Expressed sequences of arabidopsis thaliana

CROSS-REFERENCE TO RELATED APPLICATION

[0001] This application claims the benefit of U.S. Provisional Application 60/178,503 Filed Jan. 27, 2000.

FIELD OF INVENTION

[0002] The invention is in the field of polynucleotide sequences of a plant, particularly sequences expressed in arabidopsis thaliana.

BACKGROUND OF THE INVENTION

[0003] Plants and plant products have vast commercial importance in a wide variety of areas including food crops for human and animal consumption, flavor enhancers for food, and production of specialty chemicals for use in products such as medicaments and fragrances. In considering food crops for humans and livestock, genes such as those involved in a plants resistance to insects, plant viruses, and fungi; genes involved in pollination; and genes whose products enhance the nutritional value of the food, are of major importance. A number of such genes have been described, see, for example, McCaskill and Croteau (1999) Nature Biotechnol. 17:31-36.

[0004] Despite recent advances in methods for identification, cloning, and characterization of genes, much remains to be learned about plant physiology in general, including how plants produce many of the above-mentioned products; mechanisms for resistance to herbicides, insects, plant viruses, fungi; elucidation of genes involved in specific biosynthetic pathways; and genes involved in environmental tolerance, e.g., salt tolerance, drought tolerance, or tolerance to anaerobic conditions.

[0005]

Arabidopsis thaliana
is a model system for genetic, molecular and biochemical studies of higher plants. Features of this plant that make it a model system for genetic and molecular biology research include a small genome size, organized into five chromosomes and containing an estimated 20,000 genes, a rapid life cycle, prolific seed production and, since it is small, it can easily be cultivation in limited space. A. thaliana is a member of the mustard family (Brassicaceae) with a broad natural distribution throughout Europe, Asia, and North America. Many different ecotypes have been collected from natural populations and are available for experimental analysis. The entire life cycle, including seed germination, formation of a rosette plant, bolting of the main stem, flowering, and maturation of the first seeds, is completed in 6 weeks. A large number of mutant lines are available that affect nearly all aspects of its growth. These features greatly facilitate the isolation of fundamentally interesting and potentially important genes for agronomic development

[0006] Most gene products from higher plants exhibit adequate sequence similarity to deduced amino acid sequences of other plant genes to permit assignment of probable gene function, if it is known, in any higher plant. It is likely that there will be very few protein-encoding angiosperm genes that do not have orthologs or paralogs in Arabidopsis. The developmental diversity of higher plants may be largely due to changes in the cis-regulatory sequences of transcriptional regulators and not in coding sequences.

[0007] Many advances reported over the past few years offer clear evidence that this plant is not only a very important model species for basic research, but also extremely valuable for applied plant scientists and plant breeders. Knowledge gained from Arabidopsis can be used directly to develop desired traits in plants of other species.

RELEVANT LITERATURE

[0008] Cold Spring Harbor Monograph 27 (1994) E. M. Meyerowitz and C. R. Somerville, eds. (CSH Laboratory Press). Annual Plant Reviews, Vol. 1: Arabidopsis (1998) M. Anderson and J. A. Roberts, eds. (CRC Press). Methods in Molecular Biology: Arabidopsis Protocols, Vol. 82 (1997) J. M. Martinez-Zapater and J. Salinas, eds. (CRC Press).

[0009] Mayer et al (1999) Nature 402(6763):769-77; Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana. Lin et al. (1999) 402(6763):761-8, “Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana”. Meinke et al. (1998) Science 282:662-682, “Arabidopsis thaliana”: a model plant for genome analysis. Somerville and Somerville (1999) Science 285:380-383, “Plant functional genomics”. Mozo et al. (1999) Nat. Genet. 22:271-275, “A complete BAC-based physical map of the Arabidopsis thaliana genome”.

SUMMARY OF THE INVENTION

[0010] Novel nucleic acid sequences of Arabidopsis thaliana, their encoded polypeptides and variants thereof, genes corresponding to these nucleic acids, and proteins expressed by the genes, are provided.

[0011] The invention also provides diagnostic, prophylactic and therapeutic agents employing such novel nucleic acids, their corresponding genes or gene products, including expression constructs, probes, antisense constructs, and the like. The genetic sequences may also be used for the genetic manipulation of plant cells, particularly dicotyledonous plants. The encoded gene products and modified organisms are useful for introducing or improving disease resistance and stress tolerance into plants; screening of biologically active agents, e.g. fungicides, etc.; for elucidating biochemical pathways; and the like.

[0012] In one embodiment of the invention, a nucleic acid is provided that comprises a start codon; an optional intervening sequence; a coding sequence capable of hybridizing under stringent conditions as set forth in SEQ ID NO:1 to 999; and an optional terminal sequence, wherein at least one of said optional sequences is present. Such a nucleic acid may correspond to naturally occurring Arabidopsis expressed sequences.

DETAILED DESCRIPTION OF THE INVENTION

[0013] Novel nucleic acid sequences from Arabidopsis thaliana, their encoded polypeptides and variants thereof, genes corresponding to these nucleic acids and proteins expressed by the genes are provided. The invention also provides agents employing such novel nucleic acids, their corresponding genes or gene products, including expression constructs, probes, antisense constructs, and the like. The nucleotide sequences are provided in the attached SEQLIST.

[0014] Sequences include, but are not limited to, sequences that encode resistance proteins; sequences that encode tolerance factors; sequences encoding proteins or other factors that are involved, directly or indirectly in biochemical pathways such as metabolic or biosynthetic pathways, sequences involved in signal transduction, sequences involved in the regulation of gene expression, structural genes, and the like. Biosynthetic pathways of interest include, but are not limited to, biosynthetic pathways whose product (which may be an end product or an intermediate) is of commercial, nutritional, or medicinal value.

[0015] The sequences may be used in screening assays of various plant strains to determine the strains that are best capable of withstanding a particular disease or environmental stress. Sequences encoding activators and resistance proteins may be introduced into plants that are deficient in these sequences. Alternatively, the sequences may be introduced under the control of promoters that are convenient for induction of expression. The protein products may be used in screening programs for insecticides, fungicides and antibiotics to determine agents that mimic or enhance the resistance proteins. Such agents may be used in improved methods of treating crops to prevent or treat disease. The protein products may also be used in screening programs to identify agents which mimic or enhance the action of tolerance factors. Such agents may be used in improved methods of treating crops to enhance their tolerance to environmental stresses.

[0016] Still other embodiments of the invention provide methods for enhancing or inhibiting production of a biosynthetic product in a plant by introducing a nucleic acid of the invention into a plant cell, where the nucleic acid comprises sequences encoding a factor which is involved, directly or indirectly in a biosynthetic pathway whose products are of commercial, nutritional, or medicinal value include any factor, usually a protein or peptide, which regulates such a biosynthetic pathway; which is an intermediate in such a biosynthetic pathway; or which in itself is a product that increases the nutritional value of a food product; or which is a medicinal product; or which is any product of commercial value.

[0017] Transgenic plants containing the antisense nucleic acids of the invention are useful for identifying other mediators that may induce expression of proteins of interest; for establishing the extent to which any specific insect and/or pathogen is responsible for damage of a particular plant; for identifying other mediators that may enhance or induce tolerance to environmental stress; for identifying factors involved in biosynthetic pathways of nutritional, commercial, or medicinal value; or for identifying products of nutritional, commercial, or medicinal value.

[0018] In still other embodiments, the invention provides transgenic plants constructed by introducing a subject nucleic acid of the invention into a plant cell, and growing the cell into a callus and then into a plant; or, alternatively by breeding a transgenic plant from the subject process with a second plant to form an F1 or higher hybrid. The subject transgenic plants and progeny are used as crops for their enhanced disease resistance, enhanced traits of interest, for example size or flavor of fruit, length of growth cycle, etc., or for screening programs, e.g. to determine more effective insecticides, etc; used as crops which exhibit enhanced tolerance environmental stress; or used to produce a factor.

[0019] Those skilled in the art will recognize the agricultural advantages inherent in plants constructed to have either increased or decreased expression of resistance proteins; or increased or decreased tolerance to environmental factors; or which produce or over-produce one or more factors involved in a biosynthetic pathway whose product is of commercial, nutritional, or medicinal value. For example, such plants may have increased resistance to attack by predators, insects, pathogens, microorganisms, herbivores, mechanical damage and the like; may be more tolerant to environmental stress, e.g. may be better able to withstand drought conditions, freezing, and the like; or may produce a product not normally made in the plant, or may produce a product in higher than normal amounts, where the product has commercial, nutritional, or medicinal value. Plants which may be useful include dicotyledons and monocotyledons. Representative examples of plants in which the provided sequences may be useful include tomato, potato, tobacco, cotton, soybean, alfalfa, rape, and the like. Monocotyledons, more particularly grasses (Poaceae family) of interest, include, without limitation, Avena sativa (oat); Avena strigosa (black oat); Elymus (wild rye); Hordeum sp. including Hordeum vulgare (barley); Oryza sp., including Oryza glaberrima (African rice); Oryza longistaminata (long-staminate rice); Pennisetum americanum (pearl millet); Sorghum sp. (sorghum); Triticum sp., including Triticum aestivum (common wheat); Triticum durum (durum wheat); Zea mays (corn); etc.

NUCLEIC ACID COMPOSITIONS

[0020] The following detailed description describes the nucleic acid compositions encompassed by the invention, methods for obtaining cDNA or genomic DNA encoding a full-length gene product, expression of these nucleic acids and genes; identification of structural motifs of the nucleic acids and genes; identification of the function of a gene product encoded by a gene corresponding to a nucleic acid of the invention; use of the provided nucleic acids as probes, in mapping, and in diagnosis; use of the corresponding polypeptides and other gene products to raise antibodies; use of the nucleic acids in genetic modification of plant and other species; and use of the nucleic acids, their encoded gene products, and modified organisms, for screening and diagnostic purposes.

[0021] The scope of the invention with respect to nucleic acid compositions includes, but is not necessarily limited to, nucleic acids having a sequence set forth in any one of SEQ ID NOS:1-999; nucleic acids that hybridize the provided sequences under stringent conditions; genes corresponding to the provided nucleic acids; variants of the provided nucleic acids and their corresponding genes, particularly those variants that retain a biological activity of the encoded gene product.

[0022] In one embodiment, the sequences of the invention provide a polypeptide coding sequence. The polypeptide coding sequence may correspond to a naturally expressed mRNA in Arabidopsis or other species, or may encode a fusion protein between one of the provided sequences and an exogenous protein coding sequence. The coding sequence is characterized by an ATG start codon, a lack of stop codons in-frame with the ATG, and a termination codon, that is, a continuous open frame is provided between the start and the stop codon. The sequence contained between the start and the stop codon will comprise a sequence capable of hybridizing under stringent conditions to a sequence set for in SEQ ID NO:1-999, and may comprise the sequence set forth in the Seqlist.

[0023] Other nucleic acid compositions contemplated by and within the scope of the present invention will be readily apparent to one of ordinary skill in the art when provided with the disclosure here.

[0024] The invention features nucleic acids that are derived from Arabidopsis thaliana. Novel nucleic acid compositions of the invention of particular interest comprise a sequence set forth in any one of SEQ ID NOS:1-999 or an identifying sequence thereof. An identifying sequence is a contiguous sequence of residues at least about 10 nt to about 20 nt in length, usually at least about 50 nt to about 100 nt in length, that uniquely identifies a nucleic acid sequence, e.g., exhibits less than 90%, usually less than about 80% to about 85% sequence identity to any contiguous nucleotide sequence of more than about 20 nt. Thus, the subject novel nucleic acid compositions include full length cDNAs or mRNAs that encompass an identifying sequence of contiguous nucleotides from any one of SEQ ID NOS:1-999.

[0025] The nucleic acids of the invention also include nucleic acids having sequence similarity or sequence identity. Nucleic acids having sequence similarity are detected by hybridization under low stringency conditions, for example, at 50° C. and 10×SSC (0.9 M NaCl/0.09 M sodium citrate) and remain bound when subjected to washing at 55° C. in 1×SSC. Sequence identity can be determined by hybridization under stringent conditions, for example, at 50° C. or higher and 0.1×SSC (9 mM NaCl/0.9 mM sodium citrate). Hybridization methods and conditions are well known in the art, see U.S. Pat. No. 5,707,829. Nucleic acids that are substantially identical to the provided nucleic acid sequences, e.g. allelic variants, genetically altered versions of the gene, etc., bind to the provided nucleic acid sequences (SEQ ID NOS:1-999) under stringent hybridization conditions. By using probes, particularly labeled probes of DNA sequences, one can isolate homologous or related genes. The source of homologous genes can be any species, particularly grasses as previously described.

[0026] Preferably, hybridization is performed using at least 15 contiguous nucleotides of at least one of SEQ ID NOS:1-999. The probe will preferentially hybridize with a nucleic acid or mRNA comprising the complementary sequence, allowing the identification and retrieval of the nucleic acids of the biological material that uniquely hybridize to the selected probe. Probes of more than 15 nucleotides can be used, e.g. probes of from about 18 nucleotides up to the entire length of the provided nucleic acid sequences, but 15 nucleotides generally represents sufficient sequence for unique identification.

[0027] The nucleic acids of the invention also include naturally occurring variants of the nucleotide sequences, e.g. degenerate variants, allelic variants, etc. Variants of the nucleic acids of the invention are identified by hybridization of putative variants with nucleotide sequences disclosed herein, preferably by hybridization under stringent conditions For example, by using appropriate wash conditions, variants of the nucleic acids of the invention can be identified where the allelic variant exhibits at most about 25-30% base pair mismatches relative to the selected nucleic acid probe. In general, allelic variants contain 5-25% base pair mismatches, and can contain as little as even 2-5%, or 1-2% base pair mismatches, as well as a single base-pair mismatch.

[0028] The invention also encompasses homologs corresponding to the nucleic acids of SEQ ID NOS:1-999, where the source of homologous genes can be any related species, usually within the same genus or group. Homologs have substantial sequence similarity, e.g. at least 75% sequence identity, usually at least 90%, more usually at least 95% between nucleotide sequences. Sequence similarity is calculated based on a reference sequence, which may be a subset of a larger sequence, such as a conserved motif, coding region, flanking region, etc. A reference sequence will usually be at least about 18 contiguous nt long, more usually at least about 30 nt long, and may extend to the complete sequence that is being compared. Algorithms for sequence analysis are known in the art, such as BLAST, described in Altschul et al., J. Mol. Biol. (1990) 215:403-10.

[0029] In general, variants of the invention have a sequence identity greater than at least about 65%, preferably at least about 75%, more preferably at least about 85%, and can be greater than at least about 90% or more as determined by the Smith-Waterman homology search algorithm as implemented in MPSRCH program (Oxford Molecular). For the purposes of this invention, a preferred method of calculating percent identity is the Smith-Waterman algorithm, using the following. Global DNA sequence identity must be greater than 65% as determined by the Smith-Waterman homology search algorithm as implemented in MPSRCH program (Oxford Molecular) using an affine gap search with the following search parameters: gap open penalty, 12; and gap extention penalty, 1.

[0030] The subject nucleic acids can be cDNAs or genomic DNAs, as well as fragments thereof, particularly fragments that encode a biologically active gene product and/or are useful in the methods disclosed herein. The term cDNA as used herein is intended to include all nucleic acids that share the arrangement of sequence elements found in native mature mRNA species, where sequence elements are exons and 3′ and 5 ′ non-coding regions. Normally mRNA species have contiguous exons, with the introns, when present, being removed by nuclear RNA splicing, to create a continuous open reading frame encoding a polypeptide of the invention.

[0031] A genomic sequence of interest comprises the nucleic acid present between the initiation codon and the stop codon, as defined in the listed sequences, including all of the introns that are normally present in a native chromosome. It can further include the 3′ and 5′ untranslated regions found in the mature mRNA. It can further include specific transcriptional and translational regulatory sequences, such as promoters, enhancers, etc., including about 1 kb, but possibly more, of flanking genomic DNA at either the 5′ and 3′ end of the transcribed region. The genomic DNA can be isolated as a fragment of 100 kb or smaller; and substantially free of flanking chromosomal sequence. The genomic DNA flanking the coding region, either 3′ and 5′, or internal regulatory sequences as sometimes found in introns, contains sequences required for expression.

[0032] The nucleic acid compositions of the subject invention can encode all or a part of the subject expressed polypeptides. Double or single stranded fragments can be obtained from the DNA sequence by chemically synthesizing oligonucleotides in accordance with conventional methods, by restriction enzyme digestion, by PCR amplification, etc. Isolated nucleic acids and nucleic acid fragments of the invention comprise at least about 15 up to about 100 contiguous nucleotides, or up to the complete sequence provided in SEQ ID NOS:1-999. For the most part, fragments will be of at least 15 nt, usually at least 18 nt or 25 nt, and up to at least about 50 contiguous nt in length or more.

[0033] Probes specific to the nucleic acids of the invention can be generated using the nucleic acid sequences disclosed in SEQ ID NOS:1-999 and the fragments as described above. The probes can be synthesized chemically or can be generated from longer nucleic acids using restriction enzymes. The probes can be labeled, for example, with a radioactive, biotinylated, or fluorescent tag. Preferably, probes are designed based upon an identifying sequence of a nucleic acid of one of SEQ ID NOS:1-999. More preferably, probes are designed based on a contiguous sequence of one of the subject nucleic acids that remain unmasked following application of a masking program for masking low complexity (e.g., XBLAST) to the sequence., i.e. one would select an unmasked region, as indicated by the nucleic acids outside the poly-n stretches of the masked sequence produced by the masking program.

[0034] The nucleic acids of the subject invention are isolated and obtained in substantial purity, generally as other than an intact chromosome. Usually, the nucleic acids, either as DNA or RNA, will be obtained substantially free of other naturally-occurring nucleic acid sequences, generally being at least about 50%, usually at least about 90% pure and are typically recombinant, e.g., flanked by one or more nucleotides with which it is not normally associated on a naturally occurring chromosome.

[0035] The nucleic acids of the invention can be provided as a linear molecule or within a circular molecule. They can be provided within autonomously replicating molecules (vectors) or within molecules without replication sequences. They can be regulated by their own or by other regulatory sequences, as is known in the art. The nucleic acids of the invention can be introduced into suitable host cells using a variety of techniques which are available in the art, such as transferrin polycation-mediated DNA transfer, transfection with naked or encapsulated nucleic acids, liposome-mediated DNA transfer, intracellular transportation of DNA-coated latex beads, protoplast fusion, viral infection, electroporation, gene gun, calcium phosphate-mediated transfection, and the like.

[0036] The subject nucleic acid compositions can be used to, for example, produce polypeptides, as probes for the detection of mRNA of the invention in biological samples, e.g. extracts of cells, to generate additional copies of the nucleic acids, to generate ribozymes or antisense oligonucleotides, and as single stranded DNA probes or as triple-strand forming oligonucleotides. The probes described herein can be used to, for example, determine the presence or absence of the nucleic acid sequences as shown in SEQ ID NOS:1-999 or variants thereof in a sample. These and other uses are described in more detail below.

USE OF NUCLEIC ACIDS AS CODING SEQUENCES

[0037] Naturally occurring Arabidopsis polypeptides or fragments thereof are encoded by the provided nucleic acids. Methods are known in the art to determine whether the complete native protein is encoded by a candidate nucleic acid sequence. Where the provided sequence encodes a fragment of a polypeptide, methods known in the art may be used to determine the remaining sequence. These approaches may utilize a bioinformatics approach, a cloning approach, extension of mRNA species, etc.

[0038] Substantial genomic sequence is available for Arabidopsis, and may be exploited for determining the complete coding sequence corresponding to the provided sequences. The region of the chromosome to which a given sequence is located may be determined by hybridization or by database searching. The genomic sequence is then searched upstream and downstream for the presence of intron/exon boundaries, and for motifs characteristic of transcriptional start and stop sequences, for example by using Genscan (Burge and Karlin (1997) J. Mol. Biol. 268:78-94); or GRAIL (Uberbacher and Mural (1991) P.N.A.S. 88:11261-1265).

[0039] Alternatively, nucleic acid having a sequence of one of SEQ ID NOS:1-999, or an identifying fragment thereof, is used as a hybridization probe to complementary molecules in a cDNA library using probe design methods, cloning methods, and clone selection techniques as known in the art. Libraries of cDNA are made from selected cells. The cells may be those of A. thaliana, or of related species. In some cases it will be desirable to select cells from a particular stage, e.g. seeds, leaves, infected cells, etc.

[0040] Techniques for producing and probing nucleic acid sequence libraries are described, for example, in Sambrook et al., Molecular Cloning: A Laboratory Manual, 2nd Ed., (1989) Cold Spring Harbor Press, Cold Spring Harbor, N.Y.; and Current Protocols in Molecular Biology, (1987 and updates) Ausubel et al., eds. The cDNA can be prepared by using primers based on sequence from SEQ ID NOS:1-999. In one embodiment, the cDNA library can be made from only poly-adenylated mRNA. Thus, poly-T primers can be used to prepare cDNA from the mRNA.

[0041] Members of the library that are larger than the provided nucleic acids, and preferably that encompass the complete coding sequence of the native message, are obtained. In order to confirm that the entire cDNA has been obtained, RNA protection experiments are performed as follows. Hybridization of a full-length cDNA to an mRNA will protect the RNA from RNase degradation. If the cDNA is not full length, then the portions of the mRNA that are not hybridized will be subject to RNase degradation. This is assayed, as is known in the art, by changes in electrophoretic mobility on polyacrylamide gels, or by detection of released monoribonucleotides. Sambrook et al., Molecular Cloning: A Laboratory Manual, 2nd Ed., (1989) Cold Spring Harbor Press, Cold Spring Harbor, N.Y. In order to obtain additional sequences 5′ to the end of a partial cDNA, 5′ RACE (PCR Protocols: A Guide to Methods and Applications, (1990) Academic Press, Inc.) may be performed.

[0042] Genomic DNA is isolated using the provided nucleic acids in a manner similar to the isolation of full-length cDNAs. Briefly, the provided nucleic acids, or portions thereof, are used as probes to libraries of genomic DNA. Preferably, the library is obtained from the cell type that was used to generate the nucleic acids of the invention, but this is not essential. Such libraries can be in vectors suitable for carrying large segments of a genome, such as P1 or YAC, as described in detail in Sambrook et al., 9.4-9.30. In order to obtain additional 5′ or 3′ sequences, chromosome walking is performed, as described in Sambrook et a/., such that adjacent and overlapping fragments of genomic DNA are isolated. These are mapped and pieced together, as is known in the art, using restriction digestion enzymes and DNA ligase.

[0043] PCR methods may be used to amplify the members of a cDNA library that comprise the desired insert. In this case, the desired insert will contain sequence from the full length cDNA that corresponds to the instant nucleic acids. Such PCR methods include gene trapping and RACE methods. Gene trapping entails inserting a member of a cDNA library into a vector. The vector then is denatured to produce single stranded molecules. Next, a substrate-bound probe, such a biotinylated oligo, is used to trap cDNA inserts of interest. Biotinylated probes can be linked to an avidin-bound solid substrate. PCR methods can be used to amplify the trapped cDNA. To trap sequences corresponding to the full length genes, the labeled probe sequence is based on the nucleic acid sequences of the invention. Random primers or primers specific to the library vector can be used to amplify the trapped cDNA. Such gene trapping techniques are described in Gruber et aL., WO 95/04745 and Gruber et al., U.S. Pat. No. 5,500,356. Kits are commercially available to perform gene trapping experiments from, for example, Life Technologies, Gaithersburg, Md., USA.

[0044] “Rapid amplification of cDNA ends”, or RACE, is a PCR method of amplifying cDNAs from a number of different RNAs. The cDNAs are ligated to an oligonucleotide linker, and amplified by PCR using two primers. One primer is based on sequence from the instant nucleic acids, for which full length sequence is desired, and a second primer comprises sequence that hybridizes to the oligonucleotide linker to amplify the cDNA. A description of this methods is reported in WO 97/19110. A common primer may be designed to anneal to an arbitrary adaptor sequence ligated to cDNA ends. When a single gene-specific RACE primer is paired with the common primer, preferential amplification of sequences between the single gene specific primer and the common primer occurs. Commercial cDNA pools modified for use in RACE are available.

[0045] Once the full-length cDNA or gene is obtained, DNA encoding variants can be prepared by site-directed mutagenesis, described in detail in Sambrook et al., 15.3-15.63. The choice of codon or nucleotide to be replaced can be based on disclosure herein on optional changes in amino acids to achieve altered protein structure and/or function. As an alternative method to obtaining DNA or RNA from a biological material, nucleic acid comprising nucleotides having the sequence of one or more nucleic acids of the invention can be synthesized.

EXPRESSION OF POLYPEPTIDES

[0046] The provided nucleic acid, e.g. a nucleic acid having a sequence of one of SEQ ID NOS:1-999), the corresponding cDNA, the polypeptide coding sequence as described above, or the full-length gene is used to express a partial or complete gene product. Constructs of nucleic acids having sequences of SEQ ID NOS:1-999 can be generated by recombinant methods, synthetically, or in a single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides is described by, e.g. Stemmer et al., Gene (Amsterdam) (1995) 164(1):49-53.

[0047] Appropriate nucleic acid constructs are purified using standard recombinant DNA techniques as described in, for example, Sambrook et al., Molecular Cloning: A Laboratory Manual, 2nd Ed., (1989) Cold Spring Harbor Press, Cold Spring Harbor, N.Y. The gene product encoded by a nucleic acid of the invention is expressed in any expression system, including, for example, bacterial, yeast, insect, amphibian and mammalian systems.

[0048] The subject nucleic acid molecules are generally propagated by placing the molecule in a vector. Viral and non-viral vectors are used, including plasmids. The choice of plasmid will depend on the type of cell in which propagation is desired and the purpose of propagation. Certain vectors are useful for amplifying and making large amounts of the desired DNA sequence. Other vectors are suitable for expression in cells in culture. Still other vectors are suitable for transfer and expression in cells in a whole organism or person. The choice of appropriate vector is well within the skill of the art. Many such vectors are available commercially.

[0049] The nucleic acids set forth in SEQ ID NOS:1-999 or their corresponding full-length nucleic acids are linked to regulatory sequences as appropriate to obtain the desired expression properties. These can include promoters attached either at the 5′ end of the sense strand or at the 3′ end of the antisense strand, enhancers, terminators, operators, repressors, and inducers. The promoters can be regulated or constitutive. In some situations it may be desirable to use conditionally active promoters, such as tissue-specific or developmental stage-specific promoters. These are linked to the desired nucleotide sequence using the techniques described above for linkage to vectors. Any techniques known in the art can be used.

[0050] When any of the above host cells, or other appropriate host cells or organisms, are used to replicate and/or express the nucleic acids or nucleic acids of the invention, the resulting replicated nucleic acid, RNA, expressed protein or polypeptide, is within the scope of the invention as a product of the host cell or organism. The product is recovered by any appropriate means known in the art.

IDENTIFICATION OF FUNCTIONAL AND STRUCTURAL MOTIFS

[0051] Translations of the nucleotide sequence of the provided nucleic acids, cDNAs or full genes can be aligned with individual known sequences. Similarity with individual sequences can be used to determine the activity of the polypeptides encoded by the nucleic acids of the invention. Also, sequences exhibiting similarity with more than one individual sequence can exhibit activities that are characteristic of either or both individual sequences.

[0052] The six possible reading frames may be translated using programs such as GCG pepdata, or GCG Frames (Wisconsin Package Version 10.0, Genetics Computer Group (GCG) , Madison, Wis., USA. ). Programs such as ORFFinder (National Center for Biotechnology Information (NCBI) a division of the National Library of Medicine (NLM) at the National Institutes of Health (NIH) http://www.ncbi.nlm.nih.gov/) may be used to identify open reading frames (ORFs) in sequences. ORF finder identifies all possible ORFs in a DNA sequence by locating the standard and alternative stop and start codons. Other ORF identification programs include Genie (Kulp et al. (1996).

