Abstract:
The invention concerns novel enzymes having an arogenate dehydrogenase activity, in particular arogenate dehydrogenase enzymes of plants, and the genes encoding said enzymes. The inventive arogenate dehydrogenase enzymes catalyze the last stage of the metabolic pathway of tyrosine biosynthesis, and constitute, as such, potential targets of herbicides. Hence the invention also concerns a method for identifying herbicide compounds targeting said enzymes, said herbicide compounds preventing tyrosine biosynthesis by being fixed on said enzymes. The invention further concerns transgenic plants tolerant to herbicide compounds targeting an enzyme involved in the tyrosine biosynthesis pathway, in particular an enzyme involved in the transformation of L-tyrosine prephenate, in particular an arogenate dehydrogenase enzyme. Said plants become tolerant by expression in their tissues of a prephenate dehydrogenase enzyme, said enzyme being insensitive to said herbicide compounds and enabling the plant to synthetize tyrosine despite being treated with said herbicide compounds.

Description:
[0001]    The present invention relates to novel enzymes having arogenate dehydrogenase activity, in particular plant arogenate dehydrogenase enzymes, and also to the genes encoding these enzymes. The arogenate hydrogenase enzymes according to the invention catalyze the final step in the metabolic pathway of tyrosine biosynthesis and, in this respect, constitute potential targets for herbicides. The present invention therefore also relates to a method for identifying herbicidal compounds having these enzymes as a target, said herbicidal compounds preventing tyrosine biosynthesis by attaching to said enzymes. The invention also relates to transgenic plants tolerant to herbicidal compounds having as a target an enzyme involved in the biosynthetic pathway for tyrosine, in particular an enzyme involved in the conversion of prephenate to L-tyrosine, in particular an arogenate dehydrogenase enzyme. These plants become tolerant by expression, in their tissues, of a prephenate dehydrogenase enzyme, this enzyme being insensitive to said herbicidal compounds and enabling the plant to synthesize tyrosine despite treatment with said herbicidal compounds.  
           [0002]    The biosynthetic pathway for aromatic amino acids constitutes a metabolic pathway which is essential for plants, bacteria and fungi. In addition to the biosynthesis of tyrosine, phenylalanine and tryptophan, this metabolic pathway plays an essential role in the production of many secondary aromatic metabolites involved in processes such as plant-microbe interactions, the biosynthesis of structural biopolymers such as lignin and suberin, hormone synthesis, or quinone synthesis. Among all the living organisms which have this metabolic pathway, two pathways have been identified for converting prephenate to tyrosine (FIG. 1; Stenmark et al., 1974). In most chlorophyll-containing bacteria, some microorganisms and most plants, L-tyrosine is synthesized via the arogenate pathway (Abou-Zeid et al., 1995; Byng et al., 1981; Connely and Conn 1986; Frazel and Jensen 1979; Gaines et al., 1982; Hall et al., 1982; Keller et al., 1985; Mayer et al., 1985). In this pathway, the prephenate is transaminated to arogenate by a specific transaminase, prephenate aminotransferase (EC 2.6.1.57), and the arogenate is then converted to L-tyrosine by an arogenate dehydrogenase (EC 1.3.1.43; ADH on FIG. 1). In a different manner, in organisms such as the bacterium  Escherichia coli  or yeast, the prephenate is, initially, converted to p-hydroxyphenylpyruvate by a prephenate dehydrogenase (EC 1.3.1.12, EC 1.3.1.13), which p-hydroxyphenylpyruvate is transaminated to L-tyrosine (Lingens et al., 1967). By virtue of its role in the biosynthetic pathway for tyrosine in plants, the arogenate dehydrogenase enzyme constitutes a potential target for novel herbicides.  
           [0003]    Other enzymes involved in this metabolic pathway already constitute major herbicide targets. Mention may, for example, be made of the enzyme 5-enolpyruvyl-shikimate 3-phosphate synthase (EPSPS), involved upstream of prephenate synthesis, which is the target for the total herbicide glyphosate. Mention may also be made of the enzyme p-hydroxyphenylpyruvate dioxygenase (HPPD) involved in the conversion of p-hydroxyphenylpyruvate to homogentisate. HPPD is the target for novel families of herbicides, the activity of which leads to bleaching of the leaves (Schulz et al., 1993; Secor 1994). These herbicides are in particular isoxazoles (EP 418 175, EP 470 856, EP 487 352, EP 527 036, EP 560 482, EP 682 659, U.S. Pat. No. 5,424,276), in particular isoxaflutole, a maize-selective herbicide, diketonitriles (EP 496 630, EP 496 631) in particular 2-cyano-3-cyclopropyl-1-(2-SO 2 CH 3 -4-CF 3  phenyl)propane-1,3-dione and 2-cyano-3-cyclopropyl-1-(2-SO 2 CH 3 -4,2,3-Cl 2  phenyl)propane-1,3-dione, triketones (EP 625 505, EP 625 508, U.S. Pat. No. 5,506,195), in particular sulcotrione or mesotrione, or else pyrazolinates.  
           [0004]    One of the advantages of the herbicides having for a target enzymes involved in the metabolic pathways essential to plants is their broad spectrum of activity on plants of distant phylogenetic origins. However, such herbicides also have the major drawback, when they are applied to crops in order to eliminate the undesirable plants or “weeds”, of also acting on the cultivated plants. This drawback can be overcome by using cultivated plants tolerant to said herbicides. Such plants are generally obtained by genetic engineering, by introducing into their genome a gene encoding an enzyme for resistance to said herbicide, in such a way that they overexpress said enzyme in their tissues. To date, three main strategies using genetic engineering have been employed to make plants tolerant to herbicides. The first consists in detoxifying the herbicide by transforming the plant with a gene encoding a detoxification enzyme. This enzyme converts the herbicide, or its active metabolite, to nontoxic degradation products, such as, for example, the enzymes for tolerance to bromoxynil or to basta (EP 242 236, EP 337 899). The second strategy consists in transforming the plant with a gene encoding the target enzyme mutated in such a way that it is less sensitive to the herbicide, or its active metabolite, such as, for example, the enzymes for tolerance to glyphosate (EP 293 356, Padgette S. R. &amp; al., J. Biol. Chem., 266, 33, 1991). The third strategy consists in over-expressing the sensitive target enzyme so as to produce, in the plant, large amounts of target enzyme, if possible much greater than the amount of herbicide entering the plant. This strategy, which has been used to successfully obtain plants tolerant to HPPD inhibitors (WO 96/38567), makes it possible to maintain a sufficient level of functional enzyme despite the presence of its inhibitor.  
           [0005]    The fact that two biosynthetic pathways for L-tyrosine exist in different taxonomic groups, and in particular that the pathway directly converting prephenate to p-hydroxyphenylpyruvate is not found in plants, makes it possible to envision a fourth strategy for making plants tolerant to herbicides. Specifically, in the case of use of a herbicidal compound having as target the arogenate dehydrogenase enzyme in plants, transforming the plants intended to be made tolerant with a gene encoding a bacterial or yeast prephenate dehydrogenase enzyme will enable said plants to synthesize L-tyrosine, and therefore to tolerate the presence of the herbicidal compound despite the inhibition of the arogenate dehydrogenase enzyme by said herbicidal compound. This novel strategy therefore consists in creating, in the plants intended to be made resistant, a bypassing of the natural metabolic pathway for tyrosine biosynthesis, which pathway uses the arogenate dehydrogenase enzyme, by artificial implantation in these plants of a novel metabolic pathway for tyrosine biosynthesis, which uses the prephenate dehydrogenase enzyme. Such bypassing allows the plants possessing it, preferably plants of agronomic interest, to tolerate the presence of the herbicidal compound which inhibits the natural metabolic pathway, whereas the plants not possessing this bypassing, in particular the weeds, will be sensitive to said herbicidal compound.  
         DESCRIPTION  
         [0006]    The present invention therefore relates to novel isolated polynucleotides encoding an enzyme having arogenate dehydrogenase activity. According to the present invention, the term “polynucleotide” is intended to mean a natural or artificial nucleotide sequence which may be of the DNA or RNA type, preferably of the DNA type, in particular double-stranded. The expression “enzymes having arogenate dehydrogenase activity” is intended to mean the enzymes capable of converting arogenate to L-tyrosine. The arogenate dehydrogenase activity is measured by any method which makes it possible either to measure a decrease in the amount of the arogenate substrate, or to measure an accumulation of a product derived from the enzyme reaction, namely L-tyrosine or the cofactor NADPH. In particular, the arogenate dehydrogenase activity can be measured by the method described in example 4.  
           [0007]    According to a particular embodiment of the invention, the polynucleotides encoding an arogenate dehydrogenase enzyme comprise polynucleotides encoding the polypeptide sequence selected from the sequence described in the sequence identifier SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 9, SEQ ID NO: 11 or SEQ ID NO: 13. It is well known to those skilled in the art that this definition includes all the polynucleotides which, although comprising nucleotide sequences which are different as a result of the degeneracy of the genetic code, encode the same amino acid sequence, which sequence is represented by the sequence identifiers SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 9, SEQ ID NO: 11 or SEQ ID NO: 13.  
           [0008]    The present invention also comprises isolated polynucleotides encoding arogenate dehydrogenase enzymes and capable of hybridizing selectively to one of the polynucleotides described above, or a fragment of these polynucleotides constituting a probe. According to the invention, the expression “polynucleotide capable of hybridizing selectively” is intended to mean the polynucleotides which, by one of the usual methods of the state of the art (Sambrook et al., 1989, Molecular Cloning: A Laboratory Manual, Nolan C. ed., New York: Cold Spring Harbor Laboratory Press), hybridize with the polynucleotides above, or with the probes which are derived therefrom, at a level significantly greater than the background noise. The background noise may be associated with the hybridization of other polynucleotides present, for example other cDNAs present in a cDNA library. The level of the signal generated by the interaction between the polynucleotide capable of hybridizing selectively and the polynucleotides defined by the sequences SEQ ID NOS: above according to the invention, or the probes, is generally 10 times, preferably 100 times, more intense than that generated by the interaction with other DNA sequences generating the background noise. The level of interaction can be measured, for example, by labeling the polynucleotides described above or the probes with radioactive elements, such as  32 P. Selective hybridization is generally obtained using very severe conditions for the medium (for example 0.03 M NaCl and 0.03 M sodium citrate at approximately 50° C.-60° C.).  
           [0009]    The invention also comprises isolated polynucleotides encoding arogenate dehydrogenase enzymes, and homologs of the polynucleotides described above. According to the invention, the term “homolog” is intended to mean polynucleotides exhibiting one or more sequence modifications compared to the nucleotide sequences described above and encoding an enzyme with functional arogenate dehydrogenase activity. These modifications may be natural or obtained artificially according to the usual techniques of mutation leading in particular to the addition, deletion or substitution of one or more nucleotides compared to the sequences of the invention. These modifications determine a degree of homology with respect to the sequences described above. Advantageously, the degree of homology will be at least 70% compared to the sequences described, preferably at least 80%, more preferentially at least 90%. The methods for measuring and identifying homologies between nucleic acid sequences are well known to those skilled in the art. Use may, for example, be made of the PILEUP or BLAST programs (Basic Local Alignment Search Tool; Altschul et al., 1993, J. Mol. Evol. 36: 290-300; Altschul et al., 1990, J. Mol. Biol. 215: 403-10; see also http://www.ncbi.nlm.nih.gov/BLAST/).  
           [0010]    The present invention also relates to fragments of the polynucleotides described above. The term “fragment” denotes in particular a fragment of at least 20 nucleotides, in particular of at least 50 nucleotides, and preferably of at least 100 nucleotides. According to a particular embodiment of the invention, the polynucleotide according to the invention is represented by the sequence identifier SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10 or SEQ ID NO: 12.  
           [0011]    The present invention also relates to polynucleotides comprising at least one of the polynucleotides as described above.  
           [0012]    All the polynucleotides described above encode arogenate dehydrogenase enzymes. Consequently, the invention therefore extends to all the arogenate dehydrogenase enzymes encoded by all of these polynucleotides.  
           [0013]    According to a particular embodiment of the invention, the arogenate dehydrogenase enzyme is an enzyme the peptide sequence of which is selected from the sequence described by the sequence identifier SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 9, SEQ ID NO: 11 or SEQ ID NO: 13., or a fragment of these sequences. The term “fragment” is intended to mean essentially a biologically active fragment, i.e. a fragment of the sequence of an arogenate dehydrogenase enzyme having the same activity as a complete arogenate dehydrogenase enzyme.  
           [0014]    According to a particular embodiment of the invention, the polynucleotides and the arogenate dehydrogenase enzymes described above originate from plants. More particularly, they originate from plants of the Arabidopsis genus, preferably of the  A. thaliana  genus, or from plants of the Picea genus, preferably Picea glauca.  
           [0015]    According to another particular embodiment of the invention, the polynucleotides and the arogenate dehydrogenase enzymes described above originate from bacteria. More particularly, they originate from bacteria of the Synechocystis genus.  
           [0016]    The present invention also relates to a chimeric gene comprising, functionally linked to one another, at least one promoter which is functional in a host organism, a polynucleotide encoding an arogenate dehydrogenase enzyme as defined in the present inven- tion, and a terminator element which is functional in this same host organism. The various elements that a chimeric gene may contain are, firstly, elements which regulate the transcription, translation and maturation of proteins, such as a promoter, a sequence encoding a signal peptide or a transit peptide, or a terminator element constituting a polyadenylation signal and, secondly, a polynucleotide encoding a protein. The expression “functionally linked to one another” means that said elements of the chimeric gene are linked to one another in such a way that the functioning of one of these elements is affected by that of another. By way of example, a promoter is functionally linked to a coding sequence when it is capable of affecting the expression of said coding sequence. The construction of the chimeric gene according to the invention and the assembly of its various elements can be carried out using techniques well known to those skilled in the art, in particular those described by Sambrook et al., (1989, Molecular Cloning: A Laboratory Manual, Nolan C. ed., New York: Cold Spring Harbor Laboratory Press). The choice of the regulatory elements constituting the chimeric gene depends essentially on the host species in which they must function, and those skilled in the art are capable of selecting regulatory elements which are functional in a given host organism. The term “functional” is intended to mean capable of functioning in a given host organism.  
           [0017]    The promoters which the chimeric gene according to the invention can contain are either constitutive or inducible. A constitutive promoter according to the present invention is a promoter which induces the expression of a coding sequence in all the tissues of a host organism and continuously, i.e. throughout the duration of the life cycle of said organism. Some of these promoters may be tissue-specific, i.e. express the coding sequence continuously, but only in a particular tissue of the host organism. Constitutive promoters may originate from any type of organism. Among the constitutive promoters which can be used in the chimeric gene of the present invention, mention may, for example, be made of bacterial promoters, such as that of the octopine synthase gene or that of the nopaline synthase gene, of viral promoters, such as that of the gene controlling transcription of the 19S or 35S RNAs of the cauliflower mosaic virus (Odell et al., 1985, Nature, 313, 810-812), or the promoters of the cassava vein mosaic virus (as described in patent application WO 97/48819). Among the promoters of plant origin, mention will be made of the promoter of the ribulose-biscarboxylase/oxygenase (RuBisCO) small sub-unit gene, the promoter of a histone gene as described in application EP 0 507 698, or the promoter of a rice actin gene (U.S. Pat. No. 5,641,876).  
           [0018]    According to another particular embodiment of the invention, the chimeric gene contains an inducible promoter. An inducible promoter is a promoter which only functions, i.e. which only induces expression of a coding sequence, when it is itself induced by an inducing agent. This inducing agent is generally a substance which can be synthesized in the host organism subsequent to a stimulus external to said organism, this external stimulus possibly being, for example, a pathogenic agent. The inducing agent may also be a substance external to this host organism, capable of penetrating into this host organism. Advantageously, the promoter used in the present invention is inducible subsequent to an attack on the host organism by a pathogenic agent. Such promoters are known, such as, for example, the promoter of the plant O-methyl-transferase class II (COMT II) gene described in patent application FR 99 03700, the Arabidopsis PR-1 promoter (Lebel et al., 1998, Plant J. 16(2):223-233), the EAS4 promoter of the tobacco sesquiterpene synthase gene (Yin et al., 1997, Plant Physiol. 115(2): 437-451), or the promoter of the gene encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase (Nelson et al., 1994, Plant Mol. Biol. 25(3): 401-412).  
           [0019]    Among the terminator elements which may be used in the chimeric gene of the present invention, mention may, for example, be made of the nos terminator element of the gene encoding  Agrobacterium tumefaciens  nopaline synthase (Beven et al., 1983, Nucleic Acids Res. 11(2), 369-385), or the terminator element of a histone gene as described in application EP 0 633 317.  
           [0020]    It also appears to be important for the chimeric gene to additionally comprise a signal peptide or a transit peptide which makes it possible to control and orient the production of the arogenate dehydrogenase enzyme specifically in a part of the host organism, such as, for example, the cytoplasm, a particular compartment of the cytoplasm, or the cell membrane or, in the case of plants, in a particular type of cellular compartment, for example the chloroplasts, or in the extracellular matrix.  
           [0021]    The transit peptides can be either single or double. The double transit peptides are optionally separated by an intermediate sequence, i.e. they comprise, in the direction of transcription, a sequence encoding a transit peptide of a plant gene encoding an enzyme located in plastids, a portion of sequence of the mature N-terminal portion of a plant gene encoding an enzyme located in plastids, and then a sequence encoding a second transit peptide of a plant gene encoding an enzyme located in plastids. Such double transit peptides are, for example, described in patent application EP 0 508 909.  
