changed to a codon which codes for a different amino acid. Such a mutation is generally made by making the fewest nucleotide changes possible. A substitution mutation of this sort can be made to change an amino acid in the resulting protein in a non-conservative manner (i.e., by changing the codon from an amino acid belonging to a grouping of amino acids having a particular size or characteristic to an amino acid belonging to another grouping) or in a conservative manner (i.e., by changing the codon from an amino acid belonging to a grouping of amino acids having a particular size or characteristic to an amino acid belonging to the same grouping). Such a conservative change generally leads to less change in the structure and function of the resulting protein. A non-conservative change is more likely to alter the structure, activity or function of the resulting protein. The following is one example of various groupings of amino acids:  
                                  Amino acids with nonpolar R groups                             Alanine   Proline           Valine   Phenylalanine           Leucine   Tryptophan           Isoleucine   Methionine                 Amino acids with uncharged polar R groups                             Glycine   Tyrosine           Serine   Asparagine           Threonine   Glutamine           Cysteine                 Amino acids with charged polar R groups       (negatively charged at Ph 6.0)                             Aspartic acid   Glutamic acid                 Basic amino acids (positively charged at pH 6.0)                             Lysine   Arginine           Histidine (at pH 6.0)                      
 
     [0054] Another grouping may be according to molecular weight (i.e., size of R groups):  
                                                              Glycine   75   Aspartic acid   133           Alanine   89   Glutamine   146           Serine   105   Lysine   146           Proline   115   Glutamic acid   147           Valine   117   Methionine   149           Threonine   119   Histidine (at pH 6.0)   155           Cysteine   121   Phenylalanine   165           Leucine   131   Arginine   174           Isoleucine   131   Tyrosine   181           Asparagine   132   Tryptophan   204                      
 
     [0055] Another grouping may be those amino acids with phenyl groups:  
                                                      Phenylalanine   Tryptophan           Tyrosine                      
 
     [0056] Particularly preferred substitutions are:  
     [0057] Lys for Arg and vice versa such that a positive charge may be maintained;  
     [0058] Glu for Asp and vice versa such that a negative charge may be maintained;  
     [0059] Ser for Thr such that a free —OH can be maintained; and  
     [0060] Gln for Asn such that a free NH 2  can be maintained.  
     [0061] Amino acid substitutions may also be introduced to substitute an amino acid with a particularly preferable property. For example, a Cys may be introduced at a potential site for disulfide bridging with another Cys. A His may be introduced as a particularly “catalytic” site (i.e., His can act as an acid or base and is the most common amino acid in biochemical catalysis). Pro may be introduced because of its particularly planar structure, which induces β-turns in the protein&#39;s structure.  
     [0062] Purification of the proteins of the present invention from natural or recombinant sources can be accomplished by conventional purification means such as ammonium sulfate precipitation, gel filtration chromatography, ion exchange chromatography, adsorption chromatography, affinity chromatography, chromatofocusing, HPLC, FPLC, and the like. Where appropriate, purification steps can be done in batch or in columns.  
     [0063] Peptide fragments of the proteins of the present invention can be prepared by proteolysis or by chemical degradation. Typical proteolytic enzymes are trypsin, chymotrypsin, V8 protease, subtilisin and the like; the enzymes are commercially available, and protocols for performing proteolytic digests are well known. Peptide fragments are purified by conventional means, as described above. Peptide fragments can often be identified by amino acid composition or sequence. Peptide fragments are useful as immunogens to obtain antibodies against the proteins of the present invention.  
     [0064] In accordance with the present invention, all or a part of a DNA molecule according to the present invention can be stably inserted in a conventional manner into the nuclear genome of a plant cell, and the so-transformed plant cell can be used to produce a transgenic plant showing improved expression of the DNA molecule according to the present invention. In this regard, a disarmed Ti-plasmid, containing a DNA molecule according to the present invention, in Agrobacterium (e.g.,  A. tumefaciens ) can be used to transform a plant cell using the procedures described, for example, in EP 116.718 and EP 270,822, PCT publication 84.02913, EPA 87400544.0 and Gould et al. ((1991)  Plant Physiol.  95: 426) which are incorporated herein by reference). Preferred Ti-plasmid vectors contain the foregoing DNA sequence between the border sequence, or at least located to the left of the right border sequence, of the T-DNA of the Ti-plasmid.  
     [0065] Replicable expression vectors according to the present invention may include a promoter, a transcription enhancer element, a termination signal, a translation signal, or a combination of two or more of these elements, generally including at least a promoter element.  
     [0066] Replicable expression vectors are generally DNA molecules engineered for controlled expression of a desired gene, especially where it is desirable to produce large quantities of a particular gene product, or polypeptide. The vectors comprise one or more nucleotide sequences operably linked to a gene to control expression of that gene, the gene being expressed, and an origin of replication which is operable in the contemplated host. Preferably the vector encodes a selectable marker, for example, antibiotic resistance. Replicable expression vectors can be plasmids, bacteriophages, cosmids and viruses. Any expression vector comprising RNA is also contemplated. The replicable expression vectors of this invention can express the protein of the present invention at high levels. Many of these vectors are based on pBR322, M13 and lambda and are well known in the art and employ such promoters as tip, lac, P L , T7 polymerase and the like. Hence, one skilled in the art has available many choices of replicable expression vectors, compatible hosts, and well-known methods for making and using the vectors.  
     [0067] Other types of vectors can be used to transform plant cells, using procedures such as direct gene transfer (as described, for example, in EP 233,247), pollen mediated transformation (as described, for example, in EP 270,356, PCT publication WO 95/01856, and U.S. Pat. No. 4,407,956), liposome-mediated transformation (as described, for example, in U.S. Pat. No. 4,5376,475) and other methods such as the methods for transforming monocots described in Fromm et al. ((1990)  Bio/Technology  8:833) and Gordon-Kamm et al.((1990)  Plant Cell  2:603).  
     [0068] Preferably, the gene according to the present invention is inserted in a plant genome downstream of, and under the control of, a promoter which can direct the expression of the gene in the plant cells. Preferred promoters include, but are not limited to, the strong constitutive 35S promoter (Odell et al. (1985)  Nature  313:810) of cauliflower mosaic virus; 35S promoter have been obtained from different isolates (Hull et al. (1987)  Virology  86:482). Other preferred promoters include the TR1′ promoter and the TR2′ promoter (Velten et al.(1984)  EMBO J.  3:2723) Alternatively, a promoter can be utilized which is not constitutive but rather is specific for one or more tissues or organs. For example, a gene according to the present invention can be selectively expressed in the green tissues of a plant by placing the gene under control of a light-inducible promoter such as the promoter of the ribulose-1,5-phosphate-carboxylase small subunit gene as described in EPA 8300921.1. Another alternative is to use a promoter whose expression is inducible by temperature or chemical factors.  
     [0069] It as also preferred that a gene according to the present invention be inserted upstream of suitable 3′ transcription regulation signals (i.e., transcript 3′ end formation and polyadenylation signals) such as the 3′ untranslated end of the octopine synthase gene (Gielen et al.(1984)  EMBO J.,  3:835-845) or T-DNA gene 7 (Velten and Schell (1985)  Nucl. Acids Res.  13:6981-6998).  
     [0070] The resulting transformed plant of this invention expresses the inserted gene and is characterized by the production of high levels of the gene product. Such a plant can be used in a conventional breeding scheme to produce more transformed plants with the same improved phenotypic characteristics, or to introduce the gene into other varieties of the same or related plant species. Seeds, which are obtained from transformed plants, contain the gene as a stable genomic insert.  
     [0071] The present invention further encompasses compositions comprising one or more proteins according to the present invention, and a carrier therefor.  
     [0072] The present invention also provides isolated and purified banana DNA regulatory elements which are 5′ or 3′ to a gene which is differentially expressed during fruit development. In a preferred embodiment, said DNA regulatory elements are promoters. In a particularly preferred embodiment, said promoter is the 2.15 kb 5′ upstream region of the p31 gene whose nucleotide sequence is given in SEQ ID NO: 44. In another particularly preferred embodiment, said p31 promoter is modified with NcoI enzyme sites for vector insertion and whose nucleotide sequence is given in SEQ ID NO: 45. It will be appreciated by those skilled in the art that modifications can be made to the promoters without destroying the scope or spirit of the invention. The invention contemplates that nucleotide fragments of the promoters may be altered, added, or deleted without substantially affecting the promoter&#39;s ability to drive gene expression. Verification that a particular modification does not adversely impact promoter activity is easily determined by common reporter gene assays such as the one illustrated in Example 4. Said regulatory elements of the present invention control the expression of genes to which they are operatively linked, and are sensitive to a plant development signal. In a preferred embodiment, the plant development signal is an ethylene signal. The ethylene signal may be ethylene gas released by ripening fruit, either naturally or stimulated artificially; alternatively, the ethylene signal is produced by exposure of the plant or fruit to exogenous ethylene gas.  
     [0073] The DNA regulatory elements of the present invention may be linked to native plant genes via homologous recombination, e.g., via the method of U.S. Pat. No. 5,272,071, the contents of which are incorporated herein by reference. Alternatively, the DNA regulatory elements of the present invention may be operatively linked to a DNA molecule which is desired to be expressed in a plant in response to a development signal, thus forming a chimeric gene. Transformation of plants with such a chimeric gene, as described above, provides for controlled expression in fruit encoded by said DNA molecule. In a particularly preferred embodiment, said DNA molecule encodes a therapeutic protein.  
     [0074] The DNA molecules of the present invention may be used to transform any plant in which expression of the particular protein encoded by said DNA molecules is desired. In addition, the regulatory elements of the present invention may be used to trigger gene expression in any plant in which gene expression is desired. Suitable plants for transformation with the DNA molecules and regulatory elements of the present invention include Banana (e.g.,  Musa acuminata ); kiwifruit (e.g.,  Actinidia deliciosa ); grape (e.g.,  Vitis vinifera, V. labrusca, V. rotundifolia ); peach, nectarine, plum, apricot, cherry, almond (e.g.,  Prunus persica, P. domestica, P. salicina, P. avium, P. cerasus, P. amygdalus ); pear (e.g.,  Pyrus communis, P. pyrifolia. ); apple (e.g.,  Malus x domestica ); eggplant (e.g.,  Solanum melongena ); tomato (e.g.,  Lycopersicon lycopersicum, L. esculentum ); peppers (e.g., Capciscum sp.); peas and beans (e.g.,  Phaseolus vulgaris, P. lunatus, P. Limensis, Cicer arietimum, Vigna angularis, Pisum sativum, Glycine max ); cucumbers, melons, squash and pumpkins (e.g.,  Cucumis melo, C. sativus, Citrullus lanatus, Cucurbita maxima, C. pepo ); maize (e.g.,  Zea mays ); rice (e.g.,  Oryza sativa ); wheat; barley (e.g.,  Hordeum vulgare ); tobacco (e.g.,  Nicotiana tabacum ); potato (e.g.,  Solanum tuberosum ); beet (e.g.,  Beta vulgaris ); carrot (e.g.,  Daucus carota ); parsnip (e.g.,  Pastinaca sativa ); turnip, rutabaga (e.g.,  Brassica rapa, B. napus ); and radish (e.g.,  Raphanus sativus ). It will be understood that this is not an exclusive list, but merely suggestive of the wide range of utility of the DNA molecules and regulatory elements of the present invention.  
     [0075] The present invention thus also provides a method for expression of heterologous protein in fruit comprising transforming fruiting plants with a chimeric gene, replicable expression vector, or plasmid comprising a ripening-associated promoter, as described above, exposing said fruit to an ethylene signal, and harvesting fruit containing said heterologous protein. The protein may be isolated from the harvested fruit using conventional methods, including those described above. Alternatively, where the protein is a therapeutic protein, in a preferred embodiment the fruit may be directly consumed by a patient in need of the therapeutic protein, thus providing for convenient oral administration of the protein.  
     [0076] The following examples are presented in order to more fully illustrate the preferred embodiments of the invention. They should in no way be construed, however, as limiting the broad scope of the invention.  
     EXAMPLE 1  
     Differential Gene Expression in Ripening Banana ( Musa acuminata  cv. Grand Nain) Fruit  
     [0077] The experiments described in this example were designed to isolate those banana genes that are differentially expressed in ripening banana fruit.  
     Materials and Methods  
     [0078] Plant Materials  
     [0079] Ethylene treated and untreated banana fruit ( Musa acuminata  cv. Grand Nain) were obtained from the Northside Banana Company (Houston, Tex.). The pulp and peel of fruit representing each of the seven different stages of ripening (PCI 1 through 7) were separated and quick-frozen in liquid nitrogen. Tissues from ten individual fruit were pooled to obtain a uniform representative sample for each ripening stage and ground to a fine powder under liquid nitrogen in a stainless steel Waring blender. Ground samples were stored at −80° C. until utilized. Leaf, corm and root tissue were obtained from greenhouse-grown plants (cv Grand Nain), ground in liquid nitrogen using a mortar and pestle, and stored at −80° C.  
     [0080] RNA Isolation  
     [0081] Pre-warmed (65° C.) RNA extraction buffer (1.4% (w/v) SDS, 2% (w/v) polyvinylpyrrolidone, 0.5 M NaCl, 0. 1M sodium acetate, 0.05 M EDTA, pH 8.0, 0.1% (v/v) P-mercaptoethanol) was added to previously ground samples of pulp from PCI 1 and PCI 3 at a 5:1 tissue to buffer ratio. Samples were homogenized with two or three 30 second pulses of a Polytron tissue homogenizer (Brinkman) and incubated at 65° C. for 15 min. Starch and other cell debris were pelleted by centrifugation at 2,400 g for 10 min at room temperature and the supernatant transferred to a disposable 50 ml polypropylene screw-cap tube. After the addition of 0.2 vol. of 5 M potassium acetate, pH 4.8, samples were mixed by inversion and incubated on ice for 30 min. The resulting precipitate was pelleted by centrifugation at 20.2 k rpm for 10 min at 4° C. in a Sorvall SW28 rotor. The supernatant was transferred to a disposable polypropylene centrifuge tube, and the high-molecular weight RNA was precipitated by the addition of lithium chloride to a final concentration of 2.5 M and incubation overnight at 4° C. RNA was isolated from leaf and root tissues using a CTAB isolation buffer modified from Doyle and Doyle (1987). Root and leaf tissues were ground to a powder in liquid nitrogen using a mortar and pestle. Five grams of frozen powder were added to 10 ml of prewarmed (65° C.) CTAB RNA extraction buffer (100 mM Tris-Borate, pH 8.2, 1.4 M NaCl, 20 mM EDTA, 2% (w/v) CTAB (hexadecyltrimethyl-ammonium bromide), 0.1% (v/v) β-mercaptoethanol). Samples were homogenized with two or three 30 second pulses of a Polytron tissue homogenizer (Brinkman), and the homogenate was incubated at 65° C. for one hour. Samples were cooled to room temperature, extracted twice with an equal volume of chloroform, and the phases were separated by centrifugation. Following centrifugation, lithium chloride was added to a final concentration of 2M, and RNA was allowed to precipitate overnight at 4° C. RNA was pelleted at 4° C. for 20 min at 20 kg, washed with 70% ethanol and re-suspended in DEPC-treated H 2 O. The RNA was phenol:chloroform (1:1) extracted and ethanol precipitated.  
     [0082] cDNA Library Construction  
     [0083] Pulp PCI 1 and 3 cDNA libraries were generated using poly(A)+ mRNA prepared from total RNA using a magnetic bead separation protocol (Dynal) according to the manufacturer&#39;s instructions. Lambda Zap cDNA libraries were generated according to the supplier&#39;s protocol (Stratagene).  
     [0084] Differential Screening  
     [0085] Approximately 5×10 4  plaque-forming units (pfu) from each cDNA library were plated onto LB plates using the appropriate  E. coli  host strain. Duplicate plaque-lifts were generated by placing Nytran nylon filters (Schleicher and Schuell) onto plaque-containing plates for one and four minutes for the first and second filters, respectively. Filter-bound DNA was denatured for two min in 1.5 M NaCl, 0.5 M NaOH, and neutralized for four minutes in 1.5 M NaCl, 0.5 M Tris (pH 8.0). Filters were rinsed in 0.5 M Tris (pH 8.0), blotted dry, and UV crosslinked (Stratalinker, Stratagene).  
     [0086] Labeled first-strand cDNA probes used in the differential screening were synthesized from 15 mg total RNA in the presence of 1.5 μm [α-[ 32 P] dCTP (3000 mCi/mmol) using an oligo(dT) 15 , primer (Promega) and 15U MMLV reverse transcriptase according to the manufacturer&#39;s instructions (Promega). The mRNA template was removed by hydrolysis in 100 mm NaOH at 65° C. for 30 min. The reaction was neutralized in 100 mm Tris-HCl (pH 8.0), and the labeled first-strand cDNA was ethanol precipitated in the presence of 20 μg of carrier yeast tRNA.  
     [0087] Filters were pre-hybridized for 30 min in 1 mM EDTA, 0.25 M phosphate buffer (pH 7.2), 7% (w/v) SDS, and hybridized overnight at 65° C. in the same solution containing the denatured probe (1×10 7  cpm/ml). Hybridized filters were washed twice for 30 min each at 65° C. in Wash Solution One (1 mM EDTA, 40 mM phosphate buffer, pH 7.2, 5 % (w/v) SDS) and three times for 30 min each at 65° C. in Wash Solution Two (1 mM EDTA, 40 mM phosphate buffer pH 7.2, 1 % (w/v) SDS). The air-dried filters were subjected to autoradiography (X-Omat X-ray film, Kodak) for 72 h at −80° C. with an intensifying screen.  
     [0088] Banana pulp cDNA libraries from PCI 1 and PCI 3 were each probed separately and differentially with labeled cDNA from pulp at PCI 1 and PCI 3. Plaques which demonstrated strong differential signal intensities between both probes were selected as positives. Positive plaques were then subjected to secondary screening to purify single isolates by utilizing the same probes as in the primary screening. pBluescript phagemids were excised from the isolated plaques according to the manufacturer&#39;s recommendations (Stratagene).  
     [0089] Sequence Analysis  
     [0090] Small-scale alkaline lysis plasmid preparations followed by phenol:chloroform extraction and ethanol precipitation (Sambrook et al., 1989) yielded template plasmid DNA suitable for automated sequencing. Plasmid DNA templates were sequenced, using the T3 primer, on an ABI 373A DNA sequencer (Applied Biosystems, Foster City, Calif.). Vector and 3′ poly(A) residue sequences were removed from the output sequence. Edited sequences were loaded into the NCBI form for BLAST (9. 1) searching on a network server (www.ncbi.nlm.nih.gov), and searches were performed using the default settings of BLASTN (Altschul et al., 1990). For some cDNA clones, no significant homology (defined as a high score above 100) with sequences in the databases was identified using BLASTN. In that event, the default settings of the BLASTX search, an algorithm that translates the nucleic acid sequence in all six frames and searches a non-redundant amino acid database for matches, were used (Gish and States, 1993).  
     [0091] Dot-blot Hybridization  
     [0092] Comparisons of the relative transcript abundance of the individual cDNA clones between PCI 1, 3 and 5 pulp were made through dot-blot hybridization experiments. Plasmids containing the cDNA inserts were affixed to nylon membrane and hybridized with first-strand cDNA from generated from PCI 1, 3 or 5 pulp RNA. The equivalent of 1×10 11  copies of each plasmid (approximately 0.5 μg of plasmid DNA containing a 1 kb cDNA insert) was heat denatured (95° C. for 10 min), and quenched on ice. Using a vacuum dot-blot apparatus (BioRad), target DNA was applied to HyBond N+ nylon membrane (Amersham). Membranes were air-dried, UV crosslinked (Stratalinker), and hybridized as described above using 2×10 6  cpm/ml of PCI 1, 3, and 5 radiolabeled first strand cDNA as probe. Following hybridization, membranes were exposed to a phosphorescent screen (PhosphorImager, Molecular Dynamics) and the scanned image was analyzed with the ImageQuant quantitation software.  
     [0093] Northern Analyses  
     [0094] Total RNA was isolated from banana pulp and peel at PCI 3, and from root, corm, and leaf tissues of greenhouse-grown Grand Nain banana plants. Ten micrograms of each of the RNA samples were separated by electrophoresis through formaldehyde-containing agarose gels and transferred to Nytran Plus nylon membrane (Schleicher and Schuell) using a vacuum transfer apparatus (BioRad) according to the manufacturer&#39;s recommendations. Equal RNA loading was confirmed by staining the RNA-containing nylon membranes with methylene blue (Sambrook et al. ,1989). The RNA blots were hybridized with a cDNA probe representing the largest isolate from each of the eleven nonredundant groups of clones. DNA probes were synthesized using the Rad-Prime DNA Labeling System (Gibco BRL), and hybridized as described above.  
     Results  
     [0095] Differential screening of approximately 10 5  plaques with labeled pulp cDNAs resulted in the identification of approximately 100 plaques with a signal intensity sufficient to be detected by autoradiography after a 72 hour exposure to X-ray film. It was apparent from the signal intensities observed between differentially hybridized plaque lifts that the relative abundance of a number of transcripts changed between PCI 1 and 3. A total of 38 cDNA clones were isolated from banana pulp libraries by differential screening.  
     [0096] Sequence alignment and homology searches indicate that eleven non-redundant groups of cDNAs were identified (Table 1). Using sequence homology, BLAST searches were able to assign, with high scores between 167 and 1294, a putative identity for all clones. Amino acid sequence homology searches using the BLASTX algorithm were necessary to assign an identity to the clones encoding the putative lectin and senescence-related protein. According to the results of the sequence homology searches, all of the banana sequences are more similar to other plant genes than to genes from other organisms. There were many redundant isolates, especially of the smaller cDNAs such as those encoding the different metallothioneins. Ten clones encoding a putative chitinase, an especially abundant protein in banana pulp (R. López-Gómez, unpublished data), were isolated.  
     [0097] Relative abundance among the different transcripts was estimated by hybridizing isotopically labeled first-strand cDNA to an excess of cloned cDNA which was previously dot-blotted onto nylon membrane. This technique also allowed for the confirmation of differential expression of these transcripts in pulp between PCI 1 and 3, and at a later stage of ripening, PCI 5 (FIG. 1). Relative transcript abundance of starch synthase, GBSS, chitinase, and a type 2 methallothionein decreased in pulp between PCI 1 and 3, and continued to decrease through PCI 5. There was a peak in the abundance of several of the transcripts in PCI 3 pulp, including endochitinase, glucanase, thaumatin, ascorbate peroxidase, and metallothionein. The differential expression of these banana transcripts before and after the peak in ethylene biosynthesis indicates that the transcripts that increase in abundance between PCI 1 and PCI 3 respond to ethylene. The differential expression of the eleven different groups of cDNAs in banana pulp between ripening stages PCI 1 and 3 was confirmed by Northern analyses (data not shown). Results from the dotblot hybridization were also used to estimate relative abundance of each class of cDNA in the pulp of ripening banana fruit, with thaumatin and P-1,3-glucanase being the first and second most abundant transcripts, respectively (FIG. 1).  
               TABLE I                          Genes that are differentially expressed during banana       fruit ripening. Putative cDNA identities are based on       sequence homology. Number of homologous clones isolated       indicated in parentheses. High scores obtained using       BLASTN or BLASTX. Changes in pulp relative transcript       abundance from PCI 1-3 indicated as “up” or       “down” based on dot-blot hybridizations.       Transcript sizes estimated from Northern analyses of       pulp total RNA.                                             PCI   Transcript       Homology to:   Clone   High Score [P(N) a ]   1 to 3   size (kb)                                         sweet potato starch synthase (2)   pBAN 3−33   198 [6.8e−6]   down   2.2       cassava GBSS (4)   pBAN 3-18   1,121 [6.5e−95]   down   2.2       winged bean chitinase (10)   pBAN 3-30   300 [7.9e−31]   down   1.2       rice endochitinase (2)   pBAN 3-24   773 [3.4e−93   up   1.2       soybean β-1,3-glucanase (2)   pBAN 1-3   524 [3.4e−33]   up   1.3       katemfe fruit thaumatin (2)   pBAN 3-28   635 [3.0e−125]   up   1.0       rice ascorbate peroxidase   pBAN 3-25   1,294 [4.0e−110]   up   1. 1       kiwifruit metallothionein (5)   pBAN 3-6   218 [1.7e−11]   up   0.5       castor bean MT type 2 b  (6)   pBAN 3-23   518 [2.4e−33]   down   0.6       jack fruit lection (α subunit) c  (3)   pBAN 3-32   177 [2.0e−19]   down   0.8       asparagus senescence-related gene c     pBAN 3-46   167 [3.1e−16]   up   1.0                          
 
     [0098] Although these cDNAs are relatively abundant in the pulp of banana fruit, their patterns of expression are not limited to these tissues. Northern analyses indicate that starch synthase, GBSS, and chitinase transcripts were abundant in pulp and corm tissues, and present in peel. Expression of the endochitinase, thaumatin-like protein, and β-1,3 glucanase transcripts was limited to the pulp and peel of the fruit. Both classes of metallothionein transcripts were expressed in all tissues analyzed, but were most abundant in the pulp and peel. In comparison, MT was more abundant in leaves than Type-2 MT, while the converse was observed in the corm. Lectin transcripts were most abundant in pulp and root tissues, whereas the ascorbate peroxidase and senescence-related protein transcripts were ubiquitously expressed.  
     [0099] Many of the physiological changes that occur during banana fruit ripening are in response to ethylene produced in the pulp (Don-Tinguez and Vendrell, 1993; Burdon et al., 1994). In addition, ethylene also serves as a signal for other physiological changes including senescence. The cDNA clones identified in this study were isolated by differential screening at stages of fruit ripening corresponding to periods before and after the peak in ethylene biosynthesis (Agravante et al., 1991). Therefore, it is likely that some of the transcripts that increase in abundance between those stages of ripening may be regulated by ethylene, even if they do not have a direct role in the ripening process. The role of ethylene in the regulation of PR proteins (glucanase, chitinase, endochitinase, thaumatin) has been well documented. Ethylene is also believed to influence expression of ascorbate peroxidase (Mehlhorn, 1990) and metallothionein (Coupe et al., 1995)  
     EXAMPLE 2  
     The Abundant 31-Kilodalton Banana Pulp Protein is Homologous to Class-III Acidic Chitinases  
     [0100] The experiments described in this example were designed to identify and characterize the abundant 31 kD protein from the pulp of banana fruit ( Musa acuminata  cv. Grand Nain), and to isolate a cDNA encoding this protein.  
     Materials and Methods  
     [0101] Plant Materials  
     [0102] Ethylene treated and untreated banana fruit ( Musa acuminata  cv. Grand Nain) were obtained from the Northside Banana Company (Houston, Tex.). The pulp and peel of fruit representing each of the seven different stages of ripening (PCI 1 through 7) were separated and quick-frozen in liquid nitrogen. Tissues from ten individual fruit were pooled to obtain a uniform representative sample for each ripening stage and ground to a fine powder under liquid nitrogen in a stainless steel Waring blender. Ground samples were stored at −80° C. until utilized. Other banana tissues were obtained from greenhouse-grown plants (cv Grand Nain).  
     [0103] Protein Isolation for Antiserum Production, N-terminal Sequencing, and Western Blotting  
     [0104] Soluble banana pulp proteins were differentially precipitated from pulp extracts with ammonium sulfate. P31 was most abundant in the 40 to 60% ammonium sulfate fraction, as determined by SDS-PAGE separation (Laemmli, U.K. (1970)  Nature  227:680), followed by Coommassie blue staining (Sambrook et al. (1989)  Molecular Cloning, a Laboratory Manual,  Ed. 2 Cold Spring Harbor Press, Plainview, N.Y.). The 31 kDa protein band was excised from the gel, homogenized and used to immunize a rabbit for antiserum production, according to standard protocols. In addition, proteins from the 40 to 60% ammonium sulfate fraction were separated by SDS-PAGE and transferred PVDF protein sequencing membrane and stained with Coomassie blue. The stained 31 kDa protein band was excised from the membrane and the N-terminal sequence was determined.  
     [0105] Total protein isolated from banana root, corm, leaf, meristem, peel, and pulp at different stages of ripening were separated by SDS-PAGE and electrophoretically transferred to PVDF membrane. The membranes were incubated with the primary antiserum at 1:500 dilution, and the bound antibodies were visualized using chemiluminescence.  
     [0106] Northern Blot Analyses  
     [0107] Total RNA was isolated from banana leaf, corm, root, peel, and floral structures and from banana pulp at PCI 1 through 7 (López-Gómez, R., et al. (1992) 5:440). Agarose gel electrophoresis, and northern blotting and hybridization were performed according to standard protocols (Sambrook et al., supra). The cDNA clone pBAN3-30 was radiolabeled with  32 P-dCTP by random priming and used as a probe.  
     [0108] pBAN3-30 Isolation and Sequence Analysis  
     [0109] pBAN3-30 was isolated from a banana pulp cDNA library by differential screening (Clendennen, S. K. et al. (1997)  Plant Physiology ). The complete sequence of the cDNA insert was determined on both strands, and the open reading frame was translated. Sequence homology of pBAN3-30 and the translation product (P31) were determined using the BLAST search algorithm for searching GenBank (Altschul, S. F., et al. (1990)  J. Molec. Biol.  215:403). For the amino acid alignments, plant chitinase sequences showing significant homology to P31 were downloaded from GenBank and aligned manually.  
     [0110] Expression of Recombinant P31  
     [0111] A total of ten homologous chitinase clones were isolated from the banana pulp cDNA library by differential screening, including pBAN3-30, pBAN3-31, pBAN3-36, and pBAN3-45 (Clendennen et al., supra). These four clones were used for the expression of P31 for western blot analysis of the translation products. It was determined that pBAN3-36 and pBAN3-45 contained chitinase coding sequences that were in-frame with respect to β-galactosidase in the pBluescript cloning vector. All four of the cDNA clones, in  E. coli  XL1-blue host cells, were grown to log phase in selective media and then induced by IPTG. Total bacterial proteins were separated by SDS-PAGE and transferred to PVDF membrane. The western blot was hybridized with P31 antiserum and visualized using chemiluminescence.  
     Results  
     [0112] P31 Isolation and Tissue Distribution  
     [0113] SDS-PAGE analysis of total proteins isolated from pulp of banana fruit at seven ripening stages indicated changes in abundance of several proteins (FIG. 1). The most abundant protein during the pre-climacteric stage (Peel Color Index or PCI 1 and 2) is a 31 kDa protein (P31) which seemed to decrease slightly in abundance as ripening proceeded (FIG. 3). This protein (P31) was partially purified by a combination of ammonium sulfate precipitation and separation by SDS-PAGE. Polyclonal antiserum was raised against the purified protein. The P31 antiserum recognizes a single 31 kDa polypeptide in banana pulp that is not present in banana peel, meristem, corm, or root tissue (FIG. 4). These results indicate that P31 is fruit-specific.  
     [0114] The N-terminus of the partially purified protein was sequenced and the resultant 20-amino acid sequence is: GRNSCIGVYWGQKTDEGSLA (data also appear in FIG. 7). A search of the amino acid sequence databhase (GenBank) revealed that the N-terminus of P31 shares significant homology to amino-terminal peptide sequences from purified acidic chitinases of Mongolian snake-gourd ( Trichosanthes kirilowii;  see Savary et al. (1994)  Plant Physiol.  106:1195) and chick pea ( Cicer arietinum;  see, Vogelsgang, R., et al. (1993)  Planta  189:60).  
     [0115] P31 Expression in Ripening Pulp  
     [0116] P31 expression in banana pulp during ripening was investigated at the protein and transcript levels. Western blot analysis of banana pulp proteins isolated at each of seven chronological stages of ripening (FIG. 5, top panel) indicates that P31 decreases in relative abundance during ripening, consistent with the observations of P31 abundance after separation by SDS-PAGE and staining with Coomassie blue. Using differential screening, several ripening-associated genes were isolated from a banana pulp cDNA library, including clones with significant homology to chitinases (Clendennen et al., supra). For determination of relative chitinase transcript abundance during ripening, total RNA was isolated from banana pulp during ripening, at PCI 1 through 7, and probed with labeled pBAN3-30. Northern blot analysis (FIG. 5, bottom panel) shows that the P31 message is strongly expressed ruing the first few ripening stages (PCI 1 through 3) after which the chitinase transcript declines in banana pulp through the later stages of ripening. This observation is consistent with the result obtained through western analysis. Northern and western blot analysis together suggest that expression of P31 is both fruit-specific and developmentally regulated in banana. While both the P31 protein and the chitinase transcript are abundant during the pre-climacteric stages of fruit ripening (PCI 1 through 3), their relative levels decrease as ripening progresses.  
     [0117] pBAN3-30 Encodes P31  
     [0118] Three lines of evidence lead us to conclude that pBAN3-30 encodes the abundant 31 kDa pulp protein. First, the expression pattern of the pBAN3-30 transcript during ripening matches very closely with the profile of P31 abundance during ripening as determined by western blot analysis using the P31 antiserum, as seen in FIG. 5. Second, the P31 antiserum recognizes the translation product of the chitinase cDNA insert. The translation products of the cDNA clones pBAN3-36 and pBAN3-45, which are homologous to pBAN3-30 but have been determined to be in-frame with respect to the β-galactosidase gene in the pBluescript cloning vector (Stratagene), were expressed as fusion proteins with β-galactosidase. These fusion proteins were analyzed by western blotting and incubation with the P31 antiserum. The P31 antiserum recognizes a 35 kDa polypeptide produced in the IPTG-induced bacterial cells containing an in-frame chitinase cDNA (pBAN3-36 and pBAN3-45) that is not present in cell extracts from bacteria containing only the pBluescript plasmid (no insert) or out-of-frame chitinase cDNA inserts (pBAN3-30 and pBAN3-31) (FIG. 6). Finally, the N-terminal amino acid sequence obtained from the purified protein, which is underlined in FIG. 7, is identical to the deduced amino acid sequence of pBAN3-30 at 17 of 20 residues. This match is improved when the first amino acid residue, which is usually considered to be uncertain, is discounted. Despite the high sequence homology, the amino acid sequence from the partially purified protein is not completely identical to the amino acid sequence deduced from the cDNA clone pBAN3-30. It is possible that a contaminating polypeptide co-migrated with P31 and influenced the amino acid sequence results. Alternatively, it is possible that P31 is encoded by a gene family in banana, members of which are highly homologous, though not identical, and cannot be distinguished from one another by northern or western analyses.  
     [0119] Sequence Analysis of pBAN3-30  
     [0120] The complete nucleotide sequence of pBAN3-30 and the deduced amino acid sequence of the translation product is shown in FIG. 7. The cDNA insert is 1186 bp long and includes the entire chitinase coding region. The ATG beginning at position 55 is likely to be the translation initiation codon because the nucleotide sequence flanking the first ATG codon matches 8 of the 12 bases in the consensus for translation start sites in plants (Joshi, C. P. (1987)  Nucl. Acids Res.  15:6543), whereas the sequences flanking another potential in-frame downstream start site (at position 100) is identical at only 5 of the 12 bases. There is an in-frame termination codon at position 1024 and several putative polyadenlyation signals between positions 1136 and 1148.  
     [0121] The open reading frame spans 323 amino acids from which a translation product of 35,232 Da is predicted. A GenBank search using the full cDNA sequence reveals significant homology between pBAN3-30 and chitinase genes characterized from winged bean ( Psophocarpus tetragonolobus,  M Esaka and T. Teramoto, unpublished), cow pea ( Vigna unguiculata,  L. T. T. Vo et al., unpublished), azuki bean ( Vigna angularis;  see, Ishige, F., et al. (1993)  Plant Cell Physiol.  34:103), maize ( Zea mays;  see, Didierjean, L., et al. (1996)  Planta  199: 1), and chick pea ( Cicer arietinum;  see, Vogelsgang, R., et al. (1993)  Plant Physiol.  103:297). The deduced amino acid sequence of pBAN3-30 encoding P31 in banana shares sequence homology with other plant chitinases, especially with class III acidic chitinases that have been characterized from various dicots. At the amino acid level, the banana acidic chitinase amino acid sequence shows significant homology, 47-53% identity, to acidic chitinases from Arabidopsis thaliana (Samac, D. A., et al. (1990)  Plant Physiol.  93:907), wine grape ( Vitis vinifera,  Busam et al, unpublished), tobacco ( Nicotiana tabacum;  see, Lawton, K. et al. (1992)  Plant Molec. Biol.  19:735), chickpea, sugar beet ( Beta vulgaris;  see, Nielsen, K. K., et al. (1993)  Molec. Plant - Microbe Interact.  6:495), winged bean, and cucumber ( Cucumis sativus;  see, Lawton, K. A. et al. (1994)  Molec. Plant - Microbe Interact.  7:48).  
     [0122] An amino acid sequence alignment of the amino-terminal and carboxy-terminal regions of several plant acid chitinases with P31 from banana appears in FIG. 8. Hydrophilicity analysis of the deduced protein sequence of P31 reveals a hydrophobic region from amino acid 1 to 25 (underlined in FIG.  8 A). This region may represent a signal sequence that would direct targeting to the ER. If this putative signal peptide is removed, the remaining sequence closely matches the N-terminal sequence obtained from the purified protein, which suggests that P31 is post-translationally processed. This signal peptide does not share significant homology with the signal peptide sequences of other plant class III acidic chitinases (see FIG. 8A), which are typically localized to the extracellular space (Punja, Z. K. et al. (1993)  J. Nematol.  25:526; Collinge, D. V., et al. (1993)  Plant J.  3:31; Lawton, K. et al. (1992)  Plant Molec. Biol.  19:735; Graham, L. S., et al. (1994)  Canad. J. Botany  72:1057; Bol, J. F. (1990)  Ann. Rev. Phytopathol.  28:113-138).  
     [0123] In addition to the N-terminal signal peptide, the banana P31 sequence is distinguished from other chitinase sequences by the presence of an 19 amino acid C-terminal extension (underlined in FIG. 8B). C-terminal propeptides (CTPPs) have been identified in a number of monocot and dicot polypeptides that direct proteins to the plant vacuole. Among others, CTPPs have been characterized in vacuolar lectins from barley and rice, and from vacuolar β-1,3-glucanase and chitinase from tobacco (see, Bednarel, S. Y. (1992)  Plant Molec. Biol.  20:133, for review). In general there is little sequence homology among plant vacuolar targeting sequences. However, weak homology can be detected between the C-terminal extension of P31 (SNILSMP) and vacuolar targeting sequences that have been characterized in the sweet potato storage protein sporamin (NPIRLP) (Linthorst, H. J. M. (1991)  Crit. Rev. Plant Sci  10: 123) and in a 2S albumin from Brazil nut (NLSPMRCP) (Saalbach, G. et al. (1996)  Plant Physiol.  112:975).  
     [0124] Based on amino acid sequences, chitinases can be grouped into four classes. Class I includes a majority of chitinases described, possessing an N-terminal cysteine-rich lectin or “hevein” (chitin-binding) domain and a highly conserved catalytic domain. Class II chitinases lack the N-terminal cysteine-rich domain but have a high amino acid sequence identity to the main structure of class I chitinases. Class III chitinases show little sequence similarity to plant enzymes in class I or II, but may in fact be more similar to bacterial chitinases. The majority of class III chitinases are classified as such on the basis of homology to previously described lysozymes with chitinase activity. Class IV chitinases contain a cysteine-rich domain and conserved main structure which resemble those of class I chitinases by are significantly smaller due to four deletions (Punja, Z. K., et al. (1993)  J. Nematol.  25:526; Collinge, D. V., et al. (1993)  Plant J.  3:31; Graham, L. S., et al. (1994)  Canad. J. Botany  72:1057). Although the banana pulp chitinase shares significant sequence homology with other plant class III acidic chitinases, the predicted isoelectric point of P31 is 7.63 (neutral). In addition, studies to determine the chitinase active sites in bacterial chitinases appear to be conserved in plant, bacterial, and fungal sequences (Perlick, A. M., et al. (1996)  Plant Physiol.  110: 147). At least five highly conserved amino acids have been shown to be necessary for chitinase activity, and the deduced amino acid sequence of P31 indicates that only three of the five amino acids necessary for chitinase activity are conserved in banana P31 (not shown) (Watanabe, T., et al. (1993)  J. Biol. Chem.  268:18567; Tsujibo, H., et al. (1993)  Biosci. Biotech. Biochem.  57:1396).  
     [0125] Role of Chitinase in Banana Pulp  
     [0126] In plants, class III chitinases have been reported to be induced in response to various stresses such as pathogenesis and wounding (Ishige, F., et al. (1993)  Plant Cell Physiol.  34:103; Lawton, K., et al. (1992)  Plant Molec. Biol.  19:735; Nielsen, K. K., et al. (1993)  Molec. Plant - Microbe Interact.  6:495; Lawton, K. A., et al. (1994)  Molec. Plant - Microbe Interact.  7:48; Mehta, R. A., et al. (1991)  Plant Cell Physiol.  32:1057). Recently, it has been reported that the expression of several pathogenesis and stress-related proteins, including chitinases, is associated with fruit ripening. Several genes encoding pathogenesis-related proteins such as endochitinase are associated with ripening in banana pulp (Clendennen, S. K., et al. (1997)  Plant Physiol. ). Considering the antifungal activity that they exhibit in other plants, it is possible that chitinases fulfill a protective role during fruit development and ripening. However, in contrast to the ripening-associated PR-proteins studied in cherry, avocado, and tomato, banana P31 decreases in abundance during ripening. Although it is possible that the banana chitinase serves a protective role during fruit development, an alternate hypothesis is that the chitinase in banana pulp has been recruited to serve as a storage protein in this tissue.  
     [0127] Storage proteins are a heterogeneous group of proteins for which no defined assay is available. According to a recent review (Staswick, P. E. (1994)  Ann. Rev. Plant Physiol. Plant Molec. Biol.  45:303), storage proteins generally share the features listed below; we relate traits of P31 to general features of storage proteins.  
     [0128] 1) Storage proteins are very abundant. We have found P31 to be very abundant in unripe banana pulp, accounting for approximately 20 to 30% of total soluble pulp protein. 2) Storage proteins are preferentially degraded during a subsequent developmental stage. For example, a vegetative storage protein characterized from the bark of poplar trees accumulates during fall and winter and is degraded during shoot growth in the spring. P31 is preferentially degraded during banana fruit ripening. Both the transcript and protein abundance decrease during ripening. If P31 is indeed a storage protein in banana pulp, this preferential degradation implies the existence of a protease specific to the storage protein, and inhibition of the protease would inhibit degradation of the storage protein. 3) Storage proteins are generally localized in storage vacuoles within the cell. The sub-cellular localization of P31 has not yet been determined. According to the deduced amino acid sequence of P31, there is a putative signal peptide sequence for P31 that is 25 amino acids long and hydrophobic. In addition, the amino acid sequence of P31 from banana pulp is distinguished from other plat class III acid chitinases by the presence of an 18 amino acid C-terminal extension that shows some homology to previously characterized C-terminal vacuolar targeting signals, suggesting vacuolar localization of P31. 4) Many storage proteins contain a large proportion of amino acid residues with nitrogen-containing R-groups. Amino acid composition analysis of P31 indicates that 22% of residues have N-containing R-groups (Trp, Gln, Asn, Lys, Arg, His). This is approximately the same proportion of N-containing R-group amino acids in vegetative storage proteins from soybean and poplar (21-25%). Interestingly, the N-containing R-group amino acid composition of P31 is not significantly higher than the N-containing R-group content of other plant chitinases (17-23%). 5) Storageproteins typically lack any other metabolic or structural role. However, this is not necessarily true for soybean vegetative storage protein, which has retained a minimal acid phosphatase activity, and patatin, a potato tuber storage protein that exhibits residual lipid acyl hydrolase activity. Preliminary evidence suggests that protein extracts from banana pulp have very low chitinase activity, as measured by soluble chitobiose released from radiolabeled chitin. In addition, only three of the five amino acids which have been determined to be essential for chitinase activity are conserved in P31. Taken together, this evidence lends support to the hypothesis that P31, while sharing sequence homology with plant chitinases, may actually be serving as a storage protein in banana pulp.  
     EXAMPLE 3  
     A Novel Fruit-Associated Class of Metallothionein-Like Proteins from Banana ( Musa acuminata  cv Grand nain): Characterization of the Gene Family and Induction by H 2 O 2    
     [0129] In the experiments described in this Example, the gene family encoding the fruit-associated MTs is characterized, and sequence and functional evidence is provided that at least one member functions as an antioxidant during fruit ripening.  
     Materials and Methods  
     [0130] Plant Materials  
     [0131] Ethylene treated and untreated banana fruit ( Musa acuminata  cv. Grand Nain) were obtained from the Northside Banana Company (Houston, Tex.). The pulp and peel of fruit representing different stages of ripening (PCI 1 and 3) were separated and quick-frozen in liquid nitrogen. Tissues from ten individual fruit were pooled to obtain a uniform representative sample for each ripening stage and ground to a fine powder under liquid nitrogen in a stainless steel Waring blender. Ground samples were stored at −80° C. until utilized. Leaf, corm and root tissue were obtained from greenhouse-grown plants (cv Grand Nain), ground in liquid nitrogen using a mortar and pestle, and stored at −80° C.  
     [0132] RNA Isolation and Northern Blotting  
     [0133] Pre-warmed (65° C.) RNA extraction buffer (1.4% (w/v) SDS, 2% (w/v) polyvinylpyrrolidone, 0.5 M NaCl, 0.1M sodium acetate, 0.05 M EDTA (pH 8.0) 0.1% (v/v) β-mercaptoethanol) was added to previously ground samples of pulp at a ratio of 5 ml buffer per gram of tissue. Samples were homogenized with several short bursts of a tissue homogenizer (Polytron, Brinkman) and incubated at 65° C. for 15 min. Starch and other cell debris were pelleted by centrifugation at 2,400 g for 10 min at room temperature and the supernatant transferred to a disposable polypropylene tube. After the addition of 0.2 vol. of 5 M potassium acetate (pH 4.8), the samples were mixed and incubated on ice for 30 min. The resulting precipitate was pelleted by centrifugation at 20,200 rpm for 10 min at 4° C. in a Sorvall SW28 rotor. The supernatant was transferred to a disposable polypropylene centrifuge tube, and the high-molecular weight RNAs were precipitated by the addition of lithium chloride to a final concentration of 2.5 M and incubation overnight at 4° C.  
     [0134] RNA was extracted from previously frozen ground peel, root, leaf, and corm tissue using CTAB extraction.  
     [0135] Five micrograms of total RNA from root, corm, and leaf tissue of greenhouse-grown plants, and from peel and pulp (PCI 3) were separated by electrophoresis in formaldehyde-containing 2% agarose gels and transferred to nylon membrane (Nytran Plust, Schleicher and Schuell) using 20×SSPE as a transfer buffer and a vacuum transfer apparatus (Bio-Rad). Equal RNA loading was confirmed by staining the RNA on the nylon membranes with methylene blue (Sambrook et al., 1989). RNA blots were prehybridized in 1 mM EDTA, 0.25 M phosphate buffer (pH 7.2), 7% (w/v) SDS, and hybridized overnight at 65° C. in the same solution containing the denatured probe (1×10 7  cpm/ml). Hybridized filters were washed twice for 30 min each at 65° C. in Wash Solution One [1 mM EDTA, 40 mM phosphate buffer (pH 7.2) 5% (w/v) SDS] and three times for 30 min each at 65° C. in Wash Solution Two [1 mM EDTA, 40 mM phosphate buffer (pH 7.2), 1% (w/v) SDS]. The air-dried filters were subjected to autoradiography (X-Omat X-ray film, Kodak) at −80° C. with an intensifying screen. The RNA blots were hybridized with a cDNA probe representing either the MT cDNA clone isolated from library 1 or 3, using the Rad-Prime DNA Labeling System (Gibco BRL) to label the DNA probes.  
     [0136] Genomic DNA Isolation and Southern Blotting  
     [0137] Leaf tissue was ground with a mortar and pestle under liquid nitrogen and added to a tube containing pre-warmed (65° C.) DNA isolation buffer. The mixture was incubated at 65° C. for 30 minutes, then extracted twice with an equal volume of chloroform. After the second extraction, DNA was precipitated from the aqueous phase by the addition of an equal volume of isopropanol, and mixed by gently inverting the tube. DNA was pelleted by centrifugation, washed with 70% ethanol, dried briefly, and resuspended in TE (pH 8.0). DNA samples were treated with RNase, then phenol extracted with TE buffered phenol by rocking gently, chloroform extracted, and precipitated with 2.5 vol ethanol.  
     [0138] For the genomic Southern blots, 15 μg of genomic DNA was digested with restriction endonucleases BamHI, HinDIII, EcoRI, PstI, and SalI (Promega), and restriction fragments were separated by electrophoresis on a 0.7% agarose gel. DNA in the gel was denatured (1.5 M NaCl, 0.5 M NaOH) and neutralized (1.5 M NaCl, 0.5 M Tris, pH 8.0) before being transferred to nylon membrane (S&amp;S Nytran Plus) using a BioRad vacuum transfer apparatus. DNA was covalently crosslinked to membrane by UV irradiation (Stratalinker, Stratagene), and the membrane was hybridized separately with probes corresponding to the MT cDNA clones isolated from the banana pulp cDNA libraries from PCI 1 and 3 (MT-F1 and MT-F3).  
     [0139] Genomic Library Screening and Mapping  
     [0140] Approximately 6×10 5  primary plaques from a  Musa acuminata  cv Grand Nain λ FIX genomic library (Stratagene) were screened with the MT cDNA probe isolated from the PCI pulp cDNA library (MT-F1). Plaque-lifts containing filter-bound λphage DNA was denatured for two min in 1.5 M NaCl, 0.5 M NaOH, and neutralized for four minutes in 1.5 M NaCl, 0.5 M Tris (pH 8.0). Filters were rinsed in 0.5 M Tris (pH 8.0), blotted dry, and the DNA was covalently crosslinked to the filters by UV irradiation (Stratalinker, Stratagene). Plaque-lifts were hybridized as described previously. Twenty-four positives were plaque purified, and λphage DNA was isolated for generating maps of the region containing the MT gene. Southern blot analysis was used to determine the identity of the MT clone according to diagnostic restriction sites. Fragments of the genomic clones containing the coding region and 5′ and 3′ flanking region were subcloned into pBluescript KS, and subclones were mapped and sequenced.  
     [0141] Sequencing and Data Analysis  
     [0142] Small-scale alkaline lysis plasmid preparations followed by phenol:chloroform extraction and ethanol precipitation (Sambrook et al., 1989) yielded template plasmid DNA suitable for automated sequencing. Plasmid DNA templates were sequenced, using the T3 primer, on an ABI 373A DNA sequencer (Applied Biosystems, Foster City, Calif.).  
     [0143] Using the BLASTX search algorithm, it was determined that the banana cDNA clones shared significant sequence homology with MT cDNA clones isolated from other fruit. The deduced amino acid sequences of plant MT cDNA clones were aligned using Clustal. A dendrogram showing the relationship among several different classes of plat MTs was generated from the deduced amino acid sequences using Clustal.  
     [0144] Protoplast Isolation and Dot Blot Analysis of MT Transcript Abundance  
     [0145] Protoplasts from banana pulp at PCI 4 were isolated as described in Khalid et al. (in preparation). 1×10 5  protoplasts were incubated under experimental conditions for 4 h at room temperature in protoplast isolation buffer (Khalid et al. 1997), with gentle rocking to keep the cells suspended. The treatments included incubation with different concentrations of ascorbate (buffered to pH 7.0), CuCl 2 , and hydrogen peroxide from 1 to 100 mM. After the incubation, a crude RNA preparation from the protoplasts was spotted onto nylon membrane in duplicate. One membrane was hybridized to the F3 cDNA probe to determine relative transcript abundance of fruit-associated MT. The second membrane was hybridized with an 18S ribosomal RNA probe to assess RNA loading. The membranes were then exposed to a phosphorescent screen (PhosphorImager, Molecular Dynamics) and the scanned images were quantified with the ImageQuant software. The relative abundance was normalized to the measure of total RNA loaded, and is expressed in arbitrary units.  
     Results  
     [0146] The cDNA sequence of the banana fruit-associated MT clones is shown in FIG. 9. The clones were isolated by differential screening of pulp cDNA libraries (Clendennen and May, 1997). F1 was isolated from the PCI1 library, whereas F3 was isolated from the PCI3 library. The cDNA clones are slightly variable in size, and most of the differences in size and primary sequence occurs in the 3′ untranslated region (UTR), with F1 having approximately 70 more bases than F3. The two banana cDNA sequences are 60% identical at the nucleotide level, and 81% identical within the coding region.  
     [0147] While both of the banana fruit-associated MT polypeptides are 65 amino acids, the two cDNA clones encode distinct polypeptides. The N-terminal and C-terminal domains are well conserved, and separated by a variable spacer. In FIG. 10A, an alignment of deduced amino acid sequences shows the degree of similarity among the different fruit-associated MTs from banana, kiwifruit, papaya, and apple. In panel B, the relationships among a variety of plant MTs is depicted in a dendrogram generated from a cluster together, as do the type 1 MT sequences. The fruit-associated MT sequences (banana, kiwifruit, papaya, and apple) cluster together and are distinct from both type I and type 2 plant MTs.  
     [0148] Despite the sequence similarity, the size difference between the transcripts of the two banana MT cDNA clones allows them to be separated on a high percentage (2%) agarose gel and detected by northern blotting and hybridization separately with each probe (FIG. 11). Transcript sizes of F1 and F3 as determined from northern analysis are approximately 540 and 430 bases, respectively. The larger transcript (F1) is abundant in pulp, peel, and corm. It is also present in low abundance in banana leaves, but is not detected in roots. The smaller transcript (F3) is most abundant in leaves, present in pulp and peel, and barely detectable in root and corm tissue.  
     [0149] Southern analysis using both cDNAs as probes indicates the presence of up to five copies of the fruit type MT—two copies with homology to F1 and three copies with homology to F3 (data not shown). Twenty-four genomic clones of fruit MT were isolated from the genomic library, and restriction maps of the region containing the MT gene indicated that three distinct genes had been isolated. Clones representing both the F1 and F3 cDNA clones were isolated from the genomic library, as well as a gene with homology to the fruit-associated MT F!, but for which no cDNA clone has been isolated (named MT-F1b). Subclones of these different MT genes were generated and the region containing the coding region as well as 5′ and 3′ flanking regions were mapped. Maps of the different MT genes, including the coding region and at least 1 kb of 5′ and 3′ flanking regions appear in FIG. 12. Based on mapping and sequence data it can be determined that the MT F3 gene is comprised of three exons separated by two introns. The mapping resolution was not fine enough to determine the existence or position of introns in the other MT genes. The nucleotide sequence of the F3 genomic clone from the HindIII site to the SalI site, which includes the complete coding region, is depicted in FIG. 13. Several features of the sequence are highlighted in the figure, including a 10-base 5′ sequence motif beginning at −313 from the translation start site (in capital letters) that shares homology with an antioxidant response element. The putative TATA-box (starting at position −96 from the translation start site) is underlined, and the three exons (beginning from the translation start site) are depicted in capital letters. At the 3′ end of the sequence, the stop codon is underlined, as well as a potential polyadenylation signal (TAAATAAA).  
     [0150] Because of the putative ARE identified in the 5′ flanking sequence, the effect of antioxidants (ascorbate), oxidizing agents (H 2 O 2 ), and metal ions (Cu ++ ) on MT transcript abundance was determined in banana pulp protoplasts. H 2 O 2 , but not copper ions, resulted in dramatic and dose-dependent increase in the relative abundance of the fruit-associated MT transcript (FIG. 14). The presence of ascorbate resulted in a reduction in the relative MT transcript abundance as compared to an untreated control.  
     Discussion  
     [0151] Eleven non-redundant groups of ripening-associated cDNA clones were isolated from banana pulp cDNA libraries by differential screening and identified by sequence homology (Clendennen and May, 1997). One of the groups of cDNA clones includes a previously uncharacterized type of metallothionein (MT), the transcript of which is found abundantly in ripening banana pulp. There are two classes of this ripening-associated MT transcript in banana pulp that vary in primary sequence and in size. Both the larger (F1) and the smaller (F3) transcripts increase in abundance in banana pulp during ripening, but F1 increases more dramatically than F3. In addition, the tissue distribution of these transcripts differs: MT-F1 is expressed abundantly in the pulp and peel, and slightly in corm tissue, whereas MT-F3 is expressed abundantly in pulp, peel, and leaves, and very slightly in roots. Based on the isolation of two distinct cDNA clones, it was suspected that the fruit-associated MTs were encoded by a small gene family. Southern analysis confirmed this, and suggested the presence of up to five members of the fruit-associated MT gene family in banana. Three different MT genes were identified after screening twenty-four genomic clones that hybridized to F1 and F3 cDNA probes, as determined by restriction mapping of the segment containing the coding region. Genomic clones representing both cDNA clones were isolated.  
     EXAMPLE 4  
     Demonstration of Functional Banana p31 Promoter-Driven Heterologous Gene Expression in Tomato  
     [0152] In the experiments described in this Example, the p31 promoter is inserted in a plant transformation vector with a reporter gene (β-glucuronidase), which is used to transform tomato plants, providing functional evidence that the p31 promoter derived from banana is capable of driving heterologous gene expression in a dicotyledonous fruiting plant, tomato.  
     Materials and Methods  
     [0153] Banana p31 Promoter Expression Cassette Construction  
     [0154] A 4.85 kb BamHI/SalI banana genomic fragment, containing the entire coding sequence of the banana p31 protein and 2.15 kb of 5′ flanking region containing the putative promoter having nucleotide sequence SEQ ID NO: 44 (SEQ ID NO: 44: GGATCCCAACTTTTAGGAATGGATCTTAAAATTTTAGTTATAAGTT CAAAGTTAGAAAAATCTTTACCAAGAGCTTTGAGTCCATTGATGACATCCGTGA AACGGTGTACATGTCTCCGATGGACTCACTTGGTTTCATTCGGAAAAGTTCGAA AGAGTGCATAAGAATATTGATTTTGGATTCTTTCACTCGGTTGGTGCCTTCATG AGTGACCTCAAGAGTCCTCCAAATATCAAAAGCCGAATCACAAATTGAAATGT GATTGAATTCATTTTTGTCTAATGCACAAAACAGGGCATTCATAGCCTTTGTGT TTAAAGCAAAAACATTCTTCTCCGATTCATCCCATTCGCTCATCGGAAGAGAAA ATTTTTGAAATCCATTTTCGACAATAGACCAAAGCTCGAAATCCATGGAAATGA GGAAGATCCTCATATGAGTTTTCCAATACATGTAATTCGACTCATTAAACATAG GTGGATGTGTAATGAAATGACCCTCATGCSCTATCTCTCTTGGGTATTAAACCA AATATGAGAGTGAGCCTTGCTCTGATACCAATTGTTAGGATCAGAGTGGCACTA AGAGAGGGGGGGAGTGAATTAGTGCAGTGGATTAAAACTTATAAGTTTAAAAA TGAATTCGTAAATACGAGAAGATTTCGTTTTAATAGTAACTTGAGTAGATGAAA ACCAAAAGTTAACAGTAGTGTAAATAACAATTTCGGGAAAGTAAGAACTCACA CATTCAAGGAACATACCAATTTAAAGTGGTTCGGTCAAAATGACCTACATCCAC TTGTGAAGCCTTCTTCGAAGAGGCTCCCAACTTCCACTAGCAAATCACTTTGAA GGGGAAGGACAAATACCTCTCTTACNACCTTTTACAATGGTTCATACTCTTACA AATTTTCAACGAGAAAGAAGGAGGTGAACATGCAAGCAATTGAAAACAAGACT TGCTAAAGACTTTGCTAAGGCTTTTTTTCTCAATCTATTGCTTCTCAAAAGTTGT ATTCTCTGCTGAGAATTGAGGGGTATTTATAGACCCCAAGAGGATTTAAATTTG GGCTCCAAATTTCGAATGCTCTTGGGTTCCCGAGGTTGCCGGTGCCACCGCCTG TCAGTGTTTGACACTGGACAGTGTACTAGCGGTGCCACCGCCGGACCTCTCGGG TGTTGGGCGGTGCCACCGCCTAGACTTTTTCAGCTCACTGGTTGGATTCCAAAC TTGACCCAAACCAGTCCGAACTCGGGTCCAATTGACCCGTAACCGGATTATAGG ATTAACCCTTAATCCTAACCCTAATTATATGCAAACTACGCAACTGAAAATATA GTCCTAAGCAAGTTTTTAACCGGCAAACGTCGAGTCTTCTTCCGGCGATCTTTC GGCAGACTTCTGATATACCTTTGGATTTCTTCTAGCGGACTCCTAGTAGGGTCC CGATCTTGTGGCGAGTTTAGCGAGTAGCCGAACCTTCTCGGTGATCTCCGCAAA CCGCCGATGATCTCTTCGGCAGACTTTCGAAAACTTCGACAAGTCCCCGATTTC TTCTCGGTTGGTTCCGACAGCATCTCTAACGAAACTTCGGACTCCTTGAATGTC CATCGAACTTGACTCCGGTAGGCTTGCTTTATATTTTCAGGCTATCATAGTTAAT CCTACATACTTAACTCAATAATATGGATTAGATTAATTAACCCATCAATTGATT TCATCATCAAAATTCGACATTCAACAAACATCCGTACTCAATAACCCATCAGGC TATAGTTACGTGACTATCTACTGTGATCCGTACGTGAAGTTAGCGAGTCATGAT CCAGGTCGTGTCACTTATTGGCCGAACACGTATCCCTTATCCAAATCCAGTCTT CTCAACTCTTCTAGCCTACCCGTCTCTTTTTTTATTACTTTTGAAAGAATTCAAA TCAAAACAGATACAAAATAACACGGTGAGACACTGTGACATGCTAGTCTCTGG AAAGCATTAATTCGCGCATCCACAGACGTCGTCAGCTTCATCACCCACTTTTTC CTACATACCATGTCGCATGGCTTTGTTGATGACAGACCACCACAAGCTTGCCTT TGGTTGTGCCTAACAGAGAGAGAGAGAGAGACAGACCGATAGCCTCCTCATTC ACTATGG), was subcloned from a Lambda-FIX® II library (Stratagene) into pBluescriptII-SK (Stratagene) to create pBS-31. A NcoI site at position −1741 relative to the start codon was removed by digestion of pBS-31 with NcoI, filling the ends with Klenow enzyme, and religating to form p31!N. A new NcoI site was created spanning the translation start site by PCR with template p31!N and the mutagenic primer p31-Nco (5′-GATCGCCATGGTGAATG) (SEQ ID NO:42) with the M13F primer (5′-GTAAAACGACGGCCAGT) (SEQ ID NO:43), performing 25 cycles of 94° C. for 45 seconds, 46° C. for 45 seconds and 72° C. for 60 seconds. The 2.1 kb product with nucleotide sequence SEQ ID NO: 45 (SEQ ID NO: 45: GGATCCCAACTTTTAGGAATGGATCTTAAAATTTTAGTTATAAGTT CAAAGTTAGAAAAATCTTTACCAAGAGCTTTGAGTCCATTGATGACATCCGTGA AACGGTGTACATGTCTCCGATGGACTCACTTGGTTTCATTCGGAAAAGTTCGAA AGAGTGCATAAGAATATTGATTTTGGATTCTTTCACTCGGTTGGTGCCTTCATG AGTGACCTCAAGAGTCCTCCAAATATCAAAAGCCGAATCACAAATTGAAATGT GATTGAATTCATTTTTGTCTAATGCACAAAACAGGGCATTCATAGCCTTTGTGT TTAAAGCAAAAACATTCTTCTCCGATTCATCCCATTCGCTCATCGGAAGAGAAA ATTTTTGAAATCCATTTTCGACAATAGACCAAAGCTCGAAATCCATGCATGGAA ATGAGGAAGATCCTCATATGAGTTTTCCAATACATGTAATTCGACTCATTAAAC ATAGGTGGATGTGTAATGAAATGACCCTCATGCSCTATCTCTCTTGGGTATTAA ACCAAATATGAGAGTGAGCCTTGCTCTGATACCAATTGTTAGGATCAGAGTGGC ACTAAGAGAGGGGGGGAGTGAATTAGTGCAGTGGATTAAAACTTATAAGTTTA AAAATGAATTCGTAAATACGAGAAGATTTCGTTTTAATAGTAACTTGAGTAGAT GAAAACCAAAAGTTAACAGTAGTGTAAATAACAATTTCGGGAAAGTAAGAACT CACACATTCAAGGAACATACCAATTTAAAGTGGTTCGGTCAAAATGACCTACAT CCACTTGTGAAGCCTTCTTCGAAGAGGCTCCCAACTTCCACTAGCAAATCACTT TGAAGGGGAAGGACAAATACCTCTCTTACNACCTTTTACAATGGTTCATACTCT TACAAATTTTCAACGAGAAAGAAGGAGGTGAACATGCAAGCAATTGAAAACAA GACTTGCTAAAGACTTTGCTAAGGCTTTTTTTCTCAATCTATTGCTTCTCAAAAG TTGTATTCTCTGCTGAGAATTGAGGGGTATTTATAGACCCCAAGAGGATTTAAA TTTGGGCTCCAAATTTCGAATGCTCTTGGGTTCCCGAGGTTGCCGGTGCCACCG CCTGTCAGTGTTTGACACTGGACAGTGTACTAGCGGTGCCACCGCCGGACCTCT CGGGTGTTGGGCGGTGCCACCGCCTAGACTTTTTCAGCTCACTGGTTGGATTCC AAACTTGACCCAAACCAGTCCGAACTCGGGTCCAATTGACCCGTAACCGGATTA TAGGATTAACCCTTAATCCTAACCCTAATTATATGCAAACTACGCAACTGAAAA TATAGTCCTAAGCAAGTTTTTAACCGGCAAACGTCGAGTCTTCTTCCGGCGATC TTTCGGCAGACTTCTGATATACCTTTGGATTTCTTCTAGCGGACTCCTAGTAGGG TCCCGATCTTGTGGCGAGTTTAGCGAGTAGCCGAACCTTCTCGGTGATCTCCGC AAACCGCCGATGATCTCTTCGGCAGACTTTCGAAAACTTCGACAAGTCCCCGAT TTCTTCTCGGTTGGTTCCGACAGCATCTCTAACGAAACTTCGGACTCCTTGAAT GTCCATCGAACTTGACTCCGGTAGGCTTGCTTTATATTTTCAGGCTATCATAGTT AATCCTACATACTTAACTCAATAATATGGATTAGATTAATTAACCCATCAATTG ATTTCATCATCAAAATTCGACATTCAACAAACATCCGTACTCAATAACCCATCA GGCTATAGTTACGTGACTATCTACTGTGATCCGTACGTGAAGTTAGCGAGTCAT GATCCAGGTCGTGTCACTTATTGGCCGAACACGTATCCCTTATCCAAATCCAGT CTTCTCAACTCTTCTAGCCTACCCGTCTCTTTTTTTATTACTTTTGAAAGAATTC AAATCAAAACAGATACAAAATAACACGGTGAGACACTGTGACATGCTAGTCTC TGGAAAGCATTAATTCGCGCATCCACAGACGTCGTCAGCTTCATCACCCACTTT TTCCTACATACCATGTCGCATGGCTTTGTTGATGACAGACCACCACAAGCTTGC CTTTGGTTGTGCCTAACAGAGAGAGAGAGAGAGACAGACCGATAGCCTCCTCA TTCACCATGG) was gel-purified and ligated with T-tailed pBluescriptKS (Stratagene). The T-tailed pBluescriptKS was prepared by digesting the plasmid with EcoRV and treating with Taq polymerase and dTTP at 72° C. for two hours. A clone was selected and named pKS-31Nm, and the sequence surrounding and upstream of the newly created NcoI site was confirmed by DNA sequencing. The 3′ end of the p31 promoter contained in pKS-31Nm was obtained by digestion with PacI and NcoI. This 454 bp fragment of SEQ ID NO: 45 was ligated with the 1874 bp SacI/PacI fragment from p31!N and NcoI/PacI-digested vector pGEM5-zf (Promega) to form pGEM-31N!N.  
     [0155] Since DNA sequencing of the 3′ end of the p31 promoter in pKS-31Nm detected a single “T” insertion 5′ of the HindIII site at position −103 relative to the start codon, only the short fragment HindIII/NcoI was used. An intermediate vector, pKS-31TH, was constructed by ligation of the 2158 bp BamHI/NcoI fragment of pGEM-31N!N with the 956 bp NcoI/EcoRI fragment of pTH210 (Haq, et al. (1995)  Science  268:714-716) and the BamHI/EcoRI-digested vector pBluescriptKS. Ligation of the 448 bp HindIII/Kpn1 fragment of pKS-31TH with the 2089 bp BamHI/HindIII fragment of p31!N and the BamHI/KpnI-digested vector pUC19 resulted in pUC-31TH. This procedure fused the NcoI site created at the start codon via the HindIII site of the p31 promoter to avoid insertion at the aforementioned −103 site.  
     [0156] The p31 promoter was then fused with the reporter gene β-glucuronidase (GUS), the expression of which can be evaluated by histochemical staining in plant tissues (Jefferson, R. A. (1987),  Plant Mol. Biol. Rep.  5:387-405; Jefferson et al. (1987),  EMBO J.  13:3901-3907). The 2026 bp NcoI/PstI fragment of pRTL2-GUS (Carrington and Freed (1990)  J. Virol.  64:1590-1597) containing the GUS coding sequence and the cauliflower mosaic virus (CaMV) 35S RNA 3′ end was ligated with the 2154 bp BamHI/NcoI fragment of pUC-31TH containing the banana p31 promoter and the BamHI/PstI-digested vector pBluescriptKS resulting in vector pKS-31G (FIG. 20).  
     [0157] The p31-GUS expression cassette was inserted into a binary T-DNA vector for use in Agrobacterium-mediated plant transformation. The 2166 bp XbaI/NcoI fragment of pKS-31G containing the p31 promoter and the 2032 bp NcoI/EcoRI fragment of pKS-31G containing the GUS coding sequence and the CaMV 35S RNA 3′ end were ligated with XbaI/EcoRI-digested pGPTV-KAN (Becker et al. (1992)  Plant Mol. Biol.  20:1195-1197) to construct pGPT-31G (FIG. 21). Recombinant clones were confirmed by four separate restriction digests with EcoRI, XbaI, XbaI/NcoI, or BamHI/HindII.  Agrobacterium tumefaciens  LBA4404 was transformed with a positive clone. Transformed Agrobacterium were identified by plasmid preparation and digestion with EcoRI.  
     [0158] Transformation of Tomato and Evaluation of GUS Expression  
     [0159] Tomato ( Lycopersicon esculentum ) variety TA234 was transformed with pGPT-31G by Agrobacterium-mediated transfer of the T-DNA and regeneration of whole plants on medium containing kanamycin. Transgenic lines were evaluated by Northern blot for expression of mRNA encoding NptII, and several lines were selected for transplant to soil and growth in the greenhouse. Fruits of mature transgenic and control plants were assayed for GUS activity by the histochemical staining method (Jefferson, R. A. (1987),  Plant Mol. Biol. Rep.  5:387-405; Jefferson et al. (1987),  EMBO J.  13:3901-3907).  
     Results  
     [0160]FIG. 22 indicates that the expression of GUS is predominantly in the vascular and placental tissues in transgenic fruit, while no staining is observed in nontransgenic fruit. Although other additional tissues were subjected to staining, no GUS activity was observed in leaf, petiole, or stem tissues (data not shown). Thus, these data demonstrate that the p31 promoter derived from banana can drive fruit-specific heterologous gene expression in tomato. Further, these data provide support that monocot-derived (e.g. banana) promoters can be used to drive gene expression in dicots (e.g. tomato).  
     [0161] While the invention has been described and illustrated herein by references to various specific material, procedures and examples, it is understood that the invention is not restricted to the particular material, combinations of material, and procedures selected for that purpose. Numerous variations of such details can be implied and will be appreciated by those skilled in the art.  
 