[0053] A generalized Hidden Markov Model may be used for the recognition of genes in DNA. (ISMB-96, St. Louis, Mo., AAAI/MIT Press; Reese et al. (1997), “Improved splice site detection in Genie”. Proceedings of the First Annual International Conference on Computational Molecular Biology RECOMB 1997, Santa Fe, N.M., ACM Press, New York., P. 34.); BESTORF—Prediction of potential coding fragment in human or plant EST/mRNA sequence data using Markov Chain Models; and FGENEP—Multiple genes structure prediction in plant genomic DNA (Solovyev et al. (1995) Identification of human gene structure using linear discriminant functions and dynamic programming. In Proceedings of the Third International Conference on Intelligent Systems for Molecular Biology eds. Rawling et al. Cambridge, England, AAAI Press,367-375.; Solovyev et al. (1994) Nucl. Acids Res. 22(24):5156-5163; Solovyev et al,. The prediction of human exons by oligonucleotide composition and discriminant analysis of spliceable open reading frames, in: The Second International conference on Intelligent systems for Molecular Biology (eds. Altman et al.), AAAI Press, Menlo Park, Calif. (1994, 354-362) Solovyev and Lawrence, Prediction of human gene structure using dynamic programming and oligonucleotide composition, In: Abstracts of the 4th annual Keck symposium. Pittsburgh, 47,1993; Burge and Karlin (1997) J. Mol. Biol. 268:78-94; Kulp et al. (1996) Proc. Conf. on Intelligent Systems in Molecular Biology '96, 134-142).

[0054] The full length sequences and fragments of the nucleic acid sequences of the nearest neighbors can be used as probes and primers to identify and isolate the full length sequence corresponding to provided nucleic acids. Typically, a selected nucleic acid is translated in all six frames to determine the best alignment with the individual sequences. These amino acid sequences are referred to, generally, as query sequences, which are aligned with the individual sequences. Suitable databases include Genbank, EMBL, and DNA Database of Japan (DDBJ).

[0055] Query and individual sequences can be aligned using the methods and computer programs described above, and include BLAST, available by ftp at ftp://ncbi.nlm.nih.gov/.

[0056] Gapped BLAST and PSI-BLAST are useful search tools provided by NCBI. (version 2.0) (Altschul et al., 1997). Position-Specific Iterated BLAST (PSI-BLAST) provides an automated, easy-to-use version of a profile search, which is a sensitive way to look for sequence homologues. The program first performs a gapped BLAST database search. The PSI-BLAST program uses the information from any significant alignments returned to construct a position-specific score matrix, which replaces the query sequence for the next round of database searching. PSI-BLAST may be iterated until no new significant alignments are found. The Gapped BLAST algorithm allows gaps (deletions and insertions) to be introduced into the alignments that are returned. Allowing gaps means that similar regions are not broken into several segments. The scoring of these gapped alignments tends to reflect biological relationships more closely. The Smith-Waterman is another algorithm that produces local or global gapped sequence alignments, see Meth. Mol. Biol. (1997) 70: 173-187. Also, the GAP program using the Needleman and Wunsch global alignment method can be utilized for sequence alignments.

[0057] Results of individual and query sequence alignments can be divided into three categories, high similarity, weak similarity, and no similarity. Individual alignment results ranging from high similarity to weak similarity provide a basis for determining polypeptide activity and/or structure. Parameters for categorizing individual results include: percentage of the alignment region length where the strongest alignment is found, percent sequence identity, and e value.

[0058] The percentage of the alignment region length is calculated by counting the number of residues of the individual sequence found in the region of strongest alignment, e.g. contiguous region of the individual sequence that contains the greatest number of residues that are identical to the residues of the corresponding region of the aligned query sequence. This number is divided by the total residue length of the query sequence to calculate a percentage. For example, a query sequence of 20 amino acid residues might be aligned with a 20 amino acid region of an individual sequence. The individual sequence might be identical to amino acid residues 5, 9-15, and 17-19 of the query sequence. The region of strongest alignment is thus the region stretching from residue 9-19, an 11 amino acid stretch. The percentage of the alignment region length is: 11 (length of the region of strongest alignment) divided by (query sequence length) 20 or 55%.

[0059] Percent sequence identity is calculated by counting the number of amino acid matches between the query and individual sequence and dividing total number of matches by the number of residues of the individual sequences found in the region of strongest alignment. Thus, the percent identity in the example above would be 10 matches divided by 11 amino acids, or approximately, 90.9%

[0060] E value is the probability that the alignment was produced by chance. For a single alignment, the e value can be calculated according to Karlin et al., Proc. Natl. Acad. Sci. (1990) 87:2264 and Karlin et al., Proc. Natl. Acad. Sci. (1993) 90. The e value of multiple alignments using the same query sequence can be calculated using an heuristic approach described in Altschul et al., Nat. Genet. (1994) 6:119. Alignment programs such as BLAST program can calculate the e value.

[0061] Another factor to consider for determining identity or similarity is the location of the similarity or identity. Strong local alignment can indicate similarity even if the length of alignment is short. Sequence identity scattered throughout the length of the query sequence also can indicate a similarity between the query and profile sequences. The boundaries of the region where the sequences align can be determined according to Doolittle, supra; BLAST or FASTA programs; or by determining the area where sequence identity is highest.

[0062] In general, in alignment results considered to be of high similarity, the percent of the alignment region length is typically at least about 55% of total length query sequence; more typically, at least about 58%; even more typically; at least about 60% of the total residue length of the query sequence. Usually, percent length of the alignment region can be as much as about 62%; more usually, as much as about 64%; even more usually, as much as about 66%. Further, for high similarity, the region of alignment, typically, exhibits at least about 75% of sequence identity; more typically, at least about 78%; even more typically; at least about 80% sequence identity. Usually, percent sequence identity can be as much as about 82%; more usually, as much as about 84%; even more usually, as much as about 86%.

[0063] The p value is used in conjunction with these methods. The query sequence is considered to have a high similarity with a profile sequence when the p value is less than or equal to 10−2. Confidence in the degree of similarity between the query sequence and the profile sequence increases as the p value become smaller.

[0064] In general, where alignment results considered to be of weak similarity, there is no minimum percent length of the alignment region nor minimum length of alignment. A better showing of weak similarity is considered when the region of alignment is, typically, at least about 15 amino acid residues in length; more typically, at least about 20; even more typically; at least about 25 amino acid residues in length. Usually, length of the alignment region can be as much as about 30 amino acid residues; more usually, as much as about 40; even more usually, as much as about 60 amino acid residues. Further, for weak similarity, the region of alignment, typically, exhibits at least about 35% of sequence identity; more typically, at least about 40%; even more typically; at least about 45% sequence identity. Usually, percent sequence identity can be as much as about 50%; more usually, as much as about 55%; even more usually, as much as about 60%.

[0065] The query sequence is considered to have a low similarity with a profile sequence when the p value is greater than 10−2. Confidence in the degree of similarity between the query sequence and the profile sequence decreases as the p values become larger.

[0066] Sequence identity alone can be used to determine similarity of a query sequence to an individual sequence and can indicate the activity of the sequence. Such an alignment, preferably, permits gaps to align sequences. Typically, the query sequence is related to the profile sequence if the sequence identity over the entire query sequence is at least about 15%; more typically, at least about 20%; even more typically, at least about 25%; even more typically, at least about 50%. Sequence identity alone as a measure of similarity is most useful when the query sequence is usually, at least 80 residues in length; more usually, 90 residues; even more usually, at least 95 amino acid residues in length. More typically, similarity can be concluded based on sequence identity alone when the query sequence is preferably 100 residues in length; more preferably, 120 residues in length; even more preferably, 150 amino acid residues in length.

[0067] It is apparent, when studying protein sequence families, that some regions have been better conserved than others during evolution. These regions are generally important for the function of a protein and/or for the maintenance of its three-dimensional structure. By analyzing the constant and variable properties of such groups of similar sequences, it is possible to derive a signature for a protein family or domain, which distinguishes its members from all other unrelated proteins. A pertinent analogy is the use of fingerprints by the police for identification purposes. A fingerprint is generally sufficient to identify a given individual. Similarly, a protein signature can be used to assign a new sequence to a specific family of proteins and thus to formulate hypotheses about its function. The PROSITE database is a compendium of such fingerprints (motifs) and may be used with search software such as Wisconsin GCG Motifs to find motifs or fingerprints in query sequences. PROSITE currently contains signatures specific for about a thousand protein families or domains. Each of these signatures comes with documentation providing background information on the structure and function of these proteins (Hofmann et al. (1999) Nucleic Acids Res. 27:215-219; Bucher and Bairoch., A generalized profile syntax for biomolecular sequences motifs and its function in automatic sequence interpretation (In) ISMB-94; Proceedings 2nd International Conference on Intelligent Systems for Molecular Biology; Altman et al. Eds. (1994), pp 53-61, AAAI Press, Menlo Park).

[0068] Translations of the provided nucleic acids can be aligned with amino acid profiles that define either protein families or common motifs. Also, translations of the provided nucleic acids can be aligned to multiple sequence alignments (MSA) comprising the polypeptide sequences of members of protein families or motifs. Similarity or identity with profile sequences or MSAs can be used to determine the activity of the gene products (e.g., polypeptides) encoded by the provided nucleic acids or corresponding cDNA or genes.

[0069] Profiles can designed manually by (1) creating an MSA, which is an alignment of the amino acid sequence of members that belong to the family and (2) constructing a statistical representation of the alignment. Such methods are described, for example, in Birney et al., Nucl. Acid Res. (1996) 24(14): 2730-2739. MSAs of some protein families and motifs are available for downloading to a local server. For example, the PFAM database with MSAs of 547 different families and motifs, and the software (HMMER) to search the PFAM database may be downloaded from ftp://ftp.genetics.wustl.edu/pub/eddy/pfam-4.4/ to allow secure searches on a local server. Pfam is a database of multiple alignments of protein domains or conserved protein regions., which represent evolutionary conserved structure that has implications for the proteins function (Sonnhammer et al. (1998) Nucl. Acid Res. 26:320-322; Bateman et al. (1999) Nucleic Acids Res. 27:260-262).

[0070] The 3D_ali databank (Pasarella, S. and Argos, P. (1992) Prot. Engineering 5:121-137) was constructed to incorporate new protein structural and sequence data. The databank has proved useful in many research fields such as protein sequence and structure analysis and comparison, protein folding, engineering and design and evolution. The collection enhances present protein structural knowledge by merging information from proteins of similar main-chain fold with homologous primary structures taken from large databases of all known sequences. 3D_ali databank files may be downloaded to a secure local server from http://www.embl-heidelberg.de/argos/ali/ali_form.html.

[0071] The identify and function of the gene that correlates to a nucleic acid described herein can be determined by screening the nucleic acids or their corresponding amino acid sequences against profiles of protein families. Such profiles focus on common structural motifs among proteins of each family. Publicly available profiles are known in the art.

[0072] In comparing a novel nucleic acid with known sequences, several alignment tools are available. Examples include PileUp, which creates a multiple sequence alignment, and is described in Feng et al., J. Mol. Evol. (1987) 25:351. Another method, GAP, uses the alignment method of Needleman et al., J. Mol. Biol. (1970) 48:443. GAP is best suited for global alignment of sequences. A third method, BestFit, functions by inserting gaps to maximize the number of matches using the local homology algorithm of Smith et al. (1981) Adv. Appl. Math. 2:482.

IDENTIFICATION OF SECRETED & MEMBRANE-BOUND POLYPEPTIDES

[0073] Secreted and membrane-bound polypeptides of the present invention are of interest. Because both secreted and membrane-bound polypeptides comprise a fragment of contiguous hydrophobic amino acids, hydrophobicity predicting algorithms can be used to identify such polypeptides. A signal sequence is usually encoded by both secreted and membrane-bound polypeptide genes to direct a polypeptide to the surface of the cell. The signal sequence usually comprises a stretch of hydrophobic residues. Such signal sequences can fold into helical structures. Membrane-bound polypeptides typically comprise at least one transmembrane region that possesses a stretch of hydrophobic amino acids that can transverse the membrane. Some transmembrane regions also exhibit a helical structure. Hydrophobic fragments within a polypeptide can be identified by using computer algorithms. Such algorithms include Hopp & Woods, Proc. Natl. Acad. Sci. USA (1981) 78:3824-3828; Kyte & Doolittle, J. Mol. Biol. (1982) 157: 105-132; and RAOAR algorithm, Degli Esposti et al., Eur. J. Biochem. (1990) 190: 207-219.

[0074] Another method of identifying secreted and membrane-bound polypeptides is to translate the nucleic acids of the invention in all six frames and determine if at least 8 contiguous hydrophobic amino acids are present. Those translated polypeptides with at least 8; more typically, 10; even more typically, 12 contiguous hydrophobic amino acids are considered to be either a putative secreted or membrane bound polypeptide. Hydrophobic amino acids include alanine, glycine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, proline, threonine, tryptophan, tyrosine, and valine.

IDENTIFICATION OF THE FUNCTION OF AN EXPRESSION PRODUCT

[0075] The biological function of the encoded gene product of the invention may be determined by empirical or deductive methods. One promising avenue, termed phylogenomics, exploits the use of evolutionary information to facilitate assignment of gene function. The approach is based on the idea that functional predictions can be greatly improved by focusing on how genes became similar in sequence during evolution instead of focusing on the sequence similarity itself. One of the major efficiencies that has emerged from plant genome research to date is that a large percentage of higher plant genes can be assigned some degree of function by comparing them with the sequences of genes of known function.

[0076] Alternatively, reverse genetics is used to identify gene function. Large collections of insertion mutants are available for Arabidopsis, maize, petunia, and snapdragon. These collections can be screened for an insertional inactivation of any gene by using the polymerase chain reaction (PCR) primed with oligonucleotides based on the sequences of the target gene and the insertional mutagen. The presence of an insertion in the target gene is indicated by the presence of a PCR product. By multiplexing DNA samples, hundreds of thousands of lines can be screened and the corresponding mutant plants can be identified with relatively small effort. Analysis of the phenotype and other properties of the corresponding mutant will provide an insight into the function of the gene.

[0077] In one method of the invention, the gene function in a transgenic Arabidopsis plant is assessed with anti-sense constructs. A high degree of gene duplication is apparent in Arabidopsis, and many of the gene duplications in Arabidopsis are very tightly linked. Large numbers of transgenic Arabidopsis plants can be generated by infecting flowers with Agrobacterium tumefaciens containing an insertional mutagen, a method of gene silencing based on producing double-stranded RNA from bidirectional transcription of genes in transgenic plants can be broadly useful for high-throughput gene inactivation (Clough and Bent (1999) Plant J. 17; Waterhouse et al. (1998) Proc. Natl. Acad. Sci. U.S.A. 95:13959). This method may use promoters that are expressed in only a few cell types or at a particular developmental stage or in response to an external stimulus. This could significantly obviate problems associated with the lethality of some mutations.

[0078] Virus-induced gene silencing may also find use for suppressing gene function. This method exploits the fact that some or all plants have a surveillance system that can specifically recognize viral nucleic acids and mount a sequence-specific suppression of viral RNA accumulation. By inoculating plants with a recombinant virus containing part of a plant gene, it is possible to rapidly silence the endogenous plant gene.

[0079] Antisense nucleic acids are designed to specifically bind to RNA, resulting in the formation of RNA-DNA or RNA-RNA hybrids, with an arrest of DNA replication, reverse transcription or messenger RNA translation. Antisense nucleic acids based on a selected nucleic acid sequence can interfere with expression of the corresponding gene. Antisense nucleic acids are typically generated within the cell by expression from antisense constructs that contain the antisense strand as the transcribed strand. Antisense nucleic acids based on the disclosed nucleic acids will bind and/or interfere with the translation of mRNA comprising a sequence complementary to the antisense nucleic acid. The expression products of control cells and cells treated with the antisense construct are compared to detect the protein product of the gene corresponding to the nucleic acid upon which the antisense construct is based. The protein is isolated and identified using routine biochemical methods.

[0080] As an alternative method for identifying function of the gene corresponding to a nucleic acid disclosed herein, dominant negative mutations are readily generated for corresponding proteins that are active as homomultimers. A mutant polypeptide will interact with wild-type polypeptides (made from the other allele) and form a non-functional multimer. Thus, a mutation is in a substrate-binding domain, a catalytic domain, or a cellular localization domain. Preferably, the mutant polypeptide will be overproduced. Point mutations are made that have such an effect. In addition, fusion of different polypeptides of various lengths to the terminus of a protein can yield dominant negative mutants. General strategies are available for making dominant negative mutants (see for example, Herskowitz (1987) Nature 329:219). Such techniques can be used to create loss of function mutations, which are useful for determining protein function.

[0081] Another approach for discovering the function of genes utilizes gene chips and microarrays. DNA sequences representing all the genes in an organism can be placed on miniature solid supports and used as hybridization substrates to quantitate the expression of all the genes represented in a complex mRNA sample. This information is used to provide extensive databases of quantitative information about the degree to which each gene responds to pathogens, pests, drought, cold, salt, photoperiod, and other environmental variation. Similarly, one obtains extensive information about which genes respond to changes in developmental processes such as germination and flowering. One can therefore determine which genes respond to the phytohormones, growth regulators, safeners, herbicides, and related agrichemicals. These databases of gene expression information provide insights into the “pathways” of genes that control complex responses. The accumulation of DNA microarray or gene chip data from many different experiments creates a powerful opportunity to assign functional information to genes of otherwise unknown function. The conceptual basis of the approach is that genes that contribute to the same biological process will exhibit similar patterns of expression. Thus, by clustering genes based on the similarity of their relative levels of expression in response to diverse stimuli or developmental or environmental conditions, it is possible to assign functions to many genes based on the known function of other genes in the cluster.

CONSTRUCTION OF POLYPEPTIDES OF THE INVENTION AND VARIANTS THEREOF

[0082] The polypeptides of the invention include those encoded by the disclosed nucleic acids. These polypeptides can also be encoded by nucleic acids that, by virtue of the degeneracy of the genetic code, are not identical in sequence to the disclosed nucleic acids. Thus, the invention includes within its scope a polypeptide encoded by a nucleic acid having the sequence of any one of SEQ ID NOS: 1-999 or a variant thereof.

[0083] In general, the term “polypeptide” as used herein refers to both the full length polypeptide encoded by the recited nucleic acid, the polypeptide encoded by the gene represented by the recited nucleic acid, as well as portions or fragments thereof. Polypeptides also includes variants of the naturally occurring proteins, where such variants are homologous or substantially similar to the naturally occurring protein, and can be of an origin of the same or different species as the naturally occurring protein. In general, variant polypeptides have a sequence that has at least about 80%, usually at least about 90%, and more usually at least about 98% sequence identity with a differentially expressed polypeptide of the invention, as measured by BLAST using the parameters described above. The variant polypeptides can be naturally or non-naturally glycosylated, i.e., the polypeptide has a glycosylation pattern that differs from the glycosylation pattern found in the corresponding naturally occurring protein.

[0084] In general, the polypeptides of the subject invention are provided in a non-naturally occurring environment, e.g. are separated from their naturally occurring environment. In certain embodiments, the subject protein is present in a composition that is enriched for the protein as compared to a control. As such, purified polypeptide is provided, where by purified is meant that the protein is present in a composition that is substantially free of non-differentially expressed polypeptides, where by substantially free is meant that less than 90%, usually less than 60% and more usually less than 50% of the composition is made up of non-differentially expressed polypeptides.

[0085] Also within the scope of the invention are variants; variants of polypeptides include mutants, fragments, and fusions. Mutants can include amino acid substitutions, additions or deletions. The amino acid substitutions can be conservative amino acid substitutions or substitutions to eliminate non-essential amino acids, such as to alter a glycosylation site, a phosphorylation site or an acetylation site, or to minimize misfolding by substitution or deletion of one or more cysteine residues that are not necessary for function. Conservative amino acid substitutions are those that preserve the general charge, hydrophobicity/hydrophilicity, and/or steric bulk of the amino acid substituted.

[0086] Variants also include fragments of the polypeptides disclosed herein, particularly biologically active fragments and/or fragments corresponding to functional domains. Fragments of interest will typically be at least about 10 amino acids (aa) to at least about 15 aa in length, usually at least about 50 aa in length, and can be as long as 300 aa in length or longer, but will usually not exceed about 1000 aa in length, where the fragment will have a stretch of amino acids that is identical to a polypeptide encoded by a nucleic acid having a sequence of any SEQ ID NOS:1-999, or a homolog thereof.

[0087] The protein variants described herein are encoded by nucleic acids that are within the scope of the invention. The genetic code can be used to select the appropriate codons to construct the corresponding variants.

LIBRARIES AND ARRAYS

[0088] In general, a library of biopolymers is a collection of sequence information, which information is provided in either biochemical form (e.g., as a collection of nucleic acid or polypeptide molecules), or in electronic form (e.g., as a collection of genetic sequences stored in a computer-readable form, as in a computer system and/or as part of a computer program). The term biopolymer, as used herein, is intended to refer to polypeptides, nucleic acids, and derivatives thereof, which molecules are characterized by the possession of genetic sequences either corresponding to, or encoded by, the sequences set forth in the provided sequence list (seqlist). The sequence information can be used in a variety of ways, e.g., as a resource for gene discovery, as a representation of sequences expressed in a selected cell type, e.g. cell type markers, etc.

[0089] The nucleic acid libraries of the subject invention include sequence information of a plurality of nucleic acid sequences, where at least one of the nucleic acids has a sequence of any of SEQ ID NOS:1-999. By plurality is meant one or more, usually at least 2 and can include up to all of SEQ ID NOS:1-999. The length and number of nucleic acids in the library will vary with the nature of the library, e.g., if the library is an oligonucleotide array, a cDNA array, a computer database of the sequence information, etc.

[0090] Where the library is an electronic library, the nucleic acid sequence information can be present in a variety of media. “Media” refers to a manufacture, other than an isolated nucleic acid molecule, that contains the sequence information of the present invention. Such a manufacture provides the sequences or a subset thereof in a form that can be examined by means not directly applicable to the sequence as it exists in a nucleic acid. For example, the nucleotide sequence of the present invention, e.g. the nucleic acid sequences of any of the nucleic acids of SEQ ID NOS:1-999, can be recorded on computer readable media, e.g. any medium that can be read and accessed directly by a computer. Such media include, but are not limited to: magnetic storage media, such as a floppy disc, a hard disc storage medium, and a magnetic tape; optical storage media such as CD-ROM; electrical storage media such as RAM and ROM; and hybrids of these categories such as magnetic/optical storage media. One of skill in the art can readily appreciate how any of the presently known computer readable mediums can be used to create a manufacture comprising a recording of the present sequence information. “Recorded” refers to a process for storing information on computer readable medium, using any such methods as known in the art. Any convenient data storage structure can be chosen, based on the means used to access the stored information. A variety of data processor programs and formats can be used for storage, e.g. word processing text file, database format, etc. In addition to the sequence information, electronic versions of the libraries of the invention can be provided in conjunction or connection with other computer-readable information and/or other types of computer-readable files (e.g., searchable files, executable files, etc, including, but not limited to, for example, search program software, etc.) By providing the nucleotide sequence in computer readable form, the information can be accessed for a variety of purposes. Computer software to access sequence information is publicly available. For example, the BLAST (Altschul et al., supra.) and BLAZE (Brutlag et al. Comp. Chem. (1993) 17:203) search algorithms on a Sybase system can be used identify open reading frames (ORFs) within the genome that contain homology to ORFs from other organisms.

[0091] As used herein, a “computer-based system” refers to the hardware means, software means, and data storage means used to analyze the nucleotide sequence information of the present invention. The minimum hardware of the computer-based systems of the present invention comprises a central processing unit (CPU), input means, output means, and data storage means. A skilled artisan can readily appreciate that any one of the currently available computer-based system are suitable for use in the present invention. The data storage means can comprise any manufacture comprising a recording of the present sequence information as described above, or a memory access means that can access such a manufacture. “Search means” refers to one or more programs implemented on the computer-based system, to compare a target sequence or target structural motif with the stored sequence information. Search means are used to identify fragments or regions of the genome that match a particular target sequence or target motif. A variety of known algorithms are publicly known and commercially available, e.g. MacPattern (EMBL), BLASTN, BLASTX (NCBI) and tBLASTX. A target sequence can be any DNA or amino acid sequence of six or more nucleotides or two or more amino acids, preferably from about 10 to 100 amino acids or from about 30 to 300 nucleotide residues.

[0092] A “target structural motif”, or “target motif”, refers to any rationally selected sequence or combination of sequences in which the sequence(s) are chosen based on a three-dimensional configuration that is formed upon the folding of the target motif, or on consensus sequences of regulatory or active sites. There are a variety of target motifs known in the art. Protein target motifs include, but arc not limited to, enzyme active sites and signal sequences. Nucleic acid target motifs include, but are not limited to, hairpin structures, promoter sequences and other expression elements such as binding sites for transcription factors.

[0093] A variety of structural formats for the input and output means can be used to input and output the information in the computer-based systems of the present invention. One format for an output means ranks fragments of the genome possessing varying degrees of homology to a target sequence or target motif. Such presentation provides a skilled artisan with a ranking of sequences and identifies the degree of sequence similarity contained in the identified fragment.

[0094] A variety of comparing means can be used to compare a target sequence or target motif with the data storage means to identify sequence fragments of the genome. A skilled artisan can readily recognize that any one of the publicly available homology search programs can be used as the search means for the computer based systems of the present invention.

[0095] As discussed above, the “library” of the invention also encompasses biochemical libraries of the nucleic acids of SEQ ID NOS:1-999, e.g., collections of nucleic acids representing the provided nucleic acids. The biochemical libraries can take a variety of forms, e.g. a solution of cDNAs, a pattern of probe nucleic acids stably bound to a surface of a solid support (microarray) and the like. By array is meant an article of manufacture that has a solid support or substrate with one or more nucleic acid targets on one of its surfaces, where the number of distinct nucleic may be in the hundreds, thousand, or tens of thousands. Each nucleic acid will comprise at 18 nt and often at least 25 nt, and often at least 100 to 1000 nucleotides, and may represent up to a complete coding sequence or cDNA.. A variety of different array formats have been developed and are known to those of skill in the art. The arrays of the subject invention find use in a variety of applications, including gene expression analysis, drug screening, mutation analysis and the like, as disclosed in the above-listed exemplary patent documents.

[0096] In addition to the above nucleic acid libraries, analogous libraries of polypeptides are also provided, where the where the polypeptides of the library will represent at least a portion of the polypeptides encoded by SEQ ID NOS:1-999.

GENETICALLY ALTERED CELLS AND TRANSGENICS

[0097] The subject nucleic acids can be used to create genetically modified and transgenic organisms, usually plant cells and plants, which may be monocots or dicots. The term transgenic, as used herein, is defined as an organism into which an exogenous nucleic acid construct has been introduced, generally the exogenous sequences are stably maintained in the genome of the organism. Of particular interest are transgenic organisms where the genomic sequence of germ line cells has been stably altered by introduction of an exogenous construct.

[0098] Typically, the transgenic organism is altered in the genetic expression of the introduced nucleotide sequences as compared to the wild-type, or unaltered organism. For example, constructs that provide for over-expression of a targeted sequence, sometimes referred to as a knock-in, provide for increased levels of the gene product. Alternatively, expression of the targeted sequence can be down-regulated or substantially eliminated by introduction of a knock-out construct, which may direct transcription of an anti-sense RNA that blocks expression of the naturally occurring mRNA, by deletion of the genomic copy of the targeted sequence, etc.

[0099] In one method, large numbers of genes are simultaneously introduced in order to explore the genetic basis of complex traits, for example by making plant artificial chromosome (PLAC) libraries. The centromeres in Arabidopsis have been mapped and current genome sequencing efforts will extend through these regions. Because Arabidopsis telomeres are very similar to those in yeast one may use a hybrid sequence of alternating plant and yeast sequences that function in both types of organisms, developing yeast artificial chromosome-PLAC libraries, and then introducing them into a suitable plant host to evaluate the phenotypic consequences. By providing a defined chromosomal environment for cloned genes, the use of PLACs may also enhance the ability to produce transgenic plants with defined levels of gene expression.