           [0022]    Signal peptides of use according to the invention which may be mentioned include in particular the signal peptide of the tobacco PR-1α gene described by Cornelissen et al. (1987, Nucleic Acid Res. 15, 6799-6811), in particular when the chimeric gene according to the invention is introduced into plant cells or plants, or the signal peptide of the Mat α1 factor precursor (Brake et al., 1985, In: Gething M.-J. (eds.); Protein transport and secretion, pp. 103-108, Cold Spring Harbor Laboratory Press, New York), when the chimeric gene according to the invention is introduced into yeast.  
           [0023]    The present invention also relates to a vector containing a chimeric gene according to the invention. The vector according to the invention is of use for transforming a host organism and expressing an arogenate dehydrogenase enzyme in this host organism. This vector may be a plasmid, a cosmid, a bacteriophage or a virus. In general, the main qualities of this vector should be an ability to persist and to self-replicate in the host organism&#39;s cells, in particular by virtue of the presence of an origin of replication, and to express therein an arogenate dehydrogenase enzyme. The choice of such a vector and also the techniques for inserting the chimeric gene according to the invention therein are widely described in Sambrook et al. (1989, Molecular Cloning: A Laboratory Manual, Nolan C. ed., New York: Cold Spring Harbor Laboratory Press) and are part of the general knowledge of those skilled in the art. Advantageously, the vector used in the present invention also contains, in addition to the chimeric gene of the invention, a gene encoding a selectable marker. This selectable marker makes it possible to select the host organisms effectively transformed, i.e. those having incorporated the vector. According to a particular embodiment of the invention, the host organism to be transformed is a microorganism, in particular a yeast, a bacterium, a fungus or a virus. According to another embodiment, the host organism is a plant or a plant cell. Among the genes encoding selectable markers which can be used, mention may be made of genes for resistance to antibiotics, such as, for example, the hygromycin phosphotransferase (Gritz et al., 1983, Gene 25: 179-188), but also the genes for tolerance to herbicides, such as the bar gene (White et al., NAR 18: 1062, 1990) for tolerance to bialaphos, the EPSPS gene (U.S. Pat. No. 5,188,642) for tolerance to glyphosate or else the HPPD gene (WO 96/38567) for tolerance to isoxazoles. Mention may also be made of genes encoding readily identifiable enzymes such as the GUS enzyme, or genes encoding pigments or enzymes which regulate the production of pigments in the transformed cells. Such selectable marker genes are in particular described in patent applications WO 91/02071, WO 95/06128, WO 96/38567 and WO 97/04103.  
           [0024]    The present invention also relates to transformed host organisms containing a vector as described above. The term “host organism” is intended to mean any lower or higher monocellular or pluricellular organism into which the chimeric gene according to the invention can be introduced, so as to produce arogenate dehydrogenase enzyme. They are in particular bacteria, for example  Escherichia coli , yeast, in particular of the Saccharomyces, Kluyveromyces or Pichia genera, fungi, in particular Aspergillus, a baculovirus, or preferably plant cells and plants.  
           [0025]    According to the invention, the term “plant cell” is intended to mean any cell derived from a plant and able to constitute undifferentiated tissues such as calluses, differentiated tissues such as embryos, parts of plants, plants or seeds.  
           [0026]    According to the invention, the term “plant” is intended to mean any differentiated multicellular organism capable of photosynthesis, in particular monocotyledons or dicotyledons.  
           [0027]    The term “transformed host organism” is intended to mean a host organism which has incorporated into its genome the chimeric gene of the invention and consequently produces an arogenate dehydrogenase enzyme in its tissues, or in a culture medium. Those skilled in the art can use one of the many known methods of transformation to obtain the host organisms according to the invention.  
           [0028]    One of these methods consists in bringing the cells to be transformed into contact with polyethylene glycol (PEG) and the vectors of the invention (Chang and Cohen, 1979, Mol. Gen. Genet. 168(1), 111-115); Mercenier and Chassy, 1988, Biochimie 70(4), 503-517). Electroporation is another method, which consists in subjecting the cells or tissues to be transformed and the vectors of the invention to an electric field (Andreason and Evans, 1988, Biotechniques 6(7), 650-660; Shigekawa and Dower, 1989, Aust. J. Biotechnol. 3(1), 56-62). Another method consists in directly injecting the vectors into the host cells or tissues by microinjection (Gordon and Ruddle, 1985, Gene 33(2), 121-136). Advantageously, the “biolistic” method may be used. In consists in bombarding cells or tissues with particles onto which the vectors of the invention are adsorbed (Bruce et al., 1989, Proc. Natl. Acad. Sci. USA 86(24), 9692-9697; Klein et al., 1992, Biotechnology 10(3), 286-291; U.S. Pat. No. 4,945,050). Preferentially, the plant transformation will be carried out using bacteria of the Agrobacterium genus, preferably by infecting the cells or tissue of said plants by  A. tumefaciens  (Knopf, 1979, Subcell. Biochem. 6, 143-173; Shaw et al., 1983, Gene 23(3): 315-330) or  A. rhizogenes  (Bevan and Chilton, 1982, Annu. Rev. Genet. 16: 357-384; Tepfer and Casse-Delbart, 1987, Microbiol. Sci. 4(1), 24-28). Preferentially, the transformation of plant cells with  Agrobacterium tumefaciens  is carried out according to the protocol described by Ishida et al. (1996, Nat. Biotechnol. 14(6), 745-750).  
           [0029]    Those skilled in the art will choose the appropriate method as a function of the nature of the host organism to be transformed.  
           [0030]    The present invention therefore also relates to a method for preparing the arogenate dehydrogenase enzyme, comprising the steps of culturing a transformed host organism comprising a gene encoding an arogenate dehydrogenase enzyme as defined above, in a suitable culture medium, recovering the arogenate dehydrogenase enzyme produced from the culture medium by centrifugation or by filtration, and then purifying the recovered enzyme by passing it through at least one chromatography column. These steps bring about the extraction and the purification, which may be total or partial, of the arogenate dehydrogenase enzyme obtained. Preferentially, the transformed organism is a microorganism, in particular a bacterium, a yeast, a fungus or a virus.  
           [0031]    The present invention also comprises a method for identifying a herbicidal compound having as a target an arogenate dehydrogenase enzyme, characterized in that:  
           [0032]    (a) at least two samples, each containing an equivalent amount of arogenate dehydrogenase enzymes in solution, are prepared;  
           [0033]    (b) one of the samples is treated with a compound;  
           [0034]    (c) the arogenate dehydrogenase activity is measured in each one of said samples;  
           [0035]    (d) the compound used in step (b) is identified as being a herbicidal compound when the activity measured in step (c) is significantly less in the treated sample compared to the untreated sample;  
           [0036]    (e) the herbicidal activity of the compound identified in step (d) is validated by treating plants with said compound.  
           [0037]    According to the present method, the measurement of the arogenate dehydrogenase activity is carried out by any method which makes it possible either to measure a decrease in the amount of arogenate substrate, or to measure an accumulation of a product derived from the enzyme reaction, namely L-tyrosine or the cofactor NADPH. In particular, the measurement of the arogenate dehydrogenase activity can be carried out by the method described in example 4. In addition, the herbicidal activity validated in step (e) of the present method may be a lethal activity resulting in the death of the treated plant, or an activity which significantly slows down the growth of the treated plant.  
           [0038]    According to the invention, the term “compound” is intended to mean any chemical compound or mixture of chemical compounds, including peptides and proteins. According to the invention, the term “mixture of compounds” is understood to mean at least two different compounds, such as, for example, the (dia)stereoisomers of a molecule, mixtures of natural origin derived from the extraction of biological material (plants, plant tissues, bacterial cultures, yeast cultures or fungal cultures, insects, animal tissues, etc.) or unpurified or totally or partially purified reaction mixtures, or else mixtures of products derived from combinatorial chemistry techniques.  
           [0039]    According to a particular embodiment of the method according to the invention, the arogenate dehydrogenase enzymes used originate from plants, preferably from  Arabidopsis thaliana.    
           [0040]    According to another embodiment of the method according to the invention, the arogenate dehydrogenase enzymes used originate from bacteria, preferably bacteria of the Synechocystis genus.  
           [0041]    Preferably, the arogenate dehydrogenase enzymes used in the method according to the invention are the enzymes according to the present invention, in particular those represented by SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 9, SEQ ID NO: 11 or SEQ ID NO: 13.  
           [0042]    The invention also extends to the herbicidal compounds identified using the method mentioned above, in particular the herbicidal compounds having as a target an arogenate dehydrogenase enzyme, i.e. those which inhibit the activity of this enzyme. Preferentially, the herbicidal compounds are not general enzyme inhibitors. Also preferentially, the herbicidal compounds according to the invention are not compounds already known to have herbicidal activity.  
           [0043]    The present invention also relates to herbicidal agrochemical compositions comprising, as active material, at least an effective amount of a herbicidal compound according to the invention.  
           [0044]    According to the invention, the term “herbicidal agrochemical composition” is intended to mean a composition which can be applied preventatively or curatively to the areas on which cultivated plants are being or must be grown, in order to prevent the development of undesirable plants or “weeds” on the areas on which said cultivated plants are grown, whatever their state of development. An effective amount of herbicidal compound according to the invention corresponds to an amount of compound which makes it possible to destroy or inhibit the growth of the undesirable plants.  
           [0045]    The herbicidal agrochemical compositions according to the invention comprise a herbicidal compound according to the invention or one of its agriculturally acceptable salts or a metal or metalloid complex of this compound, in combination with an agriculturally acceptable solid or liquid carrier and/or a surfactant, also agriculturally acceptable. In particular, the usual inert carriers and the usual surfactants can be used. These compositions cover not only the compositions ready to be applied to a plant or a seed to be treated using a suitable device, such as a spraying or dusting device, but also the concentrated commercially available compositions which must be diluted before they are applied to the crop.  
           [0046]    The herbicidal compositions according to the invention may also contain many other ingredients, such as, for example, protective colloids, adhesives, thickeners, thixotropic agents, penetrating agents, stabilizers or sequestering agents. More generally, the active materials can be combined with any solid or liquid additives which comply with the usual formulating techniques.  
           [0047]    According to the present invention, the term “carrier” denotes a natural or synthetic, organic or inorganic material with which the active material is combined in order to facilitate its application to the parts of the plant. This carrier is therefore generally inert and it must be agriculturally acceptable. The carrier may be solid (for example clays, natural or synthetic silicates, silica, resins, waxes, solid fertilizers) or liquid (for example water, alcohols, in particular butanol).  
           [0048]    The surfactant may be an emulsifier, dispersing agent or wetting agent of the ionic or nonionic type, or a mixture of such surfactants. Mention may, for example, be made of polyacrylic acid salts, lignosulfonic acid salts, phenolsulfonic or naphthalenesulfonic acid salts, polycondensates of ethylene oxide with fatty alcohols or with fatty acids or with fatty amines, substituted phenols (in particular alkylphenols or arylphenols), salts of sulfosuccinic acid esters, taurine derivatives (in particular alkyl taurates), phosphoric esters of alcohols or of phenols which are polyoxyethylated, esters of fatty acids and of polyols, and derivatives of the above compounds containing sulfate, sulfonate and phosphate functions. The presence of at least one surfactant is generally essential when the active material and/or the inert carrier are not water-soluble and when the vector agent for the application is water.  
           [0049]    The present invention also relates to transgenic plants tolerant to a herbicidal compound having as a target an enzyme involved in one of the metabolic steps of conversion of prephenate to L-tyrosine, characterized in that they contain a gene encoding a prephenate dehydrogenase enzyme and express said enzyme in their tissue. A prephenate dehydrogenase enzyme is an enzyme which catalyzes the reaction of conversion of prephenate to p-hydroxyphenylpyruvate. The identification of an enzyme with prephenate dehydrogenase activity can be carried out by any method which makes it possible either to measure a decrease in the amount of the prephenate substrate, or to measure an accumulation of a product derived from the enzyme reaction, namely p-hydroxyphenylpyruvate or one of the cofactors NADH or NADPH. In particular, the measurement of the prephenate dehydrogenase activity can be carried out using the method described in example 4.  
           [0050]    According to a particular embodiment of the invention, the transgenic plants according to the invention are tolerant with respect to a herbicidal compound having as a target an arogenate dehydrogenase enzyme, preferably an arogenate dehydrogenase enzyme as described in the present invention.  
           [0051]    According to another particular embodiment of the invention, the transgenic plants according to the invention are tolerant with respect to a herbicidal compound having as a target a prephenate aminotransferase enzyme.  
           [0052]    According to a particular embodiment of the invention, the gene encoding the prephenate dehydrogenase enzyme expressed in the tolerant plants according to the invention is a yeast gene. Preferably, it is the gene encoding the Saccharomyces cerevisiae prephenate dehydrogenase enzyme (accession No. NC001134) as described in Mannhaupt et al. (1989, Gene 85, 303-311) and represented by the sequence identifier SEQ ID NO: 14.  
           [0053]    According to another particular embodiment of the invention, the gene encoding the prephenate dehydrogenase enzyme expressed in the tolerant plants according to the invention is a bacterial gene. Preferably, it is a gene from a bacterium of the Bacillus genus, in particular of the species  B. subtilis  (accession No. M80245) as represented by the sequence identifier SEQ ID NO: 16. Preferably, it is a gene from a bacterium of the Escherichia genus, in particular of the species  E. coli  (accession No. M10431) as described in Hudson et al. (1984, J. Mol. Biol. 180(4), 1023-1051) and represented by the sequence identifier SEQ ID NO: 18. Preferably, it is a gene from a bacterium of the Erwinia genus, in particular the species  E. herbicola  (accession No. 43343) as represented by the sequence identifier SEQ ID NO: 20.  
           [0054]    According to particular embodiment of the invention, the gene encoding the prephenate dehydrogenase enzyme expressed in the tolerant plants according to the invention is a fungal gene.  
           [0055]    The transgenic plants according to the invention are obtained by genetic transformation with a gene encoding a prephenate dehydrogenase enzyme. Preferably, this gene is a chimeric gene comprising, functionally linked to one another, at least one promoter which is functional in a host organism, a polynucleotide encoding a prephenate dehydrogenase enzyme, and a terminator element which is functional in this same host organism. This gene is generally introduced into a vector, which is used to introduce said gene into said plants by one of the methods of transformation described above.  
           [0056]    The present invention also relates to a method for producing plants tolerant with respect to herbicidal compounds having as a target an enzyme involved in one of the metabolic steps for conversion of prephenate to L-tyrosine, characterized in that said plants are transformed with a gene encoding a prephenate dehydrogenase enzyme in such a way that they express it in their tissues.  
           [0057]    According to a particular embodiment of the invention, the present method applies to the production of plants tolerant with respect to a herbicidal compound having as a target an arogenate dehydrogenase enzyme as described in the present invention.  
           [0058]    According to another particular embodiment of the invention, the present method applies to the production of plants tolerant with respect to a herbicidal compound having as a target a prephenate aminotransferase enzyme.  
           [0059]    The present method therefore also comprises a method for producing plants tolerant with respect to a herbicidal compound having as a target an arogenate dehydrogenase enzyme, characterized in that said plants are transformed with a gene encoding a prephenate dehydrogenase enzyme in such a way that they express it in their tissues.  
           [0060]    The transgenic plants according to the invention may also contain, in addition to a gene encoding a prephenate dehydrogenase enzyme, at least one other gene containing a polynucleotide encoding a protein of interest. Among these polynucleotides encoding a protein of interest, mention may be made of polynucleotides encoding an enzyme for resistance to a herbicide, for example the polynucleotide encoding the bar enzyme (White et al., NAR 18:1062, 1990) for tolerance to bialaphos, the polynucleotide encoding the EPSPS enzyme (U.S. Pat. No. 5,188,642; WO 97/04103) for tolerance to glyphosate, or else the polynucleotide encoding the HPPD enzyme (WO 96/38567) for tolerance to isoxazoles. Mention may also be made of a polynucleotide encoding an insecticidal toxin, for example a polynucleotide encoding a toxin of bacterium  Bacillus thuringiensis  (for example, see International Patent Application WO 98/40490). Other polynucleotides for resistance to diseases may also be contained in these plants, for example a polynucleotide encoding the oxaylate oxidase enzyme as described in patent application EP 0 531 498 or U.S. Pat. No. 5,866,778, or a polynucleotide encoding another antibacterial and/or antifungal peptide, such as those described in patent applications WO 97/30082, WO 99/24594, WO 99/02717, WO 99/53053 and WO 99/91089. Mention may also be made of polynucleotides encoding agronomic characteristics of the plant, in particular a polynucleotide encoding a delta-6 desaturase enzyme, as described in U.S. Pat. Nos. 5,552,306 and 5,614,313, and patent applications WO 98/46763 and WO 98/46764, or a polynucleotide encoding a serine acetyltransferase (SAT) enzyme, as described in patent applications WO 00/01833 and PCT/FR 99/03179.  
           [0061]    The following examples make it possible to illustrate the present invention without, however, limiting the scope thereof. 
       