    
     
       
         0 
         
           
               
            
               
                   
               
               
                   
               
               
                   
               
               
                                                SEQUENCE LISTING  
               
               
                   
               
               
                   
               
               
                 &lt;160&gt; NUMBER OF SEQ ID NOS: 45  
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 1  
               
               
                 &lt;211&gt; LENGTH: 1186  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: CDS  
               
               
                 &lt;222&gt; LOCATION: (55)...(1026)  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 1  
               
               
                   
               
               
                 tttggttgtg cctaacagag agagagagac agaccgatag cctcctcatt cact atg       57  
               
               
                                                                             Met  
               
               
                                                                              1  
               
               
                   
               
               
                 gcg atc cga tcg cca gct tcg ctg ctg tta ttt gcg ttc ctg atg ctt      105  
               
               
                 Ala Ile Arg Ser Pro Ala Ser Leu Leu Leu Phe Ala Phe Leu Met Leu  
               
               
                              5                   10                  15  
               
               
                   
               
               
                 gcg ctc acg gga aga ctg cag gcc cgg cgc agc tca tgc att ggc gtc      153  
               
               
                 Ala Leu Thr Gly Arg Leu Gln Ala Arg Arg Ser Ser Cys Ile Gly Val  
               
               
                          20                  25                  30  
               
               
                   
               
               
                 tac tgg gga caa aac acc gac gag gga agc tta gca gat gct tgt gcc      201  
               
               
                 Tyr Trp Gly Gln Asn Thr Asp Glu Gly Ser Leu Ala Asp Ala Cys Ala  
               
               
                      35                  40                  45  
               
               
                   
               
               
                 aca ggc aac tac gaa tac gtg aac atc gcc acc ctt ttc aag ttt ggc      249  
               
               
                 Thr Gly Asn Tyr Glu Tyr Val Asn Ile Ala Thr Leu Phe Lys Phe Gly  
               
               
                  50                  55                  60                  65  
               
               
                   
               
               
                 atg ggc caa act cca gag atc aac ctc gcc ggc cac tgt gac cct cgg      297  
               
               
                 Met Gly Gln Thr Pro Glu Ile Asn Leu Ala Gly His Cys Asp Pro Arg  
               
               
                                  70                  75                  80  
               
               
                   
               
               
                 aac aac ggc tgc gcg cgc ttg agc agc gaa atc cag tcc tgc cag gag      345  
               
               
                 Asn Asn Gly Cys Ala Arg Leu Ser Ser Glu Ile Gln Ser Cys Gln Glu  
               
               
                              85                  90                  95  
               
               
                   
               
               
                 cgt ggc gtc aag gtg atg ctc tcc atc gga ggt ggc ggg tct tat ggc      393  
               
               
                 Arg Gly Val Lys Val Met Leu Ser Ile Gly Gly Gly Gly Ser Tyr Gly  
               
               
                         100                 105                 110  
               
               
                   
               
               
                 ctg agt tcc acc gaa gac gcc aag gac gta gcg tca tac ctc tgg cac      441  
               
               
                 Leu Ser Ser Thr Glu Asp Ala Lys Asp Val Ala Ser Tyr Leu Trp His  
               
               
                     115                 120                 125  
               
               
                   
               
               
                 agt ttc ttg ggt ggt tct gct gct cgc tac tcg aga ccc ctc ggg gat      489  
               
               
                 Ser Phe Leu Gly Gly Ser Ala Ala Arg Tyr Ser Arg Pro Leu Gly Asp  
               
               
                 130                 135                 140                 145  
               
               
                   
               
               
                 gcg gtt ctg gat ggc ata gac ttc aac atc gcc gga ggg agc aca gaa      537  
               
               
                 Ala Val Leu Asp Gly Ile Asp Phe Asn Ile Ala Gly Gly Ser Thr Glu  
               
               
                                 150                 155                 160  
               
               
                   
               
               
                 cac tat gat gaa ctt gcc gct ttc ctc aag gcc tac aac gag cag gag      585  
               
               
                 His Tyr Asp Glu Leu Ala Ala Phe Leu Lys Ala Tyr Asn Glu Gln Glu  
               
               
                             165                 170                 175  
               
               
                   
               
               
                 gcc gga acg aag aaa gtt cac ttg agt gct cgt ccg cag tgt cct ttc      633  
               
               
                 Ala Gly Thr Lys Lys Val His Leu Ser Ala Arg Pro Gln Cys Pro Phe  
               
               
                         180                 185                 190  
               
               
                   
               
               
                 ccg gat tac tgg ctt ggc aac gca ctc aga aca gat ctc ttc gac ttc      681  
               
               
                 Pro Asp Tyr Trp Leu Gly Asn Ala Leu Arg Thr Asp Leu Phe Asp Phe  
               
               
                     195                 200                 205  
               
               
                   
               
               
                 gtg tgg gtg cag ttc ttc aac aac cct tcg tgc cat ttc tcc cag aac      729  
               
               
                 Val Trp Val Gln Phe Phe Asn Asn Pro Ser Cys His Phe Ser Gln Asn  
               
               
                 210                 215                 220                 225  
               
               
                   
               
               
                 gct atc aat ctt gca aat gcg ttc aac aat tgg gtc atg tcc atc cct      777  
               
               
                 Ala Ile Asn Leu Ala Asn Ala Phe Asn Asn Trp Val Met Ser Ile Pro  
               
               
                                 230                 235                 240  
               
               
                   
               
               
                 gcg caa aag ctg ttc ctt ggg ctt cct gct gct cct gag gct gct cca      825  
               
               
                 Ala Gln Lys Leu Phe Leu Gly Leu Pro Ala Ala Pro Glu Ala Ala Pro  
               
               
                             245                 250                 255  
               
               
                   
               
               
                 act ggt ggc tac att cca ccc cat gat ctc ata tct aaa gtt ctt ccg      873  
               
               
                 Thr Gly Gly Tyr Ile Pro Pro His Asp Leu Ile Ser Lys Val Leu Pro  
               
               
                         260                 265                 270  
               
               
                   
               
               
                 atc cta aag gat tcc gac aag tac gca gga atc atg ctg tgg act aga      921  
               
               
                 Ile Leu Lys Asp Ser Asp Lys Tyr Ala Gly Ile Met Leu Trp Thr Arg  
               
               
                     275                 280                 285  
               
               
                   
               
               
                 tac cac gac aga aac tcc ggc tac agt tct caa gtc aag tcc cac gtg      969  
               
               
                 Tyr His Asp Arg Asn Ser Gly Tyr Ser Ser Gln Val Lys Ser His Val  
               
               
                 290                 295                 300                 305  
               
               
                   
               
               
                 tgt cca gcg cgt cgg ttc tcc aac atc tta tct atg ccg gtg aag tct     1017  
               
               
                 Cys Pro Ala Arg Arg Phe Ser Asn Ile Leu Ser Met Pro Val Lys Ser  
               
               
                                 310                 315                 320  
               
               
                   
               
               
                 tcc aag taa acctgaacgg cgtagatgat cggtggtcga aaactccgat             1066  
               
               
                 Ser Lys  *  
               
               
                   
               
               
                 catcatgggt ccccatccgt atccgtgcgt tgctacgtta tggtgtttcc cttgtatgtt   1126  
               
               
                   
               
               
                 ggtcttttca ataatataat aaggggttag ttttacgttt ccaaaaaaaa aaaaaaaaaa   1186  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 2  
               
               
                 &lt;211&gt; LENGTH: 323  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 2  
               
               
                   
               
               
                 Met Ala Ile Arg Ser Pro Ala Ser Leu Leu Leu Phe Ala Phe Leu Met  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Ala Leu Thr Gly Arg Leu Gln Ala Arg Arg Ser Ser Cys Ile Gly  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Val Tyr Trp Gly Gln Asn Thr Asp Glu Gly Ser Leu Ala Asp Ala Cys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ala Thr Gly Asn Tyr Glu Tyr Val Asn Ile Ala Thr Leu Phe Lys Phe  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Gly Met Gly Gln Thr Pro Glu Ile Asn Leu Ala Gly His Cys Asp Pro  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Arg Asn Asn Gly Cys Ala Arg Leu Ser Ser Glu Ile Gln Ser Cys Gln  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Glu Arg Gly Val Lys Val Met Leu Ser Ile Gly Gly Gly Gly Ser Tyr  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Gly Leu Ser Ser Thr Glu Asp Ala Lys Asp Val Ala Ser Tyr Leu Trp  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 His Ser Phe Leu Gly Gly Ser Ala Ala Arg Tyr Ser Arg Pro Leu Gly  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Asp Ala Val Leu Asp Gly Ile Asp Phe Asn Ile Ala Gly Gly Ser Thr  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Glu His Tyr Asp Glu Leu Ala Ala Phe Leu Lys Ala Tyr Asn Glu Gln  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Glu Ala Gly Thr Lys Lys Val His Leu Ser Ala Arg Pro Gln Cys Pro  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Phe Pro Asp Tyr Trp Leu Gly Asn Ala Leu Arg Thr Asp Leu Phe Asp  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Phe Val Trp Val Gln Phe Phe Asn Asn Pro Ser Cys His Phe Ser Gln  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Asn Ala Ile Asn Leu Ala Asn Ala Phe Asn Asn Trp Val Met Ser Ile  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Pro Ala Gln Lys Leu Phe Leu Gly Leu Pro Ala Ala Pro Glu Ala Ala  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Pro Thr Gly Gly Tyr Ile Pro Pro His Asp Leu Ile Ser Lys Val Leu  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Pro Ile Leu Lys Asp Ser Asp Lys Tyr Ala Gly Ile Met Leu Trp Thr  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Arg Tyr His Asp Arg Asn Ser Gly Tyr Ser Ser Gln Val Lys Ser His  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Val Cys Pro Ala Arg Arg Phe Ser Asn Ile Leu Ser Met Pro Val Lys  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Ser Ser Lys  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 3  
               
               
                 &lt;211&gt; LENGTH: 90  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 3  
               
               
                   
               
               
                 Met Ala Ile Arg Ser Pro Ala Ser Leu Leu Leu Phe Ala Phe Leu Met  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Ala Leu Thr Gly Arg Leu Gln Ala Arg Arg Ser Ser Cys Ile Gly  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Val Tyr Trp Gly Gln Asn Thr Asp Glu Gly Ser Leu Ser Asp Lys Tyr  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ala Gly Ile Met Leu Trp Thr Arg Tyr His Asp Arg Asn Ser Gly Tyr  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Ser Ser Gln Val Lys Ser His Val Cys Pro Ala Arg Arg Phe Ser Asn  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ile Leu Ser Met Pro Val Lys Ser Ser Lys  
               
               
                                 85                  90  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 4  
               
               
                 &lt;211&gt; LENGTH: 67  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 4  
               
               
                   
               
               
                 Met Glu Lys Cys Phe Asn Ile Ile Pro Ser Leu Leu Leu Ile Ser Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Ile Lys Ser Ser Asn Ala Ala Gly Ile Ala Val Tyr Trp Gly Gln  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Asn Gly Asn Glu Gly Ser Leu Ser Pro Lys Tyr Gly Gly Val Met Ile  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Trp Asp Arg Phe Asn Asp Ala Gln Ser Gly Tyr Ser Asn Ala Ile Lys  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Gly Ser Val  
               
               
                 65  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 5  
               
               
                 &lt;211&gt; LENGTH: 69  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 5  
               
               
                   
               
               
                 Met Ala Arg Thr Pro Gln Ser Thr Pro Leu Leu Ile Ser Leu Ser Val  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Ala Leu Ile Lys Thr Ser Tyr Ala Gly Gly Ile Ala Ile Tyr Trp  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Gly Gln Asn Gly Asn Glu Gly Thr Leu Ser Pro Lys Tyr Gly Gly Val  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Met Ile Trp Ser Lys Phe Tyr Asp Asp Gln Ser Gly Tyr Ser Asn Ser  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Ile Lys Gly Ser Val  
               
               
                 65  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 6  
               
               
                 &lt;211&gt; LENGTH: 73  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 6  
               
               
                   
               
               
                 Met Thr Asn Met Thr Leu Arg Lys His Val Ile Tyr Pro Leu Leu Phe  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ile Ser Cys Ser Leu Ser Lys Pro Ser Asp Ala Ser Arg Gly Gly Ile  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Ala Ile Tyr Trp Gly Gln Asn Gly Asn Glu Gly Asn Leu Ser Arg Lys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Tyr Gly Gly Val Met Ile Trp Ser Lys Phe Trp Asp Asp Lys Asn Gly  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Tyr Ser Asn Ser Ile Leu Ala Ser Val  
               
               
                 65                  70  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 7  
               
               
                 &lt;211&gt; LENGTH: 64  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 7  
               
               
                   
               
               
                 Met Ile Lys Tyr Ser Pro Leu Leu Thr Ala Ser Val Ser Phe Leu Lys  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ala Leu Lys Leu Glu Ala Gly Asp Ile Val Ile Tyr Trp Gly Gln Asn  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Gly Asn Glu Gly Asn Leu Ser Pro Lys Tyr Gly Gly Val Met Ile Trp  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ser Lys Phe Tyr Asp Asn Gly Tyr Ser Asn Ala Ile Leu Ala Asn Val  
               
               
                     50                  55                  60  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 8  
               
               
                 &lt;211&gt; LENGTH: 67  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 8  
               
               
                   
               
               
                 Met Ala Ala Lys Ile Val Ser Val Leu Phe Leu Ile Ser Ser Leu Ile  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Phe Ala Ser Phe Glu Ser Ser His Gly Gly Gln Ile Val Ile Tyr Trp  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Gly Gln Asn Gly Asn Glu Gly Asn Leu Ser Ala Lys Tyr Gly Gly Val  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Met Ile Trp Ser Lys Ala Tyr Asp Asn Gly Tyr Ser Asn Ala Ile Leu  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Ala Ser Val  
               
               
                 65  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 9  
               
               
                 &lt;211&gt; LENGTH: 496  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 163, 387, 471  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 9  
               
               
                   
               
               
                 ggcacgagta catcctctgc ttcttcgagc cttttcgcct tccttcctcg tctaaccatg     60  
               
               
                   
               
               
                 tcgacctgcg gcaactgcga ctgcgttgac aagagccagt gcgtgaagaa gggaaacagc    120  
               
               
                   
               
               
                 tacggtatcg atattgttga gaccgagaag agctacgtcg acnaggtgat cgttgccgca    180  
               
               
                   
               
               
                 gaagctgccg agcatgacgg caagtgcaag tgcggcgccg cctgcgcctg caccgactgc    240  
               
               
                   
               
               
                 aagtgtggca actgagaagc acttgtgtca ctaccactaa ataaaagttt gcaatgcata    300  
               
               
                   
               
               
                 aaaaacaaaa gaacaaaaaa aaaaaaggaa gaagaagaag gtgtggctat gtactctaat    360  
               
               
                   
               
               
                 aattcgggca ggctgatagg ttgtaanatg ggataacgca gtatcatctg tgttatctct    420  
               
               
                   
               
               
                 gtcctgtgtt tacaactctc ctatctatcc tagtccatga aatattatta ntattaaaaa    480  
               
               
                   
               
               
                 aaaaaaaaaa aaaaaa                                                    496  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 10  
               
               
                 &lt;211&gt; LENGTH: 416  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 10  
               
               
                   
               
               
                 ggcacgaggg cacgaggttg cctctcgaca tgtcgacctg cggcaactgc gactgcgctg     60  
               
               
                   
               
               
                 acaagagcca gtgcgtgaag aagggaaaca gctacgctac cgagactgtt gcgaccgaga    120  
               
               
                   
               
               
                 agagcttctt ggatggtgta gtcgatgccc cagcagccgc cgagacggag ggagactgca    180  
               
               
                   
               
               
                 agtgtggtcc ttcctgcgcc tgtgttgact gccaatgtgg ccagtgacag cttcttagct    240  
               
               
                   
               
               
                 agtaatgaca atatataata tgttcgagta aataacttgg ggcttgcatg gctaatcgtt    300  
               
               
                   
               
               
                 tatcagtgtg tcatgatgtc agatgggata gggttgtgtc taccttgtct acatctgtac    360  
               
               
                   
               
               
                 tgttatcata catgataaat aaagaattat tagtattaaa aaaaaaaaaa aaaaaa        416  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 11  
               
               
                 &lt;211&gt; LENGTH: 65  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 11  
               
               
                   
               
               
                 Met Ser Thr Cys Gly Asn Cys Asp Cys Val Asp Lys Ser Gln Cys Val  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Lys Lys Gly Asn Ser Tyr Gly Ile Asp Ile Val Glu Thr Glu Lys Ser  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Tyr Val Asp Glu Val Ile Val Ala Ala Glu Ala Ala Glu His Asp Gly  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Lys Cys Lys Cys Gly Ala Ala Cys Ala Cys Thr Asp Cys Lys Cys Gly  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Asn  
               
               
                 65  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 12  
               
               
                 &lt;211&gt; LENGTH: 67  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 12  
               
               
                   
               
               
                 Met Ser Thr Cys Gly Asn Cys Asp Cys Ala Asp Lys Ser Gln Cys Val  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Lys Lys Gly Asn Ser Tyr Ala Thr Glu Thr Val Ala Thr Glu Lys Ser  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Phe Leu Asp Gly Val Val Asp Ala Pro Ala Ala Ala Glu Thr Glu Gly  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Asp Cys Lys Cys Gly Pro Ser Cys Ala Cys Val Asp Cys Lys Gln Cys  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Gly Asn Gln  
               
               
                 65  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 13  
               
               
                 &lt;211&gt; LENGTH: 63  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 13  
               
               
                   
               
               
                 Met Ser Asp Lys Cys Gly Asn Cys Asp Cys Ala Asp Ser Ser Gln Cys  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Val Lys Lys Gly Asn Ser Thr Glu Thr Val Ala Thr Asp Lys Ser Phe  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Ile Glu Asp Val Val Met Gly Val Pro Ala Ala Glu Ser Gly Gly Asp  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Cys Lys Cys Gly Thr Ser Cys Pro Cys Val Asn Cys Thr Cys Asp  
               
               
                     50                  55                  60  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 14  
               
               
                 &lt;211&gt; LENGTH: 66  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 14  
               
               
                   
               
               
                 Met Ser Gly Lys Cys Asp Asn Cys Asp Cys Ala Asp Ser Thr Gln Cys  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Val Lys Lys Gly Asn Ser Tyr Asp Leu Val Thr Val Ala Thr Asp Asn  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Arg Ser Met Glu Thr Val Phe Met Asp Val Pro Ala Ala Glu Ser Gly  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Gly Asp Cys Lys Cys Gly Thr Gly Cys Ser Cys Val Ser Cys Thr Cys  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Asp His  
               
               
                 65  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 15  
               
               
                 &lt;211&gt; LENGTH: 65  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 15  
               
               
                   
               
               
                 Met Ser Asp Lys Cys Asp Asn Cys Asp Cys Ala Asp Ser Thr Gln Cys  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Val Lys Lys Gly Ser Ser Tyr Thr Ala Val Thr Ile Ala Thr Asp Asn  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Arg Ile Met Thr Val Val Met Asp Val Pro Ala Ala Glu Asn Gly Gly  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Asp Cys Lys Cys Gly Pro Ser Cys Ser Cys Val Asn Cys Thr Cys Asp  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 His  
               
               
                 65  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 16  
               
               
                 &lt;211&gt; LENGTH: 1423  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 16  
               
               
                   
               
               
                 taagcttccg tgccaaagcg gtctgccttt ctacgccgca tcgggaaggg gaaacacaaa     60  
               
               
                   
               
               
                 aaaaagatca ggaagatgat gctgacacga gaggtggaag gaagtttacc gctctcccat    120  
               
               
                   
               
               
                 aatagagatt cctttggatg cttctcccgg tgggtgtgtg gagcacagac actgaatgtg    180  
               
               
                   
               
               
                 gtccgtcgtt ccaatccctc acgtaatcgg gccgtctccg gctataaata accccccccg    240  
               
               
                   
               
               
                 accgagcgaa cgcttctaac caggaacgca taccacacca caatttgttg agccgttgtg    300  
               
               
                   
               
               
                 cttgttgcct ctcgacatgt cgacctgcgg caactgcgac tgcgctgaca agagccagtg    360  
               
               
                   
               
               
                 cgtgtaagtt ctcttcctcc ccgccctccc acctctttgt gatacacaca acaaatatgc    420  
               
               
                   
               
               
                 atgagggttg agtttaatat tgaccacaag aacttgggtt tgctcctgca ggaagaaggg    480  
               
               
                   
               
               
                 aaacagctac gctaccgaga ctgttgcgac cgagaagagg tattattgat ctctctcatg    540  
               
               
                   
               
               
                 ggtgagggtg tgggagtatc ttgtccgcat gatgaaattc cacaacatga tgactcagca    600  
               
               
                   
               
               
                 aacaagatcc ttttattctt gagaaaacaa ctaaaagaag aaaaaaaaaa cagagaatat    660  
               
               
                   
               
               
                 atctgcgatt atttcttttt gagtgatgtg gaattccatg ccatagctta aaactatttt    720  
               
               
                   
               
               
                 cgaagtcgaa gcatattaca tacctcttga tgaattagta aggatgatta aaagtaagcc    780  
               
               
                   
               
               
                 atctaaagca gagtaactac ttacgtttct ttcatgtcat ctctgtctta cagcttcttg    840  
               
               
                   
               
               
                 gatggtgtag tcgatgcccc agcagccgcc gaaacggagg gagactgcaa gtgtggtcct    900  
               
               
                   
               
               
                 tcctgcgcct gtgttgactg ccaatgtggc cagtgacagc ttcttagcta gtaatgacaa    960  
               
               
                   
               
               
                 tatataatat gttcgagtaa ataacttggg gcttgcatgg ctaatcgttt atcagtgtgt   1020  
               
               
                   
               
               
                 catgatgtca gatgggatag ggttgtgtct accttgtcta catctgtact gttatcatac   1080  
               
               
                   
               
               
                 atgataaata aagaattatt agtattaatt tggtttcagg tgataactac tgctcctttc   1140  
               
               
                   
               
               
                 aaccgaatca ctactgttac gtgaacaaac atgtaatagt agtgattcag taggacgact   1200  
               
               
                   
               
               
                 tttgtctatt taacttttgc tttgggttgc aaaaatatgt tcttcctgat tcacgaaaga   1260  
               
               
                   
               
               
                 gggtgtccat gagcattcgg ctattgagcg atgttggatg aggcctcaaa gggaagaatt   1320  
               
               
                   
               
               
                 tatgcttagg actctgagtt cgatggttgc caccgacctc ctcaagtacc aagacacata   1380  
               
               
                   
               
               
                 cccttccttc cgaggcctat ccaacatcgc tcgtatcgtc gac                     1423  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 17  
               
               
                 &lt;211&gt; LENGTH: 3559  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: (1)...(3559)  
               
               
                 &lt;223&gt; OTHER INFORMATION: Complement  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 17  
               
               
                   
               
               
                 attggaccca cgcggtggcg gccgctctag aatagtggat cccccgggct gcaggaattc     60  
               
               
                   
               
               
                 taaaatctat tcttttttat tttattaatt aaattaaatt aattttttat tgtttggtat    120  
               
               
                   
               
               
                 ttagcctaac attcccggac tcctctattt ttggagattg aatacaaaat tcttctccca    180  
               
               
                   
               
               
                 tctaaagtta ttttaatttt gaagatcata tggctgacat ataaagcaaa tatgtcaaag    240  
               
               
                   
               
               
                 gtagttttca ccgtccacac gatagaaaca acaaagtagg gtaattaaat ttgttccgtc    300  
               
               
                   
               
               
                 atcacaaagc acaacaccaa aatattcact taatcaaatc ctcactataa ataataatcc    360  
               
               
                   
               
               
                 ttcaaactgc aactctaaac aatgaggttc tctctcccag caacgttctt ttctgaacac    420  
               
               
                   
               
               
                 aaagatttgc cacaacctta gctgactttt aatatcagtg gtctctggac aagattcttg    480  
               
               
                   
               
               
                 ttgcacgcta aaattcgaac taaaatcaga tcgagttata tccgtaattg agattgatga    540  
               
               
                   
               
               
                 ccgaaccgat tttaagagta ctctccgtaa cttgggatta ataaaattaa taaggtaggt    600  
               
               
                   
               
               
                 atcagttatt ttagatgata aaaatcttga tagtttgaat ctcatcttag tcacttattt    660  
               
               
                   
               
               
                 ttaattaaaa ataataataa taatttgatt aatctgattg gaaaaaaaaa aagttctcta    720  
               
               
                   
               
               
                 gccattaaag tctggtagga catagaaatt aatgaattaa actgtaacca taaggttgaa    780  
               
               
                   
               
               
                 tttttgaaca catgtacagg aaaattgatt tgttgaagtc atgtctaatc aatgcagcag    840  
               
               
                   
               
               
                 tttacagctt ggtgtgactt ccacaactat aggcttatcc cctgggagtc gaggatcaaa    900  
               
               
                   
               
               
                 cgtgtgagca atattctccc ttcctgatga taaactatga tggctgttag gtgtgtaagc    960  
               
               
                   
               
               
                 actccaaatt ttccatcaat gtggaattgg aagagttcac gcactgacgg accaactcgg   1020  
               
               
                   
               
               
                 tttgttcagt ctggtgacta ctgctgagca tgagaaaatg gttgatggta gcaagttgca   1080  
               
               
                   
               
               
                 aatgtacctg acctcatctt aaagactgtt gattagatgc atgcattgat tacgtctctt   1140  
               
               
                   
               
               
                 ccatctttaa ctcttttgat cgatgcatcg tcttaattag gtcaaggaca tgtgatgaca   1200  
               
               
                   
