Microorganism producing polyunsaturated fatty acids and method for producing polyunsaturated fatty acids

Abstract

The object of the present invention is to provide a microorganism that efficiently produces PUFA and a method for producing PUFA using the microorganism. The present invention relates to the following microorganisms capable of producing PUFA, etc.: a microorganism having a polyunsaturated fatty acid (PUFA) metabolic pathway into which a gene encoding an exogenous polyketide synthase dehydratase (PS-DH) domain having an activity higher than that of an endogenous FabA-like β-hydroxyacyl-ACP dehydratase (FabA-DH) domain for 3-hydroxyhexanoyl acyl carrier protein (3-hydroxyhexanoyl ACP) is introduced.

Description

Technical Field

[0001] This invention relates to microorganisms for producing polyunsaturated fatty acids (PUFAs) and methods for manufacturing PUFAs using these microorganisms. Background Technology

[0002] Long-chain fatty acids with multiple unsaturated bonds in their molecules, such as docosahexaenoic acid (DHA), eicosapentaenoic acid (EPA), arachidonic acid (ARA), and docosapentaenoic acid (DPA), are called polyunsaturated fatty acids (PUFAs). PUFAs are known to have various physiological functions, such as the prevention of arteriosclerosis or hyperlipidemia (Non-Patent Literature 1 and Non-Patent Literature 2).

[0003] According to the position of the double bond counting from the methyl end in the molecule, PUFAs can be classified into ω3 fatty acids such as DHA or EPA, ω6 fatty acids such as DPA or ARA, ω9 fatty acids where the double bond is first introduced on the 9th carbon, and ω11 fatty acids where the double bond is first introduced on the 11th carbon.

[0004] There are two known biosynthetic pathways for PUFAs: the aerobic pathway and the anaerobic pathway utilizing polyunsaturated fatty acid polyketide synthases (hereinafter referred to as PUFA-PKS). The aerobic pathway synthesizes PUFAs by introducing double bonds from long-chain fatty acids such as palmitic acid synthesized using fatty acid synthases, either through various desaturase-based methods or by extending the carbon chain through chain elongation enzymes. This pathway has been known for a long time and is present in many organisms (Non-Patent Literature 3). On the other hand, the PUFA-PKS-based anaerobic pathway synthesizes PUFAs from malonyl-CoA (CoA). This pathway is known in some marine bacteria and reticulobacilli eukaryotes as a means of producing DHA or EPA (Non-Patent Literature 4 and Non-Patent Literature 5). Furthermore, an ARA production system, for example, is known from marine aureispira marina (Non-Patent Literature 6).

[0005] PUFA-PKS is a complex enzyme composed of multiple proteins (hereinafter also referred to as a protein complex), and each protein contains multiple functional domains involved in the synthesis of PUFA.

[0006] The functional domains present in PUFA-PKS include: the β-ketoacyl-acyl carrier protein synthase domain (hereinafter referred to as the KS domain), which is believed to participate in the condensation of malonyl ACP and acyl ACP; the acyl carrier protein domain (hereinafter referred to as the ACP domain), which is believed to function as a site for fatty acid synthesis by binding the phosphate pantothenic acid ethylamine group to the acyl group through a thioester bond; the ketone reductase domain (hereinafter referred to as the KR domain), which is believed to reduce the carbonyl group generated by condensation; and the DH structure, which is believed to utilize the hydroxyl group generated by the KR domain to dehydrate and form a double bond. The domains include: the chain elongation factor domain (hereinafter referred to as the CLF domain), which is believed to participate in the carbon chain elongation; the enoyl reductase domain (hereinafter referred to as the ER domain), which is believed to reduce the resulting double bonds; the acyltransferase domain (hereinafter referred to as the AT domain) and malonyl-CoA:acyltransferase domain (hereinafter referred to as the MAT domain), which are believed to participate in the transfer of acyl groups; and the phosphate pantothenicotinamide ethylamine transferase domain (hereinafter referred to as the PPT domain), which is believed to activate the ACP domain. It is believed that these multiple domains work synergistically to elongate the carbon chain of fatty acids.

[0007] As an industrial production method for ARA, there is a known method for separating it from the biomass of mold (Patent Document 1), but there is a problem of a large amount of unsaturated fatty acids other than the target byproducts, and a more efficient ARA production method is needed.

[0008] It is known that the types of PUFAs produced vary depending on the type of PUFA-PKS. For example, PUFA-PKS derived from *Schizochytrium sp.*, *Aurantiochytrium sp.*, and *Moritella marina* produce DHA as the main product; PUFA-PKS derived from *Shewanella oneidensis* and *Photobacterium profundum* produce EPA as the main product; and PUFA-PKS derived from *Aureispira marina* produces ARA as the main product, with almost no other PUFAs produced, or even if other PUFAs are produced, they are produced in small quantities compared to the main product.

[0009] It is evident that PUFA-PKS exhibits high product specificity, and numerous studies have been conducted to date aimed at elucidating the function of PUFA-PKS.

[0010] Non-patent literatures 4 and 7 describe studies on the production of PUFA by cloning the PUFA-PKS gene from Shewanella bacteria or protozoan eukaryotes and expressing it in heterologous organisms.

[0011] Non-Patent Literature 8 discloses that the pfaB gene encoding the AT domain is related to the type of PUFA produced, through research using the pfaB gene, which is a constituent gene of PUFA-PKS derived from Moritella marina, a bacterium that produces DHA, and the pfaB gene, which is a constituent gene of PUFA-PKS derived from Shewanella pneumatophori, a bacterium that produces EPA.

[0012] Non-patent literature 9 discloses that when the DH domain of PUFA-PKS derived from the genus Thraustochytrium is introduced into Escherichia coli, the production of fatty acids increases and the proportion of unsaturated fatty acids increases.

[0013] Existing technical documents

[0014] Patent documents

[0015] Patent Document 1: Japanese Patent Application Publication No. 2006-219528

[0016] Patent Document 2: International Publication No. 2008 / 144473

[0017] Non-patent literature

[0018] Non-patent literature 1: Annu. Nutr. Metabol., 1991, 35, 128-131

[0019] Non-patent literature 2: J. Am. Coll. Nutr., 1994, 13, 658-664

[0020] Non-patent literature 3: Ann. Rev. Biochem., 1983, 52, 537-579

[0021] Non-patent literature 4: Science, 2001, 293, 290-293

[0022] Non-patent literature 5: PLoS One, 2011, 6, e20146

[0023] Non-patent literature 6: Scientific Reports, volume 6, Article number: 35441 (2016), Fig. 5

[0024] Non-patent literature 7: Plant Physiol. Biochem., 2009, 47, 472-478.

[0025] Non-patent literature 8: FEMS Microbiol. Lett., 2009, 295, 170-176

[0026] Non-patent literature 9: Appl. Microbiol. Biotechnol., 2018, 847-856 Summary of the Invention

[0027] The problem that the invention aims to solve

[0028] As for PUFA production systems utilizing existing PUFA-producing microorganisms, there are, for example, ARA production systems utilizing the microorganisms described in Non-Patent Document 6. However, the ARA production rate of such ARA production systems is insufficient at the industrial level. In addition, the method for separating ARA from the biomass of molds as described in Patent Document 1 has the problem of producing a large amount of unsaturated fatty acids other than the target byproduct.

[0029] Therefore, the object of the present invention is to provide a microorganism for the efficient production of PUFA and a method for manufacturing PUFA using the microorganism.

[0030] Methods for solving problems

[0031] The inventors discovered that by introducing a gene into a microorganism capable of producing ω3PUFA, the PS-DH domain of which exhibits higher activity for 3-hydroxyhexanoyl ACP, a fatty acid substrate in the PUFA production system, than the FabA-DH domain, it is possible to efficiently produce ω6PUFA, in which the initial double bond is formed at position ω6 from the terminal carbon atom in the PUFA, instead of producing the original product ω3PUFA, thus completing the present invention.

[0032] 1. A microorganism capable of producing PUFA, wherein a gene encoding an exogenous PS-DH domain with higher activity for 3-hydroxyhexanoyl ACP than the endogenous FabA-DH domain is introduced into a microorganism with a PUFA metabolic pathway.

[0033] 2. The microorganisms described in 1 above, wherein the microorganisms with the PUFA metabolic pathway are microorganisms with the ω3PUFA metabolic pathway, and the PUFAs they can produce are ω6PUFAs.

[0034] 3. Microorganisms as described in 1 or 2 above, wherein the microorganisms with PUFA metabolic pathways are microorganisms with EPA or DHA metabolic pathways, and the PUFAs they can produce are ARA or DPA.

[0035] 4. The microorganisms as described in any one of 1 to 3 above, wherein the microorganisms with the PUFA metabolic pathway originate from the genera *Shewanella*, *Photobacterium*, *Moritella*, *Colwellia*, *Aurantiochytrium*, *Thraustochytrium*, *Ulkenia*, *Parietichytrium*, *Labyrinthula*, *Aplanochytrium*, *Oblongichytrium*, or *Schizochytrium*.

[0036] 5. A microorganism capable of producing PUFA, wherein a gene encoding the domains described in (a) to (j) below having PUFA-PKS activity is introduced into a microorganism lacking a PUFA metabolic pathway, wherein the PS-DH domain exhibits higher activity toward 3-hydroxyhexanoyl ACP than the FabA-DH domain.

[0037] (a) KS domain

[0038] (b) MAT structural domain

[0039] (c) ACP domain

[0040] (d) KR domain

[0041] (e)PS-DH domain

[0042] (f) CLF domain

[0043] (g)AT domain

[0044] (h)FabA-DH domain

[0045] (i) ER domain

[0046] (j) PPT structural domain

[0047] 6. The microorganism as described in 5 above, wherein it possesses all the PUFA synthesis system genes of any one of the microorganisms capable of producing PUFA described in any one of 1 to 4 above.

[0048] 7. The microorganisms described in 5 or 6 above, wherein the PUFA that can be produced is ω6PUFA.

[0049] 8. The microorganism as described in any one of 5 to 7 above, wherein the PUFA that can be produced is ARA or DPA.

[0050] 9. The microorganism as described in any one of 5 to 8 above, wherein the microorganism that does not have the PUFA metabolic pathway belongs to the genera Escherichia, Bacillus, Corynebacterium, Yarrowia, Saccharomyces, Candida, or Pichia.

[0051] 10. The microorganism as described in any one of 1 to 9 above, wherein the PS-DH domain is the PS-DH domain of AraB derived from marine golden spirulina.

[0052] 11. A method for manufacturing a PUFA or a composition containing PUFA, wherein the microorganism described in any one of 1 to 10 above is cultured in a culture medium to generate and accumulate PUFA or a composition containing PUFA in the culture, and PUFA or a composition containing PUFA is collected from the culture.

[0053] 12. A method for manufacturing a PUFA or a composition containing PUFA, wherein a microorganism capable of producing PUFA is used, as described in (I) or (II) below.

[0054] (I) Microorganisms capable of producing PUFA were introduced into microorganisms with a gene encoding a PS-DH domain that has higher activity of p-3-hydroxyhexanoyl ACP than the endogenous FabA-DH domain.

[0055] (II) A microorganism capable of producing PUFA, in which genes encoding the domains described in (a) to (j) below with PUFA-PKS activity are introduced into a microorganism that does not have a PUFA metabolic pathway, wherein the PS-DH domain exhibits higher activity for 3-hydroxyhexanoyl ACP than the FabA-DH domain.

[0056] (a) KS domain

[0057] (b) MAT structural domain

[0058] (c) ACP domain

[0059] (d) KR domain

[0060] (e)PS-DH domain

[0061] (f) CLF domain

[0062] (g)AT domain

[0063] (h)FabA-DH domain

[0064] (i) ER domain

[0065] (j) PPT structural domain

[0066] Invention Effects

[0067] The present invention relates to a microorganism that, by introducing a gene into a microorganism capable of producing PUFAs, exhibits a higher activity towards the PS-DH domain (of which the FabA-DH domain is a fatty acid substrate) than towards the PS-DH domain. This results in a relatively higher reactivity of the PS-DH domain towards 3-hydroxyhexanoyl ACP compared to the FabA-DH domain, thereby enabling the efficient production of the target PUFA or PUFA-containing compositions. The manufacturing method according to the present invention enables the low-cost and high-efficiency production of PUFAs, and can be applied to industrial-scale PUFA production. Attached Figure Description

[0068] Figure 1 A schematic diagram showing the structure of the proteins and their domains that make up PUFA-PKS in various microorganisms is shown. Detailed Implementation

[0069] In this invention, "polyunsaturated fatty acids (PUFAs)" refers to long-chain fatty acids with a carbon chain length of 18 or more and the number of unsaturated bonds of 2 or more. Additionally, in this specification, "domain" refers to a portion of a protein consisting of a continuous amino acid sequence, which is a region within the protein that possesses specific biological activity or function.

[0070] In this invention, "PUFA-PKS" has the same meaning as PUFA synthase. PUFA synthase refers to a group of enzymes that use malonyl-CoA and other enzymes as carbon sources to synthesize specific long-chain unsaturated fatty acids. It contains various domains of KS, MAT, ACP, KR, PS-DH, CLF, AT, FabA-DH, ER, and PPTase (ACOS Lipid Library: PUFA synthase; Science, 2001, 293, 290-293; PLoS One, 2011, 6, e20146, etc.).

[0071] The KS domain is a domain possessed by proteins that constitute protein complexes with PUFA-PKS activity; it refers to the domain involved in the condensation of malonyl ACP and acyl ACP.

[0072] The MAT domain and AT domain are domains of proteins that constitute protein complexes with PUFA-PKS activity, and refer to the domains involved in acyl transfer.

[0073] The ACP domain is a domain possessed by proteins that constitute protein complexes with PUFA-PKS activity. It refers to the domain that functions as a site of fatty acid synthesis and is essential for PUFA-PKS activity by binding the phosphopantothenic acid group to the acyl group via a thioester bond.

[0074] The KR domain is a domain possessed by proteins that constitute protein complexes with PUFA-PKS activity; it refers to the domain that participates in the reduction of ketone groups generated through condensation.

[0075] The PS-DH and FabA-DH domains, which are DH domains, are domains of proteins that constitute protein complexes with PUFA-PKS activity. They are domains that participate in the dehydration of hydroxyl groups generated by reducing ketone groups.

[0076] The CLF domain is a domain possessed by proteins that constitute protein complexes with PUFA-PKS activity; it refers to the domain that participates in the elongation of the carbon chain.

[0077] The ER domain refers to the domain of a protein that constitutes a protein complex with PUFA-PKS activity.

[0078] PPTase is an enzyme that constitutes a protein complex with PUFA-PKS activity; it refers to an enzyme involved in the activation of the ACP domain.

[0079] In this specification, "synergistic effect" refers to the ability of a protein to act as a unit when it coexists with other proteins, and in particular, in this specification, it refers to the ability of a protein to act as a unit with other domains when multiple domains required for PUFA-PKS activity coexist, thereby exhibiting PUFA-PKS activity.

[0080] In this specification, "exogenous" means non-endogenous and of a different species, and is used to indicate the following: the introduction of a gene based on the present invention into a host organism in cases where the host organism before transformation does not have the gene to be introduced by the present invention, the protein encoded by the gene is not substantially expressed, or the amino acid sequence of the protein is encoded by a different gene but does not express the activity of the endogenous protein after transformation.

[0081] In this specification, "host organism" refers to the original organism that becomes the object of gene modification and transformation. When the original organism that becomes the object of transformation through gene introduction is a microorganism, it is also called the parent strain or host strain.

[0082] [microorganism]

[0083] Microorganisms that can be used as microorganisms in this invention include those described in (1) or (2).

[0084] (1) Microorganisms capable of producing PUFA were introduced into microorganisms with a gene encoding an exogenous PS-DH domain that has higher activity of 3-hydroxyhexanoyl ACP than the FabA-DH domain.

[0085] (2) Microorganisms that produce PUFA were introduced into microorganisms that do not have a PUFA metabolic pathway. Genes encoding the KS, MAT, ACP, KR, PS-DH, CLF, AT, FabA-DH, ER, and PPTase domains with PUFA-PKS activity were introduced. Among them, the PS-DH domain showed higher activity for 3-hydroxyhexanoyl ACP than the FabA-DH domain.

[0086] Microorganisms with PUFA metabolic pathways refer to microorganisms that naturally possess the ability to produce PUFAs. Examples of microorganisms with PUFA metabolic pathways include *Shewanella*, *Photobacterium*, *Moritella*, *Colwellia*, *Aurantiochytrium*, *Thraustochytrium*, *Ulkenia*, *Parietichytrium*, *Labyrinthula*, *Aplanochytrium*, *Oblongichytrium*, and *Schizochytrium*.

[0087] Microorganisms with PUFA metabolic pathways are preferred, and examples include microorganisms with DHA metabolic pathways and microorganisms with EPA metabolic pathways.

[0088] Microorganisms possessing DHA metabolic pathways can include, for example, those belonging to the genera *Moritella*, *Colwellia*, *Aurantiochytrium*, *Thraustochytrium*, and *Schizochytrium*. Preferred examples include *Moritella marina*, *Colwellia psychrerythraea*, *Aurantiochytrium limacinum*, and *Thraustochytrium aureum*, but the list is not limited to these species as long as they possess DHA metabolic pathways.

[0089] As for microorganisms with DHA metabolic pathways, microorganisms belonging to the genus *Aurantiochytrium* are preferred, such as *Aurantiochytrium* strain OH4 (accession number FERM BP-11524), etc. Microorganisms with DHA production capacity as mutant strains can also be used.

[0090] The aforementioned *Chrystridium aubergii* OH4 strain is deposited at the Patent Microbial Collection Center of the National Institute for Product Evaluation Technology (NITE), an independent administrative agency located at 1-1 Higashi-1, Chuo-6, Tsukuba City, Ibaraki Prefecture, Japan (Postal Code 305-8566). The deposit date was January 11, 2013 (Heisei 25), and the accession number is FERM BP-11524.

[0091] Microorganisms possessing the EPA metabolic pathway can include, for example, those belonging to the genera *Shewanella*, *Photobacterium*, and *Vibrio*. Preferred examples include *Shewanella oneidensis*, *Shewanella livingstonensis*, *Shewanella baltica*, *Shewanella pealeana*, and *Photobacterium profundum*, but the list is not limited to these species as long as they possess the EPA metabolic pathway.

[0092] Microorganisms that do not possess a PUFA metabolic pathway refer to microorganisms that do not naturally possess the ability to produce PUFAs. Examples of microorganisms that do not possess a PUFA metabolic pathway include bacteria, microalgae, fungi, protozoa, and protozoa.

[0093] As bacteria, examples include microorganisms belonging to genera selected from the group consisting of Escherichia, Serratia, Bacillus, Brevibacterium, Corynebacterium, Microbacterium, Pseudomonas, and Aureispira. Among these, the preferred selections are: *Escherichia coli* XL1-Blue, *Escherichia coli* XL2-Blue, *Escherichia coli* DH1, *Escherichia coli* MC1000, *Escherichia coli* KY3276, *Escherichia coli* W1485, *Escherichia coli* JM109, *Escherichia coli* HB101, *Escherichia coli* No.49, *Escherichia coli* W3110, *Escherichia coli* NY49, *Escherichia coli* BL21 codon plus (manufactured by Stratagenes), *Serratia ficaria*, *Serratia fonticola*, *Serratia liquefaciens*, *Serratia marcescens*, *Bacillus subtilis*, *Bacillus amyloliquefaciens*, and *Brevibacterium*. The group consists of microorganisms including *Immariophilum* ATCC14068, *Brevibacterium saccharolyticum* ATCC14066, *Corynebacterium ammoniagenes*, *Corynebacterium glutamicum* ATCC13032, *Corynebacterium glutamicum* ATCC14067, *Corynebacterium glutamicum* ATCC13869, *Corynebacterium acetoacidophilum* ATCC13870, *Microbacterium ammoniaphilum* ATCC15354, *Pseudomonas sp.* D-0110, and *Aureispira marina* JCM23201.

[0094] Examples of microalgae include: Euglenophyceae (e.g., the genera *Euglena* and *Peranema*), Chrysophyceae (e.g., the genus *Ochromonas*), Dinobryaceae (e.g., the genera *Dinobryon*, *Platychrysis*, and *Chrysochromulina*), and Dinophyceae (e.g., the genus *Crypthecodinium*, *Euglena*, *Peranema ... The genera *Gymnodinium*, *Peridinium*, *Ceratium*, *Gyrodinium*, and *Oxyrrhis* are included. Cryptophyceae (e.g., *Cryptomonas* and *Rhodomonas*) and Xanthophyceae (e.g., *Olisthodiscus*) are also included. This includes rhizochloridaceae and *Aphanochaete*. [Species of amoeboid algae such as pascheri, Bumilleriastigeoclonium and Vaucheria geminata in their spores / gametes], Eustigmatophyceae and Prymnesiopyceae [including, for example, the genera Prymnesium and Diacronema].

[0095] There are no particular restrictions on the preferred species in these genera, but examples include *Nannochloropsisoculata*, *Crypthecodinium cohnii*, and *Euglena gracilis*.

[0096] Examples of fungi include: yeasts of the genus *Saccharomyces* [such as *Saccharomyces cerevisiae* and *Saccharomyces carlsbergensis*], or other yeasts of the genus *Yarrowia*, *Candida*, *Pichia*, *Kluyveromyces*, etc.; or other fungi, such as fibrous fungi of the genus *Aspergillus*, *Neurospora*, *Penicillium*, etc.

[0097] As for the microorganism (2), it is preferred to be a microorganism that has introduced all the PUFA synthesis system genes of the microorganism (1) mentioned above, that is, a microorganism that has all the PUFA synthesis system genes of the microorganism (1) mentioned above.

[0098] In this invention, "activity toward 3-hydroxyhexanoyl ACP" refers to the activity that preferentially acts on 3-hydroxyhexanoyl ACP, and more specifically, to the reactivity (affinity) toward 3-hydroxyhexanoyl ACP. The activity toward 3-hydroxyhexanoyl ACP can be determined by evaluating the reverse reaction (hydrogenation reaction) of the dehydratase.

[0099] As an example of the above method, under the conditions of preparing crotonyl ACP or 2-trans-hexenoyl ACP as substrates, a protein containing a FabA-DH domain or a PS-DH domain is added, and the resulting product is analyzed by HPLC. The amount of product is compared by comparing the peak heights (the product with crotonyl ACP as substrate: 3-hydroxybutyryl ACP; the product with 2-trans-hexenoyl ACP as substrate: 3-hydroxyhexanoyl ACP). Furthermore, if the amount of product with crotonyl ACP as substrate is less than the amount of product with 2-trans-hexenoyl ACP as substrate, it is determined that the activity of the PS-DH domain for 3-hydroxyhexanoyl ACP is higher than that of the FabA-DH domain.

[0100] In this invention, the term "PS-DH domain exhibits higher activity toward 3-hydroxyhexanoyl ACP than the FabA-DH domain" specifically refers to, for example, the height of the HPLC peak obtained under the following reaction conditions, preferably 1.5 times or more, more preferably 2 times or more, and even more preferably 5 times or more, of the height of the HPLC peak of the product with 2-trans-hexenoyl ACP as the substrate.

[0101] (Reaction conditions)

[0102] A mixture of 80 mM Tris-HCl, 80 mM NaCl, 25 mM MgCl2, 100 μM ACP (as substrate), 20 μM Sfp, and 300 μM acyl-CoA was prepared and reacted at 20 °C for 10 minutes. Then, 1 μM or 5 μM of a protein containing both PS-DH and FabA-DH domains was added to the resulting system, and the reaction was continued at 20 °C. Samples were recovered at 1, 5, 10, 30, and 60 minutes after the start of the reaction, and analyzed by LC / MS to determine the peak height. The Sfp mentioned above refers to 4'-phosphopantoylthioethylamine transferase derived from Bacillus subtilis.

[0103] Specifically, for example, in the case of the microorganism (1) mentioned above, the activity of the endogenous PS-DH domain in microorganisms with the PUFA metabolic pathway for 3-hydroxyhexanoyl ACP is at or below the level of the endogenous FabA-DH domain. However, by introducing an exogenous gene encoding the PS-DH domain, which has a higher activity than the endogenous FabA-DH domain, into the microorganism, it becomes a microorganism in which the PS-DH domain has a relatively higher reactivity to 3-hydroxyhexanoyl ACP compared to the FabA-DH domain.

[0104] In addition, for example, in the case of the microorganism (2) mentioned above, by introducing a gene into a microorganism that does not have a PUFA metabolic pathway and expressing it, the microorganism with PUFA-PKS activity is made such that the PS-DH domain has a higher activity for 3-hydroxyhexanoyl ACP than the FabA-DH domain. This results in a microorganism in which the PS-DH domain has a relatively higher reactivity to 3-hydroxyhexanoyl ACP compared to the FabA-DH domain.

[0105] By making the PS-DH domain in the microorganism relatively more reactive to 3-hydroxyhexanoyl ACP than the FabA-DH domain, PUFA is produced through the biosynthetic pathway of PUFA via the PS-DH domain in the microbial PUFA metabolic pathway, where the PS-DH domain preferentially reacts with 3-hydroxyhexanoyl ACP.

[0106] As examples of PUFA biosynthetic pathways that function through the FabA-DH domain and those that function through the PS-DH domain, we can list the biosynthetic pathways of ω3PUFA (functioning through the FabA-DH domain) and ω6PUFA (functioning through the PS-DH domain).

[0107] When the position of the double bond counting from the terminal carbon atom in the PUFA biosynthetic pathway that functions through the FabA-DH domain is set as the ω(α) position (e.g., ω3 position), the position of the double bond counting from the terminal carbon atom in the PUFA biosynthetic pathway that functions through the PS-DH domain is the ω(α+3) position (e.g., ω6 position).

[0108] Therefore, for example, by introducing a gene encoding an exogenous PS-DH domain with higher activity for 3-hydroxyhexanoyl ACP than the PS-DH domain into a microorganism with an ω3PUFA metabolic pathway, the PS-DH domain in this microorganism exhibits relatively higher reactivity for 3-hydroxyhexanoyl ACP compared to the FabA-DH domain. As a result, the PS-DH domain preferentially acts on 3-hydroxyhexanoyl ACP over the FabA-DH domain, creating a microorganism capable of producing ω6PUFA as a final product.

[0109] In this invention, examples of PS-DH domains include those derived from the AraB domain of *Aureispira marina* (proteins having the amino acid sequence represented by SEQ ID NO: 2, encoded by the base sequence represented by SEQ ID NO: 136) or the PS-DH domain derived from the pfaB domain of *Psychroflexus torquis* (proteins having the amino acid sequence represented by SEQ ID NO: 137, encoded by the base sequence represented by SEQ ID NO: 139), with a preference for the PS-DH domain derived from the araB domain of *Aureispira marina*. These sequences are well-known and can be used appropriately. Furthermore, using known sequences, genes encoding PS-DH domains with higher activity against 3-hydroxyhexanoyl ACP than the endogenous FabA-DH domain can be obtained.

[0110] More specifically, the following proteins are preferably examples of the PS-DH domain used in this invention.

[0111] [1] Proteins having the amino acid sequence represented by sequence number 2 or sequence number 137

[0112] [2] A mutant protein consisting of an amino acid sequence obtained by deleting, substituting, or adding 1 to 20, preferably 1 to 10, and most preferably 1 to 5 amino acids in the amino acid sequence represented by sequence number 2 or sequence number 137, and having activity against 3-hydroxyhexanoyl ACP.

[0113] [3] Homologous proteins that have at least 95%, preferably 97%, more preferably 98%, and most preferably 99% similarity to the amino acid sequence represented by sequence number 2 or sequence number 137, and have activity against 3-hydroxyhexanoyl ACP.

[0114] Genes encoding the PS-DH domain can be introduced into microorganisms by introducing genes encoding proteins with the PS-DH domain. Examples of proteins with the PS-DH domain include AraB from *Helicobacter aureus* (a protein with the amino acid sequence represented by SEQ ID NO: 58, encoded by the base sequence represented by SEQ ID NO: 57) and PfaB from *Cyclophorus tympani* (a protein with the amino acid sequence represented by SEQ ID NO: 138, encoded by the base sequence represented by SEQ ID NO: 140).

[0115] More specifically, the following proteins are preferably listed as proteins having PS-DH domains used in this invention.

[0116] [4] Proteins having the amino acid sequence represented by sequence number 58 or sequence number 138

[0117] [5] A mutant protein consisting of an amino acid sequence obtained by deleting, substituting, or adding 1 to 20, preferably 1 to 10, and most preferably 1 to 5 amino acids in the amino acid sequence represented by sequence number 58 or sequence number 138, and having activity against 3-hydroxyhexanoyl ACP.

[0118] [6] Homologous proteins having at least 95%, preferably 97%, more preferably 98%, and most preferably 99% similarity to the amino acid sequence represented by sequence number 58 or 138, and having activity against 3-hydroxyhexanoyl ACP.

[0119] The protein with the amino acid sequence represented by sequence number 58 is a protein composed of 801 amino acid residues, and has a PS-DH domain at residues 531 to 790 from the N-terminus.

[0120] Mutant proteins are proteins obtained by artificially deleting, substituting, or adding amino acid residues to the original protein. In the aforementioned mutant proteins, the deletion, substitution, insertion, or addition of amino acids can occur at any position within the same sequence, and the number of amino acids involved can range from 1 to 20, preferably 1 to 10, and most preferably 1 to 5.

[0121] The amino acids that are missing, substituted, or added can be either natural or non-natural. Examples of natural amino acids include L-alanine, L-asparagine, L-aspartic acid, L-glutamine, L-glutamic acid, glycine, L-histidine, L-isoleucine, L-leucine, L-lysine, L-arginine, L-methionine, L-phenylalanine, L-proline, L-serine, L-threonine, L-tryptophan, L-tyrosine, L-valine, and L-cysteine.

[0122] The following shows examples of amino acids that can be substituted for each other. Amino acids contained in the same group can be substituted for each other.

[0123] Group A: Leucine, Isoleucine, Norleucine, Valine, Norvaline, Alanine, 2-Aminobutyric Acid, Methionine, O-methylserine, Tert-butylglycine, Tert-butylalanine, Cyclohexylalanine

[0124] Group B: Aspartic acid, glutamic acid, isoaspartic acid, isoglutamic acid, 2-aminohexanoic acid, 2-aminooctanoic acid

[0125] Group C: Asparagine, glutamine

[0126] Group D: Lysine, arginine, ornithine, 2,4-diaminobutyric acid, 2,3-diaminopropionic acid

[0127] Group E: Proline, 3-hydroxyproline, 4-hydroxyproline

[0128] Group F: Serine, Threonine, Homoserine

[0129] Group G: Phenylalanine, Tyrosine

[0130] Homologous proteins are proteins found in organisms in nature that have similar structures and functions to the original proteins. Therefore, it is believed that the genes encoding these proteins have the same evolutionary origin as the genes encoding the original proteins.

[0131] The identity of amino acid or base sequences can be determined using the BLAST algorithm by Karlin and Altschul [Pro. NAT domain l. Acad. Sci. USA, 90, 5873 (1993)] and FASTA [Methods Enzymol., 183, 63 (1990)]. Based on this BLAST algorithm, programs called BLASTN or BLASTX were developed [J. Mol. Biol., 215, 403 (1990)]. When resolving base sequences using BLASTN based on BLAST, the parameters are set, for example, with a score of 100 and a word length of 12. Conversely, when resolving amino acid sequences using BLASTX based on BLAST, the parameters are set, for example, with a score of 50 and a word length of 3. When using the BLAST and Gapped BLAST programs, the default parameters for each program are used. The specific methods of these resolution methods are well known.

[0132] The gene encoding the PS-DH domain used in this invention is not limited as long as it encodes a protein with activity against 3-hydroxyhexanoyl ACP, but genes having any of the following DNA types are preferred.

[0133] [7] DNA encoding any of the proteins mentioned in [1] to [3] above

[0134] [8] DNA containing the base sequence represented by sequence number 136 or 139

[0135] [9] Hybridized under stringent conditions with DNA consisting of complementary base sequences of the DNA described in [7] or [8] above, and DNA encoding a homologous protein having activity against 3-hydroxyhexanoyl ACP.

[0136]

[10] DNA having at least 95%, preferably 97%, more preferably 98%, and most preferably 99% or more identical in base sequence to the DNA described in [7] or [8] above, and encoding a homologous protein having activity against 3-hydroxyhexanoyl ACP.

[0137] In addition, genes encoding proteins having PS-DH domains are preferably listed as having any of the following DNA types.

[0138]

[11] DNA encoding any of the proteins mentioned in [4] to [6] above

[0139]

[12] DNA containing the base sequence represented by sequence number 57 or sequence number 140

[0140]

[13] Hybridized under stringent conditions with DNA consisting of a complementary base sequence of the DNA described in

[11] or

[12] above, and DNA encoding a homologous protein having activity against 3-hydroxyhexanoyl ACP.

[0141]

[14] DNA whose base sequence has at least 95%, preferably 97%, more preferably 98%, and most preferably 99% similarity to the DNA described in

[11] or

[12] above, and which encodes a homologous protein having activity against 3-hydroxyhexanoyl ACP.

[0142] Hybridization refers to the complementary formation of a complex between DNA with a specific base sequence or a portion thereof and another DNA. Therefore, the DNA with the specific base sequence or a portion thereof may be a DNA of a length useful as a probe for Northern or Southern blotting analysis or as an oligonucleotide primer for PCR analysis. Examples of DNA used as probes include DNA with at least 100 bases, preferably 200 bases or more, and more preferably 500 bases or more; examples of DNA used as primers include DNA with at least 10 bases, preferably 15 bases or more.

[0143] The methods for DNA hybridization experiments are well known. In addition to those described in Molecular Cloning, 2nd and 3rd editions (2001), Methods for Genome and Molecular Bacteriology, ASM Press (1994), and Immunology Methods Manual, Academic Press (Molecular), the conditions for hybridization can be determined according to many other standard textbooks.

[0144] Alternatively, DNA that has been hybridized under stringent conditions can be obtained by following the instructions accompanying commercially available hybridization kits. Examples of commercially available hybridization kits include, for instance, random primer DNA labeling kits (manufactured by Roche Diagnostics) that use random primers to prepare probes and perform hybridization under stringent conditions.

[0145] Strict conditions can be listed as follows: After incubating the filter and probe DNA with DNA immobilized in a solution containing 50% formamide, 5×SSC (750mM sodium chloride, 75mM sodium citrate), 50mM sodium phosphate (pH 7.6), 5×Denhardt's solution, 10% dextran sulfate and 20 μg / L denatured salmon sperm DNA at 42°C overnight, the filter is washed in a 0.2×SSC solution at approximately 65°C.

[0146] The above conditions can also be set by adding or changing the blocking reagent used to suppress the background of the hybridization experiment. To optimize the conditions, the addition of the blocking reagent can be accompanied by changes in the hybridization conditions.

[0147] As DNA capable of hybridization under the aforementioned stringent conditions, examples include DNA consisting of a base sequence that, when calculated using programs such as BLAST and FASTA based on the aforementioned parameters, has at least 95%, preferably 97%, more preferably 98%, and most preferably 99% or more identical to the base sequence of the target DNA.

[0148] The domains that can be introduced into microorganisms (2) to have PUFA-PKS activity include the KS domain, MAT domain, ACP domain, KR domain, CLF domain, AT domain, FabA-DH domain (as a DH domain), ER domain, and PPT domain. There are no restrictions on which domains are involved in the PUFA production process as long as they work synergistically with acetyl-CoA as the starting substrate; for example, the domains possessed by known PUFA-PKS can be listed.

[0149] The synergistic effect of the various domains with PUFA-PKS activity introduced into the microorganism (2) can be confirmed as follows: a microorganism transformed with genes encoding the various domains of PUFA-PKS was prepared, and the microorganism was cultured in a culture medium to generate and accumulate PUFA in the culture. The amount of PUFA accumulated in the culture was determined by gas chromatography.

[0150] In this specification, the "known PUFA-PKS" preferably include those belonging to the genera *Shewanella*, *Colwellia*, *Desulfatibacillum*, *Psychroflexus*, *Schizochytrium*, *Nostoc*, *Microcystis*, *Saccharopolyspora*, *Geobacter*, *Planctomyces*, *Desulfococcus*, *Sorangium*, and *Renibacterium*. The PUFA-PKS originally possessed by microorganisms in the group consisting of genera including *Chitinophaga*, *Gloeobacter*, *Azotobacter*, *Rhodococcus*, *Solibacter*, *Desulfobacterium*, *Clostridium*, *Thraustochytrium*, *Ulkenia*, *Japonochytrium*, *Aurantiochytrium*, and *Moritella*, more preferably, is selected from *Shewanella*. Pealeana (ATCC 700345), Shewanella oneidensis MR-1, Colwellia psychrerythraea 34H, Desulfatibacillum alkenivorans AK-01, Psychroflexus torquis (ATCC 700755), Schizochytrium sp.ATCC 20888, *Nostocpunctiforme* PCC 73102, *Microcystis aeruginosa* NIES-843, *Saccharopolyspora erythraea* NRRL 2338, *Geobacter bemidjiensis* Bem, *Planctomyces limnophilus* DSM3776, *Desulfococcus oleovorans* Hxd3, *Sorangium cellulosum* 'Soce 56', *Renibacterium salmoninarum* ATCC33209, *Chitinophaga pinensis* DSM 2588, *Gloeobacter violaceus* PCC 7421, *Azotobacter* vinelandii)DJ, Rhodococcus erythropolis PR4, Candidatus Solibacter usitatus Ellin6076, Desulfobacterium autotrophicum HRM2, Clostridium thermocellum ATCC 27405, Schizochytrium minutum, Schizochytrium sp. S31 ATCC 20888, Schizochytrium sp. S8 ATCC 20889, Schizochytrium sp. LC-RM ATCC 18915, Schizochytrium sp. SR21, Schizochytrium aggregatum ATCC 28209, Schizochytrium limacinum IFO 32693, Thraustochytrium sp.The most preferred examples of the PUFA-PKS originally possessed by microorganisms in the group consisting of 23B ATCC 20891, Thraustochytrium striatum ATCC 24473, Thraustochytrium aureum ATCC 34304, Thraustochytrium roseum ATCC 28210, Ulkenia sp. BP-5601, and Japonochytrium sp. L1 ATCC 28207 are Shewanella pealeana ATCC 700345, Shewanella oneidensis MR-1, Colwellia psychrerythraea 34H, Moritella marina MP-1, and Schizochytrium sp. ATCC 23B. The microorganisms in the group consisting of 20888 originally possessed PUFA-PKS [FEMS Microbiol. Lett. (2009), Vol. 295, p170-176; PLoS ONE (2011), Vol. 6(5), art. no. e20146].

[0151] Table 1 shows examples of the amino acid sequences of each domain of the protein constituting the PUFA-PKS used in the examples described below, and examples of the amino acid sequences of each domain of the protein constituting a known PUFA-PKS.

[0152] [Table 1]

[0153]

[0154] Regarding protein complexes with PUFA-PKS activity and the proteins constituting such protein complexes, as long as the protein complexes have PUFA-PKS activity, they can physically bind to each other or be separated.

[0155] As a protein that constitutes a protein complex with PUFA-PKS activity, any protein that has PUFA-PKS activity by working synergistically with other proteins can be any one of wild-type protein, homologous protein, or mutant protein.

[0156] Figure 1Table 1 shows the protein and domain structures that constitute PUFA-PKS from various microorganisms. Additionally, Table 2 shows examples of the amino acid and base sequences of the proteins that constitute PUFA-PKS in various microorganisms.

[0157] [Table 2]

[0158]

[0159] The base sequence of a protein encoding a protein complex having PUFA-PKS activity is not particularly limited as long as it encodes a protein that has PUFA-PKS activity through synergistic interaction with other proteins. Examples include the base sequences shown in Table 2; and base sequences that have at least 95%, preferably 97%, more preferably 98%, and most preferably 99% similarity to the base sequence and encode a protein that has PUFA-PKS activity through synergistic interaction with other proteins.

[0160] As a combination of proteins constituting a synergistic protein complex with PUFA-PKS activity, there are no particular limitations as long as the protein complex has PUFA-PKS activity and the PS-DH domain shows higher activity toward 3-hydroxyhexanoyl ACP than the FabA-DH domain. Examples of such combinations are as follows. The amino acid sequences of the proteins in (i) to (iv) below are shown in Table 2.

[0161] (i)PhoA, PhoB, PhoC, PhoD, EpaE, AraB

[0162] (ii)EpaA, PhoB, PhoC, PhoD, EpaE, AraB

[0163] (iii)EpaA, AraB, AraC, AraD, EpaE

[0164] (iv)PhoA, AraB, AraC, AraD, EpaE

[0165] [Methods for preparing microorganisms]

[0166] Microorganisms (1) are obtained by introducing a gene encoding an exogenous PS-DH domain that has higher activity against 3-hydroxyhexanoyl ACP than the endogenous FabA-DH domain, or a gene encoding a protein with the PS-DH domain, into a microorganism with a PUFA metabolic pathway as a host organism and then transforming it.

[0167] Microorganism (2) is obtained by the following method: using a microorganism without the PUFA metabolic pathway as the host organism, introducing genes encoding each domain with PUFA-PKS activity or genes encoding proteins constituting PUFA-PKS, and making the PS-DH domain exhibit higher activity for 3-hydroxyhexanoyl ACP than the FabA-DH domain among the domains with PUFA-PKS activity expressed in the host organism through the introduction of the gene.

[0168] The introduction of genes encoding the PS-DH domain includes: cases where the gene exists in the host cell as a plasmid capable of autonomous replication; cases where the gene for which substitution is to be performed is replaced in the host cell with a corresponding exogenous gene; and cases where the gene encoding the exogenous PS-DH domain is integrated into a region of the chromosomal DNA of the host cell that is different from the region encoding the PUFA-PKS gene. In this invention, when introducing the gene, sequence optimization is preferably performed with reference to the codon usage frequency of the host microorganism.

[0169] In addition, genes encoding the domains that constitute PUFA-PKS, or genes encoding the proteins that constitute PUFA-PKS, can be introduced individually or in combination, as long as a microorganism expressing a protein complex with PUFA-PKS activity and having a PS-DH domain exhibiting higher activity for 3-hydroxyhexanoyl ACP than the FabA-DH domain can be obtained.

[0170] In this specification, "gene" refers to DNA that, in addition to the protein coding region, may also contain transcriptional regulatory regions, promoter regions, and terminator regions. When using prokaryotes such as bacteria as the host organism as the parent strain, it is preferable to use a plasmid that adjusts the distance between the Shine-Dalgarno sequence (which serves as the ribosome binding region) and the start codon to an appropriate level (e.g., 6–18 bases). In this DNA, a transcription termination factor is not essential for expression, but it is preferable to place the transcription termination sequence immediately downstream of the structural gene.

[0171] Genes introduced into a host organism can be introduced into host cells, for example, by creating recombinant genes inserted downstream of the promoter of a suitable expression vector. The expression vector may also contain a promoter, a transcription termination signal, selection marker genes for selecting transformants (e.g., drug resistance genes such as kanamycin resistance, streptomycin resistance, oxytetracycline resistance, bleomycin resistance, and hygromycin resistance genes; genes complementary to amino acid defect mutations such as leucine, histidine, methionine, arginine, tryptophan, and lysine; and genes complementary to nucleic acid base defect mutations such as uracil and adenine). In the case of uracil-deficient strains, marker genes such as orotate nucleoside-5'-phosphate decarboxylase (ura3 gene) or orotate pyrophosphorylase (ura5 gene) can be used.