[0100] It has been found in many organisms that there is significant redundancy in the representation of genes in a genome. That is, a particular gene function is likely by represented by multiple copies of similar coding sequences in the genome. These copies are typically conserved in the amino acid sequence, but may diverge in the sequence of non-translated sequences, and in their codon usage. In order to knock out a particular genetic function in an organism, it may not be sufficient to delete a genomic copy of a single gene. In such cases it may be preferable to achieve a genetic knock-out with an anti-sense construct, particularly where the sequence is aligned with the coding portion of the mRNA.

[0101] Methods of transforming plant cells are well-known in the art, and include protoplast transformation, tungsten whiskers (Coffee et al., U.S. Pat. No. 5,302,523, issued Apr. 12, 1994), directly by microorganisms with infectious plasmids, use of transposons (U.S. Pat. No. 5,792,294), infectious viruses, the use of liposomes, microinjection by mechanical or laser beam methods, by whole chromosomes or chromosome fragments, electroporation, silicon carbide fibers, and microprojectile bombardment.

[0102] For example, one may utilize the biolistic bombardment of meristem tissue, at a very early stage of development, and the selective enhancement of transgenic sectors toward genetic homogeneity, in cell layers that contribute to germline transmission. Biolistics-mediated production of fertile, transgenic maize is described in Gordon-Kamm et al. (1990), Plant Cell 2:603; Fromm et al. (1990) Bio/Technology 8: 833, for example. Alternatively, one may use a microorganism, including but not limited to, Agrobacterium tumefaciens as a vector for transforming the cells, particularly where the targeted plant is a dicotyledonous species. See, for example, U.S. Pat. No. 5,635,381. Leung et al. (1990) Curr. Genet. 17(5):409-11 describe integrative transformation of three fertile hermaphroditic strains of Arabidopsis thaliana using plasmids and cosmids that contain an E. coli gene linked to Aspergillus nidulans regulatory sequences.

[0103] Preferred expression cassettes for cereals may include promoters that are known to express exogenous DNAs in corn cells. For example, the Adhl promoter has been shown to be strongly expressed in callus tissue, root tips, and developing kernels in corn. Promoters that are used to express genes in corn include, but are not limited to, a plant promoter such as the, CaMV 35S promoter (Odell et al., Nature, 313, 810 (1985)), or others such as CaMV 19S (Lawton et al., Plant Mol. Biol., 9, 31F (1987)), nos (Ebert et al., PNAS USA, 84, 5745 (1987)), Adh (Walker et al., PNAS USA, 84, 6624 (1987)), sucrose synthase (Yang et al., PNAS USA, 87, 4144 (1990)), .alpha.-tubulin, ubiquitin, actin (Wang et al., Mol. Cell. Biol., 12, 3399 (1992)), cab (Sullivan et al., Mol. Gen. Genet, 215, 431 (1989)), PEPCase (Hudspeth et al., Plant Mol. Biol., 12, 579 (1989)), or those associated with the R gene complex (Chandler et al., The Plant Cell, 1, 1175 (1989)). Other promoters useful in the practice of the invention are known to those of skill in the art.

[0104] Tissue-specific promoters, including but not limited to, root-cell promoters (Conkling et al., Plant Physiol., 93, 1203 (1990)), and tissue-specific enhancers (Fromm et al., The Plant Cell, 1, 977 (1989)) are also contemplated to be particularly useful, as are inducible promoters such as water-stress-, ABA- and turgor-inducible promoters (Guerrero et al., Plant Molecular Biology, 15, 11-26)), and the like.

[0105] Regulating and/or limiting the expression in specific tissues may be functionally accomplished by introducing a constitutively expressed gene (all tissues) in combination with an antisense gene that is expressed only in those tissues where the gene product is not desired. Expression of an antisense transcript of this preselected DNA segment in an rice grain, using, for example, a zein promoter, would prevent accumulation of the gene product in seed. Hence the protein encoded by the preselected DNA would be present in all tissues except the kernel.

[0106] Alternatively, one may wish to obtain novel tissue-specific promoter sequences for use in accordance with the present invention. To achieve this, one may first isolate cDNA clones from the tissue concerned and identify those clones which are expressed specifically in that tissue, for example, using Northern blotting or DNA microarrays. Ideally, one would like to identify a gene that is not present in a high copy number, but which gene product is relatively abundant in specific tissues. The promoter and control elements of corresponding genomic clones may then be localized using the techniques of molecular biology known to those of skill in the art. Alternatively, promoter elements can be identified using enhancer traps based on T-DNA and/or transposon vector systems (see, for example, Campisi et al. (1999) Plant J. 17:699-707; Gu et al. (1998) Development 125:1509-1517).

[0107] In some embodiments of the present invention expression of a DNA segment in a transgenic plant will occur only in a certain time period during the development of the plant. Developmental timing is frequently correlated with tissue specific gene expression. For example, in corn expression of zein storage proteins is initiated in the endosperm about 15 days after pollination.

[0108] Ultimately, the most desirable DNA segments for introduction into a plant genome may be homologous genes or gene families which encode a desired trait (e.g., increased disease resistance) and which are introduced under the control of novel promoters or enhancers, etc., or perhaps even homologous or tissue-specific (e.g., root-, grain- or leaf-specific) promoters or control elements.

[0109] The genetically modified cells are screened for the presence of the introduced genetic material. The cells may be used in functional studies, drug screening, etc., e.g. to study chemical mode of action, to determine the effect of a candidate agent on pathogen growth, infection of plant cells, etc.

[0110] The modified cells are useful in the study of genetic function and regulation, for alteration of the cellular metabolism, and for screening compounds that may affect the biological function of the gene or gene product. For example, a series of small deletions and/or substitutions may be made in the hosts native gene to determine the role of different domains and motifs in the biological function. Specific constructs of interest include anti-sense, as previously described, which will reduce or abolish expression, expression of dominant negative mutations, and over-expression of genes.

[0111] Where a sequence is introduced, the introduced sequence may be either a complete or partial sequence of a gene native to the host, or may be a complete or partial sequence that is exogenous to the host organism, e.g., an A. thaliana sequence inserted into wheat plants. A detectable marker, such as aldA, lac Z, etc. may be introduced into the locus of interest, where upregulation of expression will result in an easily detected change in phenotype.

[0112] One may also provide for expression of the gene or variants thereof in cells or tissues where it is not normally expressed, at levels not normally present in such cells or tissues, or at abnormal times of development, during sporulation, etc. By providing expression of the protein in cells in which it is not normally produced, one can induce changes in cell behavior.

[0113] DNA constructs for homologous recombination will comprise at least a portion of the provided gene or of a gene native to the species of the host organism, wherein the gene has the desired genetic modification(s), and includes regions of homology to the target locus (see Kempin et al. (1997) Nature 389:802-803). DNA constructs for random integration or episomal maintenance need not include regions of homology to mediate recombination. Conveniently, markers for positive and negative selection are included. Methods for generating cells having targeted gene modifications through homologous recombination are known in the art.

[0114] Embodiments of the invention provide processes for enhancing or inhibiting synthesis of a protein in a plant by introducing a provided nucleic acids sequence into a plant cell, where the nucleic acid comprises sequences encoding a protein of interest. For example, enhanced resistance to pathogens may be achieved by inserting a nucleic acid encoding an activator in a vector downstream from a promoter sequence capable of driving constitutive high-level expression in a plant cell. When grown into plants, the transgenic plants exhibit increased synthesis of resistance proteins, and increased resistance to pathogens.

[0115] Other embodiments of the invention provide processes for enhancing or inhibiting synthesis of a tolerance factor in a plant by introducing a nucleic acid of the invention into a plant cell, where the nucleic acid comprises sequences encoding a tolerance factor. For example, enhanced tolerance to an environmental stress may be achieved by inserting a nucleic acid encoding an activator in a vector downstream from a promoter sequence capable of driving constitutive high-level expression in a plant cell. When grown into plants, the transgenic plants exhibit increased synthesis of tolerance proteins, and increased tolerance to environmental stress.

[0116] Factors which are involved, directly or indirectly in biosynthetic pathways whose products are of commercial, nutritional, or medicinal value include any factor, usually a protein or peptide, which regulates such a biosynthetic pathway (e.g., an activator or repressor); which is an intermediate in such a biosynthetic pathway; or which is a product that increases the nutritional value of a food product; a medicinal product; or any product of commercial value and/or research interest. Plant and other cells may be genetically modified to enhance a trait of interest, by upregulating or down-regulating factors in a biosynthetic pathway.

SCREENING ASSAYS

[0117] The polypeptides encoded by the provided nucleic acid sequences, and cells genetically altered to express such sequences, are useful in a variety of screening assays to determine effect of candidate inhibitors, activators., or modifiers of the gene product. One may determine what insecticides, fungicides and the like have an enhancing or synergistic activity with a gene. Alternatively, one may screen for compounds that mimic the activity of the protein. Similarly, the effect of activating agents may be used to screen for compounds that mimic or enhance the activation of proteins. Candidate inhibitors of a particular gene product are screened by detecting decreased from the targeted gene product.

[0118] The screening assays may use purified target macromolecules to screen large compound libraries for inhibitory drugs; or the purified target molecule may be used for a rational drug design program, which requires first determining the structure of the macromolecular target or the structure of the macromolecular target in association with its customary substrate or ligand. This information is then used to design compounds which must be synthesized and tested further. Test results are used to refine the molecular models and drug design process in an iterative fashion until a lead compound emerges.

[0119] Drug screening may be performed using an in vitro model, a genetically altered cell, or purified protein. One can identify ligands or substrates that bind to, modulate or mimic the action of the target genetic sequence or its product. A wide variety of assays may be used for this purpose, including labeled in vitro protein-protein binding assays, electrophoretic mobility shift assays, immunoassays for protein binding, and the like. The purified protein may also be used for determination of three-dimensional crystal structure, which can be used for modeling intermolecular interactions.

[0120] Where the nucleic acid encodes a factor involved in a biosynthetic pathway, as described above, it may be desirable to identify factors, e.g., protein factors, which interact with such factors. One can identify interacting factors, ligands, substrates that bind to, modulate or mimic the action of the target genetic sequence or its product. A wide variety of assays may be used for this purpose, including labeled in vitro protein-protein binding assays, electrophoretic mobility shift assays, immunoassays for protein binding, and the like. In vivo assays for protein-protein interactions in E. coli and yeast cells are also well-established (see Hu et al. (2000) Methods 20:80-94; and Bai and Elledge (1997) Methods Enzymol. 283:141-156).

[0121] The purified protein may also be used for determination of three-dimensional crystal structure, which can be used for modeling intermolecular interactions. It may also be of interest to identify agents that modulate the interaction of a factor identified as described above with a factor encoded by a nucleic acid of the invention. Drug screening can be performed to identify such agents. For example, a labeled in vitro protein-protein binding assay can be used, which is conducted in the presence and absence of an agent being tested.

[0122] The term agent as used herein describes any molecule, e.g. protein or pharmaceutical, with the capability of altering or mimicking a physiological function. Generally a plurality of assay mixtures are run in parallel with different agent concentrations to obtain a differential response to the various concentrations. Typically, one of these concentrations serves as a negative control, i.e. at zero concentration or below the level of detection.

[0123] Candidate agents encompass numerous chemical classes, though typically they are organic molecules, preferably small organic compounds having a molecular weight of more than 50 and less than about 2,500 daltons. Candidate agents comprise functional groups necessary for structural interaction with proteins, particularly hydrogen bonding, and typically include at least an amine, carbonyl, hydroxyl or carboxyl group, preferably at least two of the functional chemical groups. The candidate agents often comprise cyclical carbon or heterocyclic structures and/or aromatic or polyaromatic structures substituted with one or more of the above functional groups. Candidate agents are also found among biomolecules including peptides, saccharides, fatty acids, steroids, purines, pyrimidines, derivatives, structural analogs or combinations thereof.

[0124] Candidate agents are obtained from a wide variety of sources including libraries of synthetic or natural compounds. For example, numerous means are available for random and directed synthesis of a wide variety of organic compounds and biomolecules, including expression of randomized oligonucleotides and oligopeptides. Alternatively, libraries of natural compounds in the form of bacterial, fungal, plant and organism extracts are available or readily produced. Additionally, natural or synthetically produced libraries and compounds are readily modified through conventional chemical, physical and biochemical means, and may be used to produce combinatorial libraries. Known pharmacological agents may be subjected to directed or random chemical modifications, such as acylation, alkylation, esterification, amidification, etc. to produce structural analogs.

[0125] Where the screening assay is a binding assay, one or more of the molecules may be joined to a label, where the label can directly or indirectly provide a detectable signal. Various labels include radioisotopes, fluorescers, chemiluminescers, enzymes, specific binding molecules, particles, e.g. magnetic particles, and the like. Specific binding molecules include pairs, such as biotin and streptavidin, digoxin and antidigoxin etc. For the specific binding members, the complementary member would normally be labeled with a molecule that provides for detection, in accordance with known procedures.

[0126] A variety of other reagents may be included in the screening assay. These include reagents like salts, neutral proteins, e.g. albumin, detergents, etc that are used to facilitate optimal protein-protein binding and/or reduce non-specific or background interactions. Reagents that improve the efficiency of the assay, such as protease inhibitors, nuclease inhibitors, anti-microbial agents, etc. may be used. The mixture of components are added in any order that provides for the requisite binding. Incubations are performed at any suitable temperature, typically between 4 and 40° C. Incubation periods are selected for optimum activity, but may also be optimized to facilitate rapid high-throughput screening. Typically between 0.1 and 1 hours will be sufficient.

[0127] The compounds having the desired biological activity may be administered in an acceptable carrier to a host. The active agents may be administered in a variety of ways. Depending upon the manner of introduction, the compounds may be formulated in a variety of ways. The concentration of therapeutically active compound in the formulation may vary from about 0.01-100 wt. %.

[0128] It must be noted that as used herein and in the appended claims, the singular forms “a”, “and”, and “the” include plural referents unless the context clearly dictates otherwise. Thus, for example, reference to “a complex” includes a plurality of such complexes and reference to the formulation includes reference to one or more formulations and equivalents thereof known to those skilled in the art, and so forth.

[0129] Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood to one of ordinary skill in the art to which this invention belongs. Although any methods, devices and materials similar or equivalent to those described herein can be used in the practice or testing of the invention, the preferred methods, devices and materials are now described.

[0130] All publications mentioned herein are incorporated herein by reference for the purpose of describing and disclosing, for example, the methods and methodologies that are described in the publications which might be used in connection with the presently described invention. The publications discussed above and throughout the text are provided solely for their disclosure prior to the filing date of the present application. Nothing herein is to be construed as an admission that the inventors are not entitled to antedate such disclosure by virtue of prior invention.

[0131] The following examples are put forth so as to provide those of ordinary skill in the art with a complete disclosure and description of how to make and use the subject invention, and are not intended to limit the scope of what is regarded as the invention. Efforts have been made to ensure accuracy with respect to the numbers used (e.g. amounts, temperature, concentrations, etc.) but some experimental errors and deviations should be allowed for. Unless otherwise indicated, parts are parts by weight, molecular weight is average molecular weight, temperature is in degrees Celsius, and pressure is at or near atmospheric.

EXPERIMENTAL

Cloning and Characterization of Arabidopsis thaliana Genes.

[0132] Following DNA isolation, sequencing was performed using the Dye Primer Sequencing protocol, below. The sequencing reactions were loaded by hand onto a 48 lane ABI 377 and run on a 36 cm gel with the 36E-2400 run module and extraction. Gel analysis was performed with ABI software.

[0133] The Phred program was used to read the sequence trace from the ABI sequencer, call the bases and produce a sequence read and a quality score for each base call in the sequence., (Ewing et al. (1998) Genome Research 8:175-185; Ewing and Green (1998) Genome Research 8:186-194.) PolyPhred may be used to detect single nucleotide polymorphisms in sequences (Kwok et al. (1994) Genomics 25:615-622; Nickerson et al. (1997) Nucleic Acids Research 25(14):2745-2751.)

[0134] MicroWave Plasmid Protocol:

[0135] Fill Beckman 96 deep-well growth blocks with 1 ml of TB containing 50 μg of ampicillin per ml. Inoculate each well with a colony picked with a toothpick or a 96-pin tool from a glycerol stock plate. Cover the blocks with a plastic lid and tape at two ends to hold lid in place. Incubate overnight (16-24 hours depending on the host stain) at 37° C. with shaking at 275 rpm in a New Brunswick platform shaker. Pellet cells by centrifugation for 20 minutes at 3250 rpm in a Beckman GS-R6K, decant TB and freeze pelleted cell in the 96 well block. Thaw blocks on the bench when ready to continue.

1Prepare the MW-Tween20 solutionFor four blocks:For 16 blocks:50 ml STET/TWEEN20200 ml STET/TWEEN2 tubes RNAse (10 mg/ml, 600 ulea)8 tubes RNAse1 tube lysozyme (25 mg)4 tubes lysozyme

[0136] Pipette RNAse and Lysozyme into the corner of a beaker. Add Tween 20 solution and swirl to mix completely. Use the Multidrop (or Biohit) to add 25 ul of sterile H2O (from the L size autoclaved bottles) to each well. Resuspend the pellets by vortexing on setting 10 of the platform vortexer. Check pellets after 4 min. and repeat as necessary to resuspend completely. Use the multidrop to add 70 μl of the freshly prepared MW-Tween 20 solution to each well. Vortex at setting 6 on the platform vortex for 15 seconds. Do not cause frothing.

[0137] Incubate the blocks at room temperature for 5 min. Place two blocks at a time in the microwave (1000 Watts) with the tape (placed on the H1 to H12 side of the block) facing away from each other and turn on at full power for 30 seconds. Rotate the blocks so that the tapes face towards each other and turn on at full power again for 30 seconds.

[0138] Immediately remove the blocks from the microwave and add 300 μl of sterile ice cold H2O with the Multidrop. Seal the blocks with foil tape and place them in an H2O ice bath.

[0139] Vortex the blocks on 5 for 15 seconds and leave them in the H2O/ice bath. Return to step 7 until all the blocks are in the ice water bath. Incubate the blocks for 15 minutes on ice. Spin the blocks for 30 minutes in the Beckman GS-6KR with GH3.8 rotor with Microplus carrier at 3250 rpm.

[0140] Transfer 100 μl of the supernatant to Corning/Costar round bottom 96 well trays. Cover with foil and put into fridge if to be sequenced right away. If not to be sequenced in the next day, freeze them at −20° C.

[0141] Dye Primer Sequencing:

[0142] Spin down the DP brew trays and DNA template by pulsing in the Beckman GS-6KR with GH3.8 rotor with Microplus carrier. Big Dye Primer reaction mix trays (one 96 well cycleplate (Robbins) for each nucleotide), 3 microliters of reaction mix per well.

[0143] Use twelve channel pipetter (Costar) to add 2 μl of template to one each G,A,T,C, trays for each template plate. Pulse again to get both the reaction mix and template into the bottom of the cycle plate and put them into the MJ Research DNA Tetrad (PTC-225).

[0144] Start program Dye-Primer. Dye-primer is:

296° C., 1 min 1 cycle96° C., 10 sec.55° C., 5 sec.70° C., 1 min 15 cycles96° C., 10 sec.70° C., 1 min. 15 cycles4° C. soak

[0145] When done cycling, using the Robbins Hydra 290 add 100 μl of 100% ethanol to the A reaction cycle plate and pool the contents of all four cycle plates into the appropriate well.

[0146] To perform ethanol precipitation: Use Hydra program 4 to add 100 μl 100% ethanol to each A tray. Use Hydra program 5 to transfer the ethanol and therefore combine the samples from plate to plate. Once the G, A, T, and C trays of each block are mixed, spin for 30 minutes at 3250 in the Beckman. Pour off the ethanol with a firm shake and blot on a paper towel before drying in the speed vac (˜10 minutes or until dry). If ready to load add 3 μl dye and denature in the oven at 95° C. for ˜5 minutes and load 2 μl. If to store, cover with tape and store at −20° C.

3Common SolutionsTerrific BrothPer liter:900 ml H2O12 g bacto tryptone24 g bacto-yeast extract4 ml glycerol

[0147] Shake until dissolved and then autoclave. Allow the solution to cool to 60° C. or less and then add 100 ml of sterile 0.17M KH2PO4, 0.72M K2HPO4 (in the hood w/ sterile technique).

40.17 M KH2PO4, 0.72 M K2HPO4Dissolve 2.31 g of KH2PO4 and 12.54 g of K2HPO4 in 90 ml of H2O.Adjust volume to 100 ml with H2O and autoclave.Sequence loading Dye20 ml deionized formamide3.6 ml dH2O400 μl 0.5 M EDTA, pH 8.00.2 g Blue Dextran*Light sensitive, cover in foil or store in the dark.

[0148]

5

STET/TWEEN

10 ml 5 M NaCl

5 ml 1 M Tris, pH 8.0

1 ml 0.5 M EDTA., pH 8.0

25 ml Tween20

Bring volume to 500 ml with H2O

[0149] The sequencing reactions are run on an ABI 377 sequencer per manufacturer's' instructions. The sequencing information obtained each run are analyzed as follows.

[0150] Sequencing reads are screened for ribosomal., mitochondrial., chloroplast or human sequence contamination.. In good sequences, vector is marked by x's. These sequences go into biolims regardless of whether or not they pass the criteria for a ‘good’ sequence. This criteria is >=100 bases with phred score of >=20 and 15 of these bases adjacent to each other.

[0151] Sequencing reads that pass the criteria for good sequences are downloaded for assembly into consensus sequences (contigs). The program Phrap (copyrighted by Phil Green at University of Washington, Seattle, Wash.) utilizes both the Phred sequence information and the quality calls to assemble the sequencing reads. Parameters used with Phrap were determined empirically to minimize assembly of chimeric sequences and maximize differential detection of closely related members of gene families. The following parameters were used with the Phrap program to perform the assembly:

6Penalty−6Penalty for mismatches(substitutions)Min-40Minimum length of matching sequence to use in assemblymatchof readsTrim 0penalty used for identifying degenerate sequence atpenaltybeginning and end of read.Min-80Minimum alignment scorescore

[0152] Results from the Phrap analysis yield either contigs consisting of a consensus of two or more overlapping sequence reads, or singlets that are non-overlapping.

[0153] The contig and singlets assembly were further analyzed to eliminate low quality sequence utilizing a program to filter sequences based on quality scores generated by the Phred program. The threshold quality for “high quality” base calls is 20. Sequences with less than 50 contiguous high quality bases calls at the beginning of the sequence, and also at the end of the sequence were discarded. Additionally, the maximum allowable percentage of “low quality base calls in the final sequence is 2%, otherwise the sequence is discarded.

[0154] The stand-alone BLAST programs and Genbank databases were downloaded from NCBI for use on secure servers at the Paradigm Genetics, Inc. site. The sequences from the assembly were compared to the GenBank NR database downloaded from NCBI using the gapped version (2.0) of BLASTX. BLASTX translates the DNA sequence in all six reading frames and compares it to an amino acid database. Low complexity sequences are filtered in the query sequence. (Altschul et al. (1997) Nucleic Acids Res 25(17):3389-402).

[0155] Genbank sequences found in the BLASTX search with an E Value of less than 1e−10 are considered to be highly similar, and the Genbank definition lines were used to annotate the query sequences.

[0156] When no significantly similar sequences were found as a result of the BLASTX search, the query sequences were compared with the PROSITE database (Bairoch, A. (1992) PROSITE: A dictionary of sites and patterns in proteins. Nucleic Acids Research 20:2013-2018. ) to locate functional motifs.

[0157] Query sequences were first translated in six reading frames using the Wisconsin GCG pepdata program (Wisconsin Package Version 10.0, Genetics Computer Group (GCG) , Madison, Wis., USA. ). The Wisconsin GCG motifs Program (Wisconsin Package Version 10.0, Genetics Computer Group (GCG), Madison, Wis., USA.) was used to locate motifs in the peptide sequence, with no missmatches allowed. Motif names from the PROSITE results were used to annotate these query sequences.