               
               
                 agaatctatt ccactatttg tgacccatat tccaaatgga acaagacttc caagtcctca   1260  
               
               
                   
               
               
                 tccagaattt tggaagggat aaggatggtg gggagaaaga acaagctgtt gcctttcgtt   1320  
               
               
                   
               
               
                 ttcttctatc aggaagccaa gagtttcaag aggagggtag acctgagggg atgatgcctg   1380  
               
               
                   
               
               
                 tgtcgaaacc tctatataag gagtaggaac acagcatgtt gatgaacaca aaccatttca   1440  
               
               
                   
               
               
                 gcggggaaga agagaaccct tttgacagag ttgttgtcat ggcaacaaaa gcttctctct   1500  
               
               
                   
               
               
                 ccataaaagg ctttgccttg ctggtttcag tccttgtagc agttccaaca agttctctct   1560  
               
               
                   
               
               
                 ctctctctct ctctctctct ctctctctct ctctctctct ctcatattat acatttgatt   1620  
               
               
                   
               
               
                 gttagctctt acaaatttat tagggttttt ataagagttc aagcttttgg taatttaatc   1680  
               
               
                   
               
               
                 atggtaggtt atattttcaa aacttgtaac ctgcattttg tctctttatt tcatgcaata   1740  
               
               
                   
               
               
                 ttcttttcct tgattggctt acgtcattta cttgagttag ctcatatgta actgtttaaa   1800  
               
               
                   
               
               
                 tatttgggat tattggttaa cggataaaaa aaattaattg attttagata caatgctata   1860  
               
               
                   
               
               
                 tatatatata tatatatata tatatatata tatatatata tatatatata ttataggtag   1920  
               
               
                   
               
               
                 aaacttggta taattcacac gtatgttcgc tttatctgaa taaaatgagt agtcctttca   1980  
               
               
                   
               
               
                 atgcagatta gtcttactcc acttgcagat gcacgaccaa tttgcttgat catcttccat   2040  
               
               
                   
               
               
                 agagcaccac agctaagtct ccgatgtgtt ctactgcagg agtgcaatcg attggtgtct   2100  
               
               
                   
               
               
                 gctacggaat gctcggcaac aatcttcccc cgcccagcga ggtggtcagt ctctacaaat   2160  
               
               
                   
               
               
                 ccaacaacat cgcgaggatg agactctacg atccaaacca ggccgccctg caagccctca   2220  
               
               
                   
               
               
                 ggaactccaa catccaagtc ctgttggatg tcccccgatc cgacgtgcag tcactggcct   2280  
               
               
                   
               
               
                 ccaatccttc ggccgccggc gactggatcc ggaggaacgt cgtcgcctac tggcccagcg   2340  
               
               
                   
               
               
                 tctcctttcg atacatagct gtcggaaacg agctgatccc cggatcggat ctggcgcagt   2400  
               
               
                   
               
               
                 acatcctccc cgccatgcgc aacatctaca atgctttgtc ctcggctggc ctgcaaaacc   2460  
               
               
                   
               
               
                 agatcaaggt ctcgaccgcg gtcgacacgg gcgtcctcgg cacgtcctac cctccctccg   2520  
               
               
                   
               
               
                 ccggcgcctt ctcctccgcc gcccaggcgt acctgagccc catcgtgcag ttcttggcga   2580  
               
               
                   
               
               
                 gtaacggagc gccgctcctg gtcaatgtgt acccttattt tagctacacc ggcaacccgg   2640  
               
               
                   
               
               
                 gacagatctc gctgccctac gccctgttca cggcctccgg cgtcgtcgtg caggatgggc   2700  
               
               
                   
               
               
                 gattcagcta tcagaacctg ttcgacgcca tcgtcgacgc ggtcttcgcg gcgctggaga   2760  
               
               
                   
               
               
                 gagtgggagg ggcgaacgtg gcggtggtgg tgtcggagag cgggtggccg tcggcgggcg   2820  
               
               
                   
               
               
                 gaggagccga agcgagcacc agcaacgcgc agacgtacaa ccagaacttg atcaggcatg   2880  
               
               
                   
               
               
                 ttggcggagg aacgccgagg agaccaggga aggagatcga ggcatacata ttcgagatgt   2940  
               
               
                   
               
               
                 tcaacgagaa ccagaaggct ggagggatcg agcagaactt tggcctgttt tatcccaaca   3000  
               
               
                   
               
               
                 agcagcccgt ataccaaata agcttttaga aactaacttg taaggttgat gaatcatctc   3060  
               
               
                   
               
               
                 ctacctacct acctacctac gaataaaaca tgaaataaag caccaaaata aagggagaat   3120  
               
               
                   
               
               
                 tctgatcttg gagaaagttg aatcatgatg atatataaca aacacccctc tttactcatt   3180  
               
               
                   
               
               
                 atcagtatgt tacaagtttc ttgaaacttg aacggatcac aatttggacc tacaagtatt   3240  
               
               
                   
               
               
                 ttgggtcata attatttcat tgaactatat attcaaaaaa agatgtgttt ggagtgctta   3300  
               
               
                   
               
               
                 atacagtatg acttcagttt gcaagattac ctcttcagcg tcagcttcag catgccaaaa   3360  
               
               
                   
               
               
                 aaccatcatc tgctatgggg catgttttac accttgatgg tgctacatca tcatcattca   3420  
               
               
                   
               
               
                 tgtttcattt taggtctcgt gctctttata tagatcacat aaaagtttgg atcgcttcaa   3480  
               
               
                   
               
               
                 gtttctaggt tacattgtat gcagcacttt gagcctactg aacattgtga ctgcctttta   3540  
               
               
                   
               
               
                 gaacattgga ctgcaggaa                                                3559  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 18  
               
               
                 &lt;211&gt; LENGTH: 3559  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 18  
               
               
                   
               
               
                 taacctgggt gcgccaccgc cggcgagatc ttatcaccta gggggcccga cgtccttaag     60  
               
               
                   
               
               
                 attttagata agaaaaaata aaataattaa tttaatttaa ttaaaaaata acaaaccata    120  
               
               
                   
               
               
                 aatcggattg taagggcctg aggagataaa aacctctaac ttatgtttta agaagagggt    180  
               
               
                   
               
               
                 agatttcaat aaaattaaaa cttctagtat accgactgta tatttcgttt atacagtttc    240  
               
               
                   
               
               
                 catcaaaagt ggcaggtgtg ctatctttgt tgtttcatcc cattaattta aacaaggcag    300  
               
               
                   
               
               
                 tagtgtttcg tgttgtggtt ttataagtga attagtttag gagtgatatt tattattagg    360  
               
               
                   
               
               
                 aagtttgacg ttgagatttg ttactccaag agagagggtc gttgcaagaa aagacttgtg    420  
               
               
                   
               
               
                 tttctaaacg gtgttggaat cgactgaaaa ttatagtcac cagagacctg ttctaagaac    480  
               
               
                   
               
               
                 aacgtgcgat tttaagcttg attttagtct agctcaatat aggcattaac tctaactact    540  
               
               
                   
               
               
                 ggcttggcta aaattctcat gagaggcatt gaaccctaat tattttaatt attccatcca    600  
               
               
                   
               
               
                 tagtcaataa aatctactat ttttagaact atcaaactta gagtagaatc agtgaataaa    660  
               
               
                   
               
               
                 aattaatttt tattattatt attaaactaa ttagactaac cttttttttt ttcaagagat    720  
               
               
                   
               
               
                 cggtaatttc agaccatcct gtatctttaa ttacttaatt tgacattggt attccaactt    780  
               
               
                   
               
               
                 aaaaacttgt gtacatgtcc ttttaactaa acaacttcag tacagattag ttacgtcgtc    840  
               
               
                   
               
               
                 aaatgtcgaa ccacactgaa ggtgttgata tccgaatagg ggaccctcag ctcctagttt    900  
               
               
                   
               
               
                 gcacactcgt tataagaggg aaggactact atttgatact accgacaatc cacacattcg    960  
               
               
                   
               
               
                 tgaggtttaa aaggtagtta caccttaacc ttctcaagtg cgtgactgcc tggttgagcc   1020  
               
               
                   
               
               
                 aaacaagtca gaccactgat gacgactcgt actcttttac caactaccat cgttcaacgt   1080  
               
               
                   
               
               
                 ttacatggac tggagtagaa tttctgacaa ctaatctacg tacgtaacta atgcagagaa   1140  
               
               
                   
               
               
                 ggtagaaatt gagaaaacta gctacgtagc agaattaatc cagttcctgt acactactgt   1200  
               
               
                   
               
               
                 tcttagataa ggtgataaac actgggtata aggtttacct tgttctgaag gttcaggagt   1260  
               
               
                   
               
               
                 aggtcttaaa accttcccta ttcctaccac ccctctttct tgttcgacaa cggaaagcaa   1320  
               
               
                   
               
               
                 aagaagatag tccttcggtt ctcaaagttc tcctcccatc tggactcccc tactacggac   1380  
               
               
                   
               
               
                 acagctttgg agatatattc ctcatccttg tgtcgtacaa ctacttgtgt ttggtaaagt   1440  
               
               
                   
               
               
                 cgccccttct tctcttggga aaactgtctc aacaacagta ccgttgtttt cgaagagaga   1500  
               
               
                   
               
               
                 ggtattttcc gaaacggaac gaccaaagtc aggaacatcg tcaaggttgt tcaagagaga   1560  
               
               
                   
               
               
                 gagagagaga gagagagaga gagagagaga gagagagaga gagtataata tgtaaactaa   1620  
               
               
                   
               
               
                 caatcgagaa tgtttaaata atcccaaaaa tattctcaag ttcgaaaacc attaaattag   1680  
               
               
                   
               
               
                 taccatccaa tataaaagtt ttgaacattg gacgtaaaac agagaaataa agtacgttat   1740  
               
               
                   
               
               
                 aagaaaagga actaaccgaa tgcagtaaat gaactcaatc gagtatacat tgacaaattt   1800  
               
               
                   
               
               
                 ataaacccta ataaccaatt gcctattttt tttaattaac taaaatctat gttacgatat   1860  
               
               
                   
               
               
                 atatatatat atatatatat atatatatat atatatatat atatatatat aatatccatc   1920  
               
               
                   
               
               
                 tttgaaccat attaagtgtg catacaagcg aaatagactt attttactca tcaggaaagt   1980  
               
               
                   
               
               
                 tacgtctaat cagaatgagg tgaacgtcta cgtgctggtt aaacgaacta gtagaaggta   2040  
               
               
                   
               
               
                 tctcgtggtg tcgattcaga ggctacacaa gatgacgtcc tcacgttagc taaccacaga   2100  
               
               
                   
               
               
                 cgatgcctta cgagccgttg ttagaagggg gcgggtcgct ccaccagtca gagatgttta   2160  
               
               
                   
               
               
                 ggttgttgta gcgctcctac tctgagatgc taggtttggt ccggcgggac gttcgggagt   2220  
               
               
                   
               
               
                 ccttgaggtt gtaggttcag gacaacctac agggggctag gctgcacgtc agtgaccgga   2280  
               
               
                   
               
               
                 ggttaggaag ccggcggccg ctgacctagg cctccttgca gcagcggatg accgggtcgc   2340  
               
               
                   
               
               
                 agaggaaagc tatgtatcga cagcctttgc tcgactaggg gcctagccta gaccgcgtca   2400  
               
               
                   
               
               
                 tgtaggaggg gcggtacgcg ttgtagatgt tacgaaacag gagccgaccg gacgttttgg   2460  
               
               
                   
               
               
                 tctagttcca gagctggcgc cagctgtgcc cgcaggagcc gtgcaggatg ggagggaggc   2520  
               
               
                   
               
               
                 ggccgcggaa gaggaggcgg cgggtccgca tggactcggg gtagcacgtc aagaaccgct   2580  
               
               
                   
               
               
                 cattgcctcg cggcgaggac cagttacaca tgggaataaa atcgatgtgg ccgttgggcc   2640  
               
               
                   
               
               
                 ctgtctagag cgacgggatg cgggacaagt gccggaggcc gcagcagcac gtcctacccg   2700  
               
               
                   
               
               
                 ctaagtcgat agtcttggac aagctgcggt agcagctgcg ccagaagcgc cgcgacctct   2760  
               
               
                   
               
               
                 ctcaccctcc ccgcttgcac cgccaccacc acagcctctc gcccaccggc agccgcccgc   2820  
               
               
                   
               
               
                 ctcctcggct tcgctcgtgg tcgttgcgcg tctgcatgtt ggtcttgaac tagtccgtac   2880  
               
               
                   
               
               
                 aaccgcctcc ttgcggctcc tctggtccct tcctctagct ccgtatgtat aagctctaca   2940  
               
               
                   
               
               
                 agttgctctt ggtcttccga cctccctagc tcgtcttgaa accggacaaa atagggttgt   3000  
               
               
                   
               
               
                 tcgtcgggca tatggtttat tcgaaaatct ttgattgaac attccaacta cttagtagag   3060  
               
               
                   
               
               
                 gatggatgga tggatggatg cttattttgt actttatttc gtggttttat ttccctctta   3120  
               
               
                   
               
               
                 agactagaac ctctttcaac ttagtactac tatatattgt ttgtggggag aaatgagtaa   3180  
               
               
                   
               
               
                 tagtcataca atgttcaaag aactttgaac ttgcctagtg ttaaacctgg atgttcataa   3240  
               
               
                   
               
               
                 aacccagtat taataaagta acttgatata taagtttttt tctacacaaa cctcacgaat   3300  
               
               
                   
               
               
                 tatgtcatac tgaagtcaaa cgttctaatg gagaagtcgc agtcgaagtc gtacggtttt   3360  
               
               
                   
               
               
                 ttggtagtag acgatacccc gtacaaaatg tggaactacc acgatgtagt agtagtaagt   3420  
               
               
                   
               
               
                 acaaagtaaa atccagagca cgagaaatat atctagtgta ttttcaaacc tagcgaagtt   3480  
               
               
                   
               
               
                 caaagatcca atgtaacata cgtcgtgaaa ctcggatgac ttgtaacact gacggaaaat   3540  
               
               
                   
               
               
                 cttgtaacct gacgtcctt                                                3559  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 19  
               
               
                 &lt;211&gt; LENGTH: 1131  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 19  
               
               
                   
               
               
                 Ile Gly Pro Thr Arg Trp Arg Pro Leu Asn Ser Gly Ser Pro Gly Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Gln Glu Phe Asn Leu Phe Phe Phe Ile Leu Leu Ile Lys Leu Asn Phe  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Phe Ile Val Trp Tyr Leu Ala His Ser Arg Thr Pro Leu Phe Leu Glu  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ile Glu Tyr Lys Ile Leu Leu Pro Ser Lys Val Ile Leu Ile Leu Lys  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Ile Ile Trp Leu Thr Tyr Lys Ala Asn Met Ser Lys Val Val Phe Thr  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Val His Thr Ile Glu Thr Thr Lys Gly Asn Ile Cys Ser Val Ile Thr  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Lys His Asn Thr Lys Ile Phe Thr Ser Asn Pro His Tyr Lys Ser Phe  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Lys Leu Gln Leu Thr Met Arg Phe Ser Leu Pro Ala Thr Phe Phe Ser  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Glu His Lys Asp Leu Pro Gln Pro Leu Thr Phe Asn Ile Ser Gly Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Trp Thr Arg Phe Leu Leu His Ala Lys Ile Arg Thr Lys Ile Arg Ser  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Ser Tyr Ile Arg Asn Asp Pro Asn Arg Phe Glu Tyr Ser Pro Leu Gly  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Ile Asn Lys Ile Asn Lys Val Gly Ile Ser Tyr Phe Arg Lys Ser Phe  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Glu Ser His Leu Ser His Leu Phe Leu Ile Lys Asn Asn Asn Asn Asn  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Leu Ile Asn Leu Ile Gly Lys Lys Lys Ser Ser Leu Ala Ile Lys Val  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Trp Asp Ile Glu Ile Asn Glu Leu Asn Cys Asn His Lys Val Glu Phe  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Leu Asn Thr Cys Thr Gly Lys Leu Ile Cys Ser His Val Ser Met Gln  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Gln Phe Thr Ala Trp Cys Asp Phe His Asn Tyr Arg Leu Ile Pro Trp  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Glu Ser Arg Ile Lys Arg Val Ser Asn Ile Leu Pro Ser Thr Met Met  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Ala Val Arg Cys Val Ser Thr Pro Asn Phe Pro Ser Met Trp Asn Trp  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Lys Ser Ser Arg Thr Asp Gly Pro Thr Arg Phe Val Gln Ser Gly Asp  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Tyr Cys Ala Glu Asn Gly Trp Gln Val Ala Asn Val Pro Asp Leu Ile  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Leu Lys Thr Val Asp Met His Ala Leu Ile Thr Ser Leu Pro Ser Leu  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Thr Leu Leu Ile Asp Ala Ser Ser Leu Gly Gln Gly His Val Met Thr  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Arg Ile Tyr Ser Thr Ile Cys Asp Pro Tyr Ser Lys Trp Asn Lys Thr  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Ser Lys Ser Ser Ser Arg Ile Leu Glu Gly Ile Arg Met Val Gly Arg  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Lys Asn Lys Leu Leu Pro Phe Val Phe Phe Tyr Gln Glu Ala Lys Ser  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Phe Lys Arg Arg Val Asp Leu Arg Gly Cys Leu Cys Arg Asn Leu Tyr  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Ile Arg Ser Arg Asn Thr Ala Cys Thr Gln Thr Ile Ser Ala Gly Lys  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Lys Arg Thr Leu Leu Thr Glu Leu Leu Ser Trp Gln Gln Lys Leu Leu  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Ser Pro Lys Ala Leu Pro Cys Trp Phe Gln Ser Leu Gln Phe Gln Gln  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Val Leu Ser Leu Ser Leu Ser Leu Ser Leu Ser Leu Ser Leu Ser Leu  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Ser His Ile Ile His Leu Ile Val Ser Ser Tyr Lys Phe Ile Arg Val  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Phe Ile Arg Val Gln Ala Phe Gly Asn Leu Ile Met Val Gly Tyr Ile  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Phe Lys Thr Cys Asn Leu His Phe Val Ser Leu Phe His Ala Ile Phe  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Phe Ser Leu Ile Gly Leu Arg His Leu Leu Glu Leu Ala His Met Leu  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Phe Lys Tyr Leu Gly Leu Leu Val Asn Gly Lys Lys Leu Ile Asp Phe  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Arg Tyr Asn Ala Ile Tyr Ile Tyr Ile Tyr Ile Tyr Ile Tyr Ile Tyr  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Ile Tyr Ile Tyr Ile Tyr Tyr Arg Lys Leu Gly Ile Ile His Thr Tyr  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Val Arg Phe Ile Ile Lys Val Val Leu Ser Met Gln Ile Ser Leu Thr  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Pro Leu Ala Asp Ala Arg Pro Ile Cys Leu Ile Ile Phe His Arg Ala  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Pro Gln Leu Ser Leu Arg Cys Val Leu Leu Gln Glu Cys Asn Arg Leu  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                 Val Ser Ala Thr Glu Cys Ser Ala Thr Ile Phe Pro Arg Pro Ala Arg  
               
               
                             660                 665                 670  
               
               
                   
               
               
                 Trp Ser Val Ser Thr Asn Pro Thr Thr Ser Arg Gly Asp Ser Thr Ile  
               
               
                         675                 680                 685  
               
               
                   
               
               
                 Gln Thr Arg Pro Pro Cys Lys Pro Ser Gly Thr Pro Thr Ser Lys Ser  
               
               
                     690                 695                 700  
               
               
                   
               
               
                 Cys Trp Met Ser Pro Asp Pro Thr Cys Ser His Trp Pro Pro Ile Leu  
               
               
                 705                 710                 715                 720  
               
               
                   
               
               
                 Arg Pro Pro Ala Thr Gly Ser Gly Gly Thr Ser Ser Pro Thr Gly Pro  
               
               
                                 725                 730                 735  
               
               
                   
               
               
                 Ala Ser Pro Phe Asp Thr Leu Ser Glu Thr Ser Ser Pro Asp Arg Ile  
               
               
                             740                 745                 750  
               
               
                   
               
               
                 Trp Arg Ser Thr Ser Ser Pro Pro Cys Ala Thr Ser Thr Met Leu Cys  
               
               
                         755                 760                 765  
               
               
                   
               
               
                 Pro Arg Leu Ala Cys Lys Thr Arg Ser Arg Ser Arg Pro Arg Ser Thr  
               
               
                     770                 775                 780  
               
               
                   
               
               
                 Arg Ala Ser Ser Ala Arg Pro Thr Leu Pro Pro Pro Ala Pro Ser Pro  
               
               
                 785                 790                 795                 800  
               
               
                   
               
               
                 Pro Pro Pro Arg Arg Thr Ala Pro Ser Cys Ser Ser Trp Arg Val Thr  
               
               
                                 805                 810                 815  
               
               
                   
               
               
                 Glu Arg Arg Ser Trp Ser Met Cys Thr Leu Ile Leu Ala Thr Pro Ala  
               
               
                             820                 825                 830  
               
               
                   
               
               
                 Thr Arg Asp Arg Ser Arg Cys Pro Thr Pro Cys Ser Arg Pro Pro Ala  
               
               
                         835                 840                 845  
               
               
                   
               
               
                 Ser Ser Cys Arg Met Gly Asp Ser Ala Ile Arg Thr Cys Ser Thr Pro  
               
               
                     850                 855                 860  
               
               
                   
               
               
                 Ser Ser Thr Arg Ser Ser Arg Arg Trp Arg Glu Trp Glu Gly Arg Thr  
               
               
                 865                 870                 875                 880  
               
               
                   
               
               
                 Trp Arg Trp Trp Cys Arg Arg Ala Gly Gly Arg Arg Arg Ala Glu Glu  
               
               
                                 885                 890                 895  
               
               
                   
               
               
                 Pro Lys Arg Ala Pro Ala Thr Arg Arg Arg Thr Thr Arg Thr Ser Gly  
               
               
                             900                 905                 910  
               
               
                   
               
               
                 Met Leu Ala Glu Glu Arg Arg Gly Asp Gln Gly Arg Arg Ser Arg His  
               
               
                         915                 920                 925  
               
               
                   
               
               
                 Thr Tyr Ser Arg Cys Ser Thr Arg Thr Arg Arg Leu Glu Gly Ser Ser  
               
               
                     930                 935                 940  
               
               
                   
               
               
                 Arg Thr Leu Ala Cys Phe Ile Pro Thr Ser Ser Pro Tyr Thr Lys Ala  
               
               
                 945                 950                 955                 960  
               
               
                   
               
               
                 Phe Arg Asn Leu Val Arg Leu Met Asn His Leu Leu Pro Thr Tyr Leu  
               
               
                                 965                 970                 975  
               
               
                   
               
               
                 Pro Thr Asn Lys Thr Asn Lys Ala Pro Lys Arg Glu Asn Ser Asp Leu  
               
               
                             980                 985                 990  
               
               
                   
               
               
                 Gly Glu Ser Ile Met Met Ile Tyr Asn Lys His Pro Ser Leu Leu Ile  
               
               
                         995                 1000                1005  
               
               
                   
               
               
                 Ile Ser Met Leu Gln Val Ser Asn Leu Asn Gly Ser Gln Phe Gly Pro  
               
               
                     1010                1015                1020  
               
               
                   
               
               
                 Thr Ser Ile Leu Gly His Asn Tyr Phe Ile Glu Leu Tyr Ile Gln Lys  
               
               
                 1025                1030                1035                1040  
               
               
                   
               
               
                 Lys Met Cys Leu Glu Cys Leu Ile Gln Tyr Asp Phe Ser Leu Gln Asp  
               
               
                                 1045                1050                1055  
               
               
                   
               
               
                 Tyr Leu Phe Ser Val Ser Phe Ser Met Pro Lys Asn His His Leu Leu  
               
               
                             1060                1065                1070  
               
               
                   
               
               
                 Trp Gly Met Phe Tyr Thr Leu Met Val Leu His His His His Ser Cys  
               
               
                         1075                1080                1085  
               
               
                   
               
               
                 Phe Ile Leu Gly Leu Val Leu Phe Ile Ile Thr Lys Phe Gly Ser Leu  
               
               
                     1090                1095                1100  
               
               
                   
               
               
                 Gln Val Ser Arg Leu His Cys Met Gln His Phe Glu Pro Thr Glu His  
               
               
                 1105                1110                1115                1120  
               
               
                   
               
               
                 Cys Asp Cys Leu Leu Glu His Trp Thr Ala Gly  
               
               
                                 1125                1130  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 20  
               
               
                 &lt;211&gt; LENGTH: 1126  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 20  
               
               
                   
               
               
                 Leu Asp Pro Arg Gly Gly Gly Arg Ser Arg Ile Val Asp Pro Pro Gly  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Cys Arg Asn Ser Lys Ile Tyr Ser Phe Leu Phe Tyr Leu Asn Asn Phe  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Leu Leu Phe Gly Ile Pro Asn Ile Pro Gly Leu Leu Tyr Phe Trp Arg  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Leu Asn Thr Lys Phe Phe Ser His Leu Lys Leu Phe Phe Arg Ser Tyr  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Gly His Ile Lys Gln Ile Cys Gln Arg Phe Ser Pro Ser Thr Arg Lys  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Gln Gln Ser Arg Val Ile Lys Phe Val Pro Ser Ser Gln Ser Thr Thr  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Pro Lys Tyr Ser Leu Asn Gln Ile Leu Thr Ile Asn Asn Asn Pro Ser  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Asn Cys Asn Ser Lys Gln Gly Ser Leu Ser Gln Gln Arg Ser Phe Leu  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Asn Thr Lys Ile Cys His Asn Leu Ser Leu Leu Ile Ser Val Val Ser  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Gly Gln Asp Ser Cys Cys Thr Leu Lys Phe Glu Leu Lys Ser Asp Arg  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Val Ile Ser Val Ile Glu Ile Asp Asp Arg Thr Asp Phe Lys Ser Thr  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Leu Arg Asn Leu Gly Leu Ile Lys Leu Ile Arg Val Ser Val Ile Leu  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Asp Asp Lys Asn Leu Asp Ser Leu Asn Leu Ile Leu Val Thr Tyr Phe  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Leu Lys Ile Ile Ile Ile Ile Leu Ile Leu Glu Lys Lys Lys Val Leu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Pro Leu Lys Ser Gly Arg Thr Lys Leu Met Asn Thr Val Thr Ile Arg  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Leu Asn Phe Thr His Val Gln Glu Asn Phe Val Glu Val Met Ser Asn  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Gln Cys Ser Ser Leu Gln Leu Gly Val Thr Ser Thr Thr Ile Gly Leu  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Ser Pro Gly Ser Arg Gly Ser Asn Val Ala Ile Phe Ser Leu Pro Asp  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Asp Lys Leu Trp Leu Leu Gly Val Ala Leu Gln Ile Phe His Gln Cys  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Gly Ile Gly Arg Val His Ala Leu Thr Asp Gln Leu Gly Leu Phe Ser  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Leu Val Thr Thr Ala Glu His Glu Lys Met Val Asp Gly Ser Lys Leu  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Gln Met Tyr Leu Thr Ser Ser Arg Leu Leu Ile Arg Cys Met His Leu  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Arg Leu Phe His Leu Leu Phe Ser Met His Arg Leu Asn Val Lys Asp  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Met Gln Glu Ser Ile Pro Leu Phe Val Thr His Ile Pro Asn Gly Thr  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Arg Leu Pro Ser Pro His Pro Glu Phe Trp Lys Gly Gly Trp Trp Gly  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Glu Arg Thr Ser Cys Cys Leu Ser Phe Ser Ser Ile Arg Lys Pro Arg  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Val Ser Arg Gly Gly Thr Gly Asp Asp Ala Cys Val Glu Thr Ser Ile  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Gly Val Gly Thr Gln His Val Asp Glu His Lys Pro Phe Gln Arg Gly  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Arg Arg Glu Pro Phe Gln Ser Cys Cys His Gly Asn Lys Ser Phe Ser  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Leu His Lys Arg Leu Cys Leu Ala Gly Phe Ser Pro Cys Ser Ser Ser  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Asn Lys Phe Ser Leu Ser Leu Ser Leu Ser Leu Ser Leu Ser Leu Ser  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Leu Ser Leu Ile Leu Tyr Ile Leu Leu Ala Leu Thr Asn Leu Leu Gly  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Phe Leu Glu Phe Lys Leu Leu Val Ile Ser Trp Val Ile Phe Ser Lys  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Leu Val Thr Cys Ile Leu Ser Leu Tyr Phe Met Gln Tyr Ser Phe Pro  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Leu Ala Tyr Val Ile Tyr Leu Ser Leu Ile Cys Asn Cys Leu Asn Ile  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Trp Asp Tyr Trp Leu Thr Asp Lys Lys Asn Leu Ile Leu Asp Thr Met  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Leu Tyr Ile Tyr Ile Tyr Ile Tyr Ile Tyr Ile Tyr Ile Tyr Ile Tyr  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Ile Tyr Ile Ile Ile Gly Arg Asn Leu Val Phe Thr Arg Met Phe Ala  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Leu Ser Glu Asn Glu Ser Phe Gln Cys Arg Leu Val Leu Leu His Leu  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Gln Met His Asp Gln Phe Ala Ser Ser Ser Ile Glu His His Ser Val  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Ser Asp Val Phe Tyr Cys Arg Ser Ala Ile Asp Trp Cys Leu Leu Arg  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                 Asn Ala Arg Gln Gln Ser Ser Pro Ala Gln Arg Gly Gly Gln Ser Leu  
               
               
                             660                 665                 670  
               
               
                   
               
               
                 Gln Ile Gln Gln His Arg Glu Asp Glu Thr Leu Arg Ser Lys Pro Gly  
               
               
                         675                 680                 685  
               
               
                   
               
               
                 Arg Pro Ala Ser Pro Gln Glu Leu Gln His Pro Ser Pro Val Gly Cys  
               
               
                     690                 695                 700  
               
               
                   
               
               
                 Pro Pro Ile Arg Arg Ala Val Thr Gly Leu Gln Ser Phe Gly Arg Arg  
               
               
                 705                 710                 715                 720  
               
               
                   
               
               
                 Arg Leu Asp Pro Glu Glu Arg Arg Arg Leu Leu Ala Gln Arg Leu Leu  
               
               
                                 725                 730                 735  
               
               
                   
               
               
                 Ser Ile His Ser Cys Arg Lys Arg Ala Asp Pro Arg Ile Gly Ser Gly  
               
               
                             740                 745                 750  
               
               
                   
               
               
                 Ala Val His Pro Pro Arg His Ala Gln His Leu Gln Cys Phe Val Leu  
               
               
                         755                 760                 765  
               
               
                   
               
               
                 Gly Trp Pro Ala Lys Pro Asp Gln Gly Leu Asp Arg Gly Arg His Gly  
               
               
                     770                 775                 780  
               
               
                   
               
               
                 Arg Pro Arg His Val Leu Pro Ser Leu Arg Arg Arg Leu Leu Leu Arg  
               
               
                 785                 790                 795                 800  
               
               
                   
               
               
                 Arg Pro Gly Val Pro Glu Pro His Arg Ala Val Leu Gly Glu Arg Ser  
               
               
                                 805                 810                 815  
               
               
                   
               
               
                 Ala Ala Pro Gly Gln Cys Val Pro Leu Phe Leu His Arg Gln Pro Gly  
               
               
                             820                 825                 830  
               
               
                   
               
               
                 Thr Asp Leu Ala Ala Leu Arg Pro Val His Gly Leu Arg Arg Arg Arg  
               
               
                         835                 840                 845  
               
               
                   
               
               
                 Ala Gly Trp Ala Ile Gln Leu Ser Glu Pro Val Arg Arg His Arg Arg  
               
               
                     850                 855                 860  
               
               
                   
               
               
                 Arg Gly Leu Arg Gly Ala Gly Glu Ser Gly Arg Gly Glu Arg Gly Gly  
               
               
                 865                 870                 875                 880  
               
               
                   
               
               
                 Gly Gly Val Gly Glu Arg Val Ala Val Gly Gly Arg Arg Ser Arg Ser  
               
               
                                 885                 890                 895  
               
               
                   
               
               
                 Glu His Gln Gln Arg Ala Asp Val Gln Pro Glu Leu Asp Gln Ala Cys  
               
               
                             900                 905                 910  
               
               
                   
               
               
                 Trp Arg Arg Asn Ala Glu Glu Thr Arg Glu Gly Asp Arg Gly Ile His  
               
               
                         915                 920                 925  
               
               
                   
               
               
                 Ile Arg Asp Val Gln Arg Glu Pro Glu Gly Trp Arg Asp Arg Ala Glu  
               
               
                     930                 935                 940  
               
               
                   
               
               
                 Leu Trp Pro Val Leu Ser Gln Gln Ala Ala Arg Ile Pro Asn Leu Leu  
               
               
                 945                 950                 955                 960  
               
               
                   
               
               
                 Glu Thr Asn Leu Gly Ile Ile Ser Tyr Leu Pro Thr Tyr Leu Arg Ile  
               
               
                                 965                 970                 975  
               
               
                   
               
               
                 Lys His Glu Ile Lys His Gln Asn Lys Gly Arg Ile Leu Ile Leu Glu  
               
               
                             980                 985                 990  
               
               
                   
               
               
                 Lys Val Glu Ser Tyr Ile Thr Asn Thr Pro Leu Tyr Ser Leu Ser Val  
               
               
                         995                 1000                1005  
               
               
                   
               
               
                 Cys Tyr Lys Phe Leu Glu Thr Thr Asp His Asn Leu Asp Leu Gln Val  
               
               
                     1010                1015                1020  
               
               
                   
               
               
                 Phe Trp Val Ile Ile Ile Ser Leu Asn Tyr Ile Phe Lys Lys Arg Cys  
               
               
                 1025                1030                1035                1040  
               
               
                   
               
               
                 Val Trp Ser Ala Tyr Ser Met Thr Ser Val Cys Lys Ile Thr Ser Ser  
               
               
                                 1045                1050                1055  
               
               
                   
               
               
                 Ala Ser Ala Ser Ala Cys Gln Lys Thr Ile Ile Cys Tyr Gly Ala Cys  
               
               
                             1060                1065                1070  
               
               
                   
               
               
                 Phe Thr Pro Cys Tyr Ile Ile Ile Ile His Val Ser Phe Val Ser Cys  
               
               
                         1075                1080                1085  
               
               
                   
               
               
                 Ser Leu Tyr Arg Ser His Lys Ser Leu Asp Arg Phe Lys Phe Leu Gly  
               
               
                     1090                1095                1100  
               
               
                   
               
               
                 Tyr Ile Val Cys Ser Thr Leu Ser Leu Leu Asn Ile Val Thr Ala Phe  
               
               
                 1105                1110                1115                1120  
               
               
                   
               
               
                 Asn Ile Gly Leu Gln Glu  
               
               
                                 1125  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 21  
               
               
                 &lt;211&gt; LENGTH: 1121  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 21  
               
               
                   
               
               
                 Asn Trp Thr His Ala Val Ala Ala Ala Leu Glu Trp Ile Pro Arg Ala  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ala Gly Ile Leu Lys Ser Ile Leu Phe Tyr Phe Ile Asn Ile Lys Ile  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Phe Tyr Cys Leu Val Phe Ser Leu Thr Phe Pro Asp Ser Ser Ile Phe  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Gly Asp Ile Gln Asn Ser Ser Pro Ile Ser Tyr Phe Asn Phe Glu Asp  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 His Met Ala Asp Ile Ser Lys Tyr Val Lys Gly Ser Phe His Arg Pro  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 His Asp Arg Asn Asn Lys Val Gly Leu Asn Leu Phe Arg His His Lys  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Ala Gln His Gln Asn Ile His Leu Ile Lys Ser Ser Leu Ile Ile Ile  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Leu Gln Thr Ala Thr Leu Asn Asn Glu Val Leu Ser Pro Ser Asn Val  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Leu Phe Thr Gln Arg Phe Ala Thr Thr Leu Ala Asp Phe Tyr Gln Trp  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Ser Leu Asp Lys Ile Leu Val Ala Arg Asn Ser Asn Asn Gln Ile Glu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Leu Tyr Pro Leu Arg Leu Met Thr Glu Pro Ile Leu Arg Val Leu Ser  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Val Thr Trp Asp Asn Gly Arg Tyr Gln Leu Phe Met Ile Lys Ile Leu  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ile Val Ile Ser Ser Ser Leu Ile Phe Asn Lys Phe Asp Ser Asp Trp  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Lys Lys Lys Lys Phe Ser Ser His Ser Leu Val Gly His Arg Asn Ile  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Lys Leu Pro Gly Ile Phe Glu His Met Tyr Arg Lys Ile Asp Leu Leu  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Lys Ser Cys Leu Ile Asn Ala Ala Val Tyr Ser Leu Val Leu Pro Gln  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Leu Ala Tyr Pro Leu Gly Val Glu Asp Gln Thr Cys Glu Gln Tyr Ser  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Pro Phe Leu Met Ile Asn Tyr Asp Gly Cys Val Cys Lys His Ser Lys  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Phe Ser Ile Asn Val Glu Leu Glu Glu Phe Thr His Arg Thr Asn Ser  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Val Cys Ser Val Trp Leu Leu Leu Ser Met Arg Lys Trp Leu Met Val  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Ala Ser Cys Lys Cys Thr Pro His Leu Lys Asp Cys Leu Asp Ala Cys  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Ile Asp Tyr Val Ser Ser Ile Phe Asn Ser Phe Asp Arg Cys Ile Val  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Leu Ile Arg Ser Arg Thr Cys Asp Asp Lys Asn Leu Phe His Tyr Leu  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Pro Ile Phe Gln Met Glu Gln Asp Phe Gln Val Leu Ile Gln Asn Phe  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Gly Arg Asp Lys Asp Gly Gly Glu Lys Glu Gln Ala Val Ala Phe Arg  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Phe Leu Leu Ser Gly Ser Gln Glu Phe Gln Glu Glu Gly Arg Pro Glu  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Gly Met Met Pro Val Ser Lys Pro Leu Tyr Lys Glu Glu His Ser Met  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Leu Met Asn Thr Asn His Phe Ser Gly Glu Glu Glu Asn Pro Phe Asp  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Arg Val Val Val Met Ala Thr Lys Ala Ser Leu Ser Ile Lys Gly Phe  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Ala Leu Leu Val Ser Val Leu Val Ala Val Pro Thr Ser Ser Leu Ser  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Leu Ser Leu Ser Leu Ser Leu Ser Leu Ser Leu Ser Leu Ser Tyr Tyr  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Thr Phe Asp Cys Leu Leu Gln Ile Tyr Gly Phe Tyr Lys Ser Ser Ser  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Phe Trp Phe Asn His Gly Arg Leu Tyr Phe Gln Asn Leu Pro Ala Phe  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Cys Leu Phe Ile Ser Cys Asn Ile Leu Phe Leu Asp Trp Leu Thr Ser  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Phe Thr Val Ser Ser Tyr Val Thr Val Ile Phe Gly Ile Ile Gly Arg  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ile Lys Lys Ile Asn Phe Ile Gln Cys Tyr Ile Tyr Ile Tyr Ile Tyr  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Ile Tyr Ile Tyr Ile Tyr Ile Tyr Ile Tyr Ile Leu Val Glu Thr Trp  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Tyr Asn Ser His Val Cys Ser Leu Tyr Asn Lys Met Ser Ser Pro Phe  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Asn Ala Asp Ser Tyr Ser Thr Cys Arg Cys Thr Thr Asn Leu Leu Asp  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 His Leu Pro Ser Thr Thr Ala Lys Ser Pro Met Cys Ser Thr Ala Gly  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Val Gln Ser Ile Gly Val Cys Tyr Gly Met Leu Gly Asn Asn Leu Pro  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                 Pro Pro Ser Glu Val Val Ser Leu Tyr Lys Ser Asn Asn Ile Ala Arg  
               
               
                             660                 665                 670  
               
               
                   
               
               
                 Met Arg Leu Tyr Asp Pro Asn Gln Ala Ala Leu Gln Ala Leu Arg Asn  
               
               
                         675                 680                 685  
               
               
                   
               
               
                 Ser Asn Ile Gln Val Leu Leu Asp Val Pro Arg Ser Asp Val Gln Ser  
               
               
                     690                 695                 700  
               
               
                   
               
               
                 Leu Ala Ser Asn Pro Ser Ala Ala Gly Asp Trp Ile Arg Arg Asn Val  
               
               
                 705                 710                 715                 720  
               
               
                   
               
               
                 Val Ala Tyr Trp Pro Ser Val Ser Phe Arg Tyr Ile Ala Val Gly Asn  
               
               
                                 725                 730                 735  
               
               
                   
               
               
                 Glu Leu Ile Pro Gly Ser Asp Leu Ala Gln Tyr Ile Leu Pro Ala Met  
               
               
                             740                 745                 750  
               
               
                   
               
               
                 Arg Asn Ile Tyr Asn Ala Leu Ser Ser Ala Gly Leu Gln Asn Gln Ile  
               
               
                         755                 760                 765  
               
               
                   
               
               
                 Lys Val Ser Thr Ala Val Asp Thr Gly Val Leu Gly Thr Ser Tyr Pro  
               
               
                     770                 775                 780  
               
               
                   
               
               
                 Pro Ser Ala Gly Ala Phe Ser Ser Ala Ala Gln Ala Tyr Leu Ser Pro  
               
               
                 785                 790                 795                 800  
               
               
                   
               
               
                 Ile Val Gln Phe Leu Ala Ser Asn Gly Ala Pro Leu Leu Val Asn Val  
               
               
                                 805                 810                 815  
               
               
                   
               
               
                 Tyr Pro Tyr Phe Ser Tyr Thr Gly Asn Pro Gly Gln Ile Ser Leu Pro  
               
               
                             820                 825                 830  
               
               
                   
               
               
                 Tyr Ala Leu Phe Thr Ala Ser Gly Val Val Val Gln Asp Gly Arg Phe  
               
               
                         835                 840                 845  
               
               
                   
               
               
                 Ser Tyr Gln Asn Leu Phe Asp Ala Ile Val Asp Ala Val Phe Ala Ala  
               
               
                     850                 855                 860  
               
               
                   
               
               
                 Leu Glu Arg Val Gly Gly Ala Asn Val Ala Val Val Val Ser Glu Ser  
               
               
                 865                 870                 875                 880  
               
               
                   
               
               
                 Gly Trp Pro Ser Ala Gly Gly Gly Ala Glu Ala Ser Thr Ser Asn Ala  
               
               
                                 885                 890                 895  
               
               
                   
               
               
                 Gln Thr Tyr Asn Gln Asn Leu Ile Arg His Val Gly Gly Gly Thr Pro  
               
               
                             900                 905                 910  
               
               
                   
               
               
                 Arg Arg Pro Gly Lys Glu Ile Glu Ala Tyr Ile Phe Glu Met Phe Asn  
               
               
                         915                 920                 925  
               
               
                   
               
               
                 Glu Asn Cys Lys Ala Gly Gly Ile Glu Gln Asn Phe Gly Leu Phe Tyr  
               
               
                     930                 935                 940  
               
               
                   
               
               
                 Pro Asn Lys Gln Pro Val Tyr Gln Ile Ser Phe Lys Leu Thr Cys Lys  
               
               
                 945                 950                 955                 960  
               
               
                   
               
               
                 Val Asp Glu Ser Ser Pro Thr Tyr Leu Pro Thr Tyr Glu Asn Met Lys  
               
               
                                 965                 970                 975  
               
               
                   
               
               
                 Ser Thr Lys Ile Lys Gly Glu Phe Ser Trp Arg Lys Leu Asn His Asp  
               
               
                             980                 985                 990  
               
               
                   
               
               
                 Asp Ile Gln Thr Pro Leu Phe Thr His Tyr Gln Tyr Val Thr Ser Phe  
               
               
                         995                 1000                1005  
               
               
                   
               
               
                 Leu Lys Leu Glu Arg Ile Thr Ile Trp Thr Tyr Lys Tyr Phe Gly Ser  
               
               
                     1010                1015                1020  
               
               
                   
               
               
                 Leu Phe His Thr Ile Tyr Ser Lys Lys Asp Val Phe Gly Val Leu Asn  
               
               
                 1025                1030                1035                1040  
               
               
                   
               
               
                 Thr Val Leu Gln Phe Ala Arg Leu Pro Leu Gln Arg Gln Leu Gln His  
               
               
                                 1045                1050                1055  
               
               
                   
               
               
                 Ala Lys Lys Pro Ser Ser Ala Met Gly His Val Leu His Leu Asp Gly  
               
               
                             1060                1065                1070  
               
               
                   
               
               
                 Ala Thr Ser Ser Ser Phe Met Phe His Phe Arg Ser Arg Ala Leu Tyr  
               
               
                         1075                1080                1085  
               
               
                   
               
               
                 Ile Asp His Ile Lys Val Trp Ile Ala Ser Ser Phe Val Thr Leu Tyr  
               
               
                     1090                1095                1100  
               
               
                   
               
               
                 Ala Ala Leu Ala Tyr Thr Leu Leu Pro Phe Arg Thr Leu Asp Cys Arg  
               
               
                 1105                1110                1115                1120  
               
               
                   
               
               
                 Lys  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 22  
               
               
                 &lt;211&gt; LENGTH: 7397  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 82, 601, 628, 640, 655, 692, 725, 774, 793, 806, 813,  
               
               
                       854, 867, 870, 876, 882, 890, 919, 946, 959, 965, 995, 999, 1002,  
               
               
                       1028, 1043, 1054, 1075, 1093, 1515, 2166, 2216, 2265, 2345,  
               
               
                       2533, 2870, 2917, 3077, 3337, 3356, 3618, 3627, 3754  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 3810, 3819, 3884, 3893, 4494, 4503, 4524, 4533, 4568,  
               
               
                       4574, 4597, 4654, 4724, 4741, 4759, 4852, 5027, 5253, 5546, 5565,  
               
               
                       5567, 5575, 5578, 5618, 5619, 5650, 5669, 5672, 5677, 5683,  
               
               
                       5694, 5704, 5708, 5732, 5741, 5754, 5758, 5772, 5778  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 5780, 5784, 5788, 5802, 5804, 5808, 5813, 5820, 5824,  
               
               
                       5832, 5834, 5836, 5854, 5858, 5863, 5872, 5875, 5889, 5915, 5922,  
               
               
                       5950, 5990, 6006, 6011, 6344, 6401, 6416, 6596, 6600, 6608,  
               
               
                       6612, 6712, 6748, 6753, 6756, 6762, 6830, 6844, 6847  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 6863, 6910, 6965, 6968, 7070, 7116, 7179, 7291, 7322,  
               
               
                       7325, 7345, 7351, 7359, 7387, 7395  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 22  
               
               
                   
               
               
                 agcgaggtcg actaatgagc tactaacatt aatgtcacag atagtaatag atgagaagcc     60  
               
               
                   
               
               
                 gtatccaaca cgcaatctgt anacttggtc acaggacttc ttatccaaag actcgcctct    120  
               
               
                   
               
               
                 gcgatttccc acattcacct catttggtcc ataggaagct tcacagcggg caggaatcca    180  
               
               
                   
               
               
                 tttctctata taagcaccac ctcccaccca caccaccacc actaccactg ctaaggagga    240  
               
               
                   
               
               
                 tgaaggcctt gttgttggtc atctttaccc tggcctcgtc gctcggcgcc ttcgccgagc    300  
               
               
                   
               
               
                 aatgcggaag gcaagccggg ggggctctct gccccggcgg gctgtgctgt agccagtacg    360  
               
               
                   
               
               
                 gctggtgcgg taacacggat ccatactgcg gccaaggatg ccagagccaa tgcggcggta    420  
               
               
                   
               
               
                 gcggcggtag cggcggtggc agcgtggcct cgatcatcag ctcctccctc ttcgagcaga    480  
               
               
                   
               
               
                 tgctgaagca tcgcaacgac gcagcctgcc ccggcaaggg tttctacacg tacaacgcct    540  
               
               
                   
               
               
                 tcatcgccgc cgccaactcc ttcagcgggt tcgggacgac cggcgacgac ccaagaagaa    600  
               
               
                   
               
               
                 naaggagatc gcggctttct tggcgcanac gtctcacgan acgacaggta attcncacat    660  
               
               
                   
               
               
                 ctcccgaagc tcgtaaactg tttatgggat anaaaactga atgtttgggg tttggcaggt    720  
               
               
                   
               
               
                 gggtnggcga cgcgcccgat ggtccgtacg ccttgggtta ctgcttcgtc caanaacaaa    780  
               
               
                   
               
               
                 accctcatcg gantactgcg tcccanctcc cantggccgt gcgctgcagc aaaaaatact    840  
               
               
                   