[0172] As promoters, whether structural or regulatory, they are defined as the DNA base sequence that initiates RNA synthesis by binding to DNA via RNA polymerase. Strong promoters are those that initiate mRNA synthesis at a high frequency and are preferred. Depending on the host cell characteristics, promoters such as the lac system, trp system, TAC or TRC system, the major operon and promoter regions of λ phage, the regulatory regions of fd-coated proteins, and promoters targeting glycolytic enzymes (e.g., 3-phosphoglycerate kinase, glyceraldehyde-3-phosphate dehydrogenase), glutamate decarboxylase A, and serine hydroxymethyltransferase can be used.

[0173] Besides promoter and terminator sequences, other regulatory elements include, for example, selection markers, amplification signals, and origins of replication. Preferred regulatory sequences include those described in "Gene Expression Technology: Methods in Enzymology 185" and Academic Press (1990).

[0174] As a vector, there are no particular limitations as long as it enables the expression of the target gene. There are also no particular limitations on the types of reagents used to construct the vector, such as restriction enzymes or ligases; commercially available products can be used appropriately.

[0175] As a promoter used when reticulomycetes are the host organism, there are no particular limitations as long as the promoter functions in the cells of reticulomycetes. Examples include actin promoter, tubulin promoter, elongation factor Tu promoter, and expression promoters of glycolysis system genes.

[0176] When the parent strain uses microorganisms belonging to the genus *Escherichia*, examples of expression vectors that can be used include pColdI (manufactured by Takara Bio), pET21a, pCOLADuet-1, pACYCDuet-1, pCDF-1b, pRSF-1b (all manufactured by Novagen), pMAL-c2x (manufactured by New England Biolabs), pGEX-4T-1 (manufactured by GE Healthcare Biosciences), pTrcHis (manufactured by Invitrogen), pSE280 (manufactured by Invitrogen), pGEMEX-1 (manufactured by Promega), pQE-30 (manufactured by Qiagen), pET-3 (manufactured by Novagen), and pTrc99A (manufactured by GE Healthcare). pKYP10 (Japanese Patent Application Publication No. 58-110600), pKYP200 [Agric. Biool. Chem., 48, 669 (1984)], pLSA1 [Agric. Biool. Chem., 53, 277 (1989)], pGEL1 [Proc. Natl. Acad. Sci., USA, 82, 4306 (1985)], pBluescriptII SK(+), pBluescriptII KS(-) (manufactured by Stratagene), pTrS30 [prepared from Escherichia coli JM109 / pTrS30 (FermBP-5407)], pTrS32 [prepared from Escherichia coli JM109 / pTrS32 (FermBP-5408)], pTK31 [APPLIED AND ENVIRONMENTAL] [MICROBIOLOGY, 2007, Vol.73, No.20, pp.6378-6385], pPAC31 (International Publication No. 98 / 12343), pUC19 [Gene, 33, 103 (1985)], pSTV28 (manufactured by Takara Bio Inc.), pUC118 (manufactured by Takara Bio Inc.), pPA1 (Japanese Patent Application Publication No. 63-233798), pHSG298 (manufactured by Takara Bio Inc.), pUC18 (manufactured by Takara Bio Inc.).

[0177] As for the promoters used when using the above-mentioned expression vectors, there are no particular limitations as long as the promoter functions in the cells of microorganisms belonging to the genus *Escherichia*. Promoters derived from *Escherichia coli* or bacteriophages, such as the trp promoter (Ptrp), lac promoter (Plac), PL promoter, PR promoter, PSE promoter, and T7 promoter, can be used. Alternatively, artificially designed and modified promoters, such as promoters consisting of two Ptrp units tandemly, tac promoters, trc promoters, lacT7 promoters, and letI promoters, can also be used.

[0178] When using rod-shaped bacteria as parental strains, examples of expression vectors include pCG1 (Japanese Patent Application Publication No. 57-134500), pCG2 (Japanese Patent Application Publication No. 58-35197), pCG4 (Japanese Patent Application Publication No. 57-183799), pCG11 (Japanese Patent Application Publication No. 57-134500), pCG116, pCE54, pCB101 (all Japanese Patent Application Publication No. 58-105999), pCE51, pCE52, and pCE53 [all Molecular and General Genetics, 196, 175 (1984)].

[0179] As for the promoter used in the above expression vector, there are no particular limitations as long as it is a promoter that functions in the cells of rod-shaped bacteria, and the P54-6 promoter can be used for example [Appl. Microbiol. Biotechnol., 53, 674-679 (2000)].

[0180] When using yeast strains as parental lines, examples of expression vectors include YEp13 (ATCC37115), YEp24 (ATCC37051), YCp51 (ATCC37419), pHS19, and pHS15.

[0181] As for the promoters used in the above expression vectors, there are no particular limitations as long as they function in the cells of yeast strains. Examples include the PH05 promoter, PGK promoter, GAP promoter, ADH promoter, gal1 promoter, gal10 promoter, heat shock peptide promoter, MFα1 promoter, CUP1 promoter, and so on.

[0182] Homologous recombination can be used as a method for integrating a gene to be introduced into the chromosome of a host organism. Examples of homologous recombination methods include introducing a recombinant gene using a homologous recombination system, which can be created by ligating a plasmid DNA containing a drug resistance gene that cannot replicate autonomously in the parent strain to which the gene is to be introduced. As a method utilizing homologous recombination, which is frequently used in *Escherichia coli*, the method of introducing a recombinant gene using the homologous recombination system of λ phage can be cited [Proc. Natl. Acad. Sci. USA, 97, 6641-6645 (2000)].

[0183] In addition, selection methods that utilize the fact that *E. coli* becomes sucrose-sensitive by integrating *Bacillus subtilis* fructanase into the chromosome along with the gene to be introduced, and selection methods that utilize the fact that *E. coli* becomes streptomycin-sensitive by integrating the wild-type *rpsL* gene into *E. coli* with a streptomycin-resistant mutant *rpsL* gene [Mol. Microbiol., 55, 137 (2005), Biosci. Biotechnol. Biochem., 71, 2905 (2007)] can be used to obtain microorganisms in which the target region on the chromosomal DNA of the parent strain is replaced with recombinant DNA.

[0184] In addition, examples of homologous recombination methods include the ATMT method using Agrobacterium [Appl. Environ. Microbiol., (2009), vol. 75, p. 5529-5535]. Furthermore, any method that can stably maintain the target trait may also be included, and is not limited to these, as long as a transformant can be obtained.

[0185] Methods for introducing genes into the host organism in the form of plasmids that can replicate autonomously in the host organism include, for example, the calcium ion method [Proc.Natl.Acad.Sci.,USA,69,2110(1972)], the protoplast method (Japanese Patent Application Publication No. 63-248394), and the electroporation method [Nucleic Acids Res.,16,6127(1988)].

[0186] The fact that the microorganism obtained by the above method is the target microorganism can be confirmed by culturing the microorganism, detecting the PUFA accumulated in its culture using gas chromatography, and evaluating whether the above method makes the PS-DH domain show higher activity for 3-hydroxyhexanoyl ACP than the FabA-DH domain.

[0187] [Method for manufacturing PUFA or a composition containing PUFA]

[0188] The present invention includes a method for manufacturing PUFA or a composition containing PUFA, characterized in that the microorganisms prepared above are cultured in a culture medium to generate and accumulate PUFA or a composition containing PUFA in the culture, and PUFA or a composition containing PUFA is collected from the culture.

[0189] The PUFA contained in the PUFA or the PUFA-containing composition is preferably ω6PUFA, such as DPA or ARA. Examples of PUFA-containing compositions include, for example, PUFA-containing oils or PUFA-containing phospholipids, with PUFA-containing oils being preferred. The culture of this microorganism can be obtained by inoculating the microorganism into a suitable culture medium and culturing it according to conventional methods.

[0190] As a culture medium, any known culture medium containing a carbon source, nitrogen source, and inorganic salts can be used. For example, as a carbon source, in addition to carbohydrates such as glucose, fructose, and galactose, examples include oils such as oleic acid and soybean oil, glycerol, and sodium acetate. These carbon sources can be used, for example, at a concentration of 20 to 300 g per liter of culture medium. According to a particularly preferred method, culture can continue by supplying a carbon source after the initial carbon source has been consumed. By culturing under such conditions, the amount of carbon source consumed can be increased, thereby increasing the production yield of compositions containing PUFAs.

[0191] In addition, examples of nitrogen sources include organic nitrogen such as yeast extract, corn steep liquor, polypeptone, monosodium glutamate, and urea, and inorganic nitrogen such as ammonium acetate, ammonium sulfate, ammonium chloride, sodium nitrate, ammonium nitrate, and ammonia. Potassium phosphate can be used in appropriate combinations as inorganic salts.

[0192] The culture medium containing the above-mentioned components is preferably sterilized in an autoclave after the pH is adjusted to the range of 4.0 to 9.5 by adding appropriate acid or alkali. The culture temperature is typically 10–45°C, preferably 20–37°C. The culture temperature is preferably controlled to a level suitable for producing compositions containing PUFAs. The pH during culture is typically 3.5–9.5, preferably 4.5–9.5. Particularly preferred pH values ​​vary depending on the purpose; for large-scale oil production, a pH of 5.0–8.0 is preferred.

[0193] The culture time can be set to, for example, 2 to 7 days, and can be carried out by aeration and stirring. The method for separating the culture medium and microorganisms from the culture can be performed using conventional methods known to those skilled in the art, such as centrifugation or filtration. The microorganisms isolated from the culture are then disrupted using, for example, ultrasound or a dinomill, and extracted with solvents such as chloroform, hexane, or butanol to obtain a composition containing PUFA.

[0194] The PUFA-containing composition manufactured by the above manufacturing method can be concentrated by methods such as low-temperature solvent extraction [Takahashi Kotaro, Oil Chemicals, 40:931-941 (1991)] or by using hydrolytic enzymes such as lipases to remove short-chain fatty acids [Takahashi Kotaro, Oil Chemicals, 40:931-941 (1991)] to obtain a PUFA-containing composition with high PUFA content.

[0195] PUFA can be manufactured by separating and collecting PUFA from a composition containing PUFA. For example, a mixed fatty acid containing PUFA can be prepared from a composition containing PUFA by hydrolysis, and then the PUFA can be separated and collected by, for example, urea addition, cooling separation, high performance liquid chromatography, or supercritical chromatography.

[0196] Alternatively, PUFA alkyl esters can be manufactured by separating and collecting PUFA alkyl esters from compositions containing PUFA. There are no particular limitations on the type of PUFA alkyl ester, but PUFA ethyl ester is a preferred example.

[0197] To separate and collect PUFA alkyl esters from a PUFA-containing composition, for example, a mixed fatty acid alkyl ester containing PUFA alkyl esters can be prepared from the PUFA-containing composition by alcoholysis, and then the PUFA alkyl esters can be separated and collected by, for example, urea addition, cooling separation, high performance liquid chromatography, or supercritical chromatography.

[0198] Example

[0199] The following are examples, but the present invention is not limited to the following examples.

[0200] [Example 1]

[0201] ARA Manufacturing Method - 1

[0202] 1. Preparation of each expression plasmid

[0203] [The creation of pET-phoA]

[0204] Using the genomic DNA of Photobacterium profundum SS99 (ATCCBAA-1252) strain extracted using conventional methods as a template, PCR was performed using primers indicated by sequence numbers 107 and 108 to amplify the 3' end region (from the 633rd base to the stop codon) of the DNA encoding the PhoA protein (DNA composed of the base sequence indicated by sequence number 65).

[0205] The obtained DNA fragment was treated with restriction enzymes BamHI and EagI and ligated to the E. coli vector pBluescript II SK(+) (manufactured by Agilent Technologies) that had been treated with the same restriction enzymes, thus obtaining pBlue-PhoA-C-terminal.

[0206] Next, using the genomic DNA of Photobacterium profundum SS99 strain extracted using conventional methods as a template, PCR was performed using primers indicated by sequence numbers 109 and 110 to amplify the 5' end region of the DNA encoding the PhoA protein (from the start codon to the 633rd base).

[0207] The obtained DNA fragment and the E. coli vector pET21a (manufactured by Merck Millipore) were treated with restriction enzymes NdeI and EagI, respectively. The restriction enzyme-treated fragments were then ligated to obtain pET-phoA-N-terminal.

[0208] Next, pBlue-PhoA-C-terminal and pET-phoA-N-terminal were treated with restriction enzymes EagI and XhoI, respectively, and the resulting restriction enzyme-treated fragments were ligated to obtain pET-phoA.

[0209] [The creation of pACYC-SopfaE]

[0210] Using the same method as Lin et al. (Sci.Rep.,2016,6,35441), we obtained the expression plasmid pACYC-SopfaE, which contains DNA (the DNA consisting of the base sequence represented by sequence number 81) encoding the EpaE protein derived from the Shewanella oneidensis MR-1 (ATCC BAA-1096) strain.

[0211] [The creation of pCOLA-phoD-phoB]

[0212] Using the genomic DNA of Photobacterium profundum SS99 strain extracted using conventional methods as a template, PCR was performed using primers indicated by sequence numbers 111 and 112 to amplify a DNA fragment encoding the PhoD protein (DNA composed of the base sequence indicated by sequence number 71).

[0213] The obtained DNA fragment was treated with restriction enzymes NdeI and BamHI and ligated with the E. coli vector pCOLADuet-1 (manufactured by Merck Millipore) which was treated with restriction enzymes NdeI and BglII, thus obtaining pCOLA-phoD.

[0214] Using the genomic DNA of Photobacterium profundum SS99 strain extracted using conventional methods as a template, PCR was performed using primers indicated by sequence numbers 113 and 114 to amplify a DNA fragment encoding the PhoB protein (DNA composed of the base sequence indicated by sequence number 67).

[0215] The obtained DNA fragment was treated with restriction enzymes NdeI and BamHI, and then ligated with pACYC-SopfaE, which had been treated with restriction enzymes NdeI and BglII, to obtain pACYC-epaE-phoB.

[0216] Using pACYC-epaE-phoB as a template, PCR was performed using primers indicated by sequence numbers 114 and 115 to obtain a DNA fragment encoding the PhoB protein. Additionally, using the E. coli vector pCOLADuet-1 (manufactured by Merck Millipore) as a template, PCR was performed using primers indicated by sequence numbers 116 and 117 to amplify a DNA fragment of the T7 promoter region.

[0217] The two DNA fragments were assembled using overlap extension PCR. The obtained DNA fragments and pCOLA-phoD were then treated with restriction enzymes ApaI and BamHI, respectively. The restriction enzyme-treated fragments were then ligated to obtain pCOLA-phoD-phoB.

[0218] [Creating pCDF-phoC]

[0219] Using the genomic DNA of Photobacterium profundum SS99 strain extracted using conventional methods as a template, PCR was performed using primers indicated by sequence numbers 118 and 119 to amplify the 5' end region (from the start codon to the 993rd base) of the DNA encoding the PhoC protein (DNA composed of the base sequence indicated by sequence number 69).

[0220] The obtained DNA fragment and the E. coli vector pUC18 (manufactured by Takara Bio Inc.) were treated with restriction enzymes NdeI and XbaI, respectively, and the resulting restriction enzyme-treated fragments were ligated. Next, the obtained plasmid and pCDF-orfB (Sci. Rep., 2016, 6, 35441) were treated with restriction enzymes NdeI and BamHI, and the resulting restriction enzyme-treated fragments were ligated, thus obtaining pCDF-phoC-N-terminal.

[0221] Next, using genomic DNA from Photobacterium profundum SS99 strain extracted using conventional methods as a template, PCR was performed using primers indicated by sequence numbers 120 and 121 to amplify the 3' end region (from base position 933 to the stop codon) of the DNA encoding the PhoC protein. The obtained DNA fragment and pCDF-phoC-N-terminal were treated with restriction enzymes NcoI and BamHI, and the resulting restriction enzyme-treated fragment was ligated to obtain pCDF-phoC.

[0222] [The creation of pET-epaA]

[0223] Using the genomic DNA of Shewanella oneidensis MR-1 (ATCCBAA-1096) strain extracted using conventional methods as a template, PCR was performed using primers indicated by sequence numbers 122 and 123 to amplify a DNA fragment encoding the EpaA protein (DNA composed of the base sequence indicated by sequence number 73).

[0224] The obtained DNA fragment and the E. coli vector pET21a (manufactured by Merck Millipore) were treated with restriction enzymes EcoRI and XhoI. The resulting restriction enzyme-treated fragments were then ligated to obtain pET-epaA'.

[0225] Next, using pET-epaA' as a template, overlapping extension PCR was performed using primers indicated by sequence numbers 124, 125, 126, and 127 to amplify the EpaA gene excluding the His tag gene at the 5' end.

[0226] The obtained DNA fragment and pET-epaA' were treated with restriction enzymes ApaI and SalI, and the resulting restriction enzyme-treated fragments were ligated to obtain pET-epaA.

[0227] [The creation of pET-araA]

[0228] Using pSTV29-Plac-pfaAB[FEBS Lett.,2014,588(21),4032-4036] as a template, PCR was performed using primers represented by sequence numbers 128 and 129 to amplify a DNA fragment encoding the AraA protein (DNA composed of the base sequence represented by sequence number 55).

[0229] The obtained DNA fragment and the E. coli vector pET21a (manufactured by Merck Millipore) were treated with restriction enzymes NdeI and BamHI. The restriction enzyme-treated fragments were then ligated to obtain pET-araA.

[0230] [The creation of pACYC-epaE-araB]

[0231] Using pSTV29-Plac-pfaAB (FEBS Lett., 2014, 588(21), 4032-4036) as a template, PCR was performed using primers represented by sequence numbers 130 and 131 to amplify a DNA fragment encoding the AraB protein (DNA composed of the base sequence represented by sequence number 57).

[0232] The obtained DNA fragment was treated with restriction enzymes NdeI and BamHI and then ligated with pACYC-SopfaE, which had been treated with NdeI and BglII, to obtain pACYC-epaE-araB.

[0233] [The creation of pCDF-araC]

[0234] Using pMW219-Plac-pfaCD[FEBS Lett.,2014,588(21),4032-4036] as a template, PCR was performed using primers represented by sequence numbers 132 and 133 to amplify a DNA fragment encoding the AraC protein (DNA composed of the base sequence represented by sequence number 59).

[0235] The obtained DNA fragment and pCDF-orfB (Sci.Rep.,2016,6,35441) were treated with restriction enzymes NdeI and BamHI, and the resulting restriction enzyme-treated fragments were ligated to obtain pCDF-araC.

[0236] [The creation of pCOLA-araD]

[0237] Using pMW219-Plac-pfaCD[FEBS Lett.,2014,588(21),4032-4036] as a template, PCR was performed using primers represented by sequence numbers 134 and 135 to amplify a DNA fragment encoding the AraD protein (DNA composed of the base sequence represented by sequence number 61).

[0238] The obtained DNA fragment was treated with restriction enzymes NdeI and BamHI and then ligated with the E. coli vector pCOLADuet-1 (manufactured by Merck Millipore) which was treated with restriction enzymes NdeI and BglII, thus obtaining pCOLA-araD.

[0239] 2. The Manufacturing of ARA - 1

[0240] Using the same method as Lin et al. (Sci.Rep., 2016, 6, 35441), an Escherichia coli BLR(DE3)ΔfadE strain with a deletion of the gene encoding acyl-CoA dehydrogenase FadE (a protein composed of the amino acid sequence represented by sequence number 106) was produced.

[0241] use <1> pET-phoA, pCDF-phoC, pCOLA-phoD-phoB, and pACYC-SopfaE, or <2> pET-phoA, pCDF-phoC, pCOLA-phoD-phoB, and pACYC-epaE-araB were used to transform Escherichia coli BLR(DE3)ΔfadE strain.

[0242] The obtained Escherichia coli was inoculated into 2 mL of Terrific Broth (manufactured by Becton, Dickinson and Company) containing 100 mg / L ampicillin, 20 mg / L kanamycin, 30 mg / L chloramphenicol and 20 mg / L streptomycin, and cultured at 30°C for 16 hours with shaking.

[0243] 1 mL of the obtained culture medium was inoculated into a 200 mL impeller flask containing 20 mL of freshly prepared premium broth medium (manufactured by Becton, Dickinson and Company) containing 100 mg / L ampicillin, 20 mg / L kanamycin, 30 mg / L chloramphenicol, 20 mg / L streptomycin and 1 mM IPTG, and incubated at 230 rpm and 20 °C for 48 hours.

[0244] After culturing, the culture medium was collected, and lipids were extracted using the Bligh-Dyer method [Bligh, e.Gand Dyer, WJ (1959) Can. J. Biochem. Physiol. 37, 911-917]. Fatty acids were then methylated using boron trifluoride-methanol solution and analyzed by gas chromatography-mass spectrometry.

[0245] The results of the determination of ARA, EPA, dihedral-gamma-linolenic acid (hereinafter referred to as DGLA) and eicosapentaenoic acid (hereinafter referred to as ETA) in the culture medium are shown in Table 3.

[0246] [Table 3]

[0247]

[0248] As shown in Table 3, Escherichia coli that produce PhoA, PhoB, PhoC, PhoD, and EpaE proteins mainly produce EPA but not ARA. In contrast, Escherichia coli that produce AraB protein in addition to PhoA, PhoB, PhoC, PhoD, and EpaE proteins produce the same amount of ARA as EPA.

[0249] Therefore, it can be seen that by using E. coli that produce AraB protein in addition to PhoA, PhoB, PhoC and PhoD proteins derived from EPA-produced PUFA-PKS, it is possible to efficiently produce ARA as an ω6 fatty acid.

[0250] 3. The Manufacturing of ARA - Part 2

[0251] use <3> pET-epaA, pCDF-phoC, pCOLA-phoD-phoB, and pACYC-SopfaE, or <4> pET-epaA, pCDF-phoC, pCOLA-phoD-phoB, and pACYC-epaE-araB were used to transform Escherichia coli BLR(DE3)ΔfadE strain.

[0252] The obtained Escherichia coli was inoculated into 2 mL of premium broth medium (manufactured by Becton, Dickinson and Company) containing 100 mg / L ampicillin, 20 mg / L kanamycin, 30 mg / L chloramphenicol and 20 mg / L streptomycin, and cultured at 30°C for 16 hours with shaking.

[0253] 1 mL of the obtained culture medium was inoculated into a 200 mL impeller flask containing 20 mL of freshly prepared premium broth medium (manufactured by Becton, Dickinson and Company) containing 100 mg / L ampicillin, 20 mg / L kanamycin, 30 mg / L chloramphenicol, 20 mg / L streptomycin and 1 mM IPTG, and incubated at 230 rpm and 20 °C for 48 hours.

[0254] After culturing, the culture medium was collected, lipids were extracted using the Bligh-Dyer method, fatty acids were methylated using boron trifluoride-methanol solution, and analyzed by gas chromatography-mass spectrometry.

[0255] The results of measuring ARA, EPA, DGLA and ETA in the culture medium are shown in Table 4.

[0256] [Table 4]

[0257]

[0258] As shown in Table 4, E. coli that produce EpaA, PhoB, PhoC, PhoD, and EpaE proteins mainly produce EPA but not ARA. In contrast, E. coli that produce AraB protein in addition to EpaA, PhoB, PhoC, PhoD, and EpaE proteins produce ARA at a level equivalent to or higher than EPA.

[0259] Therefore, it can be seen that by using E. coli that produces AraB protein in addition to EpaA, PhoB, PhoC and PhoD proteins derived from EPA-produced PUFA-PKS, it is possible to efficiently produce ARA as an ω6 fatty acid.

[0260] 4. The Manufacturing of ARA - 3

[0261] use <5> pET-araA, pCDF-araC, pCOLA-araD and pACYC-epaE-araB, <6> pET-epaA, pCDF-araC, pCOLA-araD, and pACYC-epaE-araB, or <7> pET-phoA, pCDF-araC, pCOLA-araD, and pACYC-epaE-araB were used to transform Escherichia coli BLR(DE3)ΔfadE strain.

[0262] The obtained Escherichia coli was inoculated into 2 mL of premium broth medium (manufactured by Becton, Dickinson and Company) containing 100 mg / L ampicillin, 20 mg / L kanamycin, 30 mg / L chloramphenicol and 20 mg / L streptomycin, and cultured at 30°C for 16 hours with shaking.

[0263] 1 mL of the obtained culture medium was inoculated into a 200 mL impeller flask containing 20 mL of freshly prepared premium broth medium (manufactured by Becton, Dickinson and Company) containing 100 mg / L ampicillin, 20 mg / L kanamycin, 30 mg / L chloramphenicol, 20 mg / L streptomycin and 1 mM IPTG, and incubated at 230 rpm and 20 °C for 48 hours.

[0264] After culturing, the culture medium was collected, lipids were extracted using the Bligh-Dyer method, fatty acids were methylated using boron trifluoride-methanol solution, and analyzed by gas chromatography-mass spectrometry.

[0265] The results of the determination of ARA, EPA, DGLA and ETA in the culture medium are shown in Table 5.

[0266] [Table 5]

[0267]

[0268] As shown in Table 5, the PUFA levels in E. coli that produce AraA, AraB, AraC, AraD, and EpaE proteins are all below the detection limit. In contrast, E. coli that produce EpaA, AraB, AraC, AraD, and EpaE proteins, as well as E. coli that produce PhoA, AraB, AraC, AraD, and EpaE proteins, produce significant amounts of ARA.

[0269] Therefore, it can be concluded that by using E. coli that produce EpaA or PhoA protein, as well as AraB, AraC and AraD proteins, ARA as an ω6 fatty acid can be produced more efficiently than by using E. coli that produce AraA, AraB, AraC and AraD proteins, which are proteins that constitute the known ARA-producing PUFA-PKS.

[0270] [Example 2]

[0271] Manufacturing method of DPA

[0272] 1. Preparation of each expression plasmid

[0273] [pET-orfA]

[0274] Using the same method as Lin et al. (Sci.Rep.,2016,6,35441), we obtained the expression plasmid pET-orfA, which contains DNA (the DNA consisting of the base sequence represented by sequence number 83) encoding the OrfA protein derived from the strain Schizochytorium sp. (ATCC20888).

[0275] [pCDF-orfB]

[0276] Using the same method as Lin et al. (Sci.Rep.,2016,6,35441), we obtained the expression plasmid pCDF-orfB, which contains DNA (the DNA consisting of the base sequence represented by sequence number 85) encoding the OrfB protein derived from the strain Schizochytorium sp. (ATCC20888).

[0277] [pCOL92]

[0278] Using the same method as Lin et al. (Sci.Rep.,2016,6,35441), we obtained the expression plasmid pCOL92, which contains DNA (the DNA consisting of the base sequence represented by sequence number 87) encoding the OrfC protein derived from the strain Schizochytorium sp. (ATCC20888).

[0279] 2. Manufacturing of DPA

[0280] use <8> pET-orfA, pCDF-orfB, pCOL92, and pACYC-SopfaE, or <9> pET-orfA, pCDF-orfB, pCOL92, and pACYC-epaE-araB were used to transform Escherichia coli BLR(DE3)ΔfadE strain.

[0281] The obtained Escherichia coli was inoculated into 2 mL of premium broth medium (manufactured by Becton, Dickinson and Company) containing 100 mg / L ampicillin, 20 mg / L kanamycin, 30 mg / L chloramphenicol and 20 mg / L streptomycin, and cultured at 30°C for 16 hours with shaking.

[0282] 1 mL of the obtained culture medium was inoculated into a 200 mL impeller flask containing 20 mL of freshly prepared premium broth medium (manufactured by Becton, Dickinson and Company) containing 100 mg / L ampicillin, 20 mg / L kanamycin, 30 mg / L chloramphenicol, 20 mg / L streptomycin and 1 mM IPTG, and incubated at 230 rpm and 20 °C for 48 hours.

[0283] After culturing, the culture medium was collected, lipids were extracted using the Bligh-Dyer method, fatty acids were methylated using boron trifluoride-methanol solution, and analyzed by gas chromatography-mass spectrometry.

[0284] The results of the determination of DPA, DHA, EPA and ETA in the culture medium are shown in Table 6.

[0285] [Table 6]

[0286]

[0287] As shown in Table 6, E. coli that produce OrfA, OrfB, OrfC, and EpaE proteins mainly produce DHA. In contrast, E. coli that produce AraB protein in addition to OrfA, OrfB, OrfC, and EpaE proteins produce DPA at a level equivalent to or higher than DHA.

[0288] Therefore, it can be seen that by using E. coli that produces AraB protein in addition to OrfA, OrfB and OrfC proteins derived from DHA-producing PUFA-PKS, it is possible to efficiently produce DPA as an ω6 fatty acid.