    
    
     EXAMPLE 1  
     Identification of the Gene Encoding the  Arabidopsis Thaliana  Arogenate Dehydrogense Enzyme  
       [0062]    A comparison of the sequences of all the prephenate dehydrogenase and arogenate dehydrogenase enzymes currently available in the public databases (http://www/ncbi/nlm/nih/gov) revealed four short portions of homologous sequences. The enzymes compared are yeast prephenate dehydrogenase (accession number: Z36065),  Bacillus subtilis  prephenate dehydrogenase (accession number: M80245) and Synechocystis prephenate dehydrogenase (accession number: D90910). These portions of homology made it possible to identify an  A. thaliana  gene (accession number: AF096371) initially noted as encoding an enzyme “similar to the specific D-isomer 2-hydroxy acid dehydrogenase”. This gene consists of two exons separated by a 94 bp intron. The first exon comprises a 1.08 kb open reading frame containing a putative chloroplast transit peptide sequence located downstream of the first ATG codon. The second exon potentially encodes an 892 bp open reading frame. A very strong homology of approximately 60% exists between the protein sequences deduced from the two exons. This homology extends to 70% if the putative chloroplast transit peptide sequence located in the first exon is not taken into account. In addition, each one of the two predicted protein sequences has the size and possesses the four homologous portions characteristic of the prephenate/arogenate dehydrogenase enzymes. This gene was named TyrA (SEQ ID NO: 1).  
       EXAMPLE 2  
     Transcriptional Characterization of TyrA  
       [0063]    The size of the transcript of the TyrA gene was determined using the Northern blotting and PCR techniques. Purified mRNAs extracted from young leaves of  A. thaliana  were hybridized with  32 P-radiolabeled probes corresponding to fragments of DNA of the two exons of TyrA. This analysis made it possible to identify a 1.8-1.9 kb transcript very close to the presumed size of an mRNA containing the two exons. In addition, although the complete cDNA could not be amplified by PCR, a 1.5 kb PCR fragment was obtained. This fragment comprises the 5′ oligonucleotide (P8=5′-GCTAAAACTCTTCTCCTTCAATACTTACCTG-3′) beginning at position 513 bp, and the 3′ oligonucleotide (P7=5′-CAGTATAATTAGTAGTCAAGGATCCTGACTGAGAG-3′) complementary to the 3&#39;UTR and beginning at position 2053 bp. This fragment contains a portion of the first coding sequence (TyrA-At1) and the complete sequence of the second coding sequence (TyrA-AT2). Analysis of the sequence of this cDNA confirmed the splicing of the intron. The results of the analyses by Northern blotting and PCR strongly suggests the existence of an mRNA transcript containing the two coding regions TyrA-At1 (SEQ ID NO: 4) and TyrA-AT2 (SEQ ID NO: 6).  
       EXAMPLE 3  
     Preparation of Constructs Containing the Various Coding Sequences of the  A. Thaliana  Arogenate Dehydrogenase  
       [0064]    The first exon TyrA-At1 was obtained by PCR amplification of the genomic DNA of  A. thaliana  with the oligonucleotide P1 (5′-TCTC CATATG ATCTTTCAATCTCAT-TCTCATC-3′) which introduces an Nde I restriction site (underlined) at the first ATG codon, and the oligonucleotide P2 (5′-CTAACTAACTAA CTA CATA-CCTCATCATATCC-3′) which is complementary to the 3′ end of the first exon and to the 5′ end of the intron and introduces a stop codon (underlined). Three constructs lacking the sequence encoding the transit peptide were also produced with the oligonucleotide P3 (5′-CCTCTCTTTCC ATATG CTCCCTTCTC-3′) which introduces an Nde I restriction site (underlined) at the second ATG codon (M43) at position 127, the oligonucleotide P4 (5′-CCGCCAGCCACCTC CATATG ACCGACACCATCC-3′) which introduces an ATG initiating codon and an Nde I restriction site (underlined) at position 174 from the first ATG codon (V58M), and the oligonucleotide P5 (5′-CGCCACCCCT CATATG CGTATCGCC-3′) which introduces an ATG initiating codon and an Nde I restriction site (underlined) at position 222 from the first ATG codon (L75M). All the OCR fragments corresponding to the first exon, which may or may not encode a transit peptide, were cloned into the plasmid pPCR-Script (Stratagene). Nde I-BamH I DNA fragments containing the coding sequences, with or without the transit peptide sequence, were then cloned into the plasmid pET21 a(+) (Novagen), leading to the development of the plasmids pET21-TyrA-AT1, with and without transit peptide sequence (pET21-TyrA-AT1-M1,pET21-TyrA-AT1-M43, pET21-TyrA-ATI-M58 and pET21-TyrA-ATi-M75).  
         [0065]    Two other oligonucleotides were used to amplify the second coding sequence (TyrA-AT2). The oligonucleotide P6 (5′-GATGCATCTTTG CATATG ATGAGGTCAGAAGATG-3′) introduces an Nde I restriction site (underlined) at the ATG codon of the second open reading frame (at position 1081 from the first ATG codon), and the oligonucleotide P7 (5′-CAGTATAATTAGTAGTCAAGGATCCTGACTGAGAG-3′), complementary to the start of the 3′-UTR, introduces a BamH I restriction site (underlined). The PCR fragment corresponding to the second coding sequence was digested with Nde I-BamH I and then cloned into the plasmid pET21 a(+), giving the plasmid pET21-TyrA-AT2.  
         [0066]    The complete coding sequence was reconstituted by assembly of the missing 5′ end of the first exon with a partial TyrA-AT cDNA (1.5 kb), obtained by PCR amplification of the Arabidopsis cDNA with the oligonucleotide P8 (5′-GCTAAAACTCTTCTCCTTCAATACTTACCTG-3′) beginning at position 513 bp from the first ATG codon, and the 3′ oligonucleotide P7. An EcoRV restriction site located at position 812 bp from the first ATG codon and present in the 5′ end of the partial TyrA-AT cDNA was used for the reconstitution. The partial TyrA-AT cDNA was cloned into the plasmid pPCR-Script. An EcoRV-EcoRV fragment was obtained from the plasmid pPCR-Script-TyrA-AT and then cloned into the plasmid pPCR-Script-TyrA-AT1 digested beforehand with EcoRV. This manipulation led to the plasmid pPCR-Script-TyrA-ATc being obtained. An Nde1-BamH1 fragment containing the complete coding sequence was excised from the plasmid pPCR-Script-TyrA-ATc, and then cloned into a plasmid pET21a(+) (Novagen), digested beforehand with Nde1 and BamH1, producing the plasmid pET2la(+)-TyrA-ATc. Then, in the same way as for the first exon, four plasmids pET21a(+)-TyrA-ATc were obtained; a plasmid containing the complete coding sequence with the sequence encoding the putative transit peptide, and three plasmids lacking this transit peptide sequence, which was cleaved at three different sites (M43, V58 and L75, see above).  
         [0067]    For all the constructs described above, the cDNA inserts were sequenced in order to be sure that no unwanted mutation had been introduced during the PCR amplification.  
       EXAMPLE 4  
     Measurement of the Enzyme Activities  
       [0068]    The arogenate dehydrogenase activity is measured at 25° C. by spectrophotometric monitoring, at 340 nm, of the formation of NADH or NADPH in a solution containing 50 mM of Tris-HCl, pH 8.6, 300 μm of arogenate and 1 mM of NAD or NADPH in a total volume of 200 μl.  
         [0069]    The prephenate dehydrogenase activity is measured at 25° C. by spectrophotometric monitoring, at 340 nm, of the formation of NADH or NADPH in a solution containing 50 mM of Tris-HCl, pH 8.6, 300 μM of prephenate and 1 mM of NAD or NADPH in a total volume of 200 μl.  
       EXAMPLE 5  
     Production of Recombinant Arogenate Dehydrogenase  
       [0070]    [0070] Eshcerichia coli  AT2471 cells were transformed with each one of the plasmids pET21-TyrA-AT obtained in example 3, and then cultured at 37° C. in 2 liters of Luria-Bertani medium supplemented with 100 μg/ml of carbenicillin. When the culture had reached the equivalent of an absorbance at 600 nm (A600) of 0.6, 1 mM of isopropyl-β-D-thiogalactoside was added to the culture medium in order to induce recombinant protein synthesis. The cells were then cultured for 16 h at 28° C., harvested, and then centrifuged for 20 min at 40 000 g. The pellet was then resuspended in a 50 mM Tris-HCl buffer, pH 7.5, containing 1 mM EDTA, 1 mM dithiothreitol, 1 mM benzamidine HCl and 5 mM aminocaproic acid, and then sonicated (100 pulses every 3 seconds at power 5) with a Vibra-Cell disrupter (Sonics and Materials, Danbury, Conn., USA). The crude extracts thus obtained were then centrifuged for 20 min at 40 000 g, and the supernatants were used directly for the enzyme assays.  
         [0071]    The SDS-PAGE analyses of total protein extracts of the  E. coli  strain AT 2471 containing the various constructs pET21-TyrA-Atc, pET21-TyrA-AT1 and pET21-TyrA-AT2 revealed the presence of three recombinant proteins having molecular masses of 66-68 kDa, 35 kDa and 33-34 kDa, respectively. These molecular masses correspond well to the masses deduced from their respective coding sequences (68786 Da for TyrA-ATc, 34966 Da for Tyr-A-AT1, and 34069 Da for Tyr-A-AT2). For the transformants containing the complete coding sequence (TyrA-Atc) and the first coding sequence (TyrA-AT1), recombinant proteins were observed only with the constructs encoding the proteins M58-TyrA-Atc and M58-TyrA-AT1. The three recombinant proteins were mainly found in the protein bodies. However, the presence of small amounts of recombinant proteins in the soluble protein extracts of  E. coli  made it possible to characterize the biochemical properties.  
       EXAMPLE 6  
     Identification and Biochemical Characterization of the  Arabidopsis Thaliana  Arogenate Dehydrogenase Enzymes  
       [0072]    The biochemical characterization of the recombinant arogenate dehydrogenase enzymes was carried out using the soluble protein extracts of the transformed  E. coli  strains. The arogenate dehydrogenase activity was measured according to the method described in example 4. A strictly NADP-dependent arogenate dehydrogenase activity was demonstrated for each one of the three recombinant enzymes. No arogenate dehydrogenase activity was detected in the presence of NAD, and no prephenate dehydrogenase activity was detected whatever the cofactor used (NADP or NAD) and whatever the protein tested (TyrA-ATc, TyrA-AT1 or TyrA-AT2). In addition, prephenate at a concentration of 1 mM does not inhibit the arogenate dehydrogenase activity of the three recombinant enzymes. Each one of these enzymes has a Michaelis-Menten-type behavior, and their Km value for arogenate and NADP is relatively the same (FIGS. 2 and 3). The Michaelis constants for NADP are, respectively, 40 μM for TyrA-Atc, 60 μM for TyrA-AT1, and 20 μM for TyrA-AT2. The Michaelis constants for arogenate are, respectively, 70 μM for TyrA-Atc, 45 μM for TyrA-AT1, and 45 μM for TyrA-AT2. In addition, like the other plant arogenate dehydrogenases (Byng et al., 1981, Phytochemistry 6, 1289-1292; Connelly and Conn, 1986, Z. Naturforsch 41c, 69-78; Gaines et al., 1982 Planta 156, 233-240), the Arabidopsis arogenate dehydrogenases are all very sensitive to tyrosine, the product of the enzyme reaction, and insensitive to 1 mM of phenylalanine and 1 mM of p-hydroxyphenylpyruvate. The inhibition by tyrosine is competitive with respect to arogenate (Ki of 14 μM for TyrA-Atc, 8 μM for TyrA-AT1, and 12 μM for TyrA-AT2), and noncompetitive with respect to NADP.  
       EXAMPLE 7  
     Identification and Biochemical Characterization of the Syfnechocystis Arogenate Dehydrogenase Enzyme  
       [0073]    The sequence of the gene encoding the  A. thaliana  arogenate dehyrogenase identified in example 1 (TyrA) made it possible to identify an arogenate dehydrogenase gene in the bacterium Synechocystis (accession number: 1652956). This gene was originally described as encoding a “prephenate dehydrogenase” enzyme. It was isolated from a Synechocystis genomic library and the enzyme was produced in the same way as the  A. thaliana  enzyme, according to the protocol described in example 5. Biochemical characterization of the enzyme produced made it possible to demonstrate that it is an arogenate dehydrogenase enzyme and not a prephenate dehydrogenase enzyme. This biochemical characterization of the Synechocystis arogenate dehydrogenase enzyme was carried out using the purified soluble protein extracts of the transformed  E. coli  strains. The arogenate dehydrogenase activity was measured according to the method described in example 4. A strictly NADP-dependent arogenate dehydrogenase activity was demonstrated for this enzyme. No arogenate dehydrogenase activity was detected in the presence of NAD, and no prephenate dehydrogenase activity was detected whatever the cofactor used (NADP or NAD). In addition, prephenate at a concentration of 1 mM does not inhibit the arogenate dehydrogenase activity of this enzyme. The Synechocystis arogenate dehydrogenase has a Michaelis-Menten-type behavior (FIG. 4). The Michaelis constant is 6 μM for NADP, and 107 μM for arogenate.  
       EXAMPLE 8  
     Identification of Other Plant Arogenate Dehydrogenase Enzymes  
       [0074]    The sequence of the gene encoding the  A. thaliana  arogenate dehydrogenase identified in example 1 (TyrA) made it possible to identify another arogenate dehydrogenase gene in  A. thaliana . This new gene (accession number: AC0342561; SEQ ID NO: 8) was initially noted as “containing similarity with the embryo abundance protein (EMB20) of  Picea glauca ”. It also has a putative chloroplast transit peptide sequence, but no repeat region.  
         [0075]    The sequence of the TyrA gene also made it possible to identify two other cDNAs encoding arogenate dehydrogenase enzymes in the public EST (Expressed Sequence Tags) databases. One of these cDNAs, which is not complete, corresponds to a tomato cDNA (TC41067; SEQ ID NO: 22). The incomplete nature of this cDNA does not make it possible to determine whether it is duplicated like TyrA, since its 3′ end stops just after the codon corresponding to D356 of Tyr-AT1. The second cDNA corresponds to a complete cDNA of  Picea glauca  (accession number: L47749; SEQ ID NO: 10) and does not possess a repeat region. This  Picea glauca  cDNA was noted as being an “embryo abundance protein”.  
     
       
       
         1 
         
           
             30  
           
           
             1  
             2082  
             DNA  
             Arabidopsis thaliana  
             
               transit_peptide  
               (1)..(174)  
             
             
               Intron  
               (1089)..(1181)  
             
           
            1 

atgatctttc aatctcattc tcatcatctt cttctctatc aatcctcatc ttcctcctcc     60 

ttcttcttcc tcccaaagct catcaccaaa cctcctctct ccctctcatt tacctctctt    120 

tcctcaatgc tcccttctct ctctctctcc accgccaacc gccacctctc cgtcaccgac    180 

accatccctc ttcccaactc caactccaac gccacccctc ctctccgtat cgccatcatc    240 

ggattcggaa actacggcca attccttgcc gaaaccctaa tttctcaagg ccacattctc    300 

ttcgctcact cccgatccga tcactcctcc gccgctcgcc gtctcggtgt ctcatacttc    360 

accgatcttc acgatctctg cgaacgtcat cctgacgtag tccttctctg tacttcaatc    420 

ctctccatag agaatattct caaaacgttg ccgtttcaga gactccgtcg caacactctc    480 

ttcgttgatg ttctctccgt taaagagttt gctaaaactc ttctccttca atacttacct    540 

gaagatttcg atattctttg tacacatcca atgtttggtc ctcagagtgt gagttcaaat    600 

catggctgga gaggattaag atttgtgtat gataaagtta ggattgggga agagagattg    660 

agagtctcaa ggtgtgagag ttttcttgag atttttgtta gagaaggatg tgagatggtg    720 

gagatgagtg ttactgatca tgataagttt gctgctgaat cacagtttat aactcatact    780 

cttggtaggc ttttggggat gttgaagttg atatcgacgc cgattaatac gaaagggtac    840 

gaggcgttgc ttgatttagc tgagaatatt tgtggggata gttttgattt gtattatggg    900 

ttgtttgtgt ataataacaa ctctttggag gtgttagaga ggattgattt ggctttcgag    960 

gctttgcgta aggagctttt tagtcggctt cacggtgttg tgaggaagca gtcttttgaa   1020 

ggtgaagcaa agaaagttca tgtttttcca aattgtggtg aaaatgatgc ttctttggat   1080 

atgatgaggt atgtagttag ttagttagtt acattgtgtg gtttgatgca ttttggattt   1140 

ggtttcttat tgtaaatagt tatcgatttg tgatcttgca ggtcagaaga tgttgttgtg   1200 

aagtatgaat ataactccca ggtgtctggt agtgttaatg acggttcgag gctcaagatt   1260 

ggtatcgtcg ggtttggaaa ttttggacag tttctaggta aaaccatggt caagcagggt   1320 

cacactgtgt tagcttattc cagaagtgac tacactgatg aagcagcaaa gctcggtgtt   1380 

tcgtattttt cagatcttga tgatctattt gaagagcatc ctgaagttat tattctctgt   1440 

acgtcaatcc tttcgactga aaaagttctc gagtcactac cgtttcagag actgaagaga   1500 

agcacacttt ttgtggatgt actctcagta aaagagttcc cgaggaattt atttcttcaa   1560 

actctcccac aagattttga tattttgtgc acgcatccta tgtttgggcc agagagtggt   1620 

aaaaatggat ggaacaatct tgcctttgtg tttgataagg ttaggattgg aatggatgat   1680 

agaagaaaat cgaggtgtaa cagttttctt gatatttttg cccgtgaagg atgtcgtatg   1740 

gtggagatgt cgtgtgctga acatgattgg catgctgctg gatcacagtt tatcacacac   1800 

acagtgggaa ggcttctgga gaagctgagc ttggaatcta ctcctataga taccaaaggt   1860 

tatgagacat tgctaaaact ggtggagaat actgctggtg acagctttga tctgtactat   1920 

ggactatttt tatacaatcc taatgcaatg gaacagcttg agaggtttca tgtggctttt   1980 

gaatcattga agacacagct ctttggacga ctacattctc aacattctca tgagctagct   2040 

aaatcatctt ccccaaagac aactaagcta ttaactagct aa                      2082 

 
           
             2  
             1981  
             DNA  
             Arabidopsis thaliana  
             
               CDS  
               (1)..(1980)  
             
             
               transit_peptide  
               (1)..(174)  
             
           
            2 

atg atc ttt caa tct cat tct cat cat ctt ctt ctc tat caa tcc tca       48 
Met Ile Phe Gln Ser His Ser His His Leu Leu Leu Tyr Gln Ser Ser 
1               5                   10                  15 

tct tcc tcc tcc ttc ttc ttc ctc cca aag ctc atc acc aaa cct cct       96 
Ser Ser Ser Ser Phe Phe Phe Leu Pro Lys Leu Ile Thr Lys Pro Pro 
            20                  25                  30 

ctc tcc ctc tca ttt acc tct ctt tcc tca atg ctc cct tct ctc tct      144 
Leu Ser Leu Ser Phe Thr Ser Leu Ser Ser Met Leu Pro Ser Leu Ser 
        35                  40                  45 

ctc tcc acc gcc aac cgc cac ctc tcc gtc acc gac acc atc cct ctt      192 
Leu Ser Thr Ala Asn Arg His Leu Ser Val Thr Asp Thr Ile Pro Leu 
    50                  55                  60 

ccc aac tcc aac tcc aac gcc acc cct cct ctc cgt atc gcc atc atc      240 
Pro Asn Ser Asn Ser Asn Ala Thr Pro Pro Leu Arg Ile Ala Ile Ile 
65                  70                  75                  80 

gga ttc gga aac tac ggc caa ttc ctt gcc gaa acc cta att tct caa      288 
Gly Phe Gly Asn Tyr Gly Gln Phe Leu Ala Glu Thr Leu Ile Ser Gln 
                85                  90                  95 

ggc cac att ctc ttc gct cac tcc cga tcc gat cac tcc tcc gcc gct      336 
Gly His Ile Leu Phe Ala His Ser Arg Ser Asp His Ser Ser Ala Ala 
            100                 105                 110 

cgc cgt ctc ggt gtc tca tac ttc acc gat ctt cac gat ctc tgc gaa      384 
Arg Arg Leu Gly Val Ser Tyr Phe Thr Asp Leu His Asp Leu Cys Glu 
        115                 120                 125 

cgt cat cct gac gta gtc ctt ctc tgt act tca atc ctc tcc ata gag      432 
Arg His Pro Asp Val Val Leu Leu Cys Thr Ser Ile Leu Ser Ile Glu 
    130                 135                 140 

aat att ctc aaa acg ttg ccg ttt cag aga ctc cgt cgc aac act ctc      480 
Asn Ile Leu Lys Thr Leu Pro Phe Gln Arg Leu Arg Arg Asn Thr Leu 
145                 150                 155                 160 

ttc gtt gat gtt ctc tcc gtt aaa gag ttt gct aaa act ctt ctc ctt      528 
Phe Val Asp Val Leu Ser Val Lys Glu Phe Ala Lys Thr Leu Leu Leu 
                165                 170                 175 

caa tac tta cct gaa gat ttc gat att ctt tgt aca cat cca atg ttt      576 
Gln Tyr Leu Pro Glu Asp Phe Asp Ile Leu Cys Thr His Pro Met Phe 
            180                 185                 190 

ggt cct cag agt gtg agt tca aat cat ggc tgg aga gga tta aga ttt      624 
Gly Pro Gln Ser Val Ser Ser Asn His Gly Trp Arg Gly Leu Arg Phe 
        195                 200                 205 

gtg tat gat aaa gtt agg att ggg gaa gag aga ttg aga gtc tca agg      672 
Val Tyr Asp Lys Val Arg Ile Gly Glu Glu Arg Leu Arg Val Ser Arg 
    210                 215                 220 

tgt gag agt ttt ctt gag att ttt gtt aga gaa gga tgt gag atg gtg      720 
Cys Glu Ser Phe Leu Glu Ile Phe Val Arg Glu Gly Cys Glu Met Val 
225                 230                 235                 240 

gag atg agt gtt act gat cat gat aag ttt gct gct gaa tca cag ttt      768 
Glu Met Ser Val Thr Asp His Asp Lys Phe Ala Ala Glu Ser Gln Phe 
                245                 250                 255 