               
               
                 acggccgaag cccntccaaa tttcatngtn agccanattc tnacagttcn tcgccgcgat    900  
               
               
                   
               
               
                 cgagttcaca acgatgccnt ttctaacgca acaatccgat gtgttntgcg tgcagcaant    960  
               
               
                   
               
               
                 acaantacgg gccggccggg agagccatcg gttcngacnt gntcaacaac ccagacctgg   1020  
               
               
                   
               
               
                 tggccacnga cgcgaccatc tcnttcaaga cggntctgtg gttttggatg actcntcagt   1080  
               
               
                   
               
               
                 cgcccaagcc gtngtgccac gacgtgataa ccgggagctg gacgccatcc aacgccgacc   1140  
               
               
                   
               
               
                 aggcggccgg aaggcttccg ggctacggtg tcaccaccaa catcatcaat ggagggttgg   1200  
               
               
                   
               
               
                 agtgcgggaa agggtacgat gccagggtgg cggataggat cggcttctac aagaggtact   1260  
               
               
                   
               
               
                 gcgacttgct gggggtgagc tacggagaca acttggactg ctacaaccag agaccctttg   1320  
               
               
                   
               
               
                 cttctacagc agctacagcc acattctagc ggtgagctat ggagacaact tggagtgcta   1380  
               
               
                   
               
               
                 caaccagaga ccctttactt agtccgatac tactgtgacg aatccatgta ataacgcaat   1440  
               
               
                   
               
               
                 aaacgctatt actgagatag cgactccgtg agttgactgt agaagttgcg gaggaagtct   1500  
               
               
                   
               
               
                 tcaataaaag cttanctaca tacatggccc acaactatcg ttgaccgtga tcatatgcat   1560  
               
               
                   
               
               
                 ccatcaaatg tcctcaaatg tcttggagta agtaaatgcg tattcgatcg gtaaaatgaa   1620  
               
               
                   
               
               
                 gatgttagaa taaataaaat taattatttt tttataatta taaatatttt aatatatttt   1680  
               
               
                   
               
               
                 ttaatcttaa agatcctaaa aatctaatta taaggatttt atatatggat tgggatacta   1740  
               
               
                   
               
               
                 agaatattta attataaaaa ttaatatact ttttaatctt aaagatctaa ttataagtat   1800  
               
               
                   
               
               
                 tttctatatg gattgggata ttaactcgat ttacttataa aaattttaat ataaaaattt   1860  
               
               
                   
               
               
                 taaatttaaa aattaaaata ctaaaaatat ctaaatataa cggtaatcat gagatcgaga   1920  
               
               
                   
               
               
                 acgtgatgat tgagatcatg agatcgaggt tgagagtaaa aaggaaatta cgttaatcat   1980  
               
               
                   
               
               
                 gggaaatttc gttttgtttg cacggtcgag atggtgaccg tggacaccta acatccacaa   2040  
               
               
                   
               
               
                 ccggcatgca ataaccatgt tgtcatatgt tagcttgtct catatcttat gaccatgaat   2100  
               
               
                   
               
               
                 cacatagtct tcacgaatat taattaagcc agcttagcat cacagttttg cacctttgta   2160  
               
               
                   
               
               
                 ccatanctga agtgttcgta tggcttgacc catcccgagt gtatggtctc ccggancctg   2220  
               
               
                   
               
               
                 gagcgtgtta acccgaggtc tagttgaggg gcatagacct tgttntctta ggcagaggtt   2280  
               
               
                   
               
               
                 gaagatcact cctttagcta tccgttgggt gcctatataa aggtcgaaat catgaggggg   2340  
               
               
                   
               
               
                 attcntaact cgacctattc aatatttgag ctagcaagag ttggagttac gtgtatgagg   2400  
               
               
                   
               
               
                 ttcgaccccc aatgctgttc ctggggtcgc ttttatacct attcctgcat gtgatcatac   2460  
               
               
                   
               
               
                 atagtagctt taatcatctt cagtcatcat cgtacgttgg gtgcatgcat tgtctaattt   2520  
               
               
                   
               
               
                 actcgattca atntcgttcg acactgcttc ctacctacta tgtggcccaa tacatagttg   2580  
               
               
                   
               
               
                 tattgtctca tacggcctcg agcaaagcgt gtgcagagga actgtgtcaa gtggttggct   2640  
               
               
                   
               
               
                 ggcctcgggc tcatggcatt gagttggctc gatacaacac atcggcttag ggataccatg   2700  
               
               
                   
               
               
                 ccgagtctat tgtggtagtt gacatgtcat gtggggtgga tgccaaaata tgctatatca   2760  
               
               
                   
               
               
                 ttctctccct acaaaggagt tgtgccatag gagaatcgtg gacacggctt gggttctgtg   2820  
               
               
                   
               
               
                 gtcggtcctt gttcgcctca gttgggtgga ttacttcatc aagttggccn tctgttggct   2880  
               
               
                   
               
               
                 gggcaaagta cacttggtag ggatggtcga gacaagncca aggaaggttg gctaagactt   2940  
               
               
                   
               
               
                 ggttttcgac aatcaattgt ttatgaggcg aatggtatcc ctccgttggg gtgtctgctc   3000  
               
               
                   
               
               
                 gtttcgattt gttgcgatgg attgtttgtt gtaggaggct tggttcgatt gctcttaagt   3060  
               
               
                   
               
               
                 cgggagaagg tatttgntaa ggagttcaat ttgaccatgt tgaagtgaat aaaaggactt   3120  
               
               
                   
               
               
                 gccaagaagt ttggctcgac cgtgttaaag ccagagaatg tgtatgtcga ggtctattca   3180  
               
               
                   
               
               
                 accatgtgga agctagagaa tgcaccaatt gtgaggtttg gcttgctcac gtttaaagca   3240  
               
               
                   
               
               
                 gaaggatata cttgctacga ggtttgctca accatgtgga agcaatcaaa tgcacttgct   3300  
               
               
                   
               
               
                 atgaggtttg gcttgactta ctcgacaatg gacgctngta agtgagaagg gactanccaa   3360  
               
               
                   
               
               
                 gacttagttg gcaaggacta gtcgatactt gctcgacaat agatgcctat aggtaatgga   3420  
               
               
                   
               
               
                 ttgactgaga cttagtcgac aaagactagc tgagacttag tgggcaatgg atgcctataa   3480  
               
               
                   
               
               
                 gtaagaaagg atggctcgag attaataaag atcaaataat taatataaat ttatcaaaca   3540  
               
               
                   
               
               
                 cttaatggac gcatataagt gagaaaggac ggatcgagat taataaagat caaataatta   3600  
               
               
                   
               
               
                 atataagttt atcaaacnct tattaanaca ttggacaaaa gaggtactat gtaatattaa   3660  
               
               
                   
               
               
                 aattgggagg cacaaatatt atttccaaat acttttctcc ttaagccctt cgccaccatt   3720  
               
               
                   
               
               
                 gccattttaa tctatttttt ctatataatt atcncataac attcgtacat gagatatgac   3780  
               
               
                   
               
               
                 ataaaccttc gacctgcttt agtaaacatn ttgattatng tgacaccaga agccataata   3840  
               
               
                   
               
               
                 ttgcttacct taacatgatg gagatgaact ttagttggtc caantatcta atnaatggaa   3900  
               
               
                   
               
               
                 gtggacaagc acgatgacta ggatggctac atgttcatgt gttgactttc caagtaatca   3960  
               
               
                   
               
               
                 atcaagctgg aatcgaataa gacgattaaa gtagggcgat gaccattaag ttcaatgtca   4020  
               
               
                   
               
               
                 cgctcatcaa cataattcca acaccgtgca gaaagatctt atcttacatt gacttgccca   4080  
               
               
                   
               
               
                 tccggccgcc ggcatcgatt ggcggaaacg aagggtcagt ctcccaattc acattcaaag   4140  
               
               
                   
               
               
                 gacgaattca ttttcatcag atgagcactt cagtcctgct tgattatatt ttattattat   4200  
               
               
                   
               
               
                 tattattatt aattgaatgg taagtttaca gaatatatag atattttagt ttcaataaaa   4260  
               
               
                   
               
               
                 tattttaaaa aatgataaag ggagaaggtg gatttgatct taggattttt attgtgagca   4320  
               
               
                   
               
               
                 ataaaagtct ttagttagaa cttccaaaat gtgtcaaatg aaccctaata agtgggtttg   4380  
               
               
                   
               
               
                 gtctatggtt acgatgagat cagtatttgt atataaaaaa attatcaact tgatttttat   4440  
               
               
                   
               
               
                 tttttaaccc ttaataagtg gacatgatat atcataatca aatcatgtga tgtntgatga   4500  
               
               
                   
               
               
                 gtnataacat attttttaat aatnaaaatt atnaatagag aaaaaataag attactatcc   4560  
               
               
                   
               
               
                 cttctatnga tgtnttataa tattttaatc cctttcnata tagattcacg tagaataaga   4620  
               
               
                   
               
               
                 aagattataa tcgcatcaaa tcaaatacag aatnaaatca tgcttttgac ttaattcgaa   4680  
               
               
                   
               
               
                 aaataatctt cctctcttga taatatcctt attgataagc attnttatat atatatatat   4740  
               
               
                   
               
               
                 ntatatcaac ttctaaaana tatttttaaa ttaattaaat ttatcaaaat aaaaagataa   4800  
               
               
                   
               
               
                 actaaattag ttctgcatca taatgtagta agtgtaagaa cttgtgaaat anggatctag   4860  
               
               
                   
               
               
                 aacactgata gaaaattcca aaccattact agttctactt gatgaaaaca aaaccatata   4920  
               
               
                   
               
               
                 aaagaatcct cttatatata tatatatata tatactactt tacttattct ttggacgtac   4980  
               
               
                   
               
               
                 aacacaagtc aggaaaccga aacaaaggtg gcggaaagtt ggcagangct gaagagactt   5040  
               
               
                   
               
               
                 ttcgtagaag tgaaggagac acacgtctat aagaattgtc atgactatac gctgaagaaa   5100  
               
               
                   
               
               
                 aagaggggag agagagagaa ggaagcgcca ctgttgaccg gtcttgtcca tgaggaattg   5160  
               
               
                   
               
               
                 tttgtcgact aatgagcagt acaaacattt gtgtcgacag atggcaacaa atgagaagcg   5220  
               
               
                   
               
               
                 gtatcccaac acgcaatctg tagcctttgg tcnccagact tatccaaaga cttgcctctg   5280  
               
               
                   
               
               
                 cgatttcctc atgcgcctca tctgttccaa aggaagcttc acagcgggca ggaatccatt   5340  
               
               
                   
               
               
                 tctctatata agcaccacct cccacccaca ccaccaccac caccaccact gctaaggagg   5400  
               
               
                   
               
               
                 atgaaggcct tgttgctggt catttttacc ctggcctcgt cgctcggcgc cttcgccgag   5460  
               
               
                   
               
               
                 caatgcggaa ggcaagccgg gggggctctc tgccccggcg ggctgtgctg tagccagtac   5520  
               
               
                   
               
               
                 ggctggtgcg gtaacacgga tccatnctgc ggtcaaggat gccanancca atgcncangc   5580  
               
               
                   
               
               
                 tccacgccct ccccttccac tccgagcggc ggtggcanng ttggctcgat catcatctcc   5640  
               
               
                   
               
               
                 tccctcttcn agcagatgct gaagcatcnc ancgacncag ccngccccgg caanggcttc   5700  
               
               
                   
               
               
                 tacncgtnca ccgccttcat ctccgccgcc anctccttca ncgggttcgg gacnaccngc   5760  
               
               
                   
               
               
                 gaccactcca cnaataanan gganatcncg gctttcttgg tncngacntc tcncgagacn   5820  
               
               
                   
               
               
                 acangtaatc cntncntctc ccgaggctcg tctncagntt atngatagac anctnaatgc   5880  
               
               
                   
               
               
                 attgggttng gcacgtgggt ggtccaccgt gcccnatggc cnttcgcgtg gggttactgc   5940  
               
               
                   
               
               
                 ttcgtccagn aacagaaccc tcatcggact actgcgtcgc cagctcgcan tggccgtgcg   6000  
               
               
                   
               
               
                 ctgcangcaa naaatactac ggccgaagcc ccatccaaat ctcattcaac tacaactacg   6060  
               
               
                   
               
               
                 ggccggccgg gaaaaccatc ggctccgacc tgctcaacaa cccagacctg gtggccaccg   6120  
               
               
                   
               
               
                 acccgaccat ctccttcaag acggctctgt ggttctggat gactcctcag tcgcccaagc   6180  
               
               
                   
               
               
                 cgtcgtgcca cgacgtgata accgggagct ggacgccatc caacgccgac cgggcggccg   6240  
               
               
                   
               
               
                 gaaggcttcc gggctacggt gtcaccacca acatcatcaa tggagggttg gagtgcggga   6300  
               
               
                   
               
               
                 aagggtccga tgccagggtg gcggatagga tcggcttcta caanaggtac tgcgacttgc   6360  
               
               
                   
               
               
                 tgggggtgag ctacggagac aacttggact gctacaacca nagtcccttt acttantccg   6420  
               
               
                   
               
               
                 atactatgtg cgaatccatg taataacgca ataaacgcta ctgctgaaat agcgactccg   6480  
               
               
                   
               
               
                 tgagttgatt gtagaagttg cggaggaaat cttcaataaa agctaagctg aacaagttca   6540  
               
               
                   
               
               
                 tggccctcaa tcatcgttga tcgtcgtcag atgcatccat caaatgtctt ggagtnagtn   6600  
               
               
                   
               
               
                 aatgcgtntt cnatcggtaa attgaagatg ttagaataaa taaaattatt tattttttat   6660  
               
               
                   
               
               
                 aattataaat attttaatat attttttaat cttaaagatc ctaaaaaatc tnattataag   6720  
               
               
                   
               
               
                 gattttatat atggattggg atactaanaa aanttnatta tnaaaattaa tatactttta   6780  
               
               
                   
               
               
                 atcttaagga tcctaaaaaa acataattat aaggattttc tatatggatn gggatactaa   6840  
               
               
                   
               
               
                 caanatntaa ttgtaaaaat ttnaatataa aattgttaaa tctaaaaatt aaaatactaa   6900  
               
               
                   
               
               
                 aaatatatan taatcatgat atcgagaatg tggcgcttag atctcgagat cgaggttgag   6960  
               
               
                   
               
               
                 actanagngg aaattatgtt aatcatggga aattttcttt tgtttccaag acgatgaccg   7020  
               
               
                   
               
               
                 tggaaaccta acatccgcaa tcggtcatgc aataaccatg ttatcatcan tgaacttgtc   7080  
               
               
                   
               
               
                 gtcgtcatct tacggccaca aatcacagtc ttctancaag gcacgaatat taatgagtcc   7140  
               
               
                   
               
               
                 aacgtagtat ctatattgtt ttacactttt ataccgtant cgaggtgttc gcacgatttg   7200  
               
               
                   
               
               
                 gcccatccca agtgcataag atcattgata tgacctctac gttggagcgt gttaacccga   7260  
               
               
                   
               
               
                 gatctagttg agggggcata ggtctcattt ntctacgtgg aggttaaaga tcacctttat   7320  
               
               
                   
               
               
                 tncanccctt gtagattcta aactngaggt ngatctctnt aggagatcgg tctcccttgg   7380  
               
               
                   
               
               
                 aactctntag gggtncc                                                  7397  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 23  
               
               
                 &lt;211&gt; LENGTH: 7397  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 82, 601, 628, 640, 655, 692, 725, 774, 793, 806, 813,  
               
               
                       854, 867, 870, 876, 882, 890, 919, 946, 959, 965, 995, 999, 1002,  
               
               
                       1028, 1043, 1054, 1075, 1093, 1515, 2166, 2216, 2265, 2345,  
               
               
                       2533, 2870, 2917, 3077, 3337, 3356, 3618, 3627, 3754  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 3810, 3819, 3884, 3893, 4494, 4503, 4524, 4533, 4568,  
               
               
                       4574, 4597, 4654, 4724, 4741, 4759, 4852, 5027, 5253, 5546, 5565,  
               
               
                       5567, 5575, 5578, 5618, 5619, 5650, 5669, 5672, 5677, 5683,  
               
               
                       5694, 5704, 5708, 5732, 5741, 5754, 5758, 5772, 5778  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 5780, 5784, 5788, 5802, 5804, 5808, 5813, 5820, 5824,  
               
               
                       5832, 5834, 5836, 5854, 5858, 5863, 5872, 5875, 5889, 5915, 5922,  
               
               
                       5950, 5990, 6006, 6011, 6344, 6401, 6416, 6596, 6600, 6608,  
               
               
                       6612, 6712, 6748, 6753, 6756, 6762, 6830, 6844, 6847  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 6863, 6910, 6965, 6968, 7070, 7116, 7179, 7291, 7322,  
               
               
                       7325, 7345, 7351, 7359, 7387, 7395  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 23  
               
               
                   
               
               
                 tcgctccagc tgattactcg atgattgtaa ttacagtgtc tatcattatc tactcttcgg     60  
               
               
                   
               
               
                 cataggtggt gcgttagaca tntgaaccag tgtcctgaag aataggtttc tgagcggaga    120  
               
               
                   
               
               
                 cgctaaaggg tgtaagtgga gtaaaccagg tatccttcga agtgtcgccc gtccttaggt    180  
               
               
                   
               
               
                 aaagagatat attcgtggtg gagggtgggt gtggtggtgg tgattggtga cgattcctcc    240  
               
               
                   
               
               
                 tacttccgga acaacaacca gtagaatggg accggagcag cgagccgcgg aagcggctcg    300  
               
               
                   
               
               
                 ttacgccttc cgttcggccc ccccgagaga cggggccgcc cgacacgaca tcggtcatgc    360  
               
               
                   
               
               
                 cgaccacgcc attgtgccta ggtatgacgc cggttcctac ggtctcggtt acgccgccat    420  
               
               
                   
               
               
                 cgccgccatc gccgccaccg tcgcaccgga gctagtagtc gaggagggag aagctcgtct    480  
               
               
                   
               
               
                 acgacttcgt agcgttgctg cgtcggacgg ggccgttccc aaagatgtgc atgttgcgga    540  
               
               
                   
               
               
                 agtagcggcg gcggttgagg aagtcgccca agccctgctg gccgctgctg ggttcttctt    600  
               
               
                   
               
               
                 nttcctctag cgccgaaaga accgcctntg cagagtgctn tgctgtccat taagngtgta    660  
               
               
                   
               
               
                 gagggcttcg agcatttgac aaatacccta tnttttgact tacaaacccc aaaccgtcca    720  
               
               
                   
               
               
                 cccanccgct gcgcgggcta ccaggcatgc ggaacccaat gacgaagcag gttnttgttt    780  
               
               
                   
               
               
                 tgggagtagc ctnatgacgc agggtngagg gtnaccggca cgcgacgtcg ttttttatga    840  
               
               
                   
               
               
                 tgccggcttc gggnaggttt aaagtancan tcggtntaag antgtcaagn agcggcgcta    900  
               
               
                   
               
               
                 gctcaagtgt tgctacggna aagattgcgt tgttaggcta cacaanacgc acgtcgttna    960  
               
               
                   
               
               
                 tgttnatgcc cggccggccc tctcggtagc caagnctgna cnagttgttg ggtctggacc   1020  
               
               
                   
               
               
                 accggtgnct gcgctggtag agnaagttct gccnagacac caaaacctac tgagnagtca   1080  
               
               
                   
               
               
                 gcgggttcgg cancacggtg ctgcactatt ggccctcgac ctgcggtagg ttgcggctgg   1140  
               
               
                   
               
               
                 tccgccggcc ttccgaaggc ccgatgccac agtggtggtt gtattattta cctcccaacc   1200  
               
               
                   
               
               
                 tcacgccctt tcccatgcta cggtcccacc gcctatccta gccgaagatg ttctccatga   1260  
               
               
                   
               
               
                 cgctgaacga cccccactcg atgcctctgt tgaacctgac gatgttggtc tctgggaaac   1320  
               
               
                   
               
               
                 gaagatgtcg tcgatgtcgg tgtaagatcg ccactcgata cctctgttga acctcacgat   1380  
               
               
                   
               
               
                 gttggtctct gggaaatgaa tcaggctatg atgacactgc ttaggtacat tattgcgtta   1440  
               
               
                   
               
               
                 tttgcgataa tgactctatc gctgaggcac tcaactgaca tcttcaacgc ctccttcaga   1500  
               
               
                   
               
               
                 agttattttc gaatngatgt atgtaccggg tgttgatagc aactggcact agtatacgta   1560  
               
               
                   
               
               
                 ggtagtttac aggagtttac agaacctcat tcatttacgc ataagctagc cattttactt   1620  
               
               
                   
               
               
                 ctacaatctt atttatttta attaataaaa aaatattaat atttataaaa ttatataaaa   1680  
               
               
                   
               
               
                 aattagaatt tctaggattt ttagattaat attcctaaaa tatataccta accctatgat   1740  
               
               
                   
               
               
                 tcttataaat taatattttt aattatatga aaaattagaa tttctagatt aatattcata   1800  
               
               
                   
               
               
                 aaagatatac ctaaccctat aattgagcta aatgaatatt tttaaaatta tatttttaaa   1860  
               
               
                   
               
               
                 atttaaattt ttaattttat gatttttata gatttatatt gccattagta ctctagctct   1920  
               
               
                   
               
               
                 tgcactacta actctagtac tctagctcca actctcattt ttcctttaat gcaattagta   1980  
               
               
                   
               
               
                 ccctttaaag caaaacaaac gtgccagctc taccactggc acctgtggat tgtaggtgtt   2040  
               
               
                   
               
               
                 ggccgtacgt tattggtaca acagtataca atcgaacaga gtatagaata ctggtactta   2100  
               
               
                   
               
               
                 gtgtatcaga agtgcttata attaattcgg tcgaatcgta gtgtcaaaac gtggaaacat   2160  
               
               
                   
               
               
                 ggtatngact tcacaagcat accgaactgg gtagggctca cataccagag ggcctnggac   2220  
               
               
                   
               
               
                 ctcgcacaat tgggctccag atcaactccc cgtatctgga acaanagaat ccgtctccaa   2280  
               
               
                   
               
               
                 cttctattga ggaaatcgat aggcaaccca cggatatatt tccagcttta gtactccccc   2340  
               
               
                   
               
               
                 taagnattga gctggataag ttataaactc gatcgttctc aacctcaatg cacatactcc   2400  
               
               
                   
               
               
                 aagctggggg ttacgacaag gaccccagcg aaaatatgga taaggacgta cactagtatg   2460  
               
               
                   
               
               
                 tatcatcgaa attagtagaa gtcagtagta gcatgcaacc cacgtacgta acagattaaa   2520  
               
               
                   
               
               
                 tgagctaagt tanagcaagc tgtgacgaag gatggatgat acaccgggtt atgtatcaac   2580  
               
               
                   
               
               
                 ataacagagt atgccggagc tcgtttcgca cacgtctcct tgacacagtt caccaaccga   2640  
               
               
                   
               
               
                 ccggagcccg agtaccgtaa ctcaaccgag ctatgttgtg tagccgaatc cctatggtac   2700  
               
               
                   
               
               
                 ggctcagata acaccatcaa ctgtacagta caccccacct acggttttat acagatatag   2760  
               
               
                   
               
               
                 taagagaggg tgtttcctca acacggtatc ctcttagcac ctgtgccgaa cccaagacac   2820  
               
               
                   
               
               
                 cagccaggaa caagcggagt caacccacct aatgaagtag ttcaaccggn agacaaccga   2880  
               
               
                   
               
               
                 cccgtttcat gtgaaccatc cctaccagct ctgttcnggt tccttccaac cgattctgaa   2940  
               
               
                   
               
               
                 ccaaaagctg ttagttaaca aatactccgc ttaccatagg gaggcaaccc cacagacgag   3000  
               
               
                   
               
               
                 caaagctaaa caacgctacc taacaaacaa catcctccga accaagctaa cgagaattca   3060  
               
               
                   
               
               
                 gccctcttcc ataaacnatt cctcaagtta aactggtaca acttcactta ttttcctgaa   3120  
               
               
                   
               
               
                 cggttcttca aaccgagctg gcacaatttc ggtctcttac acatacagct ccagataagt   3180  
               
               
                   
               
               
                 tggtacacct tcgatctctt acgtggttaa cactccaaac cgaacgagtg caaatttcgt   3240  
               
               
                   
               
               
                 cttcctatat gaacgatgct ccaaacgagt tggtacacct tcgttagttt acgtgaacga   3300  
               
               
                   
               
               
                 tactccaaac cgaactgaat gagctgttac ctgcgancat tcactcttcc ctgatnggtt   3360  
               
               
                   
               
               
                 ctgaatcaac cgttcctgat cagctatgaa cgagctgtta tctacggata tccattacct   3420  
               
               
                   
               
               
                 aactgactct gaatcagctg tttctgatcg actctgaatc acccgttacc tacggatatt   3480  
               
               
                   
               
               
                 cattctttcc taccgagctc taattatttc tagtttatta attatattta aatagtttgt   3540  
               
               
                   
               
               
                 gaattacctg cgtatattca ctctttcctg cctagctcta attatttcta gtttattaat   3600  
               
               
                   
               
               
                 tatattcaaa tagtttgnga ataattntgt aacctgtttt ctccatgata cattataatt   3660  
               
               
                   
               
               
                 ttaaccctcc gtgtttataa taaaggttta tgaaaagagg aattcgggaa gcggtggtaa   3720  
               
               
                   
               
               
                 cggtaaaatt agataaaaaa gatatattaa tagngtattg taagcatgta ctctatactg   3780  
               
               
                   
               
               
                 tatttggaag ctggacgaaa tcatttgtan aactaatanc actgtggtct tcggtattat   3840  
               
               
                   
               
               
                 aacgaatgga attgtactac ctctacttga aatcaaccag gttnatagat tanttacctt   3900  
               
               
                   
               
               
                 cacctgttcg tgctactgat cctaccgatg tacaagtaca caactgaaag gttcattagt   3960  
               
               
                   
               
               
                 tagttcgacc ttagcttatt ctgctaattt catcccgcta ctggtaattc aagttacagt   4020  
               
               
                   
               
               
                 gcgagtagtt gtattaaggt tgtggcacgt ctttctagaa tagaatgtaa ctgaacgggt   4080  
               
               
                   
               
               
                 aggccggcgg ccgtagctaa ccgcctttgc ttcccagtca gagggttaag tgtaagtttc   4140  
               
               
                   
               
               
                 ctgcttaagt aaaagtagtc tactcgtgaa gtcaggacga actaatataa aataataata   4200  
               
               
                   
               
               
                 ataataataa ttaacttacc attcaaatgt cttatatatc tataaaatca aagttatttt   4260  
               
               
                   
               
               
                 ataaaatttt ttactatttc cctcttccac ctaaactaga atcctaaaaa taacactcgt   4320  
               
               
                   
               
               
                 tattttcaga aatcaatctt gaaggtttta cacagtttac ttgggattat tcacccaaac   4380  
               
               
                   
               
               
                 cagataccaa tgctactcta gtcataaaca tatatttttt taatagttga actaaaaata   4440  
               
               
                   
               
               
                 aaaaattggg aattattcac ctgtactata tagtattagt ttagtacact acanactact   4500  
               
               
                   
               
               
                 cantattgta taaaaaatta ttanttttaa tanttatctc ttttttattc taatgatagg   4560  
               
               
                   
               
               
                 gaagatanct acanaatatt ataaaattag ggaaagntat atctaagtgc atcttattct   4620  
               
               
                   
               
               
                 ttctaatatt agcgtagttt agtttatgtc ttantttagt acgaaaactg aattaagctt   4680  
               
               
                   
               
               
                 tttattagaa ggagagaact attataggaa taactattcg taanaatata tatatatata   4740  
               
               
                   
               
               
                 natatagttg aagattttnt ataaaaattt aattaattta aatagtttta tttttctatt   4800  
               
               
                   
               
               
                 tgatttaatc aagacgtagt attacatcat tcacattctt gaacacttta tncctagatc   4860  
               
               
                   
               
               
                 ttgtgactat cttttaaggt ttggtaatga tcaagatgaa ctacttttgt tttggtatat   4920  
               
               
                   
               
               
                 tttcttagga gaatatatat atatatatat atatgatgaa atgaataaga aacctgcatg   4980  
               
               
                   
               
               
                 ttgtgttcag tcctttggct ttgtttccac cgcctttcaa ccgtctncga cttctctgaa   5040  
               
               
                   
               
               
                 aagcatcttc acttcctctg tgtgcagata ttcttaacag tactgatatg cgacttcttt   5100  
               
               
                   
               
               
                 ttctcccctc tctctctctt ccttcgcggt gacaactggc cagaacaggt actccttaac   5160  
               
               
                   
               
               
                 aaacagctga ttactcgtca tgtttgtaaa cacagctgtc taccgttgtt tactcttcgc   5220  
               
               
                   
               
               
                 catagggttg tgcgttagac atcggaaacc agnggtctga ataggtttct gaacggagac   5280  
               
               
                   
               
               
                 gctaaaggag tacgcggagt agacaaggtt tccttcgaag tgtcgcccgt ccttaggtaa   5340  
               
               
                   
               
               
                 agagatatat tcgtggtgga gggtgggtgt ggtggtggtg gtggtggtga cgattcctcc   5400  
               
               
                   
               
               
                 tacttccgga acaacgacca gtaaaaatgg gaccggagca gcgagccgcg gaagcggctc   5460  
               
               
                   
               
               
                 gttacgcctt ccgttcggcc cccccgagag acggggccgc ccgacacgac atcggtcatg   5520  
               
               
                   
               
               
                 ccgaccacgc cattgtgcct aggtangacg ccagttccta cggtntnggt tacgngtncg   5580  
               
               
                   
               
               
                 aggtgcggga ggggaaggtg aggctcgccg ccaccgtnnc aaccgagcta gtagtagagg   5640  
               
               
                   
               
               
                 agggagaagn tcgtctacga cttcgtagng tngctgngtc ggncggggcc gttnccgaag   5700  
               
               
                   
               
               
                 atgngcangt ggcggaagta gaggcggcgg tngaggaagt ngcccaagcc ctgntggncg   5760  
               
               
                   
               
               
                 ctggtgaggt gnttattntn cctntagngc cgaaagaacc angnctgnag agngctctgn   5820  
               
               
                   
               
               
                 tgtncattag gnangnagag ggctccgagc agangtcnaa tanctatctg tnganttacg   5880  
               
               
                   
               
               
                 taacccaanc cgtgcaccca ccaggtggca cgggntaccg gnaagcgcac cccaatgacg   5940  
               
               
                   
               
               
                 aagcaggtcn ttgtcttggg agtagcctga tgacgcagcg gtcgagcgtn accggcacgc   6000  
               
               
                   
               
               
                 gacgtncgtt ntttatgatg ccggcttcgg ggtaggttta gagtaagttg atgttgatgc   6060  
               
               
                   
               
               
                 ccggccggcc cttttggtag ccgaggctgg acgagttgtt gggtctggac caccggtggc   6120  
               
               
                   
               
               
                 tgggctggta gaggaagttc tgccgagaca ccaagaccta ctgaggagtc agcgggttcg   6180  
               
               
                   
               
               
                 gcagcacggt gctgcactat tggccctcga cctgcggtag gttgcggctg gcccgccggc   6240  
               
               
                   
               
               
                 cttccgaagg cccgatgcca cagtggtggt tgtagtagtt acctcccaac ctcacgccct   6300  
               
               
                   
               
               
                 ttcccaggct acggtcccac cgcctatcct agccgaagat gttntccatg acgctgaacg   6360  
               
               
                   
               
               
                 acccccactc gatgcctctg ttgaacctga cgatgttggt ntcagggaaa tgaatnaggc   6420  
               
               
                   
               
               
                 tatgatacac gcttaggtac attattgcgt tatttgcgat gacgacttta tcgctgaggc   6480  
               
               
                   
               
               
                 actcaactaa catcttcaac gcctccttta gaagttattt tcgattcgac ttgttcaagt   6540  
               
               
                   
               
               
                 accgggagtt agtagcaact agcagcagtc tacgtaggta gtttacagaa cctcantcan   6600  
               
               
                   
               
               
                 ttacgcanaa gntagccatt taacttctac aatcttattt attttaataa ataaaaaata   6660  
               
               
                   
               
               
                 ttaatattta taaaattata taaaaaatta gaatttctag gattttttag antaatattc   6720  
               
               
                   
               
               
                 ctaaaatata tacctaaccc tatgattntt ttnaantaat anttttaatt atatgaaaat   6780  
               
               
                   
               
               
                 tagaattcct aggatttttt tgtattaata ttcctaaaag atatacctan ccctatgatt   6840  
               
               
                   
               
               
                 gttntanatt aacattttta aanttatatt ttaacaattt agatttttaa ttttatgatt   6900  
               
               
                   
               
               
                 tttatatatn attagtacta tagctcttac accgcgaatc tagagctcta gctccaactc   6960  
               
               
                   
               
               
                 tgatntcncc tttaatacaa ttagtaccct ttaaaagaaa acaaaggttc tgctactggc   7020  
               
               
                   
               
               
                 acctttggat tgtaggcgtt agccagtacg ttattggtac aatagtagtn acttgaacag   7080  
               
               
                   
               
               
                 cagcagtaga atgccggtgt ttagtgtcag aagatngttc cgtgcttata attactcagg   7140  
               
               
                   
               
               
                 ttgcatcata gatataacaa aatgtgaaaa tatggcatna gctccacaag cgtgctaaac   7200  
               
               
                   
               
               
                 cgggtagggt tcacgtattc tagtaactat actggagatg caacctcgca caattgggct   7260  
               
               
                   
               
               
                 ctagatcaac tcccccgtat ccagagtaaa nagatgcacc tccaatttct agtggaaata   7320  
               
               
                   
               
               
                 angtngggaa catctaagat ttganctcca nctagagana tcctctagcc agagggaacc   7380  
               
               
                   
               
               
                 ttgaganatc cccangg                                                  7397  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 24  
               
               
                 &lt;211&gt; LENGTH: 2326  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 25, 164, 173, 177, 181, 193, 204, 220, 227, 231, 233,  
               
               
                       247, 251, 254, 259, 269, 278, 282, 284, 294, 296, 305, 310, 314,  
               
               
                       320, 326, 458, 656, 673, 687, 713, 774, 883, 899, 952, 1038,  
               
               
                       1043, 1163, 1180, 1183, 1202, 1204, 1397, 1400, 1412  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 1414, 1422, 1441, 1462, 1468, 1474, 1504, 1559, 1729,  
               
               
                       1735, 1736, 1739, 1740, 1753, 1764, 1770, 1771, 1773, 1775, 1778,  
               
               
                       1782, 1783, 1791, 1794, 1800, 1806, 1807, 1808, 1810, 1815,  
               
               
                       1818, 1822, 1825, 1826, 1832, 1833, 1835, 1837, 1838  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 1842, 1851, 1863, 1876, 1881, 1883, 1991, 2009, 2014,  
               
               
                       2071, 2075, 2109, 2120, 2121, 2122, 2124, 2147, 2151, 2152, 2157,  
               
               
                       2169, 2187, 2188, 2221, 2236, 2257, 2293, 2303, 2304, 2310,  
               
               
                       2312, 2323  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 24  
               
               
                   
               
               
                 Ser Glu Val Asp Ala Thr Asn Ile Asn Val Thr Asp Ser Asn Arg Glu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ala Val Ser Asn Thr Gln Ser Val Xaa Leu Val Thr Gly Leu Leu Ile  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Gln Arg Leu Ala Ser Ala Ile Ser His Ile His Leu Ile Trp Ser Ile  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Gly Ser Phe Thr Ala Gly Arg Asn Pro Phe Leu Tyr Ile Ser Thr Thr  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Asn Ala Glu Gly Lys Pro Gly Gly Leu Ser Ala Pro Ala Gly Cys Ala  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Val Ala Ser Thr Ala Gly Ala Val Thr Arg Ile His Thr Ala Ala Lys  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Ala Arg Ala Asn Ala Ala Val Ala Ala Val Ala Ala Val Ala Ala  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Trp Pro Arg Ser Ser Ala Pro Pro Ser Ser Ser Arg Cys Ser Ile Ala  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Thr Thr Gln Pro Ala Pro Ala Arg Val Ser Thr Arg Thr Thr Pro Ser  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Ser Pro Pro Pro Thr Pro Ser Ala Gly Ser Gly Arg Pro Ala Thr Thr  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Gln Glu Glu Xaa Gly Asp Arg Gly Phe Leu Gly Ala Xaa Val Ser Arg  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Xaa Asp Arg Phe Xaa His Leu Pro Lys Leu Val Asn Cys Leu Trp Asp  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Xaa Lys Leu Asn Val Trp Gly Leu Ala Gly Gly Xaa Ala Thr Arg Pro  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Met Val Arg Thr Pro Trp Val Thr Ala Ser Ser Xaa Asn Lys Thr Leu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ile Gly Xaa Leu Arg Pro Xaa Ser Xaa Trp Pro Cys Ala Ala Ala Lys  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Asn Thr Thr Ala Glu Ala Xaa Pro Asn Phe Xaa Val Ser Xaa Ile Leu  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Thr Val Xaa Arg Arg Asp Arg Val His Asn Asp Ala Xaa Ser Asn Ala  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Thr Ile Arg Cys Val Xaa Arg Ala Ala Xaa Thr Xaa Thr Gly Arg Pro  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Gly Glu Pro Ser Val Xaa Thr Xaa Ser Thr Thr Gln Thr Trp Trp Pro  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Xaa Thr Arg Pro Ser Xaa Ser Arg Arg Xaa Cys Gly Phe Gly Leu Xaa  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Ser Arg Pro Ser Arg Xaa Ala Thr Thr Pro Gly Ala Gly Arg His Pro  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Thr Pro Thr Arg Arg Pro Glu Gly Phe Arg Ala Thr Val Ser Pro Pro  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Thr Ser Ser Met Glu Gly Trp Ser Ala Gly Lys Gly Thr Met Pro Gly  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Trp Arg Ile Gly Ser Ala Ser Thr Arg Gly Thr Ala Thr Cys Trp Gly  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Ala Thr Glu Thr Thr Trp Thr Ala Thr Thr Arg Asp Pro Leu Leu Leu  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gln Gln Leu Gln Pro His Ser Ser Gly Glu Leu Trp Arg Gln Leu Gly  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Val Leu Gln Pro Glu Thr Leu Tyr Leu Val Arg Tyr Tyr Cys Asp Glu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Ser Met Arg Asn Lys Arg Tyr Tyr Asp Ser Asp Ser Val Ser Leu Lys  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Leu Arg Arg Lys Ser Ser Ile Lys Ala Xaa Leu His Thr Trp Pro Thr  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Thr Ile Val Asp Arg Asp His Met His Pro Ser Asn Val Leu Lys Cys  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Leu Gly Val Ser Lys Cys Val Phe Asp Arg Asn Glu Asp Val Arg Ile  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Asn Lys Ile Asn Tyr Phe Phe Ile Ile Ile Asn Ile Leu Ile Tyr Phe  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Leu Ile Leu Lys Ile Leu Lys Ile Leu Gly Phe Tyr Ile Trp Ile Gly  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ile Leu Arg Ile Phe Asn Tyr Lys Asn Tyr Thr Phe Ser Arg Ser Asn  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Tyr Lys Tyr Phe Leu Tyr Gly Leu Gly Tyr Leu Asp Leu Leu Ile Lys  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ile Leu Ile Lys Phe Ile Lys Leu Lys Tyr Lys Tyr Leu Asn Ile Thr  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Val Ile Met Arg Ser Arg Thr Leu Arg Ser Asp Arg Gly Glu Lys Gly  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Asn Tyr Val Asn His Gly Lys Phe Arg Phe Val Cys Thr Val Glu Met  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Val Thr Val Asp Thr His Pro Gln Pro Ala Cys Asn Asn His Val Val  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Ile Cys Leu Val Ser Tyr Leu Met Thr Met Asn His Ile Val Phe Thr  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Asn Ile Asn Ala Ser Leu Ala Ser Gln Phe Cys Thr Phe Val Pro Xaa  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                 Leu Lys Cys Ser Tyr Gly Leu Thr His Pro Glu Cys Met Val Ser Arg  
               
               
                             660                 665                 670  
               
               
                   
               
               
                 Xaa Leu Glu Arg Val Asn Pro Arg Ser Ser Gly Ala Thr Leu Xaa Ser  
               
               
                         675                 680                 685  
               
               
                   
               
               
                 Ala Glu Val Glu Asp His Ser Phe Ser Tyr Pro Leu Gly Ala Tyr Ile  
               
               
                     690                 695                 700  
               
               
                   
               
               
                 Lys Val Glu Ile Met Arg Gly Ile Xaa Asn Ser Thr Tyr Ser Ile Phe  
               
               
                 705                 710                 715                 720  
               
               
                   
               
               
                 Glu Leu Ala Arg Val Gly Val Thr Cys Met Arg Phe Asp Pro Gln Cys  
               
               
                                 725                 730                 735  
               
               
                   
               
               
                 Ser Ser Trp Gly Arg Phe Tyr Thr Tyr Ser Cys Met Ser Tyr Ile Val  
               
               
                             740                 745                 750  
               
               
                   
               
               
                 Ala Leu Ile Ile Phe Ser His His Arg Thr Leu Gly Ala Cys Ile Val  
               
               
                         755                 760                 765  
               
               
                   
               
               
                 Phe Thr Arg Phe Asn Xaa Val Arg His Cys Phe Leu Pro Thr Met Trp  
               
               
                     770                 775                 780  
               
               
                   
               
               
                 Pro Asn Thr Leu Tyr Cys Leu Ile Arg Pro Arg Ala Lys Arg Val Gln  
               
               
                 785                 790                 795                 800  
               
               
                   
               
               
                 Arg Asn Cys Val Lys Trp Leu Ala Gly Leu Gly Leu Met Ala Leu Ser  
               
               
                                 805                 810                 815  
               
               
                   
               
               
                 Trp Leu Asp Thr Thr His Arg Leu Arg Asp Thr Met Pro Ser Leu Leu  
               
               
                             820                 825                 830  
               
               
                   
               
               
                 Trp Leu Thr Cys His Val Gly Trp Met Pro Lys Tyr Ala Ile Ser Phe  
               
               
                         835                 840                 845  
               
               
                   
               
               
                 Ser Pro Tyr Lys Gly Val Val Pro Glu Asn Arg Gly His Gly Leu Gly  
               
               
                     850                 855                 860  
               
               
                   
               
               
                 Ser Val Val Gly Pro Cys Ser Pro Gln Leu Gly Gly Leu Leu His Gln  
               
               
                 865                 870                 875                 880  
               
               
                   
               
               
                 Val Gly Xaa Leu Leu Ala Gly Gln Ser Thr Leu Gly Arg Asp Gly Arg  
               
               
                                 885                 890                 895  
               
               
                   
               
               
                 Asp Lys Xaa Lys Glu Gly Trp Leu Arg Leu Gly Phe Arg Gln Ser Ile  
               
               
                             900                 905                 910  
               
               
                   
               
               
                 Val Tyr Glu Ala Asn Gly Ile Pro Pro Leu Gly Cys Leu Leu Val Ser  
               
               
                         915                 920                 925  
               
               
                   
               
               
                 Ile Cys Cys Asp Gly Leu Phe Val Val Gly Gly Leu Val Arg Leu Leu  
               
               
                     930                 935                 940  
               
               
                   
               
               
                 Leu Ser Arg Glu Lys Val Phe Xaa Lys Glu Phe Asn Leu Thr Met Leu  
               
               
                 945                 950                 955                 960  
               
               
                   
               
               
                 Lys Ile Lys Gly Leu Ala Lys Lys Phe Gly Ser Thr Val Leu Lys Pro  
               
               
                                 965                 970                 975  
               
               
                   
               
               
                 Glu Asn Val Tyr Val Glu Val Tyr Ser Thr Met Trp Lys Leu Glu Asn  
               
               
                             980                 985                 990  
               
               
                   
               
               
                 Ala Pro Ile Val Arg Phe Gly Leu Leu Thr Phe Lys Ala Glu Gly Tyr  
               
               
                         995                 1000                1005  
               
               
                   
               
               
                 Thr Cys Tyr Glu Val Cys Ser Thr Met Trp Lys Gln Ser Asn Ala Leu  
               
               
                     1010                1015                1020  
               
               
                   
               
               
                 Ala Met Arg Phe Gly Leu Thr Tyr Ser Thr Met Asp Ala Xaa Lys Glu  
               
               
                 1025                1030                1035                1040  
               
               
                   
               
               
                 Gly Thr Xaa Gln Asp Leu Val Gly Lys Asp Ser Ile Leu Ala Arg Gln  
               
               
                                 1045                1050                1055  
               
               
                   
               
               
                 Met Pro Ile Gly Asn Gly Leu Thr Glu Thr Ser Thr Lys Thr Ser Asp  
               
               
                             1060                1065                1070  
               
               
                   
               
               
                 Leu Val Gly Asn Gly Cys Leu Val Arg Lys Asp Gly Ser Arg Leu Ile  
               
               
                         1075                1080                1085  
               
               
                   
               
               
                 Lys Ile Lys Leu Ile Ile Tyr Gln Thr Leu Asn Gly Arg Ile Val Arg  
               
               
                     1090                1095                1100  
               
               
                   
               
               
                 Lys Asp Gly Ser Arg Leu Ile Lys Ile Lys Leu Ile Val Tyr Gln Thr  
               
               
                 1105                1110                1115                1120  
               
               
                   
               
               
                 Leu Ile Thr Leu Asp Lys Arg Gly Thr Met Tyr Asn Trp Glu Ala Gln  
               
               
                                 1125                1130                1135  
               
               
                   
               
               
                 Ile Leu Phe Pro Asn Thr Phe Leu Leu Lys Pro Phe Ala Thr Ile Ala  
               
               
                             1140                1145                1150  
               
               
                   
               
               
                 Ile Leu Ile Tyr Phe Phe Tyr Ile Ile Ile Xaa His Ser Tyr Met Arg  
               
               
                         1155                1160                1165  
               
               
                   
               
               
                 Tyr Asp Ile Asn Leu Arg Pro Ala Leu Val Asn Xaa Leu Ile Xaa Val  
               
               
                     1170                1175                1180  
               
               
                   
               
               
                 Thr Pro Glu Ala Ile Ile Leu Thr Leu Thr Trp Arg Thr Leu Val Gly  
               
               
                 1185                1190                1195                1200  
               
               
                   
               
               
                 Pro Xaa Ile Xaa Met Glu Val Asp Lys His Asp Asp Asp Gly Tyr Met  
               
               
                                 1205                1210                1215  
               
               
                   
               
               
                 Phe Met Cys Leu Ser Lys Ser Ile Lys Leu Glu Ser Asn Lys Thr Ile  
               
               
                             1220                1225                1230  
               
               
                   
               
               
                 Lys Val Gly Arg Pro Leu Ser Ser Met Ser Arg Ser Ser Thr Phe Gln  
               
               
                         1235                1240                1245  
               
               
                   
               
               
                 His Arg Ala Glu Arg Ser Tyr Leu Thr Leu Thr Cys Pro Ser Gly Arg  
               
               
                     1250                1255                1260  
               
               
                   
               
               
                 Arg His Arg Leu Ala Glu Thr Lys Gly Gln Ser Pro Asn Ser His Ser  
               
               
                 1265                1270                1275                1280  
               
               
                   
               
               
                 Lys Asp Glu Phe Ile Phe Ile Arg Ala Leu Gln Ser Cys Leu Ile Ile  
               
               
                                 1285                1290                1295  
               
               
                   
               
               
                 Phe Tyr Tyr Tyr Tyr Tyr Tyr Leu Asn Gly Lys Phe Thr Glu Tyr Ile  
               
               
                             1300                1305                1310  
               
               
                   
               
               
                 Asp Ile Leu Val Ser Ile Lys Tyr Phe Lys Lys Arg Glu Lys Val Asp  
               
               
                         1315                1320                1325  
               
               
                   
               
               
                 Leu Ile Leu Gly Phe Leu Leu Ala Ile Lys Val Phe Ser Asn Phe Gln  
               
               
                     1330                1335                1340  
               
               
                   
               
               
                 Asn Val Ser Asn Glu Pro Val Gly Leu Val Tyr Gly Tyr Asp Glu Ile  
               
               
                 1345                1350                1355                1360  
               
               
                   
               
               
                 Ser Ile Cys Ile Lys Asn Tyr Gln Leu Asp Phe Tyr Phe Leu Thr Leu  
               
               
                                 1365                1370                1375  
               
               
                   
               
               
                 Asn Lys Trp Thr Tyr Ile Ile Ile Lys Ser Cys Asp Val Val Ile Thr  
               
               
                             1380                1385                1390  
               
               
                   