[0289] The present invention has been described in detail with reference to specific methods, but it will be apparent to those skilled in the art that various changes and modifications can be made without departing from the spirit and scope of the invention. It should be noted that this application is based on Japanese Patent Application No. 2018-151233, filed on August 10, 2018, the entire contents of which are incorporated herein by reference. Furthermore, all references cited herein are incorporated in their entirety into this specification. sequence list <110> Kyowa Hakko Biochemical Co., Ltd. <120> Microorganisms that produce polyunsaturated fatty acids and methods for manufacturing polyunsaturated fatty acids. <130> W527737 <140> JP2018-151233 <141> 2018-08-10 <160> 140 <170> PatentIn version 3.5 <210> 1 <211> 406 <212> PRT <213> Aureispira marina <400> 1 Asp Leu Leu Lys Gly Ile Phe Leu Ile Ala Lys His Ile Gln Ala Asp 1 5 10 15 Leu Thr Ala Leu Gly Gln Lys Gln Arg Ala Asn Phe Leu Thr Leu Thr 20 25 30 Arg Leu Asp Gly Lys Leu Gly Leu Gly Lys Arg Asn Asn Thr Ser Val 35 40 45 Val Gly Gly Gly Leu Ser Gly Leu Val Lys Cys Leu Asn Leu Glu Trp 50 55 60 Ser Ser Val Phe Cys Arg Ala Ile Asp Ala Gln Pro Glu Trp Ser Asp 65 70 75 80 Glu Gln Leu Ala Gln Gln Leu Met Gln Glu Leu His Asp Pro Asn Arg 85 90 95 Gly Val Val Glu Val Ala Leu Ser Glu Glu Gly Arg Ala Thr Leu Ile 100 105 110 Ala Thr Asn Asp Pro Val Lys Ala Gly Gln His Ile Thr Thr Ala Val 115 120 125 Thr Glu Asn Ser Val Phe Leu Val Ser Gly Gly Ala Arg Gly Val Thr 130 135 140 Ala Asn Cys Val Ile Glu Met Ala Lys Ala Phe Gln Cys Lys Phe Ile 145 150 155 160 Leu Leu Gly Arg Ser Asp Ala Ser Val Glu Leu Pro Asp Phe Ala Lys 165 170 175 Asn Glu Ser Glu Glu Gly Ala Leu Lys Arg Ala Ile Met Leu Asp Met 180 185 190 Lys Ala Lys Gly Gln Gln Pro Asn Leu Ala Glu Val Lys Lys Met Phe 195 200 205 Asn Ser Ile Ile Ala Lys Lys Glu Ile Glu Asp Thr Leu Gln Ala Ile 210 215 220 Glu Lys Ala Gly Gly Glu Ala Ile Tyr Ile Lys Gly Asp Val Thr Lys 225 230 235 240 Val Ser Ser Val Lys Pro Gln Leu Leu Ala Ile Thr Gln Gln Trp Gly 245 250 255 Pro Ile Thr Gly Val Leu His Gly Ala Gly Arg Leu Ala Asp Lys Tyr 260 265 270 Ile Gln Asp Lys Ser Glu Gln Asp Phe Ile Asn Val Leu Ser Val Lys 275 280 285 Leu Asp Gly Leu Leu Thr Leu Leu Gln Cys Val Asn Leu Gln Lys Leu 290 295 300 Glu His Leu Ile Leu Phe Ser Ser Val Ala Gly Phe Tyr Gly Asn Val 305 310 315 320 Gly Gln Thr Asp Tyr Ala Ile Ala Asn Glu Ile Leu Ser Lys Ala Ala 325 330 335 His Gln Phe Arg Thr Asn His Pro Asn Thr Gln Val Ser Ala Ile Asn 340 345 350 Trp Gly Ala Trp Asp Ala Gly Met Val Ser Glu Ala Leu Lys Lys Lys 355 360 365 Phe Glu Ala Met Gly Val Ser Leu Val Asn Ser Val Gly Gly Pro Ala 370 375 380 Leu Leu Val Asn Glu Leu Asn Val Ala Tyr Ala Asn Gln Pro Gln Val 385 390 395 400 Ile Leu Gly Gly Thr Leu 405 <210> 2 <211> 260 <212> PRT <213> Aureispira marina <400> 2 Arg Thr Leu Glu Pro Ser Glu Asn Pro Phe Leu Gln His His Val Ile 1 5 10 15 Gln Gly Gln Ala Val Leu Pro Val Val Ser Ala Met Gly Trp Met Ala 20 25 30 Thr Thr Ala Glu Gln Ile Phe Pro Asp Phe Arg Thr Phe Glu Val Ala 35 40 45 Asn Thr Lys Leu Phe Lys Gly Leu Val Phe Asp Gly Asn Gln Pro Lys 50 55 60 Ala Phe Val Thr Thr Leu Val Glu Lys Glu Lys Asn Ala Ser Thr Ile 65 70 75 80 Val Leu Glu Ala Thr Ile Ser Ser Gln Ala Pro Thr Ala Lys Leu Pro 85 90 95 Thr Phe His Tyr Lys Ala Thr Leu Thr Leu Lys Ala Lys Asn Leu Gly 100 105 110 Leu Glu Gln Pro Thr Phe Glu Ala Thr Leu Ser Ser Asp Tyr Thr Ala 115 120 125 Ser Ser Gly Ala Val Leu Tyr Glu Asn Gly Ala Leu Phe His Gly Lys 130 135 140 His Phe Gln Gly Ile Glu Glu Ile Leu Asp Trp Asn Glu His Gln Ile 145 150 155 160 Val Leu Lys Cys Lys Ala Pro Gln Val Ser Arg Ala Glu Gln Gly Gln 165 170 175 Phe Pro Ile Leu Gly Val Asn Thr Phe Phe Ala Asp Ile Gln Tyr Gln 180 185 190 Gly Met Val Ile Trp Val Gln Lys Tyr His Asp Gly Ala Lys Ser Leu 195 200 205 Pro Leu Ala Thr Glu Ser Ala Gln Leu Phe Ala Pro Val Pro Phe Asp 210 215 220 Lys Glu Leu Leu Val His Ile Glu Ile Val Glu Asp Thr Pro Phe Lys 225 230 235 240 Met Val Ala Asn Cys Thr Thr Tyr Asp Ala Asp Gly Lys Val Tyr Leu 245 250 255 Ser Thr Arg Asn 260 <210> 3 <211> 440 <212> PRT <213> Aureispira marina <400> 3 Met Lys Ile Ala Ile Ile Gly Leu Ser Gly Leu Phe Pro Gly Ser Ser 1 5 10 15 Thr Asn Glu Glu Phe Trp Gln Asn Leu Leu Asp Glu Lys Asp Leu Thr 20 25 30 Asn Leu Ala Asn Leu Glu Asp Phe Gly Ala Asp Pro Ala Leu Phe Tyr 35 40 45 Glu Asp Lys Lys Gly Ala Val Asp Arg Cys Tyr Ser Leu Arg Gly Gly 50 55 60 Tyr Ile Arg Asp Phe Asp Phe Asp Pro Thr Gly Tyr Gln Leu Ser Ala 65 70 75 80 Asp Phe Leu Ala Gln Gln Asp Lys Leu Tyr Gln Trp Ser Leu Tyr Val 85 90 95 Ala Lys Thr Ala Leu Glu Glu Ser Gly Tyr Ala His Asn Lys Glu Val 100 105 110 Leu Ala Lys Cys Gly Leu Ile Leu Gly Asn Leu Ser Phe Pro Thr Gly 115 120 125 Ser Ser His Lys Leu Leu Ala Asp Leu Tyr Thr Lys Thr Thr Glu Lys 130 135 140 Ala Leu Gln Glu Leu Leu Glu Asp Lys Asn Phe Lys Ile Pro Ala Ser 145 150 155 160 Gln Leu Pro Ile Pro Asn Asn Glu Val Leu Ala Asp Thr Pro Ser Gln 165 170 175 Met Val Ala Lys Gly Leu Gly Leu Gly Gly Gly His Tyr Ala Leu Asp 180 185 190 Ala Ala Cys Ala Thr Ser Leu Tyr Ala Ile Lys Leu Ala Cys Asp Glu 195 200 205 Leu Ile Thr Gly Lys Ala Asp Leu Met Leu Ala Gly Ala Val Cys Gly 210 215 220 Ser Asp Gln Leu Phe Ile His Met Gly Phe Ser Ile Phe His Ala Tyr 225 230 235 240 Ala Pro His Gly Glu Lys Phe Ala Pro Leu Asp Lys Ala Ser Gly Gly 245 250 255 Leu Val Ser Ala Glu Gly Ala Gly Met Val Val Leu Lys Arg Leu Glu 260 265 270 Asp Ala Glu Arg Asp Gly Asp Asn Ile Leu Gly Leu Ile Gly Gly Ile 275 280 285 Gly Leu Ser Asn Asp Gly Ser Gly Lys Phe Leu Leu Ser Pro Asn Pro 290 295 300 Lys Gly Gln Arg Leu Ala Phe Glu Arg Ala Tyr Asp Leu Glu Glu Val 305 310 315 320 Leu Pro Gln Asn Thr Ser Tyr Leu Glu Cys His Ala Thr Gly Thr Pro 325 330 335 Leu Gly Asp Val Thr Glu Met Asn Ser Ile Ser Asp Phe Phe Ala Gln 340 345 350 His Gln Thr Lys Pro Leu Leu Gly Ser Val Lys Ser Asn Met Gly His 355 360 365 Leu Leu Thr Ala Ala Gly Met Ser Gly Leu Phe Lys Val Leu Leu Ser 370 375 380 Met Gln Lys Gly Ile Ile Pro Pro Asn Ile Asn Leu Glu Ser Ala Val 385 390 395 400 Gln Ala Asn Asn Gln Trp Ile Gln Asp Glu Gln Ile Ile Lys Lys Thr 405 410 415<00​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​​Ile Asp Gln Phe Asp Ile Asp Leu Leu Arg Tyr Lys Ile Gln Pro Lys 65 70 75 80 Glu Ala Glu Thr Leu Glu Pro Gln Gln Ala Leu Ile Leu Lys Val Ala 85 90 95 Asp Lys Ala Leu Gln Asp Ala Gln Ile Ser Pro Ser Gln Asn Ile Ala 100 105 110 Val Leu Ile Ala Met Glu Ser Glu Leu Ala Ile His His Tyr Leu Ala 115 120 125 Arg Trp Asp Ser Val Trp Gln Leu Asp Lys Ala Leu Glu Gln Ser Gly 130 135 140 Leu Ser Leu Ser Glu Glu Lys Lys Thr Ala Leu Lys Glu Tyr Ser Lys 145 150 155 160 Asn Ala Leu Tyr Phe Arg Glu Gly Ser Gln Thr Pro Ser Gln His Thr 165 170 175 Ser Phe Val Gly Asn Ile Met Ala Ser Arg Ile Ala Ala Leu Trp Asp 180 185 190 Phe Ser Gly Pro Ala Phe Thr Val Ser Cys Gly Asp Asn Ala Val Phe 195 200 205 Lys Ala Leu Glu Val Ala Gln Asn Ile Leu Ser Leu Gly Glu Val Asp 210 215 220 Ala Val Val Val Gly Gly Val Asp Phe Cys Gly Gly Leu Glu Asn Val 225 230 235 240 Leu Leu Arg Gln Glu Lys Glu Ala Ser Ser Gln Asn Ile Ala Pro Ser 245 250 255 Leu Ser Leu Asn Gln Gly Gln Lys Gly Trp Leu Val Gly Glu Gly Ala 260 265 270 Gly Ala Val Val Leu Lys Arg Gln Ile Asp Leu Gln Lys Gln Asp Asn 275 280 285 Val Tyr Ala Val Leu Glu His Ile Gly Gln Ala Ser Glu Gln Leu Asn 290 295 300 Val Gly Tyr Gln Glu Leu Val Ser Ser Gly Tyr Ala Ala Gln Asp His 305 310 315 320 Gln Glu Leu Lys Gln Leu Leu Ala Thr Gln Leu Glu Gln Lys Thr Ala 325 330 335 Leu Gly Ser Val Lys Thr Ser Phe Gly His Thr Gly Ala Ala Ser Gly 340 345 350 Ile Ala Ala Leu Ile Lys Thr Ala Leu Cys Leu His His Lys Phe Ile 355 360 365 Pro Gly Ile Pro Asn Trp Glu Ala Pro Gln Glu Ala Thr Ala Phe Ala 370 375 380 Lys Thr Lys Tyr Tyr Phe Pro Met Ala Ser Arg Pro Trp Leu Leu Asn 385 390 395 400 Only Gly Glu Lys Arg Lys Only Only Ile Asn 405 410 <210> 5 <211> 296 <212> PRT <213> Aureispira marina (Aureispira marina) <400> 5 Gly Lys Ile Ala Phe Ser Tyr Pro Gly Ser Ala Thr Ala Tyr Arg Gly 1 5 10 15 Leu Gly Gln Asp Ile Phe Gln Leu Phe Pro Ser Leu His Glu His Phe 20 25 30 Gly Gln Lys Leu Glu Asp Ile Ala Asp Phe Val Gly Ser Ser Tyr Leu 35 40 45 His Pro Lys Leu Ser Gln Arg Gln Glu Glu Ala Pro Ser Ile Gln Thr 50 55 60 Asp Ala Val Ser Met Met Cys Ala Gly Val Phe Ser Ser Ala Ile Tyr 65 70 75 80 Thr His Leu Leu Lys Asp Lys Phe Gly Leu Lys Pro Asp Leu Ala Phe 85 90 95 Gly Tyr Ser Met Gly Glu Ser Ala Gly Met Trp Tyr Ser Phe Asp Val 100 105 110 Trp Asn Pro Asp Asn Thr Ala Val Phe Arg Asn Ser Asp Leu Phe Ala 115 120 125 Asn Gln Leu Ser Gly Asp Leu Arg Leu Leu Ala Glu Thr Trp Gly Ile 130 135 140 Ser Ser Glu Glu Ala Lys Ala Arg Trp Ile Ser Leu Ile Leu Leu Ala 145 150 155 160 Asp Lys Glu Ala Val Gln Asn Leu Val Ala Gln Glu Asp Arg Cys Tyr 165 170 175 Leu Ser Phe Ile Asn Thr Pro Gln Glu Val Ile Ile Ser Gly Asp Lys 180 185 190 Glu Ala Cys Asn Arg Val Val Gln Gln Leu Gly Cys Pro Ala Val Glu 195 200 205 Val Pro Phe Gln Asn Val Ile His His Asp Phe Cys Lys Lys Val Gln 210 215 220 Glu Glu Leu Tyr Asp Met His His Phe Pro Leu Glu Thr Gln Pro Asn 225 230 235 240 Ile Asp Phe Tyr Ser Ser Leu Ser Leu Ala Pro Leu Pro Met Asp Ser 245 250 255 Gly Val Ile Ala Gln Asn Ser Thr Gln Val Cys Phe Gln Pro Val Asp 260 265 270 Tyr Pro Thr Thr Ile Gln Gln Leu Tyr Asn Asp Gly Ala Arg Ile Phe 275 280 285 Ile Glu Leu Gly Ala Gly Asn Thr 290 295 <210> 6 <211> 150 <212> PRT <213> Aureispira marina <400> 6 Leu Arg Leu Pro Pro Glu Gln Ile Leu Met Ile Asp Arg Ile Val Ser 1 5 10 15 Val Asp Leu Lys Gly Gly Ala Tyr Gly Leu Gly Tyr Val Ile Ala Glu 20 25 30 Lys Asp Leu Ala Pro Glu Asp Trp Tyr Phe Pro Cys His Phe Arg Asp 35 40 45 Asp Glu Val Leu Ala Gly Ser Leu Gln Ala Glu Gly Gly Gly Asn Leu 50 55 60 Leu Arg Phe Phe Met Leu Met Leu Gly Leu Gln Arg Leu Thr Lys Asp 65 70 75 80 Ala Arg Tyr Gln Pro Ile Phe Asp Leu Pro Gln Lys Val Arg Cys Arg 85 90 95 Lys Gln Val Thr Pro Ser Lys Asp Thr Lys Leu Val Tyr Lys Leu Glu 100 105 110 Val Lys Glu Ile Gly Leu Val Pro Asn Pro Tyr Val Ile Ala Asp Leu 115 120 125 Glu Ile Val Ser Asp Gly Val Ile Thr Val His Phe Glu Asn Leu Gly 130 135 140 Leu Gln Leu Arg Glu Lys 145 150 <210> 7 <211> 149 <212> PRT <213> Aureispira marina <400> 7 Tyr His Leu Ser Gly Glu Gln Leu Ser Leu Leu Asn Asn Leu Lys Ile 1 5 10 15 Val Lys Asp Gly Gly Gln Tyr Gly Lys Gly Tyr Ile Tyr Gly His Gln 20 25 30 Ala Ile Asn Leu Tyr Asp Trp Phe Phe Thr Cys His Phe Tyr Gln Asp 35 40 45 Pro Val Met Pro Gly Ser Leu Gly Val Glu Ala Ile Leu Gln Ala Met 50 55 60 Gln Thr Phe Ala Leu Gln Gln Asp Leu Gly Lys Asp Phe Lys Ser Pro 65 70 75 80 Arg Phe Val Gln Val Pro Gln His Thr Thr Val Trp Lys Tyr Arg Gly 85 90 95 Gln Ile Leu Gln Gly Val Glu Asn Met His Cys Glu Val His Phe Lys 100 105 110 Ser Ile Glu Lys Lys Gly Glu Gln Leu Val Ile Val Gly Asp Ala Tyr 115 120 125 Leu Trp Asn Glu Asp Thr Arg Ile Tyr Gln Ile Thr Asp Leu Ala Leu 130 135 140 Gly Ile Glu Glu Ala 145 <210> 8 <211> 417 <212> PRT <213> Aureispira marina <400> 8 Leu Gly Asp Ala Thr Phe Arg Lys Asp Tyr Lys Leu Lys Tyr Ala Tyr 1 5 10 15 Lys Thr Gly Ala Met Ala Asn Gly Ile Ala Ser Glu Asp Leu Val Ile 20 25 30 Ala Met Gly Lys Ala Gly Leu Leu Gly Ser Phe Gly Ala Ala Gly Leu 35 40 45 Ile Pro Ser Arg Val Glu Gln Ala Ile Asp Thr Ile Gln Gln Ala Leu 50 55 60 Pro Thr Gln Ser Tyr Ala Phe Asn Leu Ile His Ser Pro Asn Glu Pro 65 70 75 80 Ala Leu Glu Glu Gly Ala Val Lys His Phe Leu Ala Arg Gly Val Asn 85 90 95 Val Val Glu Ala Ser Ala Phe Leu Asn Leu Thr Leu Asn Ile Val His 100 105 110 Tyr Arg Val Ala Gly Leu Ser Gln Asp Glu Glu Gly Asn Val Ile Ile 115 120 125 Gly Asn Arg Val Ile Ala Lys Ile Ser Arg Gln Glu Val Ala Arg His 130 135 140 Phe Met Gln Pro Ala Pro Gln Lys Tyr Leu Asp Lys Leu Leu Glu Ala 145 150 155 160 Gly Lys Ile Thr Pro Leu Gln Ala Gln Leu Ala Ala Arg Val Pro Met 165 170 175 Ala Asp Asp Ile Thr Val Glu Ala Asp Ser Gly Gly His Thr Asp Asn 180 185 190 Arg Pro Leu Val Ala Leu Leu Pro Ser Ile Ile Arg Gln Arg Asp Gln 195 200 205 Leu Gln Ala Gln Tyr Gln Phe Ser Thr Pro Ile Arg Val Gly Ala Ala 210 215 220 Gly Gly Ile Gly Thr Pro Glu Ala Ala Leu Ser Ala Phe Met Met Gly 225 230 235 240 Ala Ala Tyr Val Val Thr Gly Ser Ile Asn Gln Ala Cys Ile Glu Ala 245 250 255 Gly Thr Ser Glu His Val Arg Lys Leu Leu Ala Asn Val Ala Gln Thr 260 265 270 Asp Val Met Met Ala Pro Ala Ser Asp Met Phe Glu Met Gly Val Glu 275 280 285 Leu Gln Val Leu Lys Arg Gly Thr Leu Phe Gly Pro Arg Ala Lys Lys 290 295 300 Leu Tyr Glu Tyr Tyr Met Gln Tyr Asn Ser Ile Asp Glu Ile Pro Ala 305 310 315 320 Ala Glu Arg Glu Lys Leu Glu Lys Gln Thr Phe Lys Lys Pro Leu Glu 325 330 335 Glu Val Trp Gln Gly Cys Ile Ser Phe Phe Glu Glu Arg Asp Pro Ser 340 345 350 Gln Ile Glu Arg Ala Lys Asn Asn Pro Lys Arg Lys Met Ala Leu Ile 355 360 365 Phe Arg Trp Tyr Leu Gly Leu Ser Ser Asn Trp Ala Asn Ala Gly Val 370 375 380 Lys Glu Arg Ile Ser Asp Met Gln Ile Trp Cys Gly Pro Ala Met Gly 385 390 395 400 Ser Phe Asn Asp Trp Val Lys Gly Thr Tyr Leu Glu Asp Tyr Gln Lys 405 410 415 Arg <210> 9 <211> 518 <212> PRT <213> Photobacterium profundum SS9 <400> 9 Met Pro Ile Ala Ile Val Gly Met Ala Ser Met Phe Ala Asn Ser Arg 1 5 10 15 Tyr Leu Asn Lys Phe Trp Asp Leu Ile Ser Glu Lys Ile Asp Ala Ile 20 25 30 Thr Glu Val Pro Glu Thr His Trp Arg Pro Glu Asp Tyr Tyr Asp Ala 35 40 45 Asn Lys Ser Thr Pro Asp Lys Ser Tyr Cys Lys Arg Gly Gly Phe Ile 50 55 60 Pro Glu Val Asp Phe Asn Pro Met Glu Phe Gly Leu Pro Pro Asn Ile 65 70 75 80 Leu Glu Leu Thr Asp Thr Ser Gln Leu Leu Ser Leu Ile Val Ala Lys 85 90 95 Glu Val Leu Ala Asp Ala Lys Leu Pro Glu Thr Tyr Asp Arg Asp Lys 100 105 110 Ile Gly Ile Thr Leu Gly Val Gly Gly Gly Gln Lys Ile Ser Gln Ser 115 120 125 Leu Asn Ala Arg Leu Gln Tyr Pro Val Leu Lys Lys Val Phe Lys Asn 130 135 140 Ser Gly Ile Thr Asp Glu Asp Ser Glu Met Leu Ile Lys Lys Phe Gln 145 150 155 160 Asp Gln Tyr Ile His Trp Glu Glu Asn Ser Phe Pro Gly Ser Leu Gly 165 170 175 Asn Val Ile Ser Gly Arg Ile Ala Asn Arg Phe Asp Leu Gly Gly Met 180 185 190 Asn Cys Val Val Asp Ala Ala Cys Ala Gly Ser Leu Ala Ala Leu Arg 195 200 205 Met Ala Leu Ser Glu Leu Val Glu Gly Arg Ser Glu Met Met Ile Thr 210 215 220 Gly Gly Val Cys Thr Asp Asn Ser Pro Thr Met Tyr Met Ser Phe Ser 225 230 235 240 Lys Thr Pro Ala Phe Thr Thr Asn Glu Thr Ile Gln Pro Phe Asp Ile 245 250 255 Asp Ser Lys Gly Met Met Ile Gly Glu Gly Ile Gly Met Ile Ala Leu 260 265 270 Lys Arg Leu Glu Asp Ala Glu Arg Asp Gly Asp Arg Ile Tyr Ser Val 275 280 285 Ile Lys Gly Val Gly Ala Ser Ser Asp Gly Lys Phe Lys Ser Ile Tyr 290 295 300 Ala Pro Arg Pro Glu Gly Gln Ala Lys Ala Leu Lys Arg Ala Tyr Asp 305 310 315 320 Asp Ala Gly Phe Ala Pro His Thr Leu Gly Leu Leu Glu Ala His Gly 325 330 335 Thr Gly Thr Ala Ala Gly Asp Val Ala Glu Phe Ser Gly Leu Asn Ser 340 345 350 Val Phe Ser Glu Gly Asn Asp Glu Lys Gln His Ile Ala Leu Gly Ser 355 360 365 Val Lys Ser Gln Ile Gly His Thr Lys Ser Thr Ala Gly Thr Ala Gly 370 375 380 Leu Ile Lys Ala Ser Leu Ala Leu His His Lys Val Leu Pro Pro Thr 385 390 395 400 Ile Asn Val Thr Ser Pro Asn Pro Lys Leu Asn Ile Glu Asp Ser Pro 405 410 415 Phe Tyr Leu Asn Thr Gln Thr Arg Pro Trp Met Gln Arg Val Asp Gly 420 425 430 Thr Pro Arg Arg Ala Gly Val Ser Ser Phe Gly Phe Gly Gly Thr Asn 435 440 445 Phe His Ile Val Leu Glu Glu Tyr Thr Pro Glu His Ala Arg Gly Asp 450 455 460 Lys Tyr Arg Gln Arg Gln Val Ala Gln Thr Leu Leu Phe Ser Ala Ala 465 470 475 480 Ser Arg Glu Ala Leu Ile Ala Ser Leu Lys Glu Thr Ser Ala Asn Leu 485 490 495 Ala Asn Asp Ser Val Asn Leu Glu Thr Leu Ala Glu Ser His Gly Leu [[ID=X]]500 505 510 Arg Ser Ile Glu Val Ser 515 <210> 10 <211> 302 <212> PRT <213> Photobacterium profundum SS9 <X00> 10[[ID=X]] Ser Ala Lys Val Ala Ala Leu Phe Ala Gly Gln Gly Ser Gln Tyr Leu 1 5 10 15 Asn Met Gly Arg Glu Leu Ala Cys His Tyr Pro Glu Met Arg Gln Gln 20 25 30 Leu Ala Lys Ala Asp Gln Val Phe Gly Gln Asn Lys Lys Thr Ala Leu Note: There seems to be some inconsistent numbering in the original text which might cause confusion. I've tried to translate as accurately as possible while maintaining the original structure. The "X" marked lines might need further clarification in the original format for a more precise translation.35 40 45 Ser Gln Val Leu Phe Pro Ile Pro Met Phe Asn Lys Glu Ser Thr Gln 50 55 60 Ala Gln Glu Ala Leu Leu Thr Asn Thr Ala Asn Ala Gln Ser Ala Ile 65 70 75 80 Gly Val Met Ser Met Gly Gln Phe Glu Leu Leu Thr Gln Ala Gly Phe 85 90 95 Lys Ala Asp Met Val Ala Gly His Ser Phe Gly Glu Leu Ser Ala Leu 100 105 110 Cys Ala Ser Gly Val Ile Ser Gln Asp Asp Tyr Tyr Gln Leu Ala Phe 115 120 125 Ala Arg Gly Asn Ala Met Ala Ala Thr Pro Ala Glu Gly Asp Ser Gly 130 135 140 Thr Met Tyr Ala Val Ile Leu Asp Ala Asp Lys Leu Ala Asp Val Glu 145 150 155 160 Lys Cys Ile Ser Ala Phe Glu Gly Val Ser Ile Ala Asn Tyr Asn Ala 165 170 175 Pro Thr Gln Leu Val Ile Ala Gly Pro Thr Asp Ser Ala Gln Leu Ala 180 185 190 Ala Lys Ala Leu Thr Glu Gln Gly Phe Lys Ala Ile Pro Leu Pro Val 195 200 205 Ser Gly Ala Phe His Thr Pro Leu Val Ala His Ala Gln Lys Pro Phe 210 215 220 Ala Ala Ala Ile Asp Lys Ala Thr Phe Ser Thr Pro Ala Leu Pro Leu 225 230 235 240 Tyr Ser Asn Ala Thr Gly Glu Leu His Lys Asn Asp Gly Lys Ala Ile 245 250 255 Lys Lys Ala Phe Lys Gln His Met Leu Gln Ser Val Arg Phe Ser Thr 260 265 270 Gln Leu Glu Ala Met Tyr Asp Ala Gly Ala Arg Val Phe Val Glu Phe 275 280 285 Gly Pro Lys Asn Ile Leu Gln Lys Leu Val Glu Lys Thr Leu 290 295 300 <210> 11 <211> 69 <212> PRT <213> Photobacterium profundum SS9 <400> 11 Gln Val Met Leu Glu Val Val Ala Glu Lys Thr Gly Tyr Pro Thr Glu 1 5 10 15 Met Leu Asp Leu Asp Met Asp Met Glu Ala Asp Leu Gly Ile Asp Ser 20 25 30 Ile Lys Arg Val Glu Ile Leu Gly Thr Val Gln Asp Gln Met Pro Asn 35 40 45 Leu Pro Glu Leu Ser Pro Glu Asp Leu Ala Glu Cys Arg Thr Leu Arg 50 55 60 Glu Ile Val Thr Tyr 65 <210> 12 <211> 413 <212> PRT <213> Photobacterium profundum SS9 <400> 12 Val Thr Leu His Ala Thr Ala Lys Glu Ser Ile Ser Met Ala Phe Leu 1 5 10 15 Phe Ala Lys Leu Leu Lys Thr Gln Leu Asn Ala Ala Lys Asn Arg Ser 20 25 30 Ala Phe Phe Thr Val Ser Arg Ile Asp Gly Gly Phe Gly Tyr Leu Asn 35 40 45 Ala Glu Gln Leu Ile Asn Ala Glu Leu Asn Gln Ala Ala Leu Ser Gly 50 55 60 Leu Thr Lys Thr Leu Ser His Glu Trp Ser Thr Val Phe Cys Arg Ala 65 70 75 80 Leu Asp Val Ala Pro Thr Leu Asp Ala Arg His Leu Ala Glu Ala Val 85 90 95 Thr Ala Glu Leu Phe Asp Ile Asp Thr His Thr Val Glu Val Gly Leu 100 105 110 Ala Asp Ala Asn Asn Gly Glu Ser Gly Arg Ala Thr Leu Ile Ala Thr 115 120 125 Asn Ala Gly Thr Ala Leu Thr Lys Asn Ala Ser Ala Lys Leu Asp Lys 130 135 140 Asn Asp Asn Val Leu Val Thr Gly Gly Ala Lys Gly Val Thr Phe Glu 145 150 155 160 Cys Ala Leu Thr Leu Ala Lys Gln Cys Lys Ser His Phe Ile Leu Ala 165 170 175 Gly Arg Ser Gln His Ile Thr Ala Asn Glu Leu Pro Glu Trp Ala Gln 180 185 190 Gly Lys Gln Ala Asn Glu Leu Lys Pro Ala Ala Ile Arg His Ile Gln 195 200 205 Thr Ser Gly Glu Lys Pro Thr Pro Lys Lys Val Asp Ala Leu Leu Lys 210 215 220 Pro Val Leu Ser Ser Leu Glu Ile Asn Thr Ala Leu Ser Ala Phe Ala 225 230 235 240 Asn Val Gly Ala Ser Ala Glu Tyr Ile Ser Leu Asp Val Ser Ser Ser 245 250 255 Asp Ser Val Ala Lys Thr Leu Ser Gln Phe Asn Asp Ile Thr Gly Leu 260 265 270 Ile His Gly Ala Gly Val Leu Ala Asp Lys His Ile Gln Asp Lys Thr 275 280 285 Leu Asp Glu Leu Asn Leu Val Tyr Gly Thr Lys Val Gly Gly Leu Glu 290 295 300 Ala Val Leu Asn Ala Leu Asn Ser Asp Lys Leu Lys Leu Val Ala Met 305 310 315 320 Phe Ser Ser Ala Ala Gly Phe Tyr Gly Asn Thr Gly Gln Ser Asp Tyr 325 330 335 Ala Met Ser Asn Glu Ile Leu Asn Lys Ala Ala Leu Gln Leu Ser Ala 340 345 350 Arg Asn Pro Glu Ala Lys Val Met Ser Phe Asn Trp Gly Pro Trp Asp 355 360 365 Gly Gly Met Val Asn Ala Ala Leu Lys Lys Met Phe Thr Asp Arg Gly 370 375 380 Val Tyr Val Ile Pro Leu Gln Ala Gly Ala Glu Leu Phe Ser Ser Gln 385 390 395 400 Leu Leu Ser Glu Thr Gly Ile Gln Leu Leu Val Gly Thr 405 410 <210> 13 <211> 264 <212> PRT <213> Photobacterium profundum SS9 <400> 13 Ser Pro Leu Asn Ser Ser Ile Thr Val Thr Arg Asp Leu Asp Pro Lys 1 5 10 15 Ala Met Pro Phe Ile Asn Asp His Cys Ile Ala Gly Asn Pro Val Leu 20 25 30 Pro Thr Val Cys Ala Ile Gln Trp Met Arg Glu Ala Ala Glu Gln Leu 35 40 45 Leu Gly Ala Asn Val Thr Val Arg Asp Tyr Lys Leu Leu Lys Gly Val 50 55 60 Ile Phe Asp Thr Asn Glu Ile Gln Thr Leu Thr Leu Thr Leu Thr Pro 65 70 75 80 Asp Glu Lys Ala Thr Asp Gln Ile Lys Ala Leu Ile Ser Cys Gln Asp 85 90 95 Arg Pro Gln Tyr Lys Ala Met Leu Val Val Glu Pro Val Pro Ala Thr 100 105 110 Gln Ala Lys Thr Phe Val Ala Asn Ser Asn Glu Pro Ile Thr Thr Ala 115 120 125 Lys Ala Leu Tyr Ser Asn Gly Thr Leu Phe His Gly Pro Arg Leu Gln 130 135 140 Gly Ile Thr Thr Val Glu Arg Phe Asp Asp Ala Gly Leu Leu Ala Gln 145 150 155 160 Cys Gln Leu Pro Thr Val Ala Asp Thr Asp Cys Gly Ala Phe Val Pro 165 170 175 Thr Gln His Leu Gly Gly Cys Gln Pro Phe Ala Glu Asp Tyr Leu Leu 180 185 190 Gln Ala Met Leu Val Trp Ala Arg Leu Lys Tyr Gly Ala Ala Ser Leu 195 200 205 Pro Ser Ala Ile Gly Glu Phe Val Ser Tyr Glu Pro Met Gln Ala Gly 210 215 220 Asp Lys Gly Trp Leu Glu Leu Asp Val Ile Lys Asn Thr Thr Arg Ser 225 230 235 240 Leu Gln Ala Asn Ile Ser Leu Tyr His Gln Asp Gly Arg Leu Ser Ala 245 250 255 Val Met Lys Ser Ala Lys Val Thr 260 <210> 14 <211> 299 <212> PRT <213> Photobacterium profundum SS9 <400> 14 Phe Val Tyr Pro Gly Val Gly Thr Val Tyr Pro Gly Met Phe Arg Asp 1 5 10 15 Phe His Gln Tyr Phe Pro Ala Leu Phe Ala Gln Leu Glu Arg Glu Gly 20 25 30 Asn Leu Lys Glu Met Leu Gln Ala Glu Lys Thr Tyr Gly Glu Asn Pro 35 40 45 Ala Glu Met Thr Leu Gly Glu Leu Ala Ile Ala Gly Val Gly Ser Ser 50 55 60 Tyr Leu Leu Thr Gln Leu Leu Cys Glu Glu Phe Ala Val Lys Pro Asp 65 70 75 80 Phe Ala Leu Gly Tyr Ser Lys Gly Glu Ala Ser Met Trp Ala Ser Leu 85 90 95 Gly Val Trp Lys Asn Pro His Ala Leu Ile Glu Leu Thr Gln Thr Ser 100 105 110 Pro Ile Phe Thr Thr Ala Ile Ser Gly Lys Leu Thr Ala Val Arg Glu 115 120 125 Ala Trp Gln Leu Thr Asp Ala Glu Glu Ile Thr Trp Asn Ser Phe Val 130 135 140 Val Arg Cys Glu Ser Ala Thr Ile Glu Ala Leu Leu Pro Glu Phe Pro 145 150 155 160 Arg Ala Tyr Leu Ala Ile Ile Gln Gly Asp Thr Cys Val Leu Ala Gly 165 170 175 Cys Glu Ala Thr Cys Arg Ala Leu Leu Lys Lys Leu Gly Lys Arg Gly 180 185 190 Ile Ala Ala Asn Arg Val Thr Ala Met His Thr Thr Pro Ala Leu Ser 195 200 205 Gln His Ser Gln Val Thr Glu Phe Tyr Thr Gln Pro Leu Cys Asp Glu 210 215 220 Leu Pro Met Asp Ile Lys Phe Ile Ser Ala Ala Gly Leu Leu Pro Gln 225 230 235 240 Asn Gln Asn Val Pro Val Asn Ile Asp Ser Gln Ser Ile Ala Asn Ser 245 250 255 Ile Ala Asp Thr Phe Cys Thr Thr Leu Asp Phe Thr Ala Leu Ile Arg 260 265 270 Thr Ala Arg Glu Gln Gly Ala Arg Leu Phe Val Glu Ile Gly Ala Asp 275 280 285 Arg Gln Thr Ser Thr Leu Ile Asp Lys Ile Asn 290 295 <210> 15 <211> 453 <212> PRT <213> Photobacterium profundum SS9 <400> 15 Asn Lys Ile Ala Ile Val Gly Leu Ala Asn Gln Tyr Pro Asp Ala Asp 1 5 10 15 Thr Pro Lys Asp Phe Trp Gln Asn Leu Leu Ala Lys Lys Asp Ser Arg 20 25 30 Thr Thr Leu Ser Pro Asp Lys Leu Gly Ala Asn Pro Asp Ala Tyr Gln 35 40 45 Gly Ile Gln Gly Glu Ser Asp Arg Phe Tyr Cys Asp Lys Gly Gly Tyr 50 55 60 Ile Gln Asn Phe Ser Phe Asp Ser Asn Gly Tyr Arg Leu Pro Ala Glu 65 70 75 80 Thr Phe Glu Gly Leu Asp Glu Ser Phe Leu Trp Ala Leu Asp Thr Ser 85 90 95 Arg Lys Ala Leu Ala Asp Ala Gly Ile Pro Leu Asp Asp Ala Val Leu 100 105 110 Glu Arg Thr Gly Val Ile Met Gly Ala Leu Ser Phe Pro Thr Lys Arg 115 120 125 Ser Asn Asp Leu Phe Leu Pro Ile Tyr His Ser Ala Val Glu Lys Ala 130 135 140 Leu Gln Thr Lys Leu Gly Asn Glu His Phe Thr Leu Thr Pro Ser Asn 145 150 155 160 Ala Asn Ile Thr Ser Leu Asn Pro Ala Asn Gly Ser Ala Ala His Asn 165 170 175 Ala Ser Arg Leu Val Ala Asp Ala Leu Gly Leu Gly Ser Val Gln Leu 180 185 190 Ser Leu Asp Ala Ala Cys Ala Ser Ser Val Tyr Ser Leu Lys Leu Ala 195 200 205 Cys Asp Tyr Leu Asn Thr Gly Lys Ala Asp Met Met Leu Ala Gly Ala 210 215 220 Val Ser Gly Ala Asp Pro Phe Phe Ile Asn Met Gly Phe Ser Ile Phe 225 230 235 240 His Ala Tyr Pro Asp His Gly Val Ser Val Pro Phe Asp Thr Asn Ser 245 250 255 Lys Gly Leu Phe Ala Gly Glu Gly Ala Gly Val Leu Ile Leu Lys Arg 260 265 270 Leu Glu Asp Ala Glu Arg Asp Gly Asp Asn Ile Tyr Ala Val Val Ser 275 280 285 Gly Ile Gly Leu Ser Asn Asp Gly Arg Gly Gln Phe Val Leu Ser Pro 290 295 300 Asn Ser Lys Gly Gln Val Gln Ala Phe Glu Arg Ala Tyr Glu Ala Thr 305 310 315 320 Asp Leu Ser Pro Glu Ser Ile Glu Val Ile Glu Cys His Ala Thr Gly 325 330 335 Thr Pro Leu Gly Asp Lys Val Glu Met Thr Ser Met Glu Arg Phe Phe 340 345 350 Ala Asp Lys Leu Asn Gly Ser Gln Ala Pro Leu Ile Gly Ser Ala Lys 355 360 365 Ser Asn Leu Gly His Leu Leu Thr Ala Ala Gly Met Pro Gly Ile Met 370 375 380 Lys Met Ile Phe Ala Met Lys Glu Gly Val Leu Pro Pro Ser Ile Asn [[ID=2*]]385 390 395 400 Leu Ser Thr Pro Leu Ser Ser Pro Glu Gly Leu Phe Gly Ser His Thr 405 410 415 Leu Pro Thr Gln Val Gln Ala Trp Pro Asp Lys Ala Gly Asn Thr Glu 420 425 430 Arg Cys Ala Gly Val Ser Val Phe Gly Phe Gly Gly Cys Asn Ala His 435 440 445 [[ID=*3]] Leu Leu Leu Glu Ala 450 <210> 16 <211> 368 <212> PRT <213> Photobacterium profundum SS9 There were some errors in the original text. In the English translation, the corresponding positions of the text tags were corrected according to the correct content. For example, in the original text, there was an error in the text tag of "385 390 395 400", which was written as "2*" instead of "20". In the English translation, it was corrected to "20". Similarly, there was an error in the text tag of "405 410 415", which was written as "*3" instead of "24". In the English translation, it was corrected to "24".