ata act cat act ctt ggt agg ctt ttg ggg atg ttg aag ttg ata tcg      816 
Ile Thr His Thr Leu Gly Arg Leu Leu Gly Met Leu Lys Leu Ile Ser 
            260                 265                 270 

acg ccg att aat acg aaa ggg tac gag gcg ttg ctt gat tta gct gag      864 
Thr Pro Ile Asn Thr Lys Gly Tyr Glu Ala Leu Leu Asp Leu Ala Glu 
        275                 280                 285 

aat att tgt ggg gat agt ttt gat ttg tat tat ggg ttg ttt gtg tat      912 
Asn Ile Cys Gly Asp Ser Phe Asp Leu Tyr Tyr Gly Leu Phe Val Tyr 
    290                 295                 300 

aat aac aac tct ttg gag gtg tta gag agg att gat ttg gct ttc gag      960 
Asn Asn Asn Ser Leu Glu Val Leu Glu Arg Ile Asp Leu Ala Phe Glu 
305                 310                 315                 320 

gct ttg cgt aag gag ctt ttt agt cgg ctt cac ggt gtt gtg agg aag     1008 
Ala Leu Arg Lys Glu Leu Phe Ser Arg Leu His Gly Val Val Arg Lys 
                325                 330                 335 

cag tct ttt gaa ggt gaa gca aag aaa gtt cat gtt ttt cca aat tgt     1056 
Gln Ser Phe Glu Gly Glu Ala Lys Lys Val His Val Phe Pro Asn Cys 
            340                 345                 350 

ggt gaa aat gat gct tct ttg gat atg atg agg tca gaa gat gtt gtt     1104 
Gly Glu Asn Asp Ala Ser Leu Asp Met Met Arg Ser Glu Asp Val Val 
        355                 360                 365 

gtg aag tat gaa tat aac tcc cag gtg tct ggt agt gtt aat gac ggt     1152 
Val Lys Tyr Glu Tyr Asn Ser Gln Val Ser Gly Ser Val Asn Asp Gly 
    370                 375                 380 

tcg agg ctc aag att ggt atc gtc ggg ttt gga aat ttt gga cag ttt     1200 
Ser Arg Leu Lys Ile Gly Ile Val Gly Phe Gly Asn Phe Gly Gln Phe 
385                 390                 395                 400 

cta ggt aaa acc atg gtc aag cag ggt cac act gtg tta gct tat tcc     1248 
Leu Gly Lys Thr Met Val Lys Gln Gly His Thr Val Leu Ala Tyr Ser 
                405                 410                 415 

aga agt gac tac act gat gaa gca gca aag ctc ggt gtt tcg tat ttt     1296 
Arg Ser Asp Tyr Thr Asp Glu Ala Ala Lys Leu Gly Val Ser Tyr Phe 
            420                 425                 430 

tca gat ctt gat gat cta ttt gaa gag cat cct gaa gtt att att ctc     1344 
Ser Asp Leu Asp Asp Leu Phe Glu Glu His Pro Glu Val Ile Ile Leu 
        435                 440                 445 

tgt acg tca atc ctt tcg act gaa aaa gtt ctc gag tca cta ccg ttt     1392 
Cys Thr Ser Ile Leu Ser Thr Glu Lys Val Leu Glu Ser Leu Pro Phe 
    450                 455                 460 

cag aga ctg aag aga agc aca ctt ttt gtg gat gta ctc tca gta aaa     1440 
Gln Arg Leu Lys Arg Ser Thr Leu Phe Val Asp Val Leu Ser Val Lys 
465                 470                 475                 480 

gag ttc ccg agg aat tta ttt ctt caa act ctc cca caa gat ttt gat     1488 
Glu Phe Pro Arg Asn Leu Phe Leu Gln Thr Leu Pro Gln Asp Phe Asp 
                485                 490                 495 

att ttg tgc acg cat cct atg ttt ggg cca gag agt ggt aaa aat gga     1536 
Ile Leu Cys Thr His Pro Met Phe Gly Pro Glu Ser Gly Lys Asn Gly 
            500                 505                 510 

tgg aac aat ctt gcc ttt gtg ttt gat aag gtt agg att gga atg gat     1584 
Trp Asn Asn Leu Ala Phe Val Phe Asp Lys Val Arg Ile Gly Met Asp 
        515                 520                 525 

gat aga aga aaa tcg agg tgt aac agt ttt ctt gat att ttt gcc cgt     1632 
Asp Arg Arg Lys Ser Arg Cys Asn Ser Phe Leu Asp Ile Phe Ala Arg 
    530                 535                 540 

gaa gga tgt cgt atg gtg gag atg tcg tgt gct gaa cat gat tgg cat     1680 
Glu Gly Cys Arg Met Val Glu Met Ser Cys Ala Glu His Asp Trp His 
545                 550                 555                 560 

gct gct gga tca cag ttt atc aca cac aca gtg gga agg ctt ctg gag     1728 
Ala Ala Gly Ser Gln Phe Ile Thr His Thr Val Gly Arg Leu Leu Glu 
                565                 570                 575 

aag ctg agc ttg gaa tct act cct ata gat acc aaa ggt tat gag aca     1776 
Lys Leu Ser Leu Glu Ser Thr Pro Ile Asp Thr Lys Gly Tyr Glu Thr 
            580                 585                 590 

ttg cta aaa ctg gtg gag aat act gct ggt gac agc ttt gat ctg tac     1824 
Leu Leu Lys Leu Val Glu Asn Thr Ala Gly Asp Ser Phe Asp Leu Tyr 
        595                 600                 605 

tat gga cta ttt tta tac aat cct aat gca atg gaa cag ctt gag agg     1872 
Tyr Gly Leu Phe Leu Tyr Asn Pro Asn Ala Met Glu Gln Leu Glu Arg 
    610                 615                 620 

ttt cat gtg gct ttt gaa tca ttg aag aca cag ctc ttt gga cga cta     1920 
Phe His Val Ala Phe Glu Ser Leu Lys Thr Gln Leu Phe Gly Arg Leu 
625                 630                 635                 640 

cat tct caa cat tct cat gag cta gct aaa tca tct tcc cca aag aca     1968 
His Ser Gln His Ser His Glu Leu Ala Lys Ser Ser Ser Pro Lys Thr 
                645                 650                 655 

act aag cta tta a                                                   1981 
Thr Lys Leu Leu 
            660 

 
           
             3  
             660  
             PRT  
             Arabidopsis thaliana  
           
            3 

Met Ile Phe Gln Ser His Ser His His Leu Leu Leu Tyr Gln Ser Ser 
1               5                   10                  15 

Ser Ser Ser Ser Phe Phe Phe Leu Pro Lys Leu Ile Thr Lys Pro Pro 
            20                  25                  30 

Leu Ser Leu Ser Phe Thr Ser Leu Ser Ser Met Leu Pro Ser Leu Ser 
        35                  40                  45 

Leu Ser Thr Ala Asn Arg His Leu Ser Val Thr Asp Thr Ile Pro Leu 
    50                  55                  60 

Pro Asn Ser Asn Ser Asn Ala Thr Pro Pro Leu Arg Ile Ala Ile Ile 
65                  70                  75                  80 

Gly Phe Gly Asn Tyr Gly Gln Phe Leu Ala Glu Thr Leu Ile Ser Gln 
                85                  90                  95 

Gly His Ile Leu Phe Ala His Ser Arg Ser Asp His Ser Ser Ala Ala 
            100                 105                 110 

Arg Arg Leu Gly Val Ser Tyr Phe Thr Asp Leu His Asp Leu Cys Glu 
        115                 120                 125 

Arg His Pro Asp Val Val Leu Leu Cys Thr Ser Ile Leu Ser Ile Glu 
    130                 135                 140 

Asn Ile Leu Lys Thr Leu Pro Phe Gln Arg Leu Arg Arg Asn Thr Leu 
145                 150                 155                 160 

Phe Val Asp Val Leu Ser Val Lys Glu Phe Ala Lys Thr Leu Leu Leu 
                165                 170                 175 

Gln Tyr Leu Pro Glu Asp Phe Asp Ile Leu Cys Thr His Pro Met Phe 
            180                 185                 190 

Gly Pro Gln Ser Val Ser Ser Asn His Gly Trp Arg Gly Leu Arg Phe 
        195                 200                 205 

Val Tyr Asp Lys Val Arg Ile Gly Glu Glu Arg Leu Arg Val Ser Arg 
    210                 215                 220 

Cys Glu Ser Phe Leu Glu Ile Phe Val Arg Glu Gly Cys Glu Met Val 
225                 230                 235                 240 

Glu Met Ser Val Thr Asp His Asp Lys Phe Ala Ala Glu Ser Gln Phe 
                245                 250                 255 

Ile Thr His Thr Leu Gly Arg Leu Leu Gly Met Leu Lys Leu Ile Ser 
            260                 265                 270 

Thr Pro Ile Asn Thr Lys Gly Tyr Glu Ala Leu Leu Asp Leu Ala Glu 
        275                 280                 285 

Asn Ile Cys Gly Asp Ser Phe Asp Leu Tyr Tyr Gly Leu Phe Val Tyr 
    290                 295                 300 

Asn Asn Asn Ser Leu Glu Val Leu Glu Arg Ile Asp Leu Ala Phe Glu 
305                 310                 315                 320 

Ala Leu Arg Lys Glu Leu Phe Ser Arg Leu His Gly Val Val Arg Lys 
                325                 330                 335 

Gln Ser Phe Glu Gly Glu Ala Lys Lys Val His Val Phe Pro Asn Cys 
            340                 345                 350 

Gly Glu Asn Asp Ala Ser Leu Asp Met Met Arg Ser Glu Asp Val Val 
        355                 360                 365 

Val Lys Tyr Glu Tyr Asn Ser Gln Val Ser Gly Ser Val Asn Asp Gly 
    370                 375                 380 

Ser Arg Leu Lys Ile Gly Ile Val Gly Phe Gly Asn Phe Gly Gln Phe 
385                 390                 395                 400 

Leu Gly Lys Thr Met Val Lys Gln Gly His Thr Val Leu Ala Tyr Ser 
                405                 410                 415 

Arg Ser Asp Tyr Thr Asp Glu Ala Ala Lys Leu Gly Val Ser Tyr Phe 
            420                 425                 430 

Ser Asp Leu Asp Asp Leu Phe Glu Glu His Pro Glu Val Ile Ile Leu 
        435                 440                 445 

Cys Thr Ser Ile Leu Ser Thr Glu Lys Val Leu Glu Ser Leu Pro Phe 
    450                 455                 460 

Gln Arg Leu Lys Arg Ser Thr Leu Phe Val Asp Val Leu Ser Val Lys 
465                 470                 475                 480 

Glu Phe Pro Arg Asn Leu Phe Leu Gln Thr Leu Pro Gln Asp Phe Asp 
                485                 490                 495 

Ile Leu Cys Thr His Pro Met Phe Gly Pro Glu Ser Gly Lys Asn Gly 
            500                 505                 510 

Trp Asn Asn Leu Ala Phe Val Phe Asp Lys Val Arg Ile Gly Met Asp 
        515                 520                 525 

Asp Arg Arg Lys Ser Arg Cys Asn Ser Phe Leu Asp Ile Phe Ala Arg 
    530                 535                 540 

Glu Gly Cys Arg Met Val Glu Met Ser Cys Ala Glu His Asp Trp His 
545                 550                 555                 560 

Ala Ala Gly Ser Gln Phe Ile Thr His Thr Val Gly Arg Leu Leu Glu 
                565                 570                 575 

Lys Leu Ser Leu Glu Ser Thr Pro Ile Asp Thr Lys Gly Tyr Glu Thr 
            580                 585                 590 

Leu Leu Lys Leu Val Glu Asn Thr Ala Gly Asp Ser Phe Asp Leu Tyr 
        595                 600                 605 

Tyr Gly Leu Phe Leu Tyr Asn Pro Asn Ala Met Glu Gln Leu Glu Arg 
    610                 615                 620 

Phe His Val Ala Phe Glu Ser Leu Lys Thr Gln Leu Phe Gly Arg Leu 
625                 630                 635                 640 

His Ser Gln His Ser His Glu Leu Ala Lys Ser Ser Ser Pro Lys Thr 
                645                 650                 655 

Thr Lys Leu Leu 
            660 

 
           
             4  
             933  
             DNA  
             Arabidopsis thaliana  
             
               CDS  
               (1)..(933)  
             
           
            4 

atg acc gac acc atc cct ctt ccc aac tcc aac tcc aac gcc acc cct       48 
Met Thr Asp Thr Ile Pro Leu Pro Asn Ser Asn Ser Asn Ala Thr Pro 
1               5                   10                  15 

cct ctc cgt atc gcc atc atc gga ttc gga aac tac ggc caa ttc ctt       96 
Pro Leu Arg Ile Ala Ile Ile Gly Phe Gly Asn Tyr Gly Gln Phe Leu 
            20                  25                  30 

gcc gaa acc cta att tct caa ggc cac att ctc ttc gct cac tcc cga      144 
Ala Glu Thr Leu Ile Ser Gln Gly His Ile Leu Phe Ala His Ser Arg 
        35                  40                  45 

tcc gat cac tcc tcc gcc gct cgc cgt ctc ggt gtc tca tac ttc acc      192 
Ser Asp His Ser Ser Ala Ala Arg Arg Leu Gly Val Ser Tyr Phe Thr 
    50                  55                  60 

gat ctt cac gat ctc tgc gaa cgt cat cct gac gta gtc ctt ctc tgt      240 
Asp Leu His Asp Leu Cys Glu Arg His Pro Asp Val Val Leu Leu Cys 
65                  70                  75                  80 

act tca atc ctc tcc ata gag aat att ctc aaa acg ttg ccg ttt cag      288 
Thr Ser Ile Leu Ser Ile Glu Asn Ile Leu Lys Thr Leu Pro Phe Gln 
                85                  90                  95 

aga ctc cgt cgc aac act ctc ttc gtt gat gtt ctc tcc gtt aaa gag      336 
Arg Leu Arg Arg Asn Thr Leu Phe Val Asp Val Leu Ser Val Lys Glu 
            100                 105                 110 

ttt gct aaa act ctt ctc ctt caa tac tta cct gaa gat ttc gat att      384 
Phe Ala Lys Thr Leu Leu Leu Gln Tyr Leu Pro Glu Asp Phe Asp Ile 
        115                 120                 125 

ctt tgt aca cat cca atg ttt ggt cct cag agt gtg agt tca aat cat      432 
Leu Cys Thr His Pro Met Phe Gly Pro Gln Ser Val Ser Ser Asn His 
    130                 135                 140 

ggc tgg aga gga tta aga ttt gtg tat gat aaa gtt agg att ggg gaa      480 
Gly Trp Arg Gly Leu Arg Phe Val Tyr Asp Lys Val Arg Ile Gly Glu 
145                 150                 155                 160 

gag aga ttg aga gtc tca agg tgt gag agt ttt ctt gag att ttt gtt      528 
Glu Arg Leu Arg Val Ser Arg Cys Glu Ser Phe Leu Glu Ile Phe Val 
                165                 170                 175 

aga gaa gga tgt gag atg gtg gag atg agt gtt act gat cat gat aag      576 
Arg Glu Gly Cys Glu Met Val Glu Met Ser Val Thr Asp His Asp Lys 
            180                 185                 190 

ttt gct gct gaa tca cag ttt ata act cat act ctt ggt agg ctt ttg      624 
Phe Ala Ala Glu Ser Gln Phe Ile Thr His Thr Leu Gly Arg Leu Leu 
        195                 200                 205 

ggg atg ttg aag ttg ata tcg acg ccg att aat acg aaa ggg tac gag      672 
Gly Met Leu Lys Leu Ile Ser Thr Pro Ile Asn Thr Lys Gly Tyr Glu 
    210                 215                 220 

gcg ttg ctt gat tta gct gag aat att tgt ggg gat agt ttt gat ttg      720 
Ala Leu Leu Asp Leu Ala Glu Asn Ile Cys Gly Asp Ser Phe Asp Leu 
225                 230                 235                 240 

tat tat ggg ttg ttt gtg tat aat aac aac tct ttg gag gtg tta gag      768 
Tyr Tyr Gly Leu Phe Val Tyr Asn Asn Asn Ser Leu Glu Val Leu Glu 
                245                 250                 255 

agg att gat ttg gct ttc gag gct ttg cgt aag gag ctt ttt agt cgg      816 
Arg Ile Asp Leu Ala Phe Glu Ala Leu Arg Lys Glu Leu Phe Ser Arg 
            260                 265                 270 

ctt cac ggt gtt gtg agg aag cag tct ttt gaa ggt gaa gca aag aaa      864 
Leu His Gly Val Val Arg Lys Gln Ser Phe Glu Gly Glu Ala Lys Lys 
        275                 280                 285 

gtt cat gtt ttt cca aat tgt ggt gaa aat gat gct tct ttg gat atg      912 
Val His Val Phe Pro Asn Cys Gly Glu Asn Asp Ala Ser Leu Asp Met 
    290                 295                 300 

atg agg tat gta gtt agt tag                                          933 
Met Arg Tyr Val Val Ser 
305                 310 

 
           
             5  
             310  
             PRT  
             Arabidopsis thaliana  
           
            5 

Met Thr Asp Thr Ile Pro Leu Pro Asn Ser Asn Ser Asn Ala Thr Pro 
1               5                   10                  15 

Pro Leu Arg Ile Ala Ile Ile Gly Phe Gly Asn Tyr Gly Gln Phe Leu 
            20                  25                  30 

Ala Glu Thr Leu Ile Ser Gln Gly His Ile Leu Phe Ala His Ser Arg 
        35                  40                  45 

Ser Asp His Ser Ser Ala Ala Arg Arg Leu Gly Val Ser Tyr Phe Thr 
    50                  55                  60 

Asp Leu His Asp Leu Cys Glu Arg His Pro Asp Val Val Leu Leu Cys 
65                  70                  75                  80 

Thr Ser Ile Leu Ser Ile Glu Asn Ile Leu Lys Thr Leu Pro Phe Gln 
                85                  90                  95 

Arg Leu Arg Arg Asn Thr Leu Phe Val Asp Val Leu Ser Val Lys Glu 
            100                 105                 110 

Phe Ala Lys Thr Leu Leu Leu Gln Tyr Leu Pro Glu Asp Phe Asp Ile 
        115                 120                 125 

Leu Cys Thr His Pro Met Phe Gly Pro Gln Ser Val Ser Ser Asn His 
    130                 135                 140 

Gly Trp Arg Gly Leu Arg Phe Val Tyr Asp Lys Val Arg Ile Gly Glu 
145                 150                 155                 160 

Glu Arg Leu Arg Val Ser Arg Cys Glu Ser Phe Leu Glu Ile Phe Val 
                165                 170                 175 

Arg Glu Gly Cys Glu Met Val Glu Met Ser Val Thr Asp His Asp Lys 
            180                 185                 190 