7TABLE 1SEQ IDReferenceAnnotation120250017E-95 >sp|P4282SIDNJH_ARATH DNAJ PROTEIN HOMOLOG ATJ>gi|535588 (L36113) [Arabidopsis thaliana] >gi|1582356|prf||121 18338A AtJ2protein_[Arabidopsis_thaliana] = 419220250026E-44 >gi|25831 34 (AC002387) proline-rich protein [Arabidopsisthai janal >gi 14895234 IgbIAAD328 19.1 IAC0076591 (AC007659) unknown protein[Arabidopsis thaliana]Length = 134320250032E-74 ) >gb|AAD25839.11AC006951218 (AC006951) 40S ribosomal protein S17[Arabidopsis thaliana] Length = 141420250044E-27 >gi|2995953 (AF053565) glutaredoxin I [Mesembryanthemumcrystallinum] Length = 134520250056E-45 >emb10AA22977.11 (AL035353) photosystem I subunit PSI-E-Iikeprotein [Arabidopsis thalianal >gi|57322031emb10AB52678.1 (AJ245908)photosystem I subunit IV precursor [Arabidopsis thaliana] Length = 14362025006Pkc_Phospho_Site(21-23)72025007Tyr_Phospho_Site(27-34)82025008Tyr_Phospho_Site(269-277)920250097E-11 >sp|P80094|FADH_AMYME NAD/MYCOTHIOL-DEPENDENTFORMALDEHYDE DEHYDROGENASE (MD-FALDH) Length = 360102025010Tyr_Phospho_Site(609-616)1120250117E-96 >gi|3790554 (AF078683) RING-H2 finger protein RHA1a[Arabidopsis thaliana]Length = 1591220250127E-34 >9b|AAD33584.1‥AF132016_1 (AF132016) RING-H2 zinc finger proteinATL6 [Arabidopsis thaliana] Length = 398132025013Tyr_Phospho_Site(382-389)1420250141E-108 >gi|1335862 (U42608) clathrin heavy chain [Glycine max] Length= 1700152025015SE-11 >gi|2795805 (AC003674) protein kinase [Arabidopsis thaliana]>gi 3355493 (AC004218) protein kinase [Arabidopsis thalianal Length = 3951620250164E-88) >gi|3941458 (AF062883) transcription factor [Arabidopsisthaliana] Length = 1841720250171E-147 >gb|AAD52685.1|(AF179371) Cu/Zn-superoxide dismutase copperchaperone precursor [Arabidopsis thaliana]Length = 3101820250183′ Pkc_Phospho_Site(63-65)192025019Pkc_Phospho_Site(19-21)202025020Tyr_Phospho_Site(1057-1064)212025021Tyr_Phospho_Site(532-539)222025022Wd Repeats(666-680)2320250232E-14 >dbj|BAAO8O94l (D45066) AOBP (ascorbate oxidase promoter-binding protein) [Cucurbita maxima]Length = 3802420250243E-80 ) >gi|3859606 (AF104919) contains similarity to cysteineproteases (Pfam: PF00112, E = 1.3e-79, N = 1) [Arabidopsis thaliana] Length = 3592520250252E-36 >gi|3168840 (U88711) copper homeostasis factor [Arabidopsisthaliana]Length = 1212620250261E-71 >embICAB46041.11 (Z97341) gibberellin oxidase-like protein[Arabidopsis thaliana]Length = 2432720250271 E-31 >gbIAAD298O6.11AC006264 14 (AC006264) disease resistance responseprotein lArabidopsis thaliana]Length = 2762820250289E-18 >gi|3150525 (AF067219) contains similarity to yeast dolichyl-phosphate-mannose-protein mannosyltransferases [Caenorhabd tis elegansiLen th = 2062920250292E-45 >gi|2829896 (AC00231 1) highly similar to auxin-regulated proteinGH3, gpjX60033118591 [Arabidopsis thaliana]Length = 578302025030Tyr_Phospho_Site(1 246-1253)3120250317E-49 >sP P54887 IP5C1_ARATH DELTA 1-PYRROLIN E-5-CARBOXYLATESYNTHETASE A (P5CS A) INCLUDES: GLUTAMATE 5-KINASE (GAMMA-GLUTAMYL KINASE) (GK); GAMMA-GLUTAMYL PHOSPHATE REDUCTASE(GPR) (GLUTAMATE-5-SEMIALDEHYDE DEHYDROG ENASE) (GLUTAMYL-GAMMA-SEM IALD E... >gi 121 295721pir1 1S66637 delta-1-pyrroline-5-carboxylatesynthetase - Arabidopsis thaliana >gi 1829100 Iemb 1CAA607401 (X87330) pyrroline-5-carboxylate synthetase [Arabidopsis thaliana]>gi 1870866 IembICAA6O446 I(X86777) pyrroline-5-carboxylate synthetase A [Arabidopsis thalianal>gi|1041248 IembICAA6 15931 (X8941 4) pyrrol ine-5-carboxylate synthase[Arabidopsis thailiana]>gi|2642 162 (ACOO3000) delta-i -pyrroline 5-carboxylasesynthetase, P5CI [Arabidopsis thaliana]Length 7173220250321E-121 >embjCAAl8469.1 (AL022347) serine/threonine kinase-like protein[Arabidopsis thaliana]Length = 9003320250332E-52 >embICAAl 9717.11(AL030978) histone H2A-like protein [Arabidopsisthaliana]Length = 131342025034Tyr_Phospho_Site(1011-1019)3520250351E-149 >pir11545033 probable imbibition protein - wild cabbage>gi 14887871emb jCAA55893 I (X79330) imbibition protein [Brassica oleracea]Length = 76S362025036Tyr_Phospho_Site(127-133)37202S0371E-101 >gi|3822223 (AF077955) branched-chain alpha keto-aciddehydrogenase El alpha subunit [Arabidopsis thaliana]Length = 472382025038SE-SO >spIP41376IlF41 ARATH EUKARYOTIC INITIATION FACTOR 4A-1(EIF-4A-1) >gi|322503jpirIjJC1452 translation initiation factor elF-4A1 -Arabidopsis thaliana >gij 1 6SS4IembICAA46l 881 (X65052) eukaryotic translationinitiation factor 4A-1 Arabido sis thaliana Len th = 41239202S039Tyr_Phospho_Site(1 162-1168)40202S0403E-76 >embICAB4588l .11 (AL080282) berberine bridge enzyme-like protein[Arabidopsis thaliana]Length = S30412025041Tyr_Phospho_Site(275-283)4220250425E-85 >spIP43293INAK_ARATH PROBABLE SERINE/THREONINE-PROTEIN KINASE NAK >giI48I2O6ipirj 1S38326 protein kinase - Arabidopsisthaliana >gi|166809 (L07248) protein kinase [Arabidopsis thaliana]Length = 38943202S043IE-113 >embjCAAO7575.11 (AJ007588) monooxygenase [Arabidopsisthaliana]>4j4467141 IembICAB375lOI (AL035540) monooxygenase 2 (M02)[Arabidopsis thaliana]Length = 407442025044TyrPhospho...5ite(807-815)4520250451 E-61 >embjCAAO7004I (AJ006404) late elongated hypocotyl [Arabidopsisthaliana]Length = 6454620250463E-1 2 >gb|AAD4641 2.1 1AF0962629 (AF096262) ER6 protein [Lycopersiconesculentum]Length = 168472025047Pkc_PhosphoSite(36-38)4820250482E-17 >embjCAB43938.1j (AJ006349) endo-beta-1,4-glucaflaSe [Fragaria xananassa]Length = 6204920250497E-93 ) >5p1P484821PP12_ARATH SERINEITHREONINE PROTEINPHOSPHATASE PP1 ISOZYME 2 >gi 1421851 IpirlIS3l 086 phosphoproteinphosphatase (EC 3.1.3.16) 1 catalytic chain (clone TOPP2) - Arabidopsis thaliana>gi|166797 (M93409) catalyt5020250505E-80 >embICAB3968l .11 (AL049483) thioredoxin [Arabidopsis thaliana]Length = 2215120250516E-24 >gb|AAD25579.1IAC0072119 (AC007211) aSPFI protein [Arabidopsisthalianal Length = 4875220250529E-68 ) >gb|AAD37363.1 IAF 144078.9 (AF 144078) alpha-xylosidase precursor[Arabidopsis thaliana]>gi|5734722jgbjAAD49987.1 jAC008075_20 (AC008075)Identical to gbIAFl 44078 alpha-xylosidase precursor from Arabidopsis thaliana.ESTs gb1W43892, gbIN96l 65, gb1T46694, gb|N37141, gb|R64965, gb1R90271,gbIAA651443, gbiAA7l23O5, gb1T04189 and gbiAA597852 c... Length 9155320250534E-1 8 >gbIAAD1 74281 (AC006284) methyltransferase [Arabidopsisthalianal Length 6195420250541 E-1 17 >embjCAA23048.11 (AL035394) polygalacturonase [Arabidopsis5520250551 E-44 >gbjAAD49770.1 1AC00793298 (AC007932) Similar to gbIYI 24655620250567E-16 >pir1lA49318 protein kinase (EC 2.7.1.37) tousled - Arabidopsis5720250573E-1 7 >gi|3482908 (AC005551) R26529_2, partial CDS [Homo sapiens]Length = 1975820250581E-19 >gij2145020 (U82982) GEC-3 [Cavia porcellus]Length = 620592025059Tyr_Phospho_Site(28-35)602025060Tyr_Phospho_Site(412-419)612025061Pkc_Phospho_Site(89-91)622025062Tyr_Phospho_Site(66-73)6320250631E-19 >dbjIBAA8362O.1I (AB029341) TBP-interacting protein TIPI2Oalternatiely spliced form Rattus norvegicusi Length = 1273642025064Tyr_Phospho_Site(1522-1529)652025065Tyr_Phospho_Site(475-482)6620250661 E-84 >gbIAAD3989I .1 IAFi 069301 (AFI 06930) translation initiation protein[Medicago truncatula]Length = 935672025067Tyr Phos ho Site 794-8016820250682E-25 >5pIP466671ATH5_ARATH HOMEOBOX-LEUCINE ZIPPER PROTEINATHB-5 (HD-ZIP PROTEIN ATHB-5) >gi|629504ipir11547135 homeotic proteinAthb-5-Arabidopsis thaliana >gi|499160IembICAA47426l (X67033) Athb-5Arabido sis thaliana L692025069Pkc_Phospho_Site(5-7)702025070Tyr_Phospho_Site(850-857)712025071Tyr_Phospho_Site 945-953 7220250724E-90 > sp|P42791|RL18_ARATH 60S RIBOSOMAL PROTEIN L18 > gi|606970(U15741) cytoplasmic ribosomal protein L18 [Arabidopsis thaliana] Length = 187 7320250734E-58 > dbj|BAA77603.1| (AB027002) plastidic aldolase [Nicotianapaniculata] Length = 398 742025074Tyr_Phospho Site(1030-1036) 752025075Tyr_Phospho Site(42-49) 7620250764E-90 > dbj|BAA78331.1| (AB014076) histidine decarboxylase [Brassicanapus] Length = 490 7720250773E-22 > pir||A30191 hypothetical protein L - Bacillus subtilis (fragment)Length = 171 7820250789E-33 > sp|O23760|COMT_CLABR CAFFEIC ACID 3-O-METHYLTRANSFERASE (S-ADENOSYSL-L-METHIONINE:CAFFEIC ACID 3-O-METHYLTRANSFERASE) (COMT) > gi|2240207 (AF006009) caffeic acid O-methyltransferase [Clarkia breweri] Length = 370 7920250792E-55 > sp|O64765|UAP1_ARATH PROBABLE UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE > gi|3033397 (AC004238)unknown protien [Arabidopsis thaliana] Length = 502 8020250807E-27 > gb|AAD46402.1|AF096246_1 (AF096246) ethylene-responsivetranscriptional coactivator [Lycopersicon esculentum] Length = 146 812025081Tyr_Phospho_Site(102-110) 822025082Rgd(1288-1290) 832025083Pkc_Phospho_Site(10-12) 8420250841E-79 > emb|CAB36755.1| (AL035523) protein-methionine-S-oxidereductase [Arabidopsis thaliana] Length = 258 8520250857E-47 > gi|2078350 (U95923) transaldolase [Solanum tuberosum] Length = 438 862025086Tyr_Phospho_Site(2057-2063) 872025087Pkc_Phospho_Site(77-79) 8820250880 > sp|P43296|RD19_ARATH CYSTEINE PROTEINASE RDI9A PRECURSOR >gi|541856|pir||JN0718 drought-inducible cysteine proteinase (EC 3.4.22.-) RD19Aprecursor - Arabidopsis thaliana > gi|435618|dbj|BAA02373| (D13042) thiolprotease [Arabidopsis thaliana] > gi|4539328|emb|CAB38829.1| (AL035679)drought-inducible cysteine proteinase RD19A precursor [Arabidopsis thaliana]Length = 368 8920250893E-98 > emb|CAA92583| (Z68291) cysteine protease [Pisum sativum]Length = 350 9020250908E-88 > gi|1245182 (U49398) sterol delta-7 reductase [Arabidopsisthaliana] Length = 430 912025091Tyr_Phospho_Site(1016-1023) 9220250929E-14 > gi|4097547 (U64906) ATFP3 [Arabidopsis thaliana] Length = 297 9320250931E-115 > gi|3785999 (AC005499) peptidyl-prolyl cis-trans isomerase[Arabidopsis thaliana] Length = 199 942025094Tyr_Phospho_Site(328-334) 9520250954E-46 > sp|Q42614|NLT1_BRANA NONSPECIFIC LIPID-TRANSFERPROTEIN 1 PRECURSOR (LTP 1) > gi|732520 (U22105) germination-specific lipidtransfer protein 1 [Brassica napus] Length = 117 962025096Tyr_Phospho_Site(512-519 972025097Tyr_Phospho_Site(781-789) 9820250981E-102 > emb|CAA04707| (AJ001374) alpha-glucosidase [Solanumtuberosum] Length = 919 992025099Pkc_Phospho_Site(320-322)1002025100Zinc_Protease(861-870)1012025101Tyr_Phospho_Site(592-600)10220251021E-29 >emblCAAl5O99l(AJ235272) SOS RIBOSOMAL PROTEIN L310320251033′ Pkc_Phospho_Site(38-40)10420251045′ Pkc Phos ho Site 18-2010520251054E-59 >pir11560129 H+-transporting ATPase (EC 3.6.1.35), vacuolar, 16Kpumping ATPase 16 kDa proteolipid [Arabidopsis thaliana]>gi|926933 (L10620251061E-116 ) >spIP46643IAATL.ARATH ASPARTATE AMINOTRANSFERASE,MITOCHONDRIAL PRECURSOR (TRANSAMINASE A) >gi|693688 (U15026)aspartate aminotransferase [Arabidopsis thaliana]>9113201622 (AC004669)aspartate aminotransferase [Arabido10720251073E-61 ) >gbIAAD5S28S.11AC00826396 (AC008263) Similar to gbIAF135422GDP-mannose pyrophosphorylase A (GMPPA) from Homo sapiens. ESTsgbIAA7I 2990, gbjN65247, gbjN38l 49, gb|T041 79, gb1Z38092, gb1T76473,gb1N96403, gbIAA394551 and gbj10820251086E-72 >splP55737IHS82_ARATH HEAT SHOCK PROTEIN 81-2 (HSP8I-2)>gij445127jprf|j1908431B heat shock protein HSP8I-2 [Arabidopsis thaliana]Length = 6991092025109Rgd(531-533)11020251103E-39 >pir11539445 DNA-directed RNA polymerase (EC 2.7.7.6)11 chain 9- fruit fly (Drosophila melanogaster) >gij4S3Ol 1 lbbsll 39686 (S66940) RNApolymerase II subunit 9, RPII15 B9 {EC 2.7.7.6}[Drosophila melanogaster,Peptide, 129 aa][Drosophila melanogaster]Length 12911120251112E-51 >embICABSO787.11 (AJ243528) glyoxalase I [Triticum aestivum]Length = 2841122025112PtsHprSer(1091-1106)11320251131 E-106 >gi|3128188 (AC004521) beta-glucosidase [Arabidopsisthaliana]Length 57711420251144E-93 >g|j3738327 (AC005170) serine carboxypeptidase [Arabidopsisthaliana]Length = 4741152025115Tyr_Phospho_Site(51 8-524)11620251164E-70 >gbIAADS0O11.1IAC0O7651fi (AC007651) Similar to translation initiationfactor 1F2 [Arabidopsis thalianal Length = 101611720251171 E-17 >spjP41 73411AH1_YEAST ISOAMYL ACETATE-HYDROLYZINGESTERASE >91110771 851pir1154991 1 hypothetical protein YORI 26c - yeast(Saccharomyces cerevisiae) >g|I600023Iemb ICAA581 041 (X82930) ORESaccharomyces cerevisiae) >g|1105011820251183′ Tyr_Phospho_Site(523-530)11920251195′ Rgd(1053-1055)12020251202E-52 >embICAAO7S66I (AJ007578) pRIBS protein Ribes nigrumi Length= 2S812120251215E-96 >gi|2708813 (AF037362) ATA2O [Arabidopsis thaliana]Length43212220251221 E-63 >emb CAB 10269.11 (Z97337) hydroxyprol me-rich glycoproteinhomolog [Arabidopsis thalianal Length = 5071232025123Tyr_Phospho_Site(1 3-20)124202S1244E-24 >embICAA74S911 (Y14199) MAP3K delta-i protein kinase[Arabidopsis thaliana]Length = 406125202512SIE-14 >gi|308906 (L18909) thioredoxin [Lilium longiflorum]Length = 2621262025126Tyr_Phospho_Site(60-68)127202S127lE-ilO ) >embfCAA06978.11 (AJ006309) protein tyrosine phosphataseArabido sis thaliana Len th = 34012820251286E-50 >embICAA7OS78I(Y09427) squamosa-promoter binding protein like3 [Arabidopsis thaliana]>g|5931 6511embICAB56579.11 (AJOI 1627) squamosapromoter binding protein-like 3 [Arabidopsis thaliana]>gi|59316631emb10AB56585.1 (AJ01 1633) squamosa promoter binding protein-like 3 [Arabidopsis thaliana]Length = 13112920251294E-47 >gi|2708813 (AF037362) ATA20 [Arabidopsis thaliana]Length = 4321302025130Tyr_Phospho_Site(88-96)13120251313′ Protein Splicing(530-537)13220251323′ Tyr_Phospho_Site(504-512)13320251333E-23 >gb|AAD55621 .1 IACOO8OI 631 (ACOO8O1 6) Is a member of PF100534Glycosyl transferases group 1. EST gb|N967O2 comes from this gene.[Arabidopsis thaliana]Length = 67013420251343E-95 >gi|1912286 (U39568) type 2A serine/threonine proteinphosphatase [Arabidopsis thaliana]>gi|2194141 (AC002062) Match to Arabidopsisprotein phosphatase PP2A (gb1U39568). EST gbjT4l 959 comes from this gene.[Arabidopsis thaliana]Length = 30713520251357E-83 >gi|3608147 (AC005314) chloroplast 31 kDa ribonucleoproteinprecursor [Arabidopsis thaliana]Length = 3081362025136Tyr_Phospho_Site(130-138)1372025137Tyr_Phospho_Site(1644-1651)13820251387E-23 >gi|2708532 (AF029351) RNA binding protein Nicotianatabacum]Length = 4821392025139Pkc_Phospho_Site(111-113)14020251403′ 2E-30 >gi|1 346756I5pIP48483IPP1 3ARATH SERINE/THREONINEPROTEIN PHOSPHATASE PP1 ISOZYME 3 >gi|421852jpirIjS31087phosphoprotein phosphatase (EC 3.1.3.16) 1 catalytic chain (clone TOPP3) -Arabidopsis thaliana >gi|166799 (M93410) phosphoprotein phosphatase I[Arabidopsis thaliana]Length = 32214120251413′ Tyr_Phospho_Site(181-188)14220251423′ 3E-54 >gi|28333801sp1Q425831KPR2_ARATH RIBOSE-PHOSPHATEPYROPHOSPHOKINASE 2 (PHOSPHORIBOSYL PYROPHOSPHATESYNTHETASE 2) (PRS II) >gij2l46772IpiriiS7l 262 ribose-phosphatepyrophosphokinase (EC 2.7.6.1)11 - Arabidopsis thaliana (fragment)>gi 1 064885IembICAA63552.1I (X92974) phosphoribosyl14320251433E-22 >gif 3790677 (AF099002) similar to human 5′ -nucleotidase(SW:P49902) [Caenorhabditis elegans]Length = 52614420251444E-82 >gi|3337361 (AC004481) ankyrin-like protein [Arabidopsisthaliana]Length 77014520251455E-43 >pir11553490 RNA-binding protein cp29 precursor - Arabidopsisthaliana >gij68l9O2jdbjIBAAO6Sl8I (D31710) cp29 [Arabidopsis thaliana]Length = 33414620251469E-79 ) >gij2062157 (AC001645)jasmonate inducible protein isolog[Arabidopsis thaliana]Length = 70514720251475′ 1E-106 >gi|1076285IpirIIS5262I amidophosphoribosyltransferase -Arabidopsis thaliana >gi 14691 9SIdbi 1BAA06024 I (D28869)amidophosphoribosyltransferaSe [Arabidopsis thaliana]Length = 54814820251489E-43 >gi|2982253 (AF051209) CROC-1 -like protein [Picea mariana]Length = 14014920251497E-87 ) >gi|3193298 (AF069298) T14P8.17 gene product [Arabidopsisthaliana]Length = 15415020251509E-78 >gi 12583125 (AC002387) transketolase precursor [Arabidopsisthaliana]Length = 74115120251512E-79 >gbIAAD2I4SI.11 (AC007017) DNA-binding protein [Arabidopsisthaliana]Length = 14515220251521E-12 >9112661079 (AF035316) similar to beta tubulin [Homo sapiens]Length = 34215320251537E-26 >gbIAAD49985.1 1AC0080759 8 (AC008075) Contains PEIOl 426 BAH(bromo-adjacent homojogy) domain. ESTs gbfN96349, gbfT42710, gb(H77084,gbfAA395 147 and gbjAA6O5500 come from this gene. [Arabidopsis thaliana]Length = 6251542025154Tyr_Phospho_Site(163-171)15520251554E-63 >gi|735880 (L40577) geranylgeranyl pyrophosphate synthaseprotein [Arabidopsis thaliana]Length = 32615620251566E-2 1 >gbIAAFOO649. 1 IACOO8 1531 (ACOO81 53) UDP-glucuronosyltransferase,5′ partial [Arabidopsis thalianal Length 22715720251573E-55 >spIP549O4IPROCARATH PYRROLINE-5-CARBOXYLATEREDUCTASE (P5CR) (P50 REDUCTASE) >gi|5418941pir11JQ2334 pyrroline-5-carboxylate reductase (EC 1.5.1.2) - Arabidopsis thaliana >giIl 66815 (M76538)pyrroline carboxylate reductase [Arabidopsis thaliana]>giI1632776jemb|CAA70148I (Y08951) TSr protein [Arabidopsis thaliana]Length = 2761582025158Tyr_Phospho_Site(482-490)1592025159Tyr_Phospho_Site(551-558)16020251603E-85 >gi|4191784 (AC005917) WD-40 repeat protein fArabidopsisthaliana]Length = 46916120251614E-52 >emblCAA478O7I (X67421) extA [Arabidopsis thaliana]Length = 12716220251627E-17 >gbjAAC96965.1 (U42580) A638R [Paramecium bursaria Chiorellavirus 1]Length = 36016320251634E-64 >embjCAAO5727j (AJ002892) AtGRP2 [Arabidopsis thaliana]Length = 15016420251643E-66 >gi|1628583 (U66916) 12S cruciferin seed storage protein[Arabidopsis thaliana]>giI284249SIembICAAl 6892.11 (ALO2 1749) 125 cruciferinseed storage protein [Arabidopsis thaliana]Length = 52416520251651E-104 >gij2160158 (AC000132) Similarto elongation factor 1-gamma(gbjEF1GXENLA). ESTs gblT20564,gb1T45940,gb1T04527 come from this gene.[Arabidopsis thalianal Length = 4141662025166Pkc_Phospho_Site(5-7)1672025167Tyr_Phospho_Site(703-709)1682025168Tyr_Phospho_Site(1038-1046)1692025169Pkc_Phospho_Site(31-33)17020251701E-22 >gij1871181 (U90439) ring zinc finger protein isolog [Arabidopsisthaliana]Length = 4251712025171Tyr_Phospho_Site(558-565)1722025172Pkc_Phospho_Site(13-15)17320251730 >embjCABl0450.11 (Z97341) acyl-CoA oxidase like protein [Arabidopsis17420251748E-65 >pirjjD36571 ubiquitin 81-aa extension protein 2 -Arabidopsis(UBO6) [Arabidopsis thaliana]Length = 15717520251753E-76 >spIO644S9IUDPGPYRPY UTP-GLUCOSE-1-PHOSPHATEURIDYLYLTRANSFERASE (UDP-GLUCOSE PYROPHOSPHORYLASE)(UDPGP) (UGPASE) >giI3 107931 idbjlBAA259l 71 (ABOl 3353) UDP-glucosepyrophosphorylase [Pyrus pyrifolia]Length = 4711762025176Pkc_PhosphoSite(29-31)17720251774E-49 >embICAA17547.11 (AL021960) photosystem II oxygen-evolvingcomplex protein 3-like [Arabidopsis thaliana]>gi|3402748femb10AA20194.1J(AL031 187) photosystem II oxygen-evolving complex protein 3-like [Arabidopsisthai1782025178Tyr_Phospho_Site(564-57l)17920251791E-109 ) >spIP43297lRD2t..ARATH CYSTEINE PROTEINASE RD2IAPRECURSOR >g|5418571pir11JN0719 drought-inducible cysteine proteinase (EC3.4.22.-) RD2IA precursor - Arabidopsis thaliana >gij435619fdbj1BAA023741D13043 thiol roteas18020251801E-113 ) >sp|Q42560|ACOC_ARATH ACONITATE HYDRATASE,CYTOPLASMIC (CITRATE HYDRO-LYASE) (ACONITASE) Length 89718120251816E-60 >gi|1785615 (U83281) protein kinase homolog PsPK4 [Pisumsativumi Length = 4431822025182Pkc_Phospho_Site(11-13)18320251834E-73 >sp10233651C973_ARATH CYTOCHROME P450 97B31842025184T r Phos ho Site 569-5761852025185Tyr_Phospho_Site(445-453)1862025186Tyr_Phospho_Site(754-761)1872025187Tyr_Phospho_Site(802-810)18820251889E-82 >gi|1009234 (L38829) SUP2 gene product [Nicotiana tabacum]Length = 40918920251895E-69 >embICAAO72511 (AJ006787) phytochelatin synthetase[Arabidopsis thaliana]Length = 3621902025190Rgd(1210-1212)19120251911E-41 >gi|2352492 (AF005047) transport inhibitor response 11922025192Tyr_Phospho_Site(231-238)19320251933E-60 >spIPIO797IRBS3_ARATH RIBULOSE BISPHOSPHATE2B) >gi|68061 IpirIIRKMUB2 ribulose-bisphosphate carboxylase (EC 4.1.1.39)small chain B2 precursor - Arabidopsis thaliana >giIl6lg4IembICAA327Ol I(X14564) ribulose bisphosphate carboxylase [Arabidopsis thaliana]Length = 18119420251942E-35 >embICAA5652I j (X80237) mitochondrial processing peptidase[Solanum tuberosum]Length = 53419520251956E-54 >embICAB53O33.1I (AJ245866) photosystem I subunitX precursorArabido sis thaliana Len th 13019620251963E-36 >gb|AAD38988.1 AEl 558181 (AFi 55818) zinc finger protein Dof4[Arabidopsis thalianal Length = 26419720251973E-41 >gi|3152606 (AC004482) ring zinc finger protein [Arabidopsisthaliana]Length = 22719820251981E-104 >gb|AAD181091 (AC006403) protein kinase [ArabidopsisthalianalLength = 40719920251993E-15 >giI3643807 (AF062071) zinc finger protein ZNF2I6 [Musmusculus Len th = 21320020252009E-12 >gi|3924605 (AF069442) inhibitor of apoptosis [Arabidopsisthaliana]Length = 86420120252017E-91 ) >embICAAOSO24I (AJOOI 808) succinyl-CoA-ligase beta subunit[Arabidopsis thaliana]>gi|4512693IgbjAAD21746.1 I (AC006569) succinyl-CoAligase beta subunit [Arabidopsis thalianal Length = 4212022025202Pkc_PhosphoSite(37-39)20320252031 E-1 13 >ir S68223lutathione s nthase EC 6.3.2.3 2 - Arabido sisthaliana (fragment) >giIl 1 O75O3IembICAA9O5l SI (Z501 53) glutathione synthetasetArabidopsis thaliana]>gi|I 5855601prf11220l 360A glutathione synthetase[Arabidopsis thaliana]Length 51020420252045E-61 >spIP34IO6IALA2_PANMI ALAN INE AMINOTRANSFERASE 2 (GPT)(GLUTAMIC-PYRUVIC TRANSAMINASE 2) (GLUTAMIC-ALANIN ETRANSAMINASE 2) (ALAAT-2) >gi|320619|pirIIS28429 alanine transaminase (EC2.6.1.2) - proso millet >gi|296204IembICAA49199l (X69421) alanineaminotransferase Panicum miliaceum Len th = 4822052025205Pkc_PhosphoSite(55-57)20620252065E-27 >spIQ388O5IMT2B_ARATH METALLOTHIONEIN-LIKE PROTEIN 2B(MT-2B) >gi|13619991pir11557862 metallothionein 2b - Arabidopsis thaliana>gi|1086463 (Ul 1256) metallothionein [Arabidopsis thaliana]Length 7720720252072E-13 >reflNP004732.1IPP13OI nucleolar phosphoprotein p130>giI2l 358421pir11138073 nucleolar phosphoprotein p130 - human>gi 1663008 lemblCAA84O63I (Z34289) nucleolar phosphoprotein p130 [Homosapiens]Length = 69920820252089E-60 >giI3201612 (AC004669) 2A6 protein [Arabidopsis thaliana]Length = 36220920252096E-64 >gij3l 57947 (ACOO2I 31) Similar to protein gbIZ74962 fromBrassica oleracea which is similar to bacterial YRN1 and HEAHIO proteins. ESTsgbIT2l 954, gbjT04283, gbjZ37609, gbjN37366, gbIR90704, gbjFl 5500 andgb1F14353 come from this gene. [Arabidopsis tha... Length = 28321020252103′ Pkc_Phospho_Site(2-4)21120252116E-32 >spIPO5100I3MG1_ECOLI DNA-3-METHYLADENINE GLYCOSYLASE I(3-METHYLADENINE-DNA GLYCOSYLASE I, CONSTITUTIVE) (TAG I) (DNA-3-METHYLADEN IN E GLYCOSIDASE I) >gij675O8jpirIIDGECM I 3-methyladenineDNA glycosylase (EC 3.2.2.