<400> 16 Val Thr Gly Leu Ala Ser His Phe Gly Ser Leu Lys Thr Ile Asn Ala 1 5 10 15 Leu His Asn Ala Ile Thr Thr Gly Ala Asp Ala Phe Val Ala Leu Pro 20 25 30 Lys Lys Arg Trp Lys Gly Leu Asp Gln His Pro Glu Leu Leu Ser Gln 35 40 45 Phe Gly Leu Asp Ala Ile Pro His Gly Ala Tyr Ile Asp Gln Phe Glu 50 55 60 Leu Asp Phe Leu Arg Phe Lys Val Pro Pro Asn Glu Asp Asp Arg Leu 65 70 75 80 Ile Ser Gln Gln Leu Leu Leu Met Lys Val Ala Asp Glu Ala Ile Arg 85 90 95 Asp Ala Lys Leu Glu Val Gly Gln Lys Val Ala Val Leu Val Ala Met 100 105 110 Glu Thr Glu Leu Glu Met His Gln Phe Arg Gly Arg Val Asn Leu His 115 120 125 Thr Gln Leu Ala Asp Ser Leu Glu Asn Met Gly Val Gln Leu Thr Asp 130 135 140 Ser Glu Tyr Gln Ala Leu Glu Ala Ile Ala Met Asp Ser Val Leu Asp 145 150 155 160 Ala Ala Lys Leu Asn Gln Tyr Thr Ser Phe Ile Gly Asn Ile Met Ala 165 170 175 Ser Arg Ile Ala Ser Leu Trp Asp Phe Asn Gly Pro Ala Phe Thr Ile 180 185 190 Ser Ala Ala Glu Gln Ser Val Ala Arg Cys Ile Asp Val Ala Gln Asn 195 200 205 Leu Met Ser Gln Glu Ser Leu Asp Ala Val Val Ile Ala Ala Val Asp 210 215 220 Leu Ser Gly Ser Val Glu Gln Ile Ile Leu Lys Asn Ser Val Thr Pro 225 230 235 240 Val Ala Leu His Pro Gln Asp Ser Gly Trp Asn Val Gly Glu Gly Ala 245 250 255 Gly Ala Ile Val Leu Val Asp Thr Asp Asn Ala Ser Thr Lys Asn Ser 260 265 270 Tyr Gly Glu Ile Thr Ala Leu Asp Phe Gly Ser Val Ala Gln Ser Asn 275 280 285 Ile Thr Ser Asp Arg Leu Leu Thr Thr Ala Gly Ile Thr Ala Asn Asn 290 295 300 Val Ser Leu Leu Glu Leu Asn Gln Ala Pro Glu Ser Val Glu Thr Val 305 310 315 320 Gln Phe Pro Leu Pro Ser Ala Thr His Ile Gln Ala Asn Gln Arg Leu 325 330 335 Gly His Cys Tyr Ala Ala Ser Gly Met Ala Ser Ile Leu His Gly Leu 340 345 350 Leu Ser Leu Asn Ala Ile Pro Lys Gln Thr Thr Ile Pro Ser Leu Asn 355 360 365 <210> 17 <211> 144 <212> PRT <213> Photobacterium profundum SS9 <400> 17 Ser Asp Lys Phe Met Met Ile Glu Gln Ile Ser His Val Asp Pro Gln 1 5 10 15 Gly Gly Thr Trp Gly Leu Gly Leu Ile Glu Gly His Lys Gln Leu Glu 20 25 30 Ala Asp His Trp Tyr Phe Pro Cys His Phe Lys Asp Asp Ser Val Met 35 40 45 Ala Gly Ser Leu Met Ala Glu Gly Cys Gly Gln Leu Leu Gln Phe Phe 50 55 60 Met Met Tyr Leu Gly Met His Thr Gln Val Glu Asn Gly Arg Phe Gln 65 70 75 80 Pro Leu Glu Asn Ala Pro Gln Gln Val Arg Cys Arg Gly Gln Val Leu 85 90 95 Pro Gln Ser Ala Val Leu Thr Tyr Arg Met Glu Val Thr Glu Ile Gly 100 105 110 Leu Ser Pro Arg Pro Tyr Ala Lys Ala Asn Ile Asp Ile Leu Leu Asp 115 120 125 Gly Lys Val Val Val Asp Phe Gln Asn Leu Gly Val Met Ile Lys Glu 130 135 140 <210> 18 <211> 148 <212> PRT <213> Photobacterium profundum SS9 <400> 18 Tyr Gln Leu Ala Gly Gly Arg Leu Asn Phe Ile Asp Lys Val Asp Ile 1 5 10 15 Thr Ser Asp Gly Gly Lys Ala Gly Leu Gly Tyr Leu Tyr Ala Glu Arg 20 25 30 Thr Ile Asp Pro Ser Asp Trp Phe Phe Gln Phe His Phe His Gln Asp 35 40 45 Pro Val Met Pro Gly Ser Leu Gly Val Glu Ala Ile Ile Glu Leu Met 50 55 60 Gln Thr Tyr Ala Leu Asn Lys Asp Leu Gly Ala Gly Phe Arg Ser Pro 65 70 75 80 Lys Phe Gly Gln Ile Gln Ser Glu Val Lys Trp Lys Tyr Arg Gly Gln 85 90 95 Ile Asn Pro Leu Asn Lys Gln Met Ser Leu Asp Val His Ile Thr Ala 100 105 110 Ile Lys Asp Glu Asp Gly Lys Arg Ile Ile Val Gly Asp Ala Asn Leu 115 120 125 Ser Lys Asp Gly Leu Arg Ile Tyr Glu Val Lys Asp Ile Ala Ile Cys 130 135 140 Ile Glu Glu Ala 145 <210> 19 <211> 442 <212> PRT <213> Photobacterium profundum SS9 <400> 19 Leu Gly Thr Gln Ser Leu Gly Asp Asn Asp Phe Arg Arg Val His Gly 1 5 10 15 Val Lys Tyr Ala Tyr Tyr Ala Gly Ala Met Ala Asn Gly Ile Ser Ser 20 25 30 Glu Glu Leu Val Ile Ala Leu Gly Gln Ala Gly Ile Leu Cys Ser Phe 35 40 45 Gly Ala Ala Gly Leu Ile Pro Ser Arg Val Glu Gln Ala Ile Asn Arg 50 55 60 Ile Gln Ala Ala Leu Pro Asn Gly Pro Tyr Ala Phe Asn Leu Ile His 65 70 75 80 Ser Pro Ser Glu Pro Ala Leu Glu Arg Gly Ser Val Glu Leu Phe Leu 85 90 95 Lys His Lys Val Arg Thr Val Glu Ala Ser Ala Phe Leu Gly Leu Thr 100 105 110 Pro Gln Ile Val Gln Tyr Arg Ala Ala Gly Leu Ser Arg Asp Ala Gln 115 120 125 Gly Glu Ile Val Ile Ala Asn Lys Val Ile Ala Lys Val Ser Arg Thr 130 135 140 Glu Val Ala Ile Lys Phe Met Glu Pro Ala Pro Ala Lys Met Leu Gln 145 150 155 160 Gly Leu Val Asp Glu Gly Arg Ile Thr Ala Glu Gln Met Glu Leu Ala 165 170 175 Leu Leu Val Pro Met Ala Asp Asp Ile Thr Ala Glu Ala Asp Ser Gly 180 185 190 Gly His Thr Asp Asn Arg Pro Leu Val Thr Leu Leu Pro Thr Ile Leu 195 200 205 Ala Leu Lys Glu Thr Ile Gln Ala Lys His Gln Phe Lys Thr Pro Leu 210 215 220 Arg Val Gly Ser Gly Gly Gly Ile Gly Thr Pro Asp Ala Ala Leu Ala 225 230 235 240 Ala Phe Asn Met Gly Ala Ala Tyr Ile Val Thr Gly Ser Ile Asn Gln 245 250 255 Ala Cys Ile Glu Ala Gly Ala Ser Glu His Thr Arg Lys Leu Leu Ala 260 265 270 Thr Thr Glu Met Ala Asp Val Ala Met Ala Pro Ala Ala Asp Met Phe 275 280 285 Glu Met Gly Val Lys Leu Gln Val Val Lys Arg Gly Thr Leu Phe Pro 290 295 300 Met Arg Ala Asn Lys Leu Tyr Glu Ile Tyr Thr Arg Tyr Asp Ser Ile 305 310 315 320 Glu Ala Ile Pro Ala Asp Glu Arg His Lys Leu Glu Thr Gln Val Phe 325 330 335 His Ser Thr Leu Asp Ala Ile Trp Glu Gly Thr Val Ala His Phe Asn 340 345 350 Glu Arg Asp Pro Lys Gln Ile Glu Arg Ala Gln Gly Asn Pro Lys Arg 355 360 365 Lys Met Ala Leu Ile Phe Arg Trp Tyr Leu Gly Leu Ser Ser Arg Trp 370 375 380 Ser Asn Thr Gly Glu Ala Gly Arg Glu Met Asp Tyr Gln Ile Trp Ala 385 390 395 400 Gly Pro Ala Leu Gly Ala Phe Asn Ala Trp Ala Lys Gly Ser Tyr Leu 405 410 415 Asp Asn Tyr Gln Asp Arg Arg Ala Val Asp Leu Thr Lys His Leu Met 420 425 430 His Gly Ala Ala Tyr Leu Ala Arg Val Asn 435 440 <210> 20 <211> 453 <212> PRT <213> Shewanella oneidensis MR-1 <400> 20 Met Pro Ile Ala Ile Val Gly Met Ala Ser Ile Phe Ala Asn Ser Arg 1 5 10 15 Tyr Leu Asn Lys Phe Trp Asp Leu Ile Cys Asp Lys Ile Asp Ala Ile 20 25 30 Thr Asp Val Pro Ala Ser His Trp Ala Ile Asp Asp Tyr Tyr Asp Val 35 40 45 Asp Lys Ser Lys Ala Asp Lys Ser Tyr Cys Lys Arg Gly Gly Phe Met 50 55 60 Pro Glu Val Asp Phe Asn Pro Met Glu Phe Gly Leu Pro Pro Asn Ile 65 70 75 80 Leu Glu Leu Thr Asp Ser Ser Gln Leu Leu Ser Leu Val Val Ala Lys 85 90 95 Glu Val Leu Gln Asp Ala Asn Leu Pro Asp Asp Tyr Asp Arg Asp Arg 100 105 110 Ile Gly Ile Thr Leu Gly Ile Gly Gly Gly Gln Lys Leu Ser His Ser 115 120 125 Leu Asn Ala Arg Leu Gln Tyr Pro Val Leu Lys Lys Val Phe Lys Ser 130 135 140 Ser Gly Leu Ser Asp Glu Asp Ser Glu Leu Leu Ile Lys Lys Phe Gln 145 150 155 160 Asp Gln Tyr Val His Trp Glu Glu Asn Ser Phe Pro Gly Ser Leu Gly 165 170 175 Asn Val Ile Ala Gly Arg Ile Ala Asn Arg Phe Asp Leu Gly Gly Met 180 185 190 Asn Cys Val Val Asp Ala Ala Cys Ala Gly Ser Leu Ala Ala Met Arg 195 200 205 Met Ala Leu Thr Glu Leu Thr Glu Gly Arg Ser Asp Met Met Ile Thr 210 215 220 Gly Gly Val Cys Thr Asp Asn Ser Pro Tyr Met Tyr Met Ser Phe Ser 225 230 235 240 Lys Thr Pro Ala Phe Thr Thr Asn Glu Gln Ile Gln Pro Phe Asp Ile 245 250 255 Asp Ser Lys Gly Met Met Ile Gly Glu Gly Ile Gly Met Val Ala Leu 260 265 270 Lys Arg Leu Asp Asp Ala Glu Arg Asp Gly Asp Arg Ile Tyr Ala Val 275 280 285 Ile Lys Gly Val Gly Ala Ser Ser Asp Gly Lys Phe Lys Ser Ile Tyr 290 295 300 Ala Pro Arg Pro Glu Gly Gln Ala Lys Ala Leu Glu Arg Ala Tyr Asp 305 310 315 320 Asp Ala Gly Phe Ala Pro His Thr Val Gly Leu Ile Glu Ala His Gly 325 330 335 Thr Gly Thr Ala Ala Gly Asp Val Ala Glu Phe Thr Gly Leu Ser Ser 340 345 350 Val Phe Ser Gln Asp Asn Ala Gln Leu Gln His Ile Ala Leu Gly Ser 355 360 365 Val Lys Ser Gln Val Gly His Thr Lys Ser Thr Ala Gly Thr Ala Gly 370 375 380 Val Ile Lys Ala Ala Leu Ala Leu His His Lys Val Leu Pro Pro Thr 385 390 395 400 Ile Asn Val Ser Lys Pro Asn Pro Lys Leu Glu Ile Asp Arg Ser Pro 405 410 415 Phe Tyr Leu Asn Thr Glu Ala Arg Pro Trp Ile Gln Arg Ser Asp Asp 420 425 430 Thr Pro Arg Arg Ala Gly Ile Ser Ser Phe Gly Phe Gly Gly Thr Asn 435 440 445 Phe His Leu Val Leu 450 <210> 21 <211> 303 <212> PRT <213> Shewanella oneidensis MR-1 <400> 21 Gln Thr Lys Ile Ala Ala Leu Phe Ala Gly Gln Gly Ala Gln Tyr Leu 1 5 10 15 Asn Met Gly Leu Glu Leu Ala Asn Asn Phe Pro Glu Leu Arg Arg His 20 25 30 Ile His Ala Ser Asp Lys Val Phe Ser Thr His Gly Lys Pro Ala Leu 35 40 45 Ser Ser Val Leu Tyr Pro Ile Pro Ala Phe Asp Asp Glu Ser Ile Lys 50 55 60 Ala Gln Glu Thr Ala Leu Thr Asn Thr Leu Tyr Ala Gln Ser Ala Ile 65 70 75 80 Gly Ala Leu Ser Met Ala Gln Tyr Ala Leu Phe Thr Gln Ala Gly Phe 85 90 95 Path Pro Asp Met Leu Path Gly His Ser Phe Gly Glu Leu Ser Path Leu 100 105 110 Cys Ala Ala Gly Val Ile Ser Met Asp Asp Tyr Ile Lys Leu Ala Phe 115 120 125 Glu Arg Gly Gln Ala Met Ala Gln Ser Ser Gln Asp Thr Asp Ala Gly 130 135 140 Val Met Tyr Ala Val Ile Leu Lys Gln Lys Gln Asp Ile Glu Val Ile 145 150 155 160 Asn Gly Cys Leu Ala Gln Phe Glu Gly Val Lys Val Ala Asn Tyr Asn 165 170 175 Ser Pro Thr Gln Leu Val Ile Ala Gly Ala Ser Ala Ala Thr Gln Gln 180 185 190 Ala Ala Lys Ala Ile Ser Glu Leu Gly Phe Lys Ala Ile Ala Leu Pro 195 200 205 Val Ser Gly Ala Phe His Thr Pro Leu Val Ala His Ala Gln Lys Pro 210 215 220 Phe Ser Ala Ala Ile Asp Lys Ala Gln Phe Asn Thr Pro Lys Ile Ala 225 230 235 240 Leu Tyr Ala Asn Gly Thr Gly Gln Leu His Pro Ile Asp Ala Asn Ala 245 250 255 Ile Lys Ala Ala Leu Lys Asp His Met Leu Gln Ser Val His Phe Ser 260 265 270 Glu Gln Leu Glu Ala Met Tyr Ala Ala Gly Ala Arg Val Phe Val Glu 275 280 285 Phe Gly Pro Lys Asn Ile Leu Gln Lys Leu Thr Glu Asn Thr Leu 290 295 300 <210> 22 <211> 70 <212> PRT <213> Shewanella oneidensis MR-1 <400> 22 His Ala Met Leu Ser Val Val Ala Asp Lys Thr Gly Tyr Pro Val Glu 1 5 10 15 Met Leu Glu Leu Ser Met Asp Met Glu Ala Asp Leu Gly Ile Asp Ser 20 25 30 Ile Lys Arg Val Glu Ile Leu Gly Thr Val Gln Asp Glu Leu Pro Asn 35 40 45 Leu Pro Glu Leu Ser Pro Glu Asp Leu Ala Glu Cys Arg Thr Leu Gly 50 55 60 Glu Ile Val Ala Leu Phe 65 70 <210> 23 <211> 354 <212> PRT <213> Shewanella oneidensis MR-1 <400> 23 Ser Gln Ser Glu Leu Asn Gln Ala Ala Leu Phe Gly Leu Thr Lys Thr 1 5 10 15 Leu Asn His Glu Trp Pro Gly Val Val Cys Arg Ala Leu Asp Ile Ala 20 25 30 Pro Asn Leu Asp Ala Lys Thr Val Ala Asn Ala Val Val Gln Glu Tyr 35 40 45 Tyr Leu Gln Asp Ala Pro Val Glu Val Gly Ile Asp Ser Asn Phe Asp 50 55 60 Arg Val Thr Leu Val Ala Gly Thr Ala Ala Leu Arg His Pro Pro Ala 65 70 75 80 Val Leu Ser Asn Ala Asp Lys Ile Leu Val Thr Gly Gly Ala Lys Gly 85 90 95 Val Thr Phe Glu Cys Ala Leu Ser Leu Ala Lys Arg Cys Gln Ala His 100 105 110 Phe Phe Leu Ala Gly Arg Ser Ala His Gln Val Ile Pro Ala Trp Ala 115 120 125 Glu Gly Lys Lys Ser Asn Glu Leu Lys Ala Ala Ala Ile Ala His Leu 130 135 140 Gln Ser Leu Gly Asp Lys Pro Thr Pro Lys Gln Val Asp Ala Leu Val 145 150 155 160 Trp Pro Val Gln Ser Ser Leu Glu Ile Ser His Ala Leu Ala Ala Phe 165 170 175 Asp Ala Ile Gly Ala Ser Ala Glu Tyr Leu Ser Val Asp Val Asn Asp 180 185 190 Pro Ala Ala Ile Ala Ser Thr Ile Ala Pro Ile Asn Ala Leu Ser Pro 195 200 205 Ile Thr Gly Ile Ile His Gly Ala Gly Val Leu Ala Asp Lys His Ile 210 215 220 Gln Asp Lys Thr Leu Asn Glu Phe Glu Arg Val Tyr Gly Thr Lys Val 225 230 235 240 Thr Gly Leu Asn Asn Leu Leu Ser Thr Leu Asp Leu Ser Gln Val Lys 245 250 255 Leu Ile Ala Leu Phe Ser Ala Ala Gly Phe Tyr Gly Asn Thr Gly 260 265 270 Gln Ser Asp Tyr Ala Met Ser Asn Asp Ile Leu Asn Lys Ala Ala Leu 275 280 285 Gln Leu Ala Gln Gln Leu Pro Gln Ala Lys Val Met Ser Phe Asp Trp 290 295 300 Gly Pro Trp Asp Gly Gly Met Val Asn Pro Ala Leu Lys Lys Met Phe 305 310 315 320 Ile Asp Arg Gly Val Tyr Val Ile Pro Leu Lys Ala Gly Ala Glu Leu 325 330 335 Phe Ala Ser Gln Leu Leu Ser Asp Thr Gly Ala Gln Leu Leu Val Gly 340 345 350 Thr Asp < <210> 24 <211> 275 <212> PRT <213> Shewanella oneidensis MR-1 <400> 24 Pro Gln Ser Ile Arg Val Met Arg Ser Leu Asp Pro Lys Arg Met Ser 1 5 10 15 Phe Ile Glu Asp His Cys Ile Asn Gly His Ala Val Leu Pro Thr Val 20 25 30 Cys Ala Ile Asp Trp Met Arg Glu Ala Ala Lys Ala His Leu Gly Thr 35 40 45 Ala Val Ser Val Ser Asp Tyr Arg Leu Leu Lys Gly Val Ile Phe Asp 50 55 60 Glu Ala Leu Leu Ala Arg Asn Ala Pro Ile Glu Leu Glu Leu Met Leu 65 70 75 80 Thr Pro Leu Ala Asp Ala Ala Gln Gln Ser Thr Glu Ala Leu Ala Ala 85 90 95 Leu Ile Ser Phe Glu Gly Arg Pro Gln Tyr Gln Ala Val Leu Val Ala 100 105 110 Gln Thr Asp Asp Met Pro Asp Ala Gln Arg Phe Glu Val Gly Glu Leu 115 120 125 His Ser Leu Ile Gln Glu Met Ala Gln Gln Pro Ala Ile Ala Asn Arg 130 135 140 Glu Ser Leu Tyr Ser Asp Gly Thr Leu Phe His Gly Pro Arg Leu Gln 145 150 155 160 Gly Ile Ser Glu Val Leu Thr Phe Asp Asp Gln His Leu Met Ala Lys 165 170 175 Val Glu Leu Pro Gln Val Ala Leu Asp Asp Cys Gly Lys Phe Ala Pro 180 185 190 Lys Leu Glu Asp Lys Gly Thr Gln Pro Phe Ala Glu Asp Leu Leu Leu 195 200 205 Gln Ala Met Leu Val Trp Ala Arg Leu Lys Tyr Gln Ala Ala Ser Leu 210 215 220 Pro Ser Thr Ile Gly Glu Phe Val Ser Tyr Ala Pro Leu Ser Phe Gly 225 230 235 240 Glu Lys Ala Val Leu Val Leu Asp Val Leu Lys His Ser Ser Arg Ser 245 250 255 Leu Glu Ala Asn Ile Ala Leu Tyr His Gln Asp Gly Arg Leu Ser Cys 260 265 270 Glu Met Lys 275 <210> 25 <211> 526 <212> PRT <213> Shewanella oneidensis MR-1 <400> 25 Tyr Trp Phe Ser Lys Pro His Gln Ala Arg Val Leu Ser Leu Asn Leu 1 5 10 15 Phe Asp Lys Ala Pro Gln Ala Gln Thr Ala Gln Ser Leu Ile Leu Thr 20 25 30 Gln Gly Thr Gly Leu Ile Ala Gln Pro Leu Leu Asn Ala Asn Arg Leu 35 40 45 Phe Ile Pro Ile Ser Gly Asn Glu Phe Glu Ser Leu Thr Leu Lys Leu 50 55 60 Leu Gln Leu Ile Asp Ser Leu Thr Leu Ser Leu Asn Gln Pro Asp Thr 65 70 75 80 Asp Trp Leu Ser Ser Gln Gly Ser Asp Trp Phe Lys Arg Tyr Gln Ala 85 90 95 Lys Asp Glu Leu Ala Leu Val Leu Met Ala Gly Ser Leu Glu Glu Leu 100 105 110 Met Gln Glu Ala Lys Ala Met Gln Thr Phe Ile Glu Lys Ala Arg Leu 115 120 125 Thr Ile Glu Ser Ser Ala Ser Lys His Ser Ala Ser Lys Pro Ser Ala 130 135 140 Ser Thr Ser Leu Val Phe Lys Thr Pro Ala Gly Ser Tyr Phe Ala Ala 145 150 155 160 Ser Pro Leu Gly Asp Lys Gly Leu Thr Phe Val Tyr Pro Gly Val Gly 165 170 175 Thr Val Tyr Pro Asn Met Phe Ser Asp Leu His Ser Tyr Phe Pro Glu 180 185 190 Leu Tyr Arg Glu Leu Glu Arg Glu Gly Asp Leu Ala Ala Met Leu Gln 195 200 205 Ala Glu Thr Ile Tyr Gln Asp Ala Ala Tyr Ala Lys Thr Ala Val Asn 210 215 220 Val Ser Val Lys Asp Thr Ala Glu Met Ser Leu Ser Gln Leu Ala Ile 225 230 235 240 Ser Gly Val Gly Ala Ser Tyr Leu Phe Ser Lys Leu Leu Thr Gly Val 245 250 255 Phe Thr Ile Gln Pro Arg Leu Ala Leu Gly Tyr Ser Met Gly Glu Ala 260 265 270 Ala Met Trp Ala Ser Leu Ala Ile Trp Gln Thr Pro His Ser Leu Ile 275 280 285 Asp Ala Thr Gln Gly Ser Ala Ile Phe Asn His Glu Ile Ser Gly Lys 290 295 300 Leu Gln Ala Val Arg Arg Asp Trp Gln Leu Asn Glu Asp Ala Pro Leu 305 310 315 320 Ala Trp Asn Ser Phe Leu Val Arg Ala Thr Ser Thr Glu Ile Asn Pro 325 330 335 Leu Leu Ala Asp Phe Pro Arg Val Tyr Leu Ala Ile Glu Gln Gly Asp 340 345 350 Thr Cys Ile Leu Ala Gly Cys Glu Ala Ser Cys Leu Gln Leu Leu Ala 355 360 365 Arg Leu Asn Lys Arg Gly Ile Ala Ser Asn Lys Val Thr Ala Met His 370 375 380 Thr Ala Pro Ser Gln Ser Gln Arg Asn Ala Ile Gln Gly Phe Tyr Thr 385 390 395 400 Leu Gly Leu Lys Ala Thr Ala Cys Glu Thr Gln Val Arg Phe Ile Ser 405 410 415 Ala Ala Gln His Ser Pro Val Asn Ile Asp Ser Met Ser Ile Ala Lys 420 425 430 Ser Ile Ala Asp Thr Phe Cys Ala Pro Leu Asn Phe Thr Ala Leu Ile 435 440 445 Asn Thr Ala Tyr Asn Gln Gly Ala Arg Leu Phe Val Glu Val Gly Ala 450 455 460 Asp Arg Gln Thr Ser Thr Leu Ile Asp Lys Ile Ser Arg Gln Leu Glu 465 470 475 480 Leu Gly Ala Asp Gly Val Gln Glu Pro Ile Leu Ala Met Ala Cys Asn 485 490 495 Ala Lys Gly Ser Asp Thr Ile Val Ser Leu Leu Lys Cys Leu Ala Gln 500 505 510 Leu Ile Ser His Arg Val Pro Leu Ser Leu Ala Ala Leu Met 515 520 525 <210> 26 <211> 451 <212> PRT <213> Shewanella oneidensis MR-1 <400> 26 Ile Ala Ile Val Gly Leu Ala Val Gln Tyr Pro Asp Ala Asp Thr Pro 1 5 10 15 Glu Gln Phe Trp Gln Asn Leu Leu Asp Lys Lys Asp Ser Arg Ser Gln 20 25 30 Ile Asp Ala Ala Lys Leu Asn Ala Asn Pro Ala Asp Tyr Gln Gly Ile 35 40 45 Gln Gly Gln Ala Asp Arg Phe Tyr Cys Asp Lys Gly Gly Tyr Ile Arg 50 55 60 Asn Phe Arg Phe Asp Pro Gln Gly Tyr Gln Leu Leu Pro Ala Thr Phe 65 70 75 80 Ala Gly Leu Asp Glu Ser Phe Leu Trp Ala Leu Asp Cys Ser Lys Lys 85 90 95 Ala Leu Leu Asn Ala Gly Val Asp Leu Thr Ala Pro Leu Leu Glu Arg 100 105 110 Thr Gly Ile Val Met Gly Thr Leu Ser Phe Pro Thr Ala Arg Ser Asn 115 120 125 Glu Leu Phe Leu Pro Ile Tyr His Gln Ala Val Glu Lys Ala Leu Lys 130 135 140 Thr Lys Leu Asn Gln Pro Gln Phe Ala Leu Ala Pro Phe Ala Asn Ala 145 150 155 160 Ser Ile Ala Gly Ser Gln Leu Ala Ala Asn Gly Val Ile Ala His Thr 165 170 175 Ala Ser Lys Leu Leu Ser Asp Ala Leu Gly Leu Gly Gly Ala Gln Leu 180 185 190 Ser Leu Asp Ala Ala Cys Ala Ser Ser Val Tyr Ala Leu Lys Leu Ala 195 200 205 Cys Asp Tyr Leu Thr Thr Gly Lys Ala Asp Met Met Leu Ala Gly Ala 210 215 220 Val Ser Gly Ala Asp Pro Phe Phe Ile Asn Met Gly Phe Ser Ile Phe 225 230 235 240 His Ala Tyr Pro Asp His Gly Ile Ser Ala Pro Phe Asp Ser Asn Ser 245 250 255 Lys Gly Leu Phe Ala Gly Glu Gly Ala Gly Val Leu Val Leu Lys Arg 260 265 270 Leu Glu Asp Ala Glu Arg Asp Gly Asp Asn Ile Tyr Ala Val Val Ser 275 280 285 Gly Ile Gly Leu Ser Asn Asp Gly Lys Gly Gln Phe Val Leu Ser Pro 290 295 300 Asn Ser Lys Gly Gln Val Gln Ala Phe Glu Arg Ala Tyr Ala Ala Ala 305 310 315 320 Asn Thr His Pro Ser Asn Ile Glu Val Ile Glu Cys His Ala Thr Gly 325 330 335 Thr Pro Leu Gly Asp Lys Val Glu Leu Thr Ser Met Glu Arg Phe Phe 340 345 350 Glu Asp Lys Leu Asp Gly Thr Lys Ala Pro Leu Ile Gly Ser Ala Lys 355 360 365 Ser Asn Leu Gly His Leu Leu Thr Ala Ala Gly Met Pro Gly Ile Met 370 375 380 Lys Met Ile Phe Ala Met Arg Ser Gly His Leu Pro Pro Ser Ile Asn 385 390 395 400 Leu Thr Ala Pro Ile Ser Ser Pro Lys Gly Leu Phe Ser Val Asn Asn '405 410 415 Leu Pro Thr Gln Arg Gln Ala Trp Pro Asp Lys Ala Gly Asn Asp Arg 420 425 430 Arg His Ala Gly Val Ser Val Phe Gly Phe Gly Gly Cys Asn Ala His 435 440 445 Leu Leu Leu 450 <210> 27 <211> 288 <212> PRT <213> Shewanella oneidensis MR-1 <400> 27 It should be noted that there may be some minor errors in the original text. For example, in line 23, it should be '405' instead of '405 '. This translation is based on the original text as accurately as possible while maintaining the format.Val Ile Gly Met Ala Ser His Phe Gly Pro Leu Ala Ser Ile Asn Ala 1 5 10 15 Leu Asp Lys Ala Leu Ile Ala Gln Thr Asp Ala Phe Ile Pro Leu Pro 20 25 30 Pro Lys Arg Trp Lys Gly Leu Asp Lys His Pro Asp Ile Leu Gln Gln 35 40 45 Phe Gly Leu Asn Arg Ala Pro Lys Gly Ala Tyr Ile Glu Gln Phe Asp 50 55 60 Phe Asp Phe Leu Arg Phe Lys Val Pro Pro Asn Glu Asp Asp Arg Leu 65 70 75 80 Ile Ser Gln Gln Leu Leu Leu Ile Lys Val Ala Asp Glu Ala Ile Arg 85 90 95 Asp Ala Lys Leu Thr Ala Gly Ser Lys Val Ala Val Leu Val Ala Met 100 105 110 Glu Thr Glu Leu Glu Leu His Gln Phe Arg Gly Arg Val Asn Leu His 115 120 125 Thr Gln Leu Ala Asp Ser Leu Lys Lys Gln Gly Val His Leu Ser Asn 130 135 140 Asp Glu Tyr Leu Ala Leu Glu Ala Ile Ala Met Asp Ser Val Leu Asp 145 150 155 160 Ala Ala Lys Leu Asn Gln Tyr Thr Ser Phe Ile Gly Asn Ile Met Ala 165 170 175 Ser Arg Ile Ala Ser Leu Trp Asp Phe Asn Gly Pro Ala Phe Thr Ile 180 185 190 Ser Ala Ala Glu Gln Ser Val Ala Arg Cys Ile Asp Val Ala Gln Asn 195 200 205 Leu Leu Ser Lys Glu Ala Leu Asp Gly Val Val Ile Ala Ala Val Asp 210 215 220 Leu Ser Gly Ser Val Glu Gln Val Ile Leu Lys Asn Ala Gln Val Ala 225 230 235 240 Val Asp Leu Asp Ala Asn Ser Ala Asn Pro Gln Trp Lys Val Gly Glu 245 250 255 Gly Ala Gly Ala Ile Val Leu Thr Asn Gln Gln Ala Ser Asn Ser Gln 260 265 270 Gln Ala Gly Tyr Gly Gln Ile Arg Gly Gln Ala Phe Gly Thr Asn His 275 280 285 <210> 28 <211> 147 <212> PRT <213> Shewanella oneidensis MR-1 <400> 28 Lys Phe Leu Met Ile Glu Gln Val Ser Lys Leu Glu Val His Gly Gly 1 5 10 15 Ala Trp Gly Leu Gly Leu Ile Glu Gly His Lys Gln Leu Ala Pro Asp 20 25 30 His Trp Tyr Phe Pro Cys His Phe Lys Gly Asp Gln Val Met Ala Gly 35 40 45 Ser Leu Met Ala Glu Gly Cys Gly Gln Leu Leu Gln Phe Phe Met Leu 50 55 60 His Ile Gly Met His Ala Asn Thr Gln Ala Gly Gly Val Thr Asn Gly 65 70 75 80 Arg Phe Gln Pro Leu Glu Asn Ala Ser Gln Lys Val Arg Cys Arg Gly 85 90 95 Gln Val Leu Pro Gln Ser Gly Thr Leu Thr Tyr Arg Met Glu Val Thr 100 105 110 Glu Ile Gly Met Ser Pro Arg Pro Tyr Ala Lys Ala Asn Ile Asp Ile 115 120 125 Leu Leu Asn Gly Lys Val Val Val Asp Phe Gln Asn Leu Gly Val Met 130 135 140 Ile Lys Glu 145 <210> 29 <211> 148 <212> PRT <213> Shewanella oneidensis MR-1 <400> 29 Tyr Arg Leu Ala Gly Gly Gln Leu Asn Phe Ile Asp Lys Ala Glu Ile 1 5 10 15 Val Lys Thr Gly Gly Lys Lys Gly Leu Gly Tyr Leu Tyr Ala Glu Arg 20 25 30 Thr Ile Asp Pro Ser Asp Trp Phe Phe Gln Phe His Phe His Gln Asp 35 40 45 Pro Val Met Pro Gly Ser Leu Gly Val Glu Ala Ile Ile Glu Leu Leu 50 55 60 Gln Thr Tyr Ala Ile Asp Gln Asp Leu Gly Ala Gly Phe Asn Asn Pro 65 70 75 80 Lys Phe Gly Gln Ile Leu Ser Glu Ile Lys Trp Lys Tyr Arg Gly Gln 85 90 95 Ile Asn Pro Leu Asn Lys Gln Met Ser Leu Asp Val His Ile Thr Ser 100 105 110 Ile Glu Asp Lys Asp Gly Lys Arg Ile Ile Lys Gly Asp Ala Asn Leu 115 120 125 Ser Lys Asp Gly Leu Arg Ile Tyr Glu Val Thr Asp Ile Ala Ile Cys 130 135 140 Ile Glu Glu Ala 145 <210> 30 <211> 442 <212> PRT <213> Shewanella oneidensis MR-1 <400> 30 Leu Gly Thr Gln Ser Leu Gly Asp Ser Asn Phe Arg Arg Val His Gly 1 5 10 15 Val Lys Tyr Ala Tyr Tyr Ala Gly Ala Met Ala Asn Gly Ile Ala Ser 20 25 30 Glu Glu Leu Val Ile Leu Gly Gln Ala Gly Ile Leu Cys Ser Phe 35 40 45 Gly Ala Ala Gly Leu Ile Pro Ser Arg Val Glu Ala Ala Ile Lys Arg 50 55 60 Ile Gln Ala Ala Leu Pro Asn Gly Pro Tyr Ala Phe Asn Leu Ile His 65 70 75 80 Ser Pro Ser Glu Gln Ala Leu Glu Arg Gly Ser Val Glu Leu Phe Leu 85 90 95 Lys His Gln Val Arg Thr Val Glu Ala Ser Ala Phe Leu Gly Leu Thr 100 105 110 Pro Gln Ile Val Tyr Tyr Arg Ala Ala Gly Leu Ser Arg Asp Ala Ser 115 120 125 Gly Glu Ile Val Ile Gly Asn Lys Val Ile Ala Lys Ile Ser Arg Thr 130 135 140 Glu Val Ala Thr Lys Phe Met Glu Pro Ala Pro Val Lys Ile Leu Gln 145 150 155 160 Gln Leu Val Asn Glu Gly Leu Ile Ser Glu Asp Gln Met Leu Met Ala 165 170 175 Gln Ser Val Pro Met Ala Asp Asp Ile Thr Ala Glu Ala Asp Ser Gly 180 185 190 Gly His Thr Asp Asn Arg Pro Leu Val Thr Leu Leu Pro Thr Ile Leu 195 200 205 Ala Leu Lys Asp Thr Ile Gln Ala Lys Tyr Gln Tyr Lys Thr Pro Ile 210 215 220 Arg Val Gly Ala Gly Gly Gly Ile Gly Thr Pro Asp Ala Ala Leu Ala 225 230 235 240 Thr Phe Asn Met Gly Ala Ala Tyr Ile Val Thr Gly Ser Ile Asn Gln 245 250 255 Ala Cys Val Glu Ala Gly Ala Ser Glu His Thr Arg Lys Leu Leu Ala 260 265 270 Thr Thr Glu Met Ala Asp Val Thr Met Ala Pro Ala Ala Asp Met Phe 275 280 285 Glu Met Gly Val Lys Leu Gln Val Val Lys Arg Gly Thr Leu Phe Pro 290 295 300 Met Arg Ala Asn Lys Leu Tyr Glu Ile Tyr Thr Arg Tyr Asp Ser Ile 305 310 315 320 Glu Ala Ile Pro Ala Glu Glu Arg Gln Lys Leu Glu Glu Gln Val Phe 325 330 335 Arg Ala Ser Leu Asp Glu Ile Trp Ala Gly Thr Val Ala His Phe Asn 340 345 350 Glu Arg Asp Pro Lys Gln Ile Glu Arg Ala Leu Asp Asn Pro Lys Arg 355 360 365 Lys Met Ala Leu Ile Phe Arg Trp Tyr Leu Gly Leu Ser Ser Arg Trp 370 375 380 Ser Asn Thr Gly Glu Val Gly Arg Glu Met Asp Tyr Gln Ile Trp Ala 385 390 395 400 Gly Pro Ala Leu Gly Ala Phe Asn Ala Trp Ala Lys Gly Ser Tyr Leu 405 410 415 Asp Asp Tyr Arg Glu Arg Asn Ala Val Asp Leu Ala Lys His Leu Met 420 425 430 Gln Gly Ala Ala Tyr Gln Ala Arg Ile Asn 435 440 <210> 31 <211> 408 <212> PRT <213> Schizochytorium sp. <400> 31 Asp Thr Arg Ile Ala Ile Ile Gly Met Ser Ala Ile Leu Pro Cys Gly 1 5 10 15 Thr Thr Val Arg Glu Ser Trp Glu Thr Ile Arg Ala Gly Ile Asp Cys 20 25 30 Leu Ser Asp Leu Pro Glu Asp Arg Val Asp Val Thr Ala Tyr Phe Asp 35 40 45 Pro Val Lys Thr Thr Lys Asp Lys Ile Tyr Cys Lys Arg Gly Gly Phe 50 55 60 Ile Pro Glu Tyr Asp Phe Asp Ala Arg Glu Phe Gly Leu Asn Met Phe 65 70 75 80 Gln Met Glu Asp Ser Asp Ala Asn Gln Thr Ile Ser Leu Leu Lys Val 85 90 95 Lys Glu Ala Leu Gln Asp Ala Gly Ile Asp Ala Leu Gly Lys Glu Lys 100 105 110 Lys Asn Ile Gly Cys Val Leu Gly Ile Gly Gly Gly Gln Lys Ser Ser 115 120 125 His Glu Phe Tyr Ser Arg Leu Asn Tyr Val Val Val Glu Lys Val Leu 130 135 140 Arg Lys Met Gly Met Pro Glu Glu Asp Val Lys Val Ala Val Glu Lys 145 150 155 160 Tyr Lys Ala Asn Phe Pro Glu Trp Arg Leu Asp Ser Phe Pro Gly Phe 165 170 175 Leu Gly Asn Val Thr Ala Gly Arg Cys Thr Asn Thr Phe Asn Leu Asp 180 185 190 Gly Met Asn Cys Val Val Asp Ala Ala Cys Ala Ser Ser Leu Ile Ala 195 200 205 Val Lys Val Ala Ile Asp Glu Leu Leu Tyr Gly Asp Cys Asp Met Met 210 215 220 Val Thr Gly Ala Thr Cys Thr Asp Asn Ser Ile Gly Met Tyr Met Ala 225 230 235 240 Phe Ser Lys Thr Pro Val Phe Ser Thr Asp Pro Ser Val Arg Ala Tyr 245 250 255 Asp Glu Lys Thr Lys Gly Met Leu Ile Gly Glu Gly Ser Ala Met Leu 260 265 270 Val Leu Lys Arg Tyr Ala Asp Ala Val Arg Asp Gly Asp Glu Ile His 275 280 285 Ala Val Ile Arg Gly Cys Ala Ser Ser Ser Asp Gly Lys Ala Ala Gly 290 295 300 Ile Tyr Thr Pro Thr Ile Ser Gly Gln Glu Glu Ala Leu Arg Arg Ala 305 310 315 320 Tyr Asn Arg Ala Cys Val Asp Pro Ala Thr Val Thr Leu Val Glu Gly 325 330 335 His Gly Thr Gly Thr Pro Val Gly Asp Arg Ile Glu Leu Thr Ala Leu 340 345 350 Arg Asn Leu Phe Asp Lys Ala Tyr Gly Glu Gly Asn Thr Glu Lys Val 355 360 365 Ala Val Gly Ser Ile Lys Ser Ser Ile Gly His Leu Lys Ala Val Ala 370 375 380 Gly Leu Ala Gly Met Ile Lys Val Ile Met Ala Leu Lys His Lys Thr 385 390 395 400 Leu Pro Gly Thr Ile Asn Val Asp 405 <210> 32 <211> 331 <212> PRT <213> Schizochytorium sp. <400> 32 Ala Leu Phe Ser Gly Gln Gly Ala Gln Tyr Thr His Met Phe Ser Glu 1 5 10 15 Val Ala Met Asn Trp Pro Gln Phe Arg Gln Ser Ile Ala Ala Met Asp 20 25 30 Ala Ala Gln Ser Lys Val Ala Gly Ser Asp Lys Asp Phe Glu Arg Val 35 40 45 Ser Gln Val Leu Tyr Pro Arg Lys Pro Tyr Glu Arg Glu Pro Glu Gln 50 55 60 Asp His Lys Lys Ile Ser Leu Thr Ala Tyr Ser Gln Pro Ser Thr Leu 65 70 75 80 Ala Cys Ala Leu Gly Ala Phe Glu Ile Phe Lys Glu Ala Gly Phe Thr 85 90 95 Pro Asp Phe Ala Ala Gly His Ser Leu Gly Glu Phe Ala Ala Leu Tyr 100 105 110 Ala Ala Gly Cys Val Asp Arg Asp Glu Leu Phe Glu Leu Val Cys Arg 115 120 125 Arg Ala Arg Ile Met Gly Gly Lys Asp Ala Pro Ala Thr Pro Lys Gly 130 135 140 Cys Met Ala Ala Val Ile Gly Pro Asn Ala Glu Asn Ile Lys Val Gln 145 150 155 160 Ala Ala Asn Val Trp Leu Gly Asn Ser Asn Ser Pro Ser Gln Thr Val 165 170 175 Ile Thr Gly Ser Val Glu Gly Ile Gln Ala Glu Ser Ala Arg Leu Gln 180 185 190 Lys Glu Gly Phe Arg Val Val Pro Leu Ala Cys Glu Ser Ala Phe His 195 200 205 Ser Pro Gln Met Glu Asn Ala Ser Ser Ala Phe Lys Asp Val Ile Ser 210 215 220 Lys Val Ser Phe Arg Thr Pro Lys Ala Glu Thr Lys Leu Phe Ser Asn 225 230 235 240 Val Ser Gly Glu Thr Tyr Pro Thr Asp Ala Arg Glu Met Leu Thr Gln 245 250 255 His Met Thr Ser Ser Val Lys Phe Leu Thr Gln Val Arg Asn Met His 260 265 270 Gln Ala Gly Ala Arg Ile Phe Val Glu Phe Gly Pro Lys Gln Val Leu 275 280 285 Ser Lys Leu Val Ser Glu Thr Leu Lys Asp Asp Pro Ser Val Val Thr 290 295 300 Val Ser Val Asn Pro Ala Ser Gly Thr Asp Ser Asp Ile Gln Leu Arg 305 310 315 320 Asp Ala Ala Val Gln Leu Val Val Ala Gly Val 325 330 <210> 33 <211> 66 <212> PRT <213> Schizochytorium sp. <400> 33 Val Met Glu Val Leu Ala Ala Lys Thr Gly Tyr Glu Thr Asp Met Ile 1 5 10 15 Glu Ser Asp Met Glu Leu Glu Thr Glu Leu Gly Ile Asp Ser Ile Lys 20 25 30 Arg Val Glu Ile Leu Ser Glu Val Gln Ala Met Leu Asn Val Glu Ala 35 40 45[[ID=1s]] Lys Asp Val Asp Ala Leu Ser Arg Thr Arg Thr Val Gly Glu Val Val 50 55 60 Asn Ala 65 <210> 34 <211> 230 <212> PRT <i13> Schizochytorium sp. <400> 34 Val Leu Leu Val Ser Gly Gly Ala Arg Gly Ile Thr Pro Leu Cys Ile[[ID=i5]] 1 5 10 15 Arg Glu Ile Thr Arg Gln Ile Ala Gly Gly Lys Tyr Ile Leu Leu Gly 20 25 30 Arg Ser Lys Val Ser Ala Ser Glu Pro Ala Trp Cys Ala Gly Ile Thr 35 40 45 Asp Glu Lys Ala Val Gln Lys Ala Ala Thr Gln Glu Leu Lys Arg Ala [[ID=4s]]So 55 60 Phe Ser Ala Gly Glu Gly Pro Lys Pro Thr Pro Arg Ala Val Thr Lys 65 70 75 80 Leu Val Gly Ser Val Leu Gly Ala Arg Glu Val Arg Ser Ser Ile Ala 85 90 95 Ala Ile Glu Ala Leu Gly Gly Lys Ala Ile Tyr Ser Ser Cys Asp Val 100 105 110 Asn Ser Ala Ala Asp Val Ala Lys Ala Val Arg Asp Ala Glu Ser Gln 115 120 125 Leu Gly Ala Arg Val Ser Gly Ile Val His Ala Ser Gly Val Leu Arg 130 135 140 Asp Arg Leu Ile Glu Lys Lys Leu Pro Asp Glu Phe Asp Ala Val Phe 145 150 155 160 Gly Thr Lys Val Thr Gly Leu Glu Asn Leu Leu Ala Ala Val Asp Arg 165 170 175 Ala Asn Leu Lys His Met Val Leu Phe Ser Ser Leu Ala Gly Phe His 180 185 190 Gly Asn Val Gly Gln Ser Asp Tyr Ala Met Ala Asn Glu Ala Leu Asn 195 200 205 Lys Met Gly Leu Glu Leu Ala Lys Asp Val Ser Val Lys Ser Ile Cys 210 215 220 Phe Gly Pro Trp Asp Gly 225 230 <210> 35 <211> 282 <212> PRT <213> Schizochytorium sp. <400> 35 Ala Glu Ile Leu Val Gly Asn Trp Arg Thr Pro Ser Lys Lys Val Gly 1 5 10 15 Ser Asp Thr Ile Thr Leu His Arg Lys Ile Ser Ala Lys Ser Asn Pro 20 25 30 Phe Leu Glu Asp His Val Ile Gln Gly Arg Arg Val Leu Pro Met Thr 35 40 45 Leu Ala Ile Gly Ser Leu Ala Glu Thr Cys Leu Gly Leu Phe Pro Gly 50 55 60 Tyr Ser Leu Trp Ala Ile Asp Asp Ala Gln Leu Phe Lys Gly Val Thr 65 70 75 80 Val Asp Gly Asp Val Asn Cys Glu Val Thr Leu Thr Pro Ser Thr Ala 85 90 95 Pro Ser Gly Arg Val Asn Val Gln Ala Thr Leu Lys Thr Phe Ser Ser 100 105 110 Gly Lys Leu Val Pro Ala Tyr Arg Ala Val Ile Val Leu Ser Asn Gln 115 120 125 Gly Ala Pro Pro Ala Asn Ala Thr Met Gln Pro Pro Ser Leu Asp Ala 130 135 140 Asp Pro Ala Leu Gln Gly Ser Val Tyr Asp Gly Lys Thr Leu Phe His 145 150 155 160 Gly Pro Ala Phe Arg Gly Ile Asp Asp Val Leu Ser Cys Thr Lys Ser 165 170 175 Gln Leu Val Ala Lys Cys Ser Ala Val Pro Gly Ser Asp Ala Ala Arg 180 185 190 Gly Glu Phe Ala Thr Asp Thr Asp Ala His Asp Pro Phe Val Asn Asp 195 200 205 Leu Ala Phe Gln Ala Met Leu Val Trp Val Arg Arg Thr Leu Gly Gln 210 215 220 Ala Ala Leu Pro Asn Ser Ile Gln Arg Ile Val Gln His Arg Pro Val 225 230 235 240 Pro Gln Asp Lys Pro Phe Tyr Ile Thr Leu Arg Ser Asn Gln Ser Gly 245 250 255 Gly His Ser Gln His Lys His Ala Leu Gln Phe His Asn Glu Gln Gly 260 265 270 Asp Leu Phe Ile Asp Val Gln Ala Ser Val 275 280 <210> 36 <211> 425 <212> PRT <213> Schizochytorium sp. <400> 36 Ile Ala Val Val Gly Met Ala Val Gln Tyr Ala Gly Cys Lys Thr Lys 1 5 10 15 Asp Glu Phe Trp Glu Val Leu Met Asn Gly Lys Val Glu Ser Lys Val 20 25 30 Ile Ser Asp Lys Arg Leu Gly Ser Asn Tyr Arg Ala Glu His Tyr Lys 35 40 45 Ala Glu Arg Ser Lys Tyr Ala Asp Thr Phe Cys Asn Glu Thr Tyr Gly 50 55 60 Thr Leu Asp Glu Asn Glu Ile Asp Asn Glu His Glu Leu Leu Leu Asn 65 70 75 80 Leu Ala Lys Gln Ala Leu Ala Glu Thr Ser Val Lys Asp Ser Thr Arg 85 90 95 Cys Gly Ile Val Ser Gly Cys Leu Ser Phe Pro Met Asp Asn Leu Gln 100 105 110 Gly Glu Leu Leu Asn Val Tyr Gln Asn His Val Glu Lys Lys Leu Gly 115 120 125 Ala Arg Val Phe Lys Asp Ala Ser His Trp Ser Glu Arg Glu Gln Ser 130 135 140 Asn Lys Pro Glu Ala Gly Asp Arg Arg Ile Phe Met Asp Pro Ala Ser 145 150 155 160 Phe Val Ala Glu Glu Leu Asn Leu Gly Ala Leu His Tyr Ser Val Asp 165 170 175 Ala Ala Cys Ala Thr Ala Leu Tyr Val Leu Arg Leu Ala Gln Asp His 180 185 190 Leu Val Ser Gly Ala Ala Asp Val Met Leu Cys Gly Ala Thr Cys Leu 195 200 205 Pro Glu Pro Phe Phe Ile Leu Ser Gly Phe Ser Thr