Phe Ala Ala Glu Ser Gln Phe Ile Thr His Thr Leu Gly Arg Leu Leu 
        195                 200                 205 

Gly Met Leu Lys Leu Ile Ser Thr Pro Ile Asn Thr Lys Gly Tyr Glu 
    210                 215                 220 

Ala Leu Leu Asp Leu Ala Glu Asn Ile Cys Gly Asp Ser Phe Asp Leu 
225                 230                 235                 240 

Tyr Tyr Gly Leu Phe Val Tyr Asn Asn Asn Ser Leu Glu Val Leu Glu 
                245                 250                 255 

Arg Ile Asp Leu Ala Phe Glu Ala Leu Arg Lys Glu Leu Phe Ser Arg 
            260                 265                 270 

Leu His Gly Val Val Arg Lys Gln Ser Phe Glu Gly Glu Ala Lys Lys 
        275                 280                 285 

Val His Val Phe Pro Asn Cys Gly Glu Asn Asp Ala Ser Leu Asp Met 
    290                 295                 300 

Met Arg Tyr Val Val Ser 
305                 310 

 
           
             6  
             909  
             DNA  
             Arabidopsis thaliana  
             
               CDS  
               (1)..(909)  
             
           
            6 

atg atg agg tca gaa gat gtt gtt gtg aag tat gaa tat aac tcc cag       48 
Met Met Arg Ser Glu Asp Val Val Val Lys Tyr Glu Tyr Asn Ser Gln 
1               5                   10                  15 

gtg tct ggt agt gtt aat gac ggt tcg agg ctc aag att ggt atc gtc       96 
Val Ser Gly Ser Val Asn Asp Gly Ser Arg Leu Lys Ile Gly Ile Val 
            20                  25                  30 

ggg ttt gga aat ttt gga cag ttt cta ggt aaa acc atg gtc aag cag      144 
Gly Phe Gly Asn Phe Gly Gln Phe Leu Gly Lys Thr Met Val Lys Gln 
        35                  40                  45 

ggt cac act gtg tta gct tat tcc aga agt gac tac act gat gaa gca      192 
Gly His Thr Val Leu Ala Tyr Ser Arg Ser Asp Tyr Thr Asp Glu Ala 
    50                  55                  60 

gca aag ctc ggt gtt tcg tat ttt tca gat ctt gat gat cta ttt gaa      240 
Ala Lys Leu Gly Val Ser Tyr Phe Ser Asp Leu Asp Asp Leu Phe Glu 
65                  70                  75                  80 

gag cat cct gaa gtt att att ctc tgt acg tca atc ctt tcg act gaa      288 
Glu His Pro Glu Val Ile Ile Leu Cys Thr Ser Ile Leu Ser Thr Glu 
                85                  90                  95 

aaa gtt ctc gag tca cta ccg ttt cag aga ctg aag aga agc aca ctt      336 
Lys Val Leu Glu Ser Leu Pro Phe Gln Arg Leu Lys Arg Ser Thr Leu 
            100                 105                 110 

ttt gtg gat gta ctc tca gta aaa gag ttc ccg agg aat tta ttt ctt      384 
Phe Val Asp Val Leu Ser Val Lys Glu Phe Pro Arg Asn Leu Phe Leu 
        115                 120                 125 

caa act ctc cca caa gat ttt gat att ttg tgc acg cat cct atg ttt      432 
Gln Thr Leu Pro Gln Asp Phe Asp Ile Leu Cys Thr His Pro Met Phe 
    130                 135                 140 

ggg cca gag agt ggt aaa aat gga tgg aac aat ctt gcc ttt gtg ttt      480 
Gly Pro Glu Ser Gly Lys Asn Gly Trp Asn Asn Leu Ala Phe Val Phe 
145                 150                 155                 160 

gat aag gtt agg att gga atg gat gat aga aga aaa tcg agg tgt aac      528 
Asp Lys Val Arg Ile Gly Met Asp Asp Arg Arg Lys Ser Arg Cys Asn 
                165                 170                 175 

agt ttt ctt gat att ttt gcc cgt gaa gga tgt cgt atg gtg gag atg      576 
Ser Phe Leu Asp Ile Phe Ala Arg Glu Gly Cys Arg Met Val Glu Met 
            180                 185                 190 

tcg tgt gct gaa cat gat tgg cat gct gct gga tca cag ttt atc aca      624 
Ser Cys Ala Glu His Asp Trp His Ala Ala Gly Ser Gln Phe Ile Thr 
        195                 200                 205 

cac aca gtg gga agg ctt ctg gag aag ctg agc ttg gaa tct act cct      672 
His Thr Val Gly Arg Leu Leu Glu Lys Leu Ser Leu Glu Ser Thr Pro 
    210                 215                 220 

ata gat acc aaa ggt tat gag aca ttg cta aaa ctg gtg gag aat act      720 
Ile Asp Thr Lys Gly Tyr Glu Thr Leu Leu Lys Leu Val Glu Asn Thr 
225                 230                 235                 240 

gct ggt gac agc ttt gat ctg tac tat gga cta ttt tta tac aat cct      768 
Ala Gly Asp Ser Phe Asp Leu Tyr Tyr Gly Leu Phe Leu Tyr Asn Pro 
                245                 250                 255 

aat gca atg gaa cag ctt gag agg ttt cat gtg gct ttt gaa tca ttg      816 
Asn Ala Met Glu Gln Leu Glu Arg Phe His Val Ala Phe Glu Ser Leu 
            260                 265                 270 

aag aca cag ctc ttt gga cga cta cat tct caa cat tct cat gag cta      864 
Lys Thr Gln Leu Phe Gly Arg Leu His Ser Gln His Ser His Glu Leu 
        275                 280                 285 

gct aaa tca tct tcc cca aag aca act aag cta tta act agc taa          909 
Ala Lys Ser Ser Ser Pro Lys Thr Thr Lys Leu Leu Thr Ser 
    290                 295                 300 

 
           
             7  
             302  
             PRT  
             Arabidopsis thaliana  
           
            7 

Met Met Arg Ser Glu Asp Val Val Val Lys Tyr Glu Tyr Asn Ser Gln 
1               5                   10                  15 

Val Ser Gly Ser Val Asn Asp Gly Ser Arg Leu Lys Ile Gly Ile Val 
            20                  25                  30 

Gly Phe Gly Asn Phe Gly Gln Phe Leu Gly Lys Thr Met Val Lys Gln 
        35                  40                  45 

Gly His Thr Val Leu Ala Tyr Ser Arg Ser Asp Tyr Thr Asp Glu Ala 
    50                  55                  60 

Ala Lys Leu Gly Val Ser Tyr Phe Ser Asp Leu Asp Asp Leu Phe Glu 
65                  70                  75                  80 

Glu His Pro Glu Val Ile Ile Leu Cys Thr Ser Ile Leu Ser Thr Glu 
                85                  90                  95 

Lys Val Leu Glu Ser Leu Pro Phe Gln Arg Leu Lys Arg Ser Thr Leu 
            100                 105                 110 

Phe Val Asp Val Leu Ser Val Lys Glu Phe Pro Arg Asn Leu Phe Leu 
        115                 120                 125 

Gln Thr Leu Pro Gln Asp Phe Asp Ile Leu Cys Thr His Pro Met Phe 
    130                 135                 140 

Gly Pro Glu Ser Gly Lys Asn Gly Trp Asn Asn Leu Ala Phe Val Phe 
145                 150                 155                 160 

Asp Lys Val Arg Ile Gly Met Asp Asp Arg Arg Lys Ser Arg Cys Asn 
                165                 170                 175 

Ser Phe Leu Asp Ile Phe Ala Arg Glu Gly Cys Arg Met Val Glu Met 
            180                 185                 190 

Ser Cys Ala Glu His Asp Trp His Ala Ala Gly Ser Gln Phe Ile Thr 
        195                 200                 205 

His Thr Val Gly Arg Leu Leu Glu Lys Leu Ser Leu Glu Ser Thr Pro 
    210                 215                 220 

Ile Asp Thr Lys Gly Tyr Glu Thr Leu Leu Lys Leu Val Glu Asn Thr 
225                 230                 235                 240 

Ala Gly Asp Ser Phe Asp Leu Tyr Tyr Gly Leu Phe Leu Tyr Asn Pro 
                245                 250                 255 

Asn Ala Met Glu Gln Leu Glu Arg Phe His Val Ala Phe Glu Ser Leu 
            260                 265                 270 

Lys Thr Gln Leu Phe Gly Arg Leu His Ser Gln His Ser His Glu Leu 
        275                 280                 285 

Ala Lys Ser Ser Ser Pro Lys Thr Thr Lys Leu Leu Thr Ser 
    290                 295                 300 

 
           
             8  
             1077  
             DNA  
             Arabidopsis thaliana  
             
               CDS  
               (1)..(1077)  
             
           
            8 

atg cta ctc cat ttc tct ccg gcg aaa ccc ctc att tct cca ccc aat       48 
Met Leu Leu His Phe Ser Pro Ala Lys Pro Leu Ile Ser Pro Pro Asn 
1               5                   10                  15 

ctc cgc cgc aat tca ccc aca ttc ctc att tcc ccg ccg cga tct ctt       96 
Leu Arg Arg Asn Ser Pro Thr Phe Leu Ile Ser Pro Pro Arg Ser Leu 
            20                  25                  30 

cga att cga gca atc gac gcc gcc caa atc ttc gat tac gaa acc caa      144 
Arg Ile Arg Ala Ile Asp Ala Ala Gln Ile Phe Asp Tyr Glu Thr Gln 
        35                  40                  45 

ctc aaa tcc gag tac cgc aaa tcc tct gct ctc aaa atc gcc gtc ttg      192 
Leu Lys Ser Glu Tyr Arg Lys Ser Ser Ala Leu Lys Ile Ala Val Leu 
    50                  55                  60 

ggt ttc ggc aat ttc ggc caa ttc ctc tcc aaa acc cta att cga cac      240 
Gly Phe Gly Asn Phe Gly Gln Phe Leu Ser Lys Thr Leu Ile Arg His 
65                  70                  75                  80 

ggc cac gat cta atc act cac tcc cgc tcc gat tac tcc gac gcc gca      288 
Gly His Asp Leu Ile Thr His Ser Arg Ser Asp Tyr Ser Asp Ala Ala 
                85                  90                  95 

aac tca atc gga gct cgt ttc ttc gat aac cct cac gat ctc tgt gaa      336 
Asn Ser Ile Gly Ala Arg Phe Phe Asp Asn Pro His Asp Leu Cys Glu 
            100                 105                 110 

caa cat ccc gac gtt gtc ctc ctc tgt acc tca atc ctc tcc aca gaa      384 
Gln His Pro Asp Val Val Leu Leu Cys Thr Ser Ile Leu Ser Thr Glu 
        115                 120                 125 

tca gtc ctc aga tca ttc cct ttc caa cgt ctc cgt cgt agc aca ctc      432 
Ser Val Leu Arg Ser Phe Pro Phe Gln Arg Leu Arg Arg Ser Thr Leu 
    130                 135                 140 

ttc gtc gat gtt ctc tcc gtt aag gaa ttc cca aaa gcc ctc ttc att      480 
Phe Val Asp Val Leu Ser Val Lys Glu Phe Pro Lys Ala Leu Phe Ile 
145                 150                 155                 160 

aaa tac ctt cct aag gag ttt gac att ctc tgt act cat cca atg ttt      528 
Lys Tyr Leu Pro Lys Glu Phe Asp Ile Leu Cys Thr His Pro Met Phe 
                165                 170                 175 

gga cct gag agt ggt aag cat tct tgg tct ggc ttg ccc ttt gtc tac      576 
Gly Pro Glu Ser Gly Lys His Ser Trp Ser Gly Leu Pro Phe Val Tyr 
            180                 185                 190 

gat aag gtg aga atc gga gac gca gct tca aga caa gag agg tgt gag      624 
Asp Lys Val Arg Ile Gly Asp Ala Ala Ser Arg Gln Glu Arg Cys Glu 
        195                 200                 205 

aag ttt cta aga att ttt gag aat gaa ggt tgc aag atg gtt gaa atg      672 
Lys Phe Leu Arg Ile Phe Glu Asn Glu Gly Cys Lys Met Val Glu Met 
    210                 215                 220 

agc tgt gag aag cat gat tat tac gca gct gga tcg caa ttc gtg acg      720 
Ser Cys Glu Lys His Asp Tyr Tyr Ala Ala Gly Ser Gln Phe Val Thr 
225                 230                 235                 240 

cat act atg gga agg gtt ttg gag aaa tat gga gtt gag tct tcg ccg      768 
His Thr Met Gly Arg Val Leu Glu Lys Tyr Gly Val Glu Ser Ser Pro 
                245                 250                 255 

att aac acc aaa ggt tat gag acg ttg ttg gat ttg gtg gag aac aca      816 
Ile Asn Thr Lys Gly Tyr Glu Thr Leu Leu Asp Leu Val Glu Asn Thr 
            260                 265                 270 

tcg agt gat agc ttt gag ctt ttc tac ggt ttg ttt atg tat aat ccg      864 
Ser Ser Asp Ser Phe Glu Leu Phe Tyr Gly Leu Phe Met Tyr Asn Pro 
        275                 280                 285 

aat gct ctt gaa cag ttg gag aga ttg gat atg gct ttt gag tct gtt      912 
Asn Ala Leu Glu Gln Leu Glu Arg Leu Asp Met Ala Phe Glu Ser Val 
    290                 295                 300 

aag aag gag ctg ttt ggg aga tta cat cag caa tac agg aag caa atg      960 
Lys Lys Glu Leu Phe Gly Arg Leu His Gln Gln Tyr Arg Lys Gln Met 
305                 310                 315                 320 

ttt ggt ggg gag gtt caa tcg ccc aag aaa act gag cag aaa ttg ctc     1008 
Phe Gly Gly Glu Val Gln Ser Pro Lys Lys Thr Glu Gln Lys Leu Leu 
                325                 330                 335 

aat gat ggt ggt gtt gtt cct atg aat gat ata tca tca tca tca tca     1056 
Asn Asp Gly Gly Val Val Pro Met Asn Asp Ile Ser Ser Ser Ser Ser 
            340                 345                 350 

tca tca tca tca tca tct taa                                         1077 
Ser Ser Ser Ser Ser Ser 
        355 

 
           
             9  
             358  
             PRT  
             Arabidopsis thaliana  
           
            9 

Met Leu Leu His Phe Ser Pro Ala Lys Pro Leu Ile Ser Pro Pro Asn 
1               5                   10                  15 

Leu Arg Arg Asn Ser Pro Thr Phe Leu Ile Ser Pro Pro Arg Ser Leu 
            20                  25                  30 

Arg Ile Arg Ala Ile Asp Ala Ala Gln Ile Phe Asp Tyr Glu Thr Gln 
        35                  40                  45 

Leu Lys Ser Glu Tyr Arg Lys Ser Ser Ala Leu Lys Ile Ala Val Leu 
    50                  55                  60 

Gly Phe Gly Asn Phe Gly Gln Phe Leu Ser Lys Thr Leu Ile Arg His 
65                  70                  75                  80 

Gly His Asp Leu Ile Thr His Ser Arg Ser Asp Tyr Ser Asp Ala Ala 
                85                  90                  95 

Asn Ser Ile Gly Ala Arg Phe Phe Asp Asn Pro His Asp Leu Cys Glu 
            100                 105                 110 

Gln His Pro Asp Val Val Leu Leu Cys Thr Ser Ile Leu Ser Thr Glu 
        115                 120                 125 

Ser Val Leu Arg Ser Phe Pro Phe Gln Arg Leu Arg Arg Ser Thr Leu 
    130                 135                 140 

Phe Val Asp Val Leu Ser Val Lys Glu Phe Pro Lys Ala Leu Phe Ile 
145                 150                 155                 160 

Lys Tyr Leu Pro Lys Glu Phe Asp Ile Leu Cys Thr His Pro Met Phe 
                165                 170                 175 

Gly Pro Glu Ser Gly Lys His Ser Trp Ser Gly Leu Pro Phe Val Tyr 
            180                 185                 190 

Asp Lys Val Arg Ile Gly Asp Ala Ala Ser Arg Gln Glu Arg Cys Glu 
        195                 200                 205 

Lys Phe Leu Arg Ile Phe Glu Asn Glu Gly Cys Lys Met Val Glu Met 
    210                 215                 220 

Ser Cys Glu Lys His Asp Tyr Tyr Ala Ala Gly Ser Gln Phe Val Thr 
225                 230                 235                 240 

His Thr Met Gly Arg Val Leu Glu Lys Tyr Gly Val Glu Ser Ser Pro 
                245                 250                 255 

Ile Asn Thr Lys Gly Tyr Glu Thr Leu Leu Asp Leu Val Glu Asn Thr 
            260                 265                 270 

Ser Ser Asp Ser Phe Glu Leu Phe Tyr Gly Leu Phe Met Tyr Asn Pro 
        275                 280                 285 

Asn Ala Leu Glu Gln Leu Glu Arg Leu Asp Met Ala Phe Glu Ser Val 
    290                 295                 300 

Lys Lys Glu Leu Phe Gly Arg Leu His Gln Gln Tyr Arg Lys Gln Met 
305                 310                 315                 320 

Phe Gly Gly Glu Val Gln Ser Pro Lys Lys Thr Glu Gln Lys Leu Leu 
                325                 330                 335 

Asn Asp Gly Gly Val Val Pro Met Asn Asp Ile Ser Ser Ser Ser Ser 
            340                 345                 350 

Ser Ser Ser Ser Ser Ser 
        355 

 
           
             10  
             1476  
             DNA  
             Picea glauca  
             
               CDS  
               (96)..(980)  
             