               
               
                 Tyr Phe Leu Ile Xaa Lys Ile Xaa Asn Arg Glu Lys Ile Arg Leu Leu  
               
               
                         1395                1400                1405  
               
               
                   
               
               
                 Ser Leu Leu Xaa Met Xaa Tyr Asn Ile Leu Ile Pro Phe Xaa Ile Asp  
               
               
                     1410                1415                1420  
               
               
                   
               
               
                 Ser Arg Arg Ile Arg Lys Ile Ile Ile Ala Ser Asn Gln Ile Gln Asn  
               
               
                 1425                1430                1435                1440  
               
               
                   
               
               
                 Xaa Ile Met Leu Leu Thr Phe Glu Lys Ser Ser Ser Leu Asp Asn Ile  
               
               
                                 1445                1450                1455  
               
               
                   
               
               
                 Leu Ile Asp Lys His Xaa Tyr Ile Tyr Ile Tyr Xaa Tyr Gln Leu Leu  
               
               
                             1460                1465                1470  
               
               
                   
               
               
                 Lys Xaa Ile Phe Lys Leu Ile Lys Phe Ile Lys Ile Lys Arg Thr Lys  
               
               
                         1475                1480                1485  
               
               
                   
               
               
                 Leu Val Leu His His Asn Val Val Ser Val Arg Thr Cys Glu Ile Xaa  
               
               
                     1490                1495                1500  
               
               
                   
               
               
                 Ile Asn Thr Asp Arg Lys Phe Gln Thr Ile Thr Ser Ser Thr Lys Gln  
               
               
                 1505                1510                1515                1520  
               
               
                   
               
               
                 Asn His Ile Lys Glu Ser Ser Tyr Ile Tyr Ile Tyr Ile Tyr Thr Thr  
               
               
                                 1525                1530                1535  
               
               
                   
               
               
                 Leu Leu Ile Leu Trp Thr Tyr Asn Thr Ser Gln Glu Thr Glu Thr Lys  
               
               
                             1540                1545                1550  
               
               
                   
               
               
                 Val Ala Glu Ser Trp Gln Xaa Leu Lys Arg Leu Phe Val Glu Val Lys  
               
               
                         1555                1560                1565  
               
               
                   
               
               
                 Glu Thr His Val Tyr Lys Asn Cys His Asp Tyr Thr Leu Lys Lys Lys  
               
               
                     1570                1575                1580  
               
               
                   
               
               
                 Arg Gly Glu Arg Glu Lys Glu Ala Pro Leu Leu Thr Gly Leu Val His  
               
               
                 1585                1590                1595                1600  
               
               
                   
               
               
                 Glu Glu Leu Phe Val Asp Ala Val Gln Thr Phe Val Ser Thr Asp Gly  
               
               
                                 1605                1610                1615  
               
               
                   
               
               
                 Asn Lys Glu Ala Val Ser Gln His Ala Ile Cys Ser Leu Trp Ser Pro  
               
               
                             1620                1625                1630  
               
               
                   
               
               
                 Asp Leu Ser Lys Asp Leu Pro Leu Arg Phe Pro His Ala Pro His Leu  
               
               
                         1635                1640                1645  
               
               
                   
               
               
                 Phe Gln Arg Lys Leu His Ser Gly Gln Glu Ser Ile Ser Leu Tyr Lys  
               
               
                     1650                1655                1660  
               
               
                   
               
               
                 His His Leu Pro Pro Thr Pro Pro Pro Pro Pro Pro Leu Leu Arg Arg  
               
               
                 1665                1670                1675                1680  
               
               
                   
               
               
                 Met Lys Ala Leu Leu Leu Val Ile Phe Thr Leu Ala Ser Ser Leu Gly  
               
               
                                 1685                1690                1695  
               
               
                   
               
               
                 Ala Phe Ala Glu Gln Cys Gly Arg Gln Ala Gly Gly Ala Leu Cys Pro  
               
               
                             1700                1705                1710  
               
               
                   
               
               
                 Gly Gly Leu Cys Cys Ser Gln Tyr Gly Trp Cys Gly Asn Thr Asp Pro  
               
               
                         1715                1720                1725  
               
               
                   
               
               
                 Xaa Cys Gly Gln Gly Cys Xaa Xaa Gln Cys Xaa Xaa Ser Thr Pro Ser  
               
               
                     1730                1735                1740  
               
               
                   
               
               
                 Pro Ser Thr Pro Ser Gly Gly Gly Xaa Val Gly Ser Ile Ile Ile Ser  
               
               
                 1745                1750                1755                1760  
               
               
                   
               
               
                 Ser Leu Phe Xaa Gln Met Leu Lys His Xaa Xaa Asp Xaa Ala Xaa Pro  
               
               
                                 1765                1770                1775  
               
               
                   
               
               
                 Gly Xaa Gly Phe Tyr Xaa Xaa Thr Ala Phe Ile Ser Ala Ala Xaa Ser  
               
               
                             1780                1785                1790  
               
               
                   
               
               
                 Phe Xaa Gly Phe Gly Thr Thr Xaa Asp His Ser Thr Asn Xaa Xaa Xaa  
               
               
                         1795                1800                1805  
               
               
                   
               
               
                 Ile Xaa Ala Phe Leu Val Xaa Thr Ser Xaa Glu Thr Thr Xaa Asn Pro  
               
               
                     1810                1815                1820  
               
               
                   
               
               
                 Xaa Xaa Ser Arg Gly Ser Ser Xaa Xaa Tyr Xaa Thr Xaa Xaa Cys Ile  
               
               
                 1825                1830                1835                1840  
               
               
                   
               
               
                 Gly Xaa Gly Thr Trp Val Val His Arg Ala Xaa Trp Pro Phe Ala Trp  
               
               
                                 1845                1850                1855  
               
               
                   
               
               
                 Gly Tyr Cys Phe Val Gln Xaa Gln Asn Pro His Arg Thr Thr Ala Ser  
               
               
                             1860                1865                1870  
               
               
                   
               
               
                 Pro Ala Arg Xaa Gly Arg Ala Leu Xaa Ala Xaa Asn Thr Thr Ala Glu  
               
               
                         1875                1880                1885  
               
               
                   
               
               
                 Ala Pro Ser Lys Ser His Ser Thr Thr Thr Thr Gly Arg Pro Gly Lys  
               
               
                     1890                1895                1900  
               
               
                   
               
               
                 Pro Ser Ala Pro Thr Cys Ser Thr Thr Gln Thr Trp Trp Pro Pro Thr  
               
               
                 1905                1910                1915                1920  
               
               
                   
               
               
                 Arg Pro Ser Pro Ser Arg Arg Leu Cys Gly Ser Gly Leu Leu Ser Arg  
               
               
                                 1925                1930                1935  
               
               
                   
               
               
                 Pro Ser Arg Arg Ala Thr Thr Pro Gly Ala Gly Arg His Pro Thr Pro  
               
               
                             1940                1945                1950  
               
               
                   
               
               
                 Thr Gly Arg Pro Glu Gly Phe Arg Ala Thr Val Ser Pro Pro Thr Ser  
               
               
                         1955                1960                1965  
               
               
                   
               
               
                 Ser Met Glu Gly Trp Ser Ala Gly Lys Gly Pro Met Pro Gly Trp Arg  
               
               
                     1970                1975                1980  
               
               
                   
               
               
                 Ile Gly Ser Ala Ser Thr Xaa Gly Thr Ala Thr Cys Trp Gly Ala Thr  
               
               
                 1985                1990                1995                2000  
               
               
                   
               
               
                 Glu Thr Thr Trp Thr Ala Thr Thr Xaa Val Pro Leu Leu Xaa Pro Ile  
               
               
                                 2005                2010                2015  
               
               
                   
               
               
                 Leu Cys Ala Asn Pro Cys Asn Asn Ala Ile Asn Ala Thr Ala Glu Ile  
               
               
                             2020                2025                2030  
               
               
                   
               
               
                 Ala Thr Pro Val Asp Cys Arg Ser Cys Gly Gly Asn Leu Gln Lys Leu  
               
               
                         2035                2040                2045  
               
               
                   
               
               
                 Ser Thr Ser Ser Trp Pro Ser Ile Ile Val Asp Arg Arg Gln Met His  
               
               
                     2050                2055                2060  
               
               
                   
               
               
                 Pro Ser Asn Val Leu Glu Xaa Val Asn Ala Xaa Ser Ile Gly Lys Leu  
               
               
                 2065                2070                2075                2080  
               
               
                   
               
               
                 Lys Met Leu Glu Ile Lys Leu Phe Ile Phe Tyr Asn Tyr Lys Tyr Phe  
               
               
                                 2085                2090                2095  
               
               
                   
               
               
                 Asn Ile Phe Phe Asn Leu Lys Asp Pro Lys Lys Ser Xaa Tyr Lys Asp  
               
               
                             2100                2105                2110  
               
               
                   
               
               
                 Phe Ile Tyr Gly Leu Gly Tyr Xaa Xaa Xaa Ile Xaa Lys Ile Asn Ile  
               
               
                         2115                2120                2125  
               
               
                   
               
               
                 Leu Leu Ile Leu Arg Ile Leu Lys Lys His Asn Tyr Lys Asp Phe Leu  
               
               
                     2130                2135                2140  
               
               
                   
               
               
                 Tyr Gly Xaa Gly Tyr Gln Xaa Xaa Ile Val Lys Ile Xaa Ile Asn Cys  
               
               
                 2145                2150                2155                2160  
               
               
                   
               
               
                 Ile Lys Leu Lys Tyr Lys Tyr Ile Xaa Ile Met Ile Ser Arg Met Trp  
               
               
                                 2165                2170                2175  
               
               
                   
               
               
                 Arg Leu Asp Leu Glu Ile Glu Val Glu Thr Xaa Xaa Glu Ile Met Leu  
               
               
                             2180                2185                2190  
               
               
                   
               
               
                 Ile Met Gly Asn Phe Leu Leu Phe Pro Arg Arg Pro Trp Lys Pro Asn  
               
               
                         2195                2200                2205  
               
               
                   
               
               
                 Ile Arg Asn Arg Ser Cys Asn Asn His Val Ile Ile Xaa Glu Leu Val  
               
               
                     2210                2215                2220  
               
               
                   
               
               
                 Val Val Ile Leu Arg Pro Gln Ile Thr Val Phe Xaa Gln Gly Thr Asn  
               
               
                 2225                2230                2235                2240  
               
               
                   
               
               
                 Ile Asn Glu Ser Asn Val Val Ser Ile Leu Phe Tyr Thr Phe Ile Pro  
               
               
                                 2245                2250                2255  
               
               
                   
               
               
                 Xaa Ser Arg Cys Ser His Asp Leu Ala His Pro Lys Cys Ile Arg Ser  
               
               
                             2260                2265                2270  
               
               
                   
               
               
                 Leu Ile Pro Leu Arg Trp Ser Val Leu Thr Arg Asp Leu Val Glu Gly  
               
               
                         2275                2280                2285  
               
               
                   
               
               
                 Ala Val Ser Phe Xaa Tyr Val Glu Val Lys Asp His Leu Tyr Xaa Xaa  
               
               
                     2290                2295                2300  
               
               
                   
               
               
                 Pro Cys Arg Phe Thr Xaa Gly Xaa Ser Leu Glu Ile Gly Leu Pro Trp  
               
               
                 2305                2310                2315                2320  
               
               
                   
               
               
                 Asn Ser Xaa Gly Val Pro  
               
               
                                 2325  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 25  
               
               
                 &lt;211&gt; LENGTH: 2258  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 27, 160, 169, 173, 190, 200, 216, 222, 227, 229, 243,  
               
               
                       247, 248, 250, 252, 255, 273, 278, 280, 290, 291, 292, 301, 306,  
               
               
                       459, 654, 669, 685, 710, 767, 878, 893, 944, 1029, 1104,  
               
               
                       1107, 1162, 1164, 1182, 1185, 1372, 1375, 1379, 1382, 1393  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 1395, 1417, 1440, 1445, 1450, 1475, 1533, 1666, 1672,  
               
               
                       1673, 1676, 1690, 1706, 1707, 1714, 1719, 1727, 1730, 1734, 1740,  
               
               
                       1742, 1743, 1744, 1750, 1751, 1752, 1754, 1756, 1757, 1760,  
               
               
                       1761, 1769, 1770, 1773, 1779, 1788, 1790, 1799, 1813  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 1818, 1820, 1930, 1949, 1954, 2011, 2012, 2015, 2016,  
               
               
                       2058, 2060, 2061, 2063, 2083, 2087, 2088, 2092, 2106, 2122, 2123,  
               
               
                       2156, 2171, 2191, 2224, 2235, 2236, 2247, 2258  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 25  
               
               
                   
               
               
                 Ala Arg Ser Thr Asn Glu Leu Leu Thr Leu Met Ser Gln Ile Val Ile  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Asp Glu Lys Pro Tyr Pro Thr Arg Asn Leu Xaa Thr Trp Ser Gln Asp  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Phe Leu Ser Lys Asp Ser Pro Leu Arg Phe Pro Thr Phe Thr Ser Phe  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Gly Pro Glu Ala Ser Gln Arg Ala Gly Ile His Phe Ser Ile Ala Pro  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Met Arg Lys Ala Ser Arg Gly Gly Ser Leu Pro Arg Arg Ala Val Leu  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Pro Val Arg Leu Val Arg His Gly Ser Ile Leu Arg Pro Arg Met Pro  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Glu Pro Met Arg Arg Arg Arg Arg Arg Trp Gln Arg Gly Leu Asp His  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Gln Leu Leu Pro Leu Arg Ala Asp Ala Glu Ala Ser Gln Arg Arg Ser  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Leu Pro Arg Gln Gly Phe Leu His Val Gln Arg Leu His Arg Arg Arg  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Gln Leu Leu Gln Arg Val Arg Asp Asp Arg Arg Arg Pro Lys Lys Xaa  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Lys Glu Ile Ala Ala Phe Leu Ala Xaa Thr Ser His Xaa Thr Thr Gly  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Asn Ser His Ile Ser Arg Ser Ser Thr Val Tyr Gly Ile Xaa Asn Met  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Phe Gly Val Trp Gln Val Gly Xaa Arg Arg Ala Arg Trp Ser Val Arg  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Leu Gly Leu Leu Leu Arg Pro Xaa Thr Lys Pro Ser Ser Xaa Tyr Cys  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Val Pro Xaa Pro Xaa Gly Arg Ala Leu Gln Gln Lys Ile Leu Arg Pro  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Lys Pro Xaa Gln Ile Ser Xaa Xaa Ala Xaa Phe Xaa Gln Phe Xaa Ala  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Ala Ile Glu Phe Thr Thr Met Pro Phe Leu Thr Gln Gln Ser Asp Val  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Xaa Cys Val Gln Gln Xaa Gln Xaa Arg Ala Gly Arg Glu Ser His Arg  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Phe Xaa Xaa Xaa Gln Gln Pro Arg Pro Gly Gly His Xaa Arg Asp His  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Leu Xaa Gln Asp Gly Ser Val Val Leu Asp Asp Ser Ser Val Ala Gln  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Ala Val Val Pro Arg Arg Asp Asn Arg Glu Leu Asp Ala Ile Gln Arg  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Arg Pro Gly Gly Arg Lys Ala Ser Gly Leu Arg Cys His His Gln His  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 His Gln Trp Arg Val Gly Val Arg Glu Arg Val Arg Cys Gln Gly Gly  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Gly Asp Arg Leu Leu Gln Glu Val Leu Arg Leu Ala Gly Gly Glu Leu  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Arg Arg Gln Leu Gly Leu Leu Gln Pro Glu Thr Leu Cys Phe Tyr Ser  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Ser Tyr Ser His Ile Leu Ala Val Ser Tyr Gly Asp Asn Leu Glu Cys  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Tyr Asn Gln Arg Pro Phe Thr Ser Asp Thr Thr Val Thr Asn Pro Cys  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Asn Asn Ala Ile Asn Ala Ile Thr Glu Ile Ala Thr Pro Val Asp Cys  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Arg Ser Cys Gly Gly Ser Leu Gln Lys Leu Xaa Tyr Ile His Gly Pro  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Gln Leu Ser Leu Thr Val Ile Ile Cys Ile His Gln Met Ser Ser Asn  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Val Leu Glu Val Asn Ala Tyr Ser Ile Gly Lys Met Lys Met Leu Glu  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Ile Lys Leu Ile Ile Phe Leu Leu Ile Phe Tyr Ile Phe Ser Arg Ser  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Lys Ser Asn Tyr Lys Asp Phe Ile Tyr Gly Leu Gly Tyr Glu Tyr Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ile Ile Lys Ile Asn Ile Leu Phe Asn Leu Lys Asp Leu Ile Ile Ser  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Ile Phe Tyr Met Asp Trp Asp Ile Asn Ser Ile Tyr Leu Lys Phe Tyr  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Lys Asn Phe Lys Phe Lys Asn Asn Thr Lys Asn Ile Ile Arg Ser Asp  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Arg Glu Arg Asp Asp Asp His Glu Ile Glu Val Glu Ser Lys Lys Glu  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Ile Thr Leu Ile Met Gly Asn Phe Val Leu Phe Ala Arg Ser Arg Trp  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Pro Trp Thr Pro Asn Ile His Asn Arg His Ala Ile Thr Met Leu Ser  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Tyr Val Ser Leu Ser His Ile Leu Pro Ile Thr Ser Ser Arg Ile Leu  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Ile Lys Pro Ala His His Ser Phe Ala Pro Leu Tyr His Xaa Ser Val  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                 Arg Met Ala Pro Ile Pro Ser Val Trp Ser Pro Gly Xaa Trp Ser Val  
               
               
                             660                 665                 670  
               
               
                   
               
               
                 Leu Thr Arg Gly Leu Val Glu Gly His Arg Pro Cys Xaa Leu Arg Gln  
               
               
                         675                 680                 685  
               
               
                   
               
               
                 Arg Leu Lys Ile Thr Pro Leu Ala Ile Arg Trp Val Pro Ile Arg Ser  
               
               
                     690                 695                 700  
               
               
                   
               
               
                 Lys Ser Gly Gly Phe Xaa Thr Arg Pro Ile Gln Tyr Leu Ser Gln Glu  
               
               
                 705                 710                 715                 720  
               
               
                   
               
               
                 Leu Glu Leu Arg Val Gly Ser Thr Pro Asn Ala Val Pro Gly Val Ala  
               
               
                                 725                 730                 735  
               
               
                   
               
               
                 Phe Ile Pro Ile Pro Ala Cys Asp His Thr Leu Ser Ser Ser Val Ile  
               
               
                             740                 745                 750  
               
               
                   
               
               
                 Ile Val Arg Trp Val His Ala Leu Ser Asn Leu Leu Asp Ser Xaa Ser  
               
               
                         755                 760                 765  
               
               
                   
               
               
                 Phe Asp Thr Ala Ser Tyr Leu Leu Cys Gly Pro Ile His Ser Cys Ile  
               
               
                     770                 775                 780  
               
               
                   
               
               
                 Val Ser Tyr Gly Leu Glu Gln Ser Val Cys Arg Gly Thr Val Ser Ser  
               
               
                 785                 790                 795                 800  
               
               
                   
               
               
                 Gly Trp Leu Ala Ser Gly Ser Trp His Val Gly Ser Ile Gln His Ile  
               
               
                                 805                 810                 815  
               
               
                   
               
               
                 Gly Leu Gly Ile Pro Cys Arg Val Tyr Cys Gly Ser His Val Met Trp  
               
               
                             820                 825                 830  
               
               
                   
               
               
                 Gly Gly Cys Gln Asn Met Leu Tyr His Ser Leu Pro Thr Lys Glu Leu  
               
               
                         835                 840                 845  
               
               
                   
               
               
                 Cys His Arg Arg Ile Val Asp Thr Ala Trp Val Leu Trp Ser Val Leu  
               
               
                     850                 855                 860  
               
               
                   
               
               
                 Val Arg Leu Ser Trp Val Asp Tyr Phe Ile Lys Leu Ala Xaa Cys Trp  
               
               
                 865                 870                 875                 880  
               
               
                   
               
               
                 Leu Gly Lys Val His Leu Val Gly Met Val Glu Thr Xaa Pro Arg Lys  
               
               
                                 885                 890                 895  
               
               
                   
               
               
                 Val Gly Asp Leu Val Phe Asp Asn Gln Leu Phe Met Arg Arg Met Val  
               
               
                             900                 905                 910  
               
               
                   
               
               
                 Ser Leu Arg Trp Gly Val Cys Ser Phe Arg Phe Val Ala Met Asp Cys  
               
               
                         915                 920                 925  
               
               
                   
               
               
                 Leu Leu Glu Ala Trp Phe Asp Cys Ser Val Gly Arg Arg Tyr Leu Xaa  
               
               
                     930                 935                 940  
               
               
                   
               
               
                 Arg Ser Ser Ile Pro Cys Ser Glu Lys Asp Leu Pro Arg Ser Leu Ala  
               
               
                 945                 950                 955                 960  
               
               
                   
               
               
                 Arg Pro Cys Ser Gln Arg Met Cys Met Ser Arg Ser Ile Gln Pro Cys  
               
               
                                 965                 970                 975  
               
               
                   
               
               
                 Gly Ser Arg Met His Gln Leu Gly Leu Ala Cys Ser Arg Leu Lys Gln  
               
               
                             980                 985                 990  
               
               
                   
               
               
                 Lys Asp Ile Leu Ala Thr Arg Phe Ala Gln Pro Cys Gly Ser Asn Gln  
               
               
                         995                 1000                1005  
               
               
                   
               
               
                 Met His Leu Leu Gly Leu Ala Leu Thr Arg Gln Trp Thr Leu Val Ser  
               
               
                     1010                1015                1020  
               
               
                   
               
               
                 Glu Lys Gly Leu Xaa Lys Thr Leu Ala Arg Thr Ser Arg Tyr Leu Leu  
               
               
                 1025                1030                1035                1040  
               
               
                   
               
               
                 Asp Asn Arg Cys Leu Val Met Asp Leu Arg Leu Ser Arg Gln Arg Leu  
               
               
                                 1045                1050                1055  
               
               
                   
               
               
                 Ala Glu Thr Trp Ala Met Asp Ala Tyr Lys Glu Arg Met Ala Arg Asp  
               
               
                             1060                1065                1070  
               
               
                   
               
               
                 Arg Ser Asn Asn Tyr Lys Phe Ile Lys His Leu Met Asp Ala Tyr Lys  
               
               
                         1075                1080                1085  
               
               
                   
               
               
                 Glu Arg Thr Asp Arg Asp Arg Ser Asn Asn Tyr Lys Phe Ile Lys Xaa  
               
               
                     1090                1095                1100  
               
               
                   
               
               
                 Leu Leu Xaa His Trp Thr Lys Glu Val Leu Cys Asn Ile Lys Ile Gly  
               
               
                 1105                1110                1115                1120  
               
               
                   
               
               
                 Arg His Lys Tyr Tyr Phe Gln Ile Leu Phe Ser Leu Ser Pro Ser Pro  
               
               
                                 1125                1130                1135  
               
               
                   
               
               
                 Pro Leu Pro Phe Ser Ile Phe Ser Ile Leu Ser His Asn Ile Arg Thr  
               
               
                             1140                1145                1150  
               
               
                   
               
               
                 Asp Met Thr Thr Phe Asp Leu Leu Thr Xaa Leu Xaa His Gln Lys Pro  
               
               
                         1155                1160                1165  
               
               
                   
               
               
                 Tyr Cys Leu Pro His Asp Gly Asp Glu Leu Leu Val Gln Xaa Ser Asn  
               
               
                     1170                1175                1180  
               
               
                   
               
               
                 Xaa Trp Lys Trp Thr Ser Thr Met Thr Arg Met Ala Thr Cys Ser Cys  
               
               
                 1185                1190                1195                1200  
               
               
                   
               
               
                 Val Asp Phe Pro Ser Asn Gln Ser Ser Trp Asn Arg Ile Arg Arg Leu  
               
               
                                 1205                1210                1215  
               
               
                   
               
               
                 Lys Gly Asp Asp His Val Gln Cys His Ala His Gln His Asn Ser Asn  
               
               
                             1220                1225                1230  
               
               
                   
               
               
                 Thr Val Gln Lys Asp Leu Ile Leu His Leu Ala His Pro Ala Ala Gly  
               
               
                         1235                1240                1245  
               
               
                   
               
               
                 Ile Asp Trp Arg Lys Arg Arg Val Ser Leu Pro Ile His Ile Gln Arg  
               
               
                     1250                1255                1260  
               
               
                   
               
               
                 Thr Asn Ser Phe Ser Ser Asp Glu His Phe Ser Pro Ala Leu Tyr Phe  
               
               
                 1265                1270                1275                1280  
               
               
                   
               
               
                 Ile Ile Ile Ile Ile Ile Asn Met Val Ser Leu Gln Asn Ile Ile Phe  
               
               
                                 1285                1290                1295  
               
               
                   
               
               
                 Phe Gln Asn Ile Leu Lys Asn Asp Lys Gly Arg Arg Trp Ile Ser Asp  
               
               
                             1300                1305                1310  
               
               
                   
               
               
                 Phe Tyr Cys Glu Gln Lys Ser Leu Val Arg Thr Ser Lys Met Cys Gln  
               
               
                         1315                1320                1325  
               
               
                   
               
               
                 Met Asn Pro Asn Lys Trp Val Trp Ser Met Val Thr Met Arg Ser Val  
               
               
                     1330                1335                1340  
               
               
                   
               
               
                 Phe Val Tyr Lys Lys Ile Ile Asn Leu Ile Phe Ile Phe Pro Leu Ile  
               
               
                 1345                1350                1355                1360  
               
               
                   
               
               
                 Ser Gly His Asp Ile Ser Ser Asn His Val Met Xaa Asp Glu Xaa His  
               
               
                                 1365                1370                1375  
               
               
                   
               
               
                 Ile Phe Xaa Lys Leu Xaa Ile Glu Lys Lys Asp Tyr Tyr Pro Phe Tyr  
               
               
                             1380                1385                1390  
               
               
                   
               
               
                 Xaa Cys Xaa Ile Ile Phe Ser Leu Ser Ile Ile His Val Glu Glu Arg  
               
               
                         1395                1400                1405  
               
               
                   
               
               
                 Leu Ser His Gln Ile Lys Tyr Arg Xaa Lys Ser Cys Phe Leu Asn Ser  
               
               
                     1410                1415                1420  
               
               
                   
               
               
                 Lys Asn Asn Leu Pro Leu Leu Ile Ile Ser Leu Leu Ile Ser Ile Xaa  
               
               
                 1425                1430                1435                1440  
               
               
                   
               
               
                 Ile Tyr Ile Tyr Xaa Tyr Ile Asn Phe Xaa Ile Phe Leu Asn Leu Asn  
               
               
                                 1445                1450                1455  
               
               
                   
               
               
                 Leu Ser Lys Lys Asp Lys Leu Asn Phe Cys Ile Ile Met Val Glu Leu  
               
               
                             1460                1465                1470  
               
               
                   
               
               
                 Val Lys Xaa Gly Ser Arg Thr Leu Ile Glu Asn Ser Lys Pro Leu Leu  
               
               
                         1475                1480                1485  
               
               
                   
               
               
                 Val Leu Leu Asp Glu Asn Lys Thr Ile Lys Asn Pro Leu Ile Tyr Ile  
               
               
                     1490                1495                1500  
               
               
                   
               
               
                 Tyr Ile Tyr Ile Leu Leu Tyr Leu Phe Phe Gly Arg Thr Thr Gln Val  
               
               
                 1505                1510                1515                1520  
               
               
                   
               
               
                 Arg Lys Pro Lys Gln Arg Trp Arg Lys Val Gly Arg Xaa Arg Asp Phe  
               
               
                                 1525                1530                1535  
               
               
                   
               
               
                 Ser Lys Arg Arg His Thr Ser Ile Arg Ile Val Met Thr Ile Arg Arg  
               
               
                             1540                1545                1550  
               
               
                   
               
               
                 Lys Arg Gly Glu Arg Glu Arg Arg Lys Arg His Cys Pro Val Leu Ser  
               
               
                         1555                1560                1565  
               
               
                   
               
               
                 Met Arg Asn Cys Leu Ser Thr Asn Glu Gln Tyr Lys His Leu Cys Arg  
               
               
                     1570                1575                1580  
               
               
                   
               
               
                 Gln Ile Cys Ser Lys Gly Ser Phe Thr Ala Gly Arg Asn Pro Phe Leu  
               
               
                 1585                1590                1595                1600  
               
               
                   
               
               
                 Tyr Ile Ser Thr Thr Ser His Pro His His His His His His His Cys  
               
               
                                 1605                1610                1615  
               
               
                   
               
               
                 Gly Gly Arg Pro Cys Cys Trp Ser Phe Leu Pro Trp Pro Arg Arg Ser  
               
               
                             1620                1625                1630  
               
               
                   
               
               
                 Ala Pro Ser Pro Ser Asn Ala Glu Gly Lys Pro Gly Gly Leu Ser Ala  
               
               
                         1635                1640                1645  
               
               
                   
               
               
                 Pro Ala Gly Cys Ala Val Ala Ser Thr Ala Gly Ala Val Thr Arg Ile  
               
               
                     1650                1655                1660  
               
               
                   
               
               
                 His Xaa Ala Val Lys Asp Ala Xaa Xaa Asn Ala Xaa Ala Pro Arg Pro  
               
               
                 1665                1670                1675                1680  
               
               
                   
               
               
                 Pro Leu Pro Leu Arg Ala Ala Val Ala Xaa Leu Ala Arg Ser Ser Ser  
               
               
                                 1685                1690                1695  
               
               
                   
               
               
                 Pro Pro Ser Ser Ser Arg Cys Ser Ile Xaa Xaa Thr Gln Pro Ala Pro  
               
               
                             1700                1705                1710  
               
               
                   
               
               
                 Ala Xaa Ala Ser Thr Arg Xaa Pro Pro Ser Ser Pro Pro Pro Xaa Pro  
               
               
                         1715                1720                1725  
               
               
                   
               
               
                 Ser Xaa Gly Ser Gly Xaa Pro Ala Thr Thr Pro Xaa Ile Xaa Xaa Xaa  
               
               
                     1730                1735                1740  
               
               
                   
               
               
                 Ser Arg Leu Ser Trp Xaa Xaa Xaa Leu Xaa Arg Xaa Xaa Val Ile Xaa  
               
               
                 1745                1750                1755                1760  
               
               
                   
               
               
                 Xaa Ser Pro Glu Ala Arg Leu Gln Xaa Xaa Asp Arg Xaa Leu Asn Ala  
               
               
                                 1765                1770                1775  
               
               
                   
               
               
                 Leu Gly Xaa Ala Arg Gly Trp Ser Thr Val Pro Xaa Gly Xaa Ser Arg  
               
               
                             1780                1785                1790  
               
               
                   
               
               
                 Gly Val Thr Ala Ser Ser Xaa Asn Arg Thr Leu Ile Gly Leu Leu Arg  
               
               
                         1795                1800                1805  
               
               
                   
               
               
                 Arg Gln Leu Ala Xaa Ala Val Arg Cys Xaa Gln Xaa Ile Leu Arg Pro  
               
               
                     1810                1815                1820  
               
               
                   
               
               
                 Lys Pro His Pro Asn Leu Ile Gln Leu Gln Leu Arg Ala Gly Arg Glu  
               
               
                 1825                1830                1835                1840  
               
               
                   
               
               
                 Asn His Arg Leu Arg Pro Ala Gln Gln Pro Arg Pro Gly Gly His Arg  
               
               
                                 1845                1850                1855  
               
               
                   
               
               
                 Pro Asp His Leu Leu Gln Asp Gly Ser Val Val Leu Asp Asp Ser Ser  
               
               
                             1860                1865                1870  
               
               
                   
               
               
                 Val Ala Gln Ala Val Val Pro Arg Arg Asp Asn Arg Glu Leu Asp Ala  
               
               
                         1875                1880                1885  
               
               
                   
               
               
                 Ile Gln Arg Arg Pro Gly Gly Arg Lys Ala Ser Gly Leu Arg Cys His  
               
               
                     1890                1895                1900  
               
               
                   
               
               
                 His Gln His His Gln Trp Arg Val Gly Val Arg Glu Arg Val Arg Cys  
               
               
                 1905                1910                1915                1920  
               
               
                   
               
               
                 Gln Gly Gly Gly Asp Arg Leu Leu Gln Xaa Val Leu Arg Leu Ala Gly  
               
               
                                 1925                1930                1935  
               
               
                   
               
               
                 Gly Glu Leu Arg Arg Gln Leu Gly Leu Leu Gln Pro Xaa Ser Leu Tyr  
               
               
                             1940                1945                1950  
               
               
                   
               
               
                 Leu Xaa Arg Tyr Tyr Val Arg Ile His Val Ile Thr Gln Thr Leu Leu  
               
               
                         1955                1960                1965  
               
               
                   
               
               
                 Leu Lys Arg Leu Arg Glu Leu Ile Val Glu Val Ala Glu Glu Ile Phe  
               
               
                     1970                1975                1980  
               
               
                   
               
               
                 Asn Lys Ser Ala Glu Gln Val His Gly Pro Gln Ser Ser Leu Ile Val  
               
               
                 1985                1990                1995                2000  
               
               
                   
               
               
                 Val Arg Cys Ile His Gln Met Ser Trp Ser Xaa Xaa Met Arg Xaa Xaa  
               
               
                                 2005                2010                2015  
               
               
                   
               
               
                 Ser Val Asn Arg Cys Asn Lys Asn Tyr Leu Phe Phe Ile Ile Ile Asn  
               
               
                             2020                2025                2030  
               
               
                   
               
               
                 Ile Leu Ile Tyr Phe Leu Ile Leu Lys Ile Leu Lys Asn Leu Ile Ile  
               
               
                         2035                2040                2045  
               
               
                   
               
               
                 Arg Ile Leu Tyr Met Asp Trp Asp Thr Xaa Lys Xaa Xaa Leu Xaa Lys  
               
               
                     2050                2055                2060  
               
               
                   
               
               
                 Leu Ile Tyr Phe Ser Gly Ser Lys Asn Ile Ile Ile Arg Ile Phe Tyr  
               
               
                 2065                2070                2075                2080  
               
               
                   
               
               
                 Met Asp Xaa Asp Thr Asn Xaa Xaa Leu Lys Phe Xaa Tyr Lys Ile Val  
               
               
                                 2085                2090                2095  
               
               
                   
               
               
                 Lys Ser Lys Asn Asn Thr Lys Asn Ile Xaa Ser Tyr Arg Glu Cys Gly  
               
               
                             2100                2105                2110  
               
               
                   
               
               
                 Ala Ile Ser Arg Ser Arg Leu Arg Leu Xaa Xaa Lys Leu Cys Ser Trp  
               
               
                         2115                2120                2125  
               
               
                   
               
               
                 Glu Ile Phe Phe Cys Phe Gln Asp Asp Asp Arg Gly Asn Leu Thr Ser  
               
               
                     2130                2135                2140  
               
               
                   
               
               
                 Ala Ile Gly His Ala Ile Thr Met Leu Ser Ser Xaa Asn Leu Ser Ser  
               
               
                 2145                2150                2155                2160  
               
               
                   
               
               
                 Ser Ser Tyr Gly His Lys Ser Gln Ser Ser Xaa Lys Ala Arg Ile Leu  
               
               
                                 2165                2170                2175  
               
               
                   
               
               
                 Met Ser Pro Thr Tyr Leu Tyr Cys Phe Thr Leu Leu Tyr Arg Xaa Arg  
               
               
                             2180                2185                2190  
               
               
                   
               
               
                 Gly Val Arg Thr Ile Trp Pro Ile Pro Ser Ala Asp His Tyr Asp Leu  
               
               
                         2195                2200                2205  
               
               
                   
               
               
                 Tyr Val Gly Ala Cys Pro Glu Ile Leu Arg Gly His Arg Ser His Xaa  
               
               
                     2210                2215                2220  
               
               
                   
               
               
                 Ser Thr Trp Arg Leu Lys Ile Thr Phe Ile Xaa Xaa Leu Val Asp Ser  
               
               
                 2225                2230                2235                2240  
               
               
                   
               
               
                 Lys Leu Glu Val Asp Leu Xaa Arg Arg Ser Val Ser Leu Gly Thr Leu  
               
               
                                 2245                2250                2255  
               
               
                   
               
               
                 Gly Xaa  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 26  
               
               
                 &lt;211&gt; LENGTH: 2359  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 23, 196, 205, 209, 214, 226, 254, 260, 264, 267, 284,  
               
               
                       285, 287, 289, 301, 309, 313, 315, 327, 328, 345, 352, 358, 494,  
               
               
                       697, 713, 728, 813, 939, 991, 1076, 1081, 1165, 1167, 1208,  
               
               
                       1226, 1229, 1250, 1253, 1442, 1445, 1452, 1455, 1465  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 1474, 1492, 1511, 1517, 1523, 1549, 1604, 1676, 1770,  
               
               
                       1777, 1780, 1781, 1794, 1795, 1805, 1812, 1814, 1816, 1820, 1823,  
               
               
                       1832, 1835, 1840, 1841, 1846, 1847, 1849, 1850, 1855, 1857,  
               
               
                       1861, 1862, 1864, 1865, 1871, 1872, 1874, 1877, 1878  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 1883, 1894, 1903, 1916, 1922, 1923, 2034, 2053, 2058,  
               
               
                       2114, 2118, 2144, 2155, 2157, 2158, 2160, 2179, 2184, 2185, 2190,  
               
               
                       2206, 2223, 2224, 2256, 2271, 2290, 2326, 2335, 2336, 2342,  
               
               
                       2344, 2347, 2356, 2359  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 26  
               
               
                   
               
               
                 Gln Arg Gly Arg Leu Met Ser Tyr His Cys His Arg Met Arg Ser Arg  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ile Gln His Ala Ile Cys Xaa Leu Gly His Arg Thr Ser Tyr Pro Lys  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Thr Arg Leu Cys Asp Phe Pro His Ser Pro His Leu Val His Arg Lys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Leu His Ser Gly Gln Glu Ser Ile Ser Leu Tyr Lys His His Leu Pro  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Pro Thr Pro Pro Pro Leu Pro Leu Leu Arg Arg Met Lys Ala Leu Leu  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Leu Val Ile Phe Thr Leu Ala Ser Ser Leu Gly Ala Phe Ala Glu Gln  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Cys Gly Arg Gln Ala Gly Gly Ala Leu Cys Pro Gly Gly Leu Cys Cys  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Gln Tyr Gly Trp Cys Gly Asn Thr Asp Pro Tyr Cys Gly Gln Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Cys Gln Ser Gln Cys Gly Gly Ser Gly Gly Ser Gly Gly Gly Ser Val  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Ala Ser Ile Ile Ser Ser Ser Leu Phe Glu Gln Met Leu Lys His Arg  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asn Asp Ala Ala Cys Pro Gly Lys Gly Phe Tyr Thr Tyr Asn Ala Phe  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Ile Ala Ala Ala Asn Ser Phe Ser Gly Phe Gly Thr Thr Gly Asp Asp  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Pro Arg Arg Xaa Arg Arg Ser Arg Leu Ser Trp Arg Xaa Arg Leu Thr  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Xaa Arg Gln Val Ile Xaa Thr Ser Pro Glu Ala Arg Lys Leu Phe Met  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Gly Xaa Lys Thr Glu Cys Leu Gly Phe Gly Arg Trp Val Gly Asp Ala  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Pro Asp Gly Pro Tyr Ala Leu Gly Tyr Cys Phe Val Gln Xaa Gln Asn  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Pro His Arg Xaa Thr Ala Ser Xaa Leu Pro Xaa Ala Val Arg Cys Ser  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Lys Lys Tyr Gly Arg Ser Pro Ser Lys Phe His Xaa Xaa Pro Xaa Ser  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Xaa Ser Ser Ser Pro Arg Ser Ser Ser Gln Arg Cys Xaa Phe Arg Asn  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Asn Pro Met Cys Xaa Ala Cys Ser Xaa Tyr Xaa Tyr Gly Pro Ala Gly  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Arg Ala Ile Gly Ser Asp Xaa Xaa Asn Asn Pro Asp Leu Val Ala Thr  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Asp Ala Thr Ile Ser Phe Lys Thr Xaa Leu Trp Phe Trp Met Thr Xaa  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Gln Ser Pro Lys Pro Xaa Cys His Asp Val Ile Thr Gly Ser Trp Thr  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Pro Ser Asn Ala Asp Gln Ala Ala Gly Arg Leu Pro Gly Tyr Gly Val  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Thr Thr Asn Ile Ile Asn Gly Gly Leu Glu Cys Gly Lys Gly Tyr Asp  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Ala Arg Val Ala Asp Arg Ile Gly Phe Tyr Lys Arg Tyr Cys Asp Leu  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Leu Gly Val Ser Tyr Gly Asp Asn Leu Asp Cys Tyr Asn Gln Arg Pro  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Phe Ala Ser Thr Ala Ala Thr Ala Thr Phe Arg Ala Met Glu Thr Thr  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Trp Ser Ala Thr Thr Arg Asp Pro Leu Leu Ser Pro Ile Leu Leu Arg  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Ile His Val Ile Thr Gln Thr Leu Leu Leu Arg Arg Leu Arg Glu Leu  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Thr Val Glu Val Ala Glu Glu Val Phe Asn Lys Ser Leu Xaa Thr Tyr  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Met Ala His Asn Tyr Arg Pro Ser Tyr Ala Ser Ile Lys Cys Pro Gln  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Met Ser Trp Ser Lys Met Arg Ile Arg Ser Val Lys Arg Cys Asn Lys  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Asn Leu Phe Phe Tyr Asn Tyr Lys Tyr Phe Asn Ile Phe Phe Asn Leu  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Lys Asp Pro Lys Asn Leu Ile Ile Arg Ile Leu Tyr Met Asp Trp Asp  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Thr Lys Asn Ile Leu Lys Leu Ile Tyr Phe Leu Ile Leu Lys Ile Leu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Val Phe Ser Ile Trp Ile Gly Ile Leu Thr Arg Phe Thr Tyr Lys Asn  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Phe Asn Ile Lys Ile Leu Asn Leu Lys Ile Lys Ile Leu Lys Ile Ser  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Lys Tyr Asn Gly Asn His Glu Ile Glu Asn Val Met Ile Glu Ile Met  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Arg Ser Arg Leu Arg Val Lys Arg Lys Leu Arg Ser Trp Glu Ile Ser  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Phe Cys Leu His Gly Arg Asp Gly Asp Arg Gly His Leu Thr Ser Thr  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                 Thr Gly Met Gln Pro Cys Cys His Met Leu Ala Cys Leu Ile Ser Tyr  
               
               
                             660                 665                 670  
               
               
                   
               
               
                 Asp His Glu Ser His Ser Leu His Glu Tyr Leu Ser Gln Leu Ser Ile  
               
               
                         675                 680                 685  
               
               
                   
               
               
                 Thr Val Leu His Leu Cys Thr Ile Xaa Glu Val Phe Val Trp Leu Asp  
               
               
                     690                 695                 700  
               
               
                   
               
               
                 Pro Ser Arg Val Tyr Gly Leu Pro Xaa Pro Gly Ala Cys Pro Glu Val  
               
               
                 705                 710                 715                 720  
               
               
                   
               
               
                 Leu Arg Gly Ile Asp Leu Val Xaa Leu Gly Arg Gly Arg Ser Leu Leu  
               
               
                                 725                 730                 735  
               
               
                   
               
               
                 Leu Ser Val Gly Cys Leu Tyr Lys Gly Arg Asn His Glu Gly Asp Ser  
               
               
                             740                 745                 750  
               
               
                   
               
               
                 Leu Asp Leu Phe Asn Ile Ala Ser Lys Ser Trp Ser Tyr Val Tyr Glu  
               
               
                         755                 760                 765  
               
               
                   
               
               
                 Val Arg Pro Pro Met Leu Phe Leu Gly Ser Leu Leu Tyr Leu Phe Leu  
               
               
                     770                 775                 780  
               
               
                   
               
               
                 His Val Ile Ile His Ser Ser Phe Asn His Leu Gln Ser Ser Ser Tyr  
               
               
                 785                 790                 795                 800  
               
               
                   
               
               
                 Val Gly Cys Met His Cys Leu Ile Tyr Ser Ile Gln Xaa Arg Ser Thr  
               
               
                                 805                 810                 815  
               
               
                   
               
               
                 Leu Leu Pro Thr Tyr Tyr Val Ala Gln Tyr Ile Val Val Leu Ser His  
               
               
                             820                 825                 830  
               
               
                   
               
               
                 Thr Ala Ser Ser Lys Ala Cys Ala Glu Glu Leu Cys Gln Val Val Gly  
               
               
                         835                 840                 845  
               
               
                   
               
               
                 Trp Pro Arg Ala His Gly Ile Glu Leu Ala Arg Tyr Asn Thr Ser Ala  
               
               
                     850                 855                 860  
               
               
                   
               
               
                 Gly Tyr His Ala Glu Ser Ile Val Val Val Asp Met Ser Cys Gly Val  
               
               
                 865                 870                 875                 880  
               
               
                   
               
               
                 Asp Ala Lys Ile Cys Tyr Ile Ile Leu Ser Leu Gln Arg Ser Cys Ala  
               
               
                                 885                 890                 895  
               
               
                   
               
               
                 Ile Gly Glu Ser Trp Thr Arg Leu Gly Phe Cys Gly Arg Ser Leu Phe  
               
               
                             900                 905                 910  
               
               
                   
               
               
                 Ala Ser Val Gly Trp Ile Thr Ser Ser Ser Trp Pro Ser Val Gly Trp  
               
               
                         915                 920                 925  
               
               
                   
               
               
                 Ala Lys Tyr Thr Trp Gly Trp Ser Arg Gln Xaa Gln Gly Arg Leu Ala  
               
               
                     930                 935                 940  
               
               
                   
               
               
                 Lys Thr Trp Phe Ser Thr Ile Asn Cys Leu Gly Glu Trp Tyr Pro Ser  
               
               
                 945                 950                 955                 960  
               
               
                   
               
               
                 Val Gly Val Ser Ala Arg Phe Gly Leu Leu Arg Trp Ile Val Cys Cys  
               
               
                                 965                 970                 975  
               
               
                   
               
               
                 Arg Arg Leu Gly Ser Ile Ala Leu Lys Ser Gly Glu Gly Ile Xaa Gly  
               
               
                             980                 985                 990  
               
               
                   
               
               
                 Val Gln Phe Asp His Val Glu Val Asn Lys Arg Thr Cys Gln Glu Val  
               
               
                         995                 1000                1005  
               
               
                   
               
               
                 Trp Leu Asp Arg Val Lys Ala Arg Glu Cys Val Cys Arg Gly Leu Phe  
               
               
                     1010                1015                1020  
               
               
                   
               
               
                 Asn His Val Glu Ala Arg Glu Cys Thr Asn Cys Glu Val Trp Leu Ala  
               
               
                 1025                1030                1035                1040  
               
               
                   
               
               
                 His Val Ser Arg Arg Ile Tyr Leu Leu Arg Gly Leu Leu Asn His Val  
               
               
                                 1045                1050                1055  
               
               
                   
               
               
                 Glu Ala Ile Lys Cys Thr Cys Tyr Glu Val Trp Leu Asp Leu Leu Asp  
               
               
                             1060                1065                1070  
               
               
                   
               
               
                 Asn Gly Arg Xaa Val Arg Arg Asp Xaa Pro Arg Leu Ser Trp Gln Gly  
               
               
                         1075                1080                1085  
               
               
                   
               
               
                 Leu Val Asp Thr Cys Ser Thr Ile Asp Ala Tyr Arg Trp Ile Asp Asp  
               
               
                     1090                1095                1100  
               
               
                   
               
               
                 Leu Val Asp Lys Asp Leu Arg Leu Ser Gly Gln Trp Met Pro Ile Ser  
               
               
                 1105                1110                1115                1120  
               
               
                   
               
               
                 Lys Lys Gly Trp Leu Glu Ile Asn Lys Asp Gln Ile Ile Asn Ile Asn  
               
               
                                 1125                1130                1135  
               
               
                   
               
               
                 Leu Ser Asn Thr Trp Thr His Ile Ser Glu Lys Gly Arg Ile Glu Ile  
               
               
                             1140                1145                1150  
               
               
                   
               
               
                 Asn Lys Asp Gln Ile Ile Asn Ile Ser Leu Asn Ser Xaa Tyr Xaa Ile  
               
               
                         1155                1160                1165  
               
               
                   
               
               
                 Gly Gln Lys Arg Tyr Tyr Val Ile Leu Lys Leu Gly Gly Thr Asn Ile  
               
               
                     1170                1175                1180  
               
               
                   