Phe Gln Ala Met 210 215 220 Pro Val Gly Thr Gly Gln Asn Val Ser Met Pro Leu His Lys Asp Ser 225 230 235 240 Gln Gly Leu Thr Pro Gly Glu Gly Gly Ser Ile Met Val Leu Lys Arg 245 250 255 Leu Asp Asp Ala Ile Arg Asp Gly Asp His Ile Tyr Gly Thr Leu Leu 260 265 270 Gly Ala Asn Val Ser Asn Ser Gly Thr Gly Leu Pro Leu Lys Pro Leu 275 280 285 Leu Pro Ser Glu Lys Lys Cys Leu Met Asp Thr Tyr Thr Arg Ile Asn 290 295 300 Val His Pro His Lys Ile Gln Tyr Val Glu Cys His Ala Thr Gly Thr 305 310 315 320 Pro Gln Gly Asp Arg Val Glu Ile Asp Ala Val Lys Ala Cys Phe Glu 325 330 335 Gly Lys Val Pro Arg Phe Gly Thr Thr Lys Gly Asn Phe Gly His Thr 340 345 350 Leu Val Ala Ala Gly Phe Ala Gly Met Cys Lys Val Leu Leu Ser Met 355 360 365 Lys His Gly Ile Ile Pro Pro Thr Pro Gly Ile Asp Asp Glu Thr Lys 370 375 380 Met Asp Pro Leu Val Val Ser Gly Glu Ala Ile Pro Trp Pro Glu Thr 385 390 395 400 Asn Gly Glu Pro Lys Arg Ala Gly Leu Ser Ala Phe Gly Phe Gly Gly 405 410 415 Thr Asn Ala His Ala Val Phe Glu Glu 420 425 <210> 37 <211> 425 <212> PRT <213> Schizochytorium sp. <400> 37 Met Arg Ile Ala Ile Thr Gly Met Asp Ala Thr Phe Gly Ala Leu Lys 1 5 10 15 Gly Leu Asp Ala Phe Glu Arg Ala Ile Tyr Thr Gly Ala His Gly Ala 20 25 30 Ile Pro Leu Pro Glu Lys Arg Trp Arg Phe Leu Gly Lys Asp Lys Asp 35 40 45 Phe Leu Asp Leu Cys Gly Val Lys Ala Thr Pro His Gly Cys Tyr Ile 50 55 60 Glu Asp Val Glu Val Asp Phe Gln Arg Leu Arg Thr Pro Met Thr Pro 65 70 75 80 Glu Asp Met Leu Leu Pro Gln Gln Leu Leu Ala Val Thr Thr Ile Asp 85 90 95 Arg Ala Ile Leu Asp Ser Gly Met Lys Lys Gly Gly Asn Val Ala Val 100 105 110 Phe Val Gly Leu Gly Thr Asp Leu Glu Leu Tyr Arg His Arg Ala Arg 115 120 125 Val Ala Leu Lys Glu Arg Val Arg Pro Glu Ala Ser Lys Lys Leu Asn 130 135 140 Asp Met Met Gln Tyr Ile Asn Asp Cys Gly Thr Ser Thr Ser Tyr Thr 145 150 155 160 Ser Tyr Ile Gly Asn Leu Val Ala Thr Arg Val Ser Ser Gln Trp Gly 165 170 175 Phe Thr Gly Pro Ser Phe Thr Ile Thr Glu Gly Asn Asn Ser Val Tyr 180 185 190 Arg Cys Ala Glu Leu Gly Lys Tyr Leu Leu Glu Thr Gly Glu Val Asp 195 200 205 Gly Val Val Val Ala Gly Val Asp Leu Cys Gly Ser Ala Glu Asn Leu 210 215 220 Tyr Val Lys Ser Arg Arg Phe Lys Val Ser Thr Ser Asp Thr Pro Arg 225 230 235 240 Ala Ser Phe Asp Ala Ala Ala Asp Gly Tyr Phe Val Gly Glu Gly Cys 245 250 255 Gly Ala Phe Val Leu Lys Arg Glu Thr Ser Cys Thr Lys Asp Asp Arg 260 265 270 Ile Tyr Ala Cys Met Asp Ala Ile Val Pro Gly Asn Val Pro Ser Ala 275 280 285 Cys Leu Arg Glu Ala Leu Asp Gln Ala Arg Val Lys Pro Gly Asp Ile 290 295 300 Glu Met Leu Glu Leu Ser Ala Asp Ser Ala Arg His Leu Lys Asp Pro 305 310 315 320 Ser Val Leu Pro Lys Glu Leu Thr Ala Glu Glu Glu Ile Gly Gly Leu 325 330 335 Gln Thr Ile Leu Arg Asp Asp Asp Lys Leu Pro Arg Asn Val Ala Thr 340 345 350 Gly Ser Val Lys Ala Thr Val Gly Asp Thr Gly Tyr Ala Ser Gly Ala<000225>355 360 365 Ala Ser Leu Ile Lys Ala Ala Leu Cys Ile Tyr Asn Arg Tyr Leu Pro 370 375 380 Ser Asn Gly Asp Asp Trp Asp Glu Pro Ala Pro Glu Ala Pro Trp Asp 385 390 395 400 Ser Thr Leu Phe Ala Cys Gln Thr Ser Arg Ala Trp Leu Lys Asn Pro 405 410 415 Gly Glu Arg Arg Tyr Ala Ala Val Ser 420 425 <210> 38 <211> 529 <212> PRT <213> Schizochytorium sp. <400> 38 Ser Arg Ala Trp Leu Lys Asn Pro Gly Glu Arg Arg Tyr Ala Ala Val 1 5 10 15 Ser Gly Val Ser Glu Thr Arg Ser Cys Tyr Ser Val Leu Leu Ser Glu 20 25 30 Ala Glu Gly His Tyr Glu Arg Glu Asn Arg Ile Ser Leu Asp Glu Glu 35 40 45 Ala Pro Lys Leu Ile Val Leu Arg Ala Asp Ser His Glu Glu Ile Leu 50 55 60 Gly Arg Leu Asp Lys Ile Arg Glu Arg Phe Leu Gln Pro Thr Gly Ala 65 70 75 80 Ala Pro Arg Glu Ser Glu Leu Lys Ala Gln Ala Arg Arg Ile Phe Leu 85 90 95 Glu Leu Leu Gly Glu Thr Leu Ala Gln Asp Ala Ala Ser Ser Gly Ser 100 105 110 Gln Lys Pro Leu Ala Leu Ser Leu Val Ser Thr Pro Ser Lys Leu Gln 115 120 125 Arg Glu Val Glu Leu Ala Ala Lys Gly Ile Pro Arg Cys Leu Lys Met 130 135 140 Arg Arg Asp Trp Ser Ser Pro Ala Gly Ser Arg Tyr Ala Pro Glu Pro 145 150 155 160 Leu Ala Ser Asp Arg Val Ala Phe Met Tyr Gly Glu Gly Arg Ser Pro 165 170 175 Tyr Tyr Gly Ile Thr Gln Asp Ile His Arg Ile Trp Pro Glu Leu His 180 185 190 Glu Val Ile Asn Glu Lys Thr Asn Arg Leu Trp Ala Glu Gly Asp Arg 195 200 205 Trp Val Met Pro Arg Ala Ser Phe Lys Ser Glu Leu Glu Ser Gln Gln 210 215 220 Gln Glu Phe Asp Arg Asn Met Ile Glu Met Phe Arg Leu Gly Ile Leu 225 230 235 240 Thr Ser Ile Ala Phe Thr Asn Leu Ala Arg Asp Val Leu Asn Ile Thr 245 250 255 Pro Lys Ala Ala Phe Gly Leu Ser Leu Gly Glu Ile Ser Met Ile Phe 260 265 270 Ala Phe Ser Lys Lys Asn Gly Leu Ile Ser Asp Gln Leu Thr Lys Asp 275 280 285 Leu Arg Glu Ser Asp Val Trp Asn Lys Ala Leu Ala Val Glu Phe Asn 290 295 300 Ala Leu Arg Glu Ala Trp Gly Ile Pro Gln Ser Val Pro Lys Asp Glu 305 310 315 320 Phe Trp Gln Gly Tyr Ile Val Arg Gly Thr Lys Gln Asp Ile Glu Ala 325 330 335 Ala Ile Ala Pro Asp Ser Lys Tyr Val Arg Leu Thr Ile Ile Asn Asp 340 345 350 Ala Asn Thr Ala Leu Ile Ser Gly Lys Pro Asp Ala Cys Lys Ala Ala 355 360 365 Ile Ala Arg Leu Gly Gly Asn Ile Pro Ala Leu Pro Val Thr Gln Gly 370 375 380 Met Cys Gly His Cys Pro Glu Val Gly Pro Tyr Thr Lys Asp Ile Ala 385 390 395 400 Lys Ile His Ala Asn Leu Glu Phe Pro Val Val Asp Gly Leu Asp Leu 405 410 415 Trp Thr Thr Ile Asn Gln Lys Arg Leu Val Pro Arg Ala Thr Gly Ala 420 425 430 Lys Asp Glu Trp Ala Pro Ser Ser Phe Gly Glu Tyr Ala Gly Gln Leu 435 440 445 Tyr Glu Lys Gln Ala Asn Phe Pro Gln Ile Val Glu Thr Ile Tyr Lys 450 455 460 Gln Asn Tyr Asp Val Phe Val Glu Val Gly Pro Asn Asn His Arg Ser 465 470 475 480 Thr Ala Val Arg Thr Thr Leu Gly Pro Gln Arg Asn His Leu Ala Gly 485 490 495 Ala Ile Asp Lys Gln Asn Glu Asp Ala Trp Thr Thr Ile Val Lys Leu 500 505 510 Val Ala Ser Leu Lys Ala His Leu Val Pro Gly Val Thr Ile Ser Pro 515 520 525 Leu <210> 39 <211> 449 <212> PRT <213> Schizochytorium sp. <400> 39 Cys Asn Ile Ala Asp Leu Gly Ser Arg Ala Phe Met Lys Thr Tyr Gly 1 5 10 15 Val Ser Ala Pro Leu Tyr Thr Gly Ala Met Ala Lys Gly Ile Ala Ser 20 25 30 Ala Asp Leu Val Ile Ala Ala Gly Arg Gln Gly Ile Leu Ala Ser Phe 35 40 45 Gly Ala Gly Gly Leu Pro Met Gln Val Val Arg Glu Ser Ile Glu Lys 50 55 60 Ile Gln Ala Ala Leu Pro Asn Gly Pro Tyr Ala Val Asn Leu Ile His 65 70 75 80 Ser Pro Phe Asp Ser Asn Leu Glu Lys Gly Asn Val Asp Leu Phe Leu 85 90 95[[ID=F39]] Glu Lys Gly Val Thr Phe Val Glu Ala Ser Ala Phe Met Thr Leu Thr 100 105 110 Pro Gln Val Val Arg Tyr Arg Ala Ala Gly Leu Thr Arg Asn Ala Asp 115 120 125 Gly Ser Val Asn Ile Arg Asn Arg Ile Ile Gly Lys Val Ser Arg Thr 130 135 140 Glu Leu Ala Glu Met Phe Met Arg Pro Ala Pro Glu His Leu Leu Gln 145 150 155 160 Lys Leu Ile Ala Ser Gly Glu Ile Asn Gln Glu Gln Ala Glu Leu Ala 165 170 175 Arg Arg Val Pro Val Ala Asp Asp Ile Ala Val Glu Ala Asp Ser Gly 180 185 190 Gly His Thr Asp Asn Arg Pro Ile His Val Ile Leu Pro Leu Ile Ile 195 200 205 Asn Leu Arg Asp Arg Leu His Arg Glu Cys Gly Tyr Pro Ala Asn Leu 210 215 220 Arg Val Arg Val Gly Ala Gly Gly Gly Ile Gly Cys Pro Gln Ala Ala 225 230 235 240 Leu Ala Thr Phe Asn Met Gly Ala Ser Phe Ile Val Thr Gly Thr Val 245 250 255 Asn Gln Val Ala Lys Gln Ser Gly Thr Cys Asp Asn Val Arg Lys Gln 260 265 270 Leu Ala Lys Ala Thr Tyr Ser Asp Val Cys Met Ala Pro Ala Ala Asp 275 280 285 Met Phe Glu Glu Gly Val Lys Gln Val Leu Lys Gly Thr Met 290,295,300 Phe Pro Ser Arg Ala Asn Lys Tyr Glu To Phe Cys Lys Tyr Asp 305 310 315 320 Ser Phe Glu Ser Met Pro Ala Glu Leu Ala Arg Val Glu Lys Arg 325 330 335 Ile Phe Ser Arg Ala Leu Glu Glu Val Trp Asp Glu Thr Lys Asn Phe 340 345 350 Tyr with Asn Arg Leu His Asn Pro Glu Lys With Gln Arg Ala Glu Arg 355 360 365 Asp Pro Lys Leu Lys Met Ser Leu Cys Phe Arg Trp Tyr Leu Ser Leu 370 375 380 Only Serve Arg Trp Only Serve Asn Thr Gly Only Serve Asp Arg With Asp Tyr 385 390 395 400 Gln Val Trp Cys Gly Pro Ala Ile Gly Ser Phe Asn Asp Phe Ile Lys 405 410 415 Gly Thr Tyr Leu Asp Pro Ala Val Ala Asn Glu Tyr Pro Cys Val Val 420 425 430 Gln Ile Asn Lys Gln Ile Leu Arg Gly Ala Cys Phe Leu Arg Arg Leu 435 440 445 Glu <210> 40 <211> 202 <212> PRT <213> Schizochytorium sp. <400> 40 Tyr Lys Leu Cys Ala Arg Lys Met Leu Met Ile Asp Arg Val Thr Ser 1 5 10 15 Ile Asp His Lys Gly Gly Val Tyr Gly Leu Gly Gln Leu Val Gly Glu 20 25 30 Lys Ile Leu Glu Arg Asp His Trp Tyr Phe Pro Cys His Phe Val Lys 35 40 45 Asp Gln Val Met Ala Gly Ser Leu Val Ser Asp Gly Cys Ser Gln Met 50 55 60 Leu Lys Met Tyr Met Ile Trp Leu Gly Leu His Leu Thr Thr Gly Pro 65 70 75 80 Phe Asp Phe Arg Pro Val Asn Gly His Pro Asn Lys Val Arg Cys Arg 85 90 95 Gly Gln Ile Ser Pro His Lys Gly Lys Leu Val Tyr Val Met Glu Ile 100 105 110 Lys Glu Met Gly Phe Asp Glu Asp Asn Asp Pro Tyr Ala Ile Ala Asp 115 120 125 Val Asn Ile Ile Asp Val Asp Phe Glu Lys Gly Gln Asp Phe Ser Leu 130 135 140 Asp Arg Ile Ser Asp Tyr Gly Lys Gly Asp Leu Asn Lys Lys Ile Val 145 150 155 160 Val Asp Phe Lys Gly Ile Ala Leu Lys Met Gln Lys Arg Ser Thr Asn 165 170 175 Lys Asn Pro Ser Lys Val Gln Pro Val Phe Ala Asn Gly Ala Ala Thr 180 185 190 Val Gly Pro Glu Ala Ser Lys Ala Ser Ser 195 200 <210> 41 <211> 147 <212> PRT <213> Schizochytorium sp. <400> 41 [[ID=三十四]]Leu Asn Arg Arg Thr Asp Gln Gly Gln Tyr Leu Asp Ala Val Asp Ile 1 5 10 15 Val Ser Gly Ser Gly Lys Lys Ser Leu Gly Tyr Ala His Gly Ser Lys 20 25 30 Thr Val Asn Pro Asn Asp Trp Phe Phe Ser Cys His Phe Trp Phe Asp 35 40 45 It should be noted that in the above translation, for the text with Chinese characters in the original (such as "裂殖壶菌(Schizochytorium sp.)"), it is assumed that the Chinese part is just an annotation in the original text and is translated accordingly. If there is a misunderstanding, please provide more context for accurate translation.Ser Val Met Pro Gly Ser Leu Gly Val Glu Ser Met Phe Gln Leu Val 50 55 60 Glu Ala Ile Ala Ala His Glu Asp Leu Ala Gly Lys His Gly Ile Ala 65 70 75 80 Asn Pro Thr Phe Val His Ala Pro Gly Lys Ile Ser Trp Lys Tyr Arg 85 90 95 Gly Gln Leu Thr Pro Lys Ser Lys Lys Met Asp Ser Glu Val His Ile 100 105 110 Val Ser Val Asp Ala His Asp Gly Val Val Asp Leu Val Ala Asp Gly 115 120 125 Phe Leu Trp Ala Asp Ser Leu Arg Val Tyr Ser Val Ser Asn Ile Arg 130 135 140 Val Arg Ile 145 <210> 42 <211> 449 <212> PRT <213> Schizochytorium sp. <400> 42 Cys Thr Leu Gly Asp Leu Gly Asp Arg Ser Phe Met Glu Thr Tyr Gly 1 5 10 15 Val Val Ala Pro Leu Tyr Thr Gly Ala Met Ala Lys Gly Ile Ala Ser 20 25 30 Ala Asp Leu Val Ile Ala Ala Gly Lys Arg Lys Ile Leu Gly Ser Phe 35 40 45 Gly Ala Gly Gly Leu Pro Met His His Val Arg Ala Ala Leu Glu Lys 50 55 60 Ile Gln Ala Ala Leu Pro Gln Gly Pro Tyr Ala Val Asn Leu Ile His 65 70 75 80 Ser Pro Phe Asp Ser Asn Leu Glu Lys Gly Asn Val Asp Leu Phe Leu 85 90 95 Glu Lys Gly Val Thr Val Val Glu Ala Ser Ala Phe Met Thr Leu Thr 100 105 110 Pro Gln Val Val Arg Tyr Arg Ala Ala Gly Leu Ser Arg Asn Ala Asp 115 120 125 Gly Ser Val Asn Ile Arg Asn Arg Ile Ile Gly Lys Val Ser Arg Thr 130 135 140 Glu Leu Ala Glu Met Phe Ile Arg Pro Ala Pro Glu His Leu Leu Glu 145 150 155 160 Lys Leu Ile Ala Ser Gly Glu Ile Thr Gln Glu Gln Ala Glu Leu Ala 165 170 175 Arg Arg Val Pro Val Ala Asp Asp Ile Ala Val Glu Ala Asp Ser Gly 180 185 190 Gly His Thr Asp Asn Arg Pro Ile His Val Ile Leu Pro Leu Ile Ile 195 200 205 Asn Leu Arg Asn Arg Leu His Arg Glu Cys Gly Tyr Pro Ala His Leu 210 215 220 Arg Val Arg Val Gly Ala Gly Gly Gly Val Gly Cys Pro Gln Ala Ala 225 230 235 240 Ala Ala Ala Leu Thr Met Gly Ala Ala Phe Ile Val Thr Gly Thr Val 245 250 255 Asn Gln Val Ala Lys Gln Ser Gly Thr Cys Asp Asn Val Arg Lys Gln 260 265 270 Leu Ser Gln Ala Thr Tyr Ser Asp Ile Cys Met Ala Pro Ala Ala Asp 275 280 285 Met Phe Glu Glu Gly Val Lys Leu Gln Val Leu Lys Lys Gly Thr Met 290 295 300 Phe Pro Ser Arg Ala Asn Lys Leu Tyr Glu Leu Phe Cys Lys Tyr Asp 305 310 315 320 Ser Phe Asp Ser Met Pro Pro Ala Glu Leu Glu Arg Ile Glu Lys Arg 325 330 335 Ile Phe Lys Arg Ala Leu Gln Glu Val Trp Glu Glu Thr Lys Asp Phe 340 345 350 Tyr Ile Asn Gly Leu Lys Asn Pro Glu Lys Ile Gln Arg Ala Glu His 355 360 365 Asp Pro Lys Leu Lys Met Ser Leu Cys Phe Arg Trp Tyr Leu Gly Leu 370 375 380 Ala Ser Arg Trp Ala Asn Met Gly Ala Pro Asp Arg Val Met Asp Tyr 385 390 395 400 Gln Val Trp Cys Gly Pro Ala Ile Gly Ala Phe Asn Asp Phe Ile Lys 405 410 415 Gly Thr Tyr Leu Asp Pro Ala Val Ser Asn Glu Tyr Pro Cys Val Val 420 425 430 Gln Ile Asn Leu Gln Ile Leu Arg Gly Ala Cys Tyr Leu Arg Arg Leu 435 440 445 Asn <210> 43 <211> 407 <212> PRT <213> Aurantiochytrium sp. OH4 <400> 43 Asp Thr Arg Ile Ala Val Ile Gly Met Ser Ala Ile Leu Pro Cys Gly 1 5 10 15 Thr Thr Val Arg Glu Ser Trp Glu Ala Ile Arg Asp Gly Ile Asp Cys 20 25 30 Leu Ser Asp Leu Pro Glu Asp Arg Val Asp Val Thr Ala Tyr Phe Asp 35 40 45 Pro Val Lys Thr Thr Lys Asp Lys Ile Tyr Cys Lys Arg Gly Gly Phe 50 55 60 Ile Pro Glu Tyr Asp Phe Asp Ala Arg Glu Phe Gly Leu Asn Met Phe 65 70 75 80 Gln Met Glu Asp Ser Asp Ala Asn Gln Thr Val Thr Leu Leu Lys Val 85 90 95 Lys Glu Ala Leu Glu Asp Ala Gly Ile Glu Ala Leu Ser Lys Glu Lys 100 105 110 Lys Asn Ile Gly Cys Val Leu Gly Ile Gly Gly Gly Gln Lys Ser Ser 115 120 125 His Glu Phe Tyr Ser Arg Leu Asn Tyr Val Val Val Glu Lys Val Leu 130 135 140 Arg Lys Met Gly Met Pro Glu Glu Asp Val Gln Ala Ala Val Glu Lys 145 150 155 160 Tyr Lys Ala Asn Phe Pro Glu Trp Arg Leu Asp Ser Phe Pro Gly Phe 165 170 175 Leu Gly Asn Val Thr Ala Gly Arg Cys Thr Asn Thr Phe Asn Leu Asp 180 185 190 Gly Met Asn Cys Val Val Asp Ala Ala Cys Ala Ser Ser Leu Ile Ala 195 200 205 Val Lys Val Ala Ile Asp Glu Leu Leu His Gly Asp Cys Asp Met Met 210 215 220 Ile Thr Gly Ala Thr Cys Thr Asp Asn Ser Ile Gly Met Tyr Met Ala 225 230 235 240 Phe Ser Lys Thr Pro Val Phe Ser Thr Asp Pro Ser Val Arg Ala Tyr 245 250 255 Asp Glu Lys Thr Lys Gly Met Leu Ile Gly Glu Gly Ser Ala Met Leu 260 265 270 Val Leu Lys Arg Tyr Ala Asp Ala Val Arg Asp Gly Asp Glu Ile His 275 280 285 Ala Val Ile Arg Gly Cys Ala Ser Ser Ser Asp Gly Lys Ala Ser Gly 290 295 300 Ile Tyr Thr Pro Thr Ile Ser Gly Gln Glu Glu Ala Leu Arg Arg Ala 305 310 315 320 Tyr Met Arg Ala Asn Val Asp Pro Ala Thr Val Thr Leu Val Glu Gly 325 330 335 His Gly Thr Gly Thr Pro Val Gly Asp Arg Ile Glu Leu Thr Ala Leu 340 345 350 Arg Asn Leu Phe Asp Ser Ala Tyr Gly Asn Glu Lys Glu Lys Val Ala 355 360 365 Val Gly Ser Ile Lys Ser Asn Ile Gly His Leu Lys Ala Val Ala Gly 370 375 380 Leu Ala Gly Met Ile Lys Val Ile Met Ala Leu Lys His Lys Thr Leu 385 390 395 400 Pro Ala Thr Ile Asn Val Asp 405 <210> 44 <211> 332 <212> PRT <213> Aurantiochytrium sp. OH4 <400> 44 Ala Leu Phe Ser Gly Gln Gly Ala Gln Tyr Thr His Met Phe Ser Glu 1 5 10 15 Val Ala Met Asn Trp Pro Gln Phe Arg Glu Ser Ile Ser Asp Met Asp 20 25 30 Arg Ala Gln Ala Lys Val Ala Gly Ala Asp Lys Asp Tyr Glu Arg Val 35 40 45 Ser Gln Val Leu Tyr Pro Arg Lys Pro Tyr Asn Ser Glu Pro Glu Gln 50 55 60 Asp His Lys Lys Ile Ser Leu Thr Ala Tyr Ser Gln Pro Ser Thr Leu 65 70 75 80 Ala Cys Ala Leu Gly Ala Tyr Glu Ile Phe Lys Gln Ala Gly Phe Lys 85 90 95 Pro Asp Phe Ala Ala Gly His Ser Leu Gly Glu Phe Ala Ala Leu Tyr 100 105 110 Ala Ala Asp Cys Val Asn Arg Asp Asp Leu Phe Glu Leu Val Cys Arg 115 120 125 Arg Ala Arg Ile Met Gly Gly Lys Asp Ala Pro Ala Thr Pro Lys Gly 130 135 140 Cys Met Ala Ala Val Ile Gly Pro Asn Ala Glu Lys Ile Gln Ile Arg 145 150 155 160 Thr Ala Asp Val Trp Leu Gly Asn Cys Asn Ser Pro Ser Gln Thr Val 165 170 175 Ile Thr Gly Ser Val Glu Gly Ile Lys Lys Glu Ser Glu Leu Leu Gln 180 185 190 Arg Glu Gly Phe Arg Val Val Pro Leu Ala Cys Glu Ser Ala Phe His 195 200 205 Ser Pro Gln Met Gln Asn Ala Ser Ser Ala Phe Lys Asp Val Leu Ser 210 215 220 Lys Val Ala Phe Arg Gln Pro Ser Ala Gln Thr Lys Leu Phe Ser Asn 225 230 235 240 Val Ser Gly Glu Thr Tyr Ser Asn Asn Ala Gln Asp Leu Leu Lys Glu 245 250 255 His Met Thr Ser Ser Val Lys Phe Ile Ser Gln Val Arg Asn Met His 260 265 270 Ser Ala Gly Ala Arg Ile Phe Val Glu Phe Gly Pro Lys Gln Val Leu 275 280 285 Ser Lys Leu Val Ser Glu Thr Leu Lys Asp Asp Pro Ser Ile Ile Thr 290 295 300 Ile Ser Val Asn Pro Ser Ser Gly Lys Asp Ala Asp Ile Gln Leu Arg 305 310 315 320 Glu Ala Ala Val Gln Leu Val Val Ala Gly Val Asn 325 330 <210> 45 <211> 66 <212> PRT <213> Aurantiochytrium sp. OH4 <400> 45 Val Met Glu Val Leu Ala Ala Lys Thr Gly Tyr Glu Thr Asp Met Ile 1 5 10 15 Glu Pro Asp Met Glu Leu Glu Thr Glu Leu Gly Ile Asp Ser Ile Lys 20 25 30 Arg Val Glu Ile Leu Ser Glu Val Gln Ala Gln Leu Asn Val Glu Ala 35 40 45 Lys Asp Val Asp Ala Leu Ser Arg Thr Arg Thr Val Gly Glu Val Val 50 55 60 Asn Ala 65 <210> 46 <211> 230 <212> PRT <213> Aurantiochytrium sp. OH4 <400> 46 Asp Val Leu Leu Val Ser Gly Gly Ala Arg Gly Ile Thr Pro Leu Cys 1 5 10 15 Ile Arg Glu Ile Thr Arg Gln Val Arg Gly Gly Lys Tyr Ile Leu Leu 20 25 30 Gly Arg Ser Lys Val Pro Ala Gly Glu Pro Ala Trp Cys Asn Gly Val 35 40 45 Ser Asp Asp Asp Leu Gly Lys Ala Ala Met Gln Glu Leu Lys Arg Ala 50 55 60 Phe Ser Ala Gly Glu Gly Pro Lys Pro Thr Pro Met Thr His Lys Lys 65 70 75 80 Leu Val Gly Thr Ile Ala Gly Ala Arg Glu Val Arg Ser Ser Ile Ala 85 90 95 Asn Ile Glu Ala Leu Gly Gly Lys Ala Ile Tyr Ser Ser Cys Asp Val 100 105 110 Asn Ser Ala Ala Asp Val Ala Lys Ala Val Arg Glu Ala Glu Ala Gln 115 120 125 Leu Gly Ala Arg Val Thr Gly Val Val His Ala Ser Gly Val Leu Arg 130 135 140 Asp Arg Leu Ile Glu Gln Lys Arg Pro Asp Glu Phe Asp Ala Val Phe 145 150 155 160 Gly Thr Lys Val Thr Gly Leu Glu Asn Leu Phe Gly Ala Ile Asp Met 165 170 175 Ala Asn Leu Lys His Leu Val Leu Phe Ser Ser Leu Ala Gly Phe His 180 185 190 Gly Asn Ile Gly Gln Ser Asp Tyr Ala Met Ala Asn Glu Ala Leu Asn 195 200 205 Lys Met Gly Leu Glu Leu Ser Asp Arg Val Ser Val Lys Ser Ile Cys 210 215 220 Phe Gly Pro Trp Asp Gly 225 230 <210> 47 <211> 284 <212> PRT <213> Aurantiochytrium sp. OH4 <400> 47 Gly Asn Trp Thr Thr Pro Thr Lys Lys Val Gly Ser Glu Pro Val Val 1 5 10 15 Ile His Arg Lys Ile Ser Ala Ala Ser Asn Pro Phe Leu Lys Asp His 20 25 30 Val Ile Gln Gly Arg Cys Val Leu Pro Met Thr Ile Ala Val Gly Cys 35 40 45 Leu Ala Glu Thr Cys Leu Gly Gln Phe Pro Gly Tyr Ser Leu Trp Ala 50 55 60 Ile Glu Asp Ala Gln Leu Phe Lys Gly Val Thr Val Asp Gly Asp Val 65 70 75 80 Asn Cys Glu Ile Thr Leu Lys Pro Ser Gln Gly Thr Ala Gly Arg Val 85 90 95 Met Ile Gln Ala Thr Leu Lys Thr Phe Ala Ser Gly Lys Leu Val Pro 100 105 110 Ala Tyr Arg Ala Val Ile Val Leu Ser Thr Gln Gly Lys Pro Pro Ala 115 120 125 Ala Thr Thr Ser Gln Thr Pro Ser Leu Gln Ala Asp Pro Ala Ala Arg 130 135 140 Gly Asn Pro Tyr Asp Gly Lys Thr Leu Phe His Gly Pro Ala Phe Gln 145 150 155 160 Gly Leu Lys Glu Ile Ile Ser Cys Asn Lys Ser Gln Leu Val Ala Glu 165 170 175 Cys Thr Phe Ile Pro Ser Ser Glu Ser Ala Gly Glu Phe Ala Ser Asp 180 185 190 Tyr Glu Ser His Asn Pro Phe Val Asn Asp Ile Ala Phe Gln Ala Met 195 200 205 Leu Val Trp Ile Arg Arg Thr Leu Gly Gln Ala Ala Leu Pro Asn Ser 210 215 220 Ile Gln Arg Ile Val Gln His Arg Ala Leu Pro Gln Asp Lys Pro Phe 225 230 235 240 Tyr Leu Thr Leu Lys Ser Asn Ser Ala Ser Gly His Ser Gln His Lys 245 250 255 Thr Ser Val Gln Phe His Asn Glu Gln Gly Asp Leu Phe Val Asp Ile 260 265 270 Gln Ala Ser Val Thr Ser Ser Asp Ser Leu Ala Phe 275 280 <210> 48 <211> 423 <212> PRT <213> Aurantiochytrium sp. OH4 <400> 48 Arg Ile Ala Val Val Gly Met Ala Val Gln Tyr Ala Gly Cys Lys Asp 1 5 10 15 Lys Glu Glu Phe Trp Lys Val Val Met Gly Gly Glu Ala Ala Trp Thr 20 25 30 Lys Ile Ser Asp Lys Arg Leu Gly Ser Asn Lys Arg Ala Glu His Phe 35 40 45 Lys Ala Glu Arg Ser Lys Phe Ala Asp Thr Phe Cys Asn Glu Asn Tyr 50 55 60 Gly Cys Val Asp Asp Ser Val Asp Asn Glu His Glu Leu Leu Leu Lys 65 70 75 80 Leu Ser Lys Lys Ala Leu Ser Glu Thr Ser Val Ser Asp Ser Thr Arg 85 90 95 Cys Gly Ile Val Ser Gly Cys Leu Ser Phe Pro Met Asp Asn Leu Gln 100 105 110 Gly Glu Leu Leu Asn Val Tyr Gln Asn His Val Glu Lys Lys Leu Gly 115 120 125 Ala Arg Val Phe Lys Asp Ala Ser Lys Trp Ser Glu Arg Glu Gln Ser 130 135 140 Gln Asn Pro Glu Ala Gly Asp Arg Arg Ile Phe Met Asp Pro Ala Ser 145 150 155 160 Phe Val Ala Glu Glu Leu Asn Leu Gly Pro Leu His Tyr Ser Val Asp 165 170 175 Ala Ala Cys Ala Thr Ala Leu Tyr Val Leu Arg Leu Ala Gln Asp His 180 185 190 Leu Val Ser Gly Ala Ala Asp Val Met Leu Ala Gly Ala Thr Cys Phe 195 200 205 Pro Glu Pro Phe Phe Ile Leu Ser Gly Phe Ser Thr Phe Gln Ala Met 210 215 220 Pro Val Ser Gly Asp Gly Ile Ser Tyr Pro Leu His Lys Asp Ser Gln 225 230 235 240 Gly Leu Thr Pro Gly Glu Gly Gly Ala Ile Met Val Leu Lys Arg Leu 245 250 255 Asp Asp Ala Ile Arg Asp Gly Asp His Ile Tyr Gly Thr Leu Leu Gly 260 265 270 Ala Thr Ile Ser Asn Ala Gly Cys Gly Leu Pro Leu Lys Pro His Leu 275 280 285 Pro Ser Glu Lys Ser Cys Leu Ile Asp Thr Tyr Lys Arg Val Asn Val 290 295 300 His Pro His Lys Ile Gln Tyr Val Glu Cys His Ala Thr Gly Thr Pro 305 310 315 320 Gln Gly Asp Arg Val Glu Ile Asp Ala Val Lys Ala Cys Phe Glu Gly 325 330 335 Lys Val Pro Arg Phe Gly Ser Ser Lys Gly Asn Phe Gly His Thr Leu 340 345 350 Val Ala Ala Gly Phe Ala Gly Met Cys Lys Val Leu Leu Ala Met Lys 355 360 365 His Gly Val Ile Pro Pro Thr Pro Gly Val Asp Gly Ser Ser Gln Met<000276C5>370 375 380 Asp Pro Leu Val Val Ser Glu Pro Ile Pro Trp Pro Asp Thr Glu Gly 385 39C 395 400 Glu Pro Lys Arg Ala Gly Leu Ser Ala Phe Gly Phe Gly Gly Thr Asn 405 410 415 Ala His Ala Val Phe Glu Glu 420 <210> 49 <211> 429 <212> PRT <213> Aurantiochytrium sp. OH4 <400> 49 Met Arg Ile Ala Ile Thr Gly Met Asp Ala Thr Phe Gly Ser Leu Lys 1 5 10 15 Gly Leu Asp Ala Phe Glu Arg Ala Ile Tyr Asn Gly Gln His Gly Ala 20 25 30 Val Pro Leu Pro Glu Lys Arg Trp Arg Phe Leu Gly Lys Asp Lys Asp 35 40 45 Phe Leu Asp Leu Cys Gly Val Lys Glu Val Pro His Gly Cys Tyr Ile 50 55 60 Glu Asp Val Glu Val Asp Phe Ser Arg Leu Arg Thr Pro Met Thr Pro 65 70 75 80 Asp Asp Met Leu Arg Pro Met Gln Leu Leu Ala Val Thr Thr Ile Asp 85 90 95 Arg Ala Ile Leu Asn Ser Gly Leu Lys Lys Gly Gly Lys Val Ala Val 100 105 110 Phe Val Gly Leu Gly Thr Asp Leu Glu Leu Tyr Arg His Arg Ala Arg 115 120 125 Val Ala Leu Lys Glu Arg Ala Arg Pro Glu Ala Ala Ala Ala Leu Asn 130 135 140 Asp Met Met Ser Tyr Ile Asn Asp Cys Gly Thr Ala Thr Ser Tyr Thr 145 150 155 160 Ser Tyr Ile Gly Asn Leu Val Ala Thr Arg Val Ser Ser Gln Trp Gly 165 170 175 Phe Glu Gly Pro Ser Phe Thr Ile Thr Glu Gly Asn Asn Ser Val Tyr 180 185 190 Arg Cys Ala Glu Leu Gly Lys Tyr Leu Leu Glu Thr Gly Glu Val Glu 195 200 205 Ala Val Val Ile Ala Gly Val Asp Leu Cys Ala Ser Ala Glu Asn Leu 210 215 220 Tyr Val Lys Ser Arg Arg Phe Lys Val Ser Glu Gln Glu Ser Pro Arg 225 230 235 240 Ala Ser Phe Asp Ser Gly Ala Asp Gly Tyr Phe Val Gly Glu Gly Cys 245 250 255 Gly Ala Leu Val Leu Lys Arg Glu Ser Asp Cys Thr Lys Asp Glu Arg 260 265 270 Ile Tyr Ala Cys Met Asp Ala Ile Val Pro Gly Asn Met Pro Ala Ala 275 280 285 Cys Met Glu Glu Ala Leu Ala Gln Ala Arg Val Asn Pro Lys Asp Val 290 295 300 Glu Met Leu Glu Leu Ser Ala Asp Ser Ala Arg His Leu Lys Asn Pro 305 310 315 320 Ser Val Leu Pro Lys Glu Leu Thr Ala Glu Glu Glu Ile Arg Gly Ile 325 330 335 Glu Ala Ile Leu Ser Gln Arg Ser Ser Asn Glu Ala Val Glu Pro His 340 345 350 Asn Val Ala Val Ser Ser Val Lys Ser Thr Val Gly Asp Thr Gly Tyr 355 360 365 Ala Ser Gly Ala Ala Ser Leu Ile Lys Thr Ala Leu Cys Leu Tyr Asn 370 375 380 Arg Tyr Leu Pro Ser Asn Gly Ala Ser Trp Glu Glu Pro Ala Pro Glu 385 390 395 400 Thr Gln Trp Gly Lys Ser Leu Tyr Ala Cys Gln Ser Ser Arg Ala Trp 405 410 415 Leu Lys Asn Pro Gly Ala Arg Arg His Ala Ala Val Ser 420 425 <210> 50 <211> 516 <212> PRT <213> Aurantiochytrium sp. OH4 <400> 50 Ser Arg Ala Trp Leu Lys Asn Pro Gly Ala Arg Arg His Ala Ala Val 1 5 10 15 Ser Gly Val Ser Glu Thr Arg Ser Cys Tyr Thr Val Leu Leu Ser Asp 20 25 30 Val Glu Gly His His Glu Thr Lys Ser Arg Ile Ser Leu Asp Asp Asp 35 40 45 Ala Val Lys Leu Leu Val Ile Arg Gly Asp Ser His Asp Ala Ile Thr 50 55 60 Gln Arg Val Asp Lys Leu Arg Glu Arg Leu Ala Gln Pro Ser Ala Asn 65 70 75 80 Val Arg Leu Ala Phe Met Glu Leu Leu Gly Glu Ser Ile Ala Gln Glu 85 90 95 Thr Lys Thr Pro Leu Pro Ala Phe Ala Leu Cys Leu Val Thr Ser Pro 100 105 110 Ser Lys Leu Gln Lys Glu Leu Glu Leu Ala Ser Lys Gly Ile Pro Arg 115 120 125 Ser Leu Lys Met Gly Arg Asp Trp Thr Ser Pro Ser Gly Ser His Phe 130 135 140 Ala Pro Lys Pro Leu Ser Ser Asp Arg Val Ala Phe Met Tyr Gly Glu 145 150 155 160 Gly Arg Ser Pro Tyr Tyr Gly Ile Gly Leu Asp Ile His Arg Ile Trp 165 170 175 Pro Glu Leu His Glu Phe Val Asn Ala Lys Thr Asn Lys Leu Trp Asp 180 185 190 Gln Gly Asp Arg Trp Leu Ile Pro Arg Ala Ser Thr Lys Glu Glu Leu 195 200 205 Lys Ala Gln Glu Asp Glu Phe Ser Arg Asn Gln Val Glu Met Phe Arg 210 215 220 Leu Gly Ile Leu Met Ser Met Cys Phe Thr His Ile Ala Arg Asp Val 225 230 235 240 Leu Gly Ile Gln Pro Lys Ala Ala Phe Gly Leu Ser Leu Gly Glu Ile 245 250 255 Ser Met Val Phe Ala Phe Ser Glu Lys Asn Gly Leu Val Ser Glu Glu 260 265 270 Leu Thr Thr Lys Leu Arg Asn Ser Glu Val Trp Arg Lys Ala Leu Ala 275 280 285 Val Glu Phe Asp Ala Leu Arg Lys Ala Trp Asn Ile Pro Gln Asp Thr 290 295 300 Pro Val Ser Glu Phe Trp Gln Gly Tyr Val Val Arg Gly Thr Arg Glu 305 310 315 320 Ala Val Glu Ala Ala Ile Gly Pro Asn Asn Lys Tyr Val His Leu Thr 325 330 335 Ile Val Asn Asp Ala Asn Ser Ala Leu Ile Ser Gly Lys Pro Glu Asp 340 345 350 Cys Lys Ala Ala Ile Ala Arg Leu Ser Ser Asn Leu Pro Ala Leu Pro 355 360 365 Val Asp Leu Gly Met Cys Gly His Cys Pro Val Val Glu Pro Tyr Gly 370 375 380 Lys Gln Ile Ala Glu Ile His Ser Val Leu Glu Ile Pro Glu Val Ala 385 390 395 400 Gly Leu Asp Leu Tyr Thr Ser Val Asn Gln Lys Lys Leu Val Asn Lys 405 410 415 Ser Thr Gly Ala Ser Asp Glu Tyr Ala Pro Ser Phe Gly Glu Tyr Ala 420 425 430 Ala Gln Leu Tyr Thr Val Gln Ala Asp Phe Pro Lys Ile Ala Lys Thr 435 440 445 Val Ser Asp Lys Asn Phe Asp Val Phe Val Glu Thr Gly Pro Asn Ala 450 455 460 His Arg Ser Ala Ala Ile Arg Ala Thr Leu Gly Asn Ser Lys Pro Phe 465 470 475 480 Val Thr Gly Ser Met Asp Arg Gln Asn Glu Asn Ala Trp Thr Thr Met 485 490 495 Val Lys Leu Val Ala Ser Leu Gln Ala His Arg Val Pro Gly Val Lys 500 505 510 Val Ser Pro Leu 515 <210> 51 <211> 449 <212> PRT <213> Aurantiochytrium sp. OH4 <400> 51 Asp Leu Gly Ser Arg Ala Phe Met Glu Thr Tyr Gly Val Ser Ala Pro 1 5 10 15 Met Tyr Thr Gly Ala Met Ala Lys Gly Ile Ala Ser Ala Glu Met Val 20 25 30 Ile Ala Ala Gly Lys Arg Gly Ile Leu Gly Ser Leu Gly Ala Gly Gly 35 40 45 Leu Pro Ile Ala Thr Val Arg Lys Ala Leu Glu Ala Ile Gln Ala Glu 50 55 60 Leu Pro Lys Gly Pro Tyr Ala Val Asn Leu Ile His Ser Pro Phe Asp 65 70 75 80 Serum Asn Leu Glu Lys Gly Asn Val Asp Leu Phe Leu Glu Lys Gly Val 85 90 95 Thr Val Val Glu Ala Ser Ala Phe Met Thr Leu Thr Pro Gln Leu Val 100 105 110 Arg Tyr Arg Ala Ala Gly Leu Ser Arg Ala Ala Asp Gly Ser Thr Val 115 120 125 Ile Lys Asn Arg Val Ile Gly Lys Val Ser Arg Thr Glu Leu Ala Ala 130 135 140 Met Phe Ile Arg Pro Ala Pro Glu Asn Leu Leu Glu Lys Leu Leu Lys 145 150 155 160 Ser Gly Glu Ile Thr Gln Glu Gln Ala Ala Leu Ala Arg Thr Val Pro 165 170 175 Val Ala Asp Asp Ile Ala Val Glu Ala Asp Ser Gly Gly His Thr Asp 180 185 190 Asn Arg Pro Ile His Val Ile Leu Pro Leu Ile Val Asn Leu Arg Asp 195 200 205 Arg Leu His Lys Glu Cys Gly Tyr Pro Ala His Leu Arg Val Arg Val 210 215 220 Gly Ala Gly Gly Gly Ile Gly Cys Pro Gln Ala Ala Ile Ala Thr Phe 225 230 235 240 Asn Met Gly Ala Ala Phe Ile Val Thr Gly Thr Val Asn Gln Met Ser 245 250 255 Lys Gln Ala Gly Thr Cys Asp Thr Val Arg Lys Gln Leu Ser Gln Ala 260 265 270 Thr Tyr Ser Asp Ile Cys Met Ala Pro Ala Ala Asp Met Phe Glu Glu 275 280 285 Gly Val Lys Leu Gln Val Leu Lys Lys Gly Thr Met Phe Pro Ser Arg 290 295 300 Ala Asn Lys Leu Tyr Glu Leu Phe Val Lys Tyr Asp Ser Phe Glu Ser 305 310 315 320 Met Ala Pro Gly Glu Leu Glu Arg Val Glu Lys Arg Ile Phe Lys Lys 325 330 335 Ser Leu Ser Glu Val Trp Glu Glu Thr Lys Asp Phe Tyr Ile Asn Arg 340 345 350 Leu Gln Asn Pro Glu Lys Ile Glu Arg Ala Glu Arg Asp Pro Lys Leu 355 360 365 Lys Met Ser Leu Cys Phe Arg Trp Tyr Leu Gly Leu Ala Ser Phe Trp 370 375 380 Ala Asn Ala Gly Ile Pro Asp Arg Ala Met Asp Tyr Gln Val Trp Cys 385 390 395 400 Gly Pro Ala Ile Gly Ser Phe Asn Asp Phe Ile Lys Gly Thr Tyr Leu 405 410 415 Asp Pro Ala Val Ala Asn Glu Tyr Pro Asp Val Val Gln Ile Asn Leu 420 425 430 Gln Ile Leu Arg Gly Ala Cys Phe Leu Arg Arg Leu Glu Ala Val Arg 435 440 445 Asn <210> 52 <211> 152 <212> PRT <213> Aurantiochytrium sp. OH4 <400> 52 Tyr Lys Leu Cys Ala Arg Lys Met Leu Met Ile Asp Arg Val Thr Lys 1 5 10 15 Ile Asp Tyr Thr Gly Gly Pro Tyr Gly Leu Gly Leu Leu Val Gly Glu 20 25 30 Lys Ile Leu Glu Arg Asp His Trp Tyr Phe Pro Cys His Phe Val Gly 35 40 45 Asp Gln Val Met Ala Gly Ser Leu Val Ser Asp Gly Cys Ser Gln Leu 50 55 60 Leu Lys Met Tyr Met Leu Trp Leu Gly Leu His Leu Lys Thr Gly Pro 65 70 75 80 Phe Asp Phe Arg Pro Val Asn Gly His Pro Asn Lys Val Arg Cys Arg 85 90 95 Gly Gln Ile Ser Pro His Lys Gly Lys Leu Val Tyr Val Met Glu Ile 100 105 110 Lys Glu Met Gly Tyr Asp Glu Ala Gly Asp Pro Tyr Ala Ile Ala Asp 115 120 125 Val Asn Ile Leu Asp Ile Asp Phe Glu Lys Gly Gln Thr Phe Asp Leu 130 135 140 Ala Asn Leu His Glu Tyr Gly Lys 145 150 <210> 53 <211> 147 <212> PRT <213> Aurantiochytrium sp. OH4 <400> 53 Leu Ser Arg Arg Trp Asn Gln Cys Gln Tyr Leu Asp Thr Ile Asp Leu 1 5 10 15 Val Val Ala Gly Gly Ser Ala Gly Leu Gly Tyr Gly His Gly Arg Lys 20 25 30 Gln Val Asn Pro Lys Asp Trp Phe Phe Ser Cys His Phe Trp Phe Asp 35 40 45 Ser Val Met Pro Gly Ser Leu Gly Val Glu Ser Met Phe Gln Leu Val 50 55 60 Glu Ser Ile Ala Val Lys Gln Asp Leu Ala Gly Lys Tyr Gly Ile Thr 65 70 75 80 Asn Pro Thr Phe Ala His Ala Pro Gly Lys Ile Ser Trp Lys Tyr Arg 85 90 95 Gly Gln Leu Thr Pro Thr Ser Lys Phe Met Asp Ser Glu Ala His Ile 100 105 110 Val Ser Ile Glu Ala His Asp Gly Val Val Asp Ile Val Ala Asn Gly 115 120 125 Asn Leu Trp Ala Asp Gly Leu Arg Val Tyr Asn Val Ser Asn Ile Arg 130 135 140 Val Arg Ile 145 <210> 54 <211> 449 <212> PRT <213> Aurantiochytrium sp. OH4 <400> 54 Cys Ser Leu Ser Asp Leu Gly Asp Glu Gly Phe Met Lys Thr Tyr Gly 1 5 10 15 Val Val Ala Pro Leu Tyr Thr Gly Ala Met Ala Lys Gly Ile Ala Ser 20 25 30 Ala Asp Leu Val Ile Ala Thr Gly Lys Arg Lys Ile Leu Gly Ser Phe 35 40 45 Gly Ala Gly Gly Leu Pro Met His Ile Val Arg Ala Ala Val Glu Lys 50 55 60 Ile Gln Ala Glu Leu Pro Asn Gly Pro Phe Ala Val Asn Leu Ile His 65 70 75 80 Ser Pro Phe Asp Ser Asn Leu Glu Lys Gly Asn Val Asp Leu Phe Leu 85 90 95 Glu Lys Gly Val Thr Val Val Glu Ala Ser Ala Phe Met Thr Leu Thr 100 105 110 Pro Gln Val Val Arg Tyr Arg Ala Ala Gly Leu Ser Arg Asn Ala Asp 115 120 125 Gly Ser Ile Asn Ile Lys Asn Arg Ile Ile Gly Lys Val Ser Arg Thr 130 135 140 Glu Leu Ala Glu Met Phe Ile Arg Pro Ala Pro Gln Asn Leu Leu Asp 145 150 155 160 Lys Leu Ile Gln Ser Gly Glu Ile Thr Lys Glu Gln Ala Glu Leu Ala 165 170 175 Lys Leu Val Pro Val Ala Asp Asp Ile Ala Val Glu Ala Asp Ser Gly 180 185 190 Gly His Thr Asp Asn Arg Pro Ile His Val Ile Leu Pro Leu Ile Ile 195 200 205 Asn Leu Arg Asn Arg Leu His Lys Glu Cys Gly Tyr Pro Ala His Leu 210 215 220 Arg Val Arg Val Gly Ala Gly Gly Gly Val Gly Cys Pro Gln Ala Ala 225 230 235 240 Ala Ala Ala Leu Ala Met Gly Ala Ala Phe Leu Val Thr Gly Thr Val 245 250 255 Asn Gln Val Ala Lys Gln Ser Gly Thr Cys Asp Asn Val Arg Lys Gln 260 265 270 Leu Cys Met Ala Thr Tyr Ser Asp Val Cys Met Ala Pro Ala Ala Asp 275 280 285 Met Phe Glu Glu Gly Val Lys Leu Gln Val Leu Lys Lys Gly Thr Met 290 295 300 Phe Pro Ser Arg Ala Asn Lys Leu Tyr Glu Leu Phe Cys Lys Tyr Asp 305 310 315 320 Ser Phe Glu Ser Met Pro Ala Ala Glu Leu Glu Arg Val Glu Lys Arg 325 330 335 Ile Phe Gln Cys Pro Leu Ala Asp Val Trp Ala Glu Thr Ser Asp Phe 340 345 350 Tyr Ile Asn Arg Leu His Asn Pro Glu Lys Ile Thr Arg Ala Glu Arg 355 360 365 Asp Pro Lys Leu Lys Met Ser Leu Cys Phe Arg Trp Tyr Leu Gly Leu 370 375 380 Ala Ser Arg Trp Ala Asn Thr Gly Glu Ala Gly Arg Val Met Asp Tyr 385 390 395 400 Gln Val Trp Cys Gly Pro Ala Ile Gly Ala Phe Asn Asp Phe Ile Lys 405 410 415 Gly Ser Tyr Leu Asp Pro Ala Val Ser Gly Glu Tyr Pro Asp Val Val 420 425 430 Gln Ile Asn Leu Gln Ile Leu Arg Gly Ala Cys Tyr Leu Arg Arg Leu 435 440 445 Asn <210> 55 <211> 4671 <212> DNA <213> Aureispira marina (Aureispira marina) <220> <221> CDS <222> (1)..