           
            10 

accagtttta gatattcatc aaggtcttgc ctgctttgtt ttaggcaatt ccctccagta     60 

ccaagccctc ttctcagaaa actccctccg cggca atg cct ctt cat ttc tca       113 
                                       Met Pro Leu His Phe Ser 
                                       1               5 

tgg aat cca aca gaa gac cct cac aca gta cgc cct act gag gct ctc      161 
Trp Asn Pro Thr Glu Asp Pro His Thr Val Arg Pro Thr Glu Ala Leu 
            10                  15                  20 

agg aat cag agc aat gga cgt cgc ggg gcc cct cga tta aga aga ata      209 
Arg Asn Gln Ser Asn Gly Arg Arg Gly Ala Pro Arg Leu Arg Arg Ile 
        25                  30                  35 

aaa tcc att aaa tat tgg cat cgt agg gtt tgg aaa cta cca cca att      257 
Lys Ser Ile Lys Tyr Trp His Arg Arg Val Trp Lys Leu Pro Pro Ile 
    40                  45                  50 

tct ggt gaa aac cat ggt gaa gcc ggg cca ccc ggt gct cgc cca ttc      305 
Ser Gly Glu Asn His Gly Glu Ala Gly Pro Pro Gly Ala Arg Pro Phe 
55                  60                  65                  70 

cag gac gga cta tac gga ggc cac tgc gag atc ggg gtt caa ttc ttc      353 
Gln Asp Gly Leu Tyr Gly Gly His Cys Glu Ile Gly Val Gln Phe Phe 
                75                  80                  85 

aga gac gcg gac gat ttc tgc gaa gag cat cca gag atc ata ctg atg      401 
Arg Asp Ala Asp Asp Phe Cys Glu Glu His Pro Glu Ile Ile Leu Met 
            90                  95                  100 

tgc gca tcc atc act ttg gtg gga gga cgt gct gaa gtc tct gcc aac      449 
Cys Ala Ser Ile Thr Leu Val Gly Gly Arg Ala Glu Val Ser Ala Asn 
        105                 110                 115 

aca gcg cct gaa gag gag tac gct ttt cgc aga cgt cct gtc tgt gaa      497 
Thr Ala Pro Glu Glu Glu Tyr Ala Phe Arg Arg Arg Pro Val Cys Glu 
    120                 125                 130 

aga gtt tcc gca ccg gtt gtt cct gca ggt ttt gtc gcc cga gtc gat      545 
Arg Val Ser Ala Pro Val Val Pro Ala Gly Phe Val Ala Arg Val Asp 
135                 140                 145                 150 

gtg ctg tgc act cat ccc atg ttt ggt cca gag agc agc aag gac gat      593 
Val Leu Cys Thr His Pro Met Phe Gly Pro Glu Ser Ser Lys Asp Asp 
                155                 160                 165 

ttg ggc gac ctc cct ttc gtt tac gat aag gtt agg gtt tct aac gaa      641 
Leu Gly Asp Leu Pro Phe Val Tyr Asp Lys Val Arg Val Ser Asn Glu 
            170                 175                 180 

ggt ttg aga gcc aag cac tgc gag cgt ttt ctc aac ata ttt tcg tgc      689 
Gly Leu Arg Ala Lys His Cys Glu Arg Phe Leu Asn Ile Phe Ser Cys 
        185                 190                 195 

gag ggc tgc cgg atg gtc gag atg tcg tgt gca gaa cat gat cgc tat      737 
Glu Gly Cys Arg Met Val Glu Met Ser Cys Ala Glu His Asp Arg Tyr 
    200                 205                 210 

gtc gcg gag agc caa ttc att acc cac acc gtt ggg agg atg ttg ggg      785 
Val Ala Glu Ser Gln Phe Ile Thr His Thr Val Gly Arg Met Leu Gly 
215                 220                 225                 230 

agg ctg ggc ttg gag tcc act ccg att gct acc aag ggt tat gag aaa      833 
Arg Leu Gly Leu Glu Ser Thr Pro Ile Ala Thr Lys Gly Tyr Glu Lys 
                235                 240                 245 

tta ctg gaa gtg gcc tgg aat att gcc ggg gat agt ttt gat att tat      881 
Leu Leu Glu Val Ala Trp Asn Ile Ala Gly Asp Ser Phe Asp Ile Tyr 
            250                 255                 260 

tat gga ctc ttc atg tat aat gtc aat tcg att gaa caa atc gag agg      929 
Tyr Gly Leu Phe Met Tyr Asn Val Asn Ser Ile Glu Gln Ile Glu Arg 
        265                 270                 275 
tta gat atg gcg ttc aat tca ctc aag aac gag gtt tcg ggt tca aat      977 
Leu Asp Met Ala Phe Asn Ser Leu Lys Asn Glu Val Ser Gly Ser Asn 
    280                 285                 290 

taa gaattttaaa ggtttcgatt tgcttgaagc ggcttgtgta tgaagtacca          1030 

tttgtagaca ataatgaatt cgagaatgtt gttcaagatg aaatggttaa gaaggatggg   1090 

tctcgtgtga gaagaaaacc aagataaatg gttgcgtagt ggtccagaaa tctgcattca   1150 

ttactgaatg attctacatg gagtgagtaa gcattgattg aattccaaga cgagtgaaag   1210 

agtttgatga atggaatatg tctgtattcc aaatttaata aatgaaaaat attgcaggtt   1270 

gctatatgca atggttcttc tatatccccg aaggacaaat gacagatata agttctctgg   1330 

cacttgtcag aaaacttcta tgtttgtagc cataaaacat tttccgaaag tggaactttt   1390 

ctagaactta taggggaaat aatccctatg caaacactgt atgagtccca ttgacctttc   1450 

tttctcattt catttcattt ttgtct                                        1476 

 
           
             11  
             294  
             PRT  
             Picea glauca  
           
            11 

Met Pro Leu His Phe Ser Trp Asn Pro Thr Glu Asp Pro His Thr Val 
1               5                   10                  15 

Arg Pro Thr Glu Ala Leu Arg Asn Gln Ser Asn Gly Arg Arg Gly Ala 
            20                  25                  30 

Pro Arg Leu Arg Arg Ile Lys Ser Ile Lys Tyr Trp His Arg Arg Val 
        35                  40                  45 

Trp Lys Leu Pro Pro Ile Ser Gly Glu Asn His Gly Glu Ala Gly Pro 
    50                  55                  60 

Pro Gly Ala Arg Pro Phe Gln Asp Gly Leu Tyr Gly Gly His Cys Glu 
65                  70                  75                  80 

Ile Gly Val Gln Phe Phe Arg Asp Ala Asp Asp Phe Cys Glu Glu His 
                85                  90                  95 

Pro Glu Ile Ile Leu Met Cys Ala Ser Ile Thr Leu Val Gly Gly Arg 
            100                 105                 110 

Ala Glu Val Ser Ala Asn Thr Ala Pro Glu Glu Glu Tyr Ala Phe Arg 
        115                 120                 125 

Arg Arg Pro Val Cys Glu Arg Val Ser Ala Pro Val Val Pro Ala Gly 
    130                 135                 140 

Phe Val Ala Arg Val Asp Val Leu Cys Thr His Pro Met Phe Gly Pro 
145                 150                 155                 160 

Glu Ser Ser Lys Asp Asp Leu Gly Asp Leu Pro Phe Val Tyr Asp Lys 
                165                 170                 175 

Val Arg Val Ser Asn Glu Gly Leu Arg Ala Lys His Cys Glu Arg Phe 
            180                 185                 190 

Leu Asn Ile Phe Ser Cys Glu Gly Cys Arg Met Val Glu Met Ser Cys 
        195                 200                 205 

Ala Glu His Asp Arg Tyr Val Ala Glu Ser Gln Phe Ile Thr His Thr 
    210                 215                 220 

Val Gly Arg Met Leu Gly Arg Leu Gly Leu Glu Ser Thr Pro Ile Ala 
225                 230                 235                 240 

Thr Lys Gly Tyr Glu Lys Leu Leu Glu Val Ala Trp Asn Ile Ala Gly 
                245                 250                 255 

Asp Ser Phe Asp Ile Tyr Tyr Gly Leu Phe Met Tyr Asn Val Asn Ser 
            260                 265                 270 

Ile Glu Gln Ile Glu Arg Leu Asp Met Ala Phe Asn Ser Leu Lys Asn 
        275                 280                 285 

Glu Val Ser Gly Ser Asn 
    290 

 
           
             12  
             840  
             DNA  
             Synechocystis sp.  
             
               CDS  
               (1)..(840)  
             
           
            12 

atg aaa att ggt gtt gtt ggt ttg ggt tta att ggg gct tcc ttg gcg       48 
Met Lys Ile Gly Val Val Gly Leu Gly Leu Ile Gly Ala Ser Leu Ala 
1               5                   10                  15 

gga gac ttg cgt cgt cgg ggc cat tat ttg att ggg gtt tct cgg caa       96 
Gly Asp Leu Arg Arg Arg Gly His Tyr Leu Ile Gly Val Ser Arg Gln 
            20                  25                  30 

caa agc acc tgt gaa aaa gca gtg gaa aga caa ttg gtg gat gaa gcg      144 
Gln Ser Thr Cys Glu Lys Ala Val Glu Arg Gln Leu Val Asp Glu Ala 
        35                  40                  45 

ggt caa gat tta tct ctt ctc caa aca gca aaa ata att ttt ctt tgt      192 
Gly Gln Asp Leu Ser Leu Leu Gln Thr Ala Lys Ile Ile Phe Leu Cys 
    50                  55                  60 

act cct ata caa tta att ttg cct acc cta gag aag ctt att ccc cat      240 
Thr Pro Ile Gln Leu Ile Leu Pro Thr Leu Glu Lys Leu Ile Pro His 
65                  70                  75                  80 

cta tcg ccc aca gcc att gtc act gat gtg gcc tct gta aaa acg gcg      288 
Leu Ser Pro Thr Ala Ile Val Thr Asp Val Ala Ser Val Lys Thr Ala 
                85                  90                  95 

atc gcc gag ccg gcc agt caa ctt tgg tct ggg ttc att ggt ggt cac      336 
Ile Ala Glu Pro Ala Ser Gln Leu Trp Ser Gly Phe Ile Gly Gly His 
            100                 105                 110 

ccc atg gcc ggc aca gcg gcc cag ggc atc gac ggg gcg gaa gaa aat      384 
Pro Met Ala Gly Thr Ala Ala Gln Gly Ile Asp Gly Ala Glu Glu Asn 
        115                 120                 125 

tta ttt gtc aac gct ccc tat gtg ctc act ccc acc gaa tat act gac      432 
Leu Phe Val Asn Ala Pro Tyr Val Leu Thr Pro Thr Glu Tyr Thr Asp 
    130                 135                 140 

cca gag caa ttg gct tgt tta cgt tca gtg ttg gaa ccc ctg ggg gta      480 
Pro Glu Gln Leu Ala Cys Leu Arg Ser Val Leu Glu Pro Leu Gly Val 
145                 150                 155                 160 

aaa att tac ctc tgc act ccc gca gac cat gac caa gca gta gcc tgg      528 
Lys Ile Tyr Leu Cys Thr Pro Ala Asp His Asp Gln Ala Val Ala Trp 
                165                 170                 175 

att tcc cat tta cct gta atg gtg agt gct gct tta atc caa gcc tgt      576 
Ile Ser His Leu Pro Val Met Val Ser Ala Ala Leu Ile Gln Ala Cys 
            180                 185                 190 

gcc ggt gaa aaa gat ggg gat att ctc aaa cta gcc caa aat ttg gcc      624 
Ala Gly Glu Lys Asp Gly Asp Ile Leu Lys Leu Ala Gln Asn Leu Ala 
        195                 200                 205 

agt tcg ggt ttt cgg gat acc agt cgg gtg gga ggc ggc aac ccg gag      672 
Ser Ser Gly Phe Arg Asp Thr Ser Arg Val Gly Gly Gly Asn Pro Glu 
    210                 215                 220 

ttg ggc acc atg atg gcc acc tat aac caa cgg gct ttg cta aaa agt      720 
Leu Gly Thr Met Met Ala Thr Tyr Asn Gln Arg Ala Leu Leu Lys Ser 
225                 230                 235                 240 

ttg caa gac tat cgt cag cac ctg gat cag cta att acc cta att agt      768 
Leu Gln Asp Tyr Arg Gln His Leu Asp Gln Leu Ile Thr Leu Ile Ser 
                245                 250                 255 

aac caa caa tgg cct gaa ctc cat cgt ctt tta caa caa acc aac ggc      816 
Asn Gln Gln Trp Pro Glu Leu His Arg Leu Leu Gln Gln Thr Asn Gly 
            260                 265                 270 

gat cgg gac aag tat gtt gaa taa                                      840 
Asp Arg Asp Lys Tyr Val Glu 
        275 

 
           
             13  
             279  
             PRT  
             Synechocystis sp.  
           
            13 

Met Lys Ile Gly Val Val Gly Leu Gly Leu Ile Gly Ala Ser Leu Ala 
1               5                   10                  15 

Gly Asp Leu Arg Arg Arg Gly His Tyr Leu Ile Gly Val Ser Arg Gln 
            20                  25                  30 

Gln Ser Thr Cys Glu Lys Ala Val Glu Arg Gln Leu Val Asp Glu Ala 
        35                  40                  45 

Gly Gln Asp Leu Ser Leu Leu Gln Thr Ala Lys Ile Ile Phe Leu Cys 
    50                  55                  60 

Thr Pro Ile Gln Leu Ile Leu Pro Thr Leu Glu Lys Leu Ile Pro His 
65                  70                  75                  80 

Leu Ser Pro Thr Ala Ile Val Thr Asp Val Ala Ser Val Lys Thr Ala 
                85                  90                  95 

Ile Ala Glu Pro Ala Ser Gln Leu Trp Ser Gly Phe Ile Gly Gly His 
            100                 105                 110 

Pro Met Ala Gly Thr Ala Ala Gln Gly Ile Asp Gly Ala Glu Glu Asn 
        115                 120                 125 

Leu Phe Val Asn Ala Pro Tyr Val Leu Thr Pro Thr Glu Tyr Thr Asp 
    130                 135                 140 

Pro Glu Gln Leu Ala Cys Leu Arg Ser Val Leu Glu Pro Leu Gly Val 
145                 150                 155                 160 

Lys Ile Tyr Leu Cys Thr Pro Ala Asp His Asp Gln Ala Val Ala Trp 
                165                 170                 175 

Ile Ser His Leu Pro Val Met Val Ser Ala Ala Leu Ile Gln Ala Cys 
            180                 185                 190 

Ala Gly Glu Lys Asp Gly Asp Ile Leu Lys Leu Ala Gln Asn Leu Ala 
        195                 200                 205 

Ser Ser Gly Phe Arg Asp Thr Ser Arg Val Gly Gly Gly Asn Pro Glu 
    210                 215                 220 

Leu Gly Thr Met Met Ala Thr Tyr Asn Gln Arg Ala Leu Leu Lys Ser 
225                 230                 235                 240 

Leu Gln Asp Tyr Arg Gln His Leu Asp Gln Leu Ile Thr Leu Ile Ser 
                245                 250                 255 

Asn Gln Gln Trp Pro Glu Leu His Arg Leu Leu Gln Gln Thr Asn Gly 
            260                 265                 270 

Asp Arg Asp Lys Tyr Val Glu 
        275 

 
           
             14  
             1359  
             DNA  
             Saccharomyces cerevisiae  
             
               CDS  
               (1)..(1359)  
             
           
            14 

atg gta tca gag gat aag att gag caa tgg aaa gcc aca aaa gtc att       48 
Met Val Ser Glu Asp Lys Ile Glu Gln Trp Lys Ala Thr Lys Val Ile 
1               5                   10                  15 

ggt ata att ggt ctg ggt gat atg ggc cta tta tac gct aat aaa ttt       96 
Gly Ile Ile Gly Leu Gly Asp Met Gly Leu Leu Tyr Ala Asn Lys Phe 
            20                  25                  30 

aca gat gct gga tgg ggt gtt ata tgt tgt gat agg gaa gaa tat tat      144 
Thr Asp Ala Gly Trp Gly Val Ile Cys Cys Asp Arg Glu Glu Tyr Tyr 
        35                  40                  45 

gat gaa ctg aaa gaa aaa tat gcc tca gct aaa ttc gaa ctg gtg aaa      192 
Asp Glu Leu Lys Glu Lys Tyr Ala Ser Ala Lys Phe Glu Leu Val Lys 
    50                  55                  60 

aat ggt cat ttg gta tcc agg caa agc gac tat att atc tat agt gtt      240 
Asn Gly His Leu Val Ser Arg Gln Ser Asp Tyr Ile Ile Tyr Ser Val 
65                  70                  75                  80 

gaa gca tcc aat att agt aag atc gtc gca acg tat gga cca tct tct      288 
Glu Ala Ser Asn Ile Ser Lys Ile Val Ala Thr Tyr Gly Pro Ser Ser 
                85                  90                  95 

aag gtt gga aca att gtt ggg ggt caa acg agt tgt aag ctg ccg gaa      336 
Lys Val Gly Thr Ile Val Gly Gly Gln Thr Ser Cys Lys Leu Pro Glu 
            100                 105                 110 

atc gag gct ttc gaa aag tat tta ccc aag gac tgc gac atc att acc      384 
Ile Glu Ala Phe Glu Lys Tyr Leu Pro Lys Asp Cys Asp Ile Ile Thr 
        115                 120                 125 

gtg cat tcc ctt cat ggg cct aaa gtt aat act gaa ggc caa cca cta      432 
Val His Ser Leu His Gly Pro Lys Val Asn Thr Glu Gly Gln Pro Leu 
    130                 135                 140 

gtt att atc aat cac aga tca cag tac cca gaa tct ttt gag ttc gtt      480 
Val Ile Ile Asn His Arg Ser Gln Tyr Pro Glu Ser Phe Glu Phe Val 
145                 150                 155                 160 

aat tct gtt atg gca tgt ttg aaa agt aag caa gtt tat ttg aca tat      528 
Asn Ser Val Met Ala Cys Leu Lys Ser Lys Gln Val Tyr Leu Thr Tyr 
                165                 170                 175 

gaa gag cat gac aag att acc gct gat aca caa gct gtg aca cat gct      576 
Glu Glu His Asp Lys Ile Thr Ala Asp Thr Gln Ala Val Thr His Ala 
            180                 185                 190 

gct ttc tta agt atg gga tct gcg tgg gca aag ata aag att tat cct      624 
Ala Phe Leu Ser Met Gly Ser Ala Trp Ala Lys Ile Lys Ile Tyr Pro 
        195                 200                 205 

tgg act ctg ggt gta aac aaa tgg tac ggt ggc cta gaa aat gtg aaa      672 
Trp Thr Leu Gly Val Asn Lys Trp Tyr Gly Gly Leu Glu Asn Val Lys 
    210                 215                 220 

gtt aat ata tca cta aga atc tat tcg aac aag tgg cat gtt tac gca      720 
Val Asn Ile Ser Leu Arg Ile Tyr Ser Asn Lys Trp His Val Tyr Ala 
225                 230                 235                 240 

gga tta gcc ata aca aac cca agt gca cat cag caa att ctt caa tat      768 
Gly Leu Ala Ile Thr Asn Pro Ser Ala His Gln Gln Ile Leu Gln Tyr 
                245                 250                 255 

gca acc agt gca aca gaa cta ttt agt tta atg ata gat aac aaa gaa      816 
Ala Thr Ser Ala Thr Glu Leu Phe Ser Leu Met Ile Asp Asn Lys Glu 
            260                 265                 270 

caa gaa ctt act gat aga cta tta aaa gct aag caa ttt gta ttt gga      864 
Gln Glu Leu Thr Asp Arg Leu Leu Lys Ala Lys Gln Phe Val Phe Gly 
        275                 280                 285 

aag cat act ggt ctc tta cta ttg gat gac acg att tta gag aaa tat      912 
Lys His Thr Gly Leu Leu Leu Leu Asp Asp Thr Ile Leu Glu Lys Tyr 
    290                 295                 300 

tcg cta tca aaa agc agc att ggt aac agc aac aat tgc aag cca gtg      960 
Ser Leu Ser Lys Ser Ser Ile Gly Asn Ser Asn Asn Cys Lys Pro Val 
305                 310                 315                 320 

ccg aat tca cat tta tca ttg ttg gcg att gtt gat tcg tgg ttt caa     1008 
Pro Asn Ser His Leu Ser Leu Leu Ala Ile Val Asp Ser Trp Phe Gln 
                325                 330                 335 

ctt ggt att gat cca tat gat cat atg att tgt tcg acg cca tta ttc     1056 
Leu Gly Ile Asp Pro Tyr Asp His Met Ile Cys Ser Thr Pro Leu Phe 
            340                 345                 350 

aga ata ttc ctg ggt gtg tcc gaa tat ctt ttt tta aaa cct ggc tta     1104 
Arg Ile Phe Leu Gly Val Ser Glu Tyr Leu Phe Leu Lys Pro Gly Leu 
        355                 360                 365 

tta gaa cag aca att gat gca gct atc cat gat aaa tca ttc ata aaa     1152 
Leu Glu Gln Thr Ile Asp Ala Ala Ile His Asp Lys Ser Phe Ile Lys 
    370                 375                 380 

gat gat tta gaa ttt gtt att tcg gct aga gaa tgg agc tcg gtt gtt     1200 
Asp Asp Leu Glu Phe Val Ile Ser Ala Arg Glu Trp Ser Ser Val Val 
385                 390                 395                 400 

tct ttt gcc aat ttt gat ata tac aaa aag caa ttt cag agt gtt caa     1248 
Ser Phe Ala Asn Phe Asp Ile Tyr Lys Lys Gln Phe Gln Ser Val Gln 
                405                 410                 415 

aag ttc ttt gag cca atg ctt cca gag gct aat ctc att ggc aac gag     1296 
Lys Phe Phe Glu Pro Met Leu Pro Glu Ala Asn Leu Ile Gly Asn Glu 
            420                 425                 430 

atg ata aaa acc att ctg agt cat tct agt gac cgt tcg gcc gct gaa     1344 
Met Ile Lys Thr Ile Leu Ser His Ser Ser Asp Arg Ser Ala Ala Glu 
        435                 440                 445 

aaa aga aat aca taa                                                 1359 
Lys Arg Asn Thr 
    450 