               
               
                 Ile Ser Lys Tyr Phe Ser Pro Ala Leu Arg His His Cys His Phe Asn  
               
               
                 1185                1190                1195                1200  
               
               
                   
               
               
                 Leu Phe Phe Leu Tyr Asn Tyr Xaa Ile Thr Phe Val His Glu Ile His  
               
               
                                 1205                1210                1215  
               
               
                   
               
               
                 Lys Pro Ser Thr Cys Phe Ser Lys His Xaa Asp Tyr Xaa Asp Thr Arg  
               
               
                             1220                1225                1230  
               
               
                   
               
               
                 Ser His Asn Ile Ala Tyr Leu Asn Met Met Glu Met Asn Phe Ser Trp  
               
               
                         1235                1240                1245  
               
               
                   
               
               
                 Ser Xaa Tyr Leu Xaa Asn Gly Ser Gly Gln Ala Arg Leu Gly Trp Leu  
               
               
                     1250                1255                1260  
               
               
                   
               
               
                 His Val His Val Leu Thr Phe Gln Val Ile Asn Gln Ala Gly Ile Glu  
               
               
                 1265                1270                1275                1280  
               
               
                   
               
               
                 Asp Asp Ser Arg Ala Met Thr Ile Lys Phe Asn Val Thr Leu Ile Asn  
               
               
                                 1285                1290                1295  
               
               
                   
               
               
                 Ile Ile Pro Thr Pro Cys Arg Lys Ile Leu Ser Tyr Ile Asp Leu Pro  
               
               
                             1300                1305                1310  
               
               
                   
               
               
                 Ile Arg Pro Pro Ala Ser Ile Gly Gly Asn Glu Gly Ser Val Ser Gln  
               
               
                         1315                1320                1325  
               
               
                   
               
               
                 Phe Thr Phe Lys Gly Arg Ile His Phe His Gln Met Ser Thr Ser Val  
               
               
                     1330                1335                1340  
               
               
                   
               
               
                 Leu Leu Asp Tyr Ile Leu Leu Leu Leu Leu Leu Leu Ile Glu Trp Val  
               
               
                 1345                1350                1355                1360  
               
               
                   
               
               
                 Tyr Arg Ile Tyr Arg Tyr Phe Ser Phe Asn Lys Ile Phe Lys Met Ile  
               
               
                                 1365                1370                1375  
               
               
                   
               
               
                 Lys Gly Glu Gly Gly Phe Asp Leu Arg Ile Phe Ile Val Ser Asn Lys  
               
               
                             1380                1385                1390  
               
               
                   
               
               
                 Ser Leu Leu Glu Leu Pro Lys Cys Val Lys Thr Leu Ile Ser Gly Phe  
               
               
                         1395                1400                1405  
               
               
                   
               
               
                 Gly Leu Trp Leu Arg Asp Gln Tyr Leu Tyr Ile Lys Lys Leu Ser Thr  
               
               
                     1410                1415                1420  
               
               
                   
               
               
                 Phe Leu Phe Phe Asn Pro Val Asp Met Ile Tyr His Asn Gln Ile Met  
               
               
                 1425                1430                1435                1440  
               
               
                   
               
               
                 Cys Xaa Met Ser Xaa Asn Ile Phe Phe Asn Asn Xaa Asn Tyr Xaa Arg  
               
               
                                 1445                1450                1455  
               
               
                   
               
               
                 Lys Asn Lys Ile Thr Ile Pro Ser Xaa Asp Val Leu Tyr Phe Asn Pro  
               
               
                             1460                1465                1470  
               
               
                   
               
               
                 Phe Xaa Tyr Arg Phe Thr Asn Lys Lys Asp Tyr Asn Arg Ile Lys Ser  
               
               
                         1475                1480                1485  
               
               
                   
               
               
                 Asn Thr Glu Xaa Asn His Ala Phe Asp Leu Ile Arg Lys Ile Ile Phe  
               
               
                     1490                1495                1500  
               
               
                   
               
               
                 Leu Ser Tyr Pro Tyr Ala Xaa Leu Tyr Ile Tyr Ile Xaa Ile Ser Thr  
               
               
                 1505                1510                1515                1520  
               
               
                   
               
               
                 Ser Lys Xaa Tyr Phe Ile Asn Ile Tyr Gln Asn Lys Lys Ile Asn Ile  
               
               
                                 1525                1530                1535  
               
               
                   
               
               
                 Ser Ser Ala Ser Cys Ser Lys Cys Lys Asn Leu Asn Xaa Asp Leu Glu  
               
               
                             1540                1545                1550  
               
               
                   
               
               
                 His Lys Ile Pro Asn His Tyr Phe Tyr Leu Met Lys Thr Lys Pro Tyr  
               
               
                         1555                1560                1565  
               
               
                   
               
               
                 Lys Arg Ile Leu Leu Tyr Ile Tyr Ile Tyr Ile Tyr Tyr Phe Thr Tyr  
               
               
                     1570                1575                1580  
               
               
                   
               
               
                 Ser Leu Asp Val Gln His Lys Ser Gly Asn Arg Asn Lys Gly Gly Gly  
               
               
                 1585                1590                1595                1600  
               
               
                   
               
               
                 Lys Leu Ala Xaa Ala Glu Glu Thr Phe Arg Arg Ser Glu Gly Asp Thr  
               
               
                                 1605                1610                1615  
               
               
                   
               
               
                 Arg Leu Glu Leu Ser Leu Tyr Ala Glu Glu Lys Glu Gly Arg Glu Arg  
               
               
                             1620                1625                1630  
               
               
                   
               
               
                 Glu Gly Ser Ala Thr Val Asp Arg Ser Cys Pro Gly Ile Val Cys Arg  
               
               
                         1635                1640                1645  
               
               
                   
               
               
                 Leu Met Ser Ser Thr Asn Ile Cys Val Asp Arg Trp Gln Gln Met Arg  
               
               
                     1650                1655                1660  
               
               
                   
               
               
                 Ser Gly Ile Pro Thr Arg Asn Leu Pro Leu Val Xaa Arg Leu Ile Gln  
               
               
                 1665                1670                1675                1680  
               
               
                   
               
               
                 Arg Leu Ala Ser Ala Ile Ser Ser Cys Ala Ser Ser Val Pro Lys Glu  
               
               
                                 1685                1690                1695  
               
               
                   
               
               
                 Ala Ser Gln Arg Ala Gly Ile His Phe Ser Ile Ala Pro Pro Pro Thr  
               
               
                             1700                1705                1710  
               
               
                   
               
               
                 His Thr Thr Thr Thr Thr Thr Thr Ala Lys Glu Asp Glu Gly Leu Val  
               
               
                         1715                1720                1725  
               
               
                   
               
               
                 Ala Gly His Phe Tyr Pro Gly Leu Val Ala Arg Arg Leu Arg Arg Ala  
               
               
                     1730                1735                1740  
               
               
                   
               
               
                 Met Arg Lys Ala Ser Arg Gly Gly Ser Leu Pro Arg Arg Ala Val Leu  
               
               
                 1745                1750                1755                1760  
               
               
                   
               
               
                 Pro Val Arg Leu Val Arg His Gly Ser Xaa Leu Arg Ser Arg Met Pro  
               
               
                                 1765                1770                1775  
               
               
                   
               
               
                 Xaa Pro Met Xaa Xaa Leu His Ala Leu Pro Phe His Ser Glu Arg Arg  
               
               
                             1780                1785                1790  
               
               
                   
               
               
                 Trp Xaa Xaa Trp Leu Asp His His Leu Leu Pro Leu Xaa Ala Asp Ala  
               
               
                         1795                1800                1805  
               
               
                   
               
               
                 Glu Ala Ser Xaa Arg Xaa Ser Xaa Pro Arg Gln Xaa Leu Leu Xaa Val  
               
               
                     1810                1815                1820  
               
               
                   
               
               
                 His Arg Leu His Leu Arg Arg Xaa Leu Leu Xaa Arg Val Arg Asp Xaa  
               
               
                 1825                1830                1835                1840  
               
               
                   
               
               
                 Xaa Arg Pro Leu His Xaa Xaa Gly Xaa Xaa Gly Phe Leu Gly Xaa Asp  
               
               
                                 1845                1850                1855  
               
               
                   
               
               
                 Xaa Ser Arg Asp Xaa Xaa Ser Xaa Xaa Leu Pro Arg Leu Val Xaa Xaa  
               
               
                             1860                1865                1870  
               
               
                   
               
               
                 Leu Xaa Ile Asp Xaa Xaa Met His Trp Val Xaa His Val Gly Gly Pro  
               
               
                         1875                1880                1885  
               
               
                   
               
               
                 Pro Cys Pro Met Ala Xaa Arg Val Gly Leu Leu Leu Arg Pro Xaa Thr  
               
               
                     1890                1895                1900  
               
               
                   
               
               
                 Glu Pro Ser Ser Asp Tyr Cys Val Ala Ser Ser Xaa Trp Pro Cys Ala  
               
               
                 1905                1910                1915                1920  
               
               
                   
               
               
                 Ala Xaa Xaa Lys Tyr Tyr Gly Arg Ser Pro Ile Gln Ile Ser Phe Asn  
               
               
                                 1925                1930                1935  
               
               
                   
               
               
                 Tyr Asn Tyr Gly Pro Ala Gly Lys Thr Ile Gly Ser Asp Leu Leu Asn  
               
               
                             1940                1945                1950  
               
               
                   
               
               
                 Asn Pro Asp Leu Val Ala Thr Asp Pro Thr Ile Ser Phe Lys Thr Ala  
               
               
                         1955                1960                1965  
               
               
                   
               
               
                 Leu Trp Phe Trp Met Thr Pro Gln Ser Pro Lys Pro Ser Cys His Asp  
               
               
                     1970                1975                1980  
               
               
                   
               
               
                 Val Ile Thr Gly Ser Trp Thr Pro Ser Asn Ala Asp Arg Ala Ala Gly  
               
               
                 1985                1990                1995                2000  
               
               
                   
               
               
                 Arg Leu Pro Gly Tyr Gly Val Thr Thr Asn Ile Ile Asn Gly Gly Leu  
               
               
                                 2005                2010                2015  
               
               
                   
               
               
                 Glu Cys Gly Lys Gly Ser Asp Ala Arg Val Ala Asp Arg Ile Gly Phe  
               
               
                             2020                2025                2030  
               
               
                   
               
               
                 Tyr Xaa Arg Tyr Cys Asp Leu Leu Gly Val Ser Tyr Gly Asp Asn Leu  
               
               
                         2035                2040                2045  
               
               
                   
               
               
                 Asp Cys Tyr Asn Xaa Ser Pro Phe Thr Xaa Ser Asp Thr Met Cys Glu  
               
               
                     2050                2055                2060  
               
               
                   
               
               
                 Ser Met Arg Asn Lys Arg Tyr Cys Asn Ser Asp Ser Val Ser Leu Lys  
               
               
                 2065                2070                2075                2080  
               
               
                   
               
               
                 Leu Arg Arg Lys Ser Ser Ile Lys Ala Lys Leu Asn Lys Phe Met Ala  
               
               
                                 2085                2090                2095  
               
               
                   
               
               
                 Leu Asn His Arg Ser Ser Ser Asp Ala Ser Ile Lys Cys Leu Gly Val  
               
               
                             2100                2105                2110  
               
               
                   
               
               
                 Ser Xaa Cys Val Phe Xaa Arg Ile Glu Asp Val Arg Ile Asn Lys Ile  
               
               
                         2115                2120                2125  
               
               
                   
               
               
                 Ile Tyr Phe Leu Leu Ile Phe Tyr Ile Phe Ser Arg Ser Lys Ile Xaa  
               
               
                     2130                2135                2140  
               
               
                   
               
               
                 Leu Gly Phe Tyr Ile Trp Ile Gly Ile Leu Xaa Lys Xaa Xaa Tyr Xaa  
               
               
                 2145                2150                2155                2160  
               
               
                   
               
               
                 Asn Tyr Thr Phe Asn Leu Lys Asp Pro Lys Lys Thr Leu Gly Phe Ser  
               
               
                                 2165                2170                2175  
               
               
                   
               
               
                 Ile Trp Xaa Gly Ile Leu Thr Xaa Xaa Asn Cys Lys Asn Xaa Asn Ile  
               
               
                             2180                2185                2190  
               
               
                   
               
               
                 Lys Leu Leu Asn Leu Lys Ile Lys Ile Leu Lys Ile Tyr Xaa Asn His  
               
               
                         2195                2200                2205  
               
               
                   
               
               
                 Asp Ile Glu Asn Val Ala Leu Arg Ser Arg Asp Arg Gly Asp Xaa Xaa  
               
               
                     2210                2215                2220  
               
               
                   
               
               
                 Gly Asn Tyr Val Asn His Gly Lys Phe Ser Phe Val Ser Lys Thr Met  
               
               
                 2225                2230                2235                2240  
               
               
                   
               
               
                 Thr Val Glu Thr His Pro Gln Ser Val Met Gln Pro Cys Tyr His Xaa  
               
               
                                 2245                2250                2255  
               
               
                   
               
               
                 Thr Cys Arg Arg His Leu Thr Ala Thr Asn His Ser Leu Leu Xaa Arg  
               
               
                             2260                2265                2270  
               
               
                   
               
               
                 His Glu Tyr Val Gln Arg Ser Ile Tyr Ile Val Leu His Phe Tyr Thr  
               
               
                         2275                2280                2285  
               
               
                   
               
               
                 Val Xaa Glu Val Phe Ala Arg Phe Gly Pro Ser Gln Val His Lys Ile  
               
               
                     2290                2295                2300  
               
               
                   
               
               
                 Ile Asp Met Thr Ser Thr Leu Glu Arg Val Asn Pro Arg Ser Ser Gly  
               
               
                 2305                2310                2315                2320  
               
               
                   
               
               
                 Gly Ile Gly Leu Ile Xaa Leu Arg Gly Gly Arg Ser Pro Leu Xaa Xaa  
               
               
                                 2325                2330                2335  
               
               
                   
               
               
                 Pro Leu Ile Leu Asn Xaa Arg Xaa Ile Ser Xaa Gly Asp Arg Ser Pro  
               
               
                             2340                2345                2350  
               
               
                   
               
               
                 Leu Glu Leu Xaa Arg Gly Xaa  
               
               
                         2355  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 27  
               
               
                 &lt;211&gt; LENGTH: 4924  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 879, 3691, 4119  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 27  
               
               
                   
               
               
                 ggatcccaac ttttaggaat ggatcttaaa attttagtta taagttcaaa gttagaaaaa     60  
               
               
                   
               
               
                 tctttaccaa gagctttgag tccattgatg acatccgtga aacggtgtac atgtctccga    120  
               
               
                   
               
               
                 tggactcact tggtttcatt cggaaaagtt cgaaagagtg cataagaata ttgattttgg    180  
               
               
                   
               
               
                 attctttcac tcggttggtg ccttcatgag tgacctcaag agtcctccaa atatcaaaag    240  
               
               
                   
               
               
                 ccgaatcaca aattgaaatg tgattgaatt catttttgtc taatgcacaa aacagggcat    300  
               
               
                   
               
               
                 tcatagcctt tgtgtttaaa gcaaaaacat tcttctccga ttcatcccat tcgctcatcg    360  
               
               
                   
               
               
                 gaagagaaaa tttttgaaat ccattttcga caatagacca aagctcgaaa tccatggaaa    420  
               
               
                   
               
               
                 tgaggaagat cctcatatga gttttccaat acatgtaatt cgactcatta aacataggtg    480  
               
               
                   
               
               
                 gatgtgtaat gaaatgaccc tcatgcscta tctctcttgg gtattaaacc aaatatgaga    540  
               
               
                   
               
               
                 gtgagccttg ctctgatacc aattgttagg atcagagtgg cactaagaga gggggggagt    600  
               
               
                   
               
               
                 gaattagtgc agtggattaa aacttataag tttaaaaatg aattcgtaaa tacgagaaga    660  
               
               
                   
               
               
                 tttcgtttta atagtaactt gagtagatga aaaccaaaag ttaacagtag tgtaaataac    720  
               
               
                   
               
               
                 aatttcggga aagtaagaac tcacacattc aaggaacata ccaatttaaa gtggttcggt    780  
               
               
                   
               
               
                 caaaatgacc tacatccact tgtgaagcct tcttcgaaga ggctcccaac ttccactagc    840  
               
               
                   
               
               
                 aaatcacttt gaaggggaag gacaaatacc tctcttacna ccttttacaa tggttcatac    900  
               
               
                   
               
               
                 tcttacaaat tttcaacgag aaagaaggag gtgaacatgc aagcaattga aaacaagact    960  
               
               
                   
               
               
                 tgctaaagac tttgctaagg ctttttttct caatctattg cttctcaaaa gttgtattct   1020  
               
               
                   
               
               
                 ctgctgagaa ttgaggggta tttatagacc ccaagaggat ttaaatttgg gctccaaatt   1080  
               
               
                   
               
               
                 tcgaatgctc ttgggttccc gaggttgccg gtgccaccgc ctgtcagtgt ttgacactgg   1140  
               
               
                   
               
               
                 acagtgtact agcggtgcca ccgccggacc tctcgggtgt tgggcggtgc caccgcctag   1200  
               
               
                   
               
               
                 actttttcag ctcactggtt ggattccaaa cttgacccaa accagtccga actcgggtcc   1260  
               
               
                   
               
               
                 aattgacccg taaccggatt ataggattaa cccttaatcc taaccctaat tatatgcaaa   1320  
               
               
                   
               
               
                 ctacgcaact gaaaatatag tcctaagcaa gtttttaacc ggcaaacgtc gagtcttctt   1380  
               
               
                   
               
               
                 ccggcgatct ttcggcagac ttctgatata cctttggatt tcttctagcg gactcctagt   1440  
               
               
                   
               
               
                 agggtcccga tcttgtggcg agtttagcga gtagccgaac cttctcggtg atctccgcaa   1500  
               
               
                   
               
               
                 accgccgatg atctcttcgg cagactttcg aaaacttcga caagtccccg atttcttctc   1560  
               
               
                   
               
               
                 ggttggttcc gacagcatct ctaacgaaac ttcggactcc ttgaatgtcc atcgaacttg   1620  
               
               
                   
               
               
                 actccggtag gcttgcttta tattttcagg ctatcatagt taatcctaca tacttaactc   1680  
               
               
                   
               
               
                 aataatatgg attagattaa ttaacccatc aattgatttc atcatcaaaa ttcgacattc   1740  
               
               
                   
               
               
                 aacaaacatc cgtactcaat aacccatcag gctatagtta cgtgactatc tactgtgatc   1800  
               
               
                   
               
               
                 cgtacgtgaa gttagcgagt catgatccag gtcgtgtcac ttattggccg aacacgtatc   1860  
               
               
                   
               
               
                 ccttatccaa atccagtctt ctcaactctt ctagcctacc cgtctctttt tttattactt   1920  
               
               
                   
               
               
                 ttgaaagaat tcaaatcaaa acagatacaa aataacacgg tgagacactg tgacatgcta   1980  
               
               
                   
               
               
                 gtctctggaa agcattaatt cgcgcatcca cagacgtcgt cagcttcatc acccactttt   2040  
               
               
                   
               
               
                 tcctacataa ccatgtcgca tggctttgtt gatgacagac caccacaagc ttgcctttgg   2100  
               
               
                   
               
               
                 ttgtgcctaa cagagagaga gagacagacc gatagcctcc tcattcacta tggcgatccg   2160  
               
               
                   
               
               
                 atcgccagct tcgctgctgt tatttgcgtt cctgatgctt gcgctcacgg gaagactgca   2220  
               
               
                   
               
               
                 ggcccggcgc agctcatgca ttggcgtcta ctggggacaa aacaccgacg agggaagctt   2280  
               
               
                   
               
               
                 agcagatgct tgtgccacag gcaactacga atacgtgaac atcgccaccc ttttcaagtt   2340  
               
               
                   
               
               
                 tggcatgggc caaactccag agatcaacct cgccggccac tgtgaccctc ggaacaacgg   2400  
               
               
                   
               
               
                 ctgcgcgcgc ttgagcagcg aaatccagtc ctgccaggag cgtggcgtca aggtgatgct   2460  
               
               
                   
               
               
                 ctccatcgga ggtggcgggt cttatggcct gagttccacc gaagacgcca aggacgtagc   2520  
               
               
                   
               
               
                 gtcatacctc tggcacagtt tcttgggtgg ttctgctgct cgctactcga gacccctcgg   2580  
               
               
                   
               
               
                 ggatgcggtt ctggatggca tagacttcaa catcgccgga gggagcacag aacactatga   2640  
               
               
                   
               
               
                 tgaacttgcc gctttcctca aggcctacaa cgagcaggag gccggaacga agaaagttca   2700  
               
               
                   
               
               
                 cttgagtgct cgtccgcagt gtcctttccc ggattactgg cttggcaacg cactcagaac   2760  
               
               
                   
               
               
                 agatctcttc gacttcgtgt gggtgcagtt cttcaacaac ccttcgtgcc atttctccca   2820  
               
               
                   
               
               
                 gaacgctatc aatcttgcaa atgcgttcaa caattgggtc atgtccatcc ctgcgcaaaa   2880  
               
               
                   
               
               
                 gctgttcctt gggcttcctg ctgctcctga ggctgctcca actggtggct acattccacc   2940  
               
               
                   
               
               
                 ccatgatctc atatctaaag ttcttccgat cctaaaggat tccgacaagt acgcaggaat   3000  
               
               
                   
               
               
                 catgctgtgg actagatacc acgacagaaa ctccggctac agttctcaag tcaagtccca   3060  
               
               
                   
               
               
                 cgtgtgtcca gcgcgtcggt tctccaacat cttatctatg ccggtgaagt cttccaagta   3120  
               
               
                   
               
               
                 aacctgaacg gcgtagatga tcggtggtcg aaaactccga tcatcatggg tccccatccg   3180  
               
               
                   
               
               
                 tatccgtgcg ttgctacgtt atggtgtttc ccttgtatgt tggtcttttc aataatataa   3240  
               
               
                   
               
               
                 taaggggtta gttttacgtt tccatatttt ccatgttcga aaacagtata tttgctgccc   3300  
               
               
                   
               
               
                 cttccaaatt tgaaaaagat aaaataaata tataactaaa aatatcctct tttttttttc   3360  
               
               
                   
               
               
                 tttcgacaaa tatataactc ttaactttcc caattgttta agcaaaagat ataaatcctc   3420  
               
               
                   
               
               
                 ttccacacaa aagacgaatc catgattgct ggattgctgt ctactggtgc cgaaatggcg   3480  
               
               
                   
               
               
                 acgagagaag cttgtgctac ctgcaattac aagttcgtca acattgtctt ccttgccatg   3540  
               
               
                   
               
               
                 tttggtgacg ccatactccc gtgatcagga cacacctctg gaacagtttc ttgggaagtt   3600  
               
               
                   
               
               
                 aatcttcttc tcggctcctc ggcgaccaat cttgtgaggt tcttctcctg aatggtgtcc   3660  
               
               
                   
               
               
                 acttcgacat cgaaggtcta cctgagcgca natccacagt tccgactacg tgtgggtgca   3720  
               
               
                   
               
               
                 gttctactac acaggcaact cgcagatgcc cggtaacaat gggttctcca tcctgcatgg   3780  
               
               
                   
               
               
                 aaggtgttcc ctggacttcc tgctgctcct caggctgctg gaaggagctc cattccacta   3840  
               
               
                   
               
               
                 gtgatcttac acgtgtctta tcatcaagaa ttatagcaag taccgaggga ttattaaaat   3900  
               
               
                   
               
               
                 aaaaaaaaag ggaagaatgg gaattagaat taaaactgaa accggccatg aagaacgttt   3960  
               
               
                   
               
               
                 cgagtgaaga caaacgacag tatgagacgg tagtttgcta tggacatgga tcgttcccaa   4020  
               
               
                   
               
               
                 agcagtccaa gtctttatga accggtctat cggttcagcc ttcaagaacc gcgaggataa   4080  
               
               
                   
               
               
                 ccggcccaag agaaacaaca aattgtggtg agcttttant ataaaccgaa cggtgccgtc   4140  
               
               
                   
               
               
                 cgtcagatgt taaatggacg gcggatagat ctccagagta aatctgagga aaatcgttcc   4200  
               
               
                   
               
               
                 ggccccccta ccacgaccca cgcgatccgt cctctccccc accccctaca cctttttctt   4260  
               
               
                   
               
               
                 cttccgctcc tgcgatcggt tatttgattt tgtgtatgat atccaatttc ttttctggag   4320  
               
               
                   
               
               
                 tggtatccta ttctaatttc ttagattgtt gtattgaacc atcagttttg gtttaagcgc   4380  
               
               
                   
               
               
                 atgatggcgg agagtttcgg gagatgggag tcagatccct tgttttctgc tgccgaagtg   4440  
               
               
                   
               
               
                 gtgcaagatt cggccgatag gttttttctc tcattttaag ctcaattatg cggtcattct   4500  
               
               
                   
               
               
                 tgttaggctt tggagaattt gctctatttc gaaagaaatt gctgctttct agttttgatt   4560  
               
               
                   
               
               
                 agtccctata aaatttgctt tcggttctga atatccgaga atgtcgtatc gtcaatgacg   4620  
               
               
                   
               
               
                 attctttttt agaattctaa tactttgtcc tgttttctgt gatttaatgg agaaaatatt   4680  
               
               
                   
               
               
                 gttcctttta gtgatctatg ctctcccgac cattaggatg agggttgaag gtgaaaatac   4740  
               
               
                   
               
               
                 tttctggtaa ttttcctctc taaattcttc caaacacgac acaagtataa ttatagacca   4800  
               
               
                   
               
               
                 agattgattc ttcttatgca ccgattctca cttcccttcc ctctgtgtta tggttatcgt   4860  
               
               
                   
               
               
                 tgttactgat ggttgcttaa ctcatggggt agcgcctggg tgatccgttg acctgcaggt   4920  
               
               
                   
               
               
                 cgac                                                                4924  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 28  
               
               
                 &lt;211&gt; LENGTH: 4924  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 879, 3691, 4119  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 28  
               
               
                   
               
               
                 cctagggttg aaaatcctta cctagaattt taaaatcaat attcaagttt caatcttttt     60  
               
               
                   
               
               
                 agaaatggtt ctcgaaactc aggtaactac tgtaggcact ttgccacatg tacagaggct    120  
               
               
                   
               
               
                 acctgagtga accaaagtaa gccttttcaa gctttctcac gtattcttat aactaaaacc    180  
               
               
                   
               
               
                 taagaaagtg agccaaccac ggaagtactc actggagttc tcaggaggtt tatagttttc    240  
               
               
                   
               
               
                 ggcttagtgt ttaactttac actaacttaa gtaaaaacag attacgtgtt ttgtcccgta    300  
               
               
                   
               
               
                 agtatcggaa acacaaattt cgtttttgta agaagaggct aagtagggta agcgagtagc    360  
               
               
                   
               
               
                 cttctctttt aaaaacttta ggtaaaagct gttatctggt ttcgagcttt aggtaccttt    420  
               
               
                   
               
               
                 actccttcta ggagtatact caaaaggtta tgtacattaa gctgagtaat ttgtatccac    480  
               
               
                   
               
               
                 ctacacatta ctttactggg agtacgsgat agagagaacc cataatttgg tttatactct    540  
               
               
                   
               
               
                 cactcggaac gagactatgg ttaacaatcc tagtctcacc gtgattctct ccccccctca    600  
               
               
                   
               
               
                 cttaatcacg tcacctaatt ttgaatattc aaatttttac ttaagcattt atgctcttct    660  
               
               
                   
               
               
                 aaagcaaaat tatcattgaa ctcatctact tttggttttc aattgtcatc acatttattg    720  
               
               
                   
               
               
                 ttaaagccct ttcattcttg agtgtgtaag ttccttgtat ggttaaattt caccaagcca    780  
               
               
                   
               
               
                 gttttactgg atgtaggtga acacttcgga agaagcttct ccgagggttg aaggtgatcg    840  
               
               
                   
               
               
                 tttagtgaaa cttccccttc ctgtttatgg agagaatgnt ggaaaatgtt accaagtatg    900  
               
               
                   
               
               
                 agaatgttta aaagttgctc tttcttcctc cacttgtacg ttcgttaact tttgttctga    960  
               
               
                   
               
               
                 acgatttctg aaacgattcc gaaaaaaaga gttagataac gaagagtttt caacataaga   1020  
               
               
                   
               
               
                 gacgactctt aactccccat aaatatctgg ggttctccta aatttaaacc cgaggtttaa   1080  
               
               
                   
               
               
                 agcttacgag aacccaaggg ctccaacggc cacggtggcg gacagtcaca aactgtgacc   1140  
               
               
                   
               
               
                 tgtcacatga tcgccacggt ggcggcctgg agagcccaca acccgccacg gtggcggatc   1200  
               
               
                   
               
               
                 tgaaaaagtc gagtgaccaa cctaaggttt gaactgggtt tggtcaggct tgagcccagg   1260  
               
               
                   
               
               
                 ttaactgggc attggcctaa tatcctaatt gggaattagg attgggatta atatacgttt   1320  
               
               
                   
               
               
                 gatgcgttga cttttatatc aggattcgtt caaaaattgg ccgtttgcag ctcagaagaa   1380  
               
               
                   
               
               
                 ggccgctaga aagccgtctg aagactatat ggaaacctaa agaagatcgc ctgaggatca   1440  
               
               
                   
               
               
                 tcccagggct agaacaccgc tcaaatcgct catcggcttg gaagagccac tagaggcgtt   1500  
               
               
                   
               
               
                 tggcggctac tagagaagcc gtctgaaagc ttttgaagct gttcaggggc taaagaagag   1560  
               
               
                   
               
               
                 ccaaccaagg ctgtcgtaga gattgctttg aagcctgagg aacttacagg tagcttgaac   1620  
               
               
                   
               
               
                 tgaggccatc cgaacgaaat ataaaagtcc gatagtatca attaggatgt atgaattgag   1680  
               
               
                   
               
               
                 ttattatacc taatctaatt aattgggtag ttaactaaag tagtagtttt aagctgtaag   1740  
               
               
                   
               
               
                 ttgtttgtag gcatgagtta ttgggtagtc cgatatcaat gcactgatag atgacactag   1800  
               
               
                   
               
               
                 gcatgcactt caatcgctca gtactaggtc cagcacagtg aataaccggc ttgtgcatag   1860  
               
               
                   
               
               
                 ggaataggtt taggtcagaa gagttgagaa gatcggatgg gcagagaaaa aaataatgaa   1920  
               
               
                   
               
               
                 aactttctta agtttagttt tgtctatgtt ttattgtgcc actctgtgac actgtacgat   1980  
               
               
                   
               
               
                 cagagacctt tcgtaattaa gcgcgtaggt gtctgcagca gtcgaagtag tgggtgaaaa   2040  
               
               
                   
               
               
                 aggatgtatt ggtacagcgt accgaaacaa ctactgtctg gtggtgttcg aacggaaacc   2100  
               
               
                   
               
               
                 aacacggatt gtctctctct ctctgtctgg ctatcggagg agtaagtgat accgctaggc   2160  
               
               
                   
               
               
                 tagcggtcga agcgacgaca ataaacgcaa ggactacgaa cgcgagtgcc cttctgacgt   2220  
               
               
                   
               
               
                 ccgggccgcg tcgagtacgt aaccgcagat gacccctgtt ttgtggctgc tcccttcgaa   2280  
               
               
                   
               
               
                 tcgtctacga acacggtgtc cgttgatgct tatgcacttg tagcggtggg aaaagttcaa   2340  
               
               
                   
               
               
                 accgtacccg gtttgaggtc tctagttgga gcggccggtg acactgggag ccttgttgcc   2400  
               
               
                   
               
               
                 gacgcgcgcg aactcgtcgc tttaggtcag gacggtcctc gcaccgcagt tccactacga   2460  
               
               
                   
               
               
                 gaggtagcct ccaccgccca gaataccgga ctcaaggtgg cttctgcggt tcctgcatcg   2520  
               
               
                   
               
               
                 cagtatggag accgtgtcaa agaacccacc aagacgacga gcgatgagct ctggggagcc   2580  
               
               
                   
               
               
                 cctacgccaa gacctaccgt atctgaagtt gtagcggcct ccctcgtgtc ttgtgatact   2640  
               
               
                   
               
               
                 acttgaacgg cgaaaggagt tccggatgtt gctcgtcctc cggccttgct tctttcaagt   2700  
               
               
                   
               
               
                 gaactcacga gcaggcgtca caggaaaggg cctaatgacc gaaccgttgc gtgagtcttg   2760  
               
               
                   
               
               
                 tctagagaag ctgaagcaca cccacgtcaa gaagttgttg ggaagcacgg taaagagggt   2820  
               
               
                   
               
               
                 cttgcgatag ttagaacgtt tacgcaagtt gttaacccag tacaggtagg gacgcgtttt   2880  
               
               
                   
               
               
                 cgacaaggaa cccgaaggac gacgaggact ccgacgaggt tgaccaccga tgtaaggtgg   2940  
               
               
                   
               
               
                 ggtactagag tatagatttc aagaaggcta ggatttccta aggctgttca tgcgtcctta   3000  
               
               
                   
               
               
                 gtacgacacc tgatctatgg tgctgtcttt gaggccgatg tcaagagttc agttcagggt   3060  
               
               
                   
               
               
                 gcacacaggt cgcgcagcca agaggttgta gaatagatac ggccacttca gaaggttcat   3120  
               
               
                   
               
               
                 ttggacttgc cgcatctact agccaccagc ttttgaggct agtagtaccc aggggtaggc   3180  
               
               
                   
               
               
                 ataggcacgc aacgatgcaa taccacaaag ggaacataca accagaaaag ttattatatt   3240  
               
               
                   
               
               
                 attccccaat caaaatgcaa aggtataaaa ggtacaagct tttgtcatat aaacgacggg   3300  
               
               
                   
               
               
                 gaaggtttaa actttttcta ttttatttat atattgattt ttataggaga aaaaaaaaag   3360  
               
               
                   
               
               
                 aaagctgttt atatattgag aattgaaagg gttaacaaat tcgttttcta tatttaggag   3420  
               
               
                   
               
               
                 aaggtgtgtt ttctgcttag gtactaacga cctaacgaca gatgaccacg gctttaccgc   3480  
               
               
                   
               
               
                 tgctctcttc gaacacgatg gacgttaatg ttcaagcagt tgtaacagaa ggaacggtac   3540  
               
               
                   
               
               
                 aaaccactgc ggtatgaggg cactagtcct gtgtggagac cttgtcaaag aacccttcaa   3600  
               
               
                   
               
               
                 ttagaagaag agccgaggag ccgctggtta gaacactcca agaagaggac ttaccacagg   3660  
               
               
                   
               
               
                 tgaagctgta gcttccagat ggactcgcgt ntaggtgtca aggctgatgc acacccacgt   3720  
               
               
                   
               
               
                 caagatgatg tgtccgttga gcgtctacgg gccattgtta cccaagaggt aggacgtacc   3780  
               
               
                   
               
               
                 ttccacaagg gacctgaagg acgacgagga gtccgacgac cttcctcgag gtaaggtgat   3840  
               
               
                   
               
               
                 cactagaatg tgcacagaat agtagttctt aatatcgttc atggctccct aataatttta   3900  
               
               
                   
               
               
                 tttttttttc ccttcttacc cttaatctta attttgactt tggccggtac ttcttgcaaa   3960  
               
               
                   
               
               
                 gctcacttct gtttgctgtc atactctgcc atcaaacgat acctgtacct agcaagggtt   4020  
               
               
                   
               
               
                 tcgtcaggtt cagaaatact tggccagata gccaagtcgg aagttcttgg cgctcctatt   4080  
               
               
                   
               
               
                 ggccgggttc tctttgttgt ttaacaccac tcgaaaatna tatttggctt gccacggcag   4140  
               
               
                   
               
               
                 gcagtctaca atttacctgc cgcctatcta gaggtctcat ttagactcct tttagcaagg   4200  
               
               
                   
               
               
                 ccggggggat ggtgctgggt gcgctaggca ggagaggggg tgggggatgt ggaaaaagaa   4260  
               
               
                   
               
               
                 gaaggcgagg acgctagcca ataaactaaa acacatacta taggttaaag aaaagacctc   4320  
               
               
                   
               
               
                 accataggat aagattaaag aatctaacaa cataacttgg tagtcaaaac caaattcgcg   4380  
               
               
                   
               
               
                 tactaccgcc tctcaaagcc ctctaccctc agtctaggga acaaaagacg acggcttcac   4440  
               
               
                   
               
               
                 cacgttctaa gccggctatc caaaaaagag agtaaaattc gagttaatac gccagtaaga   4500  
               
               
                   
               
               
                 acaatccgaa acctcttaaa cgagataaag ctttctttaa cgacgaaaga tcaaaactaa   4560  
               
               
                   
               
               
                 tcagggatat tttaaacgaa agccaagact tataggctct tacagcatag cagttactgc   4620  
               
               
                   
               
               
                 taagaaaaaa tcttaagatt atgaaacagg acaaaagaca ctaaattacc tcttttataa   4680  
               
               
                   
               
               
                 caaggaaaat cactagatac gagagggctg gtaatcctac tcccaacttc cacttttatg   4740  
               
               
                   
               
               
                 aaagaccatt aaaaggagag atttaagaag gtttgtgctg tgttcatatt aatatctggt   4800  
               
               
                   
               
               
                 tctaactaag aagaatacgt ggctaagagt gaagggaagg gagacacaat accaatagca   4860  
               
               
                   
               
               
                 acaatgacta ccaacgaatt gagtacccca tcgcggaccc actaggcaac tggacgtcca   4920  
               
               
                   
               
               
                 gctg                                                                4924  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 29  
               
               
                 &lt;211&gt; LENGTH: 1568  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 1180, 1313  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 29  
               
               
                   
               
               
                 Gly Ser Gln Leu Leu Gly Met Asp Leu Lys Ile Leu Val Ile Ser Ser  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Lys Leu Glu Lys Ser Leu Pro Arg Ala Leu Ser Pro Leu Met Thr Ser  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Val Lys Arg Cys Thr Cys Leu Arg Trp Thr His Leu Val Ser Phe Gly  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Lys Val Arg Lys Ser Ala Glu Tyr Phe Trp Ile Leu Ser Leu Gly Trp  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Cys Leu His Glu Pro Gln Glu Ser Ser Lys Tyr Gln Lys Pro Asn His  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Lys Leu Lys Cys Asp Ile His Phe Cys Leu Met His Lys Thr Gly His  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Ser Pro Leu Cys Leu Lys Gln Lys His Ser Ser Pro Ile His Pro Ile  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Arg Ser Ser Glu Glu Lys Ile Phe Glu Ile His Phe Arg Gln Thr Lys  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Ala Arg Asn Pro Trp Lys Gly Arg Ser Ser Tyr Glu Phe Ser Asn Thr  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Cys Asn Ser Thr His Thr Val Asp Val Asn Asp Pro His Ala Leu Ser  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Leu Leu Gly Ile Lys Pro Asn Met Arg Val Ser Leu Ala Leu Ile Pro  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Ile Val Arg Ile Arg Val Ala Leu Arg Glu Gly Gly Ser Glu Leu Val  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Gln Trp Ile Lys Thr Tyr Lys Phe Lys Asn Glu Phe Val Asn Thr Arg  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Arg Phe Arg Phe Asn Ser Asn Leu Ser Arg Lys Pro Lys Val Asn Ser  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ser Val Asn Asn Asn Phe Gly Lys Val Arg Thr His Thr Phe Lys Glu  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 His Thr Asn Leu Lys Trp Phe Gly Gln Asn Asp Leu His Pro Leu Val  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Lys Pro Ser Ser Lys Arg Leu Pro Thr Ser Thr Ser Lys Ser Leu Arg  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly Arg Thr Asn Thr Ser Leu Thr Thr Phe Tyr Asn Gly Ser Tyr Ser  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Tyr Lys Phe Ser Thr Arg Lys Lys Glu Val Asn Met Gln Ala Ile Glu  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Asn Lys Thr Cys Arg Leu Cys Gly Phe Phe Ser Gln Ser Ile Ala Ser  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Gln Lys Leu Tyr Ser Leu Leu Arg Ile Glu Gly Tyr Leu Thr Pro Arg  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Gly Phe Lys Phe Gly Leu Gln Ile Ser Asn Ala Leu Gly Phe Pro Arg  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Leu Pro Val Pro Pro Pro Val Ser Val His Trp Thr Val Tyr Arg Cys  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 His Arg Arg Thr Ser Arg Val Leu Gly Gly Ala Thr Ala Thr Phe Ser  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Ala His Trp Leu Asp Ser Lys Leu Asp Pro Asn Gln Ser Glu Leu Gly  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Ser Asn Pro Val Thr Gly Leu Asp Pro Leu Ile Leu Thr Leu Ile Ile  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Cys Lys Leu Arg Asn Lys Tyr Ser Pro Lys Gln Val Phe Asn Arg Gln  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Thr Ser Ser Leu Leu Pro Ala Ile Phe Arg Gln Thr Ser Asp Ile Pro  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Leu Asp Phe Phe Arg Thr Pro Ser Arg Val Pro Ile Leu Trp Arg Val  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Arg Val Ala Glu Pro Ser Arg Ser Pro Gln Thr Ala Asp Asp Leu Phe  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Gly Arg Leu Ser Lys Thr Ser Thr Ser Pro Arg Phe Leu Leu Gly Trp  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Phe Arg Gln His Leu Arg Asn Phe Gly Leu Leu Glu Cys Pro Ser Asn  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Leu Thr Pro Val Gly Leu Leu Tyr Ile Phe Arg Leu Ser Leu Ile Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 His Thr Leu Asn Asn Met Asp Ile Asn Pro Ile Asn Phe His His Gln  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Asn Ser Thr Phe Asn Lys His Pro Tyr Ser Ile Thr His Gln Ala Ile  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Val Thr Leu Ser Thr Val Ile Thr Arg Ser Arg Val Met Ile Gln Val  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Val Ser Leu Ile Gly Arg Thr Arg Ile Pro Tyr Pro Asn Pro Val Phe  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Ser Thr Leu Leu Ala Tyr Pro Ser Leu Phe Leu Leu Leu Leu Lys Glu  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Phe Lys Ser Lys Gln Ile Gln Asn Asn Thr Val Arg His Cys Asp Met  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Leu Val Ser Gly Lys His Phe Ala His Pro Gln Thr Ser Ser Ala Ser  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Ser Pro Thr Phe Ser Tyr Ile Thr Met Ser His Gly Phe Val Asp Asp  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                 Arg Pro Pro Gln Ala Cys Leu Trp Leu Cys Leu Thr Glu Arg Glu Arg  
               
               
                             660                 665                 670  
               
               
                   
               
               
                 Gln Thr Asp Ser Leu Leu Ile His Tyr Gly Asp Pro Ile Ala Ser Phe  
               
               
                         675                 680                 685  
               
               
                   
               
               
                 Ala Ala Val Ile Cys Val Pro Asp Ala Cys Ala His Gly Lys Thr Ala  
               
               
                     690                 695                 700  
               
               
                   
               
               
                 Gly Pro Ala Gln Leu Met His Trp Arg Leu Leu Gly Thr Lys His Arg  
               
               
                 705                 710                 715                 720  
               
               
                   
               
               
                 Arg Gly Lys Leu Ser Arg Cys Leu Cys His Arg Gln Leu Arg Ile Arg  
               
               
                                 725                 730                 735  
               
               
                   
               
               
                 Glu His Arg His Pro Phe Gln Val Trp His Gly Pro Asn Ser Arg Asp  
               
               
                             740                 745                 750  
               
               
                   
               
               
                 Gln Pro Arg Arg Pro Leu Pro Ser Glu Gln Arg Leu Arg Ala Leu Glu  
               
               
                         755                 760                 765  
               
               
                   
               
               
                 Gln Arg Asn Pro Val Leu Pro Gly Ala Trp Arg Gln Gly Asp Ala Leu  
               
               
                     770                 775                 780  
               
               
                   
               
               
                 His Arg Arg Trp Arg Val Leu Trp Pro Glu Phe His Arg Arg Arg Gln  
               
               
                 785                 790                 795                 800  
               
               
                   
               
               
                 Gly Arg Ser Val Ile Pro Leu Ala Gln Phe Leu Gly Trp Phe Cys Cys  
               
               
                                 805                 810                 815  
               
               
                   
               
               
                 Ser Leu Leu Glu Thr Pro Arg Gly Cys Gly Ser Gly Trp His Arg Leu  
               
               
                             820                 825                 830  
               
               
                   
               
               
                 Gln His Arg Arg Arg Glu His Arg Thr Leu Thr Cys Arg Phe Pro Gln  
               
               
                         835                 840                 845  
               
               
                   
               
               
                 Gly Leu Gln Arg Ala Gly Gly Arg Asn Glu Glu Ser Ser Leu Glu Cys  
               
               
                     850                 855                 860  
               
               
                   
               
               
                 Ser Ser Ala Val Ser Phe Pro Gly Leu Leu Ala Trp Gln Arg Thr Gln  
               
               
                 865                 870                 875                 880  
               
               
                   
               
               
                 Asn Arg Ser Leu Arg Leu Arg Val Gly Ala Val Leu Gln Gln Pro Phe  
               
               
                                 885                 890                 895  
               
               
                   
               
               
                 Val Pro Phe Leu Pro Glu Arg Tyr Gln Ser Cys Lys Cys Val Gln Gln  
               
               
                             900                 905                 910  
               
               
                   
               
               
                 Leu Gly His Val His Pro Cys Ala Lys Ala Val Pro Trp Ala Ser Cys  
               
               
                         915                 920                 925  
               
               
                   
               
               
                 Cys Ser Gly Cys Ser Asn Trp Trp Leu His Ser Thr Pro Ser His Ile  
               
               
                     930                 935                 940  
               
               
                   
               
               
                 Ser Ser Ser Asp Pro Lys Gly Phe Arg Gln Val Arg Arg Asn His Ala  
               
               
                 945                 950                 955                 960  
               
               
                   
               
               
                 Val Asp Ile Pro Arg Gln Lys Leu Arg Leu Gln Phe Ser Ser Gln Val  
               
               
                                 965                 970                 975  
               
               
                   
               
               
                 Pro Arg Val Ser Ser Ala Ser Val Leu Gln His Leu Ile Tyr Ala Gly  
               
               
                             980                 985                 990  
               
               
                   
               
               
                 Glu Val Phe Gln Val Asn Leu Asn Gly Val Asp Asp Arg Trp Ser Lys  
               
               
                         995                 1000                1005  
               
               
                   
               
               
                 Thr Pro Ile Ile Met Gly Pro His Pro Tyr Pro Cys Val Ala Thr Leu  
               
               
                     1010                1015                1020  
               
               
                   
               
               
                 Trp Cys Phe Pro Cys Met Leu Val Phe Ser Ile Ile Gly Val Ser Phe  
               
               
                 1025                1030                1035                1040  
               
               
                   
               
               
                 Thr Phe Pro Tyr Phe Pro Cys Ser Lys Thr Val Tyr Leu Leu Pro Leu  
               
               
                                 1045                1050                1055  
               
               
                   
               
               
                 Pro Asn Leu Lys Lys Ile Lys Ile Tyr Asn Lys Tyr Pro Leu Phe Phe  
               
               
                             1060                1065                1070  
               
               
                   
               
               
                 Phe Phe Arg Gln Ile Tyr Asn Ser Leu Ser Gln Leu Phe Lys Gln Lys  
               
               
                         1075                1080                1085  
               
               
                   
               
               
                 Ile Ile Leu Phe His Thr Lys Asp Glu Ser Met Ile Ala Gly Leu Leu  
               
               
                     1090                1095                1100  
               
               
                   
               
               
                 Ser Thr Gly Ala Glu Met Ala Thr Arg Glu Ala Cys Ala Thr Cys Asn  
               
               
                 1105                1110                1115                1120  
               
               
                   
               
               
                 Tyr Lys Phe Val Asn Ile Val Phe Leu Ala Met Phe Gly Asp Ala Ile  
               
               
                                 1125                1130                1135  
               
               
                   
               
               
                 Leu Pro Ser Gly His Thr Ser Gly Thr Val Ser Trp Glu Val Asn Leu  
               
               
                             1140                1145                1150  
               
               
                   
               
               
                 Leu Leu Gly Ser Ser Ala Thr Asn Leu Val Arg Phe Phe Ser Met Val  
               
               
                         1155                1160                1165  
               
               
                   
               
               
                 Ser Thr Ser Thr Ser Lys Val Tyr Leu Ser Ala Xaa Pro Gln Phe Arg  
               
               
                     1170                1175                1180  
               
               
                   
               
               