-) I - Escherichia coli >gi|430301emb10AA274721(X03845) TA21220252122E-78 >embICAA72l 771 (YI 1336) RGAI protein [Arabidopsis thaliana]Length = 58721320252132E-78 >gb|AAD39281.1 1AC007576A (AC007576) initiation factor 5A-4[Arabidopsis thaliana]Length = 15821420252141 E-28 >g113860261 (AC005824) acidic ribosomal protein [Arabidopsis2152025215Tyr_Phospho_Site(284-291)216202S216T r Phos ho Site 598-6042172025217Pkc_Phospho_Site(45-47)2182025218Pkc_Phospho_Site(16-18)2192025219Tyr_Phospho_Site(43-51)22020252207E-59 >pir|1S581 18 thioredoxin - Arabidopsis thaliana22120252217E-65 >spIP49O78IASNS_ARATH ASPARAGINE SYNTHETASE[Arabidopsis thaliana]>gi|5541 701 lembiCABsi 206.11 (AL096860) glutamine-dependent asparagine synthetase [Arabidopsis thaliana]Length = 58422220252223′ Tyr_Phospho_Site(1 63-170)22320252235′ 2E-38 >gij4126809jdbj1BAA36759i (ABOl 7042) glyoxalase I [Oryza sativa]Length = 291224202S2242E-68 >gi|3980385 (AC004561) 18 kDa class I heat shock protein[Arabidopsis thaliana]Length = 153225202S2251 E-21 >gbIAAC787O4.11 (AF001308) predicted glycosyl transferase[Arabidopsis thaliana]Length = 34622620252269E-91 >gi|2286069 (U721 55) beta-glucosidase [Arabidopsis thaliana]Length = 52822720252272E-33 >9bIAAD23647.11AC007119 13 (AC007119) 40S ribosomal protein S25(Arab idopsis thaliana]Length = 1082282025228Tyr_Phospho_Site(1003-1010)2292025229Tyr_Phospho_Site(381 -387)23020252306E-1 9 >spJQ46948ITHIJECOLI 4-METHYL-5(B-HYDROXYETHYL)-THIAZOLE MONOPHOSPHATE BIOSYNTHESIS ENZYME >giIl 100872(U34923) ThiJ [Escherichia coli]>9|I 1773108 (U82664) 4-methyl-5(b-hydroxyethyl)-thiazole monophosphate biosynthesis23120252313E-60 >gi|3193289 (AF069298) similar to several small proteins (-100aa) that are induced by heat, auxin, ethylene and wounding such as Phaseolusaureus indole-3-acetic acid induced protein ARG (SW:32292) [Arabidopsi2322025232Tyr_Phospho_Site(384-391)23320252333E-55 >gbjAAD154321 (AC006218) nonspecific lipid-transfer proteinprecursor [Arabidopsis thaliana]>g114726121 jgbjAAD2832l .1 1AC006436_12(AC006436) nonspecific lipid-transfer protein precursor [Arabidopsis thalianalLength = 16923420252341 E-100 >embICAA66959I (X9831 5) peroxidase [Arabidopsis thaliana]>gi 11429221 IembICAA673 I 3j (X98777) peroxidase ATP1 6a (Arabidopsis thaliana]>giI44SS8O2jembjCAB37l 931 (AJ 133036) peroxidase [Arabidopsis thaliana]Length = 35223520252355E-57 >gbIAADS5746.1 1AF0261671 (AF026167) ankyrin repeat protein EMB5O6[Arabidopsis thaliana]Length = 31523620252363′ RnpI (959-966)23720252373′ 1E-44 >gij5689168Idbj|BAA82843.1|(AB023651) miraculin homologue[Solanum melongena]Length = 16023820252385′ Pkc_Phospho_Site(26-28)2392025239Tyr_Phospho_Site(52-59)24020252401 E-71 >gi|2213592 (AC000348) T7N9.12 [Arabidopsis thaliana]Length = 55324120252411 E-1 12 >spjOO4l 3OJSERAARATH 0-3-PHOSPHOGLYCERATEDEHYDROGENASE PRECURSOR (PGDH) >giI2I 89964Idb1IBAA204051(AB003280) Phosphoglycerate dehydrogenase [Arabidopsis thaliana]>gi|28042581dbj 1BAA244401 (ABO 10407) phosphoglycerate dehydrogenase[Arabidopsis thaliana]Length = 6242422025242Tyr_Phospho_Site(599-606)24320252433E-25 >gbIAAD49986.1 1AC008075 19 (AC008075) Similar to gbIAFO23472peptide transporter from Hordeum vulgare and is a member of the PF100854Peptide transporter family. ESTs gb1T41927 and gbIAA395024 come from thisgene. [Arabidops24420252445E-29 >gi 12642157 (ACOO3000) ankyrin-like protein [Arabidopsisthaliana]Length = 69424520252451 E-1 02 ) >spIQO2283IHAT5ARATH HOMEOBOX-LEUCINE ZIPPERPROTEIN HATS (HD-ZIP PROTEIN 5) (HD-ZIP PROTEIN ATHB-1)>gi|996591pir1 ISi 6325 homeotic protein Athb-1 - Arabidopsis thaliana>gi|1 6329IembICAA4l 6251 (X58821) Athb-1 protein24620252467E-74 >emblCAB3655O.1 I (AL035440) SNF8 like protein [Arabidopsisthaliana]Length = 1812472025247Tyr_Phospho_Site(268-276)248202S2482E-91 >spl P25248 IACEABRANA ISOCITRATE LYASE (ISOC ITRASE)(ISOCITRATASE) (ICL) >gi 16821 1 Ipir1lWZRPI isocitrate lyase (EC 4.1.3.1) - rape>gi|2552201bbs11 12862 isocitrate lyase, threo-D 5-isocitrate glyoxylate-lyase, IL{EC 4.1.3.1}[Brassica napus, seedlings, Peptide, 576 aa]>giIl67l44 (L08482)isocitrate lyase [Brassica napusi >gi 14471 42lprfl 1191 3424A isocitrate lyaseIBrassica napus]Length = 57624920252495E-90 >gbIAABS3I 01 .21 (U6821 9) catalase [Brassica napus]Length 49225020252503′ 3E-13 >gi|1076634IpirIiS52578 protein-serine/threonine kinase NPK1S -common tobacco >giISO5l 46ldbj 1BAA065381 (D31 737) protein-serine/threoninekinase Nicotiana tabacum]Length = 42225120252513′ Pkc_Phospho_Site(4-6)25220252525′ 5E-68 >gi|45861 l6lembICAB4O9S2.1 I (AL049638) C-4 sterol methyl oxidase[Arabidopsis thalianal Length = 3032532025253Tyr_Phospho_Site(318-324)2542025254Tyr_Phospho_Site(350-358)25520252553E-43 >dbiIBAA229401 (D45900) LEDI-3 protein [Lithospermumerythrorhizonl Length = 2012562025256Pkc_Phospho_Site(1 3-15)2572025257Pkc_Phospho_Site(1 6-18)25820252582E-93 ) >gi|1669387 (U41 998) actin 2 [Arabidopsis thaliana]Length = 37725920252597E-50 >embICAB38952.1 I(AL049171) ribosomal protein [Arabidopsis2602025260Tyr_Phospho_Site 517-5232612025261Tyr_Phospho_Site(55-62)26220252621E-108 >embICABl 0398.11 (Z97340) cysteine proteinase like protein26320252631E-74 >pirIlSl 9226 cold-regulated protein cor47 - Arabidopsis thaliana(fragment) >gi|388259jembICAA42483I (X59814) Cold and ABA regulated gene[Arabidopsis thaliana]Length = 29426420252649E-65 >gi|42051 15 (AF000521) cell wall invertase precursor [Fragaria xananassa]Length = 57726520252659E-40 >5pIP52424IPUR5_VIGUNPHOSPHORIBOSYLFORMYLGLYCINAMIDIN E CYCLO-LIGASE PRECURSOR(AIRS) (PHOSPHORIBOSYL-AMINOIMIDAZOLE SYNTHETASE) (AIRSYNTHASE) >gi 1945060 (U30895) am inoimidazole ribonucleotide (Al RS)synthetase [Vigna unguiculata]Length = 38826620252661 E-38 >dbjIBAA7579l .11 (AB017977) Aps2 [Arabidopsis thaliana]Length = 9626720252672E-87 >embICAA23O33.1 I (AL035394) major latex protein [Arabidopsisthaliana]Length = 1512682025268Tyr_Phospho_Site(931 -938)2692025269SE-93 >embjCAB43643.1 I (ALOSO3SI) phenylalanyl-trna synthetase-likeprotein [Arabidopsis thaliana]Length = 42827020252701 E-30 >gbjAAB8l 870 IAAB81 870 (AC002983) phosphoglyceride transferprotein [Arabidopsis thaliana]Length 30127120252715E-59 ) >spIQ963I9IERW.ARATH ENHANCER OF RUDIMENTARYHOMOLOG >gi|1595812 (U67398) enhancer of rudimentary homolog ATER[Arabidopsis thalianal Length = 10927220252727E-60 ) >gi|3426037 (ACOOSI 68) ABC transporter protein [Arabidopsisthaliana]Length = 142027320252732E-14 >embICAB1 0269.11 (Z97337) hydroxyproline-rich glycoproteinhomolog [Arabidopsis thaliana]Length = 50727420252744E-28 >5pIP49597IP2C1_ARATH PROTEIN PHOSPHATASE 2C ABIl (PP2C)>gij2129699|pirjIA54588 protein phosphatase ABIl - Arabidopsis thaliana>gijSO94l9IembICAA5S484l (X78886) ABII [Arabidopsis thalianal Length = 4342752025275Pkc_Phospho_Site(55-57)2762025276Tyr_Phospho_Site 221-2292772025277Zinc Protease(1485-1494)27820252783′ 2E-16 >gi|5640155jemblCAB51557.lf (AJ242530) gibberellin response2792025279lE-lOl >gi|452470 (U05218) ATP sulfurylase [Arabidopsis thaliana]28020252802E-80 >embICAB38935.1 (AL035709) phosphoenolpyruvate carboxykinase2812025281IE-39 >embICAA749651 (Y14615) Importin alpha-like protein [Arabidopsis2822025282Pkc PhosphoSite(32-34)28320252831 E-38 >embICAA68l 9|(X99938) RNA helicase [Arabidopsis thaliana]Length = 67128420252849E-31 >gi|974294 (U31309) LP6 [Pinus taeda]Length = 2162852025285Tyr_Phospho_Site(200-206)28620252862E-38 >embjCABl6270.11 (Z99165) hypothetical zinc-finger protein[Schizosaccharomyces pombel Length 4252872025287Tyr_Phospho_Site 1014-10212882025288Tyr_Phospho_Site(981-988)2892025289Tyr_Phospho_Site(55-63)29020252905′ Pkc_Phospho_Site(12-14)29120252911E-108 >gbIAAD4I43O.11AC007727_19 (AC007727) Similar to gb1Z11499 proteindisulfide isomerase from Medicago sativa. ESTs gbIAl099693, gb1R65226,gbIAA657311, gbjT43068, gb1T42754, gbjTl4005, gb1T76445, gb|H36733,gbJT43168 and gbjT20649 come from t... Length = 50129220252922E-65 >embICAA67425I (X98925) stromal ascorbate peroxidase[Arabidopsis thalianal Length 37229320252932E-93 >spIP23686IM ETKARATH S-AD ENOSYLMETHION IN E SYNTHETASE1 (METHIONINE ADENOSYLTRANSFERASE 1) (ADOMET SYNTHETASE 1)>giI8l 647f pirlIJNOl 31 methionine adenosyltransferase (EC 2.5.1.6) - Arabidopsisthaliana >gi|166872 (M55077) 5-adenosylmethion me synthetase [Arabidopsisthaliana]Length = 39329420252947E-35 >gbjAAD49969.1 1AC0080752 (AC008075) Contains similarity togbIAFI 14753 polytropic murine leukamia virus receptor SYGi from Musmusculus. EST gb|N96331 comes from this gene. [Arabidopsis thaliana]Length = 87329520252953E-19 >gbIAAD1S482I (AC006266) glucosyltransferase [Arabidopsisthaliana Len th 6992962025296Pkc PhosphoSite(26-28)29720252971E-80) >embjCAB38935.1| (AL035709) phosphoenolpyruvatecarboxykinase (ATP)-like protein [Arabidopsis thaliana]Length = 6712982025298SE-Si >dbjIBAA3Il43I (ABOI 091 5) responce regulatori [Arabidopsisthaliana]>gi|3323583 (AF057282) two-component response regulator homolog[Arabidopsis thaliana]>gi|3953597fdbj|BAA34726|(AB008487) response regulator42992025299Tyr_Phospho_Site(140-147)30020253005E-52 >pirIIS27OlO aminoacylase (EC 3.5.1.14)1 - pig>giIl845fembjCAA48565j (X68564) aminoacylase I [Sus scrofa]Length = 40630120253013E-76 ) >dbjIBAA7484OI (AB007802) cytochrome b5 [Arabidopsis thalianalLength = 14030220253022E-65 >pirIIS5l 697 oleoyl-[acyl-carrier-protein]hydrolase (EC 3.1.2.14) -Arabidopsis thaliana >gij21295301pir1 1S69195 acyl-(acyl carrier protein)thioesterase (clone TE 1-1) - Arabidopsis thaliana >giI634003jembICAA85387|(Z3691 0) acyl-(acyl carrier protein) thioesterase [Arabidopsis thalianal Length = 41230320253033′ Tyr_Phospho_Site(474-482)30420253043′ 7E-77 >gij5915829jsp10657871C7B6_ARATH CYTOCHROME P450 71B6>gij3164138(dbjjBAA28536j (D78604) cytochrome p450 monooxygenase[Arabidopsis thaliana]>9114115378 (AC005967) cytochrome p450 monooxygenase[Arabidopsis thaliana]Length 5033052025305Tyr_Phospho_Site(237-245)30620253064E-49 >9113355468 (A00042 18) ribosomal protein L35 [Arabidopsisthaliana]Length = 12330720253073E-22 >gb IAAC951 69.1 | (AC005970) subtilisin-like protease [Arabidopsisthalianal Length = 75430820253084E-57 >gb|AAD1 7402 | (AC006248) RING-H2 finger protein [Arabidopsisthaliana]Length 20430920253099E-41 >embICAA655O21 (X96727) isocitrate dehydrogenase (NAD+)[Nicotiana tabacum]Length = 36431020253109E-63 ) >gi|21 04957 (U96924) immunophilin [Arabidopsis thalianalLength = 11231120253111E-159 >gbIAAD23681.1|AC006841_9 (AC006841) fructose biphosphatealdolase [Arabidopsis thaliana]Length = 39331220253123′ Tyr_Phospho_Site(29-36)31320253135′ 3E-18 >9111590814 (U52851) arginine decarboxylase [Arabidopsisthalianal Length = 70231420253146E-44 >gij3033385 (AC004238) similar to Human XE169 protein(escapes X-chromosome inactivation) [Arabidopsis thaliana]Length = 8063152025315Pkc_PhosphoSite(20-22)31620253161E-104 >spIQ42569IC9O1ARATH CYTOONROME P450 90A1>911107631 51pirjjS55379 cytochrome P450 - Arabidopsis thaliana>gi|853719lemb1CAA607931 (X87367) CYP9O protein [Arabidopsis thaliana]|871 988(emb 1CAA607941 (X87368) CYP9O protein [Arabidopsis thaliana]Length 4723172025317Pkc_Phospho_Site(54-56)3182025318Tyr_Phospho_Site(489-496)31920253194E-81 >spjP271 62ICAL1PETHY CALMODULIN I >gij7l 684IpirIIMCPZDCcalmodulin - carrot >giI478632jpirI|S22971 calmodulin - trumpet lily>911541 8391pir11S40301 calmodulin - Red bryony >giI2l 299701pir11S70768calmodulin CAM81 - garden petunia >gi|18326jemb10AA42423l (X59751)calmodulin [Daucus carotal >giIl9447iembICAA783Ol I (Zi 2839) calmodulin[Lilium longiflorum]>gi|169207 (M80836) calmodulin [Petunia hybridal >gij308900(Li 8912) calmodulin [Lilium longiflorumi >gijSOSl s4jemblCAA43l 43j (X60738)Calmodulin [Malus domestica]>gi|535444 (U13882) calmodulin [Pisum sativum]>giI5825598Igb|AAD5331 3.1 IAFi 780731 (AFi 78073) calmodulin 7 [Arabidopsisthaliana >I 445602 if 1909349A calmodulin Daucus carota Len th = 14932020253207E-59 >emblCABlO267.1 I (Z97337) cytosolic O-acetylserine(thiol)lyase (EC4.2.99.8) [Arabidopsis thaliana]Length = 32232120253215E-12 >refjNP 006775.1 IPWDR3j WD repeat domain 3>gij5639663jgb1AAD45865.1 jAF08321 71 (AF08321 7) WD repeat protein WDR3[Homo sapiens]Length = 9433222025322Tyr_Phospho_Site(324-331)32320253233E-65 >emblCAB43899.11 (AL078468) cellulose synthase catalytic subunit-like protein [Arabidopsis thalianal Length = 68932420253241E-101) >embICAAl67l3.1I (AL021687) cytochrome P450 [Arabidopsisthaliana]Length = 45732520253256E-46 >giI3l 76690 (AC003671) Similar to ubiquitin ligase gb1063905from S. cerevisiae. EST gb|R65295 comes from this gene. [Arabidopsis thaliana]Length = 112632620253261E-109 >gb|AAB70445I (AC000104) Arabidopsis thaliana ethylenereceptor (ERS2) gene (gbjAF047976). EST gb|W43451 comes from this gene.[Arabidopsis thaliana]>gi|3687656 (AF047976) ethylene receptor; ERS2[Arabidopsis thaliana]Length = 64532720253272E-76 >5pIP49637IRL2A_ARATH 60S RIBOSOMAL PROTEIN L27A>gi|2129719IpirjjS71256 ribosomal protein L27a - Arabidopsis thaliana>gi|11074871emb1CAA630251 (X91959) 60S ribosomal protein L27a [Arabidopsisthaliana]>gi 61751 50 jgb|AAF04877. 1 IACQI 0796_13 (ACOl 0796) 60S ribosomalprotein L27A [Arabidopsis thaliana]Length = 1463282025328Tyr_Phospho_Site(1 098-1105)32920253291E-142 >spIO0442OIURIC_ARATH URICASE (URATE OXIDASE) (NODULIN35 HOMOLOG) >gi|2208944IembjCAA72005I (Y11120) nodulin-35 homologue[Arabidopsis thalianall Length = 30933020253301E-124 >embjCAB389O8.1 I (AL035708) cytochrome P450-like proteinArabido sis thaliana Length = 5413312025331Tyr_Phospho_Site(344-35O)33220253323E-56 >gbjAAD2l762.1 j(AC006569) photosystem I reaction centersubunit IV precursor [Arabidopsis thalianal >gi|5732205jemb|CAB52679.1 I(AJ245909) photosystem I subunit IV precursor [Arabidopsis thaliana]Length = 14533320253333′ 6E-47 >gi|3806098 (AF0791 00) arginine-tRNA-prOtein transferase1; Atel p [Arabidopsis thaliana]Length = 62933420253345′ Pkc_Phospho_Site(31 9-321)33520253351E-91 >spIP46875IKATC_ARATH KINESIN-LIKE PROTEIN C>gij1084342jpiri1548020 kinesin-related protein katO - Arabidopsis thaliana>gi|14388441dbjlBAA046741 (021138) heavy chain polypeptide of kinesin-likeprotein [Arabidopsis thalianal Length = 75433620253368E-36 >spIQOO8O8IHETI_PODAN VEGETATIBLE INCOMPATIBILITYPROTEIN HET-E-1 >gi|607003 (L281 25) beta transducin-Iike protein [Podosporaanserinal Length 13563372025337Pkc_Phospho_Site(1 6-18)33820253382E-44 >embICAAO6667.1 I (AJ005671) cytochrome b6f complex subunit[Arabidopsis thaliana]Length = 9633920253399E-40 >spjP52836jF3ST_FLACH FLAVONOL 3-SULFOTRANSFERASE (F3-ST) >gi|285285|pirIIB4021 6 flavonol 3′ -sulfotransferase - Flaveria chloraefoliaLength = 31134020253404E-94 >gi|4056432 (AC005990) Similar to gi|2245014glucosyltransferase homolog from Arabidopsis thaliana chromosome 4 contiggbjZ97341. ESTs gb|T20778 and gbIAA586281 come from this gene. [Arabidopsisthaliana]Length = 44834120253419E-21 >gi|488189 (U00063) weakly similar to R. rickettsii protein P34[Caenorhabditis elegansi Length = 4353422025342Pkc_PhosphoSite(200-202)34320253431 E-49 >gi|2642434 (AC002391) Reri protein [Arabidopsis thaliana]Length = 21134420253442E-1 6 >gb|AAD24653.1 1AC0062209 (AC006220) glycine rich protein[Arabidopsis thaliana]Length = 13534520253453′ 4E-43 >gi|4559380lgbfAA023040.1 1AC0065265 (AC006526) auxin-responsive GH3 protein (Arabidopsis thalianaj Length = 57634620253463E-57 >gij3482923(AC003970) Highly similar to cinnamyl alcoholdehydrogenase, gi|l 143445 [Arabidopsis thaliana]Length = 3223472025347Pkc_Phospho_Site(41-43)34820253482E-71 >gij3004563 (AC003673) similar to APG (non proline-rich region)[Arabidopsis thaliana]>gi 31 76703 (AC002392) proline-rich protein APG[Arabidopsis thaliana]Length = 34434920253494E-66 >gij3152581 (AC002986) Similar to E. coli sulfurtransferase(rhodanese) gbIAEOO338. ESTs gb1T03984, gb1T03983 and gb1W43228 comefrom this gene. [Arabidopsis thaliana]>gij5834508|emb|CAB55306.1 (AJOI 1045)thiosulfate sulfurtransferase [Arabidopsis thaliana]>gi|6009981 jdbj IBAA851 48.11(AB032864) mercaptopyruvate sulfurtransferase lArabidopsis thalianal Length = 3793502025350Pkc_PhosphoSite(5-7)35120253513E-71) >embICAB5365IAI (AL110123) ribosomal protein L32-like protein[Arabidopsis thaliana]Length = 13335220253521E-136 >gbIAADO2499I (AF049870) thaumatin-like protein [Arabidopsisthaliana]Length = 25335320253539E-78) >dbjlBAA28828I (AB015313) MAP kinase kinase 2 [Arabidopsis3542025354Tyr_Phospho_Site(720-727)3552025355Tyr_Phospho_Site(647-654)35620253561E-105 >gij4 102703 (AF015274) ribulose-5-phosphate-3-epimerase[Arabidopsis thaliana]Length = 28135720253571E-100 >gi|1657617 (U72503) G2p [Arabidopsis thaliana]>gij3068707(AF049236) nuclear DNA-binding protein G2p [Arabidopsis thaliana]Length = 3923582025358Tyr_Phospho_Site(391 -398)35920253593′ 4E-39 >giI3643085Igb|AAC36698f (AF075580) protein phosphatase-2C;PP2C [Mesembryanthemum crystallinum]Length = 35936020253603′ Tyr_Phospho_Site(776-782)36120253615′ Tyr_Phospho_Site(94-102)3622025362Pkc_Phospho_Site(50-52)36320253632E-29 >embICABlO321.11 (Z97338) UFD1 like protein [Arabidopsis thaliana]Length = 77836420253642E-57 >gi|3337361 (AC004481) ankyrin-like protein [Arabidopsisthaliana]Length = 77036520253651 E-108 >gbIAAD3O2S4.1 1AC007296_15 (AC007296) Strong similarity togblU74319 obtusifoliol 14-alpha demethylase (CYPSI) from Sorghum bicolor andis a member of the PF100067 cytochrome P450 family. ESTs gblAA72O3O,gblN65031 and gbIAA36620253665E-34 >emb(CAA1 8841 .11 (AL023094) ribosomal protein S16 [Arabidopsisthaliana]Length = 11336720253671E-65) >gi|1905876 (U90879) biotin carboxylase subunit [Arabidopsisthaliana]>gi|1916300 (U9 1414) heteromeric acetyl-CoA carboxylase biotincarboxylase subunit [Arabidopsis thaliana]>gi 13047099 (AF058826) Arabidopsisthaliana biotin carboxylase subunit (GB:U90879) [Arabidopsis thaliana]Length = 53736820253681E-103 >sp 1P54887jP5C 1 ARATH DELTA I -PYRROLINE-5-CARBOXYLATESYNTHETASE A (P5CS A) [INCLUDES: GLUTAMATE 5-KINASE (GAMMA-GLUTAMYL KINASE) (GK); GAMMA-GLUTAMYL PHOSPHATE REDUCTASE(GPR) (GLUTAMATE-5-SEMIALDEHYDE DEHYDROGENASE) (GLUTAMYLGAMMA-SEM IALD E... >gi 121 295721 pin 1566637 delta-I -pyrrol ine-5-carboxylatesynthetase - Arabidopsis thaliana >gi|829100jembICAA60740I (X87330) pyrroline-5-carboxylate synthetase [Arabidopsis thaliana]>gi l870866lemblCAA60446 I(X86777) pyrrol ine-5-carboxylate synthetase A [Arabidopsis thaliana]>gi|1041 248lemblCAA6l 593j (X894 14) pyrroline-5-carboxylate synthase[Arabidopsis thaliana]>gi|26421 62 (AC003000) delta-i -pyrroline 5-carboxylasesynthetase, P5C1 [Arabidopsis thaliana]Length 71736920253691 E-43 >pirIIJUOl 82 monodehydroascorbate reductase (NADH) (EC1.6.5.4) - cucumber >gij452165|dbj|BAA05408j (D26392) monodehydroascorbatereductase [Cucumis sativus]Length = 43437020253701 E-36 >giIl 669387 (U41 998) actin 2 [Arabidopsis thalianal Length = 37737120253712E-39 >sp1Q42351 1RL34_ARATH 60S RIBOSOMAL PROTEIN L34>gij4262177jgbjAAD14494i (ACOOSSO8) 23552 [Arabidopsis thaliana]Length = 12037220253721 E-52 >embjCAAl 65521 (ALO21 635) HSP associated protein like[Arabidopsis thalianal Length = 6273732025373Tyr_Phospho_Site(1431-1438)3742025374Tyr_Phospho_Site(347-354)37520253755E-29 >emblCAA6734l I (X98809) peroxidase ATP5a [Arabidopsisthalianal Length = 3503762025376Tyr_Phospho_Site(1514-1521)37720253771 E-66 >pir1l533612 isocitrate dehydrogenase - soybean Length = 45137820253782E-15 >gb|AAD24393.1IAC00608195 (AC006081) zinc finger protein37920253796E-74 >embICAA7O946I (Y09817) Ca2+-ATPase [Arabidopsis thaliana]38020253803′ Pkc_Phospho_Site(12-14)38120253815′ Pkc_Phospho_Site(152-154)38220253823E-67 >giI3l 50402(ACOO41 65) malonyl-CoA:ACyl carrier protein38320253833E-83 >gi|31 35261(AC003058) 18.5 KDa class I heat shock protein38420253841 E-121 >embICAB45447.11 (AL079347) invertase-like protein [Arabidopsisthaliana] Length = 57138520253859E-36 >9114056460 (AC005990) Contains similarity to gbIL26505 Met3Opfrom Saccharomyces cerevisiae. ESTs gbIFl4l33, gbIT46217, gbiAA404758 andgb|Z37647 come from this gene. [Arabidopsis thaliana]Length = 47538620253865E-23 >gbjAAC27O73.1 I (AF067858) embryo-specific protein 3[Arabidopsis thaliana]Length = 21338720253872E-33 >embICABlO3O9.1 I (Z97338) cytochrome P450 like protein[Arabidopsis thaliana]Length = 48738820253884E-46 >spIQ3941 1 1RL26_BRARA 60S RIBOSOMAL PROTEIN L26>gi|2160300idbjIBAA1 89411 (D78495) ribosomal protein [Brassica rapa]Length = 14638920253891E-102 >embICAB45O74.1I (AL078637) transport inhibitor response-likeprotein [Arabidopsis thalianal Length = 61439020253902E-73 ) >emblCAB37456.1 j (AL035526) shaggy-like protein kinase etha (EC2.7.1 .