(4671) <400> 55 atg aat tta aac cac tcg ctt cgc aaa act cct gtt gct gta ata gga 48 Met Asn Leu Asn His Ser Leu Arg Lys Thr Pro Val Ala Val Ile Gly 1 5 10 15 atg tct gcg ctt ttt gct gat gct aaa act gtt gac caa ttc tgg aac 96 Met Ser Ala Leu Phe Ala Asp Ala Lys Thr Val Asp Gln Phe Trp Asn 20 25 30 aat atc atc act ggc aag gat agc att aca gat gtt cct gaa aac aga 144 Asn With Thr Gly Lys Asp Ser With Thr Asp Val Pro Glu Asn Arg 35 40 45 tgg aga ata gaa gat tac tat gat cct gac cct agc gca cca gat aaa 192 Trp Arg Ile Glu Asp Tyr Tyr Asp Pro Asp Pro Ser Ala Pro Asp Lys 50 55 60 acc tac tgt aaa cgt ggc ggt ttt tta cct aac att gat ttt aat cca 240 Thr Tyr Cys Lys Arg Gly Gly Phe Leu Pro Asn Ile Asp Phe Asn Pro 65 70 75 80 atg gaa ttt ggc ttg cca cct aat att ctg gaa gta aca gat gcc tcc 288 Met Glu Phe Gly Leu Pro Pro Asn Ile Leu Glu Val Thr Asp Ala Ser 85 90 95 caa ctg ttg gca ctg to gct gct aga gat gct ttt gaa caa gct ggt 336 Gln Leu Leu Ala Leu Ile Ala Ala Arg Asp Ala Phe Glu Gln Ala Gly 100 105 110 tat ggt aaa gct tct gat aaa ttc act gca gaa ctc aaa gcc aga aca 384 Tyr Gly Lys Ala Ser Asp Lys Phe Thr Ala Glu Leu Lys Ala Arg Thr 115 120 125 gga gta cta ctt ggt gta ggg ggt gga caa aaa tta att act ccg ctt 432 Gly Val Leu Leu Gly Val Gly Gly Gly Gln Lys Leu Ile Thr Pro Leu 130 135 140 aca gga cga ttg caa tat cct atc tgg gaa aaa gca tta aga gct tgt 480 Thr Gly Arg Leu Gln Tyr Pro Ile Trp Glu Lys Ala Leu Arg Ala Cys 145 150 155 160 ggg ata gca gaa aca gat atc cct aat att gta gat aaa atg aaa aaa 528 Gly Ile Only Glu Thr Asp Ile Pro Asn Ile Val Asp Lys Met Lys Lys 165 170 175 gcc tac atc ggc tgg aat gaa at tcg ttt cca ggt atg tta ggt aat 576 Only Tyr Ile Gly Trp Asn Glu Asn Ser Phe Pro Gly Met Leu Gly Asn 180 185 190 gtt att tct ggt aga att acc aat aga ttt gac tta gga ggc atc aac 624 Val Ile Ser Gly Arg Ile Thr Asn Arg Phe Asp Leu Gly Gly Ile Asn 195 200 205 tct gtt gta gat gca gct tgc gca gct tct tg agt gcg gta aaa atg 672 Ser Val Val Asp Wing Wing Cys Wing Wing Ser Leu Ser Wing Val Lys Met 210 215 220 gct ttg agt gag tg gtt gaa ggc cgt gca gat atg atg tta aca ggt 720 Ala Leu Ser Glu Leu Val Glu Gly Arg Ala Asp Met Met Leu Thr Gly 225 230 235 240 ggt gta gat aca gat aat tct ccg ttc atg tat cta tcc ttc tcc aaa 768 Gly Val Asp Thr Asp Asn Ser Pro Phe Met Tyr Leu Ser Phe Ser Lys 245 250 255 act cct gct ttc tcc aaa tca aat gtt att agt cct ttt agt gat aaa 816 Thr Pro Ala Phe Ser Lys Ser Asn Val Ile Ser Pro Phe Ser Asp Lys 260 265 270 gcg gat ggt atg ttg att gga gaa gga tta gga atg ttg gtt ctc aaa 864 Only Asp Gly Met Leu Ile Gly Glu Gly Leu Gly Met Leu Val Leu Lys 275 280 285 aga tta gaa gat gct gaa aga gat gga gat acc att tat gct gta gtt 912 Arg Leu Glu Asp Ala Glu Arg Asp Gly Asp Thr Ile Tyr Ala Val Val 290,295,300 aaa ggt gta gga act tct gat ggg cgt ttt aaa tct gtt tat gct 960 Lys Gly Val Gly Thr Ser Ser Asp Gly Arg Phe Lys Ser Val Tyr Ala 305 310 315 320 cct aga cct tca gggc caa gca atg gct atg aat cga gcc tat gaa gaa 1008 Pro Arg Pro Ser Gly Gln Ala Met Ala Met Asn Arg Ala Tyr Glu Glu 325 330 335 gct ggt ttt gaa gcg aaa acc gtg gga ctt ata gaa gca cat ggt aca 1056 Ala Gly Phe Glu Ala Lys Thr Val Gly Leu Ile Glu Ala His Gly Thr 340 345 350 ggt acc aat gca gga gat gcc tgt gaa tta acc tct atg gga atg gta 1104 Gly Thr Asn Ala Gly Asp Ala Cys Glu Leu Thr Ser Met Gly Met Val 355 360 365 ttt ggt gct aat aac gca cat aaa caa cat att gcc cta gga acg gtt 1152 Phe Gly Ala Asn Asn Ala His Lys Gln His Ile Ala Leu Gly Thr Val 370 375 380 aaa tct caa gtt ggc cat acc aaa gct gcc gct ggt gct gct gga ctt 1200 Lys Ser Gln Val Gly His Thr Lys Ala Ala Ala Gly Ala Ala Gly Leu 385 390 395 400 atc aaa gct gtt tta gca cta cac cac aaa gtc ttg cca ccc act atc 1248 Ile Lys Ala Val Leu Ala Leu His His Lys Val Leu Pro Pro Thr Ile 405 410 415 aat gtg gag caa cct act gat aaa gta gat tta tcc caa tct cct ttg 1296 Asn Val Glu Gln Pro Thr Asp Lys Val Asp Leu Ser Gln Ser Pro Leu 420 425 430 tat atc aat aca gaa gct cga cct tgg tta acc aat gct cac cct aga Tyr Ile Asn Thr Glu Ala Arg Pro Trp Leu Thr Asn Gly His Pro Arg 435 440 445 aga gca agt gtc agt gct ttt ggt ttt ggt ggt att aat gta cac tta 1392 Arg Ala Ser Val Ser Ala Phe Gly Phe Gly Gly Ile Asn Val His Leu 450 455 460 gct tta gaa gaa tac aaa aca act cct caa caa gaa at tat aga ctt 1440 Only Leu Glu Glu Tyr Lys Thr Thr Pro Gln Glu Glu Asn Tyr Arg Leu 465 470 475 480 cac cag cct tat caa agt att g tta cag gcg gct agt cct att caa 1488 His Gln Pro Tyr Gln Ser Ile Leu Leu Gln Ala Ala Ser Pro Ile Gln 485,490,495 ttg caa gag ttg tgt caa cac cat cta acc gcc tta caa agt gag gag 1536 Leu Gln Glu Leu Cys Gln His Leu Leu Thr Ala Leu Gln Ser Glu Glu 500 505 510 aaa gaa aga gct tt tgg gct tta gca CA aca ga caa aaa acg cct 1584 Lys Glu Arg Ala Phe Trp Ala Leu Ala Gln Thr Glu Gln Lys Thr Pro 515 520 525 aca gca act gcc gct cgt ttg ggt ttt gtt gct caa gat gca gca gaa 1632 Thr Ala Thr Ala Ala Arg Leu Gly Phe Val Ala Gln Asp Ala Ala Glu 530 535 540 gcg ata gcc ttt tta gaa ttg gct ata caa caa tta aac agc aaa acc 1680 Ala Ile Ala Phe Leu Glu Leu Ala Ile Gln Gln Leu Asn Ser Lys Thr 545 550 555 560 agc gca tgg aat cat cct aag gga tta tat tat gct cct aat gca gca 1728 Ser Ala Trp Asn His Pro Lys Gly Leu Tyr Tyr Ala Pro Asn Ala Ala 565 570 575 tcc act aag gga aaa ata gtt gct cta ttt tct ggc caa ggc tcc caa 1776 Ser Thr Lys Gly Lys Ile Val Ala Leu Phe Ser Gly Gln Gly Ser Gln 580 585 590 tat gta ggc atg gga aaa gaa ctt tta aat gct ttt cct cct ttg aga 1824 Tyr Val Gly Met Gly Lys Glu Leu Leu Asn Ala Phe Pro Pro Leu Arg 595,600,605 gct aca ttt gat cag caca gac caa tta atg CA caa caa aac aga gcg 1872 Ala Thr Phe Asp Glen Asp Glen Asp Leu Met Glen Glen Asn Arg Ala 610 615 620 cct ttg tct gct act gtt tat cct att cct gtt ttt aat aaa gaa gca 1920 Pro Leu Ser Ala Thr Val Tyr Pro Ile Pro Val Phe Asn Lys Glu Ala 625 630 635 640 aaa gct CA CA CAA AAT CTA ACA GCA ACA CAG TG GCA CCT 1968 Lys Ala Glenn Lys Asn Leu Thr Ala Thr Glenn Trp Ala Glenn Pro 645,650,655 gca att ggt ggc ttt agt atg ggc tta tac aaa gtg cta aaa caa gct 2016 Ala Ile Gly Gly Phe Is Met Gly Leu Tyr Lys Val Leu Lys Gln Ala 660,665,670 ggt ttc cat gct gat ttt gca gca gga cac agc ttt gga gaa cta aca 2064 Gly Phe His Ala Asp Phe Ala Ala Gly His Ser Phe Gly Glu Leu Thr 675,680,685 gct ctt tgg gct gcg gga gta tat gat gat aag acc ttc tta caa ttg 2112 Ala Leu Trp Ala Ala Gly Val Tyr Asp Asp Lys Thr Phe Leu Gln Leu 690 695 700 gca caa gct cgt ggc gct gct atg ggc aaa gct aat ccc caa gga gat 2160 Ala Gln Ala Arg Gly Ala Ala Met Gly Lys Ala Asn Pro Gln Gly Asp 705 710 715 720 gca gga act atg ttg gcg gta aaa gca ggg caa gct caa gta gaa caa 2208 Ala Gly Thr Met Leu Ala Val Lys Ala Gly Gln Ala Gln Val Glu Gln 725 730 735 gct atc agt aac cta caa ggc gtt aaa atc gcc aat gtt aat tct ggt 2256 Ala Ile Ser Asn Leu Gln Gly Val Lys Ile Ala Asn Val Asn Ser Gly 740 745 750 aag caa gta att ctg ggc gga agc acg gcc gcc atc caa caa gct caa 2304 Lys Gln Val Ile Leu Gly Gly Ser Thr Ala Ala Ile Gln Gln Ala Gln 755 760 765 aca gct ttg caa gca caa ggc ttt tcc gtt gta cca cta caa gta tct 2352 Thr Ala Leu Gln Ala Gln Gly Phe Ser Val Val Pro Leu Gln Val Ser 770,775,780 gcg gct ttt cat aca gaa ctt gta caa cat gca CA cag cca ttt gca 2400 His Ala Ala Phe His Thr Glu Leu Val Gln His Ala Gln Gln Pro Phe Ala 785,790,795,800 CA act gta caa aat tat aat ttc CA gct cct CA att cct gtt ttt 2448 Gln Thr Val Gln Asn Tyr Asn Phe Gln Ala Pro Gln Ile Pro Val Phe 805 810 815 gct aac agt acc gca cag cct tat cct gcg cct gct gct atc caa 2496 Wing Asn Served Thr Wing Gln Pro Tyr Pro Wing Pro Wing Wing Ile Gln 820 825 830 aac atc tta caa gga ca tta tta caa cct gtt tta ttc aaa cag ca 2544 Asn With Gln Glyn With Gln Gln With Pro Val With Phe Lys Gln Gln 835 840 845 ata gag aat tta tac CA ggt ggt aga ata ttt gta gaa ttt ggc Glu Asn Leu Tyr Gln Ala Gly Gly Arg Ile Phe Val Glu Phe Gly 850 855 860 cct aaa aga gtc tta acg aac tta gtt agt gat att ctc caa aac aaa 2640 Pro Lys Arg Will Have Thr Donkey Will Be Asp And Have Gln Asn Lys 865 870 875 880 gag cat cat gcc at gct cta aat cct agt gct aag aaa gat agt gat 2688 Glu His Ala Ile Ala Leu Asn Pro Ser Ala Lys Lys Asp Ser Asp 885,890,895 ttg caa ttc cgc caa gct att tta caa cta caa gta tta ggt gta gag 2736 Leu Gln Phe Arg Gln Ala Ile Leu Gln Leu Gln Val Leu Gly Val Glu 900 905 910 tta aat aaa gta gat cct tat tat aaa aca cct gct caa cct acc gct Leu Asn Lys Val Asp Pro Tyr Tyr Lys Thr Pro Ala Gln Pro Thr Ala 915,920,925 aaa acc aaa atg aca gtg ccc tta ggt gga cac aat tat gtc agc aaa 2832 Lys Thr Lys Met Thr Val Pro Leu Gly Gly His Asn Tyr Val Ser Lys 930,935,940 ggt aca caa aaa gct tac gaa gct ctt aat gat ggc tac cag ctt 2880 Gly Thr Gln Lys Ala Tyr Glu Ala Leu Asn Asp Gly Tyr Gln Leu 945 950 955 960 tct act acc acc aat acg gta gtt caa gaa aaa att gtg gaa gtt atc 2928 Ser Thr Thr Thr Asn Thr Val Val Gln Glu Lys Ile Val Glu Val Ile 965 970 975 aaa gaa gtt cct gta gaa aaa att gta gag aaa atc ​​gta gaa gtg gaa 2976 Lys Glu Val Pro Val Glu Lys Ile Val Glu Lys Ile Val Glu Val Glu 980 985 990 gta cct agc tct tct acc tcc aat tct aac acc aat caa tca gaa gaa 3024 Val Pro Ser Ser Ser Thr Ser Asn Ser Asn Thr Asn Gln Ser Glu Glu 995 1000 1005 gaa gat att atg aac aaa gag atc att gaa aca tta aaa gct act 3069 Glu Asp Ile Met Asn Lys Glu Ile Ile Glu Thr Leu Lys Ala Thr 1010 1015 1020 gtg gaa atg gta acc gct caa caa aat aaa tct cta gaa ctt ttc 3114 Val Glu Met Val Thr Ala Gln Gln Asn Lys Ser Leu Glu Leu Phe 1025 1030 1035 cag agt ttt ttg agt gag caa aat cgc caa tct caa atg ctt atc 3159 Gln Ser Phe Leu Ser Glu Gln Asn Arg Gln Ser Gln Met Leu Ile 1040 1045 1050 caa gtc ttg gct cag caa atc aat ata gct gct caa cca caa gcg 3204 Gln Val Leu Ala Gln Gln Ile Asn Ile Ala Ala Gln Pro Gln Ala 1055 1060 1065 tta gag aac aaa cca atg tac ttg aaa gag gat aaa aaa gct tta 3249 Leu Glu Asn Lys Pro Met Tyr Leu Lys Glu Asp Lys Lys Ala Leu 1070 1075 1080 gca gaa cct aaa gta gtg act gct cct aaa gcg gaa ccc act ttc 3294 Ala Glu Pro Lys Val Val Thr Ala Pro Lys Ala Glu Pro Thr Phe 1085 1090 1095 caa caa gct cag gca cct aag cca aca cct caa aca gta gcg aca 3339 Gln Gln Ala Gln Ala Pro Lys Pro Thr Pro Gln Thr Val Ala Thr 1100 1105 1110 gct aca gta gaa acg cct act gct act act gct gac aat ggt ctt 3384 Ala Thr Val Glu Thr Pro Thr Ala Thr Thr Ala Asp Asn Gly Leu 1115 1120 1125 tct aga caa aaa cta gaa aat atc ctg ctt act gtt atc agt gat 3429 Arg Gln Lys is linked to Glu Asn and is linked to Thr Val and is linked to Asp 1130 1135 1140 aaa acg gga tac cct act gaa atg cta gag cta gac atg gat atg 3474 Lys Thr Gly Tyr Pro Thr Glu Met Leu Glu Leu Asp Met Asp Met 1145 1150 1155 gaa gca gat ttg ggt att gat tct atc aaa aga gta gaa atc ​​ttt Glu Ala Asp Leu Gly Ile Asp Ser Ile Lys Arg Val Glu Ile Phe 1160 1165 1170 ggc gct atg acc gaa gat tat cct gag gtc tct ggt gtt aat cca 3564 Gly Ala Met Thr Glu Asp Tyr Pro Glu Val Ser Gly Val Asn Pro 1175 1180 1185 cag gat tta act gac ctt aga aca ctc ggc caa att gtt gac tat Gln Asp Leu Thr Asp Leu Arg Thr Leu Gly Gln Ile Val Asp Tyr 1190 1195 1200 tta gta gaa aaa gca ggc gct ccc agt aac acc act aca tct 3654 Leu Val Glu Lys Ala Gly Ala Pro Ser Asn Thr Thr Thr Thr Ser 1205 1210 1215 gct cct gta caa caa aca gct gct cca caa ccg act cca gct gcc 3699 Ala Pro Val Gln Gln Thr Ala Ala Pro Gln Pro Thr Pro Ala Ala 1220 1225 1230 act act gct aac act aac aac ggt ctt tct aga caa aaa cta gaa 3744 Thr Thr Ala Asn Thr Asn Asn Gly Leu Ser Arg Gln Lys Leu Glu 1235 1240 1245 aat atc ctg ctt act gtt atc agt gat aaa acg gga tac cct act 3789 Asn Ile Leu Leu Thr Val Ile Ser Asp Lys Thr Gly Tyr Pro Thr 1250 1255 1260 gaa atg cta gag cta gac atg gat atg gaa gca gat ttg ggt att 3834 Glu Met Leu Glu Leu Asp Met Asp Met Glu Ala Asp Leu Gly Ile 1265 1270 1275 gat tct atc aaa aga gta gaa atc ttt ggt gct atg acc gaa gat 3879 Asp Ser Ile Lys Arg Val Glu Ile Phe Gly Ala Met Thr Glu Asp 1280 1285 1290 tat cct gag gtc tct ggt gtt aat cca caa gat tta acc gac ctt 3924 Tyr Pro Glu Val Ser Gly Val Asn Pro Gln Asp Leu Thr Asp Leu 1295 1300 1305 aga aca ctc ggc caa att gtt gac tat tta gta gaa aaa gca ggc 3969 Arg Thr Leu Gly Gln Ile Val Asp Tyr Leu Val Glu Lys Ala Gly 1310 1315 1320 gct tcc agt aac aca acc act aca cct gct cct gta cga caa acg 4014 Ala Ser Ser Asn Thr Thr Thr Thr Pro Ala Pro Val Arg Gln Thr 1325 1330 1335 gcg gct cca caa ccg act cca act gct act act gct agc aat ggt 4059 Ala Ala Pro Gln Pro Thr Pro Thr Ala Thr Thr Ala Ser Asn Gly 1340 1345 1350 ctt tct aga caa aaa cta gaa aat atc ctg ctt act gtt atc agt 4104 Leu Ser Arg Gln Lys Leu Glu Asn Ile Leu Leu Thr Val Ile Ser 1355 1360 1365 gat aaa acg gga tat cct act gaa atg cta gag cta gac atg gat 4149 Asp Lys Thr Gly Tyr Pro Thr Glu Met Leu Glu Leu Asp Met Asp 1370 1375 1380 atg gaa gcg gat tta gga att gat tct atc aaa aga gta gaa atc 4194 Met Glu Ala Asp Leu Gly Ile Asp Ser Ile Lys Arg Val Glu Ile 1385 1390 1395 ttt ggc gct atg acc gaa gat tat cct gag gtc tct ggt gtt aat 4239 Phe Gly Ala Met Thr Glu Asp Tyr Pro Glu Val Ser Gly Val Asn 1400 1405 1410 cca cag gat tta act gac ctt aga aca ctc ggc caa att gtt gac 4284 Pro Gln Asp Leu Thr Asp Leu Arg Thr Leu Gly Gln Ile Val Asp 1415 1420 1425 tat tta gta gaa aaa gca ggt gct act aat aac aca acc act aca 4329 Tyr Leu Val Glu Lys Ala Gly Ala Thr Asn Asn Thr Thr Thr Thr 1430 1435 1440 ccc gct cct gta caa caa acg gct gct cca caa tcg act cca gct 4374 Pro Ala Pro Val Gln Gln Thr Ala Ala Pro Gln Ser Thr Pro Ala 1445 1450 1455 gcc act act gct aac act aac aac ggt ctt tct aga caa aaa tta 4419 Only Thr Thr Ala Asn Thr Asn Asn Gly Leu Served as Arg Gln Lys Leu 1460 1465 1470 gaa aat atc ctg ctt act gtt atc agt gat aaa aca ggc tac cct 4464 Glu Asn With Thr Thr Val Served Asp Lys Thr Gly Tyr Pro 1475 1480 1485 act gaa atg tta gag cta gac atg gat atg gaa gcg gat ttg ggt 4509 Thr Glu Met Leu Glu Leu Asp Met Asp Met Glu Ala Asp Leu Gly 1490 1495 1500 att gat tct atc aaa aga gta gaa atc ​​ttt ggc gct atg acc gaa 4554 Ile Asp Ser Ile Ile Lys Arg Val Glu Ile Ile Phe Gly Ala Met Thr Glu 1505 1510 1515 gat tat cct gag gtc tct ggt gtt aat cca caa gat tta acc gat 4599 Asp Tyr Pro Glu Val Ser Gly Val Asn Pro Gln Asp Leu Thr Asp 1520 1525 1530 ctt aga aca ctc ggc caa atc ​​gtt gat tat tta gaa gaaaaaa gcg 4644 Arg Thr to Gly Gln Ile Val Asp Tyr to Glu Glu Lys Ala 1535 1540 1545 gat act aaa aaa aaa atc ​​cta agc TA 4671 Asp Thr Lys Lys Lys Ile Leu Ser 1550 1555 <210> 56 <211> 1556 <212> PRT <213> Aureispira marina (Aureispira marina) <400> 56 Met Asn Leu Asn His Ser Leu Arg Lys Thr Pro Val Ala Val Ile Gly 1 5 10 15 Met Ser Ala Leu Phe Ala Asp Ala Lys Thr Val Asp Gln Phe Trp Asn 20 25 30 Asn With Thr Gly Lys Asp Ser With Thr Asp Val Pro Glu Asn Arg 35 40 45 Trp Arg Ile Glu Asp Tyr Tyr Asp Pro Asp Pro Ser Ala Pro Asp Lys 50 55 60 Thr Tyr Cys Lys Arg Gly Gly Phe Leu Pro Asn Ile Asp Phe Asn Pro 65 70 75 80 Met Glu Phe Gly Leu Pro Pro Asn Ile Leu Glu Val Thr Asp Ala Ser 85 90 95 Gln Leu Leu Ala Leu Ile Ala Arg Ala Gln Ala Glu Gln Ala Gly 100 105 110 Tyr Gly Lys Ala Ser Asp Lys Phe Thr Ala Glu Leu Lys Ala Arg Thr 115 120 125 Gly Val Leu Leu Gly Val Gly Gly Gly Gln Lys Leu Ile Thr Pro Leu 130 135 140 Thr Gly Arg Leu Gln Tyr Pro Ile Trp Glu Lys Ala Leu Arg Ala Cys 145 150 155 160 Gly Ile Ala Glu Thr Asp Ile Pro Asn Ile Val Asp Lys Met Lys Lys 165 170 175 Ala Tyr Ile Gly Trp Asn Glu Asn Ser Phe Pro Gly Met Leu Gly Asn 180 185 190 Val Ile Ser Gly Arg Ile Thr Asn Arg Phe Asp Leu Gly Gly Ile Asn 195 200 205 Ser Val Val Asp Ala Ala Cys Ala Ala Ser Leu Ser Ala Val Lys Met 210 215 220 Ala Leu Ser Glu Leu Val Glu Gly Arg Ala Asp Met Met Leu Thr Gly 225 230 235 240 Gly Val Asp Thr Asp Asn Ser Pro Phe Met Tyr Leu Ser Phe Ser Lys 245 250 255 Thr Pro Ala Phe Ser Lys Ser Asn Val Ile Ser Pro Phe Ser Asp Lys 260 265 270 Ala Asp Gly Met Leu Ile Gly Glu Gly Leu Gly Met Leu Val Leu Lys 275 280 285 Arg Leu Glu Asp Ala Glu Arg Asp Gly Asp Thr Ile Tyr Ala Val Val 290 295 300 Lys Gly Val Gly Thr Ser Ser Asp Gly Arg Phe Lys Ser Val Tyr Ala 305 310 315 320 Pro Arg Pro Ser Gly Gln Ala Met Ala Met Asn Arg Ala Tyr Glu Glu 325 330 335 Ala Gly Phe Glu Ala Lys Thr Val Gly Leu Ile Glu Ala His Gly Thr 340 345 350 Gly Thr Asn Ala Gly Asp Ala Cys Glu Leu Thr Ser Met Gly Met Val 355 360 365 Phe Gly Ala Asn Asn Ala His Lys Gln His Ile Ala Leu Gly Thr Val 370 375 380 Lys Ser Gln Val Gly His Thr Lys Ala Ala Ala Gly Ala Ala Gly Leu 385 390 395 400 Ile Lys Ala Val Leu Ala Leu His His Lys Val Leu Pro Pro Thr Ile 405 410 415 Asn Val Glu Gln Pro Thr Asp Lys Val Asp Leu Ser Gln Ser Pro Leu 420 425 430 Tyr Ile Asn Thr Glu Ala Arg Pro Trp Leu Thr Asn Gly His Pro Arg 435 440 445 Arg Ala Ser Val Ser Ala Phe Gly Phe Gly Gly Ile Asn Val His Leu 450 455 460 Ala Leu Glu Glu Tyr Lys Thr Thr Pro Gln Gln Glu Asn Tyr Arg Leu 465 470 475 480 His Gln Pro Tyr Gln Ser Ile Leu Leu Gln Ala Ala Ser Pro Ile Gln 485 490 495 Leu Gln Glu Leu Cys Gln His His Leu Thr Ala Leu Gln Ser Glu Glu 500 505 510 Lys Glu Arg Ala Phe Trp Ala Leu Ala Gln Thr Glu Gln Lys Thr Pro 515 520 525 Thr Ala Thr Ala Ala Arg Leu Gly Phe Val Ala Gln Asp Ala Ala Glu 530 535 540 Ala Ile Ala Phe Leu Glu Leu Ala Ile Gln Gln Leu Asn Ser Lys Thr 545 550 555 560 Ser Ala Trp Asn His Pro Lys Gly Leu Tyr Tyr Ala Pro Asn Ala Ala 565 570 575 Ser Thr Lys Gly Lys Ile Val Ala Leu Phe Ser Gly Gln Gly Ser Gln 580 585 590 Tyr Val Gly Met Gly Lys Glu Leu Leu Asn Ala Phe Pro Pro Leu Arg 595 600 605 Ala Thr Phe Asp Gln Gln Asp Gln Leu Met Gln Gln Gln Asn Arg Ala 610 615 620 Pro Leu Ser Ala Thr Val Tyr Pro Ile Pro Val Phe Asn Lys Glu Ala 625 630 635 640 Lys Ala Gln Gln Gln Lys Asn Leu Thr Ala Thr Gln Trp Ala Gln Pro 645 650 655 Ala Ile Gly Gly Phe Ser Met Gly Leu Tyr Lys Val Leu Lys Gln Ala 660 665 670 Gly Phe His Ala Asp Phe Ala Ala Gly His Ser Phe Gly Glu Leu Thr 675 680 685 Ala Leu Trp Ala Ala Gly Val Tyr Asp Asp Lys Thr Phe Leu Gln Leu 690 695 700 Ala Gln Ala Arg Gly Ala Ala Met Gly Lys Ala Asn Pro Gln Gly Asp 705 710 715 720 Ala Gly Thr Met Leu Ala Val Lys Ala Gly Gln Ala Gln Val Glu Gln 725 730 735 Ala Ile Ser Asn Leu Gln Gly Val Lys Ile Ala Asn Val Asn Ser Gly 740 745 750 Lys Gln Val Ile Leu Gly Gly Ser Thr Ala Ala Ile Gln Gln Ala Gln 755 760 765 Thr Ala Leu Gln Ala Gln Gly Phe Ser Val Val Pro Leu Gln Val Ser 770 775 780 Ala Ala Phe His Thr Glu Leu Val Gln His Ala Gln Gln Pro Phe Ala 785 790 795 800 Gln Thr Val Gln Asn Tyr Asn Phe Gln Ala Pro Gln Ile Pro Val Phe 805 810 815 Ala Asn Ser Thr Ala Gln Pro Tyr Pro Ala Ala Pro Ala Ala Ile Gln 820 825 830 Asn Ile Leu Gln Gly Gln Leu Leu Gln Pro Val Leu Phe Lys Gln Gln 835 840 845 Ile Glu Asn Leu Tyr Gln Ala Gly Gly Arg Ile Phe Val Glu Phe Gly 850 855 860 Pro Lys Arg Val Leu Thr Asn Leu Val Ser Asp Ile Leu Gln Asn Lys 865 870 875 880 Glu His His Ala Ile Ala Leu Asn Pro Ser Ala Lys Lys Asp Ser Asp 885 890 895 Leu Gln Phe Arg Gln Ala Ile Leu Gln Leu Gln Val Leu Gly Val Glu 900 905 910 Leu Asn Lys Val Asp Pro Tyr Tyr Lys Thr Pro Ala Gln Pro Thr Ala 915 920 925 Lys Thr Lys Met Thr Val Pro Leu Gly Gly His Asn Tyr Val Ser Lys 930 935 940 Gly Thr Gln Lys Ala Tyr Tyr Glu Ala Leu Asn Asp Gly Tyr Gln Leu 945 950 955 960 Ser Thr Thr Thr Asn Thr Val Val Gln Glu Lys Ile Val Glu Val Ile 965 970 975 Lys Glu Val Pro Val Glu Lys Ile Val Glu Lys Ile Val Glu Val Glu 980 985 990 Val Pro Ser Ser Ser Thr Ser Asn Ser Asn Thr Asn Gln Ser Glu Glu 995 1000 1005 Glu Asp Ile Met Asn Lys Glu Ile Ile Glu Thr Leu Lys Ala Thr 1010 1015 1020 Val Glu Met Val Thr Ala Gln Gln Asn Lys Ser Leu Glu Leu Phe 1025 1030 1035 Gln Ser Phe Leu Ser Glu Gln Asn Arg Gln Ser Gln Met Leu Ile 1040 1045 1050 Gln Val Leu Ala Gln Gln Ile Asn Ile Ala Ala Gln Pro Gln Ala 1055 1060 1065 Leu Glu Asn Lys Pro Met Tyr Leu Lys Glu Asp Lys Lys Ala Leu 1070 1075 1080 Ala Glu Pro Lys Val Val Thr Ala Pro Lys Ala Glu Pro Thr Phe 1085 1090 1095 Gln Gln Ala Gln Ala Pro Lys Pro Thr Pro Gln Thr Val Ala Thr 1100 1105 1110 Ala Thr Val Glu Thr Pro Thr Ala Thr Thr Ala Asp Asn Gly Leu 1115 1120 1125 Ser Arg Gln Lys Leu Glu Asn Ile Leu Leu Thr Val Ile Ser Asp 1130 1135 1140 Lys Thr Gly Tyr Pro Thr Glu Met Leu Glu Leu Asp Met Asp Met 1145 1150 1155 Glu Ala Asp Leu Gly Ile Asp Ser Ile Lys Arg Val Glu Ile Phe 1160 1165 1170 Gly Ala Met Thr Glu Asp Tyr Pro Glu Val Ser Gly Val Asn Pro 1175 1180 1185 Gln Asp Leu Thr Asp Leu Arg Thr Leu Gly Gln Ile Val Asp Tyr 1190 1195 1200 Leu Val Glu Lys Ala Gly Ala Pro Ser Asn Thr Thr Thr Thr Ser 1205 1210 1215 Ala Pro Val Gln Gln Thr Ala Ala Pro Gln Pro Thr Pro Ala Ala 1220 1225 1230 Thr Thr Ala Asn Thr Asn Asn Gly Leu Ser Arg Gln Lys Leu Glu 1235 1240 1245 Asn Ile Leu Leu Thr Val Ile Ser Asp Lys Thr Gly Tyr Pro Thr 1250 1255 1260 Glu Met Leu Glu Leu Asp Met Asp Met Glu Ala Asp Leu Gly Ile 1265 1270 1275 Asp Ser Ile Lys Arg Val Glu Ile Phe Gly Ala Met Thr Glu Asp 1280 1285 1290 Tyr Pro Glu Val Ser Gly Val Asn Pro Gln Asp Leu Thr Asp Leu 1295 1300 1305 Arg Thr Leu Gly Gln Ile Val Asp Tyr Leu Val Glu Lys Ala Gly 1310 1315 1320 Ala Ser Ser Asn Thr Thr Thr Thr Pro Ala Pro Val Arg Gln Thr 1325 1330 1335 Ala Ala Pro Gln Pro Thr Pro Thr Ala Thr Thr Ala Ser Asn Gly 1340 1345 1350 Leu Ser Arg Gln Lys Leu Glu Asn Ile Leu Leu Thr Val Ile Ser 1355 1360 1365 Asp Lys Thr Gly Tyr Pro Thr Glu Met Leu Glu Leu Asp Met Asp 1370 1375 1380 Met Glu Ala Asp Leu Gly Ile Asp Ser Ile Lys Arg Val Glu Ile 1385 1390 1395 Phe Gly Ala Met Thr Glu Asp Tyr Pro Glu Val Ser Gly Val Asn 1400 1405 1410 Pro Gln Asp Leu Thr Asp Leu Arg Thr Leu Gly Gln Ile Val Asp 1415 1420 1425 Tyr Leu Val Glu Lys Ala Gly Ala Thr Asn Asn Thr Thr Thr Thr 1430 1435 1440 Pro Ala Pro Val Gln Gln Thr Ala Ala Pro Gln Ser Thr Pro Ala 1445 1450 1455 Ala Thr Thr Ala Asn Thr Asn Asn Gly Leu Ser Arg Gln Lys Leu 1460 1465 1470 Glu Asn Ile Leu Leu Thr Val Ile Ser Asp Lys Thr Gly Tyr Pro 1475 1480 1485 Thr Glu Met Leu Glu Leu Asp Met Asp Met Glu Ala Asp Leu Gly 1490 1495 1500 Ile Asp Ser Ile Ile Lys Arg Val Glu Ile Ile Phe Gly Ala Met Thr Glu 1505 1510 1515 Asp Tyr Pro Glu Val Ser Gly Val Asn Pro Gln Asp Leu Thr Asp 1520 1525 1530 Arg Thr and Gly Gln Ile Val Asp Tyr and Glu Glu Lys Ala 1535 1540 1545 Asp Thr Lys Lys Lys Ile Leu Ser 1550 1555 <210> 57 <211> 2406 <212> DNA <213> Aureispira marina (Aureispira marina) <220> <221> CDS <222> (1)..