                 Leu Arg Val Gly Ala Val Leu Leu His Arg Gln Leu Ala Asp Ala Arg  
               
               
                 1185                1190                1195                1200  
               
               
                   
               
               
                 Gln Trp Val Leu His Pro Ala Trp Lys Val Phe Pro Gly Leu Pro Ala  
               
               
                                 1205                1210                1215  
               
               
                   
               
               
                 Ala Pro Gln Ala Ala Gly Arg Ser Ser Ile Pro Leu Val Ile Leu His  
               
               
                             1220                1225                1230  
               
               
                   
               
               
                 Val Ser Tyr His Gln Glu Leu Gln Val Pro Arg Asp Tyr Asn Lys Lys  
               
               
                         1235                1240                1245  
               
               
                   
               
               
                 Lys Gly Lys Asn Gly Asn Asn Asn Asn Arg Pro Arg Thr Phe Arg Val  
               
               
                     1250                1255                1260  
               
               
                   
               
               
                 Lys Thr Asn Asp Ser Met Arg Arg Phe Ala Met Asp Met Asp Arg Ser  
               
               
                 1265                1270                1275                1280  
               
               
                   
               
               
                 Gln Ser Ser Pro Ser Leu Tyr Glu Pro Val Tyr Arg Phe Ser Leu Gln  
               
               
                                 1285                1290                1295  
               
               
                   
               
               
                 Glu Pro Arg Gly Pro Ala Gln Glu Lys Gln Gln Ile Val Val Ser Phe  
               
               
                             1300                1305                1310  
               
               
                   
               
               
                 Xaa Tyr Lys Pro Asn Gly Ala Val Arg Gln Met Leu Asn Gly Arg Arg  
               
               
                         1315                1320                1325  
               
               
                   
               
               
                 Ile Asp Leu Gln Ser Lys Ser Glu Glu Asn Arg Ser Gly Pro Pro Thr  
               
               
                     1330                1335                1340  
               
               
                   
               
               
                 Thr Thr His Ala Ile Arg Pro Leu Pro His Pro Leu His Leu Phe Leu  
               
               
                 1345                1350                1355                1360  
               
               
                   
               
               
                 Leu Pro Leu Leu Arg Ser Val Ile Phe Cys Val Tyr Pro Ile Ser Phe  
               
               
                                 1365                1370                1375  
               
               
                   
               
               
                 Leu Glu Trp Tyr Pro Ile Leu Ile Ser Ile Val Val Leu Asn His Gln  
               
               
                             1380                1385                1390  
               
               
                   
               
               
                 Phe Trp Phe Lys Arg Met Met Ala Glu Ser Phe Gly Arg Trp Glu Ser  
               
               
                         1395                1400                1405  
               
               
                   
               
               
                 Asp Pro Leu Phe Ser Ala Ala Glu Val Val Gln Asp Ser Ala Asp Arg  
               
               
                     1410                1415                1420  
               
               
                   
               
               
                 Phe Phe Leu Ser Phe Ala Gln Leu Cys Gly His Ser Cys Ala Leu Glu  
               
               
                 1425                1430                1435                1440  
               
               
                   
               
               
                 Asn Leu Leu Tyr Phe Glu Arg Asn Cys Cys Phe Leu Val Leu Ile Ser  
               
               
                                 1445                1450                1455  
               
               
                   
               
               
                 Pro Tyr Lys Ile Cys Phe Arg Phe Ile Ser Glu Asn Val Val Ser Ser  
               
               
                             1460                1465                1470  
               
               
                   
               
               
                 Met Thr Ile Leu Phe Asn Ser Asn Thr Leu Ser Cys Phe Leu Phe Asn  
               
               
                         1475                1480                1485  
               
               
                   
               
               
                 Gly Glu Asn Ile Val Pro Phe Ser Asp Leu Cys Ser Pro Asp His Asp  
               
               
                     1490                1495                1500  
               
               
                   
               
               
                 Glu Gly Arg Lys Tyr Phe Leu Val Ile Phe Leu Ser Lys Phe Phe Gln  
               
               
                 1505                1510                1515                1520  
               
               
                   
               
               
                 Thr Arg His Lys Tyr Asn Tyr Arg Pro Arg Leu Ile Leu Leu Met His  
               
               
                                 1525                1530                1535  
               
               
                   
               
               
                 Arg Phe Ser Leu Pro Phe Pro Leu Cys Tyr Gly Tyr Arg Cys Tyr Trp  
               
               
                             1540                1545                1550  
               
               
                   
               
               
                 Leu Leu Asn Ser Trp Gly Ser Ala Trp Val Ile Arg Pro Ala Gly Arg  
               
               
                         1555                1560                1565  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 30  
               
               
                 &lt;211&gt; LENGTH: 1574  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 158, 271, 1179, 1317  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 30  
               
               
                   
               
               
                 Asp Pro Asn Phe Glu Trp Ile Leu Lys Phe Leu Val Gln Ser Lys Asn  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Tyr Gln Glu Leu Val His His Pro Asn Gly Val His Val Ser Asp  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Gly Leu Thr Trp Phe His Ser Glu Lys Phe Glu Arg Val His Lys Asn  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ile Asp Phe Gly Phe Phe His Ser Val Gly Ala Phe Met Ser Asp Leu  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Lys Ser Pro Pro Asn Ile Lys Ser Arg Ile Thr Asn Asn Val Ile Glu  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Phe Ile Phe Val Cys Thr Lys Gln Gly Ile His Ser Leu Cys Val Ser  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Lys Asn Ile Leu Leu Arg Phe Ile Pro Phe Ala His Arg Lys Arg Lys  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Phe Leu Lys Ser Ile Phe Asp Asn Arg Pro Lys Leu Glu Ile His Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Asn Glu Glu Asp Pro His Met Ser Phe Pro Ile His Val Ile Arg Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Ile Lys His Arg Trp Met Cys Asn Glu Met Thr Leu Met Xaa Tyr Leu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Ser Trp Val Leu Asn Gln Ile Glu Ala Leu Leu Tyr Gln Leu Leu Gly  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Ser Glu Trp His Glu Arg Gly Gly Val Asn Cys Ser Gly Leu Lys Leu  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ile Ser Leu Lys Met Asn Ser Ile Arg Glu Asp Phe Val Leu Ile Val  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Thr Val Asp Glu Asn Gln Lys Leu Thr Val Val Ile Thr Ile Ser Gly  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Lys Glu Leu Thr His Ser Arg Asn Ile Pro Ile Ser Gly Ser Val Lys  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Met Thr Tyr Ile His Leu Ser Leu Leu Arg Arg Gly Ser Gln Leu Pro  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Leu Ala Asn His Phe Glu Gly Glu Gly Gln Ile Pro Leu Leu Xaa Pro  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Phe Thr Met Val His Thr Leu Thr Asn Phe Gln Arg Glu Arg Arg Arg  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Thr Cys Lys Gln Leu Lys Thr Arg Leu Ala Lys Asp Phe Ala Lys Ala  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Phe Phe Leu Asn Leu Leu Leu Leu Lys Ser Cys Ile Leu Cys Glu Leu  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Arg Gly Ile Tyr Arg Pro Gln Glu Asp Leu Asn Leu Gly Ser Lys Phe  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Arg Met Leu Leu Gly Ser Arg Gly Cys Arg Cys His Arg Leu Ser Val  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Phe Asp Thr Gly Gln Cys Thr Ser Gly Ala Thr Ala Gly Pro Leu Gly  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Cys Trp Ala Val Pro Pro Pro Arg Leu Phe Gln Leu Thr Gly Trp Ile  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Pro Asn Leu Thr Gln Thr Ser Pro Asn Ser Gly Pro Ile Asp Pro Pro  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Asp Tyr Arg Ile Asn Pro Ser Pro Leu Tyr Ala Asn Tyr Ala Thr Glu  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Asn Ile Val Leu Ser Lys Phe Leu Thr Gly Lys Arg Arg Val Phe Phe  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Arg Arg Ser Phe Gly Arg Leu Leu Ile Tyr Leu Trp Ile Ser Ser Ser  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Gly Leu Leu Val Gly Ser Arg Ser Cys Gly Glu Phe Ser Glu Pro Asn  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Leu Leu Gly Asp Leu Arg Lys Pro Pro Met Ile Ser Ser Ala Asp Phe  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Arg Lys Leu Arg Gln Val Pro Asp Phe Phe Ser Val Gly Ser Asp Ser  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Ile Ser Asn Glu Thr Ser Asp Ser Leu Asn Val His Arg Thr Leu Arg  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Ala Cys Phe Ile Phe Ser Gly Tyr His Ser Ser Tyr Ile Leu Asn Ser  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ile Ile Trp Ile Arg Leu Ile Asn Pro Ser Ile Asp Phe Ile Ile Lys  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Ile Arg His Ser Thr Asn Ile Arg Thr Gln Pro Ile Arg Leu Leu Arg  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Asp Tyr Leu Leu Ser Val Arg Glu Val Ser Glu Ser Ser Arg Ser Cys  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 His Leu Leu Ala Glu His Val Ser Leu Ile Gln Ile Gln Ser Ser Gln  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Leu Phe Pro Thr Arg Leu Phe Phe Tyr Tyr Phe Lys Asn Ser Asn Gln  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Asn Arg Tyr Lys Ile Thr Arg Asp Thr Val Thr Cys Ser Leu Glu Ser  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Ile Asn Ser Arg Ile His Arg Arg Arg Gln Leu His His Pro Leu Phe  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Pro Thr Pro Cys Arg Met Ala Leu Leu Met Thr Asp His His Lys Leu  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                 Ala Phe Gly Cys Ala Gln Arg Glu Arg Asp Arg Pro Ile Ala Ser Ser  
               
               
                             660                 665                 670  
               
               
                   
               
               
                 Phe Thr Met Ala Ile Arg Ser Pro Ala Ser Leu Leu Leu Phe Ala Phe  
               
               
                         675                 680                 685  
               
               
                   
               
               
                 Leu Met Leu Ala Leu Thr Gly Arg Leu Gln Ala Arg Arg Ser Ser Cys  
               
               
                     690                 695                 700  
               
               
                   
               
               
                 Ile Gly Val Tyr Trp Gly Gln Asn Thr Asp Glu Gly Ser Leu Ala Asp  
               
               
                 705                 710                 715                 720  
               
               
                   
               
               
                 Ala Cys Ala Thr Gly Asn Tyr Glu Tyr Val Asn Ile Ala Thr Leu Phe  
               
               
                                 725                 730                 735  
               
               
                   
               
               
                 Lys Phe Gly Met Gly Gln Thr Pro Glu Ile Asn Leu Ala Gly His Cys  
               
               
                             740                 745                 750  
               
               
                   
               
               
                 Asp Pro Arg Asn Asn Gly Cys Ala Arg Leu Ser Ser Glu Ile Gln Ser  
               
               
                         755                 760                 765  
               
               
                   
               
               
                 Cys Gln Glu Arg Gly Val Lys Val Met Leu Ser Ile Gly Gly Gly Gly  
               
               
                     770                 775                 780  
               
               
                   
               
               
                 Ser Tyr Gly Leu Ser Ser Thr Glu Asp Ala Lys Asp Val Ala Ser Tyr  
               
               
                 785                 790                 795                 800  
               
               
                   
               
               
                 Leu Trp His Ser Phe Leu Gly Gly Ser Ala Ala Arg Tyr Ser Arg Pro  
               
               
                                 805                 810                 815  
               
               
                   
               
               
                 Leu Gly Asp Ala Val Leu Asp Gly Ile Asp Phe Asn Ile Ala Gly Gly  
               
               
                             820                 825                 830  
               
               
                   
               
               
                 Ser Thr Glu His Tyr Asp Glu Leu Ala Ala Phe Leu Lys Ala Tyr Asn  
               
               
                         835                 840                 845  
               
               
                   
               
               
                 Glu Gln Glu Ala Gly Thr Lys Lys Val His Leu Ser Ala Arg Pro Gln  
               
               
                     850                 855                 860  
               
               
                   
               
               
                 Cys Pro Phe Pro Asp Tyr Trp Leu Gly Asn Ala Leu Arg Thr Asp Leu  
               
               
                 865                 870                 875                 880  
               
               
                   
               
               
                 Phe Asp Phe Val Trp Val Gln Phe Phe Asn Asn Pro Ser Cys His Phe  
               
               
                                 885                 890                 895  
               
               
                   
               
               
                 Ser Gln Asn Ala Ile Asn Leu Ala Asn Ala Phe Asn Asn Trp Val Met  
               
               
                             900                 905                 910  
               
               
                   
               
               
                 Ser Ile Pro Ala Gln Lys Leu Phe Leu Gly Leu Pro Ala Ala Pro Glu  
               
               
                         915                 920                 925  
               
               
                   
               
               
                 Ala Ala Pro Thr Gly Gly Tyr Ile Pro Pro His Asp Leu Ile Ser Lys  
               
               
                     930                 935                 940  
               
               
                   
               
               
                 Val Leu Pro Ile Leu Lys Asp Ser Asp Lys Tyr Ala Gly Ile Met Leu  
               
               
                 945                 950                 955                 960  
               
               
                   
               
               
                 Trp Thr Arg Tyr His Asp Arg Asn Ser Gly Tyr Ser Ser Gln Val Lys  
               
               
                                 965                 970                 975  
               
               
                   
               
               
                 Ser His Val Cys Pro Ala Arg Arg Phe Ser Asn Ile Leu Ser Met Pro  
               
               
                             980                 985                 990  
               
               
                   
               
               
                 Val Lys Ser Ser Lys Thr Thr Ala Met Ile Gly Gly Arg Lys Leu Arg  
               
               
                         995                 1000                1005  
               
               
                   
               
               
                 Ser Ser Trp Val Pro Ile Arg Ile Arg Ala Leu Leu Arg Tyr Gly Val  
               
               
                     1010                1015                1020  
               
               
                   
               
               
                 Ser Leu Val Cys Trp Ser Phe Gln Tyr Asn Lys Gly Leu Val Leu Arg  
               
               
                 1025                1030                1035                1040  
               
               
                   
               
               
                 Phe His Ile Phe His Val Arg Lys Gln Tyr Ile Cys Cys Pro Phe Gln  
               
               
                                 1045                1050                1055  
               
               
                   
               
               
                 Ile Lys Arg Asn Lys Tyr Ile Thr Lys Asn Ile Leu Phe Phe Phe Ser  
               
               
                             1060                1065                1070  
               
               
                   
               
               
                 Phe Asp Lys Tyr Ile Thr Leu Asn Phe Pro Asn Cys Leu Ser Lys Arg  
               
               
                         1075                1080                1085  
               
               
                   
               
               
                 Tyr Lys Ser Ser Ser Thr Gln Lys Thr Asn Pro Leu Leu Asp Cys Cys  
               
               
                     1090                1095                1100  
               
               
                   
               
               
                 Leu Leu Val Pro Lys Trp Arg Arg Glu Lys Leu Val Leu Pro Ala Ile  
               
               
                 1105                1110                1115                1120  
               
               
                   
               
               
                 Thr Ser Ser Ser Thr Leu Ser Ser Leu Pro Cys Leu Val Thr Pro Tyr  
               
               
                                 1125                1130                1135  
               
               
                   
               
               
                 Ser Arg Asp Gln Asp Thr Pro Leu Glu Gln Phe Leu Gly Lys Leu Ile  
               
               
                             1140                1145                1150  
               
               
                   
               
               
                 Phe Phe Ser Ala Pro Arg Arg Pro Ile Leu Gly Ser Ser Pro Glu Trp  
               
               
                         1155                1160                1165  
               
               
                   
               
               
                 Cys Pro Leu Arg His Arg Arg Ser Thr Ala Xaa Ile His Ser Ser Asp  
               
               
                     1170                1175                1180  
               
               
                   
               
               
                 Tyr Val Trp Val Gln Phe Tyr Tyr Thr Gly Asn Ser Gln Met Pro Gly  
               
               
                 1185                1190                1195                1200  
               
               
                   
               
               
                 Asn Asn Gly Phe Ser Ile Leu His Gly Arg Cys Ser Leu Asp Phe Leu  
               
               
                                 1205                1210                1215  
               
               
                   
               
               
                 Leu Leu Leu Arg Leu Leu Glu Gly Ala Pro Phe His Ser Tyr Thr Cys  
               
               
                             1220                1225                1230  
               
               
                   
               
               
                 Leu Ile Ile Lys Asn Tyr Ser Lys Tyr Arg Gly Ile Ile Lys Ile Lys  
               
               
                         1235                1240                1245  
               
               
                   
               
               
                 Lys Lys Gly Arg Met Gly Ile Arg Ile Lys Thr Glu Thr Gly His Glu  
               
               
                     1250                1255                1260  
               
               
                   
               
               
                 Glu Arg Phe Glu Arg Gln Thr Thr Val Asp Gly Ser Leu Leu Trp Thr  
               
               
                 1265                1270                1275                1280  
               
               
                   
               
               
                 Trp Ile Val Pro Lys Ala Val Gln Val Phe Met Asn Arg Ser Ile Gly  
               
               
                                 1285                1290                1295  
               
               
                   
               
               
                 Ser Ala Phe Lys Asn Arg Glu Asp Asn Arg Pro Lys Arg Asn Asn Lys  
               
               
                             1300                1305                1310  
               
               
                   
               
               
                 Leu Trp Ala Phe Xaa Ile Asn Arg Thr Val Pro Ser Val Arg Cys Met  
               
               
                         1315                1320                1325  
               
               
                   
               
               
                 Asp Gly Gly Ile Ser Arg Val Asn Leu Arg Lys Ile Val Pro Ala Pro  
               
               
                     1330                1335                1340  
               
               
                   
               
               
                 Leu Pro Arg Pro Thr Arg Ser Val Leu Ser Pro Thr Pro Tyr Thr Phe  
               
               
                 1345                1350                1355                1360  
               
               
                   
               
               
                 Phe Phe Phe Arg Ser Cys Asp Arg Leu Phe Asp Phe Val Tyr Asp Ile  
               
               
                                 1365                1370                1375  
               
               
                   
               
               
                 Gln Phe Leu Phe Trp Ser Gly Ile Leu Phe Phe Leu Arg Leu Leu Tyr  
               
               
                             1380                1385                1390  
               
               
                   
               
               
                 Thr Ile Ser Phe Gly Leu Ser Ala Trp Arg Arg Val Ser Gly Asp Gly  
               
               
                         1395                1400                1405  
               
               
                   
               
               
                 Ser Gln Ile Pro Cys Phe Leu Leu Pro Lys Trp Cys Lys Ile Arg Pro  
               
               
                     1410                1415                1420  
               
               
                   
               
               
                 Ile Gly Phe Phe Ser His Phe Lys Leu Asn Tyr Ala Val Ile Leu Val  
               
               
                 1425                1430                1435                1440  
               
               
                   
               
               
                 Arg Leu Trp Arg Ile Cys Ser Ile Ser Lys Glu Ile Ala Ala Phe Phe  
               
               
                                 1445                1450                1455  
               
               
                   
               
               
                 Leu Val Pro Ile Lys Phe Ala Phe Gly Ser Glu Tyr Pro Arg Met Ser  
               
               
                             1460                1465                1470  
               
               
                   
               
               
                 Tyr Arg Gln Arg Phe Phe Phe Arg Ile Leu Ile Leu Cys Pro Val Phe  
               
               
                         1475                1480                1485  
               
               
                   
               
               
                 Cys Asp Leu Met Glu Lys Ile Leu Phe Leu Leu Val Ile Tyr Ala Leu  
               
               
                     1490                1495                1500  
               
               
                   
               
               
                 Pro Thr Ile Arg Met Arg Val Glu Gly Glu Asn Thr Phe Trp Phe Ser  
               
               
                 1505                1510                1515                1520  
               
               
                   
               
               
                 Ser Leu Asn Ser Ser Lys His Asp Thr Ser Ile Ile Ile Asp Gln Asp  
               
               
                                 1525                1530                1535  
               
               
                   
               
               
                 Phe Phe Leu Cys Thr Asp Ser His Phe Pro Ser Leu Cys Val Met Val  
               
               
                             1540                1545                1550  
               
               
                   
               
               
                 Ile Val Val Thr Asp Gly Cys Leu Thr His Gly Val Ala Pro Gly Ser  
               
               
                         1555                1560                1565  
               
               
                   
               
               
                 Val Asp Leu Gln Val Asp  
               
               
                     1570  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 31  
               
               
                 &lt;211&gt; LENGTH: 1562  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 163, 271, 1170, 1311  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 31  
               
               
                   
               
               
                 Arg Ile Pro Thr Phe Arg Asn Gly Ser Asn Phe Ser Tyr Lys Phe Lys  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Val Arg Lys Ile Phe Thr Lys Ser Phe Glu Ser Ile Asp Asp Ile Arg  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Glu Thr Val Tyr Met Ser Pro Met Asp Ser Leu Gly Phe Ile Arg Lys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ser Ser Lys Glu Cys Ile Arg Ile Leu Ile Leu Asp Ser Phe Thr Arg  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Leu Val Pro Ser Val Thr Ser Arg Val Leu Gln Ile Ser Lys Ala Glu  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ser Gln Ile Glu Met Leu Asn Ser Phe Leu Ser Asn Ala Gln Asn Arg  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Ala Phe Ile Ala Phe Val Phe Lys Ala Lys Thr Phe Phe Ser Asp Ser  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser His Ser Leu Ile Gly Arg Glu Asn Phe Asn Pro Phe Ser Thr Ile  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Asp Gln Ser Ser Lys Ser Met Glu Met Arg Lys Ile Leu Ile Val Phe  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Gln Tyr Met Phe Asp Ser Leu Asn Ile Gly Gly Cys Val Met Lys Pro  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Ser Cys Xaa Ile Ser Leu Gly Tyr Thr Lys Tyr Glu Ser Glu Pro Cys  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Ser Asp Thr Asn Cys Asp Gln Ser Gly Thr Lys Arg Gly Gly Glu Ile  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ser Ala Val Asp Asn Leu Val Lys Ile Arg Lys Tyr Glu Lys Ile Ser  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Phe Leu Glu Met Lys Thr Lys Ser Gln Cys Lys Gln Phe Arg Glu Ser  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Lys Asn Ser His Ile Gln Gly Thr Tyr Gln Phe Lys Val Val Arg Ser  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Lys Pro Thr Ser Thr Cys Glu Ala Phe Phe Glu Glu Ala Pro Asn Phe  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 His Gln Ile Thr Leu Lys Gly Lys Asp Lys Tyr Leu Ser Tyr Xaa Leu  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Leu Gln Trp Phe Ile Leu Leu Gln Ile Phe Asn Glu Lys Glu Gly Gly  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Glu His Ala Ser Asn Lys Gln Asp Leu Leu Lys Thr Leu Leu Arg Leu  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Phe Phe Ser Ile Tyr Cys Phe Ser Lys Val Val Phe Ser Ala Glu Asn  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Gly Val Phe Ile Asp Pro Lys Arg Ile Ile Trp Ala Pro Asn Phe Glu  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Cys Ser Trp Val Pro Glu Val Ala Gly Ala Thr Ala Cys Gln Cys Leu  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Thr Leu Asp Ser Val Leu Ala Val Pro Pro Pro Asp Leu Ser Gly Val  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Gly Arg Cys His Arg Leu Asp Phe Phe Ser Ser Leu Val Gly Phe Gln  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Thr Pro Lys Pro Val Arg Thr Arg Val Gln Leu Thr Arg Asn Arg Ile  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Ile Gly Leu Thr Leu Asn Pro Asn Pro Asn Tyr Met Gln Thr Thr Gln  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Leu Lys Ile Ser Ala Ser Phe Pro Ala Asn Val Glu Ser Ser Ser Gly  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Asp Leu Ser Ala Asp Phe Tyr Thr Phe Gly Phe Leu Leu Ala Asp Ser  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Gly Pro Asp Leu Val Ala Ser Leu Ala Ser Ser Arg Thr Phe Ser Val  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Ile Ser Ala Asn Arg Arg Ser Leu Arg Gln Thr Phe Glu Asn Phe Asp  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Lys Ser Pro Ile Ser Ser Arg Leu Val Pro Thr Ala Ser Leu Thr Lys  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Leu Arg Thr Pro Met Ser Ile Glu Leu Asp Ser Gly Arg Leu Ala Leu  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Tyr Phe Gln Ala Ile Ile Val Asn Pro Thr Tyr Leu Thr Gln Tyr Gly  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Leu Asp Leu Thr His Gln Leu Ile Ser Ser Ser Lys Phe Asp Ile Gln  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Gln Thr Ser Val Leu Asn Asn Pro Ser Gly Tyr Ser Tyr Val Thr Ile  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Tyr Cys Asp Pro Tyr Val Lys Leu Ala Ser His Asp Pro Gly Arg Val  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Thr Tyr Trp Pro Asn Thr Tyr Pro Leu Ser Lys Ser Ser Leu Leu Asn  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Ser Ser Ser Leu Pro Val Ser Phe Phe Ile Thr Phe Glu Arg Ile Gln  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ile Lys Thr Asp Thr Lys His Gly Glu Thr Leu His Ala Ser Leu Trp  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Lys Ala Leu Ile Arg Ala Ser Thr Asp Val Val Ser Phe Ile Thr His  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Phe Phe Leu His Asn His Val Ala Trp Leu Cys Gln Thr Thr Thr Ser  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                 Leu Pro Leu Val Val Pro Asn Arg Glu Arg Glu Thr Asp Arg Pro Pro  
               
               
                             660                 665                 670  
               
               
                   
               
               
                 His Ser Leu Trp Arg Ser Asp Arg Gln Leu Arg Cys Cys Tyr Leu Arg  
               
               
                         675                 680                 685  
               
               
                   
               
               
                 Ser Cys Leu Arg Ser Arg Glu Asp Cys Arg Pro Gly Ala Ala His Ala  
               
               
                     690                 695                 700  
               
               
                   
               
               
                 Leu Ala Ser Thr Gly Lys Thr Pro Thr Arg Glu Ala Gln Met Leu Val  
               
               
                 705                 710                 715                 720  
               
               
                   
               
               
                 Pro Gln Ala Thr Thr Asn Thr Thr Ser Pro Pro Phe Ser Ser Leu Ala  
               
               
                                 725                 730                 735  
               
               
                   
               
               
                 Trp Ala Lys Leu Gln Arg Ser Thr Ser Pro Ala Thr Val Thr Leu Gly  
               
               
                             740                 745                 750  
               
               
                   
               
               
                 Thr Thr Ala Ala Arg Ala Ala Ala Lys Ser Ser Pro Ala Arg Ser Val  
               
               
                         755                 760                 765  
               
               
                   
               
               
                 Ala Ser Arg Cys Ser Pro Ser Glu Val Ala Gly Leu Met Ala Val Pro  
               
               
                     770                 775                 780  
               
               
                   
               
               
                 Pro Lys Thr Pro Arg Thr Arg His Thr Ser Gly Thr Val Ser Trp Val  
               
               
                 785                 790                 795                 800  
               
               
                   
               
               
                 Val Leu Leu Leu Ala Thr Arg Asp Pro Ser Gly Met Arg Phe Trp Met  
               
               
                                 805                 810                 815  
               
               
                   
               
               
                 Ala Thr Ser Thr Ser Pro Glu Gly Ala Gln Asn Thr Met Met Asn Leu  
               
               
                             820                 825                 830  
               
               
                   
               
               
                 Pro Leu Ser Ser Arg Pro Thr Thr Ser Arg Arg Pro Glu Arg Arg Lys  
               
               
                         835                 840                 845  
               
               
                   
               
               
                 Phe Thr Val Leu Val Arg Ser Val Leu Ser Arg Ile Thr Gly Leu Ala  
               
               
                     850                 855                 860  
               
               
                   
               
               
                 Thr His Ser Glu Gln Ile Ser Ser Thr Ser Cys Gly Cys Ser Ser Ser  
               
               
                 865                 870                 875                 880  
               
               
                   
               
               
                 Thr Thr Leu Arg Ala Ile Ser Pro Arg Thr Leu Ser Ile Leu Gln Met  
               
               
                                 885                 890                 895  
               
               
                   
               
               
                 Arg Ser Thr Ile Gly Ser Cys Pro Ser Leu Arg Lys Ser Cys Ser Leu  
               
               
                             900                 905                 910  
               
               
                   
               
               
                 Gly Phe Leu Leu Leu Leu Arg Leu Leu Gln Leu Val Ala Thr Phe His  
               
               
                         915                 920                 925  
               
               
                   
               
               
                 Pro Met Ile Ser Tyr Leu Lys Phe Phe Arg Ser Arg Ile Pro Thr Ser  
               
               
                     930                 935                 940  
               
               
                   
               
               
                 Thr Gln Glu Ser Cys Cys Gly Leu Asp Thr Thr Thr Glu Thr Pro Ala  
               
               
                 945                 950                 955                 960  
               
               
                   
               
               
                 Thr Val Leu Lys Ser Ser Pro Thr Cys Val Gln Arg Val Gly Ser Pro  
               
               
                                 965                 970                 975  
               
               
                   
               
               
                 Thr Ser Tyr Leu Cys Arg Ser Leu Pro Ser Lys Pro Glu Arg Arg Arg  
               
               
                             980                 985                 990  
               
               
                   
               
               
                 Ser Val Val Glu Asn Ser Asp His His Gly Ser Pro Ser Val Ser Val  
               
               
                         995                 1000                1005  
               
               
                   
               
               
                 Arg Cys Tyr Val Met Val Phe Pro Leu Tyr Val Gly Leu Phe Asn Asn  
               
               
                     1010                1015                1020  
               
               
                   
               
               
                 Ile Ile Arg Gly Phe Tyr Val Ser Ile Phe Ser Met Phe Glu Asn Ser  
               
               
                 1025                1030                1035                1040  
               
               
                   
               
               
                 Ile Phe Ala Ala Pro Ser Lys Phe Glu Lys Asp Lys Ile Asn Ile Leu  
               
               
                                 1045                1050                1055  
               
               
                   
               
               
                 Lys Ile Ser Ser Phe Phe Phe Leu Ser Thr Asn Ile Leu Leu Thr Phe  
               
               
                             1060                1065                1070  
               
               
                   
               
               
                 Pro Ile Val Ala Lys Asp Ile Asn Pro Leu Pro His Lys Arg Arg Ile  
               
               
                         1075                1080                1085  
               
               
                   
               
               
                 His Asp Cys Trp Ile Ala Val Tyr Trp Cys Arg Asn Gly Asp Glu Arg  
               
               
                     1090                1095                1100  
               
               
                   
               
               
                 Ser Leu Cys Tyr Leu Gln Leu Gln Val Arg Gln His Cys Leu Pro Cys  
               
               
                 1105                1110                1115                1120  
               
               
                   
               
               
                 His Val Trp Arg His Thr Pro Val Ile Arg Thr His Leu Trp Asn Ser  
               
               
                                 1125                1130                1135  
               
               
                   
               
               
                 Phe Leu Gly Ser Ser Ser Ser Arg Leu Leu Gly Asp Gln Ser Cys Glu  
               
               
                             1140                1145                1150  
               
               
                   
               
               
                 Val Leu Leu Leu Asn Gly Val His Phe Asp Ile Glu Gly Leu Pro Glu  
               
               
                         1155                1160                1165  
               
               
                   
               
               
                 Arg Xaa Ser Thr Val Pro Thr Thr Cys Gly Cys Ser Ser Thr Thr Gln  
               
               
                     1170                1175                1180  
               
               
                   
               
               
                 Ala Thr Arg Arg Cys Pro Val Thr Met Gly Ser Pro Ser Cys Met Glu  
               
               
                 1185                1190                1195                1200  
               
               
                   
               
               
                 Gly Val Pro Trp Thr Ser Cys Cys Ser Ser Gly Cys Trp Lys Glu Leu  
               
               
                                 1205                1210                1215  
               
               
                   
               
               
                 His Ser Thr Ser Asp Leu Thr Arg Val Leu Ser Ser Arg Ile Ile Ala  
               
               
                             1220                1225                1230  
               
               
                   
               
               
                 Ser Thr Glu Gly Leu Leu Lys Lys Lys Arg Glu Glu Trp Glu Leu Glu  
               
               
                         1235                1240                1245  
               
               
                   
               
               
                 Leu Lys Leu Lys Pro Ala Met Lys Asn Val Ser Ser Glu Asp Lys Arg  
               
               
                     1250                1255                1260  
               
               
                   
               
               
                 Gln Tyr Glu Thr Val Val Cys Tyr Gly His Gly Ser Phe Pro Lys Gln  
               
               
                 1265                1270                1275                1280  
               
               
                   
               
               
                 Ser Lys Ser Leu Thr Gly Leu Ser Val Gln Pro Ser Arg Thr Ala Arg  
               
               
                                 1285                1290                1295  
               
               
                   
               
               
                 Ile Thr Gly Pro Arg Glu Thr Thr Asn Cys Gly Glu Leu Leu Xaa Thr  
               
               
                             1300                1305                1310  
               
               
                   
               
               
                 Glu Arg Cys Arg Pro Ser Asp Val Lys Trp Thr Ala Asp Arg Ser Pro  
               
               
                         1315                1320                1325  
               
               
                   
               
               
                 Glu Ile Gly Lys Ser Phe Arg Pro Pro Tyr His Asp Pro Arg Asp Pro  
               
               
                     1330                1335                1340  
               
               
                   
               
               
                 Ser Ser Pro Pro Pro Pro Thr Pro Phe Ser Ser Ser Ala Pro Ala Ile  
               
               
                 1345                1350                1355                1360  
               
               
                   
               
               
                 Gly Tyr Leu Ile Leu Cys Met Ile Ser Asn Phe Phe Ser Gly Val Val  
               
               
                                 1365                1370                1375  
               
               
                   
               
               
                 Ser Tyr Ser Asn Phe Leu Asp Cys Cys Ile Glu Pro Ser Val Leu Val  
               
               
                             1380                1385                1390  
               
               
                   
               
               
                 Ala His Asp Gly Gly Glu Phe Arg Glu Met Gly Val Arg Ser Leu Val  
               
               
                         1395                1400                1405  
               
               
                   
               
               
                 Phe Cys Cys Arg Ser Gly Ala Arg Phe Gly Arg Val Phe Ser Leu Ile  
               
               
                     1410                1415                1420  
               
               
                   
               
               
                 Leu Ser Ser Ile Met Arg Ser Phe Leu Leu Gly Phe Gly Glu Phe Ala  
               
               
                 1425                1430                1435                1440  
               
               
                   
               
               
                 Leu Phe Arg Lys Lys Leu Leu Leu Ser Ser Phe Asp Ser Leu Asn Leu  
               
               
                                 1445                1450                1455  
               
               
                   
               
               
                 Leu Ser Val Leu Asn Ile Arg Glu Cys Arg Ile Val Asn Asp Asp Ser  
               
               
                             1460                1465                1470  
               
               
                   
               
               
                 Phe Leu Glu Phe Tyr Phe Val Leu Phe Ser Val Ile Trp Arg Lys Tyr  
               
               
                         1475                1480                1485  
               
               
                   
               
               
                 Cys Ser Phe Ser Met Leu Ser Arg Pro Leu Gly Gly Leu Lys Val Lys  
               
               
                     1490                1495                1500  
               
               
                   
               
               
                 Ile Leu Ser Gly Asn Phe Pro Leu Ile Leu Pro Asn Thr Thr Gln Val  
               
               
                 1505                1510                1515                1520  
               
               
                   
               
               
                 Leu Thr Lys Ile Asp Ser Ser Tyr Ala Pro Ile Leu Thr Ser Leu Pro  
               
               
                                 1525                1530                1535  
               
               
                   
               
               
                 Ser Val Leu Trp Leu Ser Leu Leu Leu Met Val Ala Leu Met Gly Arg  
               
               
                             1540                1545                1550  
               
               
                   
               
               
                 Leu Gly Asp Pro Leu Thr Cys Arg Ser Thr  
               
               
                         1555                1560  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 32  
               
               
                 &lt;211&gt; LENGTH: 2392  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 1721  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 32  
               
               
                   
               
               
                 tcactggtac ggggcccccc tcgaggtcga cggtatcgat aagctttgat ctcttctctc     60  
               
               
                   
               
               
                 aatctctctc tctctctctc tctctctctc tctctgtatg tctttaaata tggttgtaat    120  
               
               
                   
               
               
                 gctgaattgc tatgtttatc ttggccaaac tgtgtccatc tttgagcaga taaatctggc    180  
               
               
                   
               
               
                 gataatgttc tttttactga aagcactgca ggatgagggc ctgaaatcac atcggacgcc    240  
               
               
                   
               
               
                 cactgggtca tgatgatatg gactcctcca cagcgagcag ccatgggatg tgagatccac    300  
               
               
                   
               
               
                 atagcagcgt agataaggga agcccgcaac actaggctgt tgttgttcca gtaaagatcg    360  
               
               
                   
               
               
                 aaaggtcagg cgacagtgac gatcgacttt ttcgagcatg atgacaacga cgacctgctc    420  
               
               
                   
               
               
                 ctgcaatatc cgtcccctac cgtagagtgg gaataaatgg gtttgtagtt gcactatttc    480  
               
               
                   
               
               
                 tcgcaggaat taattgaaag ccctgcaaat tgctgtttct ctttccttat attaaacctt    540  
               
               
                   
               
               
                 cctcctgtta cattaaaatt gcatgttaag acatttctgt atggatccga acatgagatc    600  
               
               
                   
               
               
                 tatcattgaa gtaatgggta ggatttacat tatcatcatc atcatcatct ccatgggttt    660  
               
               
                   
               
               
                 ggatctaatt agaccgaaaa cctcatttaa aatccaaccc caatattggc ttgacttgct    720  
               
               
                   
               
               
                 ccatctccaa gaaaaataca acaagaacaa caaaaattta ggatgcacat tgaattgatt    780  
               
               
                   
               
               
                 tggtcactat gagagaatca tggattaaaa atattaaaat aaaaaataaa tcataatcat    840  
               
               
                   
               
               
                 ctactcactc taacgattca cattctatcc accaaatttg acatcggctt ctaattaatt    900  
               
               
                   
               
               
                 tcatatatta ggttctaaaa aatctctccc tttgacagat gaataaatat ttcttttaat    960  
               
               
                   
               
               
                 tcgttaggga aggatctaat ataatatata tatatatata tatttattta ttagattcta   1020  
               
               
                   
               
               
                 accatttctc tcaccagaat atgaatcgac ggccatatct gcaaaaaccc accaattgtt   1080  
               
               
                   
               
               
                 cacagtaaac gctcattgaa ttaaggtcga aattactttt aaatttctag agatttccaa   1140  
               
               
                   
               
               
                 taaaatatac tcgtatcttt tacagtgatg atgctccgga tgataagatg gaaggatgcg   1200  
               
               
                   
               
               
                 tgtgtcagcc gcctgcgatc tctgtggcgg ggacgagacg aagacaagga cgtgagcgga   1260  
               
               
                   
               
               
                 cgataccaag tcttctcctc ccccaccacg cacgtctcag attcccgata cggcctatcc   1320  
               
               
                   
               
               
                 cggtggcgtg tggactgcac agacgaacga gtaaatgccc atcccccctc tttcattctt   1380  
               
               
                   
               
               
                 tctctttgcg tgtgtgagag gagcgcctat aaataagcac gaaacaagcc ccttttctct   1440  
               
               
                   
               
               
                 ccaagaacac accacaccat tcacacacta catcctctgc ttcttcgagc cttttcgcct   1500  
               
               
                   
               
               
                 tccttcctcg tctaaccatg tcgacctgcg gcaactgcga ctgcgttgac aagagccagt   1560  
               
               
                   
               
               
                 gcgtgtaagt catcctccat ccctccacct cttcttcttc ttcttcttct tcttcttcta   1620  
               
               
                   
               
               
                 acctcgcccc gtttgtgttt gatgagtcga ctcttcccac atcgctcgtc aaaactcaga   1680  
               
               
                   
               
               
                 gctttattag ggaacatcag caatactata tgtatatgta naaggtcaac gttggctgaa   1740  
               
               
                   
               
               
                 gaacttggtt ttgcctttgc aggaagaaag gaaacagcta cggtatcgat attgttgaga   1800  
               
               
                   
               
               
                 ccgagaagag gtactgatta gcttcttctc cctcctcctc gtcgaggatg atcaaactaa   1860  
               
               
                   
               
               
                 ttaggattac accttattac cttacctaat gctttttccg tattcgtttc gtctcttcag   1920  
               
               
                   
               
               
                 ctacgtcgac gaggtgatcg ttgccgcaga agctgccgag catgacggca agtgcaagtg   1980  
               
               
                   
               
               
                 cggcgccgcc tgcgcctgca ccgactgcaa gtgtggcaac tgagaagcac ttgtgtcact   2040  
               
               
                   
               
               
                 accactaaat aaaagtttgc aatgcataaa aaacaaaaga acaaaaaaaa aaaaggaaga   2100  
               
               
                   
               
               
                 agaagaaggt gtggctatgt actctaataa ttcgggcagg ctgataggtt gtaagatggg   2160  
               
               
                   
               
               
                 ataacgcagt atcatctgtg ttatctctgt cctgtgttac aactctccta tctatcctag   2220  
               
               
                   
               
               
                 tcaatgaaat attattagta ttaatctggt tgtgtcattc atatatgctg ctgctgctgc   2280  
               
               
                   
               
               
                 tgcttcctct ttcaccaatc aacccaaagg atcgattgca ctgtaaggcc caacttcctc   2340  
               
               
                   
               
               
                 accgatatgc tcgctcagtt acgatgaatg aacagcaacc aaacgagtct gc           2392  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 33  
               
               
                 &lt;211&gt; LENGTH: 2392  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 1721  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 33  
               
               
                   
               
               
                 agtgaccatg ccccgggggg agctccagct gccatagcta ttcgaaacta gagaagagag     60  
               
               
                   
               
               
                 ttagagagag agagagagag agagagagag agagacatac agaaatttat accaacatta    120  
               
               
                   
               
               
                 cgacttaacg atacaaatag aaccggtttg acacaggtag aaactcgtct atttagaccg    180  
               
               
                   
               
               
                 ctattacaag aaaaatgact ttcgtgacgt cctactcccg gactttagtg tagcctgcgg    240  
               
               
                   
               
               
                 gtgacccagt actactatac ctgaggaggt gtcgctcgtc ggtaccctac actctaggtg    300  
               
               
                   
               
               
                 tatcgtcgca tctattccct tcgggcgttg tgatccgaca acaacaaggt catttctagc    360  
               
               
                   
               
               
                 tttccagtcc gctgtcactg ctagctgaaa aagctcgtac tactgttgct gctggacgag    420  
               
               
                   
               
               
                 gacgttatag gcaggggatg gcatctcacc cttatttacc caaacatcaa cgtgataaag    480  
               
               
                   
               
               
                 agcgtcctta attaactttc gggacgttta acgacaaaga gaaaggaata taatttggaa    540  
               
               
                   
               
               
                 ggaggacaat gtaattttaa cgtacaattc tgtaaagaca tacctaggct tgtactctag    600  
               
               
                   
               
               
                 atagtaactt cattacccat cctaaatgta atagtagtag tagtagtaga ggtacccaaa    660  
               
               
                   
               
               
                 cctagattaa tctggctttt ggagtaaatt ttaggttggg gttataaccg aactgaacga    720  
               
               
                   
               
               
                 ggtagaggtt ctttttatgt tgttcttgtt gtttttaaat cctacgtgta acttaactaa    780  
               
               
                   
               
               
                 accagtgata ctctcttagt acctaatttt tataatttta ttttttattt agtattagta    840  
               
               
                   
               
               
                 gatgagtgag attgctaagt gtaagatagg tggtttaaac tgtagccgaa gattaattaa    900  
               
               
                   
               
               
                 agtatataat ccaagatttt ttagagaggg aaactgtcta cttatttata aagaaaatta    960  
               
               
                   
               
               
                 agcaatccct tcctagatta tattatatat atatatatat ataaataaat aatctaagat   1020  
               
               
                   
               
               
                 tggtaaagag agtggtctta tacttagctg ccggtataga cgtttttggg tggttaacag   1080  
               
               
                   
               
               
                 gtgtcatttg cgagtaactt aattccagct ttaatgaaaa tttaaagatc tctaaaggtt   1140  
               
               
                   
               
               
                 attttatatg agcatagaaa atgtcactac tacgaggcct actattctac cttcctacgc   1200  
               
               
                   
               
               
                 acacagtcgg cggacgctag agacaccgcc cctgctctgc ttctgttcct gcactcgcct   1260  
               
               
                   
               
               
                 gctatggttc agaagaggag ggggtggtgc gtgcagagtc taagggctat gccggatagg   1320  
               
               
                   
               
               
                 gccaccgcac acctgacgtg tctgcttgct catttacggg taggggggag aaagtaagaa   1380  
               
               
                   
               
               
                 agagaaacgc acacactctc ctcgcggata tttattcgtg ctttgttcgg ggaaaagaga   1440  
               
               
                   
               
               
                 ggttcttgtg tggtgtggta agtgtgtgat gtaggagacg aagaagctcg gaaaagcgga   1500  
               
               
                   
               
               
                 aggaaggagc agattggtac agctggacgc cgttgacgct gacgcaactg ttctcggtca   1560  
               
               
                   
               
               
                 cgcacattca gtaggaggta gggaggtgga gaagaagaag aagaagaaga agaagaagat   1620  
               
               
                   
               
               
                 tggagcgggg caaacacaaa ctactcagct gagaagggtg tagcgagcag ttttgagtct   1680  
               
               
                   
               
               
                 cgaaataatc ccttgtagtc gttatgatat acatatacat nttccagttg caaccgactt   1740  
               
               
                   
               
               
                 cttgaaccaa aacggaaacg tccttctttc ctttgtcgat gccatagcta taacaactct   1800  
               
               
                   
               
               
                 ggctcttctc catgactaat cgaagaagag ggaggaggag cagctcctac tagtttgatt   1860  
               
               
                   
               
               
                 aatcctaatg tggaataatg gaatggatta cgaaaaaggc ataagcaaag cagagaagtc   1920  
               
               
                   
               
               
                 gatgcagctg ctccactagc aacggcgtct tcgacggctc gtactgccgt tcacgttcac   1980  
               
               
                   
               
               
                 gccgcggcgg acgcggacgt ggctgacgtt cacaccgttg actcttcgtg aacacagtga   2040  
               
               
                   
               
               
                 tggtgattta ttttcaaacg ttacgtattt tttgttttct tgtttttttt ttttccttct   2100  
               
               
                   
               
               
                 tcttcttcca caccgataca tgagattatt aagcccgtcc gactatccaa cattctaccc   2160  
               
               
                   
               
               
                 tattgcgtca tagtagacac aatagagaca ggacacaatg ttgagaggat agataggatc   2220  
               
               
                   
               
               
                 agttacttta taataatcat aattagacca acacagtaag tatatacgac gacgacgacg   2280  
               
               
                   
               
               
                 acgaaggaga aagtggttag ttgggtttcc tagctaacgt gacattccgg gttgaaggag   2340  
               
               
                   
               
               
                 tggctatacg agcgagtcaa tgctacttac ttgtcgttgg tttgctcaga cg           2392  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 34  
               
               
                 &lt;211&gt; LENGTH: 758  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 548  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 34  
               
               
                   
               
               