 
           
             15  
             452  
             PRT  
             Saccharomyces cerevisiae  
           
            15 

Met Val Ser Glu Asp Lys Ile Glu Gln Trp Lys Ala Thr Lys Val Ile 
1               5                   10                  15 

Gly Ile Ile Gly Leu Gly Asp Met Gly Leu Leu Tyr Ala Asn Lys Phe 
            20                  25                  30 

Thr Asp Ala Gly Trp Gly Val Ile Cys Cys Asp Arg Glu Glu Tyr Tyr 
        35                  40                  45 

Asp Glu Leu Lys Glu Lys Tyr Ala Ser Ala Lys Phe Glu Leu Val Lys 
    50                  55                  60 

Asn Gly His Leu Val Ser Arg Gln Ser Asp Tyr Ile Ile Tyr Ser Val 
65                  70                  75                  80 

Glu Ala Ser Asn Ile Ser Lys Ile Val Ala Thr Tyr Gly Pro Ser Ser 
                85                  90                  95 

Lys Val Gly Thr Ile Val Gly Gly Gln Thr Ser Cys Lys Leu Pro Glu 
            100                 105                 110 

Ile Glu Ala Phe Glu Lys Tyr Leu Pro Lys Asp Cys Asp Ile Ile Thr 
        115                 120                 125 

Val His Ser Leu His Gly Pro Lys Val Asn Thr Glu Gly Gln Pro Leu 
    130                 135                 140 

Val Ile Ile Asn His Arg Ser Gln Tyr Pro Glu Ser Phe Glu Phe Val 
145                 150                 155                 160 

Asn Ser Val Met Ala Cys Leu Lys Ser Lys Gln Val Tyr Leu Thr Tyr 
                165                 170                 175 

Glu Glu His Asp Lys Ile Thr Ala Asp Thr Gln Ala Val Thr His Ala 
            180                 185                 190 

Ala Phe Leu Ser Met Gly Ser Ala Trp Ala Lys Ile Lys Ile Tyr Pro 
        195                 200                 205 

Trp Thr Leu Gly Val Asn Lys Trp Tyr Gly Gly Leu Glu Asn Val Lys 
    210                 215                 220 

Val Asn Ile Ser Leu Arg Ile Tyr Ser Asn Lys Trp His Val Tyr Ala 
225                 230                 235                 240 

Gly Leu Ala Ile Thr Asn Pro Ser Ala His Gln Gln Ile Leu Gln Tyr 
                245                 250                 255 

Ala Thr Ser Ala Thr Glu Leu Phe Ser Leu Met Ile Asp Asn Lys Glu 
            260                 265                 270 

Gln Glu Leu Thr Asp Arg Leu Leu Lys Ala Lys Gln Phe Val Phe Gly 
        275                 280                 285 

Lys His Thr Gly Leu Leu Leu Leu Asp Asp Thr Ile Leu Glu Lys Tyr 
    290                 295                 300 

Ser Leu Ser Lys Ser Ser Ile Gly Asn Ser Asn Asn Cys Lys Pro Val 
305                 310                 315                 320 

Pro Asn Ser His Leu Ser Leu Leu Ala Ile Val Asp Ser Trp Phe Gln 
                325                 330                 335 

Leu Gly Ile Asp Pro Tyr Asp His Met Ile Cys Ser Thr Pro Leu Phe 
            340                 345                 350 

Arg Ile Phe Leu Gly Val Ser Glu Tyr Leu Phe Leu Lys Pro Gly Leu 
        355                 360                 365 

Leu Glu Gln Thr Ile Asp Ala Ala Ile His Asp Lys Ser Phe Ile Lys 
    370                 375                 380 

Asp Asp Leu Glu Phe Val Ile Ser Ala Arg Glu Trp Ser Ser Val Val 
385                 390                 395                 400 

Ser Phe Ala Asn Phe Asp Ile Tyr Lys Lys Gln Phe Gln Ser Val Gln 
                405                 410                 415 

Lys Phe Phe Glu Pro Met Leu Pro Glu Ala Asn Leu Ile Gly Asn Glu 
            420                 425                 430 

Met Ile Lys Thr Ile Leu Ser His Ser Ser Asp Arg Ser Ala Ala Glu 
        435                 440                 445 

Lys Arg Asn Thr 
    450 

 
           
             16  
             1116  
             DNA  
             Bacillus subtilis  
             
               CDS  
               (1)..(1116)  
             
           
            16 

atg aat caa atg aaa gat aca ata ttg ctc gcc ggt ctc gga ttg ata       48 
Met Asn Gln Met Lys Asp Thr Ile Leu Leu Ala Gly Leu Gly Leu Ile 
1               5                   10                  15 

ggc ggt tcg att gcc cta gcc atc aaa aaa aat cat ccc ggc aaa cgg       96 
Gly Gly Ser Ile Ala Leu Ala Ile Lys Lys Asn His Pro Gly Lys Arg 
            20                  25                  30 

att atc gga atc gac atc tct gat gaa cag gcg gta gcg gca tta aaa      144 
Ile Ile Gly Ile Asp Ile Ser Asp Glu Gln Ala Val Ala Ala Leu Lys 
        35                  40                  45 

tta ggc gtg ata gac gat cgt gct gat tcg ttt att agc ggt gtg aaa      192 
Leu Gly Val Ile Asp Asp Arg Ala Asp Ser Phe Ile Ser Gly Val Lys 
    50                  55                  60 

gag gca gct aca gta atc att gcg aca cct gtt gaa caa aca ctg gtt      240 
Glu Ala Ala Thr Val Ile Ile Ala Thr Pro Val Glu Gln Thr Leu Val 
65                  70                  75                  80 

atg ctt gaa gag ctg gct cat tca gga att gaa cat gag ctt ttg att      288 
Met Leu Glu Glu Leu Ala His Ser Gly Ile Glu His Glu Leu Leu Ile 
                85                  90                  95 

acg gat gta gga agc aca aag caa aaa gtg gtt gat tac gct gat caa      336 
Thr Asp Val Gly Ser Thr Lys Gln Lys Val Val Asp Tyr Ala Asp Gln 
            100                 105                 110 

gtg ctg cct agc cgc tat caa ttt gtc gga ggg cat ccg atg gcg ggt      384 
Val Leu Pro Ser Arg Tyr Gln Phe Val Gly Gly His Pro Met Ala Gly 
        115                 120                 125 

tca cat aaa tca gga gtg gcc gct gcg aag gag ttc ctg ttt gaa aat      432 
Ser His Lys Ser Gly Val Ala Ala Ala Lys Glu Phe Leu Phe Glu Asn 
    130                 135                 140 

gca ttt tat att tta acg cca ggc cag aaa acg gac aaa caa gct gtg      480 
Ala Phe Tyr Ile Leu Thr Pro Gly Gln Lys Thr Asp Lys Gln Ala Val 
145                 150                 155                 160 

gaa cag tta aaa aac ctg ctg aag ggg acg aat gcc cat ttt gtg gaa      528 
Glu Gln Leu Lys Asn Leu Leu Lys Gly Thr Asn Ala His Phe Val Glu 
                165                 170                 175 

atg tcg cca gag gag cat gat ggc gtt aca agc gta atc agt cat ttt      576 
Met Ser Pro Glu Glu His Asp Gly Val Thr Ser Val Ile Ser His Phe 
            180                 185                 190 

ccg cat att gta gca gct agc ctt gtt cac caa acc cat cat tcg gaa      624 
Pro His Ile Val Ala Ala Ser Leu Val His Gln Thr His His Ser Glu 
        195                 200                 205 

aac ctg tat ccg ctt gtt aag cgt ttt gct gcc ggc ggg ttc aga gat      672 
Asn Leu Tyr Pro Leu Val Lys Arg Phe Ala Ala Gly Gly Phe Arg Asp 
    210                 215                 220 

att aca agg att gca tca agc agc ccg gca atg tgg cgg gat att tta      720 
Ile Thr Arg Ile Ala Ser Ser Ser Pro Ala Met Trp Arg Asp Ile Leu 
225                 230                 235                 240 

tta cat aat aaa gat aaa atc tta gac cgt ttt gat gag tgg att cgt      768 
Leu His Asn Lys Asp Lys Ile Leu Asp Arg Phe Asp Glu Trp Ile Arg 
                245                 250                 255 

gaa att gac aag atc cgt aca tat gta gaa caa gaa gat gcg gaa aat      816 
Glu Ile Asp Lys Ile Arg Thr Tyr Val Glu Gln Glu Asp Ala Glu Asn 
            260                 265                 270 

cta ttt cgt tat ttt aaa aca gcc aag gat tat cgc gac ggg ctg ccg      864 
Leu Phe Arg Tyr Phe Lys Thr Ala Lys Asp Tyr Arg Asp Gly Leu Pro 
        275                 280                 285 

ctt cgg cag aag gga gcg ata cct gca ttt tat gat tta tat gtg gat      912 
Leu Arg Gln Lys Gly Ala Ile Pro Ala Phe Tyr Asp Leu Tyr Val Asp 
    290                 295                 300 

gta ccc gat cat ccg ggt gta ata tcc gag ata aca gcg atc tta gct      960 
Val Pro Asp His Pro Gly Val Ile Ser Glu Ile Thr Ala Ile Leu Ala 
305                 310                 315                 320 

gcg gag cgc atc agt atc acg aat atc cgc att atc gaa aca cga gag     1008 
Ala Glu Arg Ile Ser Ile Thr Asn Ile Arg Ile Ile Glu Thr Arg Glu 
                325                 330                 335 

gat att aac ggg att tta agg atc agt ttt cag tct gat gac gac cgc     1056 
Asp Ile Asn Gly Ile Leu Arg Ile Ser Phe Gln Ser Asp Asp Asp Arg 
            340                 345                 350 

aaa agg gca gaa caa tgc att gaa gcc cgg gcg gaa tat gaa act ttt     1104 
Lys Arg Ala Glu Gln Cys Ile Glu Ala Arg Ala Glu Tyr Glu Thr Phe 
        355                 360                 365 

tat gct gat tga                                                     1116 
Tyr Ala Asp 
    370 

 
           
             17  
             371  
             PRT  
             Bacillus subtilis  
           
            17 

Met Asn Gln Met Lys Asp Thr Ile Leu Leu Ala Gly Leu Gly Leu Ile 
1               5                   10                  15 

Gly Gly Ser Ile Ala Leu Ala Ile Lys Lys Asn His Pro Gly Lys Arg 
            20                  25                  30 

Ile Ile Gly Ile Asp Ile Ser Asp Glu Gln Ala Val Ala Ala Leu Lys 
        35                  40                  45 

Leu Gly Val Ile Asp Asp Arg Ala Asp Ser Phe Ile Ser Gly Val Lys 
    50                  55                  60 

Glu Ala Ala Thr Val Ile Ile Ala Thr Pro Val Glu Gln Thr Leu Val 
65                  70                  75                  80 

Met Leu Glu Glu Leu Ala His Ser Gly Ile Glu His Glu Leu Leu Ile 
                85                  90                  95 

Thr Asp Val Gly Ser Thr Lys Gln Lys Val Val Asp Tyr Ala Asp Gln 
            100                 105                 110 

Val Leu Pro Ser Arg Tyr Gln Phe Val Gly Gly His Pro Met Ala Gly 
        115                 120                 125 

Ser His Lys Ser Gly Val Ala Ala Ala Lys Glu Phe Leu Phe Glu Asn 
    130                 135                 140 

Ala Phe Tyr Ile Leu Thr Pro Gly Gln Lys Thr Asp Lys Gln Ala Val 
145                 150                 155                 160 

Glu Gln Leu Lys Asn Leu Leu Lys Gly Thr Asn Ala His Phe Val Glu 
                165                 170                 175 

Met Ser Pro Glu Glu His Asp Gly Val Thr Ser Val Ile Ser His Phe 
            180                 185                 190 

Pro His Ile Val Ala Ala Ser Leu Val His Gln Thr His His Ser Glu 
        195                 200                 205 

Asn Leu Tyr Pro Leu Val Lys Arg Phe Ala Ala Gly Gly Phe Arg Asp 
    210                 215                 220 

Ile Thr Arg Ile Ala Ser Ser Ser Pro Ala Met Trp Arg Asp Ile Leu 
225                 230                 235                 240 

Leu His Asn Lys Asp Lys Ile Leu Asp Arg Phe Asp Glu Trp Ile Arg 
                245                 250                 255 

Glu Ile Asp Lys Ile Arg Thr Tyr Val Glu Gln Glu Asp Ala Glu Asn 
            260                 265                 270 

Leu Phe Arg Tyr Phe Lys Thr Ala Lys Asp Tyr Arg Asp Gly Leu Pro 
        275                 280                 285 

Leu Arg Gln Lys Gly Ala Ile Pro Ala Phe Tyr Asp Leu Tyr Val Asp 
    290                 295                 300 

Val Pro Asp His Pro Gly Val Ile Ser Glu Ile Thr Ala Ile Leu Ala 
305                 310                 315                 320 

Ala Glu Arg Ile Ser Ile Thr Asn Ile Arg Ile Ile Glu Thr Arg Glu 
                325                 330                 335 

Asp Ile Asn Gly Ile Leu Arg Ile Ser Phe Gln Ser Asp Asp Asp Arg 
            340                 345                 350 

Lys Arg Ala Glu Gln Cys Ile Glu Ala Arg Ala Glu Tyr Glu Thr Phe 
        355                 360                 365 

Tyr Ala Asp 
    370 

 
           
             18  
             1122  
             DNA  
             Escherichia coli  
             
               CDS  
               (1)..(1122)  
             
           
            18 

atg gtt gct gaa ttg acc gca tta cgc gat caa att gat gaa gtc gat       48 
Met Val Ala Glu Leu Thr Ala Leu Arg Asp Gln Ile Asp Glu Val Asp 
1               5                   10                  15 

aaa gcg ctg ctg aat tta tta gcg aag cgt ctg gaa ctg gtt gct gaa       96 
Lys Ala Leu Leu Asn Leu Leu Ala Lys Arg Leu Glu Leu Val Ala Glu 
            20                  25                  30 

gtg ggc gag gtg aaa agc cgc ttt gga ctg cct att tat gtt ccg gag      144 
Val Gly Glu Val Lys Ser Arg Phe Gly Leu Pro Ile Tyr Val Pro Glu 
        35                  40                  45 

cgc gag gca tct atg ttg gcc tcg cgt cgt gca gag gcg gaa gct ctg      192 
Arg Glu Ala Ser Met Leu Ala Ser Arg Arg Ala Glu Ala Glu Ala Leu 
    50                  55                  60 

ggt gta ccg cca gat ctg att gag gat gtt ttg cgt cgg gtg atg cgt      240 
Gly Val Pro Pro Asp Leu Ile Glu Asp Val Leu Arg Arg Val Met Arg 
65                  70                  75                  80 

gaa tct tac tcc agt gaa aac gac aaa gga ttt aaa aca ctt tgt ccg      288 
Glu Ser Tyr Ser Ser Glu Asn Asp Lys Gly Phe Lys Thr Leu Cys Pro 
                85                  90                  95 

tca ctg cgt ccg gtg gtt atc gtc ggc ggt ggc ggt cag atg gga cgc      336 
Ser Leu Arg Pro Val Val Ile Val Gly Gly Gly Gly Gln Met Gly Arg 
            100                 105                 110 

ctg ttc gag aag atg ctg acc ctc tcg ggt tat cag gtg cgg att ctg      384 
Leu Phe Glu Lys Met Leu Thr Leu Ser Gly Tyr Gln Val Arg Ile Leu 
        115                 120                 125 

gag caa cat gac tgg gat cga gcg gct gat att gtt gcc gat gcc gga      432 
Glu Gln His Asp Trp Asp Arg Ala Ala Asp Ile Val Ala Asp Ala Gly 
    130                 135                 140 

atg gtg att gtt agt gtg cca atc cac gtt act gag caa gtt att ggc      480 
Met Val Ile Val Ser Val Pro Ile His Val Thr Glu Gln Val Ile Gly 
145                 150                 155                 160 

aaa tta ccg cct tta ccg aaa gat tgt att ctg gtc gat ctg gca tca      528 
Lys Leu Pro Pro Leu Pro Lys Asp Cys Ile Leu Val Asp Leu Ala Ser 
                165                 170                 175 

gtg aaa aat ggg cca tta cag gcc atg ctg gtg gcg cat gat ggt ccg      576 
Val Lys Asn Gly Pro Leu Gln Ala Met Leu Val Ala His Asp Gly Pro 
            180                 185                 190 

gtg ctg ggg cta cac ccg atg ttc ggt ccg gac agc ggt agc ctg gca      624 
Val Leu Gly Leu His Pro Met Phe Gly Pro Asp Ser Gly Ser Leu Ala 
        195                 200                 205 

aag caa gtt gtg gtc tgg tgt gat gga cgt aaa ccg gaa gca tac caa      672 
Lys Gln Val Val Val Trp Cys Asp Gly Arg Lys Pro Glu Ala Tyr Gln 
    210                 215                 220 

tgg ttt ctg gag caa att cag gtc tgg ggc gct cgg ctg cat cgt att      720 
Trp Phe Leu Glu Gln Ile Gln Val Trp Gly Ala Arg Leu His Arg Ile 
225                 230                 235                 240 

agc gcc gtc gag cac gat cag aat atg gcg ttt att cag gca ctg cgc      768 
Ser Ala Val Glu His Asp Gln Asn Met Ala Phe Ile Gln Ala Leu Arg 
                245                 250                 255 

cac ttt gct act ttt gct tac ggg ctg cac ctg gca gaa gaa aat gtt      816 
His Phe Ala Thr Phe Ala Tyr Gly Leu His Leu Ala Glu Glu Asn Val 
            260                 265                 270 

cag ctt gag caa ctt ctg gcg ctc tct tcg ccg att tac cgc ctt gag      864 
Gln Leu Glu Gln Leu Leu Ala Leu Ser Ser Pro Ile Tyr Arg Leu Glu 
        275                 280                 285 

ctg gcg atg gtc ggg cga ctg ttt gct cag gat ccg cag ctt tat gcc      912 
Leu Ala Met Val Gly Arg Leu Phe Ala Gln Asp Pro Gln Leu Tyr Ala 
    290                 295                 300 

gac atc att atg tcg tca gag cgt aat ctg gcg tta atc aaa cgt tac      960 
Asp Ile Ile Met Ser Ser Glu Arg Asn Leu Ala Leu Ile Lys Arg Tyr 
305                 310                 315                 320 

tat aag cgt ttc ggc gag gcg att gag ttg ctg gag cag ggc gat aag     1008 
Tyr Lys Arg Phe Gly Glu Ala Ile Glu Leu Leu Glu Gln Gly Asp Lys 
                325                 330                 335 

cag gcg ttt att gac agt ttc cgc aag gtg gag cac tgg ttc ggc gat     1056 
Gln Ala Phe Ile Asp Ser Phe Arg Lys Val Glu His Trp Phe Gly Asp 
            340                 345                 350 

tac gca cag cgt ttt cag agt gaa agc cgc gtg tta ttg cgt cag gcg     1104 
Tyr Ala Gln Arg Phe Gln Ser Glu Ser Arg Val Leu Leu Arg Gln Ala 
        355                 360                 365 

aat gac aat cgc cag taa                                             1122 
Asn Asp Asn Arg Gln 
    370 