-) [Arabidopsis thaliana]Length = 38039120253911E-101) >pinIIS7l273 lamin - Arabidopsis thaliana>gi|1262754|embICAA65750I (X97023) lamin [Arabidopsis thaliana]>gi|3395760(U77721) unknown [Arabidopsis thaliana]Length = 17239220253922E-46 >spIP46687IGAS3_ARATH GIBBERELLIN-REGULATED PROTEIN 3PRECURSOR >gi|2129590ipinIiS60231 GASTi protein homolog (clone GASA3) -Arabidopsis thaliana >gi|887935 (U11764) GASTI protein homolog [Arabidopsisthaliana] >gi|5916443|gbIAAD55954.1 1AC007633 3 (AC007633) giberellinregulated protein GASA3 precursor [Arabidopsis thaliana]Length = 9939320253932E-92 >spIP139Q5IEF1A ARATH ELONGATION FACTOR 1-ALPHA (EF-1-ALPHA) >gi|81 6O6IpirI jS06724 translation elongation factor eEF-1 alpha chain -Arabidopsis thaliana >gi|2957881emb10AA344531 (X16430) elongation factor 1-alpha [Arabidopsis thalianal >gi|1369927|embjCAA34454l (XI 6431) elongationfactor 1-alpha [Arabidopsis thalianal >gi|1369928IembiCAA34455I (Xl 6431)elongation factor 1-alpha [Arabidopsis thaliana]>gi|1532172 (U63815) EF-lalpha3942025394Pkc_PhosphoSite(44-46)39520253956E-64 >9113851559 (AF084829) methyl chloride transferase [Batistransferase [Batis maritima]Length = 23039620253965′ Pkc_Phospho_Site(47-49)39720253975E-56 >gij3337352 (AC004481) chromatin structural protein Suptshp[Arabidopsis thaliana]Length = 99039820253981E-37 >9b1AAD34676.11AC00634t.4 (AC006341) Similar to gbIYl2Ol4 RAD23protein isoform II from Daucus carota. This gene is probably cut off. ESTgbIAA651284 comes from this gene. [Arabidopsis thalianal Length = 1133992025399Pkc_PhosphoSite(111-113)4002025400lE-lOl >gi|3193316(AF069299) contains similarity to nucleotide sugarepimerases [Arabidopsis thaliana]Length = 4304012025401TyrPhosphQ.5ite(88-95)40220254023E-40 >gi|3329368 (AF031244) nodulin-like protein [Arabidopsisthaliana]Length = 55940320254036E-57 >spIP34O91IRL6_MESCR60S RIBOSOMAL PROTEIN L6 (YL1 6-LIKE)>gi|2803741pir11S28586 ribosomal protein ML16 - common ice plant>gi 119539 lemblCAA49 1751 (X69378) ribosomal protein YL1 6[Mesembryanthemum crystallinum]Length = 2344042025404Tyr_Phospho_Site(998-1 006)40520254053E-50 >gi|2462763 (AC002292) Highly similar to auxin-induced protein(aldo/keto reductase family) [Arabidopsis thaliana]Length = 34240620254061E-35 >spIP32I32ITYPA_ECOLI GTP-BINDING PROTEIN TYPAJBIPA(TYROSINE PHOSPHORYLATED PROTEIN A) >gij62873SIpiri 1540816hypothetical protein o591 - Escherichia coli >gij304976 (Li 9201) matchesPSOOO17: ATP_GTP_A and PS00301: EFACTOR_GTP; similar to elongationfactor G, TetMITetO tetracycline-resistance proteins [Escherichia coli]>gi|1790302(AE000462) GTP-binding factor [Escherichia coli]Length = 5914072025407Tyr_Phospho_Site(425-432)40820254087E-25 >emblCAB4l72l.1I (AL049730) pEARLI 1-like protein [Arabidopsisthaliana]>gi|4725951jembICAB41722.1l (AL049730) pEARLI 1-like protein[Arabidopsis thaliana]Length = 1294092025409Pkc_Phospho_Site(1 8-20)4102025410Tyr_Phospho_Site(652-659)41120254113′ Pkc_Phospho_Site(21-23)41220254125′ Tyr_Phospho_Site(283-290)41320254135′ Tyr_Phospho_Site(901-908)4142025414Pkc_Phospho_Site(2-4)41520254151E-120 >sp|P46645|AAT2ARATH ASPARTATE AMINOTRANSFERASE,CYTOPLASMIC ISOZYME 1 (TRANSAMINASE A) >g|693690 (U15033)aspartate aminotransferase [Arabidopsis thaliana]Length = 40541620254163E-68 >emb|CAA74051 | (Y1 3723) Transcription factor [Arabidopsisthalianal Length = 14141720254177E-89 >splP46267lF1 60 BRANA FRUCTOSE-1,6-BISPHOSPHATASECYTOSOLIC (D-FRUCTOSE-1,6-BISPHOSPHATE |-PHOSPHOHYDROLASE)(FBPASE) >gi|885894 (U20179) fructose 1,6-bisphosphatase [Brassica napus]Length 3394182025418Rgd(688-690)41920254194E-13 >gbjAAD3l375.11AC006053.j7 (AC006053) proton phosphatase[Arabidopsis thaliana]Length = 39242020254204E-37 >emblCAB4l7l6.1l(AL049730) SWHI protein [Arabidopsis thalianalLength 6944212025421Tyr_Phospho_Site (256-263)42220254223E-86 >gbIAAC24833I (AFO6I 520) copper/zinc superoxide dismutase[Arabidopsis thalianal Length = 16242320254238E-56 >pirll556707 histone H3 homolog - common tobacco Length = 13642420254241E-98 >spl02206015P51_CITUN SUCROSE-PHOSPHATE SYNTHASE 1(UDP-GLUCOSE-FRUCTOSE-PHOSPHATE GLUCOSYLTRANSFERASE 1)j25888881dbj | BAA232 131 (AB005023) sucrose-phosphate synthase [Citrusunshiul Length = 105742520254253E-14 >gb|AAC32439.11 (AC004786) serine carboxypeptidase IArabido sis thaliana Len th 43542620254263E-85 >gb|AAC3631 8.11 (AF053127) leucine-rich receptor-like proteinkinase [Malus domestical Length = 99942720254274E-71 >embICAB39787.1 I (AL049488) chlorophyll a/b-binding protein-like[Arabidopsis thalianal >g|14741 958|9b1AAD28776. 1 |AF|341291 (AF 134129)Lhcb5 protein [Arabidopsis thaliana]Length = 28042820254281E-105>sp|P19456|PMA2_ARATH PLASMAMEMBRANEATPASE2(PROTON PUMP) >g|67973jpir||PXMUP2 H+-transporting ATPase (EC 3.6.1.35)type 2, plasma membrane - Arabidopsis thaliana >gi|166629 (J05570) H+-ATPase[Arabidopsis thalianal >gi|5730129IembICAB52463.1 I (AL109796) H+-transportingATPase type 2, plasma membrane [Arabidopsis thalianal Length = 9484292025429Tyr_Phospho_Site(35-43)4302025430Tyr_Phospho_Site(772-780)43120254313′ IE-104 >gi|2146742jpirIIS65572 pattern-formation protein GNOM -Arabidopsis thaliana >gi|1209631 (U36432) GNOM gene product [Arabidopsisthaliana]Length = 145143220254323′ 3E-66 >gij2244819IembiCABl 0242.11 (Z97336) germin precursor oxalateoxidase [Arabidopsis thaliana]Length = 2224332025433Tyr_Phospho_Site(330-337)43420254342E-33 >5pIO23095IRLA1 ARATH 60S ACIDIC RIBOSOMAL PROTEIN P1>gi|2252857 (AF013294) similar to acidic ribosomal protein pl [Arabidopsisthaliana]Length = 1104352025435Tyr_Phospho_Site(1062-1069)4362025436Tyr_Phospho_Site(1166-1173)4372025437T r Phos ho Site 1176-11844382025438Zinc Finger C2h2(279-300)4392025439Tyr_Phospho_Site(619-626)44020254405′ 4E-96 >giIl 502430 (U62331) phosphate transporter [Arabidopsisthaliana]>gij2564661 (AF022872) phosphate transporter [Arabidopsis thaliana]>gi 13869206idbj 1BAA343981 (ABO 16166) Phosphate Transporter 4 [Arabidopsisthaliana]>giI3928081 (AC005770) phosphate transporter, AtPT244120254415′ T r Phos ho Site 262-26944220254425′ Rgd(475-477)4432025443Tyr_Phospho_Site(800-808)44420254441 E-61 >giI2l 91131 (AF007269) A_1G002N01 .8 gene product[Arabidopsis thaliana]Length = 44444520254457E-74 >embICAA711O31 (Y09987) CDSP32 protein (Chioroplast Drought-induced Stress Protein of 32kDa) [Solanum tuberosum]Length = 29644620254461 E-1 19 >dbjIBAA84437.1 I (AP000423) NADH dehydrogenase ND4[Arabidopsis thaliana]Length = 50644720254474E-16 >embjCAAl 8840.1 I (AL023094) Homeodomain-like protein4482025448Pkc_Phospho_Site(90-92)4492025449Pkc_Phospho_Site(40-42)4502025450T r Phos ho Site 1144-115245120254512E-67 >spjQ40082jXYLAHORVU XYLOSE I SOM ERASE>gi|2130052Ipirj j565467 xylose isomerase (EC 5.3.1.5) - barley>gi I 1296809 IembICAA64545I (X95257) xylose isomerase [Hordeum vulgare]Length = 4794522025452Pkc_Phospho_Site(31 -33)45320254533′ 7E-63 >gi|586036jsp|P37106ISR51_ARATH SIGNAL RECOGNITIONPARTICLE 54 KD PROTEIN I (SRP54) >gi|629560IpirIIS42550 signal recognitionparticle 54K protein - Arabidopsis thaliana >gi|3O41 11 (Li 9997) signal recognitionparticle 54 kDa subunit [Arabidopsis thalianal >giISl 03829IgbIAAD39659.1 ACO45420254545′ Tyr_Phospho_Site(307-31 5)45520254554E-79 >giI3l 57931 (AC002131) Similar to pyrophosphate-dependentphosphofuctokinase beta subunit gb1Z32850 from Ricinus communis. ESTsgb1N65773, gb1N64925 and gb1F15232 come from this gene. [Arabidopsisthaliana]Length = 57445620254569E-70 >gi|1669387 (U41 998) actin 2 [Arabidopsis thaliana]Length = 3774572025457Tyr_Phospho_Site(43-50)45820254582E-25 >spIP54I2IIAIG2_ARATH AIG2 PROTEIN >gij1127806 (U40857) AIG2[Arabidopsis thalianal Length = 17045920254591 E-32 >g113377850 (AF076274) contains simlarity to Canis familiarissignal peptidase complex 25 kDa subunit (GB:U12687) [Arabidopsis thaliana]Length = 1254602025460Pkc_PhosphoSite(24-26)46120254611E-120 >gi|3108209 (AF028809) eukaryotic cap-binding protein[Arabidopsis thaliana]Length 2214622025462Tyr_Phospho_Site(711-718)46320254635′ Pkc_Phospho_Site(37-39)4642025464Pkc_Phospho_Site(26-28)4652025465Tyr_Phospho_Site(1 3-19)4662025466Tyr_Phospho_Site(21 1-219)4672025467Tyr_Phospho_Site(726-733)46820254682E-90 >giI3l 28180 (AC004521) citrate synthetase [Arabidopsis thaliana]Length = 47446920254696E-94 >gbjAAD35003.1 1AF1443859 (AF144385) thioredoxin fi [Arabidopsisthaliana]Length = 17847020254701E-128 >gbIAAD2S546.1 1AC0058509 (AC005850) protein kinase [Arabidopsisthaliana]Length = 42447120254717E-81 >spIQ43644INUAM_SOLTU NADH-UBIQUINONE OXIDOREDUCTASE75 KD SUBUNIT PRECURSOR (COMPLEX I-75KD) (CI-75KD) (76 KDMITOCHONDRIAL COMPLEX I SUBUNIT) >gi|1084434IpirI 1S52737 NADHdehydrogenase (ubiquinone) (EC 1.6.5.3) 76K chain precursor - potato>gi|758340IembICAA59818i (X85808) 76 kDa mitochondrial complex I subunit[Solanum tuberosum]Length = 7384722025472IE-101) >pir11556718 protein kinase 1-Arabidopsis thaliana >gi|166817(L05561) protein kinase [Arabidopsis thaliana]Length = 36247320254738E-47 >gbIAAD2364O.1 1AC0071 196 (AC0071 19) unknown protein [Arabidopsisthalianal Length = 10147420254744E-64 ) >spIP53665IACPM_ARATH ACYL CARRIER PROTEIN,MITOCHONDRIAL PRECURSOR (ACP) (NADH-UBIQUINONEOXIDOREDUCTASE 9.6 KD SUBUNIT) (MTACP-1) >gi|903689 (L23574) acylcarrier protein precursor [Arabidopsis thaliana]>gi|3341 6824752025475Tyr_Phospho_Site(1 275-1282)47620254767E-80 ) >gi|41 85515 (AFi 02824) actin depolymerizing factor 6[Arabidopsis thalianal >gi|6007773IgbIAAF01 035.1 1AF183576 1 (AF183576) actindepolymerizing factor 6 [Arabidopsis thalianal Length = 1464772025477Tyr_Phospho_Site(1 113-1120)47820254786E-65 >spIP49O78IASNS_ARATH ASPARAGINE SYNTHETASE[GLUTAMINE-HYDROLYZING](GLUTAMINE-DEPENDENT ASPARAGINESYNTHETASE) >gij507946 (L29083) glutamine-dependent asparagine synthetase[Arabidopsis thaliana]>gi|5541 701 lembiCABsi 206.11 (AL096860) glutamine-dependent asparagine synthetase [Arabidopsis thaliana]Length = 58447920254797E-18 >embjCAB10394.11 (Z97340) transcription factor like protein[Arabidopsis thalianal Length = 9544802025480Tyr_Phospho_Site(75-83)4812025481Tyr_Phospho_Site(1220-1227)48220254822E-24 >gij4050087 (AFi 09907) S164 [Homo sapiens]Length = 7354832025483Tyr_Phospho_Site(632-639)4842025484Tyr_Phospho_Site(662-668)48520254851 E-92 >gi|2459446 (AC002332) cinnamoyl-CoA reductase [Arabidopsisthaliana]Length = 32148620254863E-42 >9b1AAD56335.1 1AC00932Q22 (AC009326) 60S acidic ribosomal protein,5′ partial [Arabidopsis thalianal Length = 23048720254873′ Tyr_Phospho_Site(674-681)4882025488Zinc Finger C2h2(644-666)4892025489Pkc_Phospho_Site(33-35)49020254908E-81 >gb|AAD49991 .1 1AC007259A (AC007259) Highly similar to Mb proteins[Arabidopsis thalianal Length = 57349120254911E-1 19 >gi|3859599 (AF104919) similar to class I chitinases (Pfam:PF00182, E = 1.2e-142, N = 1) [Arabidopsis thaliana]Length = 28049220254929E-70 >giI4l 91785 (AC00591 7) hydrolase [Arabidopsis thaliana]Length= 3324932025493Pkc_PhosphoSite(10-12)49420254944E-74 ) >gij2914701(AC003974) cytochrome b5 [Arabidopsis thaliana]Length = 1344952025495Pkc_Phospho Site(1 3-15)49620254963E-89 ) >embICAA74372l(YI 4044) geranylgeranyl reductase [Arabidopsisthaliana]Length = 4724972025497Pkc_PhosphoSite(28-30)49820254982E-50 >gi|2613143 (AF030548) tubulin [Oryza sativa]Length = 45149920254995E-23 >gb1AAD45998.1 IACOOS9I 610 (AC00591 6) Contains similarity togb1D88035 glycoprotein specific U OP-glucuronyltransferase from Rattusnorvegicus. [Arabidopsis thaliana]Length = 40550020255002E-23 >embICAAl 6874.21 (AL021749) copper-binding protein-like[Arabidopsis thaliana]Length = 33650120255011E-109 ) >gi|3342249 (AF047719) GA3 [Arabidopsis thaliana]>gi 13342251 (AF047720) GA3 [Arabidopsis thaI iana]>gi|5107824|gbIAAD40137.1 1AF149413_18 (AFI 49413) Arabidopsis thalianacytochrome P450 GA3 (GB:AF047720); Pfam PF00067, Score = 248.8, E = 7.7e-71,N = 1 Length = 50950220255029E-93 >dbjIBAA778l2.1I (AB027228) FASi [Arabidopsis thaliana]Length = 3665032025503Tyr_Phospho_Site(85-93)5042025504Tyr_Phospho_Site(210-217)5052025505Tyr_Phospho_Site(214-221)50620255065E-86 ) >embICAB37Sl4I (AL035540) farnesylated protein (ATFP6)[Arabidopsis thaliana]Length = 15350720255073E-33 >embjCAA96O6Sj (Z71450) CLC-d chloride channel protein[Arabidopsis thalianal Length = 79250820255085′ IE-25 >gi 12245394 (U89771) ARFi-binding protein [Arabidopsisthaliana]Length = 45450920255095′ Pkc_Phospho_Site(63-65)51020255101E-71 >gi|3395756 (U76297) plantacyanin [Arabidopsis thaliana]>gi|3461812 (AC004138) basic blue protein [Arabidopsis thaliana]Length = 1295112025511Pkc_Phospho_Site(147-149)5122025512Pkc_Phospho_Site(30-32)51320255134E-69 >gbIAAB70035.1 IAAB7003S (AC002534) chloroplast prephenatedehydratase Arabido sis thaliana Len th = 4245142025514Tyr_Phospho_Site(48-55)5152025515Tyr_Phospho_Site(771-779)51620255169E-97 >gb|AAD32773.1IAC007661j10 (AC007661) growth regulator protein[Arabidopsis thaliana]Length = 63851720255171E-14 >giI4l 00433 (AF000378) beta-glucosidase [Glycine max]Length = 2065182025518IE-43>spIPI1139ITBAI_ARATH TUBULIN ALPHA-i CHAIN>gi|71583IpirIjUBMUAM tubulin alpha-i chain - Arabidopsis thaliana >gi|166896(M21 414) alpha-i -tubulin [Arabidopsis thaliana]>gi|504241 0|gbIAAD38249.1 jACOO6I 93_5 (ACOO61 93) alphal tubulin[Arabidopsis thaliana]Length = 45051920255195′ 1 E-68 >gi 1464621 8jgbjAAD26884.1 1AC007290_3 (AC007290) GTP-bindingprotein [Arabidopsis thaliana]Length = 53752020255205′ Pkc_Phospho_Site(35-37)5212025521Tyr_Phospho_Site(300-307)52220255222E-39 >gbIAAD24368.1 1AC00717t.4 (AC007171) disease resistance responseprotein [Arabidopsis thaliana]Length = 44752320255231E-17 >gi|3128219 (AC004077) selenium-binding protein [Arabidopsisthaliana]Length = 3985242025524Pkc_Phospho_Site(2-4)5252025525Pkc Phos ho Site 2-452620255262E-45 >embfCAB4O994.1 I (AL049640) auxilin-like protein [Arabidopsis5272025527Tyr_Phospho_Site(373-379)5282025528SE-37 >gi 13201613 (AC004669) glutathione 5-transferase [Arabidopsisthaliana]Length = 2155292025529lE-IQ0 >spIP42762IERD1ARATH ERDi PROTEIN PRECURSOR>gi|541859Ipir|IJN0901 ERDi protein - Arabidopsis thaliana>gi|497629IdbjjBAA04506i (D17582) ERDi protein [Arabidopsis thaliana]Length = 94553020255303′ Pkc_Phospho_Site(193-195)53120255313′ Tyr_Phospho_Site(15-22)5322025532Tyr_Phospho_Site(850-857)53320255333E-94 >spIO24456IGBLPARATHGUANINE NUCLEOTIDE-BINDINGPROTEIN BETA SUBUNIT-LIKE PROTEIN (WD-40 REPEAT AUXIN-DEPENDENT PROTEIN ARCA) >gij2289095 (U77381) WD-40 repeat protein[Arabidopsis thalianal Length = 3275342025534Tyr_Phospho_Site(133-140)5352025535Tyr_Phospho_Site(493-499)5362025536Tyr_Phospho_Site(1079-1086)53720255371E-67 >sp1038799|ODPBARATH PYRUVATE DEHYDROGENASE ElCOMPONENT BETA SUBUN IT, MITOCHONDRIAL PRECURSOR (PDHEl -B)>gi|520478 (U09137) pyruvate dehydrogenase El beta subunit [Arabidopsisthaliana]>gij 1090498 jprfj 201 9230A pyruvate dehydrogenase [Arabidopsisthalianal Length = 36353820255388E-66 >gbIAAD25555A JAC005850 12 (AC005850) PSI type III chlorophyll a/b-binding protein [Arabidopsis thaliana]Length 27353920255393′ Pkc PhosphoSite(34-36)54020255403′ Tyr_Phospho_Site(l 061-1067)54120255415′ 3E-50 >gi|3850823jembjCAA77136|(Y18351) U2 snRNP auxiliary factor,large subunit [Nicotiana plumbaginifolia]Length = 55554220255425′ 4E-83 >9iI2506276Isp1P21238IRUBA_ARATH RUBISCO SUBUNITBINDING-PROTEIN ALPHA SUBUNIT PRECURSOR (60 KD CHAPERONINALPHA SUBUNIT) (CPN-60 ALPHA) >gi|2129561 IpirIlS7l 235 chaperonin-60alpha chain - Arabidopsis thaliana >gif 1223910 (U49357) chaperonin-60 alphasubunit [Arabidopsis thaliana]>gi54320255438E-13 >gb|AAD55496.1 jAC0081486 (AC008148) phosphoglucomutase[Arabidopsis thalianal Length = 61554420255447E-86 >emb(CAB42911.1 (AL049862) protein I photosystem II oxygen-evolving complex [Arabidopsis thaliana]>gi|57485021emb1CAB53092.1(AJ 145957) precursor of the 33 kDa subunit of the oxygen evolving complex[Arabidopsis thaliana]Length = 33154520255451 E-58 >gbIAAD22371.11AC0065803 (AC006580) chloroplast nucleoid DNAbinding protein (Arabidopsis thaliana]Length = 52754620255467E-17 >gi|2708750 (AC003952) physical impedence protein[Arabidopsis thaliana]Length = 45254720255472E-30 >gbIAAD4998O.1 (AC008075 13 (AC008075) Similar to gbjAFl 10333PrMC3 protein from Pinus radiata and is a member of PFjOO135Carboxylesterases family. EST gb(N37841 comes from this gene. [Arabidopsisthalianal Length = 33654820255482E-86 >embICAAl 65521 (AL021635) HSP associated protein like[Arabidopsis thalianal Length = 6275492025549Pkc_PhosphoSite(49-51)55020255502E-68 >gbjAAD23619.1fAC007168_10 (AC007168) beta-hydroxyacyl-ACPdehydratase [Arabidopsis thaliana]Length = 1455512025551Rgd(323-325)55220255521E-10g >spIP53780IMETCARATH CYSTATHIONINE BETA-LYASEPRECURSOR (CBL) (BETA-CYSTATHIONASE) (CYSTEINE LYASE)>gi|21295671pir1 jS61429 cystathionine beta-lyase (EC 4.4.1.8) - Arabidopsisthaliana >gi|704397 (L4051 1) cystathionine55320255531E-12 >gblAAD464l2.1 1AF0962629 (AF096262) ER6 protein (Lycopersiconesculentum]Length = 1685542025554Pkc_PhosphoSite(90-92)55520255554E-40 >gb IAAD251 38.11AC007 1274 (AC007 127) ubiquitin protein [Arabidopsisthalianal Length = 55155620255561E-91 >emb(CAB43428.11 (AL050300) protein [Arabidopsis thaliana]Length = 20955720255574E-98 >gi|3l 38972 (AF038505) dihydrolipoylacyltransferase subunit ofthe branched-chain aipha-keto acid dehydrogenase complex [Arabidopsis thaliana]Length48355820255583′ Tyr_Phospho_Site(373-380)55920255598E-36 >gif3831439 (AC005819) cytochrome b5 [Arabidopsis thalianall>gi|44159451gb1AAD20175j (AC006418) cytochrome b5 [Arabidopsis thaliana)Length = 13256020255602E-41 >db1IBAA82866.1 I (AB023895) tubby-like protein [Lemnapaucicostata]Length 4285612025561Tyr_Phospho_Site(276-283)5622025562Pkc_Phospho_Site(241-243)5632025563Tyr_Phospho_Site(1211-1218)5642025564Tyr_Phospho_Site(260-266)56520255657E-50 >spjOO4421jSRI4ARATH SIGNAL RECOGNITION PARTICLE 14 KD56620255664E-76 >embjCAB4S9 14.11 (AL080283) putaive DNA-binding protein5672025567Tyr_Phospho_Site(3 19-327)5682025568Rgd(832-834)56920255692E-60 >gij2583125(AC002387) transketolase precursor [Arabidopsisthaliana]Length = 7415702025570Zinc Finger C2h2(1 13-134)5712025571Tyr_Phospho_Site(562-568)5722025572Tyr_Phospho_Site(142-150)57320255732E-67 >gi|3249066(AC004473) Similar to S. cerevisiae SIKI P proteingb1984964. ESTs gbjFl 5433 and gbjAA39Sl 58 come from this gene. [Arabidopsisthalianal Length = 5115742025574Tyr_Phospho_Site(110-116)5752025575Tyr_Phospho_Site(37-45)57620255764E-52 >embICAB37481.11 (AL035539) amino acid transport protein[Arabidopsis thaliana]Length 43657720255779E-37 >gb|AAD27568.1jAF1141719 (AF114171) H beta 58 homolog [Sorghumbicolor]Length = 61657820255783E-31 >gbIAAD31847.1IAF133531 I (AF133531) water channel protein MipI[Mesembryanthemum crystallinumi Length = 25257920255796E-47 >pirIlS7l 372 embryonic abundant protein Em6 - Arabidopsisthaliana >gi|556805fembICAA77508I (Zi 1157) Em protein [Arabidopsis thaliana]Length = 9258020255805′ 7E-1 8 >gi|2792338 (AF040570) oxidoreductase [Amycolatopsismediterranei]Length 3305812025581Tyr_Phospho_Site(1158-1 165)5822025582SE-32 ′ dbjIBAA24863I (AB007893) K1AA0433 [Homo sapiens]Length = 12435832025583Pkc_Phospho Site(1 0-12)58420255848E-45 >gbIAAD4392O.1 AFi 304411 (AFI 30441) UVB-resistance protein UVR8[Arabidopsis thaliana]Length = 44058520255851E-104 >dbjlBAA040491 (D16628) ATsEH [Arabidopsis thaliana]>gi|2760840 IgbIAAB95308.1 (AC003 105) soluble epoxide hydrolase [Arabidopsisthaliana]Length = 3215862025586Rgd(21 3-21 5)5872025587Pkc_Phospho_Site(21-23)58820255881E-26 >dbjIBAA33Ol2i (AB017026) oxysterol-binding protein [Musmusculus]Length = 41058920255897E-85 ) >gi|2642159 (ACOO3000) mannose-1-phosphateguanyltransferase [Arabidopsis thaliana}>gi(3598958 (AF076484) GDP-mannosepyrophosphorylase [Arabidopsis thalianal >giI4l 51 925 (AF108660) CYTi protein[Arabidopsis thaliana]Length = 36159020255901E-47 >spIP9341IICGIC_ORYSA G1JS-SPECIFIC CYCLIN C-TYPE>gi|16956981dbjjBAA13181 I (D86925) C-type cyclin [Oryza satival Length = 25759120255910 >gij22621 70 (AC002329) predicted glycosyl hydrofase [Arabidopsisthaliana]Length = 37559220255925′ Tyr_Phospho_Site(839-847)59320255935′ Pkc_Phospho_Site(34-36)5942025594Tyr_Phospho_Site(153-160)59520255954E-55 >9i13367536 (AC004392) Contains similarity to symbiosis-relatedlike protein F1N2O.80 gi|2961343 from A. thaliana BAG gbIALO22l4O. ESTgbjT04695 comes from this gene. [Arabidopsis thaliana]Length = 1495962025596Pkc_Phospho_Site(57-59)5972025597Pkc_Phospho_Site(5-7)5982025598Tyr_Phospho_Site(542-548)5992025599Pkc_Phospho_Site(65-67)60020256002E-63 >spjPl 95951UDPG_SOLTU UTP-GLUCOSE-1 -PHOSPHATEURIDYLYLTRANSFERASE (UDP-GLUCOSE PYROPHOSPHORYLASE)(UDPGP) (UGPASE) >gi|67061 pin IXNPOU UTP-glucose-1 -phosphateuridylyltransferase (EC 2.7.7.9) - potato >gi 1218001 ldbi IBAAOOS7OI (D00667)UDP-glucose pyrophosphorylase precursor [Solanum tuberosum]Length = 47760120256016E-59 >gbIAAD24412.1 1AF0363099 (AF036309) scarecrow-like 14 [Arabidopsisthalianal Length = 80860220256024E-89 >emblCAB42558.1I (AJ131214) SF2IASF-like splicing modulatorSrp3O, variant 1 [Arabidopsis thaliana]Length = 25660320256031 E-1 24 ) >dbjlBAA34687I (ABOI 6819) UDP-glucose glucosyltransferase[Arabidopsis thaliana]Length = 4816042025604Rgd(263-265)60520256059E-96 >gbiAAD2S9S2.1 IAFO8S7ILI (AF085717) callose synthase catalyticsubunit [Gossypium hirsutum]Length = 189960620256065E-63 >spIP16972IFER_ARATH FERREDOXIN PRECURSOR1996921 pin 1S09979 ferredoxin [2Fe-25]precursor - Arabidopsis thalianaill 6437 IembICAA35754 I (X51 370) ferredoxin precursor [Arabidopsis thaliana]>gi|166698 (M35868) ferro60720256072E-45 >pirl 1S59548 1 -aminocyclopropane-1 -carboxylate oxidase homolog(clone 2A6) - Arabidopsis thaliana >giI599622iembICAA58l 511 (X83096) 2A6[Arabidopsis thaliana]>gii2809261 (AC002560) F21 B7.30 [Arabidopsis thalian60820256085E-63 >spIP25O7OITCH2_ARATH CALMODULIN-RELATED PROTEIN 2,TOUCH-INDUCED >gij25831 69 (AF026473) calmodulin-related protein[Arabidopsis thaliana]Length = 16160920256094E-68 >pir11A36571 ubiquitin I ribosomal protein CEPS2 - Arabidopsisthaliana >gi|166930 (J05507) ubiquitin extension protein (UBQI) [Arabidopsisthaliana]>gi|166932 (J05508) ubiquitin extension protein (UBQ2) [Arabi61020256103E-59 >gbIAAD46006.1 1AC007894A (AC007894) Strong similarity togbIAF092432 protein phosphatase type 2C from Lotus japonicus. EST gb1T76026comes from this gene. [Arabidopsis thalianal Length = 2826112025611TyrphosphoSite(259-265)6122025612lE-ill >sp1023755IEF2BETVU ELONGATION FACTOR 2 (EF-2)>gi|12369714 IembICABO9900 I (Z971 78) elongation factor 2 [Beta vulgaris]Length= 84361320256132E-75 >emblCAB40376.11(AJ012281) adenosine kinase [Zea mays]Length= 33161420256143′ 2E-48 >gi|3660467jembICAA05023l (AJ001807) succinyl-CoA-ligase alphasubunit [Arabidopsis thaliana]Length = 34761520256154E-16 >emb|CAA201 301 (ALO31 179) serine-threonine protein phosphatase[Schizosaccharomyces pombe]Length 33261620256163E-86 >gbIAAD18O95I (AC006416) Similar to gi|1573829 H10816aminopeptidase P homolog (pepP) from Haemophilus influenzae genomegb1U32764. [Arabidopsis thaliana]Length = 45161720256171E-62 ) >pirl1A36571 ubiquitin I ribosomal protein CEP52 - Arabidopsisthaliana >911166930 (J05507) ubiquitin extension protein (UBQI) [Arabidopsisthaliana]>gi|166932 (J05508) ubiguitin extension protein (UBQ2) [Arab6182025618Tyr_Phospho_Site(21 0-218)61920256191E-157 >emblCAA756O2I (Y15382) RNA binding protein [Arabidopsisthalianal Length 3746202025620Pkc_PhosphoSite(34-36)62120256212E-65 ) >embICAB43488.1I (AJ012278) ATP-dependent Cip proteasesubunit CIpP [Arabidopsis thaliana]>gi|5360579ldbj1BAA82065.1 j (AB022326)nCIpPl [Arabidopsis thaliana]Length = 2986222025622Pkc_Phospho_Site(65-67)6232025623Pkc_Phospho_Site(7-9)6242025624Pkc_Phospho_Site(33-35)6252025625lE-SI >spIP42825IDNJH_ARATH DNAJ PROTEIN HOMOLOG ATJ>gi|535588 (L361 13) [Arabidopsis thaliana3 >gi|I 5823561prf1121 1 8338A AtJ2protein [Arabidopsis thaliana]Length = 41962620256264E-25 >spIP2S86OIMT2A_ARATH METALLOTHIONEIN-LIKE PROTEIN 2A(MT-2A) (MT-K) (MT-i G) >giIl 361 9981pir1 1557861 metallothionein 2a -Arabidopsis thaliana >gi|555976 (UI 5108) metallothionein-like protein [Arabidopsisthaliana]>giIiS8O892jprfiI2l 16236A metallothionein 1 [Arabidopsis thaliana]Length = 8162720256275′ 1 E-36 >giIl 066501 (L22302) serine/threonine protein kinase[Arabidopsis thaliana]Length = 42562820256286E-1 I >refINP 006824.1 IPMOV34-34KD1 COP9 subunit 6 (M0V34 homolog, 34kD) >gi 12360945 (U70735) 34 kDa Mov34 homolog [Homo sapiens]Length = 2976292025629Rgd(81 4-816)6302025630Pkc_Phospho_Site(69-71)63120256314E-52 >spIP428SSIZBI4_BRAJU 14 KD ZINC-BINDING PROTEIN (PROTEINKINASE C INHIBITOR) (PKCI) >gij493053 (U09406) protein kinase C inhibitor[Brassica juncea]Length = 1136322025632Pkc_Phospho_Site 39-4163320256337E-53 >gi|3033375 (AC004238) berberine bridge enzyme [Arabidopsisthaliana]Length = 53263420256343E-53 >gbIAAD20097I (AC006532) NADH dehydrogenase [Arabidopsisthaliana]Length = 1036352025635Pkc_PhosphoSite(26-28)63620256361 E-100 >gi|2736147 (AFO21 804) fatty acid hydroxylase Fahip[Arabidopsis thaI lana]>9113132481 (AC003096) fatty acid hydroxylase, FAH 1[Arabidopsis thaliana]Length = 23763720256375E-81 >spjP42799 IGSA1_ARATH GLUTAMATE-i -SEMIALDEHYDE 2,1 -AMINOMUTASE I PRECURSOR (GSA 1) (GLUTAMATE-i -SEMIALDEHYDEAMINOTRANSFERASE 1) (GSA-AT 1) >gi|454357 (U03773) glutamate-i-semialdehyde-2,i-am inomutase [Arabidopsis thalia6382025638Pkc_Phospho_Site(151-153)63920256393E-66 >sp1P496921RL7A_ARATH 60S RIBOSOMAL PROTEIN L7A>gi|2529665 (AC002535) ribosomal protein L7A [Arabidopsis thaliana]Length = 25764020256403E-42 >gb|AAD30649.11AC00608592 (AC006085) photosystem II S KD protein[Arabidopsis thalianal Length = 1066412025641Tyr_Phospho_Site(477-485)64220256421E-64 >gbIAAB94O84.1 I (AF024623) galactose kinase [Arabidopsisthaliana]Length = 4966432025643Pkc_PhosphoSite(60-62)64420256445E-74 >gi|1800281 (U82086) polyubiquitin [Fragaria x ananassa]Length= 38164520256457E-66 >embICAB56l 49.1 (AJ242970) BTF3b-Iike factor [Arabidopsisthaliana]Length = 1656462025646TyrPhosphQSite(636-643)64720256479E-22 >embICAAl 8474.1(AL022347) serine/threonine kinase [Arabidopsisthaliana]Length = 58164820256485E-96 >spIP258I8ITIPG_ARATH TONOPLAST INTRINSIC PROTEIN,GAMMA (GAMMA TIP) (AQUAPORIN-TIP) >gi 199761 lpirl1522202 tonoplastintrinsic protein gamma - Arabidopsis thaliana >gi|16312IembfCAA451 151(X63552) tonoplast intrinsic protein, gamma-TIP(Ara). [Arabidopsis thalianal>gi|166732 (M84344) tonoplast intrinsic protein [Arabidopsis thaliana]>gi 4883600 IgbIAAD3I 569.1 jAC006922_1 (AC006922) tonoplast intrinsic proteingamma [Arabidopsis thaliana]>gi j4451 29lprfI Ii 908432B tonoplast intrinsic proteingamma [Arabidopsis thaliana]Length = 25164920256496E-23 >gi|3763932 (AC004450) protein kinase [Arabidopsis thaliana]Len th = 36765020256504E-77 >gi|3738287 (AC005309) glutathione s-transferase, GST6[Arabidopsis thalianal Length = 26365120256511E-1 0 >gi 14091808 (AF053307) deacetylvindol me 4-0-acetyltransferase[Catharanthus roseus]Length = 43965220256527E-92 >gi|2281 09S (AC002333) cysteine synthase, cpACS1 [Arabidopsisthaliana]Length = 3926532025653Pkc Phos ho Site 24-266542025654Pkc_Phospho_Site(58-60)65520256557E-48 >giI3l 28168 (AC004521) carboxyl-terminal peptidase[Arabidopsis thaliana]Length = 4156562025656S′ Tyr_Phospho_Site(434-441)65720256S75′ 9E-43 >gi|3219782IspIQ60809ICAF1_MOUSE CCR4-ASSOCIATEDFACTOR 1 (CAFi) >gi|726136 (U21 855) mCAF1 protein [Mus musculus]Length = 285658202S6589E-28 >gi|324271 8 (AC003040) acetone-cyanohydrin lyase [Arabidopsisthaliana]Length = 17965920256S93E-12 >gbIAAD14S35i (AC006200) NADC homolog [Arabidopsis thaliana]Length = 323660202S6603E-89 >giI3l 32696 (AFO6I 962) SAR DNA-binding protein-i [Pisumsativum]Length = 56066120256613E-91 >gi|3426048 (ACOOSI 68) hydroxymethylglutaryl-COA lyaseprecursor [Arabidopsis thaliana]Length = 43366220256621E-103 >gbjAAFOl284.11AF1779899 (AF177989) alpha-soluble NSF attachmentprotein; alpha-SNAP [Arabidopsis thaliana]Length = 28966320256634E-96 >emblCAAl 8628.1 j (AL022580) pectinacetylesterase protein[Arabidopsis thaliana]Length = 36266420256646E-58 >gbIAAD46412.1 1AF096262 1 (AF096262) ER6 protein [Lycopersiconesculentum] Length = 16866520256651E-93 >embICAA7l 5871 (Y1 0555) CONSTANS [Arabidopsis thalianal>91 j2695705jembjCAA71 5881 (Y10556) CONSTANS [Arabidopsis thaliana]Length= 3556662025666Tyr_Phospho_Site(598-605)6672025667Pkc_Phospho_Site(1 7-19)6682025668Tyr_Phospho_Site(432-439)66920256691 E-1 02 >gi|832876 (L41 345) ascorbate free radical reductase [Solanumlycopersicumil >gi|10973681prf1121 13407A ascorbate free radical reductase[Lycopersicon esculentum]Length = 43367020256702E-27 >ref IN P004634.1 IPPABP2 I poly(A)-bind ing protein-2 >gi|2895276AF026029 ol A bindin rotein II Homo sa lens Len th = 30667120256713E-59 >embICAA6734Ol (X98808) peroxidase ATP3a [Arabidopsisthalianal Length 33167220256725′ Tyr_Phospho_Site(503-51 1)67320256735′ 2E-35 >gi|24648991emb10AB16803.1 I (Z99708) geranylgeranylpyrophosphate synthase [Arabidopsis thaliana] Length = 37167420256742E-58 >gi|4097555 (U64910) ATFP7 [Arabidopsis thaliana]Length = 11267520256753E-12 >gb|AAD1 56111 (AC006232) beta-1,3-glucanase [Arabidopsis67620256762E-31 >emb|CAB40131.11(Y1 7914) cyclic nucleotide and calmodulin-67720256774E-88 >emb|CAB45799.11(AL080252) nodulin-like protein [Arabidopsis67820256783E-1 5 >emb|CAA74021 (Y1 3673) TATA binding protein-associated factor[Arabidopsis thaliana]Length = 5276792025679Tyr_Phospho_Site(302-31 0)6802025680Tyr_Phospho_Site(1366-1372)6812025681Tyr_Phospho_Site(805-813)6822025682Tyr_Phospho_Site(1200-1208)6832025683Rgd(965-967)68420256847E-41 >giI2l 94138 (AC002062) Similar to Arabidopsis receptor-likeprotein kinase precursor (gbIM84659). [Arabidopsis thaliana]Length 5746852025685IE-22 >spIQ43OI9INLT3_PRUDU NONSPECIFIC LIPID-TRANSFERPROTEIN 3 PRECURSOR (LTP 3) >gi|1321915IembICAA65477l (X96716) lipidtransfer protein [Prunus dulcis]Length = 12368620256863′ Tyr_Phospho_Site(232-240)68720256875′ Pkc_Phospho_Site(13-15)68820256885′ T r Phos ho Site 953-95968920256891E-47 >embICAA544l9I (X77199) heat shock cognate 70-1 [Arabidopsisthaliana]Length = 63769020256903E-60 >gi|3927831 (AC005727) similar to mouse ankyrin 3 [Arabidopsisthaliana]Length = 4266912025691Tyr_Phospho_Site(565-572)6922025692T r Phos ho Site 216-2226932025693Tyr_Phospho_Site(545-552)69420256941 E-33 >embICAA73l 051 (Y1 2503) Man9-mannosidaSe [Sus scrofa]Length= 6596952025695Tyr_Phospho_Site(569-576)6962025696Tyr_Phospho_Site(2-8)69720256971 E-81 >sp1065788IC7B2_ARATH CYTOCHROME P450 71 B2>gi|3164140IdbjIBAA28537I (078605) cytochrome P450 monooxygenaseArabidoysis thaliana Length = 50269820256984E-22 >pir11562626 protein disulfide-isomerase (EC 5.3.4.1) - Castorbean >gi|1134968 (U41385) protein disulphide isomerase PDI [Ricinus communis]>gij15872101prfI12206331A protein disulfide isomerase [Ricinus communi6992025699Tyr_Phospho_Site(1 030-1037)70020257006E-81 ) >gbIAAD38059.1 1AF1533521 (AF153352) CDPK-related kinase 2[Arabidopsis thaliana]Length = 59470120257011 E-1 12 >gi|2529663 (AC002535) lysophospholipase [Arabidopsisthaliana]>gi 13738277 (AC005309) lysophosphol ipase [Arabidopsis thaliana]Length = 32670220257022E-57 >spjQ39O8OIDAD1ARATH DEFENDER AGAINST CELL DEATH 1(DAD-I) >gi 12129570 jpirj 1S71269 DAD-i homolog - Arabidopsis thaliana>giIl 1841 93lemblCAA64837l (X95585) DAD-i homologue [Arabidopsis thaliana]Length = 11570320257034E-37 >spjP02308iH4_WHEAT HISTONE H4 >91170771 IpirIIHSZM4 histoneH4 - maize >gi|816421pir1l506904 histone H4 - Arabidopsis thaliana>gi|21190281pir1lS60475 histone H4 - garden pea >gij21795jemb1CAA249241(X00043) histone H4 [Triticum aestivum]>gi|166740 (M17132) histone H4[Arabidopsis thaliana]>gij166742 (M17133) histone H4 [Arabidopsis thaliana]>gi|168499 (M36659) histone H4 (H4C13) [Zea mays]>gijl68SOl (M13370)histone H4 [Zea mays]>gi|168503 (M13377) histone H4 [Zea mays]>gi|498898(U10042) histone H4 homolog [Pisum sativum]>giIl8O628SIembICABOl 9141(Z79638) histone H4 homologue [Sesbania rostratal >gif3927823 (AC005727)histone H4 [Arabidopsis thaliana]>gij45803851gblAAD24364.11AC007184_4(AC007184) histone H4 [Arabidopsis thaliana]>gi|600991 5IdbilBAA8Sl 20.11(ABOI 8245) histone H4-like protein [Solanum melongena]>gi|2258381prf1|1314298A histone H4 [Arabidopsis thaliana]Length = 10370420257042E-56 >embICAAl 8841 .11 (AL023094) ribosomal protein S16 [Arabidopsisthaliana]Length 11370520257053′ Pkc_Phospho Site(1 0-12)70620257063′ 4E-57 >gij49721 141 emb 1CAB43971 .11 (AL078579) beta-glucosidase[Arabidopsis thaliana]Length = 51770720257075′ Tyr_Phospho_Site(585-591)70820257085′ 3E-69 >giI1169544IspIP42762IERD1_ARATH ERDI PROTEINPRECURSOR >gii54l859lpirlIJNO9Ol ERDI protein - Arabidopsis thaliana>gi|4976291dbj1BAA045061 (017582) ERDi protein [Arabidopsis thaliana]Length = 94570920257099E-30 >emblCABlO2l6.1I (Z97336) disease resistance N like protein[Arabidopsis thaliana]Length = 19967102025710Tyr_Phospho_Site(202-209)7112025711Tyr_Phospho_Site(731-739)71220257121E-103 >embICAAO92O5j (AJ010466) RNA helicase [Arabidopsis thaliana]Length = 45171320257139E-24 >dbj(BAA79274.11 (AP000059) 180aa long hypothetical proteinase I[Aeropyrum pern ix]Length = 18071420257141E-1 21 >gbjAAD26885.11AC007290A (AC007290) purple acid phosphataseprecursor [Arabidopsis thaliana]Length = 4697152025715Tyr_Phospho_Site(1 51-158)71620257161E-17 >gi|2252866 (AF013294) contains region of similarity to SYT[Arabidopsis thaliana]Length = 2307172025717Pkc PhosphoSite(183-185)71820257181E-12 >gi|2586153 (AFOO1S3O) ripening-associated protein [Musaacuminata]Length = 6871920257198E-58 >gb1AAC78267.1 1AAC78267(AC002330) cullin-like 1 protein[Arabidopsis thaliana]Length = 67672020257201E-58 >gbIAAD173I3I (AF123310) NAC domain protein NAM[Arabidopsis thaliana]>gi|43252861gbjAAD1 731 4j (AFI 23311) NAC domainprotein NAM [Arabidopsis thalianal Length = 32072120257215′ 2E-94 >gif2129648|pirjfS71284 MYB-related protein 33,3K - Arabidopsisthaliana >gi|12630951emb1CAA908091 (Z54136) MYB-related protein [Arabidopsisthaliana]Length = 3057222025722Tyr_Phospho_Site(576-584)72320257239E-39 >gbIAAD25662.1 fAC0070204 (AC007020) receptor protein kinase[Arabidopsis thaliana]Length = 23872420257241E-42 >gij3927825 (AC005727) dTDP-glucose 4-6-dehydratase[Arabidoysis thaliana] Length = 34372520257253E-50 >dbj|BAA16755j (090900) dihydrolipoamide dehydrogenase[Synechocystis sp.1 Length = 47872620257262E-73 >spIQ07098IP2A1ARATH SERINE/THREONINE PROTEINPHOSPHATASE PP2A-1 CATALYTIC SUBUNIT >gij4l 87791pirll531 162phosphoprotein phosphatase (EC 3.1.3.16) 2A-alpha catalytic chain (clone EP14a)[Arabidopsis thaliana]>gi|166823 (M96733) protein phosphatase [Arabidopsisthalianal7272025727IE-102 >embjCABl 021 5.11 (Z97336) ankyrin like protein [Arabidopsisthaliana]Length = 9367282025728Tyr_Phospho_Site(854-861)7292025729Tyr_Phospho_Site(1041-1047)73020257303E-28 >spIP41 0561R33B YEAST 605 RIBOSOMAL PROTEIN L33-B (L37B)(YL37) (RP47) >gi|630323jpir1j544069 ribosomal protein L35a.e.cl S - yeast(Saccharomyces cerevisiae) >gi|484241 (L23923) ribosomal protein L37[Saccharomyces cerevisiae] >gi|11420537 Iemb 1CAA994541 (Z751 42) ORFYOR234c Saccharom ces cerevisiae Length = 1077312025731Tyr_Phospho_Site(762-769)73220257322E-29 >embICAA047491 (AJ001414) GTPase activating protein [Yarrowialipolytical Length = 73073320257332E-40 >gij2317912 (U89959) cathepsin B-like cysteine proteinase[Arabidopsis thaliana]Length = 35773420257345E-27 >sPIQ388O5IMT2BARATH METALLOTHIONEIN-LIKE PROTEIN 2B(MT-2B) >gijl36l 9991pir1 557862 metallothionein 2b - Arabidopsis thaliana>gi|1086463 (Ul 1256) metallothionein [Arabidopsis thaliana]Length = 7773520257353E-26 >spIP37223IMAOX_MESCR MALATE OXIDOREDUCTASE (MALICENZYME) (ME) (NADP-DEPENDENT MALIC ENZYME) (NADP-ME)>gi Ii 0843001pir1 1543718 malate dehydrogenase (oxaloacetate-decarboxylating)(NADP+) (EC 1.1.1.40) - common ice plant >gij432380jembjCAA45772j (X64434)malate dehydrogenase (oxaloacetate decarboxylating) (NADP+)[Mesembryanthemum crystallinum]Length = 5857362025736Tyr_Phospho_Site(4-1 0)73720257372E-24 >gi|2435604 (AF026213) strong similarity to Saccharomycescerevisiae endosomal P24A protein (SP:P32802) [Caenorhabditis elegans]Length= 65573820257381E-106 >spIP46O77I143HARATH 14-3-3-LIKE PROTEIN GF14 PHI>gi|1493805 (L091 11) GFI4 protein phi chain [Arabidopsis thaliana]>gi|2232146(AF001414) 14-3-3-like protein GFI4 phi [Arabidopsis thaliana]Length = 26773920257391 E-103 >dbjIBAA34687f (AB016819) UDP-gtucose glucosyltransferase[Arabidopsis thaliana]Length = 48174020257403′ Tyr_Phospho_Site(212-218)74120257415′ 8E-57 >gij7299051sp1Q05999jKPK7 ARATH SERINE/THREONINEPROTEIN KINASE PK7 >gij3205621pir1jJ01385 protein kinase (EC 2.7.1.37) -Arabidopsis thaliana >gi|303500ldbjIBAAO1 716.11 (010910) serine/threonineprotein kinase [Arabidopsis thalianal Length = 57874220257421 E-115 >gi 12435517 (AF024504) contains similarity to peptidase familyAl|Arabidopsis thalianal Length 47274320257431 E-70 >9112688839 (AF003347) ATP phosphoribosyltransferase [Thiaspigoesingense]Length = 40374420257448E-36 >gi|3193326 (AF069299) contains similarity to transcriptionalactivators such as Ra-like and myc-like regulatory R proteins [Arabidopsisthaliana]Length = 3297452025745Tyr_Phospho_Site(l 17-125)74620257461E-103 ) >gbIAAD2I44I.11 (AC006921) salt-inducible protein [Arabidopsisthalianal Length 49774720257471 E-68 >gbjAADl 53971 (AC006223) CCR4-associated transcription factor[Arabidopsis thaliana]Length 25274820257481E-162 >gbjAAD3l347.11AC007212 3 (AC007212) mitochondrial protein[Arabidopsis thaliana]Length 9967492025749Tyr_Phospho_Site(986-993)7502025750Pkc_Phospho_Site(90-92)7512025751Pkc_Phospho_Site(30-32)7522025752Tyr_Phospho_Site(375-382)75320257533′ Pkc_Phospho_Site(68-70)75420257545′ Pkc_Phospho_Site(42-44)75520257551E-165 >embICABS6692.11 (AJ249794) lipoxygenase [Arabidopsis thaliana]Length = 9197562025756Tyr_Phospho_Site(778-786)75720257571 E-48 >embjCABlO248.1 I (Z97336) light induced protein like [Arabidopsisthaliana]Length = 31875820257582E-91 ) >gb|AAD39329.1 IAC007258_18 (AC007258) ABC transporter[Arabidopsis thaliana]Length 14697592025759Tyr_Phospho_Site(71 5-722)76020257601 E-23 >gi|262291 I (AE000933) stomatin-like protein liMethanobacteriumthermoautotrophicuml Length = 2977612025761Tyr_Phospho_Site(245-253)76220257622E-86 >gblAAD38O33.1 1AF1490539 (AF149053) phytochrome kinase substrate76320257636E-96 >spjO64637IC7C2ARATH CYTOCHROME P450 76C2 >gi|29795497642025764Tyr_Phospho_Site(1 3-19)76520257653E-77 ) >gi|2454184 (U80186) pyruvate dehydrogenase El beta subunit[Arabidopsis thaliana]Length = 40676620257662E-71 >spIP492O3IRS13ARATH 40S RIBOSOMAL PROTEIN S13 Length = 15076720257671E-83 >embjCAB55622. 1J(AJOl 1044) cysteine synthase [Arabidopsisthaliana]Length = 17676820257681 E-90 ) >gi|3219355(AF062371) ROOT HAIRLESS I [Arabidopsisthaliana]>gi(5733871I9bIAAD49759.11AC007932_7 (AC007932) Identical togb1AF062371 ROOT HAIRLESS 1 (RHLI) from Arabidopsis thaliana. ESTsgb1H37372, gbIAA6513l3 and gb1Z29767 come from this gene. Length = 35576920257697E-56 >emblCAB5275O.l I (AJ245632) photosystem I subunit VI precursor[Arabidopsis thaliana]Length = 14577020257701E-59 >sp1P49691IRL4_ARATH605 RIBOSOMAL PROTEIN L4 (Li) Length = 40477120257712E-34 >gbjAAD4898l .1 jAF162444 13 (AFi 62444) contains similarity to Solanumlycopersicum (tomato) wound induced protein (GB:X59882) [Arabidopsis thaliana]Length = 8777220257721E-40 >embjCAB4352O.1 f (AJ238802) MAP kinase [Arabidopsis thaliana]Length = 5497732025773Tyr_Phospho_Site(1 248-1254)77420257745′ 4E-91 >911441 5924IgbIAAD201 551 (AC006282) glucosyl transferase[Arabidopsis thalianal Length = 4957752025775Pkc_PhosphoSite(30-32)77620257769E-94 >gij2062156 (AC001645) jasmonate inducible protein isolog[Arabidopsis thaliana]Length = 45177720257775E-44 >gbjAAD56998.1 1AC0094659 2 (AC009465) mitogen activated proteinkinase kinase [Arabidopsis thaliana]Length = 70077820257780 >gbIAAD4599O.11AC0059162 (AC005916) Similar to gb1U04299 mannosyl-oligosaccharide alpha-1,2-mannosidase from Mus musculus. ESTs gb|R84145and gbIAA3947O7 come from this gene. [Arabidopsis thaliana]Length = 57477920257791E-120 >spIP43288IKSGAARATH SHAGGY RELATED PROTEIN KINASEASK-ALPHA >911541901 IpirlIS4l 596 protein kinase ASK-alpha (EC 2.7.1 .