                 Ser Leu Val Arg Gly Pro Pro Arg Gly Arg Arg Tyr Arg Ala Leu Ile  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ser Ser Leu Asn Leu Ser Leu Ser Leu Ser Leu Ser Leu Ser Leu Tyr  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Val Phe Lys Tyr Gly Cys Asn Ala Glu Leu Leu Cys Leu Ser Trp Pro  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Asn Cys Val His Leu Ala Asp Lys Ser Gly Asp Asn Val Leu Phe Thr  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Glu Ser Thr Ala Gly Gly Pro Glu Ile Thr Ser Asp Ala His Trp Val  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Met Met Ile Trp Thr Pro Pro Gln Arg Ala Ala Met Gly Cys Glu Ile  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 His Ile Ala Ala Ile Arg Glu Ala Arg Asn Thr Arg Leu Leu Leu Phe  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Gln Arg Ser Lys Gly Gln Ala Thr Val Thr Ile Asp Phe Phe Glu His  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Asp Asp Asn Asp Asp Leu Leu Leu Gln Tyr Pro Ser Pro Thr Val Glu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Trp Glu Met Gly Leu Leu His Tyr Phe Ser Gln Glu Leu Ile Glu Ser  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Pro Ala Asn Cys Cys Phe Ser Phe Leu Ile Leu Asn Leu Pro Pro Val  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Thr Leu Lys Leu His Val Lys Thr Phe Leu Tyr Gly Ser Glu His Glu  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ile Tyr His Ser Asn Gly Asp Leu His Tyr His His His His His Leu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 His Gly Phe Gly Ser Asn Thr Glu Asn Leu Ile Asn Pro Thr Pro Ile  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Leu Ala Leu Ala Pro Ser Pro Arg Lys Ile Gln Gln Glu Gln Gln Lys  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Phe Arg Met His Ile Glu Leu Ile Trp Ser Leu Glu Asn His Gly Leu  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Lys Ile Leu Lys Ile Asn His Asn His Leu Leu Thr Leu Thr Ile His  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Ile Leu Ser Thr Lys Phe Asp Ile Gly Phe Leu Ile Ser Tyr Ile Arg  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Phe Lys Ile Ser Pro Phe Asp Arg Ile Asn Ile Ser Phe Asn Ser Leu  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Gly Lys Asp Leu Ile Tyr Ile Tyr Ile Tyr Ile Phe Ile Tyr Ile Leu  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Thr Ile Ser Leu Thr Arg Ile Ile Asp Gly His Ile Cys Lys Asn Pro  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Pro Ile Val His Ser Lys Arg Ser Leu Asn Gly Arg Asn Tyr Phe Ile  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Ser Arg Asp Phe Gln Asn Ile Leu Val Ser Phe Thr Val Met Met Leu  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Arg Met Ile Arg Trp Lys Asp Ala Cys Val Ser Arg Leu Arg Ser Leu  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Trp Arg Gly Arg Asp Glu Asp Lys Asp Val Ser Gly Arg Tyr Gln Val  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Phe Ser Ser Pro Thr Thr His Val Ser Asp Ser Arg Tyr Gly Leu Ser  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Arg Trp Arg Val Asp Cys Thr Asp Glu Arg Val Asn Ala His Pro Pro  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Ser Phe Ile Leu Ser Leu Cys Val Cys Glu Arg Ser Ala Tyr Lys Ala  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Arg Asn Lys Pro Leu Phe Ser Pro Arg Thr His His Thr Ile His Thr  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Leu His Pro Leu Leu Leu Arg Ala Phe Ser Pro Ser Phe Leu Val Pro  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Cys Arg Pro Ala Ala Thr Ala Thr Ala Leu Thr Arg Ala Ser Ala Cys  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Lys Ser Ser Ser Ile Pro Pro Pro Leu Leu Leu Leu Leu Leu Leu Leu  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Leu Leu Thr Ser Pro Arg Leu Cys Leu Met Ser Arg Leu Phe Pro His  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Arg Ser Ser Lys Leu Arg Ala Leu Leu Gly Asn Ile Ser Asn Thr Ile  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Cys Ile Cys Xaa Arg Ser Thr Leu Ala Glu Glu Leu Gly Phe Ala Phe  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ala Gly Arg Lys Glu Thr Ala Thr Val Ser Ile Leu Leu Arg Pro Arg  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Arg Gly Thr Asp Leu Leu Leu Pro Pro Pro Arg Arg Gly Ser Asn Leu  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Gly Leu His Leu Ile Thr Leu Pro Asn Ala Phe Ser Val Phe Val Ser  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ser Leu Gln Leu Arg Arg Arg Gly Asp Arg Cys Arg Arg Ser Cys Arg  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Ala Arg Gln Val Gln Val Arg Arg Arg Leu Arg Leu His Arg Leu Gln  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Val Trp Gln Leu Arg Ser Thr Cys Val Thr Thr Thr Lys Lys Phe Ala  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                 Met His Lys Lys Gln Lys Asn Lys Lys Lys Lys Gly Arg Arg Arg Arg  
               
               
                             660                 665                 670  
               
               
                   
               
               
                 Cys Tyr Val Leu Phe Gly Gln Ala Asp Arg Leu Asp Gly Ile Thr Gln  
               
               
                         675                 680                 685  
               
               
                   
               
               
                 Tyr His Leu Cys Tyr Leu Cys Pro Val Leu Gln Leu Ser Tyr Leu Ser  
               
               
                     690                 695                 700  
               
               
                   
               
               
                 Ser Met Lys Tyr Tyr Tyr Ser Gly Cys Val Ile His Ile Cys Cys Cys  
               
               
                 705                 710                 715                 720  
               
               
                   
               
               
                 Cys Cys Cys Phe Leu Phe His Gln Ser Thr Gln Arg Ile Asp Cys Thr  
               
               
                                 725                 730                 735  
               
               
                   
               
               
                 Val Arg Pro Asn Phe Leu Thr Asp Met Leu Ala Gln Leu Arg Met Asn  
               
               
                             740                 745                 750  
               
               
                   
               
               
                 Ser Asn Gln Thr Ser Leu  
               
               
                         755  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 35  
               
               
                 &lt;211&gt; LENGTH: 758  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 541  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 35  
               
               
                   
               
               
                 His Trp Tyr Gly Ala Pro Leu Glu Val Asp Gly Ile Asp Lys Leu Ser  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Leu Ser Ile Ser Leu Ser Leu Ser Leu Ser Leu Ser Leu Cys Met  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Ser Leu Asn Met Val Val Met Leu Asn Cys Tyr Val Tyr Leu Gly Gln  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Thr Val Ser Ile Phe Glu Gln Ile Asn Leu Ala Ile Met Phe Phe Leu  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Leu Lys Ala Leu Gln Asp Glu Gly Leu Lys Ser His Arg Thr Pro Thr  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Gly Ser Tyr Gly Leu Leu His Ser Glu Gln Pro Trp Asp Val Arg Ser  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Thr Gln Arg Arg Gly Lys Pro Ala Thr Leu Gly Cys Cys Cys Ser Ser  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Lys Asp Arg Lys Val Arg Arg Gln Arg Ser Thr Phe Ser Ser Met Met  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Thr Thr Thr Thr Cys Ser Cys Asn Ile Arg Pro Leu Pro Ser Gly Asn  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Lys Trp Val Cys Ser Cys Thr Ile Ser Arg Arg Asn Leu Lys Ala Leu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Gln Ile Ala Val Ser Leu Ser Leu Tyr Thr Phe Leu Leu Leu His Asn  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Cys Met Leu Arg His Phe Cys Met Asp Pro Asn Met Arg Ser Ile Ile  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Glu Val Met Gly Arg Ile Tyr Ile Ile Ile Ile Ile Ile Ile Ser Met  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Leu Asp Leu Ile Arg Pro Lys Thr Ser Phe Lys Ile Gln Pro Gln  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Tyr Trp Leu Asp Leu Leu His Leu Gln Glu Lys Tyr Asn Lys Asn Asn  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Lys Asn Leu Gly Cys Thr Leu Asn Phe Gly His Tyr Glu Arg Ile Met  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Asp Lys Tyr Asn Lys Lys Ile Ile Ile Ile Tyr Ser Leu Arg Phe Thr  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Phe Tyr Pro Pro Asn Leu Thr Ser Ala Ser Asn Phe His Ile Leu Gly  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Ser Lys Lys Ser Leu Pro Leu Thr Asp Glu Ile Phe Leu Leu Ile Arg  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Gly Arg Ile Tyr Asn Ile Tyr Ile Tyr Ile Tyr Leu Phe Ile Arg Phe  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Pro Phe Leu Ser Pro Glu Tyr Glu Ser Thr Ala Ile Ser Ala Lys Thr  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 His Gln Leu Phe Thr Val Asn Ala His Ile Lys Val Glu Ile Thr Phe  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Lys Phe Leu Glu Ile Ser Asn Lys Ile Tyr Ser Tyr Leu Leu Gln Cys  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ser Gly Asp Gly Arg Met Arg Val Ser Ala Ala Cys Asp Leu Cys Gly  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Gly Asp Glu Thr Lys Thr Arg Thr Ala Asp Asp Thr Lys Ser Ser Pro  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Pro Pro Pro Arg Thr Ser Gln Ile Pro Asp Thr Ala Tyr Pro Gly Gly  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Val Trp Thr Ala Gln Thr Asn Glu Met Pro Ile Pro Pro Leu Ser Phe  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Phe Leu Phe Ala Cys Val Arg Gly Ala Pro Ile Asn Lys His Glu Thr  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Ser Pro Phe Ser Leu Gln Glu His Thr Thr Pro Phe Thr His Tyr Ile  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Leu Cys Phe Phe Glu Pro Phe Arg Leu Pro Ser Ser Ser Asn His Val  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Asp Leu Arg Gln Leu Arg Leu Arg Gln Glu Pro Val Arg Val Ser His  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Pro Pro Ser Leu His Leu Phe Phe Phe Phe Phe Phe Phe Phe Pro Arg  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Pro Val Cys Val Val Asp Ser Ser His Ile Ala Arg Gln Asn Ser Glu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Leu Tyr Gly Thr Ser Ala Ile Leu Tyr Val Tyr Val Xaa Gly Gln Arg  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Trp Leu Lys Asn Leu Val Leu Pro Leu Gln Glu Glu Arg Lys Gln Leu  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Arg Tyr Arg Tyr Cys Asp Arg Glu Glu Val Leu Ile Ser Phe Phe Ser  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Leu Leu Leu Val Glu Asp Asp Gln Thr Asn Asp Tyr Thr Leu Leu Pro  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Tyr Leu Met Leu Phe Pro Val Ser Phe Arg Leu Phe Ser Tyr Val Asp  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Glu Val Ile Val Ala Ala Glu Ala Ala Glu His Asp Gly Lys Cys Lys  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Cys Gly Ala Ala Cys Ala Cys Thr Asp Cys Lys Cys Gly Asn Glu Ala  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Leu Val Ser Leu Pro Leu Asn Asn Lys Ser Leu Gln Cys Ile Lys Asn  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                 Lys Arg Thr Lys Lys Lys Lys Glu Glu Glu Glu Gly Val Ala Met Tyr  
               
               
                             660                 665                 670  
               
               
                   
               
               
                 Ser Asn Asn Ser Gly Arg Leu Ile Gly Cys Lys Met Gly Arg Ser Ile  
               
               
                         675                 680                 685  
               
               
                   
               
               
                 Ile Cys Val Ile Ser Val Leu Cys Tyr Asn Ser Pro Ile Tyr Pro Ser  
               
               
                     690                 695                 700  
               
               
                   
               
               
                 Gln Asn Ile Ile Ser Ile Asn Leu Val Val Ser Phe Ile Tyr Ala Ala  
               
               
                 705                 710                 715                 720  
               
               
                   
               
               
                 Ala Ala Ala Ala Ser Ser Phe Thr Asn Gln Pro Lys Gly Ser Ile Ala  
               
               
                                 725                 730                 735  
               
               
                   
               
               
                 Leu Gly Pro Thr Ser Ser Pro Ile Cys Ser Leu Ser Tyr Asp Glu Thr  
               
               
                             740                 745                 750  
               
               
                   
               
               
                 Ala Thr Lys Arg Val Cys  
               
               
                         755  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 36  
               
               
                 &lt;211&gt; LENGTH: 762  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 546  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 36  
               
               
                   
               
               
                 Leu Thr Gly Thr Gly Pro Pro Ser Arg Ser Thr Val Ser Ile Ser Phe  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Asp Leu Phe Ser Gln Ser Leu Ser Leu Ser Leu Ser Leu Ser Leu Ser  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Val Cys Leu Ile Trp Leu Cys Ile Ala Met Phe Ile Leu Ala Lys Leu  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Cys Pro Ser Leu Ser Arg Ile Trp Arg Cys Ser Phe Tyr Lys His Cys  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Arg Met Arg Ala Asn His Ile Gly Arg Pro Leu Gly His Asp Asp Met  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Asp Ser Ser Thr Ala Ser Ser His Gly Met Asp Pro His Ser Ser Val  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Lys Gly Ser Pro Gln His Ala Val Val Val Pro Val Lys Ile Glu  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Arg Ser Gly Asp Ser Asp Asp Arg Leu Phe Arg Ala Gln Arg Arg Pro  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Ala Pro Ala Ile Ser Val Pro Tyr Arg Arg Val Gly Ile Asn Gly Phe  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Val Val Ala Leu Phe Leu Ala Gly Ile Asn Lys Pro Cys Lys Leu Leu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Phe Leu Phe Pro Tyr Ile Lys Pro Ser Ser Cys Tyr Ile Lys Ile Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Cys Asp Ile Ser Val Trp Ile Arg Thr Asp Leu Ser Leu Lys Trp Val  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Gly Phe Thr Leu Ser Ser Ser Ser Ser Ser Pro Trp Val Trp Ile Leu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Asp Arg Lys Pro His Leu Lys Ser Asn Pro Asn Ile Gly Leu Thr Cys  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ser Ile Ser Lys Lys Asn Thr Thr Arg Thr Thr Lys Ile Asp Ala His  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Ile Asp Leu Val Thr Met Arg Glu Ser Trp Ile Lys Asn Ile Lys Ile  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Lys Asn Lys Ser Ser Ser Thr His Ser Asn Asp Ser His Ser Ile His  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gln Ile His Arg Leu Leu Ile Asn Phe Ile Tyr Val Leu Lys Asn Leu  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Ser Leu Gln Met Asn Lys Tyr Phe Phe Phe Val Arg Glu Gly Ser Asn  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Ile Ile Tyr Ile Tyr Ile Tyr Ile Tyr Leu Leu Asp Ser Asn His Phe  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Ser His Gln Asn Met Asn Arg Arg Pro Tyr Leu Gln Lys Pro Thr Asn  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Cys Ser Gln Thr Leu Ile Glu Leu Arg Ser Lys Leu Leu Leu Asn Phe  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Arg Phe Pro Ile Lys Tyr Thr Arg Ile Phe Tyr Ser Asp Asp Ala Pro  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Asp Asp Lys Met Glu Gly Cys Val Cys Gln Pro Pro Ala Ile Ser Val  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Ala Gly Thr Arg Arg Arg Gln Gly Arg Glu Arg Thr Ile Pro Ser Leu  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Leu Leu Pro His His Ala Arg Leu Arg Phe Pro Ile Arg Pro Ile Pro  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Val Ala Cys Gly Leu His Arg Arg Thr Ser Lys Cys Pro Ser Pro Leu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Phe His Ser Phe Ser Leu Arg Val Glu Glu Arg Leu Ile Ser Thr Lys  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Gln Ala Pro Phe Leu Ser Lys Asn Thr Pro His His Ser His Thr Thr  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Ser Ser Ala Ser Ser Ser Leu Phe Ala Phe Leu Pro Arg Leu Thr Met  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Ser Thr Cys Gly Asn Cys Asp Cys Val Asp Lys Ser Gln Cys Val Val  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Ile Leu His Pro Ser Thr Ser Ser Ser Ser Ser Ser Ser Ser Ser Ser  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Asn Leu Ala Pro Phe Val Phe Asp Glu Ser Thr Leu Pro Thr Ser Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Val Lys Thr Gln Ser Phe Ile Arg Glu His Gln Gln Tyr Tyr Met Tyr  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Met Xaa Lys Val Asn Val Gly Arg Thr Trp Phe Cys Leu Cys Arg Lys  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Lys Gly Asn Ser Tyr Gly Ile Asp Ile Val Glu Thr Glu Lys Arg Tyr  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Leu Ala Ser Ser Pro Ser Ser Ser Ser Arg Met Ile Lys Leu Ile Arg  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Ile Thr Pro Tyr Tyr Leu Thr Cys Phe Phe Arg Ile Arg Phe Val Ser  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ser Ala Thr Ser Thr Arg Ser Leu Pro Gln Lys Leu Pro Ser Met Thr  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Ala Ser Ala Ser Ala Ala Pro Pro Ala Pro Ala Pro Thr Ala Ser Val  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Ala Thr Glu Lys His Leu Cys His Tyr His Ile Lys Val Cys Asn Ala  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                 Lys Thr Lys Glu Gln Lys Lys Lys Arg Lys Lys Lys Lys Val Trp Leu  
               
               
                             660                 665                 670  
               
               
                   
               
               
                 Cys Thr Leu Ile Ile Arg Ala Gly Val Val Arg Trp Asp Asn Ala Val  
               
               
                         675                 680                 685  
               
               
                   
               
               
                 Ser Ser Val Leu Ser Leu Ser Cys Val Thr Thr Leu Leu Ser Ile Leu  
               
               
                     690                 695                 700  
               
               
                   
               
               
                 Val Asn Glu Ile Leu Leu Val Leu Ile Trp Leu Cys His Ser Tyr Met  
               
               
                 705                 710                 715                 720  
               
               
                   
               
               
                 Leu Leu Leu Leu Leu Leu Pro Leu Ser Pro Ile Asn Pro Lys Asp Arg  
               
               
                                 725                 730                 735  
               
               
                   
               
               
                 Leu His Cys Lys Ala Gln Leu Pro His Arg Tyr Ala Arg Ser Val Thr  
               
               
                             740                 745                 750  
               
               
                   
               
               
                 Met Asn Glu Gln Gln Pro Asn Glu Ser Ala  
               
               
                         755                 760  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 37  
               
               
                 &lt;211&gt; LENGTH: 1880  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 1721, 1782, 1788, 1799  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 37  
               
               
                   
               
               
                 tcactggtac ggggcccccc tcgaggtcga cggtatcgat aagctttgat ctcttctctc     60  
               
               
                   
               
               
                 aatctctctc tctctctctc tctctctctc tctctgtatg tctttaaata tggttgtaat    120  
               
               
                   
               
               
                 gctgaattgc tatgtttatc ttggccaaac tgtgtccatc tttgagcaga taaatctggc    180  
               
               
                   
               
               
                 gataatgttc tttttactga aagcactgca ggatgagggc ctgaaatcac atcggacgcc    240  
               
               
                   
               
               
                 cactgggtca tgatgatatg gactcctcca cagcgagcag ccatgggatg tgagatccac    300  
               
               
                   
               
               
                 atagcagcgt agataaggga agcccgcaac actaggctgt tgttgttcca gtaaagatcg    360  
               
               
                   
               
               
                 aaaggtcagg cgacagtgac gatcgacttt ttcgagcatg atgacaacga cgacctgctc    420  
               
               
                   
               
               
                 ctgcaatatc cgtcccctac cgtagagtgg gaataaatgg gtttgtagtt gcactatttc    480  
               
               
                   
               
               
                 tcgcaggaat taattgaaag ccctgcaaat tgctgtttct ctttccttat attaaacctt    540  
               
               
                   
               
               
                 cctcctgtta cattaaaatt gcatgttaag acatttctgt atggatccga acatgagatc    600  
               
               
                   
               
               
                 tatcattgaa gtaatgggta ggatttacat tatcatcatc atcatcatct ccatgggttt    660  
               
               
                   
               
               
                 ggatctaatt agaccgaaaa cctcatttaa aatccaaccc caatattggc ttgacttgct    720  
               
               
                   
               
               
                 ccatctccaa gaaaaataca acaagaacaa caaaaattta ggatgcacat tgaattgatt    780  
               
               
                   
               
               
                 tggtcactat gagagaatca tggattaaaa atattaaaat aaaaaataaa tcataatcat    840  
               
               
                   
               
               
                 ctactcactc taacgattca cattctatcc accaaatttg acatcggctt ctaattaatt    900  
               
               
                   
               
               
                 tcatatatta ggttctaaaa aatctctccc tttgacagat gaataaatat ttcttttaat    960  
               
               
                   
               
               
                 tcgttaggga aggatctaat ataatatata tatatatata tatttattta ttagattcta   1020  
               
               
                   
               
               
                 accatttctc tcaccagaat atgaatcgac ggccatatct gcaaaaaccc accaattgtt   1080  
               
               
                   
               
               
                 cacagtaaac gctcattgaa ttaaggtcga aattactttt aaatttctag agatttccaa   1140  
               
               
                   
               
               
                 taaaatatac tcgtatcttt tacagtgatg atgctccgga tgataagatg gaaggatgcg   1200  
               
               
                   
               
               
                 tgtgtcagcc gcctgcgatc tctgtggcgg ggacgagacg aagacaagga cgtgagcgga   1260  
               
               
                   
               
               
                 cgataccaag tcttctcctc ccccaccacg cacgtctcag attcccgata cggcctatcc   1320  
               
               
                   
               
               
                 cggtggcgtg tggactgcac agacgaacga gtaaatgccc atcccccctc tttcattctt   1380  
               
               
                   
               
               
                 tctctttgcg tgtgtgagag gagcgcctat aaataagcac gaaacaagcc ccttttctct   1440  
               
               
                   
               
               
                 ccaagaacac accacaccat tcacacacta catcctctgc ttcttcgagc cttttcgcct   1500  
               
               
                   
               
               
                 tccttcctcg tctaaccatg tcgacctgcg gcaactgcga ctgcgttgac aagagccagt   1560  
               
               
                   
               
               
                 gcgtgtaagt catcctccat ccctccacct cttcttcttc ttcttcttct tcttcttcta   1620  
               
               
                   
               
               
                 acctcgcccc gtttgtgttt gatgagtcga ctcttcccac atcgctcgtc aaaactcaga   1680  
               
               
                   
               
               
                 gctttattag ggaacatcag caatactata tgtatatgta naaggtcaac gttggctgaa   1740  
               
               
                   
               
               
                 gaacttggtt ttgcctttgc aggaagaaag gaaacagcta cngtatcnat attgttgana   1800  
               
               
                   
               
               
                 ccgagaagag gtactgatta gcttcttctc cctcctcctc gtcgaggatg atcaaactaa   1860  
               
               
                   
               
               
                 ttaggattac accttattac                                               1880  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 38  
               
               
                 &lt;211&gt; LENGTH: 1878  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 1720, 1768, 1781, 1787, 1798, 1807, 1820, 1845, 1869  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 38  
               
               
                   
               
               
                 agtgaccatg ccccgggggg agctccagct gccatagcta ttcgaaacta gagaagagag     60  
               
               
                   
               
               
                 ttagagagag agagagagag agagagagag agagacatac tgaaatttat accaacatta    120  
               
               
                   
               
               
                 cgacttaacg atacaaatag aaccggtttg acacaggtag aaactcgtct atttagaccg    180  
               
               
                   
               
               
                 ctattacaag aaaaatgact ttcgtgacgt cctactcccg gactttagtg tagcctgcgg    240  
               
               
                   
               
               
                 gtgacccagt actactatac ctgaggaggt gtcgctcgtc ggtaccctac actctaggtg    300  
               
               
                   
               
               
                 tatcgtcgca tctattccct tcgggcgttg tgatccgaca acaacaaggt catttctagc    360  
               
               
                   
               
               
                 tttccagtcc gctgtcactg ctagctgaaa aagctcgtac tactgttgct gctggacgag    420  
               
               
                   
               
               
                 gacgttatag gcaggggatg gcatctcacc cttatttacc caaacatcaa cgtgataaag    480  
               
               
                   
               
               
                 agcgtcctta attaactttc gggacgttta acgacaaaga gaaaggaata taatttggaa    540  
               
               
                   
               
               
                 ggaggacaat gtaattttaa cgtacaattc tgtaaagaca tacctaggct tgtactctag    600  
               
               
                   
               
               
                 atagtaactt cattacccat cctaaatgta atagtagtag tagtagtaga ggtacccaaa    660  
               
               
                   
               
               
                 cctagattaa tctggctttt ggagtaaatt ttaggttggg ttataaccga actgaacgag    720  
               
               
                   
               
               
                 gtagaggttc tttttatgtt gttcttgttg tttttaaatc ctacgtgtaa cttaactaaa    780  
               
               
                   
               
               
                 ccagtgatac tctcttagtg cctaattttt ataattttat tttttattta gtattagtag    840  
               
               
                   
               
               
                 atgagtgaga ttgctaagtg taagataggt ggtttaaact gtagccgaag attaattaaa    900  
               
               
                   
               
               
                 gtatataatc caagattttt tagagaggga aactgtctac ttatttataa agaaaattaa    960  
               
               
                   
               
               
                 gcaatccctt cctagattat attatatata tatatatata taaataaata atctaagatt   1020  
               
               
                   
               
               
                 ggtaaagaga gtggtcttat acttagctgc cggtatagac gtttttgggt ggttaacaag   1080  
               
               
                   
               
               
                 tgtcatttgc gagtaactta tctccagctt taatgaaaat ttaaagatct ctaaaggtta   1140  
               
               
                   
               
               
                 ttttatatga gcatagaaaa tgtcactact acgaggccta ctattctacc ttcctacgca   1200  
               
               
                   
               
               
                 cacagtcggc ggacgctaga gacaccgccc ctgctctgct tctgttcctg cactcgcctg   1260  
               
               
                   
               
               
                 ctatggttca gaagaggagg gggtggtgcg tgcagagtct aagggctatg ccggataggg   1320  
               
               
                   
               
               
                 ccaccgcaca cctgacgtgt ctgcttgctc atttacgggt aggggggaga aagtaagaaa   1380  
               
               
                   
               
               
                 gagaaacgca cacactctcc tcgcggatat ttattcgtgc tttgttcggg gaaaagagag   1440  
               
               
                   
               
               
                 gttcttgtgt ggtgtggtaa gtgtgtgatg taggagacga agaagctcgg aaaagcggaa   1500  
               
               
                   
               
               
                 ggaaggagca gattggtaca gctggacgcc gttgacgctg acgcaactgt tctcggtcac   1560  
               
               
                   
               
               
                 gcacattcag taggaggtag ggaggtggag aagaagaaga agaagaagaa gaagaagatt   1620  
               
               
                   
               
               
                 ggagcggggc aaacacaaac tactcagctg agaagggtgt agcgagcagt tttgagtctc   1680  
               
               
                   
               
               
                 gaaataatcc cttgtagtcg ttatgatata catatacatn ttccagttgc aaccgacttc   1740  
               
               
                   
               
               
                 ttgaaccaaa acggaaacgt ccttcttncc tttgtcgatg ncatagntat aacaactntg   1800  
               
               
                   
               
               
                 gcttttntcc atgactaatn gaagaagagg gaggaggagc agctntacta gtttgattaa   1860  
               
               
                   
               
               
                 tcctaatgng gaataatg                                                 1878  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 39  
               
               
                 &lt;211&gt; LENGTH: 597  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 546, 562, 572, 575, 579, 588, 594  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 39  
               
               
                   
               
               
                 Ser Leu Val Arg Gly Pro Pro Arg Gly Arg Arg Tyr Arg Ala Leu Ile  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ser Ser Leu Asn Leu Ser Leu Ser Leu Ser Leu Ser Leu Ser Leu Tyr  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Phe Lys Tyr Gly Cys Asn Ala Glu Leu Leu Cys Leu Ser Trp Pro Asn  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Cys Val His Leu Ala Asp Lys Ser Gly Asp Asn Val Leu Phe Thr Glu  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Ser Thr Ala Gly Gly Pro Glu Ile Thr Ser Asp Ala His Trp Val Met  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Met Ile Trp Thr Pro Pro Gln Arg Ala Ala Met Gly Cys Glu Ile His  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Ala Ala Ile Arg Glu Ala Arg Asn Thr Arg Leu Leu Leu Phe Gln Arg  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Lys Gly Gln Ala Thr Val Thr Ile Asp Phe Phe Glu His Asp Asp  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Asn Asp Asp Leu Leu Leu Gln Tyr Pro Ser Pro Thr Val Glu Trp Glu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Met Gly Leu Leu His Tyr Phe Ser Gln Glu Leu Ile Glu Ser Pro Ala  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asn Cys Cys Phe Ser Phe Leu Ile Leu Asn Leu Pro Pro Val Thr Leu  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Lys Leu His Val Lys Thr Phe Leu Tyr Gly Ser Glu His Glu Ile Tyr  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 His Ser Asn Gly Asp Leu His Tyr His His His His His Leu His Gly  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Phe Gly Ser Asn Thr Glu Asn Leu Ile Asn Pro Thr Ile Leu Ala Leu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ala Pro Ser Pro Arg Lys Ile Gln Gln Glu Gln Gln Lys Phe Arg Met  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 His Ile Glu Leu Ile Trp Ser Leu Glu Asn His Gly Leu Lys Ile Leu  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Lys Lys Ile Asn His Asn His Leu Leu Thr Leu Thr Ile His Ile Leu  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Ser Thr Lys Phe Asp Ile Gly Phe Leu Ile Ser Tyr Ile Arg Phe Lys  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Ile Ser Pro Phe Asp Arg Ile Asn Ile Ser Phe Asn Ser Leu Gly Lys  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Asp Leu Ile Tyr Ile Tyr Ile Tyr Ile Phe Ile Tyr Ile Leu Thr Ile  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Ser Leu Thr Arg Ile Ile Asp Gly His Ile Cys Lys Asn Pro Pro Ile  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Val His Ser Lys Arg Ser Leu Asn Gly Arg Asn Tyr Phe Ile Ser Arg  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Asp Phe Gln Asn Ile Leu Val Ser Phe Thr Val Met Met Leu Arg Met  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ile Arg Trp Lys Asp Ala Cys Val Ser Arg Leu Arg Ser Leu Trp Arg  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Gly Arg Asp Glu Asp Lys Asp Val Ser Gly Arg Tyr Gln Val Phe Ser  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Ser Pro Thr Thr His Val Ser Asp Ser Arg Tyr Gly Leu Ser Arg Trp  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Arg Val Asp Cys Thr Asp Glu Arg Val Asn Ala His Pro Pro Ser Phe  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Ile Leu Ser Leu Cys Val Cys Glu Arg Ser Ala Tyr Lys Ala Arg Asn  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Lys Pro Leu Phe Ser Pro Arg Thr His His Thr Ile His Thr Leu His  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Pro Leu Leu Leu Arg Ala Phe Ser Pro Ser Phe Leu Val Pro Cys Arg  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Pro Ala Ala Thr Ala Thr Ala Leu Thr Arg Ala Ser Ala Cys Lys Ser  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Ser Ser Ile Pro Pro Pro Leu Leu Leu Leu Leu Leu Leu Leu Leu Leu  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Thr Ser Pro Arg Leu Cys Leu Met Ser Arg Leu Phe Pro His Arg Ser  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ser Lys Leu Arg Ala Leu Leu Gly Asn Ile Ser Asn Thr Ile Cys Ile  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Cys Xaa Arg Ser Thr Leu Ala Glu Glu Leu Gly Phe Ala Phe Ala Gly  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Arg Xaa Glu Thr Ala Thr Val Ser Ile Leu Leu Xaa Pro Lys Xaa Gly  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Thr Asp Xaa Leu Leu Leu Pro Pro Pro Arg Arg Xaa Ser Asn Leu Gly  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Leu Xaa Leu Ile Thr  
               
               
                         595  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 40  
               
               
                 &lt;211&gt; LENGTH: 590  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 540, 556, 560, 562, 565, 568, 572, 580, 588  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 40  
               
               
                   
               
               
                 His Trp Tyr Gly Ala Pro Leu Glu Val Asp Gly Ile Asp Lys Leu Ser  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Leu Ser Ile Ser Leu Ser Leu Ser Leu Ser Leu Ser Leu Cys Met  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Ser Leu Asn Met Val Val Met Leu Asn Cys Tyr Val Tyr Leu Gly Gln  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Thr Val Ser Ile Phe Glu Gln Ile Asn Leu Ala Ile Met Phe Phe Leu  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Leu Lys Ala Leu Gln Asp Glu Gly Leu Lys Ser His Arg Thr Pro Thr  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Gly Ser Tyr Gly Leu Leu His Ser Glu Gln Pro Trp Asp Val Arg Ser  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Thr Gln Arg Arg Gly Lys Pro Ala Thr Leu Gly Cys Cys Cys Ser Ser  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Lys Asp Arg Lys Val Arg Arg Gln Arg Ser Thr Phe Ser Ser Met Met  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Thr Thr Thr Thr Cys Ser Cys Asn Ile Arg Pro Leu Pro Ser Gly Asn  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Lys Trp Val Cys Ser Cys Thr Ile Ser Arg Arg Asn Leu Lys Ala Leu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Gln Ile Ala Val Ser Leu Ser Leu Tyr Thr Phe Leu Leu Leu His Asn  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Cys Met Leu Arg His Phe Cys Met Asp Pro Asn Met Arg Ser Ile Ile  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Glu Val Met Gly Arg Ile Tyr Ile Ile Ile Ile Ile Ile Ile Ser Met  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Leu Asp Leu Ile Arg Pro Lys Thr Ser Phe Lys Ile Gln Pro Tyr  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Trp Leu Asp Leu Leu His Leu Gln Glu Lys Tyr Asn Lys Asn Asn Lys  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Asn Leu Gly Cys Thr Leu Asn Phe Gly His Tyr Glu Arg Ile Asp Lys  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Tyr Asn Lys Lys Ile Ile Ile Ile Tyr Ser Leu Arg Phe Thr Phe Tyr  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Pro Pro Asn Leu Thr Ser Ala Ser Asn Phe His Ile Leu Gly Ser Lys  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Lys Ser Leu Pro Leu Thr Asp Glu Ile Phe Leu Leu Ile Arg Gly Arg  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Ile Tyr Asn Ile Tyr Ile Tyr Ile Tyr Leu Phe Ile Arg Phe Pro Phe  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Leu Ser Pro Glu Tyr Glu Ser Thr Ala Ile Ser Ala Lys Thr His Gln  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Leu Phe Thr Val Asn Ala His Ile Lys Val Glu Ile Thr Phe Lys Phe  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Leu Glu Ile Ser Asn Lys Ile Tyr Ser Tyr Leu Leu Gln Cys Ser Gly  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Asp Gly Arg Met Arg Val Ser Ala Ala Cys Asp Leu Cys Gly Gly Asp  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Glu Thr Lys Thr Arg Thr Ala Asp Asp Thr Lys Ser Ser Pro Pro Pro  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Pro Arg Thr Ser Gln Ile Pro Asp Thr Ala Tyr Pro Gly Gly Val Trp  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Thr Ala Gln Thr Asn Glu Met Pro Ile Pro Pro Leu Ser Phe Phe Leu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Phe Ala Cys Val Arg Gly Ala Pro Ile Asn Lys His Glu Thr Ser Pro  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Phe Ser Leu Gln Glu His Thr Thr Pro Phe Thr His Tyr Ile Leu Cys  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Phe Phe Glu Pro Phe Arg Leu Pro Ser Ser Ser Asn His Val Asp Leu  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Arg Gln Leu Arg Leu Arg Gln Glu Pro Val Arg Val Ser His Pro Pro  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Ser Leu His Leu Phe Phe Phe Phe Phe Phe Phe Phe Phe Pro Arg Pro  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Val Cys Val Val Asp Ser Ser His Ile Arg Ala Gln Asn Ser Glu Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Tyr Gly Thr Ser Ala Ile Leu Tyr Val Tyr Val Xaa Gly Gln Arg Trp  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Leu Lys Asn Leu Val Leu Pro Leu Gln Glu Glu Xaa Lys Gln Leu Xaa  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Tyr Xaa Tyr Cys Xaa Arg Lys Xaa Val Leu Ile Xaa Phe Phe Ser Leu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Leu Leu Val Xaa Asp Asp Gln Thr Asn Asp Tyr Xaa Leu Leu  
               
               
                             580                 585                 590  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 41  
               
               
                 &lt;211&gt; LENGTH: 441  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 41  
               
               
                   
               
               
                 Thr Gly Thr Gly Pro Pro Ser Arg Ser Thr Val Ser Ile Ser Phe Asp  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Phe Ser Gln Ser Leu Ser Leu Ser Leu Ser Leu Ser Leu Ser Val  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Cys Leu Ile Trp Leu Cys Ile Ala Met Phe Ile Leu Ala Lys Leu Cys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Pro Ser Leu Ser Arg Ile Trp Arg Cys Ser Phe Tyr Lys His Cys Arg  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Met Arg Ala Asn His Ile Gly Arg Pro Leu Gly His Asp Asp Met Asp  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ser Ser Thr Ala Ser Ser His Gly Met Asp Pro His Ser Ser Val Asp  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Lys Gly Ser Pro Gln His Ala Val Val Val Pro Val Lys Ile Glu Arg  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Gly Asp Ser Asp Asp Arg Leu Phe Arg Ala Gln Arg Arg Pro Ala  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Pro Ala Ile Ser Val Pro Tyr Arg Arg Val Gly Ile Asn Gly Phe Val  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Val Ala Leu Phe Leu Ala Gly Ile Asn Lys Pro Cys Lys Leu Leu Phe  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Leu Phe Pro Tyr Ile Lys Pro Ser Ser Cys Tyr Ile Lys Ile Ala Cys  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Asp Ile Ser Val Ser Trp Ile Arg Thr Asp Leu Ser Leu Lys Trp Val  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Gly Phe Thr Leu Ser Ser Ser Ser Ser Ser Pro Trp Val Trp Ile Leu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Asp Arg Lys Pro His Leu Lys Ser Asn Pro Asn Ile Gly Leu Thr Cys  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ser Ile Ser Lys Lys Asn Thr Thr Arg Thr Thr Lys Ile Asp Ala His  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Ile Asp Leu Val Thr Met Arg Glu Ser Trp Ile Lys Asn Ile Lys Ile  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Lys Asn Lys Ser Ser Ser Thr His Ser Asn Asp Ser His Ser Ile His  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gln Ile His Arg Leu Leu Ile Asn Phe Ile Tyr Val Leu Lys Asn Leu  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Ser Leu Gln Met Asn Lys Tyr Phe Phe Phe Val Arg Glu Gly Ser Asn  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Ile Ile Tyr Ile Tyr Ile Tyr Leu Arg Ser Lys Leu Leu Leu Asn Phe  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Arg Phe Pro Ile Lys Tyr Thr Arg Ile Phe Tyr Ser Asp Asp Ala Pro  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Asp Asp Lys Met Glu Gly Cys Val Cys Gln Pro Pro Ala Ile Ser Val  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Ala Gly Thr Arg Arg Arg Gln Gly Arg Glu Arg Thr Ile Pro Ser Leu  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Leu Leu Pro His His Ala Arg Leu Arg Phe Pro Ile Arg Pro Ile Pro  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Val Ala Cys Gly Leu His Arg Arg Thr Ser Lys Cys Pro Ser Pro Leu  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Phe His Ser Phe Ser Leu Arg Val Glu Glu Arg Leu Ile Ser Thr Lys  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Gln Ala Pro Phe Leu Ser Lys Asn Thr Pro His His Ser His Thr Thr  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Ser Ser Ala Ser Ser Ser Leu Phe Ala  
               
               
                         435                 440  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 42  
               
               
                 &lt;211&gt; LENGTH: 17  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Artificial Sequence  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;223&gt; OTHER INFORMATION: primer  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 42  
               
               
                   
               
               
                 gatcgccatg gtgaatg                                                    17  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 43  
               
               
                 &lt;211&gt; LENGTH: 17  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Artificial Sequence  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;223&gt; OTHER INFORMATION: primer  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 43  
               
               
                   
               
               
                 gtaaaacgac ggccagt                                                    17  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 44  
               
               
                 &lt;211&gt; LENGTH: 2156  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 879  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 44  
               
               
                   
               
               
                 ggatcccaac ttttaggaat ggatcttaaa attttagtta taagttcaaa gttagaaaaa     60  
               
               
                   
               
               
                 tctttaccaa gagctttgag tccattgatg acatccgtga aacggtgtac atgtctccga    120  
               
               
                   
               
               
                 tggactcact tggtttcatt cggaaaagtt cgaaagagtg cataagaata ttgattttgg    180  
               
               
                   
               
               
                 attctttcac tcggttggtg ccttcatgag tgacctcaag agtcctccaa atatcaaaag    240  
               
               
                   
               
               
                 ccgaatcaca aattgaaatg tgattgaatt catttttgtc taatgcacaa aacagggcat    300  
               
               
                   
               
               
                 tcatagcctt tgtgtttaaa gcaaaaacat tcttctccga ttcatcccat tcgctcatcg    360  
               
               
                   
               
               
                 gaagagaaaa tttttgaaat ccattttcga caatagacca aagctcgaaa tccatggaaa    420  
               
               
                   
               
               
                 tgaggaagat cctcatatga gttttccaat acatgtaatt cgactcatta aacataggtg    480  
               
               
                   
               
               
                 gatgtgtaat gaaatgaccc tcatgcscta tctctcttgg gtattaaacc aaatatgaga    540  
               
               
                   
               
               
                 gtgagccttg ctctgatacc aattgttagg atcagagtgg cactaagaga gggggggagt    600  
               
               
                   
               
               
                 gaattagtgc agtggattaa aacttataag tttaaaaatg aattcgtaaa tacgagaaga    660  
               
               
                   
               
               
                 tttcgtttta atagtaactt gagtagatga aaaccaaaag ttaacagtag tgtaaataac    720  
               
               
                   
               
               
                 aatttcggga aagtaagaac tcacacattc aaggaacata ccaatttaaa gtggttcggt    780  
               
               
                   
               
               
                 caaaatgacc tacatccact tgtgaagcct tcttcgaaga ggctcccaac ttccactagc    840  
               
               
                   
               
               
                 aaatcacttt gaaggggaag gacaaatacc tctcttacna ccttttacaa tggttcatac    900  
               
               
                   
               
               
                 tcttacaaat tttcaacgag aaagaaggag gtgaacatgc aagcaattga aaacaagact    960  
               
               
                   
               
               
                 tgctaaagac tttgctaagg ctttttttct caatctattg cttctcaaaa gttgtattct   1020  
               
               
                   
               
               
                 ctgctgagaa ttgaggggta tttatagacc ccaagaggat ttaaatttgg gctccaaatt   1080  
               
               
                   
               
               
                 tcgaatgctc ttgggttccc gaggttgccg gtgccaccgc ctgtcagtgt ttgacactgg   1140  
               
               
                   
               
               
                 acagtgtact agcggtgcca ccgccggacc tctcgggtgt tgggcggtgc caccgcctag   1200  
               
               
                   
               
               
                 actttttcag ctcactggtt ggattccaaa cttgacccaa accagtccga actcgggtcc   1260  
               
               
                   
               
               
                 aattgacccg taaccggatt ataggattaa cccttaatcc taaccctaat tatatgcaaa   1320  
               
               
                   
               
               
                 ctacgcaact gaaaatatag tcctaagcaa gtttttaacc ggcaaacgtc gagtcttctt   1380  
               
               
                   
               
               
                 ccggcgatct ttcggcagac ttctgatata cctttggatt tcttctagcg gactcctagt   1440  
               
               
                   
               
               
                 agggtcccga tcttgtggcg agtttagcga gtagccgaac cttctcggtg atctccgcaa   1500  
               
               
                   
               
               
                 accgccgatg atctcttcgg cagactttcg aaaacttcga caagtccccg atttcttctc   1560  
               
               
                   
               
               
                 ggttggttcc gacagcatct ctaacgaaac ttcggactcc ttgaatgtcc atcgaacttg   1620  
               
               
                   
               
               
                 actccggtag gcttgcttta tattttcagg ctatcatagt taatcctaca tacttaactc   1680  
               
               
                   
               
               
                 aataatatgg attagattaa ttaacccatc aattgatttc atcatcaaaa ttcgacattc   1740  
               
               
                   
               
               
                 aacaaacatc cgtactcaat aacccatcag gctatagtta cgtgactatc tactgtgatc   1800  
               
               
                   
               
               
                 cgtacgtgaa gttagcgagt catgatccag gtcgtgtcac ttattggccg aacacgtatc   1860  
               
               
                   
               
               
                 ccttatccaa atccagtctt ctcaactctt ctagcctacc cgtctctttt tttattactt   1920  
               
               
                   
               
               
                 ttgaaagaat tcaaatcaaa acagatacaa aataacacgg tgagacactg tgacatgcta   1980  
               
               
                   
               
               
                 gtctctggaa agcattaatt cgcgcatcca cagacgtcgt cagcttcatc acccactttt   2040  
               
               
                   
               
               
                 tcctacatac catgtcgcat ggctttgttg atgacagacc accacaagct tgcctttggt   2100  
               
               
                   
               
               
                 tgtgcctaac agagagagag agagagacag accgatagcc tcctcattca ctatgg       2156  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 45  
               
               
                 &lt;211&gt; LENGTH: 2160  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Musa acuminata  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 883  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 45  
               
               
                   
               
               
                 ggatcccaac ttttaggaat ggatcttaaa attttagtta taagttcaaa gttagaaaaa     60  
               
               
                   
               
               
                 tctttaccaa gagctttgag tccattgatg acatccgtga aacggtgtac atgtctccga    120  
               
               
                   
               
               
                 tggactcact tggtttcatt cggaaaagtt cgaaagagtg cataagaata ttgattttgg    180  
               
               
                   
               
               
                 attctttcac tcggttggtg ccttcatgag tgacctcaag agtcctccaa atatcaaaag    240  
               
               
                   
               
               
                 ccgaatcaca aattgaaatg tgattgaatt catttttgtc taatgcacaa aacagggcat    300  
               
               
                   
               
               
                 tcatagcctt tgtgtttaaa gcaaaaacat tcttctccga ttcatcccat tcgctcatcg    360  
               
               
                   
               
               
                 gaagagaaaa tttttgaaat ccattttcga caatagacca aagctcgaaa tccatgcatg    420  
               
               
                   
               
               
                 gaaatgagga agatcctcat atgagttttc caatacatgt aattcgactc attaaacata    480  
               
               
                   
               
               
                 ggtggatgtg taatgaaatg accctcatgc sctatctctc ttgggtatta aaccaaatat    540  
               
               
                   
               
               
                 gagagtgagc cttgctctga taccaattgt taggatcaga gtggcactaa gagagggggg    600  
               
               
                   
               
               
                 gagtgaatta gtgcagtgga ttaaaactta taagtttaaa aatgaattcg taaatacgag    660  
               
               
                   
               
               
                 aagatttcgt tttaatagta acttgagtag atgaaaacca aaagttaaca gtagtgtaaa    720  
               
               
                   
               
               
                 taacaatttc gggaaagtaa gaactcacac attcaaggaa cataccaatt taaagtggtt    780  
               
               
                   
               
               
                 cggtcaaaat gacctacatc cacttgtgaa gccttcttcg aagaggctcc caacttccac    840  
               
               
                   
               
               
                 tagcaaatca ctttgaaggg gaaggacaaa tacctctctt acnacctttt acaatggttc    900  
               
               
                   
               
               
                 atactcttac aaattttcaa cgagaaagaa ggaggtgaac atgcaagcaa ttgaaaacaa    960  
               
               
                   
               
               
                 gacttgctaa agactttgct aaggcttttt ttctcaatct attgcttctc aaaagttgta   1020  
               
               
                   
               
               
                 ttctctgctg agaattgagg ggtatttata gaccccaaga ggatttaaat ttgggctcca   1080  
               
               
                   
               
               
                 aatttcgaat gctcttgggt tcccgaggtt gccggtgcca ccgcctgtca gtgtttgaca   1140  
               
               
                   
               
               
                 ctggacagtg tactagcggt gccaccgccg gacctctcgg gtgttgggcg gtgccaccgc   1200  
               
               
                   
               
               
                 ctagactttt tcagctcact ggttggattc caaacttgac ccaaaccagt ccgaactcgg   1260  
               
               
                   
               
               
                 gtccaattga cccgtaaccg gattatagga ttaaccctta atcctaaccc taattatatg   1320  
               
               
                   
               
               
                 caaactacgc aactgaaaat atagtcctaa gcaagttttt aaccggcaaa cgtcgagtct   1380  
               
               
                   
               
               
                 tcttccggcg atctttcggc agacttctga tatacctttg gatttcttct agcggactcc   1440  
               
               
                   
               
               
                 tagtagggtc ccgatcttgt ggcgagttta gcgagtagcc gaaccttctc ggtgatctcc   1500  
               
               
                   
               
               
                 gcaaaccgcc gatgatctct tcggcagact ttcgaaaact tcgacaagtc cccgatttct   1560  
               
               
                   
               
               
                 tctcggttgg ttccgacagc atctctaacg aaacttcgga ctccttgaat gtccatcgaa   1620  
               
               
                   
               
               
                 cttgactccg gtaggcttgc tttatatttt caggctatca tagttaatcc tacatactta   1680  
               
               
                   
               
               
                 actcaataat atggattaga ttaattaacc catcaattga tttcatcatc aaaattcgac   1740  
               
               
                   
               
               
                 attcaacaaa catccgtact caataaccca tcaggctata gttacgtgac tatctactgt   1800  
               
               
                   
               
               
                 gatccgtacg tgaagttagc gagtcatgat ccaggtcgtg tcacttattg gccgaacacg   1860  
               
               
                   
               
               
                 tatcccttat ccaaatccag tcttctcaac tcttctagcc tacccgtctc tttttttatt   1920  
               
               
                   
               
               
                 acttttgaaa gaattcaaat caaaacagat acaaaataac acggtgagac actgtgacat   1980  
               
               
                   
               
               
                 gctagtctct ggaaagcatt aattcgcgca tccacagacg tcgtcagctt catcacccac   2040  
               
               
                   
               
               
                 tttttcctac ataccatgtc gcatggcttt gttgatgaca gaccaccaca agcttgcctt   2100  
               
               
                   
               
               
                 tggttgtgcc taacagagag agagagagag acagaccgat agcctcctca ttcaccatgg   2160