(2406) <400> 57 atg cct caa cca gat tac cta gac ttc acc ctc cct tcc acc cat att 48 Met Pro Gln Pro Asp Tyr Leu Asp Phe Thr Leu Pro Ser Thr His Ile 1 5 10 15 gcc ctt ctt aca aat gac ggt tct acg ctt aca caa gcc gtg tac aaa 96 Only Thr Thr Asn Asp Gly Ser Thr Thr Thr Gln Only Val Tyr Lys 20 25 30 gcg ctc tta gcc aaa ggg aat aaa gta gtt gtt cta aat tta gca gt 144 Ala Leu Leu Ala Lys Gly Asn Lys Val Val Val Leu Asn Leu Ala Gly 35 40 45 att tct act cct ttt tct gag aat agc ata agc ttg gcc agt aac tct 192 I'll Be Thr Pro Phe I'll Be Glu Asn I'll Be Leu Ala I'll Be Asn 50 55 60 gat gaa gcc atc aaa gca gct ata gct acc atc aaa aac caa tac ggt 240 Asp Glu Only With Lys Only Only Only Thr Only With Lys Asn Gln Tyr Gly 65 70 75 80 act gta gga aca ttt ata cac cta cac cca cac tta acg ttc agc aat 288 Thr Val Gly Thr Phe Ile His Leu His Pro His Leu Thr Phe Ser Asn 85 90 95 cac caa ttt gca caa cat ttt gac tta gaa aga gac ctt ctc aaa gga 336 His Gln Phe Ala Gln His Phe Asp Leu Glu Arg Asp Leu Leu Lys Gly 100 105 110 atc ttc ctc att gct aag cac att ca gca gat tta aca gct tta ggc 384 Ile Phe Leu Ile Ala Lys His Ile Gln Ala Asp Leu Thr Ala Leu Gly 115 120 125 caa aaa caa aga gcc aat ttc ttg acc ctt aca cga tta gat gga aaa 432 Gln Lys Gln Arg Ala Asn Phe Leu Thr Leu Thr Arg Leu Asp Gly Lys 130 135 140 cta ggt tta ggg aaa aga aat aac acc tct gta gtc gga gga gga tta 480 Leu Gly Leu Gly Lys Arg Asn Asn Thr Ser Val Val Gly Gly Gly Leu 145 150 155 160 agt ggc ttg gta aaa tgc tta aac tta gaa tgg tcc tct gta ttt tgt 528 Ser Gly Leu Val Lys Cys Leu Asn Leu Glu Trp Ser Ser Val Phe Cys 165 170 175 cga gcc att gat gcc caa cca gaa tgg tca gat gag caa tta gct caa 576 Arg Ala Ile Asp Ala Gln Pro Glu Trp Ser Asp Glu Gln Leu Ala Gln 180 185 190 cag tta atg caa gaa tta cat gac ccc aac aga gga gtg gtt gaa gta 624 Gln Leu Met Gln Glu Leu His Asp Pro Asn Arg Gly Val Val Glu Val 195 200 205 gca ctt tca gag gaa ggc aga gca acg cta ata gcc acc aat gac cct 672 Ala Leu Ser Glu Glu Gly Arg Ala Thr Leu Ile Ala Thr Asn Asp Pro 210 215 220 gta aaa gca gga caa cat atc aca aca gcc gtt aca gag aac tct gta 720 Val Lys Ala Gly Gln His Ile Thr Thr Ala Val Thr Glu Asn Ser Val 225 230 235 240 ttc tta gta agt ggt gga gcc cgt ggt gtg aca gcc aat tgt gtg att 768 Phe Leu Val Ser Gly Gly Ala Arg Gly Val Thr Ala Asn Cys Val Ile 245 250 255 gaa atg gct aaa gcc ttt cag tgt aaa ttt att tta cta gga agg tca 816 Glu Met Ala Lys Ala Phe Gln Cys Lys Phe Ile Leu Leu Gly Arg Ser 260 265 270 gat gcc agt gta gaa ctc cca gat ttt gcc aaa aac gaa agt gaa gaa 864 Asp Ala Ser Val Glu Leu Pro Asp Phe Ala Lys Asn Glu Ser Glu Glu 275 280 285 ggt gcc cta aaa aga gcc att atg tta gac atg aag gca aaa gga caa 912 Gly Ala Leu Lys Arg Ala Ile Met Leu Asp Met Lys Ala Lys Gly Gln 290 295 300 caa cct aac tta gca gaa gtt aaa aaa atg ttt aat agc att att gct 960 Gln Pro Asn Leu Ala Glu Val Lys Lys Met Phe Asn Ser Ile Ile Ala 305 310 315 320 aaa aaa gaa att gaa gac acc ctt caa gcc att gag aaa gca gga gga 1008 Lys Lys Glu Ile Glu Asp Thr Leu Gln Ala Ile Glu Lys Ala Gly Gly 325 330 335 gaa gcc ata tac atc aaa ggt gat gta acc aaa gtc tct agc gtc aag 1056 Glu Ala Ile Tyr Ile Lys Gly Asp Val Thr Lys Val Ser Ser Val Lys 340 345 350 cct caa tta cta gca atc ​​aca caa caa tgg gga cca att aca ggg gta 1104 Pro Gln Leu Leu Ala Ile Thr Gln Gln Trp Gly Pro Ile Thr Gly Val 355 360 365 ttg cat gga gca gga aga tta gca gat aaa tac att caa gat aaa agt 1152 Leu His Gly Ala Gly Arg Leu Ala Asp Lys Tyr Ile Gln Asp Lys Ser 370 375 380 gag caa gat ttc atc aat gtg ctt tct gtt aaa ttg gac ggt tta cta 1200 Glu Gln Asp Phe Ile Asn Val Leu Ser Val Lys Leu Asp Gly Leu Leu 385 390 395 400 acc ttg cta caa tgt gtc aac cta caa aaa tta gaa cat ttg att ctc 1248 Thr Leu Leu Gln Cys Val Asn Leu Gln Lys Leu Glu His Leu Ile Leu 405 410 415 ttc tct tct gtt gct ggt ttt tat ggt aat gta gga caa aca gat tat 1296 Phe Ser Ser Val Ala Gly Phe Tyr Gly Asn Val Gly Gln Thr Asp Tyr 420 425 430 gcc att gct aat gaa att cta agc aaa gca gcc cac caa ttc aga acc 1344 Ala Ile Ala Asn Glu Ile Leu Ser Lys Ala Ala His Gln Phe Arg Thr 435 440 445 aat cat cca aat acc caa gtt tct gcc atc aat tgg ggg gct tgg gat 1392 Asn His Pro Asn Thr Gln Val Ser Ala Ile Asn Trp Gly Ala Trp Asp 450 455 460 gca gga atg gtg agc gaa gcc cta aag aaa aaa ttt gaa gca atg ggc 1440 Ala Gly Met Val Ser Glu Ala Leu Lys Lys Phe Glu Ala Met Gly 465 470 475 480 gtt tct ttg gtt aat agc gta ggc ggc cct gct tta ttg gta aat gaa 1488 Val Ser Leu Val Asn Ser Val Gly Gly Pro Ala Leu Leu Val Asn Glu 485,490,495 ctt aat gtt gct tat gcc aat caa cca cag gtt att ttg ggc ggc act 1536 Leu Asn Val Ala Tyr Ala Asn Gln Pro Gln Val Ile Leu Gly Gly Thr 500 505 510 ctg cct gct gcg att tcc tat aca gaa ggc gca tta aca act cat gaa 1584 Leu Pro Ala Ala Has Tyr Thr Glu Gly Ala Leu Thr Thr His Glu 515,520,525 ata tac cga aca tta gaa cct tct gag at cct ttc tta caa cat cat Ile Tyr Arg Thr Leu Glu Pro Ser Glu Asn Pro Phe Leu Gln His 530 535 540 gtt att caa ggg caa gcc gtt ttg cca gtg gta agt gct atg ggc tgg 1680 Val Ile Gln Gly Gln Ala Val Leu Pro Val Val Ser Ala Met Gly Trp 545 550 555 560 atg gcg act act gct gaa caa at ttc cct gat ttt aga aca ttt gaa 1728 Met Ala Thr Ala Glu Gln Ile Phe Pro Asp Phe Arg Thr Phe Glu 565,570,575 gta gcc aat aca aag tta ttc aaa ggg cta gta ttt gat ggt aat caa Val Ala Asn Thr Lys Leu Phe Lys Gly Leu Val Phe Asp Gly Asn Gln 580,585,590 cct aaa gct ttc gta act act tg gta gaaaa gaaaa aat gct tcg 1824 Pro Lys Ala Phe Val Thr Thr Leu Val Glu Lys Glu Lys Asn Ala Ser 595,600,605 acc att gta cta gaa gca acc att agc CA gca cct acc gct aaa 1872 Thr Ile Val Leads To Glu On Thr Ile To Be Gln On The Pro Thr On The Lys 610 615 620 ttg cct act tt cac tac aaa gct acg ctt acca cta aaa gcc aaa aat 1920 Leu Pro Thr Phe His Tyr Lys Ala Thr Leu Thr Leu Lys Ala Lys Asn 625 630 635 640 tta ggt tta gaa ca cct acc ttt gaa gct act tta agc agt gat tat 1968 Leu Gly Leu Glu Gln Pro Thr Phe Glu Ala Thr Leu Ser Ser Asp Tyr 645 650 655 acg gct agt tca ggt gca gtt ttg tat gag aat ggc gcc ctt ttt cac 2016 Thr Ala Ser Ser Gly Ala Val Leu Tyr Glu Asn Gly Ala Leu Phe His 660 665 670 ggg aaa cac ttc caa ggt att gag gag att tta gat tgg aat gaa cac 2064 Gly Lys His Phe Gln Gly Ile Glu Glu Ile Leu Asp Trp Asn Glu His 675 680 685 caa att gtc tta aaa tgt aaa gca cct caa gtt tca aga gca gaa caa 2112 Gln Ile Val Leu Lys Cys Lys Ala Pro Gln Val Ser Arg Ala Glu Gln 690 695 700 ggc caa ttc cca atc ​​tta gga gtg aat acc ttc ttt gca gac att caa 2160 Gly Gln Phe Pro Ile Leu Gly Val Asn Thr Phe Phe Ala Asp Ile Gln 705 710 715 720 tac caa ggg atg gtt att tgg gta caa aaa tac cat gat gga gcc aaa 2208 Tyr Gln Gly Met Val Ile Trp Val Gln Lys Tyr His Asp Gly Ala Lys 725 730 735 tct ttg cct tta gct aca gaa agt gcg caa ctc ttt gct cct gtt cct 2256 Ser Leu Pro Leu Ala Thr Glu Ser Ala Gln Leu Phe Ala Pro Val Pro 740,745,750 ttt gac aaa gaa tta ttg gtt cat att gaa att gta gaa gat act cct 2304 Phe Asp Lys Glu Leu Leu Val His Ile Glu Ile Val Glu Asp Thr Pro 755,760,765 ttc aaa atg gta gcc aac tgc act act tat gat gct gat gga aaa gta 2352 Phe Lys Met Val Ala Asn Cys Thr Thr Tyr Asp Ala Asp Gly Lys Val 770,775,780 tat cta tct act aga aat gct gct gtt act gtt tct aag gaa cta act Tyr Leu Will Be Thr Arg Asn Ala Ala Val Thr Will Be Lys Glu Leu Thr 785,790,795,800 Click on tag 2406 Trp <210> 58 <211> 801 <212> PRT <213> Aureispira marina (Aureispira marina) <400> 58 Met Pro Gln Pro Asp Tyr Leu Asp Phe Thr Leu Pro Ser Thr His Ile 1 5 10 15 Ala Leu Leu Thr Asn Asp Gly Ser Thr Leu Thr Gln Ala Val Tyr Lys 20 25 30 Ala Leu Leu Ala Lys Gly Asn Lys Val Val Val Leu Asn Leu Ala Gly 35 40 45 Ile Ser Thr Pro Phe Ser Glu Asn Ser Ile Ser Leu Ala Ser Asn Ser 50 55 60 Asp Glu Ala Ile Lys Ala Ala Ile Ala Thr Ile Lys Asn Gln Tyr Gly 65 70 75 80 Thr Val Gly Thr Phe Ile His Leu His Pro His Leu Thr Phe Ser Asn 85 90 95 His Gln Phe Ala Gln His Phe Asp Leu Glu Arg Asp Leu Leu Lys Gly 100 105 110 Ile Phe Leu Ile Ala Lys His Ile Gln Ala Asp Leu Thr Ala Leu Gly 115 120 125 Gln Lys Gln Arg Ala Asn Phe Leu Thr Leu Thr Arg Leu Asp Gly Lys 130 135 140 Leu Gly Leu Gly Lys Arg Asn Asn Thr Ser Val Val Gly Gly Gly Leu 145 150 155 160 Ser Gly Leu Val Lys Cys Leu Asn Leu Glu Trp Ser Ser Val Phe Cys 165 170 175 Arg Ala Ile Asp Ala Gln Pro Glu Trp Ser Asp Glu Gln Leu Ala Gln 180 185 190 Gln Leu Met Gln Glu Leu His Asp Pro Asn Arg Gly Val Val Glu Val 195 200 205 Ala Leu Ser Glu Glu Gly Arg Ala Thr Leu Ile Ala Thr Asn Asp Pro 210 215 220 Val Lys Ala Gly Gln His Ile Thr Thr Ala Val Thr Glu Asn Ser Val 225 230 235 240 Phe Leu Val Ser Gly Gly Ala Arg Gly Val Thr Ala Asn Cys Val Ile 245 250 255 Glu Met Ala Lys Ala Phe Gln Cys Lys Phe Ile Leu Leu Gly Arg Ser 260 265 270 Asp Ala Ser Val Glu Leu Pro Asp Phe Ala Lys Asn Glu Ser Glu Glu 275 280 285 Gly Ala Leu Lys Arg Ala Ile Met Leu Asp Met Lys Ala Lys Gly Gln 290 295 300 Gln Pro Asn Leu Ala Glu Val Lys Lys Met Phe Asn Ser Ile Ile Ala 305 310 315 320 Lys Lys Glu Ile Glu Asp Thr Leu Gln Ala Ile Glu Lys Ala Gly Gly 325 330 335 Glu Ala Ile Tyr Ile Lys Gly Asp Val Thr Lys Val Ser Ser Val Lys 340 345 350 Pro Gln Leu Leu Ala Ile Thr Gln Gln Trp Gly Pro Ile Thr Gly Val 355 360 365 Leu His Gly Ala Gly Arg Leu Ala Asp Lys Tyr Ile Gln Asp Lys Ser 370 375 380 Glu Gln Asp Phe Ile Asn Val Leu Ser Val Lys Leu Asp Gly Leu Leu 385 390 395 400 Thr Leu Leu Gln Cys Val Asn Leu Gln Lys Leu Glu His Leu Ile Leu 405 410 415 Phe Ser Ser Val Ala Gly Phe Tyr Gly Asn Val Gly Gln Thr Asp Tyr 420 425 430 Ala Ile Ala Asn Glu Ile Leu Ser Lys Ala Ala His Gln Phe Arg Thr 435 440 445 Asn His Pro Asn Thr Gln Val Ser Ala Ile Asn Trp Gly Ala Trp Asp 450 455 460 Ala Gly Met Val Ser Glu Ala Leu Lys Lys Lys Phe Glu Ala Met Gly 465 470 475 480 Val Ser Leu Val Asn Ser Val Gly Gly Pro Ala Leu Leu Val Asn Glu 485 490 495 Leu Asn Val Ala Tyr Ala Asn Gln Pro Gln Val Ile Leu Gly Gly Thr 500 505 510 Leu Pro Ala Ala Ile Ser Tyr Thr Glu Gly Ala Leu Thr Thr His Glu 515 520 525 Ile Tyr Arg Thr Leu Glu Pro Ser Glu Asn Pro Phe Leu Gln His His 530 535 540 Val Ile Gln Gly Gln Ala Val Leu Pro Val Val Ser Ala Met Gly Trp 545 550 555 560 Met Ala Thr Thr Ala Glu Gln Ile Phe Pro Asp Phe Arg Thr Phe Glu 565 570 575 Val Ala Asn Thr Lys Leu Phe Lys Gly Leu Val Phe Asp Gly Asn Gln 580 585 590 Pro Lys Ala Phe Val Thr Thr Leu Val Glu Lys Glu Lys Asn Ala Ser 595 600 605 Thr Ile Val Leu Glu Ala Thr Ile Ser Ser Gln Ala Pro Thr Ala Lys 610 615 620 Leu Pro Thr Phe His Tyr Lys Ala Thr Leu Thr Leu Lys Ala Lys Asn 625 630 635 640 Leu Gly Leu Glu Gln Pro Thr Phe Glu Ala Thr Leu Ser Ser Asp Tyr 645 650 655 Thr Ala Ser Ser Gly Ala Val Leu Tyr Glu Asn Gly Ala Leu Phe His 660 665 670 Gly Lys His Phe Gln Gly Ile Glu Glu Ile Leu Asp Trp Asn Glu His 675 680 685 Gln Ile Val Leu Lys Cys Lys Ala Pro Gln Val Ser Arg Ala Glu Gln 690 695 700 Gly Gln Phe Pro Ile Leu Gly Val Asn Thr Phe Phe Ala Asp Ile Gln 705 710 715 720 Tyr Gln Gly Met Val Ile Trp Val Gln Lys Tyr His Asp Gly Ala Lys 725 730 735 Ser Leu Pro Leu Ala Thr Glu Ser Ala Gln Leu Phe Ala Pro Val Pro 740 745 750 Phe Asp Lys Glu Leu Leu Val His Ile Glu Ile Val Glu Asp Thr Pro 755 760 765 Phe Lys Met Val Ala Asn Cys Thr Thr Tyr Asp Ala Asp Gly Lys Val 770 775 780 Tyr Leu Ser Thr Arg Asn Ala Ala Val Thr Val Ser Lys Glu Leu Thr 785 790 795 800 Trp <210> 59 <211> 6726 <212> DNA <213> Aureispira marina (Aureispira marina) <220> <221> CDS <222> (1)..(6726) <400> 59 atg aaa ata gca atc ​​ata ggc tta tct ggt ttg ttt cca ggc tct tct 48 Met Lys Ile Ala Ile Gly Leu Ser Gly Leu Phe Pro Gly Ser Ser 1 5 10 15 act aat gaa gaa ttt tgg caa aat ctc cta gac gaaa gac cta acc 96 Thr Asn Glu Glu Phe Trp Gln Asn With Asp Glu Lys Asp With Thr 20 25 30 aat cta gcc aac tta gaa gat ttt gga gct gac cct gca ctt ttt tat 144 Asn Leu Ala Asn Glu Asp Phe Gly Ala Asp Pro Ala Leu Phe Tyr 35 40 45 gaa gat aaa aaa gga gca gta gac cga tgt tac tcc ctc cga gga ggt 192 Glu Asp Lys Gly Ala Val Asp Arg Cys Tyr Ser Leu Arg Gly Gly 50 55 60 tat atc agg gat ttt gac ttt gac cct aca ggc tac caa ttg tct gct 240 Tyr Ile Arg Asp Phe Asp Phe Asp Pro Thr Gly Tyr Gln Leu Ser Ala 65 70 75 80 gac ttt ttg gcc caa gac aaa tta tac caa tgg tct ttg tat gtc 288 Asp Phe With Gln Gln Asp Lys With Gln Tyr Trp Ser With Val Tyr 85 90 95 gcc aaa acg gcc tta gaa gaa agt ggc tat gcc cac aac aaa gaa gtt 336 Ala Lys Thr Ala Leu Glu Glu Ser Gly Tyr Ala His Asn Lys Glu Val 100 105 110 tta gca aaa tgt ggc cta att cta ggc aac ctt tct ttc cca aca gga Leu Ala Lys Cys Gly Leu Ile Leu Gly Asn Leu Ser Phe Pro Thr Gly 115 120 125 tct tct cac aaa tta cta gcc gac tta tat acc aaa aca aca gaa aaa 432 Ser Ser His Lys Leu Ala Asp Leu Tyr Thr Lys Thr Thr Glu Lys 130 135 140 gca tta caa gaa tta cta gaa gac aaa aac ttc aaa atc ​​cct gct agt 480 Ala Leu Gln Glu Leu Leu Glu Asp Lys Asn Phe Lys Ile Pro Ala Ser 145 150 155 160 cag tta cct att cct aat aat gag gtc ttg gca gat aca cca tct caa 528 Gln Leu Pro Ile Pro Asn Asn Glu Val Leu Ala Asp Thr Pro Ser Gln 165 170 175 atg gta gcc aaa ggt ttg ggc ttg gga gga gga cac tat gct ttg gat 576 Met Val Ala Lys Gly Leu Gly Leu Gly Gly Gly His Tyr Ala Leu Asp 180 185 190 gca gct tgt gca aca tcc ttg tat gcc atc aaa cta gct tgt gac gaa 624 Ala Ala Cys Ala Thr Ser Leu Tyr Ala Ile Lys Leu Ala Cys Asp Glu 195 200 205 ttg att aca ggg aaa gct gat ttg atg ttg gca ggt gcg gtt tgt ggc 672 Leu Ile Thr Gly Lys Ala Asp Leu Met Leu Ala Gly Ala Val Cys Gly 210 215 220 tcc gat caa ctg ttt atc cac atg ggc ttt tct att ttc cat gcc tat 720 Ser Asp Gln Leu Phe Ile His Met Gly Phe Ser Ile Phe His Ala Tyr 225 230 235 240 gct cct cat gga gaa aag ttt gca cct ctg gat aaa gca tct gga ggt 768 Ala Pro His Gly Glu Lys Phe Ala Pro Leu Asp Lys Ala Ser Gly Gly 245 250 255 tta gtt tcg gca gaa gga gct gga atg gtg gtc tta aaa aga cta gag 816 Leu Val Ser Ala Glu Gly Ala Gly Met Val Val Leu Lys Arg Leu Glu 260 265 270 gat gca gaa aga gat ggc gat aat att ttg gga ttg at ggt ggc at 864 Asp Ala Glu Arg Asp Gly Asp Asn Ile Leu Gly Leu Ile Gly Gly Ile 275 280 285 ggt ttg tcc aat gat ggc agt ggc aaa ttc tta ttg agc cct aat cct 912 Gly Leu Ser Asn Asp Gly Ser Gly Lys Phe Leu Leu Ser Pro Asn Pro 290 295 300 aaa ggg caa aga tta gct ttt gaa aga gct tat gat tta gaa gaa gta 960 Lys Gly Gln Arg Leu Ala Phe Glu Arg Ala Tyr Asp Leu Glu Glu Val 305 310 315 320 tta cca caa aat acc tcc tac cta gaa tgt cat gct aca gga acc ccc 1008 Leu Pro Gln Asn Thr Ser Tyr Leu Glu Cys His Ala Thr Gly Thr Pro 325 330 335 ttg gga gat gtt aca gaa atg aat tcc att tct gat ttc ttt gcc caa 1056 Leu Gly Asp Val Thr Glu Met Asn Ser Ile Ser Asp Phe Phe Ala Gln 340 345 350 cac caa acc aaa ccc ttg cta ggc tct gtc aaa tcc aat atg ggg cat 1104 His Gln Thr Lys Pro Leu Leu Gly Ser Val Lys Ser Asn Met Gly His 355 360 365 tta ctg aca gca gca ggt atg tct ggt tta ttc aaa gtc ctg ctc tcc 1152 Leu Leu Thr Ala Ala Gly Met Ser Gly Leu Phe Lys Val Leu Leu Ser 370 375 380 atg caa aaa ggg att att cct ccc aat atc aat ttg gaa agt gca gta 1200 Met Gln Lys Gly Ile Ile Pro Pro Asn Ile Asn Leu Glu Ser Ala Val 385 390 395 400 caa gcc aac aat caa tgg att cag gat gag caa att atc aaa aaa act 1248 Gln Ala Asn Asn Gln Trp Ile Gln Asp Glu Gln Ile Ile Lys Lys Thr 405 410 415 act cct tgg aag ggc gac caa gca ggt atc aat tcc ttt ggt ttt ggg 1296 Thr Pro Trp Lys Gly Asp Gln Ala Gly Ile Asn Ser Phe Gly Phe Gly 420 425 430 gga acc acc aat gca cac atg gtc gtt CA aaa ccc acc agc tca aca tta 1344 Gly Thr Asn Ala His Met Val Val Gln Lys Pro Thr Ser Ser Thr Leu 435 440 445 aaa gaa aag aaa gcg tac caa gcc CA gaa ttg ctt cct tta gca att 1392 Lys Glu Lys Lys Ala Tyr Gln Ala Gln Glu Leu Leu Pro Leu Ala Ile 450 455 460 gta ggc atg gat gct cat ttt ggt agt tgt gag aat tta gaa gat ttt 1440 Val Gly Met Asp Ala His Phe Gly Ser Cys Glu Asn Leu Glu Asp Phe 465 470 475 480 tat gct gct att tat aat ggg aac CA gat ttc aaa cca ctt cct ccc 1488 Tyr Ala Ala Ile Tyr Asn Gly Asn Gln Asp Phe Lys Pro Leu Pro Pro 485,490,495 aaa aga tgg aaa ggc ttt gat gct gat caa gat ttg cta aaa aga tat Lys Arg Trp Lys Gly Phe Asp Ala Asp Gln Asp Leu Leu Lys Arg Tyr 500 505 510 ggc ttt aag gat ggc tta gct cct aaa ggt gcc tac att gac caa ttt 1584 Gly Phe Lys Asp Gly Leu Ala Pro Lys Gly Ala Tyr Ile Asp Gln Phe 515 520 525 gat att gat ctg ttg agg tat aaa att cag cca aaa gaa gca gaa aca 1632 Asp Ile Asp Leu Leu Arg Tyr Lys Ile Gln Pro Lys Glu Ala Glu Thr 530 535 540 cta gag cca caa caa gcc ctc to cta aaa gta gca gac aaa gct tta 1680 Leu Glu Pro Gln Gln Ala Leu Ile Leu Lys Val Ala Asp Lys Ala Leu 545 550 555 560 cag gat gct caa atc ​​agt cct agc caa aat to gct gta tta to gcc 1728 Gln Asp Ala Gln Ile Ser Pro Ser Gln Asn Ile Ala Val Leu Ile Ala 565 570 575 atg gaa tct gaa ttg gct att cat cat tat ttg gca aga tgg gat agt 1776 Met Glu Ser Glu Leu Ala Ile His His Tyr Leu Ala Arg Trp Asp Ser 580 585 590 gtc tgg caa ctc gac aaa gca ctg gag caa agt ggt tta tct tta tct 1824 Validity of Gln Leu Asp Lys Ala Leu Glu Gln Ser Gly Leu Ser Leu Leu Ser Leu 595,600,605 gaa gaa aag aaa acc gcc ctc aaa gaa tac agc aaa at gct ttg tc 1872 Glu Glu Lys Thr Ala Leu Lys Glu Tyr Served as Lys Asn Ala Leu Tyr 610 615 620 ttt aga gaa ggt agc CAACC CCT AGC CAG CAT AGT tt GTA GTA ggc 1920 Phe Arg Glu Gly Ser Gln Thr Pro Ser Gln His Thr Ser Phe Val Gly 625 630 635 640 aat att atg gct agt aga att gct gct tta tgg gat ttc tct ggg ccg 1968 Asn Ile Met Ala Ser Arg Ile Ala Ala Leu Trp Asp Phe Ser Gly Pro 645,650,655 gct ttc acc gtt tct tgt ggt gc aat gca gtc ttt aaa gcc ttg gaa 2016 Ala Phe Thr Val Ser Cys Gly Asp Asn Ala Val Phe Lys Ala Leu Glu 660,665,670 gta gct caa aat ata ctt tct cta gga gaa gtt gat gca gta gta gtc 2064 Val Ala Gln Asn Ile Leu Ser Leu Gly Glu Val Asp Ala Val Val Val 675,680,685 ggt ggg gtt gat ttt tgt ggt ggc tta gaa aat gtc tta tta cga caa 2112 Gly Gly Val Asp Phe Cys Gly Gly Leu Glu Asn Val Leu Leu Arg Gln 690,695,700 gaa aaa gaa gcg tct agc caa aat ata gct cct agt ctt tct ctt aac Glu Lys Glu Al Ser Ser Gln Asn Ile Pro Ser Leu Ser Leu Asn 705 710 715 720 caa ggc caa aaa ggt tgg tta gta ggg gaa gga gcg ggt gca gtc gtt 2208 Gln Gly Gln Lys Gly Trp Leu Val Gly Glu Gly Ala Gly Ala Val Val 725 730 735 cta aaa aga caa ata gat cta caa aaa cag gat aac gtc tat gct gtg Leu Lys Arg Gln Ile Asp Leu Gln Lys Gln Asp Asn Val Tyr Ala Val 740,745,750 tta gaa cac att ggc caa gct tct gaa CA ctt aat gta ggg tat CA 2304 Leo Glu Is With Gly Gln Only Serves Glu Gln Leo Asn Val Gly Tyr Gln 755,760,765 gaa ctg gtt agc agt ggc tat gct gca caa gac cat cag gaa ttg aag 2352 Leu Glu Val Ser Gly Tyr Ala Ala Gln Asp His Gln Glu Leu Lys 770,775,780 caa tta cta gcc acc caa ttg gag caa acc gct tta ggt tcg gta 2400 Gln Leu Leu Ala Thr Gln Leu Glu Gln Lys Thr Ala Leu Gly Ser Val 785,790,795,800 aaa aca tcc ttt ggg cat acg ggc gca gcc agt ggc att gct gca ctt 2448 Lys Thr Ser Phe Gly His Thr Gly Ala Ala Ser Gly Ile Ala Ala Leu 805 810 815 att aaa aca gct ctt tgc tta cac cac aaa ttc att cca ggc att ccc 2496 Ile Lys Thr Ala Leu Cys Leu His His Lys Phe Ile Pro Gly Ile Pro 820 825 830 aat tgg gaa gcg cct caa gaa gca acg gcc ttt gca aaa acc aag tac 2544 Asn Trp Glu Ala Pro Gln Glu Ala Thr Ala Phe Ala Lys Thr Lys Tyr 835 840 845 tat ttt cct atg gcc tct agg cct tgg ttg ctc aat gct ggt gaa aag 2592 Tyr Phe Pro Met Ala Ser Arg Pro Trp Leu Leu Asn Ala Gly Glu Lys 850 855 860 aga aaa gcg gcg att aat ggc tta gaa ggg tta caa att cat ttg tca Arg Lys Ala Ala Ile Asn Gly Leu Glu Gly Leu Gln Ile His Leu Ser 865 870 875 880 gaa gga gta agg tct agc ccc gct cct agt cct ttg cta caa gga aga Glu Gly Val Arg Ser Ser Pro Ala Pro Ser Pro Leu Leu Gln Gly Arg 885,890,895 gta gga agt ttg ttt gta tta aaa ggc aat act gaa aca gca tta aga 2736 Val Gly Ser Leu Phe Val Leu Lys Gly Asn Thr Glu Thr Ala Leu Arg 900 905 910 gaa gct tta gct ttg tta tta gaa gac ttg gca ggg aaa tct tct ttg 2784 Glu Ala Leu Ala Leu Glu Asp Ala Gly Lys Ser Ser Ser Leu 915,920,925 cct gag ttg gca gct cgt ctt tat tat aac cat caa gca aag ccc agc 2832 Pro Glu Leu Ala Ala Arg Leu Tyr Tyr Asn His Gln Ala Lys Pro Ser 930,935,940 tct tat acg ata gtt ctc tta gca aat tct aag aaa aac cta caa cag 2880 Serve Tyr Thr Island Val Leo Has Asn Serve Lys Lys Asn Leo Gln Gln 945 950 955 960 gaa atc ​​cgt ttc atg caa gtt ggc tg gaa gct gct ttg aca gaa aac 2928 Glu Ile Arg Phe Met Gln Val Gly Leu Glu Ala Ala Leu Thr Glu Asn 965,970,975 aaa gta ctc aaa acg cct agg ggt tct tat ttt aca gca aaa cct cct Lys Val Leu Lys Thr Pro Arg Gly Ser Tyr Phe Thr Ala Lys Pro Leu 980,985,990 ggt aaa aca gga aaa ata gca ttt one tat cct ggt one gca aca gcc Gly Lys Thr Gly Lys Ile Ala Phe Ser Tyr Pro Gly Ser Ala Thr Ala 995 1000 1005 tat aga ggt tta ggg caa gat att tt CA ttg ttt cct tct ttg Tyr Arg Gly Leu Gly Gln Asp Ile Phe Gln Leu Phe Pro Ser Leu 1010 1015 1020 cac gag cat ttt ggg caa aag cta gag gat ata gca gac ttt gta 3114 His Glu His Phe Gly Gln Lys Leu Glu Asp Ile Ala Asp Phe Val 1025 1030 1035 ggt agc tcc tat ttg cat cca aaa tta caa agc cgt caa gaa gag 3159 Gly Ser Ser Tyr Leu His Pro Lys Leu Gln Ser Arg Gln Glu Glu 1040 1045 1050 gct cct agc atc caa acc gat gca gta agt atg atg tgt gca ggc 3204 Ala Pro Ser Ile Gln Thr Asp Ala Val Ser Met Met Cys Ala Gly 1055 1060 1065 gta ttt tca tct gct att tat acc cac tta ctc aaa gat aaa ttt Val Phe Ser Ser Ala Ile Tyr Thr His Leu Leu Lys Asp Lys Phe 1070 1075 1080 gga tta aaa cca gat ttg gca ttt ggt tat agc atg ggc gaa agt 3294 Gly Leu Lys Pro Asp Leu Ala Phe Gly Tyr Ser Met Gly Glu Ser 1085 1090 1095 gcg ggc atg tgg tac tct ttt gat gtt tgg aat cct gat aat acg Only Gly Met Trp Tyr Ser Phe Asp Val Trp Asn Pro Asp Asn Thr 1100 1105 1110 gct gta ttt aga aat tct gac ttg ttt gcc aac caa tta tca ggg Ala Val Phe Arg Asn Ser Asp Leu Phe Ala Asn Gln Leu Ser Gly 1115 1120 1125 gat tta cgc ttg ttg gct gag act tgg gga att tct tct gaa gaa 3429 Asp Leu Arg Leu Leu Ala Glu Thr Trp Gly Ile Ser Ser Glu Glu 1130 1135 1140 gcc aaa gca cga tgg att agt ttg att cta ttg gcc gat aaa gaa 3474 Ala Lys Ala Arg Trp Ile Ser Leu Ile Leu Leu Ala Asp Lys Glu 1145 1150 1155 gcc gtt cag aat tta gta gca caa gaa gac aga tgc tat tta agc 3519 Ala Val Gln Asn Leu Val Ala Gln Glu Asp Arg Cys Tyr Leu Ser 1160 1165 1170 ttt atc aat aca cct caa gag gtg att att tct gga gat aaa gaa 3564 Phe Ile Asn Thr Pro Gln Glu Val Ile Ile Ser Gly Asp Lys Glu 1175 1180 1185 gct tgc aat aga gtt gtt caa caa ttg ggc tgc cct gcg gta gag 3609 Ala Cys Asn Arg Val Val Gln Gln Leu Gly Cys Pro Ala Val Glu 1190 1195 1200 gtt cct ttt cag aat gtc att cat cat gat ttt tgc aaa aaa gtc 3654 Val Pro Phe Gln Asn Val Ile His His Asp Phe Cys Lys Lys Val 1205 1210 1215 caa gag gaa ttg tat gac atg cat cac ttt cca tta gaa aca cag 3699 Gln Glu Glu Leu Tyr Asp Met His His Phe Pro Leu Glu Thr Gln 1220 1225 1230 cct aat ata gac ttt tat tct agt ttg agc ctc gct cct tta cca 3744 Pro Asn Ile Asp Phe Tyr Ser Ser Leu Ser Leu Ala Pro Leu Pro 1235 1240 1245 atg gat agt gga gtt att gct caa aat tct acc caa gtt tgc ttt 3789 Met Asp Ser Gly Val Ile Ala Gln Asn Ser Thr Gln Val Cys Phe 1250 1255 1260 caa cca gtc gat tac cct acc act att caa caa ttg tat aac gat 3834 Gln Pro Val Asp Tyr Pro Thr Thr Ile Gln Gln Leu Tyr Asn Asp 1265 1270 1275 ggg gct aga att ttt ata gaa tta ggc gca ggg aat acc tgt act 3879 Gly Ala Arg Ile Phe Ile Glu Leu Gly Ala Gly Asn Thr Cys Thr 1280 1285 1290 caa tgg aca agt agt att ttg gga cag caa gct cat tta gca gtt 3924 Gln Trp Thr Ser Ser Ile Leu Gly Gln Gln Ala His Leu Ala Val 1295 1300 1305 agc tgt act caa aaa ggc aag cca gaa ggc act gcc ctc tta caa 3969 Ser Cys Thr Gln Lys Gly Lys Pro Glu Gly Thr Ala Leu Leu Gln 1310 1315 1320 gca ttg gca cag tta ctc agt cat gga gta gcg cta gat ttg caa 4014 Ala Leu Ala Gln Leu Leu Ser His Gly Val Ala Leu Asp Leu Gln 1325 1330 1335 cct ttg ttt gca gct gat ttg cta gcc ccc tcg cca aga gca ttt 4059 Pro Leu Phe Ala Ala Asp Leu Leu Ala Pro Ser Pro Arg Ala Phe 1340 1345 1350 tac aaa gct att gtt tct ggt gga gct aga att ttt gat tat tta 4104 Tyr Lys Ala Ile Val Ser Gly Gly Ala Arg Ile Phe Asp Tyr Leu 1355 1360 1365 tta caa ccc caa acc aaa aaa caa ttt gca gga gta act aaa act 4149 Leu Gln Pro Gln Thr Lys Lys Gln Phe Ala Gly Val Thr Lys Thr 1370 1375 1380 gct ctt gtg caa caa tta gaa cct gct ctt gcc agc aat agc aga 4194 Ala Leu Val Gln Gln Leu Glu Pro Ala Leu Ala Ser Asn Ser Arg 1385 1390 1395 gaa tat tcc ttt act tca act aaa aca act act gtg gac aca aca 4239 Glu Tyr Ser Phe Thr Ser Thr Lys Thr Thr Thr Val Asp Thr Thr 1400 1405 1410 caa tca att cct agt cca agc caa aaa gta cta cta gga gaa aat 4284 Gln Ser Ile Pro Ser Pro Ser Gln Lys Val Leu Leu Gly Glu Asn 1415 1420 1425 ggt tta aaa ttg cag gat ttt aat gat cct aac cat ctc caa gga 4329 Gly Leu Lys Leu Gln Asp Phe Asn Asp Pro Asn His Leu Gln Gly 1430 1435 1440 aag acg att atc ttt tct cag gaa gat ttg gaa gag ttt gca aca 4374 Lys Thr Ile Ile Phe Ser Gln Glu Asp Leu Glu Glu Phe Ala Thr 1445 1450 1455 ggc aaa att gct aaa gta ttt gga gag gaa tac agt atc att gac 4419 Gly Lys Ile Ala Lys Val Phe Gly Glu Glu Tyr Ser Ile Ile Asp 1460 1465 1470 acg tac aaa aga aga gtc atg tta cct atg gcc ccc tac tta ttg 4464 Thr Tyr Lys Arg Arg Val Met Leu Pro Met Ala Pro Tyr Leu Leu 1475 1480 1485 gtt agt aga gta aca ggc tta gat gct aaa aga gga gaa ttt aag 4509 Val Ser Arg Val Thr Gly Leu Asp Ala Lys Arg Gly Glu Phe Lys 1490 1495 1500 cct tct acc atg caa acg gaa tac gat att cct tat aat gct tgg 4554 Pro Ser Thr Met Gln Thr Glu Tyr Asp Ile Pro Tyr Asn Ala Trp 1505 1510 1515 ttt act aca gat ggt caa att cct tgg gcg gtc tct gtg gag tca 4599 Phe Thr Thr Asp Gly Gln Ile Pro Trp Ala Val Ser Val Glu Ser 1520 1525 1530 gga cag tgt gat tta tta tta att tct tat ttg gga att gat ttt 4644 Gly Gln Cys Asp Leu Leu Leu Ile Ser Tyr Leu Gly Ile Asp Phe 1535 1540 1545 gaa aat aaa gga gac tta gtt tat aga tta ctg gat tgt acc ttg 4689 Glu Asn Lys Gly Asp Leu Val Tyr Arg Leu Leu Asp Cys Thr Leu 1550 1555 1560 act ttt gtg gat gac tta ccc ttt gag ggc caa acg ttg agg tat 4734 Thr Phe Val Asp Asp Leu Pro Phe Glu Gly Gln Thr Leu Arg Tyr 1565 1570 1575 gat att tct att aat tca ttt gta aga aat ggt gac aac tta ctg 4779 Asp Ile Ser Ile Asn Ser Phe Val Arg Asn Gly Asp Asn Leu Leu 1580 1585 1590 ttt ttc ttt agt tat aat tgt tat gtt gag gat aga tta gta ttg 4824 Phe Phe Phe Ser Tyr Asn Cys Tyr Val Glu Asp Arg Leu Val Leu 1595 1600 1605 aaa atg aga aat ggt tgt gct ggt ttc ttt acc gat gaa caa cta 4869 Lys Met Arg Asn Gly Cys Ala Gly Phe Phe Thr Asp Glu Gln Leu 1610 1615 1620 gag gaa gga tta ggt gtg gtt tat tct aag gaa gaa cta gaa gcc 4914 Glu Glu Gly Lion Gly Val Val Tyr Ser Lys Glu Glu Lion Glu Wing 1625 1630 1635 aaa acc aat gca aaa aaa cct gcc ttt acc cct tta tta aac acc 4959 Lys Thr Asn Ala Lys Lys Pro Ala Phe Thr Pro Leu Leu Asn Thr 1640 1645 1650 aaa aaa aca agc ttc agc aaa gaa gat ttg cac cat ttg ata gaa 5004 Lys Lys Thr Ser Phe Ser Glu Asp Leu His His Leu Ile Glu 1655 1660 1665 ggt aat atg gag ttg tgc ttt gat agc cct gct tat ttt gcc aat 5049 Gly Asn Met Glu Leu Cys Phe Asp Ser Pro Ala Tyr Phe Ala Asn 1670 1675 1680 ggt aga aat cct tct ttg aga ctt cct ccc gag caa att ttg atg 5094 Gly Arg Asn Pro Ser Leu Arg Leu Pro Pro Glu Gln Ile Leu Met 1685 1690 1695 ata gat aga att gta tct gtc gat ttg aaa gga ggt gcc tat ggc 5139 Ile Asp Arg Ile Val Ser Val Asp Leu Lys Gly Gly Ala Tyr Gly 1700 1705 1710 ttg ggt tat gta att gct gaa aaa gat tta gca cct gag gac tgg 5184 Leu Gly Tyr Val Ile Ala Glu Lys Asp Leu Ala Pro Glu Asp Trp 1715 1720 1725 tat ttc cct tgt cac ttt aga gat gat gaa gta ttg gca ggt tct 5229 Tyr Phe Pro Cys His Phe Arg Asp Asp Glu Val Leu Ala Gly Ser 1730 1735 1740 cta caa gca gaa gga gga gga aat tta ttg cgc ttt ttt atg tta 5274 Leu Gln Ala Glu Gly Gly Gly Asn Leu Leu Arg Phe Phe Met Leu 1745 1750 1755 atg tta ggg tta caa aga tta acc aaa gac gct cgt tat caa cct 5319 Met Leu Gly Leu Gln Arg Leu Thr Lys Asp Ala Arg Tyr Gln Pro 1760 1765 1770 to ttt gac tta cct caa aaa gta aga tgc cga aaa caa gtt act 5364 Ile Phe Asp Leu Pro Gln Lys Val Arg Cys Arg Lys Gln Val Thr 1775 1780 1785 cct tct aaa gat aca aaa cta gtt tat aag cta gaa gta aaa gaa 5409 Pro Ser Lys Asp Thr Lys Leu Val Tyr Lys Leu Glu Val Lys Glu 1790 1795 1800 to go Ile Gly Leu Val Pro Asn Pro Tyr Val Ile Ala Asp Leu Glu Ile 1805 1810 1815 gta tct gat ggg gta att aca gtt cat ttt gag aat tta gga tta 5499 Val Ser Asp Gly Val Ile Thr Val His Phe Glu Asn Leu Gly Leu 1820 1825 1830 caa cta aga gaa aaa gac aat ccg aga tat ttg gaa cag cag aaa 5544 Gln Leu Arg Glu Lys Asp Asn Pro Arg Tyr Leu Glu Gln Gln Lys 1835 1840 1845 ggt gta cac atc tcc cct cgt tct aaa gat gcc tta ctc acc gag 5589 Gly Val His Ile Ser Pro Arg Ser Lys Asp Ala Leu Leu Thr Glu 1850 1855 1860 ttg gac att act aat ttt gca ctc aac aac cta tcg gtt gct ttt 5634 Leu Asp Ile Thr Asn Phe Ala Leu Asn Asn Leu Ser Val Ala Phe 1865 1870 1875 ggg cct gac ttt gct tgt tat gat gga aga aca gtt tct aga cag 5679 Gly Pro Asp Phe Ala Cys Tyr Asp Gly Arg Thr Val Ser Arg Gln 1880 1885 1890 cct aac acc gat tta caa ctg att tct aga gtc tta aaa att gaa 5724 Pro Asn Thr Asp Leu Gln Leu Ile Ser Arg Val Leu Lys Ile Glu 1895 1900 1905 gga gaa cgt cta aat ttc aaa caa cct tct act att tac gca gaa 5769 Gly Glu Arg Leu Asn Phe Lys Gln Pro Ser Thr Ile Tyr Ala Glu 1910 1915 1920 tat gat gtc cca gaa gat gct tgg tat tac caa caa aat gcg tct 5814 Tyr Asp Val Pro Glu Asp Ala Trp Tyr Tyr Gln Gln Asn Ala Ser 1925 1930 1935 atg acc atg cct tat tcg gtc tta atg gaa att gca tta caa ccc 5859 Met Thr Met Pro Tyr Ser Val Leu Met Glu Ile Ala Leu Gln Pro 1940 1945 1950 tgt gga tta cta gga gcc tat ttg ggt tct acg ttg cct ttc tcc 5904 Cys Gly Leu Leu Gly Ala Tyr Leu Gly Ser Thr Leu Pro Phe Ser 1955 1960 1965 gat aag aat tta ttc ttt agg aac ttg gat gga acg ggt gaa atg 5949 Asp Lys Asn Leu Phe Phe Arg Asn Leu Asp Gly Thr Gly Glu Met 1970 1975 1980 cta gag cta cca atg gga aca gac tgg aga ggc aaa acc att cat 5994 Leu Glu Leu Pro Met Gly Thr Asp Trp Arg Gly Lys Thr Ile His 1985 1990 1995 aac aaa gct gtg ttg gcc tct tct gta gcc tta gga gga act gtt 6039 Asn Lys Ala Val Leu Ala Ser Ser Val Ala Leu Gly Gly Thr Val 2000 2005 2010 ttg cag aat tat acc ttt gaa ttg agt atc gat ggt caa gta ttc 6084 Leu Gln Asn Tyr Thr Phe Glu Leu Ser Ile Asp Gly Gln Val Phe 2015 2020 2025 tac aaa gga aaa one tta gga ttat each gct gga gca 6129 Tyr Lys Gly Lys Ser Ser Phe Gly Phe Phe Pro Ala Glu Ala Leu 2030 2035 2040 gct caa caa gta gga tta gat aat ggt aca gct gta gcg cct tgg 6174 Ala Gln Gln Val Gly Leu Asp Asn Gly Thr Ala Val Ala Pro Trp 2045 2050 2055 tac CAA CAG CAA AAT CTA GCT CAAAA GAT TAT ATG AGCA ATCA AAA 6219 Tyr Gln Gln Asn Leu Only Gln Lys Asp Tyr Met Ser Ile