-) -Arabidopsis thaliana >gi(460832jemblCAA53181 I (X75432) shaggy related kinase[Arabidopsis thaliana]>gij17698891embl0AA485381 (X68525) serine /threonineprotein kinase [Arabidopsis thaliana]Length = 40578020257804E-16 >spIOO2414IDYL1ANTCR DYNEIN LIGHT CHAIN LC6, FLAGELLAROUTER ARM >gi|22089141dbj1BAA205251 (AB004830) outer arm dynein LC6[Anthocidaris crassispina]Length = 8978120257813E-48 >emblCAA23O48.1 I (AL035394) polygalacturonase [Arabidopsisthaliana]Length = 44478220257821E-36 >gi|3335347 (AC004512) Contains similarity to ARI, RING fingerprotein gb(X98309 from Drosophila melanogaster. ESTs gbjT44383, gb1W43120,gb1N65868, gbIH36Ol 3, gbjAA042241, gb1T76869 and gbIAA042359 come from7832025783Tyr_Phospho_Site(12-19)7842025784Tyr_Phospho_Site(600-606)78520257858E-29 >emblCAAl67l6I (AL021710) glycolate oxidase - like protein7862025786T r Phos ho Site 841-84878720257872E-16 >splP47735RLK5ARATH RECEPTOR-LIKE PROTEIN KINASE 5Arabidopsis thaliana >gi 1166850 (M84660) receptor-like protein kinase[Arabidopsis thaliana]>gij2842492jemb|CAA1 6889.1|(ALO2 1749) receptor-likeprotein kinase 5 precursor (RLKS) [Arabidopsis thaliana]Length = 9997882025788Tyr_Phospho_Site(378-385)78920257892E-62 >gbIAAD28243.1 1AF1213569 (AF121356) peroxiredoxin TPx2[Arabidopsis thaliana]Length = 16279020257902E-24 >gbIAAD4O132.1 1AF149413.93 (AF149413) contains similarity toarabinosidase [Arabidopsis thaliana]Length 52179120257919E-80 >gbjAAD34674.11AC0063412 (AC006341) Is a member of PF1004817922025792Rgd(373-375)79320257933′ 9E-24 >gif13507831sp1P47735jRLK5_ARATH RECEPTOR-LIKE PROTEINprecursor - Arabidopsis thaliana >giIl 66850 (M84660) receptor-like protein kinase[Arabidopsis thaliana]>gi|28424921embiCAA16889.1 I (AL021749) receptor-likeprotein kinase 5 recursor RLK5 Arabido sis thaliana Len th 99979420257943′ Pkc_Phospho_Site(27-29)79520257955′ Pkc_Phospho_Site(25-27)7962025796Tyr_Phospho_Site(1216-1224)7972025797Zinc Protease(338-347)79820257981E-104 >gij3661 595 (AFO91 844) aminoalcoholphosphotransferaseArabido sis thaliana Len th 38979920257998E-73 >gi|41 85143 (AC005724) signal recognition particle receptor beta80020258005E-62 >spIO222O3IC983ARATHCYTOCHROME P450 98A3 >gi|26233038012025801Pkc_PhosphoSite(73-75)80220258024E-77 >embICABlO4l9.1 I (Z97341) transcription factor like protein80320258037E-18 >gi(2576361 (U39782) lysine and histidine specific transporter8042025804Tyr_Phospho_Site(1043-1051)80520258055′ Srp54(488-501)80620258065′ Tyr_Phospho_Site(228-236)8072025807IE-14 >gi|1657619 (U72504) G5p [Arabidopsis thaliana]>gij3068710(AF049236) transmembrane protein G5p [Arabidopsis thalianal Length = 58880820258088E-83 >spIP1 61 27ICHLIARATH MAGNESIUM-CHELATASE SUBUNIT CHLIPRECURSOR (PROTEIN CS/CH-42) (MG-PROTOPORPHYRIN IX CHELATASE)>gi|81656fpirf IS 12785 protein ch-42 precursor, chloroplast - Arabidopsis thaliana>gi|10201001embjCAA62754I (X91 411) protoporphyrin-IX Mg-chetalase[Arabidopsis thalianal >giI2832653IembICAA16728|(AL021710) protein ch-42precursor, chloroplast [Arabidopsis thaliana]>gi 14490290 lemb 1CAB3856 1.11(X51 799) chloroplast protein [Arabidopsis thaliana]>911228771 jprfj|1 811 226A ccsAgene [Euglena gracilis]Length = 4248092025809Tyr_Phospho_Site(960-967)81020258105E-32 >gi121 941 38 (AC002062) Similar to Arabidopsis receptor-likeprotein kinase precursor (gb1M84659). [Arabidopsis thaliana]Length 5748112025811Pkc_PhosphoSite(29-31)81220258124E-50 ) >embICAAl 8735.1 j (AL022604) UDP-galactose transporter-likeprotein [Arabidopsis thaliana]Length 1028132025813Tyr_Phospho_Site(1219-1225)8142025814T r Phos ho Site 473-4808152025815Pkc_Phospho_Site(80-82)81620258162E-45 >embjCAB375O7I(AL035540) probable H+-transporting ATPase82120258213E-82 >gi 132491 10 (ACOO3I 14) T12M4.6 [Arabidopsis thaliana]Length = 46782220258221E-1 14 >9113894157 (AC005312) protein kinase, 3′ partial [Arabidopsisthaliana]Length = 91082320258234E-39 >gbJAAD34674.1 AC0063412 (AC006341) Is a member of PF100481Protein hos hatase 2C famil . Arabido sis thaliana Len th = 49182420258248E-88 ) >gbIAAD40139.1|AF149413_20 (AF149413) similar to malatedehydrogenases; Pfam PF00390, Score = 1290.5. E = 0, N1 [Arabidopsis thaliana]Length = 58882520258251 E-50 >emblCAB4S5Ol .1 (AL079349) serine/threonine-specific proteinkinase MHK [Arabidopsis thaliana]Length = 4438262025826Rgd(784-786)82720258274E-42 >dbj|BAA83470.1 (AB008847) Csf-2 [Cucumis sativusj Length = 15182820258282E-59 >gij3335378 (AC003028) Myb-related transcription activator[Arabidopsis thaliana]Length = 29182920258293E-22 >refjNP 000657.1 IPACYl I aminoacylase 1>gi|461 4661sp1Q031 54IACY1_HUMAN AMINOACYLASE-1 (N-ACYL-L-AMINO-ACID AMIDOHYDROLASE) (ACY-1) >gi|1082202|pir|IA47488 aminoacylase (EC3.5.1.14) - human >gi(178071 (L07548) aminoacylase-1 [Homo sapiens]>gi|285903jdbjfBAA033971 (D14524) aminoacylase-1 [Homo sapiens]>gi|303595IdbjjBAAO38141 (D16307) 45kDa protein [Homo sapiens]Length = 40883020258301 E-24 >embJCABl 0449.11 (Z97341) limonene cyclase like protein[Arabidopsis thaliana]Length = 102483120258311E-135 >gbIAAD4O139.11AF149413_20 (AF149413) similar to malatedehydrogenases; Pfam PF00390, Score = 1 290.5. E0, N1 [Arabidopsis thaliana]Length = 58883220258325E-28 >dbjjBAAl3l35j (D86598) antifreeze-like protein (af7O) |Piceaabies]Length = 77983320258333′ Tyr_Phospho_Site(548-554)83420258345′ 3E-55 >gij3522931 (AC002535) Na+ICa2+exchanger [Arabidopsisthaliana]Length = 53883520258355′ Wd Repeats(44-58)83620258365′ Pkc Phos ho Site 32-348372025837Tyr_Phospho_Site(62-69)83820258384E-48 >gi|2739044 (AF024651) polyphosphoinositide binding proteinSshlp [Glycine max]Length = 32483920258399E-23 >spjP29 1 O2fLEU3BRANA 3-ISOPROPYLMALATEDEHYDROGENASE PRECURSOR (BETA-IPM DEHYDROGENASE) (IMDH) (3-IPM-DH) >gij8l 6761pir1152051 0 3-isopropylmalate dehydrogenase (EC 1.1.1.85)precursor - rape >gi 117827 IembICAA42596 I (X59970) 3-isopropylmalatedehydrogenase [Brassica napusi8402025840Pkc_PhosphoSite(2-4)84120258412E-27 >gbIAAD29832.1 1AC006202 10 (AC006202) carbonic anhydrase[Arabidopsis thaliana]Length = 2488422025842Tyr_Phospho_Site(1 194-1201)84320258438E-80 >gbIAAD48948.1 IAFi 47262.91 (AF147262) contains similarity to Pfamfamily PFOO400 -WD domain, G-beta repeat; score37.6, E2.9e-07, N = 3(Arabidopsis thaliana]Length = 72884420258441E-102 >emblCAB45976.1 I (AL080318) copper amine oxidase-like protein[Arabidopsis thaliana]Length = 7568452025845Pkc_Phospho_Site(64-66)8462025846Tyr_Phospho_Site(41 5-422)84720258471E-75 >embICAA648I9I (X95572) salt-tolerance protein [Arabidopsis85020258507E-13 >gif3643807 (AF062071) zinc finger protein ZNF216 [Musmusculus]Length = 2138512025851Pkc_PhosphoSite(246-248)85220258525′ 4E-80 >gi|3264805 (AFO7I 788) phosphoenolpyruvate carboxylase[Arabidopsis thaliana]>gif4O7963OjembjCAAl 04861 (AJ 131710) phospho enolepyruvate carboxylase [Arabidopsis thaliana]Length = 96885320258535′ 2E-28 >gi|58817151dbj1BAA84406.1I (AP000423) ribosomal protein L33[Arabidopsis thaliana]Length = 6685420258541E-11 >dbjlBAA24382l (ABOOl 389) CLBI [Lycopersicon esculentumiLength = 5058552025855Tyr_Phospho_Site(342-349)85620258562E-14 >embICAB56l46.1l(AL117669) large secreted proteinI$treptomyces coelicolor A3(2)]Length = 80985720258574E-69 >gi|2914700 (AC003974) tRNA-processing protein SEN3-likeArabido sis thaliana Len th = 100485820258585E-16 >9114191 794 (AC005917) zinc finger-like protein [Arabidopsisthaliana]Length = 6828592025859Pkc_PhosphoSite(102-104)86020258601 E-74 ) >gij2088653 (AFOO21 09) Hsl pro-i related protein isolog[Arabidopsis thaliana]Length = 43586120258611E-26 >gi|2688824 (U93273) auxin-repressed protein [Prunusarmeniaca]Length13386220258623E-66 >spIPl 7S62IMETLARATH S-ADENOSYLMETHIONINE SYNTHETASE2 (METHIONINE ADENOSYLTRANSFERASE 2) (ADOMET SYNTHETASE 2)>gij99756jpir1jJQ0410 methionine adenosyltransferase (EC 2.5.1.6) 2 -Arabidopsis thaliana >gi 1166874 (M3321 7) 5-adenosylmethionine synthetase(sam-2) [Arabidopsis thalianal >gi|45585541gb1AA022647.1 IACOO7I 38_11(AC007138) 5-adenosylmethionine synthase 2 [Arabidopsis thaliana]Length = 3938632025863Tyr_Phospho_Site(514-520)86420258643′ Tyr_Phospho_Site(435-442)86520258653′ Tyr_Phospho_Site(670-676)86620258665′ 9E-1 1 >gij2344901 (AC002388) serine/threonine protein kinaseisolo Arabido sis thaliana Len th = 76286720258675′ Tyr_Phospho_Site(874-881)86820258685′ Tyr_Phospho_Site(769-777)86920258695E-57 >gi|21 60694 (U73528) B′ regulatory subunit of PP2A [Arabidopsis87020258701E-103) >gi|2109293 (U97568) serine/threonine protein kinase[Arabidopsis thaliana]Length = 3478712025871Pkc PhosphoSite(180-182)87220258721E-45 >gbIAAB81 870fAAB81 870 (AC002983) phosphoglyceride transferprotein [Arabidopsis thaliana]Length = 3018732025873Tyr_Phospho_Site(823-829)87420258749E-76 >embl0AB367231 (AL035522) 0-methyltransferase-like protein[Arabidopsis thaliana]Length = 38287520258751 E-31 >embICAAO6997.1 I (AJ006376) subtilisin-like protease [Lycopersiconesculentum]>gi 13687309 IembICAAO700 1.11 (AJ006380) subtilisin-like protease[Lycopersicon esculentum]Length = 76187620258761 E-109 >piriIS372l2 beta-fructofuranosidase (EC 3.2.1.26) - Arabidopsisthaliana >giI4O274OIembICAA526 191 (X7451 4) beta-fructofuranosidase[Arabidopsis thaliana]>gi|757536 Iemb 1CAA52620 |(X74515) beta-fructofuranosidas87720258772E-35 >gi|2702277 (AC003033) cyclin g-associated kinase [Arabidopsis87820258784E-51 >pir11S08534translation elongation factor eEF-1 alpha chain (gene87920258791E-107 >pir11S65533cysteine synthase (EC 4.2.99.8) 3A - Arabidopsisthaliana >gi 1804950 lem bICAA58893I (X84097) cysteine synthase [Arabidopsisthaliana]>gi|10961961prf1121 1 1276A Ser(Ac) thiol lyase [Arabidopsis thalia88020258805E-35 >giI3l 69719 (AFOO7I 09) similar to yeast dcpl [Arabidopsisthaliana]Length = 37088120258811 E-24 >gij40391 53 (AFi 04221)10w temperature and salt responsiveprotein LTI6A [Arabidopsis thaliana]>gi|4325217IgbIAAD17302l (AF122005)hydrophobic protein [Arabidopsis thaliana]Length = 548822025882Pkc_Phospho_Site(13-15)8832025883Pkc_Phospho_Site(45-47)88420258843E-74 >embICAB45999.1 I (Z97338) cytochrome P450 like protein[Arabidopsis thaliana]Length = 47788520258851 E-1 33 >gi|2462753 (AC002292) polygalacturonase [Arabidopsisthaliana]Length = 54088620258863′ 1 E-69 >gi|3522931 (AC002535) Na+ICa2+exchanger [Arabidopsisthaliana]Length = 53888720258875′ Tyr_Phospho_Site(92-98)88820258885′ 9E-94 >gi|4220528jembICAA23001 I (AL035356) glucose-6-phosphateisomerase [Arabidopsis thaliana]Length = 61188920258895′ 5E-33 >giI5454O46IrefINP_006314.1 IpSEC24I secretory protein 24>gi|39476901emb1CAA10335.1I (AJ131245) Sec24B protein [Homo sapiens]Length 12688902025890IE-117 >gi|2353171 (AFOl 5542) sigma factor 1 [Arabidopsis thaliana]>gi 124434081dbi 1BAA2242 Ij (D89993) SigA [Arabidopsis thaliana]>gi 1255851 4IembICAA7464O I (Y1 4252) plastid RNA polymerase sigma factor[Arabidopsis thaliana]>gi 15042421 jgbjAAD3826O. 1 IACOO6I 93 16 (ACOO6189120258919E-93 >dbjIBAA84445.1 I (AP000423) ycf I [Arabidopsis thaliana]Length178689220258928E-51 >pir11553492 RNA-binding protein cp3l precursor - Arabidopsisthaliana >gi|681906IdbjIBAA06520I (D31712) cp3l [Arabidopsis thalianal Length = 3148932025893SE-71 >gbjAAD22128.1 1AC00622490 (AC006224) SOs ribosomal protein L3[Arabidopsis thaliana]Length = 27189420258944E-44 >gbjAAD38269.1 1AC00619355 (AC006193) cytochrome P450[Arabidopsis thaliana]Length = 51089520258952E-63 >embICAA67426I (X98926) thylakoid-bound ascorbate peroxidase[Arabidopsis thaliana]Length = 42689620258961E-30 >dbjjBAA236711 (D89063) oligosaccharyltransferaSe [Musmusculus]Length = 4418972025897Tyr_Phospho_Site(228-234)89820258983E-82 >pirIIS20918 probable serine/threonine-specific protein kinaseATPK64 (EC 2.7.I.-)-Arabidopsis thaliana >gi|217843IdbjIBAA01731I (D10937)protein kinase [Arabidopsis thaliana]Length = 49889920258998E-76 >sp 1004921 IHMZ2_ARATH FERROCHELATASE II, CHLOROPLASTPRECURSOR (PROTOHEME FERRO-LYASE) (HEME SYNTHETASE)>gi 11946377 (U932 15) ferrochelatase precusor isolog [Arabidopsis thai ana]>gi|2347202 (AC002338) ferrochelatase pr900202S900Pkc_PhosphoSite(17-19)90120259011E-25 >gij3873408 (L76926) zinc finger protein [Arabidopsis thaliana]Length = 30490220259025′ Tyr_Phospho_Site(462-470)90320259035′ 2E-82 >gi|2444271 (AFOl 9637) amino acid or GABA permease[Arabidopsis thaliana]Length = 51690420259044E-67 >dbj(BAA84422.1 I (AP000423) ribosomal protein L16 [Arabidopsisthaliana Length = 13590520259051E-96 >pirIIS35701 translation elongation factor G, chioroplast - soybeanLength 7879062025906Tyr_Phospho_Site(1 072-1079)90720259071E-33 >gbIAAD45999.11AC00591611 (AC005916) Similar to gb1Z84571anthranilate N-hydroxycinnamoyl/benzoyltransferase from Dianthus caryophyl us.[Arabidopsis thalianal Length 4429082025908Pkc_Phospho_Site(10-12)9092025909Tyr_Phospho_Site(918-925)9102025910Tyr_Phospho_Site(1165-1171)91120259114E-82 >gi|3887237 (AC005169) Cys3His zinc-finger protein [Arabidopsisthalianal Length = 35991220259124E-91 >gi|3643609 (AC005395) Cys3His zinc finger protein [Arabidopsisthalianal Length = 3159132025913Tyr_Phospho_Site(1 80-187)91420259145E-38 >gbIAAD19755I (AC006413) nuclear phosphoprotein (containsmultiple TPR repeats prosite:Q00050005) [Arabidopsis thaliana]Length = 11159152025915Tyr Phospho S,te(31-39)9162025916Tyr_Phospho_Site(619-625)91720259174E-85 >pir11S57784 4-coumarate-CoA ligase (EC 6.2.1.12) - Arabidopsisthaliana >gi|609340 (U18675) 4-coumarate----coenzyme A ligase [Arabidopsisthaliana]>gij57021 84IgbIAAD471 91 .1 AFi 06084_1 (AFi 06084) 4-coumarate:CoAligase I (Arabidopsis thaliana]Length = 5619182025918T r Phos ho Site 1401-14099192025919Tyr_Phospho_Site(165-171)9202025920Tyr_Phospho_Site(218-225)92120259213′ Tyr_Phospho_Site(167-173)92220259225′ Pkc_Phospho_Site(1 16-118)92320259235′ 1 E-75 >gij6l 1 9523Igb1AAF041 67.1 jACOI 15608 (ACOI 1560) amino acidtransporter [Arabidopsis thaliana]Length = 58492420259245′ 4E-22 >gi|495366embjCAA933l6j (Z69370) nitrite transporter [Cucumissativusi Length 4849252025925IE-82 ) >gi 2829900 (AC002311) similar to ripening-induced protein,gpjAJ001449 2465015 and major latex protein, gpIX91961 1107495 [Arabidopsisthaliana]Length 1489262025926Tyr_Phospho_Site(270-276)9272025927Tyr_Phospho_Site(902-910)9282025928Tyr_Phospho_Site(477-483)9292025929Pkc_Phospho_Site(39-41)9302025930Tyr_Phospho_Site(214-222)93120259315E-52 >dbjjBAA33I96j (ABOl 7564) dof zinc finger protein [Arabidopsisthaliana]Length = 19493220259321 E-69 >gbjAAD28777.1 1AF1341301 (AF134130) Lhcb6 protein [Arabidopsisthaliana]Length = 2589332025933Tyr_Phospho_Site(333-340)93420259342E-58 >gbiAAFOO665.11AC00815397 (AC008153) 40S ribosomal protein s14[Arabidopsis thaliana]Length = 1509352025935Tyr_Phospho_Site(622-628)93620259361E-89 >dbjIBAA84424.1 I (AP000423) ribosomal protein L22 [Arabidopsisthaliana]Length = 16093720259378E-82 ) >gi|1946360 (U93215) elicitor response element binding proteinWRKY3 isolog [Arabidopsis thaliana]Length = 38093820259385′ Pkc_Phospho_Site(190-192)9392025939Tyr_Phospho_Site(1103-1110)94020259401E-1 14 >gi|321 2875 (AC004005) polygalacturonase [Arabidopsisthaliana]Length = 39494120259411E-67 >embICAA2003OI (ALO31 135) protein kinase - like protein[Arabidopsis thaliana]Length = 35694220259421E-1 17 >gbIAADI 81091 (AC006403) protein kinase [Arabidopsis thaliana]Length = 4079432025943Tyr_Phospho_Site(288-296)94420259444E-93 >gbIAADI 73671 (AF128396) contains similarity to Medicagotruncatula N7 protein (GB:Y1 761 3) [Arabidopsis thaliana]Length 3179452025945Pkc_Phospho Site(1 30-132)94620259461 E-159 >gi|2340166 (AFOO8 124) glutathione S-conjugate transportingATPase [Arabidopsis thaliana]>gi|2459949 (AF008125) multidrug resistance-associated protein homolog [Arabidopsis thaliana]Length = 16229472025947Tyr_Phospho_Site(1 152-1158)9482025948Tyr_Phospho_Site(671-678)94920259491E-13 >gbIAAD237I8.11AC005956_7 (AC005956) zinc finger protein[Arabidopsis thaliana]Length = 2179502025950Pkc_Phospho_Site(37-39)95120259512E-18 >gbIAADI6006.1I (AF078035) translation initiation factor 1F2 [Homosapiens]Length = 122095220259526E-99 >gi 139831 25 (AF097648) phosphate/triose-phosphate translocatorprecursor [Arabidopsis thaliana]Length = 4109532025953Tyr_Phospho_Site(1 72-179)95420259544E-61 >emblCABIO33l .11 (Z97339) pyruvate, orthophosphate dikinaseArabido sis thaliana Len th 96095520259553′ Tyr_Phospho_Site(635-643)95620259563′ Tyr_Phospho_Site(592-599)95720259573′ Pkc_Phospho_Site(94-96)95820259585′ Tyr_Phospho_Site(463-470)95920259595′ 1 E-1 1 >giJ6321 OO7lrefINP_011086.1 IBUR6I Transcriptional regulator whichfunctions in modulating the activity of the general transcription machinery in vivo;Bur6p >gi|731531jspIP40096jNCB1_YEAST CLASS 2 TRANSCRIPTIONREPRESSOR >gij1077721jpirjjS50662 hypothetical protein YER159c - yeast (Sa96020259601 E-92 >gb(AAD22 126.1 lACOO622kfi (AC006224) pectinesterase [Arabidopsisthaliana Length = 51896120259612E-14 >gij1572819 (U70855) similar to the RAS gene family[Caenorhabditis elegansi Length = 62596220259621 E-33 >gbIAADI 74151 (AC006248) serinefthreonine kinase [Arabidopsisthaliana]Length = 3659632025963Rgd(742-744)96420259641E-62 >gbIAAD258O5.1jAC006550_13 (AC006550) Contains FF100010 helix-loop-helix DNA-binding domain. ESTs gblT45640 and gbjT22783 come from thisgene. [Arabidopsis thaliana]Length = 2979652025965Tyr_Phospho_Site(403-41 0)96620259662E-82 >gi|31 76680 (AC003671) Identical to polygajacuronase isoenzymeI beta subunit homolog mRNA gb1U63373. EST gbjAA404878 comes from thisgene. (Arabidopsis thaliana]Length = 62696720259673E-85 ) >gbfAAD223O9.1 1AC007047_18 (AC007047) beta-ketoacyl-CoAsynthase [Arabidopsis thaliana]Length 51296820259682E-57 >gbIAAD29842.1 jAF0646941 (AF064694) catechol 0-methyltransferase;Omt ll;THATU;2 [Thalictrum tuberosum]Length = 3629692025969Pkc_PhosphoSite(43-45)97020259706E-29 >dbjjBAA32422I (AB008107) ethylene responsive element bindingfactor 5 [Arabidopsis thaliana]Length = 3009712025971Pkc_Phospho_Site(164-166)9722025972Pkc_Phospho_Site(36-38)97320259733′ 1E-48 >gi|2129516jpir1 jS59548 1-aminocyclopropane-1-carboxylateoxidase homolog (clone 2A6) - Arabidopsis thaliana >gi|5996221emb1CAA581 511(X83096) 2A6 [Arabidopsis thaliana]>gi|2809261 (AC002560) F21 B7.30[Arabidopsis thaliana]Length = 36197420259743′ 5E-47 >gi|3650034 (AC005396) flavonol sulfotransferase[Arabidopsis thaliana]Length = 33397520259753′ Tyr_Phospho_Site(371-378)97620259763′ Pkc_Phospho_Site(144-146)97720259775′ 3E-97 >gi|1103318(embjCAA55395( (X78818) casein kinase I [Arabidopsisthaliana]>gij2244791(emb(CAB1O213.1I (Z97336) casein kinase I [Arabidopsisthaliana Len th = 45797820259785′ Pkc_Phospho_Site(9-1 1)97920259795′ Wd Repeats(14-28)98020259805′ 8E-16 >gij45O6Ol3jrefINPOO27O3.IJpPPPIR7j protein phosphatase 1,regulatory subunit 7 >gij2136139jpirjj568209 sds22 protein homolog - human>giI108S028|emb|CAA9O626I (Z50749) yeast sds22 homolog [Homo sapiens]>giJ4633067|gb|AA02661 1.11 (AF067136) protein phosphatase-1 regulatorysubunit 798120259815′ T r Phos ho Site 441-44998220259826E-67 ) >gi|1477480 (U40341) carbamoyl phosphate synthetase largechain [Arabidopsis thaliana]Length = 118798320259834E-50 >gi 141 85141 (AC005724) calmodulin-binding protein [Arabidopsisthaliana]Length = 6529842025984Tyr_Phospho_Site(650-657)98520259858E-15 >gi|3264767 (AF071893) AP2 domain containing protein [Prunusarmeniaca]Length = 2809862025986Pkc_Phospho_Site(8-1 0)9872025987Pkc_Phospho_Site(172-174)98820259882E-25 >gbIAAD1741 5|(AC006248) serine/threonine kinase [Arabidopsisthaliana]Length = 36598920259891 E-91 >gi|2924792 (AC002334) similar to synaptobrevin [Arabidopsisthalianal Length = 2219902025990Tyr_Phospho_Site(947-953)9912025991Tyr_Phospho_Site(2-9)9922025992Tyr_Phospho_Site(41 9-426)99320259935E-47 >gbIAAD25856.1 JAC007197′ 9 (AC007197) dynamin-like protein ADL2[Arabidopsis thaliana]Length = 78299420259945′ 8E-97 >giIl 345132 (U47029) ERECTA [Arabidopsis thaliana]>giIl389566IdbjIBAAl 18691 (D83257) receptor protein kinase [Arabidopsisthaliana]>g 13075386 (A0004484) receptor protein kinase, ERECTA [Arab idopsisthalianal Length = 97699520259955′ 2E-97 >gi|23399781embJGAA721771 (Y11336) RGA1 protein [Arabidopsisthaliana]Length = 58799620259965′ Tyr_Phospho_Site(898-905)99720259975′ 3E-57 >gif1765899lembj0AA692221 (Y07917) Spot 3 protein [Arabidopsisthaliana]>gi|1839244 (U86700) EGE receptor like protein [Arabidopsis thaliana]Length = 62399820259982E-77 >emb10AB45976.1 (AL080318) copper amine oxidase-like protein[Arabidopsis thaliana]Length = 75699920259992E-70 ) >gif3522929 (AC002535) dTDP-glucose 4-6-dehydratase[Arabidopsis thaliana]>gif3738279 (AC005309) dTDP-glucose 4-6-dehydratase[Arabidopsis thalianal Length = 443

[0158]

Expressed sequences of arabidopsis thaliana

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