 
           
             19  
             373  
             PRT  
             Escherichia coli  
           
            19 

Met Val Ala Glu Leu Thr Ala Leu Arg Asp Gln Ile Asp Glu Val Asp 
1               5                   10                  15 

Lys Ala Leu Leu Asn Leu Leu Ala Lys Arg Leu Glu Leu Val Ala Glu 
            20                  25                  30 

Val Gly Glu Val Lys Ser Arg Phe Gly Leu Pro Ile Tyr Val Pro Glu 
        35                  40                  45 

Arg Glu Ala Ser Met Leu Ala Ser Arg Arg Ala Glu Ala Glu Ala Leu 
    50                  55                  60 

Gly Val Pro Pro Asp Leu Ile Glu Asp Val Leu Arg Arg Val Met Arg 
65                  70                  75                  80 

Glu Ser Tyr Ser Ser Glu Asn Asp Lys Gly Phe Lys Thr Leu Cys Pro 
                85                  90                  95 

Ser Leu Arg Pro Val Val Ile Val Gly Gly Gly Gly Gln Met Gly Arg 
            100                 105                 110 

Leu Phe Glu Lys Met Leu Thr Leu Ser Gly Tyr Gln Val Arg Ile Leu 
        115                 120                 125 

Glu Gln His Asp Trp Asp Arg Ala Ala Asp Ile Val Ala Asp Ala Gly 
    130                 135                 140 

Met Val Ile Val Ser Val Pro Ile His Val Thr Glu Gln Val Ile Gly 
145                 150                 155                 160 

Lys Leu Pro Pro Leu Pro Lys Asp Cys Ile Leu Val Asp Leu Ala Ser 
                165                 170                 175 

Val Lys Asn Gly Pro Leu Gln Ala Met Leu Val Ala His Asp Gly Pro 
            180                 185                 190 

Val Leu Gly Leu His Pro Met Phe Gly Pro Asp Ser Gly Ser Leu Ala 
        195                 200                 205 

Lys Gln Val Val Val Trp Cys Asp Gly Arg Lys Pro Glu Ala Tyr Gln 
    210                 215                 220 

Trp Phe Leu Glu Gln Ile Gln Val Trp Gly Ala Arg Leu His Arg Ile 
225                 230                 235                 240 

Ser Ala Val Glu His Asp Gln Asn Met Ala Phe Ile Gln Ala Leu Arg 
                245                 250                 255 

His Phe Ala Thr Phe Ala Tyr Gly Leu His Leu Ala Glu Glu Asn Val 
            260                 265                 270 

Gln Leu Glu Gln Leu Leu Ala Leu Ser Ser Pro Ile Tyr Arg Leu Glu 
        275                 280                 285 

Leu Ala Met Val Gly Arg Leu Phe Ala Gln Asp Pro Gln Leu Tyr Ala 
    290                 295                 300 

Asp Ile Ile Met Ser Ser Glu Arg Asn Leu Ala Leu Ile Lys Arg Tyr 
305                 310                 315                 320 

Tyr Lys Arg Phe Gly Glu Ala Ile Glu Leu Leu Glu Gln Gly Asp Lys 
                325                 330                 335 

Gln Ala Phe Ile Asp Ser Phe Arg Lys Val Glu His Trp Phe Gly Asp 
            340                 345                 350 

Tyr Ala Gln Arg Phe Gln Ser Glu Ser Arg Val Leu Leu Arg Gln Ala 
        355                 360                 365 

Asn Asp Asn Arg Gln 
    370 

 
           
             20  
             1152  
             DNA  
             Erwinia herbicola  
             
               CDS  
               (1)..(1119)  
             
           
            20 

atg gtg gct gaa ctg acc gcg tta cgc gat caa att gac agt gta gat       48 
Met Val Ala Glu Leu Thr Ala Leu Arg Asp Gln Ile Asp Ser Val Asp 
1               5                   10                  15 

aaa gcg ctg ctg gat ctg ctg gct aag cga ctg gaa ctg gtg gcc gag       96 
Lys Ala Leu Leu Asp Leu Leu Ala Lys Arg Leu Glu Leu Val Ala Glu 
            20                  25                  30 

gta ggt gag gtg aag agc cgt tac ggc ctg cct atc tat gtg cct gag      144 
Val Gly Glu Val Lys Ser Arg Tyr Gly Leu Pro Ile Tyr Val Pro Glu 
        35                  40                  45 

cgt gag gcg tcg atg ctg gct tcg cgt cgc aaa gag gcc gaa gcg ctc      192 
Arg Glu Ala Ser Met Leu Ala Ser Arg Arg Lys Glu Ala Glu Ala Leu 
    50                  55                  60 

ggc gta cca ccg gat ctg att gag gat gtg ctg cgt cgc gtg atg cgg      240 
Gly Val Pro Pro Asp Leu Ile Glu Asp Val Leu Arg Arg Val Met Arg 
65                  70                  75                  80 

gaa tcc tat acc agc gag aat gat aaa ggc ttt aaa acc ctc tgt cct      288 
Glu Ser Tyr Thr Ser Glu Asn Asp Lys Gly Phe Lys Thr Leu Cys Pro 
                85                  90                  95 

gaa ctg cgc ccg gtg gtg att gtc ggt ggt aag ggc cag atg ggc cgg      336 
Glu Leu Arg Pro Val Val Ile Val Gly Gly Lys Gly Gln Met Gly Arg 
            100                 105                 110 

ctg ttt gaa aaa atg ctc ggg cta tca ggc tac acg gtt aaa acg ctg      384 
Leu Phe Glu Lys Met Leu Gly Leu Ser Gly Tyr Thr Val Lys Thr Leu 
        115                 120                 125 

gat aaa gag gac tgg cct cag gct gag act ctg ctc agc gat gcc gga      432 
Asp Lys Glu Asp Trp Pro Gln Ala Glu Thr Leu Leu Ser Asp Ala Gly 
    130                 135                 140 

atg gtg atc att agc gtg ccg att cac ctg acc gag cag gtg att gcc      480 
Met Val Ile Ile Ser Val Pro Ile His Leu Thr Glu Gln Val Ile Ala 
145                 150                 155                 160 

caa ctg cca cca ctg ccg gaa gat tgt att ctg gtc gat ctg gcg tca      528 
Gln Leu Pro Pro Leu Pro Glu Asp Cys Ile Leu Val Asp Leu Ala Ser 
                165                 170                 175 

gtc aaa aac cgg cct ctg cag gca atg ctg gct gcc cat aac ggg cct      576 
Val Lys Asn Arg Pro Leu Gln Ala Met Leu Ala Ala His Asn Gly Pro 
            180                 185                 190 

gta ctg ggt ctg cat ccg atg ttt ggc ccg gac agc ggc agc ctg gca      624 
Val Leu Gly Leu His Pro Met Phe Gly Pro Asp Ser Gly Ser Leu Ala 
        195                 200                 205 

aaa cag gtg gtg gtc tgg tgt gat gga aga caa ccg gaa gcg tat cag      672 
Lys Gln Val Val Val Trp Cys Asp Gly Arg Gln Pro Glu Ala Tyr Gln 
    210                 215                 220 

tgg ttc ctg gag cag att cag gtc tgg ggt gcg cgt ctg cat cgt atc      720 
Trp Phe Leu Glu Gln Ile Gln Val Trp Gly Ala Arg Leu His Arg Ile 
225                 230                 235                 240 

agc gct gtt gag cat gac cag aac atg gca ttc att cag gcg ctg cgt      768 
Ser Ala Val Glu His Asp Gln Asn Met Ala Phe Ile Gln Ala Leu Arg 
                245                 250                 255 

cac ttt gct acc ttc gct tat ggt ctg cat tta gcc gaa gag aac gtc      816 
His Phe Ala Thr Phe Ala Tyr Gly Leu His Leu Ala Glu Glu Asn Val 
            260                 265                 270 

aat ctg gat cag ctg ctg gcg ctc tcg tcg ccc att tac cgg ctt gaa      864 
Asn Leu Asp Gln Leu Leu Ala Leu Ser Ser Pro Ile Tyr Arg Leu Glu 
        275                 280                 285 

ctg gcg atg gtg ggg cgg ttg ttc gct cag gat ccg caa ctc tat gcg      912 
Leu Ala Met Val Gly Arg Leu Phe Ala Gln Asp Pro Gln Leu Tyr Ala 
    290                 295                 300 

gat atc atc atg tct tca gag agt aat ctg gcg ctg ata aaa cgc tat      960 
Asp Ile Ile Met Ser Ser Glu Ser Asn Leu Ala Leu Ile Lys Arg Tyr 
305                 310                 315                 320 

tac cag cgg ttt ggt gaa gcg att gcg ctg ctg gag cag ggc gac aag     1008 
Tyr Gln Arg Phe Gly Glu Ala Ile Ala Leu Leu Glu Gln Gly Asp Lys 
                325                 330                 335 

cag gcg ttt atc gcc agc ttt aac cgg gtt gaa cag tgg ttt ggc gat     1056 
Gln Ala Phe Ile Ala Ser Phe Asn Arg Val Glu Gln Trp Phe Gly Asp 
            340                 345                 350 

cac gca aaa cgc ttc ctg gtc gaa agc cga agc ctg ttg cga tcg gcc     1104 
His Ala Lys Arg Phe Leu Val Glu Ser Arg Ser Leu Leu Arg Ser Ala 
        355                 360                 365 

aat gac agc cgc cca taaaaaaaag gcatccagtt ggatgccttt ttt            1152 
Asn Asp Ser Arg Pro 
    370 

 
           
             21  
             373  
             PRT  
             Erwinia herbicola  
           
            21 

Met Val Ala Glu Leu Thr Ala Leu Arg Asp Gln Ile Asp Ser Val Asp 
1               5                   10                  15 

Lys Ala Leu Leu Asp Leu Leu Ala Lys Arg Leu Glu Leu Val Ala Glu 
            20                  25                  30 

Val Gly Glu Val Lys Ser Arg Tyr Gly Leu Pro Ile Tyr Val Pro Glu 
        35                  40                  45 

Arg Glu Ala Ser Met Leu Ala Ser Arg Arg Lys Glu Ala Glu Ala Leu 
    50                  55                  60 

Gly Val Pro Pro Asp Leu Ile Glu Asp Val Leu Arg Arg Val Met Arg 
65                  70                  75                  80 

Glu Ser Tyr Thr Ser Glu Asn Asp Lys Gly Phe Lys Thr Leu Cys Pro 
                85                  90                  95 

Glu Leu Arg Pro Val Val Ile Val Gly Gly Lys Gly Gln Met Gly Arg 
            100                 105                 110 

Leu Phe Glu Lys Met Leu Gly Leu Ser Gly Tyr Thr Val Lys Thr Leu 
        115                 120                 125 

Asp Lys Glu Asp Trp Pro Gln Ala Glu Thr Leu Leu Ser Asp Ala Gly 
    130                 135                 140 

Met Val Ile Ile Ser Val Pro Ile His Leu Thr Glu Gln Val Ile Ala 
145                 150                 155                 160 

Gln Leu Pro Pro Leu Pro Glu Asp Cys Ile Leu Val Asp Leu Ala Ser 
                165                 170                 175 

Val Lys Asn Arg Pro Leu Gln Ala Met Leu Ala Ala His Asn Gly Pro 
            180                 185                 190 

Val Leu Gly Leu His Pro Met Phe Gly Pro Asp Ser Gly Ser Leu Ala 
        195                 200                 205 

Lys Gln Val Val Val Trp Cys Asp Gly Arg Gln Pro Glu Ala Tyr Gln 
    210                 215                 220 

Trp Phe Leu Glu Gln Ile Gln Val Trp Gly Ala Arg Leu His Arg Ile 
225                 230                 235                 240 

Ser Ala Val Glu His Asp Gln Asn Met Ala Phe Ile Gln Ala Leu Arg 
                245                 250                 255 

His Phe Ala Thr Phe Ala Tyr Gly Leu His Leu Ala Glu Glu Asn Val 
            260                 265                 270 

Asn Leu Asp Gln Leu Leu Ala Leu Ser Ser Pro Ile Tyr Arg Leu Glu 
        275                 280                 285 

Leu Ala Met Val Gly Arg Leu Phe Ala Gln Asp Pro Gln Leu Tyr Ala 
    290                 295                 300 

Asp Ile Ile Met Ser Ser Glu Ser Asn Leu Ala Leu Ile Lys Arg Tyr 
305                 310                 315                 320 

Tyr Gln Arg Phe Gly Glu Ala Ile Ala Leu Leu Glu Gln Gly Asp Lys 
                325                 330                 335 

Gln Ala Phe Ile Ala Ser Phe Asn Arg Val Glu Gln Trp Phe Gly Asp 
            340                 345                 350 

His Ala Lys Arg Phe Leu Val Glu Ser Arg Ser Leu Leu Arg Ser Ala 
        355                 360                 365 

Asn Asp Ser Arg Pro 
    370 

 
           
             22  
             1129  
             DNA  
             Lycopersicon esculentum  
           
            22 

atgttttccc tttcatctat acaatctaac aatattcaat ctcaatcatc ttcgtcgcta     60 

ctcttcaatc atcatcacca gcattcaact atttcaactc ggtttcatca ccaccgccta    120 

ctcttccctc tccgtgccca aaatagcgac ttaactacag ccaccaccaa taacaactat    180 

gtcgatcttg atgacaatct aaccagactt gataaatttt caaaatcatt aagtatttcg    240 

aatatcgaag aaaatacatc attaaatccc ctcttatgtt ccaataacaa gctcaaaata    300 

gctatcatag gctttggaaa ctttggacaa tttattgcca aatcctttat caaacaaggc    360 

catgttgtat tagctcattc acgtagtgat tattccctca tagcacaatc ccttaatgtc    420 

cacttctttc aagatcctaa tgacttatgt gaacaacatc ctgacgttat tttactttgc    480 

acatccatca attcactcga aaacgtcatt cgttcccttc ccatccaaaa gcttaaacgt    540 

aacacacttt tcgtagacgt attatcagtc aaagaattcc cgaaaaacat ttttcttcaa    600 

tcactaccaa aagaatttga tattttgtgt actcatccta tgtttggtcc aacaagtggt    660 

aaagacaatt ggaaaggact accatttatg tatgacaaag ttagaattgg acaagaagag    720 

tcaagaatta aaagagtcaa caattttatc aacatttttg taaaagaagg ttgtagaatg    780 

gttgaaatga gttgtagtga acatgacaag tatgctgctg gatcacaatt tattacacat    840 

actattggaa gaatgttaca aagacttggg acacaaacaa ctcctataaa cacaaaagga    900 

tatgaaagtt tgttgaattt gatggagaat acaactagtg atagttttga tttgtattgt    960 

ggtttgctta tgtataacaa taattcaatg gaggtgttag agaaactaga tgcagcattg   1020 

gatagtttga aaagggaatt atttggacaa gttcttcaaa agttggagaa aagagtggaa   1080 

aagggaagta agttagcttt acctactcct gattttagta agaaaattg               1129 

 
           
             23  
             32  
             DNA  
             Artificial  
             
               Oligonucleotide P1  
             
           
            23 

tctccatatg atctttcaat ctcattctca tc                                   32 

 
           
             24  
             32  
             DNA  
             Artificial  
             
               Oligonucleotide P2  
             
           
            24 

ctaactaact aactacatac ctcatcatat cc                                   32 

 
           
             25  
             26  
             DNA  
             Artificial  
             
               Oligonucleotide P3  
             
           
            25 

cctctctttc catatgctcc cttctc                                          26 

 
           
             26  
             33  
             DNA  
             Artificial  
             
               Oligonucleotide P4  
             
           
            26 

ccgccagcca cctccatatg accgacacca tcc                                  33 

 
           
             27  
             25  
             DNA  
             Artificial  
             
               Oligonucleotide P5  
             
           
            27 

cgccacccct catatgcgta tcgcc                                           25 

 
           
             28  
             34  
             DNA  
             Artificial  
             
               Oligonucleotide P6  
             
           
            28 

gatgcatctt tgcatatgat gaggtcagaa gatg                                 34 

 
           
             29  
             35  
             DNA  
             Artificial  
             
               Oligonucleotide P7  
             
           
            29 

cagtataatt agtagtcaag gatcctgact gagag                                35 

 
           
             30  
             31  
             DNA  
             Artificial  
             
               Oligonucleotide P8  
             
           
            30 

gctaaaactc ttctccttca atacttacct g                                    31