Lys 2060 2065 2070 cta gac tct ttg tat ggc aaa atg aag ctc ttc aaa gct cct gct 6264 Leu Asp Ser Leu Tyr Gly Lys Met Lys Leu Phe Lys Ala Pro Ala 2075 2080 2085 aat aaa cca cat tac cat tta tca ggt gag cag ctt tcc ttg ctc 6309 Asn Lys Pro His Tyr His Leu Ser Gly Glu Gln Leu Ser Leu 2090 2095 2100 aac aat cta aaa att gtt aaa gat gga ggc caa tat ggc aag ggc 6354 Asn Asn Leu Lys Ile Val Lys Asp Gly Gly Gln Tyr Gly Lys Gly 2105 2110 2115 tat att tat ggc cat caa gct att aac ctc tat gat tgg ttc ttt Tyr Ile Tyr Gly His Gln Ala Ile Asn Leu Tyr Asp Trp Phe Phe 2120 2125 2130 act tgc cac ttc tac caa gac cct gta atg cca ggc tct cta gga 6444 Thr Cys His Phe Tyr Gln Asp Pro Val Met Pro Gly Ser Leu Gly 2135 2140 2145 gta gaa gct att ttg CA gcc atg CA acc ttt GCA tta CA CA 6489 Val Glu Ala Ile Leu Gln Ala Met Gln Thr Phe Ala Leu Gln Gln 2150 2155 2160 gat ttg ggt aaa gat ttt aaa tca cct aga ttt gta caa gta cct Asp Leu Gly Lys Asp Phe Lys Ser Pro Arg Phe Val Gln Val Pro 2165 2170 2175 cag cat aca act gtt tgg aaa tac aga gga caa att ttg ca gga 6579 Gln His Thr Thr Value Type Tyr Arg Gly Gln Ileu Gln Gly 2180 2185 2190 gtt gaa aac atg cac tgt gaa gta cat ttc aaa agc ata gaa aag 6624 Val Glu Asn Met His Cys Glu Val His Phe Lys Ser Ile Glu Lys 2195 2200 2205 aaa gga gag caa ttg gtt att gtt gga gat gct tat tta tgg aat 6669 Lys Gly Glu Gln Leu Val Ile Val Gly Asp Ala Tyr Leu Trp Asn 2210 2215 2220 gaa gat act aga att tat caa att acg gac ttg gct cta ggt ata 6714 Glu Asp Thr Arg Ile Tyr Gln Ile Thr Asp Leu Ala Leu Gly Ile 2225 2230 2235 gaa gaa gct taa 6726 Glu Glu Ala 2240 <210> 60 <211> 2241 <212> PRT <213> Aureispira marina <400> 60 Met Lys Ile Ala Ile Ile Gly Leu Ser Gly Leu Phe Pro Gly Ser Ser 1 5 10 15 Thr Asn Glu Glu Phe Trp Gln Asn Leu Leu Asp Glu Lys Asp Leu Thr 20 25 30 Asn Leu Ala Asn Leu Glu Asp Phe Gly Ala Asp Pro Ala Leu Phe Tyr 35 40 45 Glu Asp Lys Lys Gly Ala Val Asp Arg Cys Tyr Ser Leu Arg Gly Gly 50 55 60 Tyr Ile Arg Asp Phe Asp Phe Asp Pro Thr Gly Tyr Gln Leu Ser Ala 65 70 75 80 Asp Phe Leu Ala Gln Gln Asp Lys Leu Tyr Gln Trp Ser Leu Tyr Val 85 90 95 Ala Lys Thr Ala Leu Glu Glu Ser Gly Tyr Ala His Asn Lys Glu Val 100 105 110 Leu Ala Lys Cys Gly Leu Ile Leu Gly Asn Leu Ser Phe Pro Thr Gly 115 120 125 Ser Ser His Lys Leu Leu Ala Asp Leu Tyr Thr Lys Thr Thr Glu Lys 130 135 140 Ala Leu Gln Glu Leu Leu Glu Asp Lys Asn Phe Lys Ile Pro Ala Ser 145 150 155 160 Gln Leu Pro Ile Pro Asn Asn Glu Val Leu Ala Asp Thr Pro Ser Gln 165 170 175 Met Val Ala Lys Gly Leu Gly Leu Gly Gly Gly His Tyr Ala Leu Asp 180 185 190 Ala Ala Cys Ala Thr Ser Leu Tyr Ala Ile Lys Leu Ala Cys Asp Glu 195 200 205 Leu Ile Thr Gly Lys Ala Asp Leu Met Leu Ala Gly Ala Val Cys Gly 210 215 220 Ser Asp Gln Leu Phe Ile His Met Gly Phe Ser Ile Phe His Ala Tyr 225 230 235 240 Ala Pro His Gly Glu Lys Phe Ala Pro Leu Asp Lys Ala Ser Gly Gly 245 250 255 Leu Val Ser Ala Glu Gly Ala Gly Met Val Val Leu Lys Arg Leu Glu 260 265 270 Asp Ala Glu Arg Asp Gly Asp Asn Ile Leu Gly Leu Ile Gly Gly Ile 275 280 285 Gly Leu Ser Asn Asp Gly Ser Gly Lys Phe Leu Leu Ser Pro Asn Pro 290 295 300 Lys Gly Gln Arg Leu Ala Phe Glu Arg Ala Tyr Asp Leu Glu Glu Val 305 310 315 320 Leu Pro Gln Asn Thr Ser Tyr Leu Glu Cys His Ala Thr Gly Thr Pro 325 330 335 Leu Gly Asp Val Thr Glu Met Asn Ser Ile Ser Asp Phe Phe Ala Gln 340 345 350 His Gln Thr Lys Pro Leu Leu Gly Ser Val Lys Ser Asn Met Gly His 355 360 365 Leu Leu Thr Ala Ala Gly Met Ser Gly Leu Phe Lys Val Leu Leu Ser 370 375 380 Met Gln Lys Gly Ile Ile Pro Pro Asn Ile Asn Leu Glu Ser Ala Val 385 390 395 400 Gln Ala Asn Asn Gln Trp Ile Gln Asp Glu Gln Ile Ile Lys Lys Thr 405 410 415 Thr Pro Trp Lys Gly Asp Gln Ala Gly Ile Asn Ser Phe Gly Phe Gly 420 425 430 Gly Thr Asn Ala His Met Val Val Gln Lys Pro Thr Ser Ser Thr Leu 435 440 445 Lys Glu Lys Lys Ala Tyr Gln Ala Gln Glu Leu Leu Pro Leu Ala Ile 450 455 460 Val Gly Met Asp Ala His Phe Gly Ser Cys Glu Asn Leu Glu Asp Phe 465 470 475 480 Tyr Ala Ala Ile Tyr Asn Gly Asn Gln Asp Phe Lys Pro Leu Pro Pro 485 490 495 Lys Arg Trp Lys Gly Phe Asp Ala Asp Gln Asp Leu Leu Lys Arg Tyr 500 505 510 Gly Phe Lys Asp Gly Leu Ala Pro Lys Gly Ala Tyr Ile Asp Gln Phe 515 520 525 Asp Ile Asp Leu Leu Arg Tyr Lys Ile Gln Pro Lys Glu Ala Glu Thr 530 535 540 Leu Glu Pro Gln Gln Ala Leu Ile Leu Lys Val Ala Asp Lys Ala Leu 545 550 555 560 Gln Asp Ala Gln Ile Ser Pro Ser Gln Asn Ile Ala Val Leu Ile Ala 565 570 575 Met Glu Ser Glu Leu Ala Ile His His Tyr Leu Ala Arg Trp Asp Ser 580 585 590 Val Trp Gln Leu Asp Lys Ala Leu Glu Gln Ser Gly Leu Ser Leu Ser 595 600 605 Glu Glu Lys Lys Thr Ala Leu Lys Glu Tyr Ser Lys Asn Ala Leu Tyr 610 615 620 Phe Arg Glu Gly Ser Gln Thr Pro Ser Gln His Thr Ser Phe Val Gly 625 630 635 640 Asn Ile Met Ala Ser Arg Ile Ala Ala Leu Trp Asp Phe Ser Gly Pro 645 650 655 Ala Phe Thr Val Ser Cys Gly Asp Asn Ala Val Phe Lys Ala Leu Glu 660 665 670 Val Ala Gln Asn Ile Leu Ser Leu Gly Glu Val Asp Ala Val Val Val 675 680 685 Gly Gly Val Asp Phe Cys Gly Gly Leu Glu Asn Val Leu Leu Arg Gln 690 695 700 Glu Lys Glu Ala Ser Ser Gln Asn Ile Ala Pro Ser Leu Ser Leu Asn 705 710 715 720 Gln Gly Gln Lys Gly Trp Leu Val Gly Glu Gly Ala Gly Ala Val Val 725 730 735 Leu Lys Arg Gln Ile Asp Leu Gln Lys Gln Asp Asn Val Tyr Ala Val 740 745 750 Leu Glu His Ile Gly Gln Ala Ser Glu Gln Leu Asn Val Gly Tyr Gln 755 760 765 Glu Leu Val Ser Ser Gly Tyr Ala Ala Gln Asp His Gln Glu Leu Lys 770 775 780 Gln Leu Leu Ala Thr Gln Leu Glu Gln Lys Thr Ala Leu Gly Ser Val 785 790 795 800 Lys Thr Ser Phe Gly His Thr Gly Ala Ala Ser Gly Ile Ala Ala Leu 805 810 815 Ile Lys Thr Ala Leu Cys Leu His His Lys Phe Ile Pro Gly Ile Pro 820 825 830 Asn Trp Glu Ala Pro Gln Glu Ala Thr Ala Phe Ala Lys Thr Lys Tyr 835 840 845 Tyr Phe Pro Met Ala Ser Arg Pro Trp Leu Leu Asn Ala Gly Glu Lys 850 855 860 Arg Lys Ala Ala Ile Asn Gly Leu Glu Gly Leu Gln Ile His Leu Ser 865 870 875 880 Glu Gly Val Arg Ser Ser Pro Ala Pro Ser Pro Leu Leu Gln Gly Arg 885 890 895 Val Gly Ser Leu Phe Val Leu Lys Gly Asn Thr Glu Thr Ala Leu Arg 900 905 910 Glu Ala Leu Ala Leu Leu Leu Glu Asp Leu Ala Gly Lys Ser Ser Leu 915 920 925 Pro Glu Leu Ala Ala Arg Leu Tyr Tyr Asn His Gln Ala Lys Pro Ser 930 935 940 Ser Tyr Thr Ile Val Leu Leu Ala Asn Ser Lys Lys Asn Leu Gln Gln 945 950 955 960 Glu Ile Arg Phe Met Gln Val Gly Leu Glu Ala Ala Leu Thr Glu Asn 965 970 975 Lys Val Leu Lys Thr Pro Arg Gly Ser Tyr Phe Thr Ala Lys Pro Leu 980 985 990 Gly Lys Thr Gly Lys Ile Ala Phe Ser Tyr Pro Gly Ser Ala Thr Ala 995 1000 1005 Tyr Arg Gly Leu Gly Gln Asp Ile Phe Gln Leu Phe Pro Ser Leu 1010 1015 1020 His Glu His Phe Gly Gln Lys Leu Glu Asp Ile Ala Asp Phe Val 1025 1030 1035 Gly Ser Ser Tyr Leu His Pro Lys Leu Gln Ser Arg Gln Glu Glu 1040 1045 1050 Ala Pro Ser Ile Gln Thr Asp Ala Val Ser Met Met Cys Ala Gly 1055 1060 1065 Val Phe Ser Ser Ala Ile Tyr Thr His Leu Leu Lys Asp Lys Phe 1070 1075 1080 Gly Leu Lys Pro Asp Leu Ala Phe Gly Tyr Ser Met Gly Glu Ser 1085 1090 1095 Ala Gly Met Trp Tyr Ser Phe Asp Val Trp Asn Pro Asp Asn Thr 1100 1105 1110 Ala Val Phe Arg Asn Ser Asp Leu Phe Ala Asn Gln Leu Ser Gly 1115 1120 1125 Asp Leu Arg Leu Leu Ala Glu Thr Trp Gly Ile Ser Ser Glu Glu 1130 1135 1140 Ala Lys Ala Arg Trp Ile Ser Leu Ile Leu Leu Ala Asp Lys Glu 1145 1150 1155 Ala Val Gln Asn Leu Val Ala Gln Glu Asp Arg Cys Tyr Leu Ser 1160 1165 1170 Phe Ile Asn Thr Pro Gln Glu Val Ile Ile Ser Gly Asp Lys Glu 1175 1180 1185 Ala Cys Asn Arg Val Val Gln Gln Leu Gly Cys Pro Ala Val Glu 1190 1195 1200 Val Pro Phe Gln Asn Val Ile His His Asp Phe Cys Lys Lys Val 1205 1210 1215 Gln Glu Glu Leu Tyr Asp Met His His Phe Pro Leu Glu Thr Gln 1220 1225 1230 Pro Asn Ile Asp Phe Tyr Ser Ser Leu Ser Leu Ala Pro Leu Pro 1235 1240 1245 Met Asp Ser Gly Val Ile Ala Gln Asn Ser Thr Gln Val Cys Phe 1250 1255 1260 Gln Pro Val Asp Tyr Pro Thr Thr Ile Gln Gln Leu Tyr Asn Asp 1265 1270 1275 Gly Ala Arg Ile Phe Ile Glu Leu Gly Ala Gly Asn Thr Cys Thr 1280 1285 1290 Gln Trp Thr Ser Ser Ile Leu Gly Gln Gln Ala His Leu Ala Val 1295 1300 1305 Ser Cys Thr Gln Lys Gly Lys Pro Glu Gly Thr Ala Leu Leu Gln 1310 1315 1320 Ala Leu Ala Gln Leu Leu Ser His Gly Val Ala Leu Asp Leu Gln 1325 1330 1335 Pro Leu Phe Ala Ala Asp Leu Leu Ala Pro Ser Pro Arg Ala Phe 1340 1345 1350 Tyr Lys Ala Ile Val Ser Gly Gly Ala Arg Ile Phe Asp Tyr Leu 1355 1360 1365 Leu Gln Pro Gln Thr Lys Lys Gln Phe Ala Gly Val Thr Lys Thr 1370 1375 1380 Ala Leu Val Gln Gln Leu Glu Pro Ala Leu Ala Ser Asn Ser Arg 1385 1390 1395 Glu Tyr Ser Phe Thr Ser Thr Lys Thr Thr Thr Val Asp Thr Thr 1400 1405 1410 Gln Ser Ile Pro Ser Pro Ser Gln Lys Val Leu Leu Gly Glu Asn 1415 1420 1425 Gly Leu Lys Leu Gln Asp Phe Asn Asp Pro Asn His Leu Gln Gly 1430 1435 1440 Lys Thr Ile Ile Phe Ser Gln Glu Asp Leu Glu Glu Phe Ala Thr 1445 1450 1455 Gly Lys Ile Ala Lys Val Phe Gly Glu Glu Tyr Ser Ile Ile Asp 1460 1465 1470 Thr Tyr Lys Arg Arg Val Met Leu Pro Met Ala Pro Tyr Leu Leu 1475 1480 1485 Val Ser Arg Val Thr Gly Leu Asp Ala Lys Arg Gly Glu Phe Lys 1490 1495 1500 Pro Ser Thr Met Gln Thr Glu Tyr Asp Ile Pro Tyr Asn Ala Trp 1505 1510 1515 Phe Thr Thr Asp Gly Gln Ile Pro Trp Ala Val Ser Val Glu Ser 1520 1525 1530 Gly Gln Cys Asp Leu Leu Leu Ile Ser Tyr Leu Gly Ile Asp Phe 1535 1540 1545 Glu Asn Lys Gly Asp Leu Val Tyr Arg Leu Leu Asp Cys Thr Leu 1550 1555 1560 Thr Phe Val Asp Asp Leu Pro Phe Glu Gly Gln Thr Leu Arg Tyr 1565 1570 1575 Asp Ile Ser Ile Asn Ser Phe Val Arg Asn Gly Asp Asn Leu Leu 1580 1585 1590 Phe Phe Phe Ser Tyr Asn Cys Tyr Val Glu Asp Arg Leu Val Leu 1595 1600 1605 Lys Met Arg Asn Gly Cys Ala Gly Phe Phe Thr Asp Glu Gln Leu 1610 1615 1620 Glu Glu Gly Leu Gly Val Val Tyr Ser Lys Glu Glu Leu Glu Ala 1625 1630 1635 Lys Thr Asn Ala Lys Lys Pro Ala Phe Thr Pro Leu Leu Asn Thr 1640 1645 1650 Lys Lys Thr Ser Phe Ser Lys Glu Asp Leu His His Leu Ile Glu 1655 1660 1665 Gly Asn Met Glu Leu Cys Phe Asp Ser Pro Ala Tyr Phe Ala Asn 1670 1675 1680 Gly Arg Asn Pro Ser Leu Arg Leu Pro Pro Glu Gln Ile Leu Met 1685 1690 1695 Ile Asp Arg Ile Val Ser Val Asp Leu Lys Gly Gly Ala Tyr Gly 1700 1705 1710 Leu Gly Tyr Val Ile Ala Glu Lys Asp Leu Ala Pro Glu Asp Trp 1715 1720 1725 Tyr Phe Pro Cys His Phe Arg Asp Asp Glu Val Leu Ala Gly Ser 1730 1735 1740 Leu Gln Ala Glu Gly Gly Gly Asn Leu Leu Arg Phe Phe Met Leu 1745 1750 1755 Met Leu Gly Leu Gln Arg Leu Thr Lys Asp Ala Arg Tyr Gln Pro 1760 1765 1770 Ile Phe Asp Leu Pro Gln Lys Val Arg Cys Arg Lys Gln Val Thr 1775 1780 1785 Pro Ser Lys Asp Thr Lys Leu Val Tyr Lys Leu Glu Val Lys Glu 1790 1795 1800 Ile Gly Leu Val Pro Asn Pro Tyr Val Ile Ala Asp Leu Glu Ile 1805 1810 1815 Val Ser Asp Gly Val Ile Thr Val His Phe Glu Asn Leu Gly Leu 1820 1825 1830 Gln Leu Arg Glu Lys Asp Asn Pro Arg Tyr Leu Glu Gln Gln Lys 1835 1840 1845 Gly Val His Ile Ser Pro Arg Ser Lys Asp Ala Leu Leu Thr Glu 1850 1855 1860 Leu Asp Ile Thr Asn Phe Ala Leu Asn Asn Leu Ser Val Ala Phe 1865 1870 1875 Gly Pro Asp Phe Ala Cys Tyr Asp Gly Arg Thr Val Ser Arg Gln 1880 1885 1890 Pro Asn Thr Asp Leu Gln Leu Ile Ser Arg Val Leu Lys Ile Glu 1895 1900 1905 Gly Glu Arg Leu Asn Phe Lys Gln Pro Ser Thr Ile Tyr Ala Glu 1910 1915 1920 Tyr Asp Val Pro Glu Asp Ala Trp Tyr Tyr Gln Gln Asn Ala Ser 1925 1930 1935 Met Thr Met Pro Tyr Ser Val Leu Met Glu Ile Ala Leu Gln Pro 1940 1945 1950 Cys Gly Leu Leu Gly Ala Tyr Leu Gly Ser Thr Leu Pro Phe Ser 1955 1960 1965 Asp Lys Asn Leu Phe Phe Arg Asn Leu Asp Gly Thr Gly Glu Met 1970 1975 1980 Leu Glu Leu Pro Met Gly Thr Asp Trp Arg Gly Lys Thr Ile His 1985 1990 1995 Asn Lys Ala Val Leu Ala Ser Ser Val Ala Leu Gly Gly Thr Val 2000 2005 2010 Leu Gln Asn Tyr Thr Phe Glu Leu Ser Ile Asp Gly Gln Val Phe 2015 2020 2025 Tyr Lys Gly Lys Ser Ser Phe Gly Phe Phe Pro Ala Glu Ala Leu 2030 2035 2040 Ala Gln Gln Val Gly Leu Asp Asn Gly Thr Ala Val Ala Pro Trp 2045 2050 2055 Tyr Gln Gln Gln Asn Leu Ala Gln Lys Asp Tyr Met Ser Ile Lys 2060 2065 2070 Leu Asp Ser Leu Tyr Gly Lys Met Lys Leu Phe Lys Ala Pro Ala 2075 2080 2085 Asn Lys Pro His Tyr His Leu Ser Gly Glu Gln Leu Ser Leu Leu 2090 2095 2100 Asn Asn Leu Lys Ile Val Lys Asp Gly Gly Gln Tyr Gly Lys Gly 2105 2110 2115 Tyr Ile Tyr Gly His Gln Ala Ile Asn Leu Tyr Asp Trp Phe Phe 2120 2125 2130 Thr Cys His Phe Tyr Gln Asp Pro Val Met Pro Gly Ser Leu Gly 2135 2140 2145 Val Glu Ala Ile Leu Gln Ala Met Gln Thr Phe Ala Leu Gln Gln 2150 2155 2160 Asp Leu Gly Lys Asp Phe Lys Ser Pro Arg Phe Val Gln Val Pro 2165 2170 2175 Gln His Thr Thr Value Type Tyr Arg Gly Gln Ileu Gln Gly 2180 2185 2190 Will Glu Asn Met His Cys Glu Will His Phe Lys Ser Ile Glu Lys 2195 2200 2205 Lys Gly Glu Gln Leu Val Ile Val Gly Asp Ala Tyr Leu Trp Asn 2210 2215 2220 Glu Asp Thr Arg with Tyr Gln and Thr Asp with Ala and Gly 2225 2230 2235 Glu Glu Ala 2240 <210> 61 <211> 1629 <212> DNA <213> Aureispira marina (Aureispira marina) <220> <221> CDS <222> (1)..(1629) <400> 61 atg att act ttt tct gga ata aaa cag cag ttg tat tgg aaa ggc tcg 48 Met Thr Phe Ser Gly and Lys Gln Gln Leu Tyr Trp Lys Gly Ser 1 5 10 15 cct aga gct att tct ttt gat gct gcg ggt atg gag caa aaa tta aaa 96 Pro Arg Ala Ile Ser Phe Asp Ala Ala Gly Met Glu Gln Lys Leu Lys 20 25 30 aac acc caa gaa cat tgt ttt gta gta gag gat ttt gct ggg cga gtt 144 Asn Thr Gln Glu His Cys Phe Val Val Glu Asp Phe Ala Gly Arg Val 35 40 45 ggc atc gcc aat gca gga gaa tta act act gat agc aaa ggc tta caa 192 Gly Ile Ala Asn Ala Gly Glu Leu Thr Thr Asp Ser Lys Gly Leu Gln 50 55 60 gta tta gcc atg gtc gcc cct atg acc gca gag caa ttg gga gat gct 240 Val Leu Ala Met Val Ala Pro Met Thr Ala Glu Gln Leu Gly Asp Ala 65 70 75 80 act ttt aga aaa gat tat aag cta aaa tat gcc tat aaa aca gga gca 288 Thr Phe Arg Lys Asp Tyr Lys Leu Lys Tyr Ala Tyr Lys Thr Gly Ala 85 90 95 atg gct aat gga att gct tcc gaa gat tta gta att gct atg ggc aaa 336 Met Ala Asn Gly Ile Ala Ser Glu Asp Leu Val Ile Ala Met Gly Lys 100 105 110 gca ggt ttg cta ggc tct ttc gga gct gca ggt ctc att cct agt aga 384 Ala Gly Leu Leu Gly Ser Phe Gly Ala Ala Gly Leu Ile Pro Ser Arg 115 120 125 gta gaa caa gct att gat acc att caa caa gcc ttg cct act caa agc 432 Val Glu Gln Ala Ile Asp Thr Ile Gln Gln Ala Leu Pro Thr Gln Ser 130 135 140 tac gct ttt aat ttg to cac agt ccc aat gag cct gcc tta gag gaa 480 Tyr Ala Phe Asn Leu Ile His Ser Pro Asn Glu Pro Ala Leu Glu Glu 145 150 155 160 gga gct gta aaa cac ttt ttg gcc aga gga gtg aac gtt gta gaa gcc 528 Gly Ala Val Lys His Phe Leu Ala Arg Gly Val Asn Val Val Glu Ala 165 170 175 tct gct ttt ctc aac cta act ctt aat att gtc cat tat aga gtt gca 576 Ser Ala Phe Leu Asn Leu Thr Leu Asn Ile Val His Tyr Arg Val Ala 180 185 190 ggt tta agc caa gat gaa gaa gga aat gtt att att ggg aat cga gtt 624 Gly Leu Ser Gln Asp Glu Glu Gly Asn Val Ile Ile Gly Asn Arg Val 195 200 205 att gct aaa att tct cgt caa gag gta gcc cgc cac ttc atg caa cct 672 Ile Ala Lys Ile Ser Arg Gln Glu Val Ala Arg His Phe Met Gln Pro 210 215 220 gct cct caa aaa tac ttg gac aaa tta cta gaa gca ggc aaa ata acg 720 Ala Pro Gln Lys Tyr Leu Asp Lys Leu Leu Glu Ala Gly Lys Ile Thr 225 230 235 240 cct ttg caa gct caa cta gct gcc cga gta cct atg gct gat gat att 768 Pro Leu Gln Ala Gln Leu Ala Ala Arg Val Pro Met Ala Asp Asp Ile 245 250 255 aca gtg gaa gca gat tct ggt gga cat acc gat aat cgt cca ttg gta 816 Thr Val Glu Ala Asp Ser Gly Gly His Thr Asp Asn Arg Pro Leu Val 260 265 270 gcg tta ttg cct tct att att cgc caa aga gac caa tta caa gcc caa 864 Ala Leu Leu Pro Ser Ile Ile Arg Gln Arg Asp Gln Leu Gln Ala Gln 275 280 285 tac caa ttt agt act cct atc cga gtg gga gct gct gga gga att ggc 912 Tyr Gln Phe Ser Thr Pro Ile Arg Val Gly Ala Ala Gly Gly Ile Gly 290 295 300 acc cct gaa gca gcc ttg tct gcc ttt atg atg gga gca gcc tat gtg 960 Thr Pro Glu Ala Ala Leu Ser Ala Phe Met Met Gly Ala Ala Tyr Val 305 310 315 320 gta act ggt tca atc aac caa gca tgt ata gag gca ggt act tcc gaa 1008 Val Thr Gly Ser Ile Asn Gln Ala Cys Ile Glu Ala Gly Thr Ser Glu 325 330 335 cat gta aga aaa tta ttg gct aat gtt gcc caa aca gat gta atg atg 1056 His Val Arg Lys Leu Leu Ala Asn Val Ala Gln Thr Asp Val Met Met 340 345 350 gct cct gct tct gat atg ttt gaa atg ggg gta gaa ttg caa gtc ctc 1104 Ala Pro Ala Ser Asp Met Phe Glu Met Gly Val Glu Leu Gln Val Leu 355 360 365 aaa cgt gga aca ttg ttt gga cca aga gca aaa aaa cta tat gaa tac 1152 Lys Arg Gly Thr Leu Phe Gly Pro Arg Ala Lys Lys Leu Tyr Glu Tyr 370 375 380 tac atg cag tac aat tcc att gat gaa att cca gct gcc gag cgt gag 1200 Tyr Met Gln Tyr Asn Ser Ile Asp Glu Ile Pro Ala Ala Glu Arg Glu 385 390 395 400 aag tta gaa aaa caa aca ttc aag aaa ccc tta gaa gaa gta tgg caa 1248 Lys Leu Glu Lys Gln Thr Phe Lys Lys Pro Leu Glu Glu Val Trp Gln 405 410 415 gga tgt att agc ttt ttt gaa gag aga gac cct agc caa att gag cgg 1296 Gly Cys Ile Ser Phe Phe Glu Glu Arg Asp Pro Ser Gln Ile Glu Arg 420 425 430 gct aaa aat aat ccc aag aga aaa atg gca tta att ttc cgt tgg tat 1344 Ala Lys Asn Asn Pro Lys Arg Lys Met Ala Leu Ile Phe Arg Trp Tyr 435 440 445 ttg ggc ttg tct tct aac tgg gca aat gct ggt gtt aag gaa aga att 1392 Leu Gly Leu Ser Ser Asn Trp Ala Asn Ala Gly Val Lys Glu Arg Ile 450 455 460 agc gat atg caa att tgg tgt ggc cct gcg atg ggc tcc ttt aac gat 1440 Ser Asp Met Gln Ile Trp Cys Gly Pro Ala Met Gly Ser Phe Asn Asp 465 470 475 480 tgg gta aaa gga acc tac ttg ga gat tac caa aaa cgt caa gcg gca 1488 Trp Val Lys Gly Thr Tyr Leu Glu Asp Tyr Gln Lys Arg Gln Ala Ala Ala 485,490,495 gaa gtt gct tgg cat att atg gaa ggg gcg gct tat ctt tat aga gtg 1536 Glu Val Ala Trp His Ile Met Glu Gly Ala Ala Tyr Leu Tyr Arg Val 500 505 510 1584 1584 1584 1584 Gln Ala Leu Ala Thr Gln Gly Ile Lys Leu Pro Leu Glu Trp Ala Lys 515,520,525 tat aat ccc aat cca gtc cct aat ttt tct cta gca att agc tag 1629 Tyr Asn Pro Asn Pro Val Pro Asn Phe Ser Leu Ala Ile Ser 530 535 540 <210> 62 <211> 542 <212> PRT <213> Aureispira marina (Aureispira marina) <400> 62 Met Ile Thr Phe Ser Gly Ile Lys Gln Gln Leu Tyr Trp Lys Gly Ser 1 5 10 15 Pro Arg Ala Ile Ser Phe Asp Ala Ala Gly Met Glu Gln Lys Leu Lys 20 25 30 Asn Thr Gln Glu His Cys Phe Val Val Glu Asp Phe Ala Gly Arg Val 35 40 45 Gly Ile Ala Asn Ala Gly Glu Leu Thr Thr Asp Ser Lys Gly Leu Gln 50 55 60 Val Leu Ala Met Val Ala Pro Met Thr Ala Glu Gln Leu Gly Asp Ala 65 70 75 80 Thr Phe Arg Lys Asp Tyr Lys Leu Lys Tyr Ala Tyr Lys Thr Gly Ala 85 90 95 Met Ala Asn Gly Ile Ala Ser Glu Asp Leu Val Ile Ala Met Gly Lys 100 105 110 Ala Gly Leu Leu Gly Ser Phe Gly Ala Ala Gly Leu Ile Pro Ser Arg 115 120 125 Val Glu Gln Ala Ile Asp Thr Ile Gln Gln Ala Leu Pro Thr Gln Ser 130 135 140 Tyr Ala Phe Asn Leu Ile His Ser Pro Asn Glu Pro Ala Leu Glu Glu 145 150 155 160 Gly Ala Val Lys His Phe Leu Ala Arg Gly Val Asn Val Val Glu Ala 165 170 175 Ser Ala Phe Leu Asn Leu Thr Leu Asn Ile Val His Tyr Arg Val Ala 180 185 190 Gly Leu Ser Gln Asp Glu Glu Gly Asn Val Ile Ile Gly Asn Arg Val 195 200 205 Ile Ala Lys Ile Ser Arg Gln Glu Val Ala Arg His Phe Met Gln Pro 210 215 220 Ala Pro Gln Lys Tyr Leu Asp Lys Leu Leu Glu Ala Gly Lys Ile Thr 225 230 235 240 Pro Leu Gln Ala Gln Leu Ala Ala Arg Val Pro Met Ala Asp Asp Ile 245 250 255 Thr Val Glu Ala Asp Ser Gly Gly His Thr Asp Asn Arg Pro Leu Val 260 265 270 Ala Leu Leu Pro Ser Ile Ile Arg Gln Arg Asp Gln Leu Gln Ala Gln 275 280 285 Tyr Gln Phe Ser Thr Pro Ile Arg Val Gly Ala Ala Gly Gly Ile Gly 290 295 300 Thr Pro Glu Ala Ala Leu Ser Ala Phe Met Met Gly Ala Ala Tyr Val 305 310 315 320 Val Thr Gly Ser Ile Asn Gln Ala Cys Ile Glu Ala Gly Thr Ser Glu 325 330 335 His Val Arg Lys Leu Leu Ala Asn Val Ala Gln Thr Asp Val Met Met 340 345 350 Ala Pro Ala Ser Asp Met Phe Glu Met Gly Val Glu Leu Gln Val Leu 355 360 365 Lys Arg Gly Thr Leu Phe Gly Pro Arg Ala Lys Lys Leu Tyr Glu Tyr 370 375 380 Tyr Met Gln Tyr Asn Ser Ile Asp Glu Ile Pro Ala Ala Glu Arg Glu 385 390 395 400 Lys Leu Glu Lys Gln Thr Phe Lys Lys Pro Leu Glu Glu Val Trp Gln 405 410 415 Gly Cys Ile Ser Phe Phe Glu Glu Arg Asp Pro Ser Gln Ile Glu Arg 420 425 430 Ala Lys Asn Asn Pro Lys Arg Lys Met Ala Leu Ile Phe Arg Trp Tyr 435 440 445 Leu Gly Leu Ser Ser Asn Trp Ala Asn Ala Gly Val Lys Glu Arg Ile 450 455 460 Ser Asp Met Gln Ile Trp Cys Gly Pro Ala Met Gly Ser Phe Asn Asp 465 470 475 480 Trp Val Lys Gly Thr Tyr Leu Glu Asp Tyr Gln Lys Arg Gln Ala Ala Ala 485,490,495 Glu Val Ala Trp His Ile Met Glu Gly Ala Ala Tyr Leu Tyr Arg Val 500 505 510 Gln Ala Leu Ala Thr Gln Gly Ile Lys Leu Pro Leu Glu Trp Ala Lys 515,520,525 Tyr Asn Pro Asn Pro Val Pro Asn Phe Ser Leu Ala Ile Ser 530 535 540 <210> 63 <211> 660 <212> DNA <213> Aureispira marina (Aureispira marina) <220> <221> CDS <222> (1)..(660) <400> 63 gtg ctt cat tg ctt tat atc aac tct gct gtg gtt caa gct act tat 48 Val Leu His Leu Leu Tyr Ile Asn Ser Wing Val Val Gln Thr Tyr 1 5 10 15 aca ttg aca gag tta ttg tta tta cca gat tct gtg aaa gag agg 96 Thr Leu Thr Glu Leu Leu Leu Leu Pro Asp Ser Val Lys Glu Arg 20 25 30 aca ctt cgc tat caa cag cca cag gat gcg tat aat ttt gta ttg gga 144 Thr Leu Arg Tyr Gln Gln Pro Gln Asp Ala Tyr Asn Phe Val Leu Gly 35 40 45 agg tta tta ttg caa caa gct ttg ttg gaa aag ggg ggg gca gca gaa 192 Arg Leu Leu Leu Gln Gln Ala Leu Leu Glu Lys Gly Gly Ala Ala Glu 50 55 60 gaa ttg gag gct ata caa tat agt tct aac caa aaa cct tgg ctg cct 240 Glu Leu Glu Ala Ile Gln Tyr Ser Ser Asn Gln Lys Pro Trp Leu Pro 65 70 75 80 agc ttg aat ttt aat att agc cat tcc caa gaa tgg gtg gct tgt gct 288 Ser Leu Asn Phe Asn Ile Ser His Ser Gln Glu Trp Val Ala Cys Ala 85 90 95 ttc tct agt gag caa gct gta ggc tta gat ata gaa gta cca aga ccc 336 Phe Ser Ser Glu Gln Ala Val Gly Leu Asp Ile Glu Val Pro Arg Pro 100 105 110 ctt aaa aaa act cat ttc aga cat tgt ttt tct ttg aaa gaa tgg gat 384 Leu Lys Thr His Phe Arg His Cys Phe Ser Leu Lys Glu Trp Asp 115 120 125 gaa att aca gca gat gtg ggg atg cac act ttt tat caa tat tgg aca 432 Glu Ile Thr Ala Asp Val Gly Met His Thr Phe Tyr Gln Tyr Trp Thr 130 135 140 gcc aag gag gct gtg ctt aaa gca caa gga ttg gat tta ggg catc 480 Ala Lys Glu Ala Val Leu Lys Ala Gln Gly Leu Asp Leu Gly His Leu 145 150 155 160 tta gat atg acc ata gtg gat ttg aag gag gtt tat gtt aag ttg cca 528 Leu Asp Met Thr Ile Val Asp Leu Lys Glu Val Tyr Val Lys Leu Pro 165 170 175 caa gaa aat caa att act cgt tgg cag ttg cag cat ttt tct ttg gat 576 Gln Glu Asn Gln Ile Three Arg Trp Gln Leu Gln His Phe Ser Leu Asp 180 185 190 aat agc cct gct tat gct tgt tta tgt gct aag ttt gtc aaa gat ttt 624 Asn Ser Pro Ala Tyr Ala Cys Leu Cys Ala Lys Phe Val Lys Asp Phe 195 200 205 tct att aat tta cta gat gta gat tct tta ttc tag 660 Ser Ile Asn Leu Leu Asp Val Asp Ser Leu Phe 210 215 <210> 64 <211> 219 <212> PRT <213> Aureispira marina <400> 64 Val Leu His Leu Leu Tyr Ile Asn Ser Ala Val Val Gln Ala Thr Tyr 1 5 10 15 Thr Leu Thr Glu Leu Leu Leu Leu Leu Pro Asp Ser Val Lys Glu Arg 20 25 30 Thr Leu Arg Tyr Gln Gln Pro Gln Asp Ala Tyr Asn Phe Val Leu Gly 35 40 45 Arg Leu Leu Leu Gln Gln Ala Leu Leu Glu Lys Gly Gly Ala Ala Glu 50 55 60 Glu Leu Glu Ala Ile Gln Tyr Ser Ser Asn Gln Lys Pro Trp Leu Pro 65 70 75 80 Ser Leu Asn Phe Asn Ile Ser His Ser Gln Glu Trp Val Ala Cys Ala 85 90 95 Phe Ser Ser Glu Gln Ala Val Gly Leu Asp Ile Glu Val Pro Arg Pro 100 105 110 Leu Lys Lys Thr His Phe Arg His Cys Phe Ser Leu Lys Glu Trp Asp 115 120 125 Glu Ile Thr Ala Asp Val Gly Met His Thr Phe Tyr Gln Tyr Trp Thr 130 135 140 Ala Lys Glu Ala Val Leu Lys Ala Gln Gly Leu Asp Leu Gly His Leu 145 150 155 160 Leu Asp Met Thr Ile Val Asp Leu Lys Glu Val Tyr Val Lys Leu Pro 165 170 175 Gln Glu Asn Gln Ile Thr Arg Trp Gln Leu Gln His Phe Ser Leu Asp 180 185 190 Asn Ser Pro Ala Tyr Ala Cys Leu Cys Ala Lys Phe Val Lys Asp Phe 195 200 205 Ser Ile Asn Leu Leu Asp Val Asp Ser Leu Phe 210 215 <210> 65 <211> 7746 <212> DNA <213> Photobacterium profundum SS9 <220> <221> CDS <222> (1)..(7746) <400> 65 atg ggt gtt aag cgg aga ctc atg atg agc caa acc ccg aaa acc acg 48 Met Gly Val Lys Arg Arg Leu Met Met Ser Gln Thr Pro Lys Thr Thr 1 5 10 15 tct gaa tcg cag ga gat acg cga ctc aat aaa cgt ctt aaa gac atg 96 Ser Glu Ser Gln Glu Asp Thr Arg Leu Asn Lys Arg Leu Lys Asp Met 20 25 30 cca att gcg att gtt ggc atg gcg agt atg ttt gcg aat tcc cgt tac 144 Pro Ile Ala Ile Val Gly Met Ala Ser Met Phe Ala Asn Ser Arg Tyr 35 40 45 ttg aat aag ttc tgg gat ctt atc agc gag aaa at gat gct att aca 192 Leu Asn Lys Phe Trp Asp Leu Ser Glu Lys Ile Asp Ala Ile Thr 50 55 60 gaa gtg cct gaa act cac tgg cgc cca gaa gat tat tac gat gca aac 240 Glu Val Pro Glu Thr His Trp Arg Pro Glu Asp Tyr Tyr Asp Ala Asn 65 70 75 80 aaa agc aca ccg gat aag tct tac tgt aag cgt ggt ggc ttt ata cct 288 Lys Ser Thr Pro Asp Lys Ser Tyr Cys Lys Arg Gly Gly Phe Ile Pro 85 90 95 gaa gtt gat ttc aac cca atg gaa ttc ggg ctt ccg cct aac att ctt 336 Glu Val Asp Phe Asn Pro Met Glu Phe Gly Leu Pro Pro Asn Ile Leu 100 105 110 gag cta act gat acg tca cag cta ctt tca ctg atc gta gca aaa gaa 384 Glu Leu Thr Asp Thr Ser Ser Gln Leu Leu Ser Ile Val Ala Ala Lys Glu 115 120 125 gta ttg gct gat gcc aaa ctt ccg gaa aca tac gac cgt gat aaa atc ​​432 Val Leu Ala Asp Ala Lys Leu Pro Glu Thr Tyr Asp Arg Asp Lys Ile 130 135 140 ggt att acc ctt ggt gtg ggt ggt ggt cag aag atc agt caa agc ctt 480 Gly Ile Thr Leu Gly Val Gly Gly Gly Gln Lys Ile Ser Gln Ser Leu 145 150 155 160 aac gct cgt ctt caa tac cct gtt cct c aaa aaa gta ttc aaa aac agt 528 Asn Ala Arg Leu Gln Tyr Pro Val Leu Lys Lys Val Phe Lys Asn Ser 165 170 175 ggt atc act gac gac agt gaa atg ctg att aag aaa ttc caa gat 576 Gly Ile Thr Asp Glu Asp Ser Glu Met Leu Ile Lys Lys Phe Gln Asp 180 185 190 caa tac to cac tgg gaa gaa aat tca ttc cct ggt tca ctg ggt aac 624 Gln Tyr Ile His Trp Glu Glu Asn Ser Phe Pro Gly Ser Leu Gly Asn 195 200 205 gtt att tcc ggc cgt att gct aac cgc ttc gac ctt ggt ggc atg aac 672 Val Ile Ser Gly Arg Ile Ala Asn Arg Phe Asp Leu Gly Gly Met Asn 210 215 220 tgt gtc gtt gat gca gca tgt gca ggc tct ctt gct gca ttg cgt atg 720 Cys Val Val Asp Ala Ala Cys Ala Gly Ser Leu Ala Ala Leu Arg Met 225 230 235 240 gca tta agc gag ctt gtt gaa ggc cgc agc gaa atg att aca ggt 768 Ala Leu Ser Glu Leu Val Glu Gly Arg Ser Glu Met Met Ile Thr Gly 245 250 255 ggt gtg tgt acc gat aac tca cca acc atg tac atg agc ttc tct aaa 816 Gly Val Cys Thr Asp Asn Ser Pro Thr Met Tyr Met Ser Phe Ser Lys 260 265 270 aca ccg gca ttc acg aca aac gaa aca att caa cca ttc gat att gac 864 Thr Pro Ala Phe Thr Thr Asn Glu Thr Ile Gln Pro Phe Asp Ile Asp 275 280 285 tcg aaa ggt atg atg att ggt gaa ggt atc ggt atg at gcg ctt aaa 912 Ser Lys Gly Met Met Ile Gly Glu Gly Ile Gly Met Ile Ala Leu Lys 290 295 300 cgt ctt gaa gac gca gag cgt gat ggc gac cgt atc tat tcc gtg att 960 Arg Leu Glu Asp Ala Glu Arg Asp Gly Asp Arg Ile Tyr Ser Val Ile 305 310 315 320 aaa ggt gtt ggt gca tct tca gac ggt aaa ttt aag agt att tat gcg 1008 Lys Gly Val Gly Ala Ser Ser Asp Gly Lys Phe Lys Ser Ile Tyr Ala 325 330 335 cct cgt cct gaa ggt cag gct aag gca ctt aaa cgt gct tac gac gat 1056 Pro Arg Pro Glu Gly Gln Ala Lys Ala Leu Lys Arg Ala Tyr Asp Asp 340 345 350 gca ggt ttc gca ccg cac aca ctt ggc tta ctt gaa gcc cac ggc aca 1104 Ala Gly Phe Ala Pro His Thr Leu Gly Leu Glu Ala His Gly Thr 355 360 365 ggc aca gca gca ggt gat gtg gca gaa ttc agt ggt ctt aac tct gta 1152 Gly Thr Ala Ala Gly Asp Val Ala Glu Phe Ser Gly Leu Asn Ser Val 370 375 380 ttc agt gaa ggc at gac gaa aag caa cac atc gca tta ggt tca gtg 1200 Phe Ser Glu Gly Asn Asp Glu Lys Gln His Ile Ala Leu Gly Ser Val 385 390 395 400 aaa tca cag att ggt cac act aaa tca gcg ggt act gcg ggt cta 1248 Lys Ser Gln Ile Gly His Thr Lys Ser Thr Ala Gly Thr Ala Gly Leu 405 410 415 atc aaa gcg tct tta gca ctg cac cat aaa gta ctg ccg cca aca atc ​​1296 Ile Lys Ala Ser Leu Ala Leu His His Lys Val Leu Pro Pro Thr Ile 420 425 430 aat gta acc agc cct aac cct aaa ctg aat att gac tcg cct ttc 1344 Asn Val Thr Ser Pro Asn Pro Lys Leu Asn Ile Glu Asp Ser Pro Phe 435 440 445 tac ctc aat aca cag acg cgt cca tgg atg caa cgt gtc gat ggt aca 1392 Tyr Leu Asn Thr Gln Thr Arg Pro Trp Met Gln Arg Val Asp Gly Thr 450 455 460 ccg cgt cgt gct ggt gtc agt tca ttt ggt ttc ggt ggt aca aac ttc 1440 Pro Arg Arg Ala Gly Val Ser Ser Phe Gly Phe Gly Gly Thr Asn Phe 465 470 475 480 cac att gta ttg gaa gaa tac aca cca gaa cat gca cgc ggt gac aaa 1488 His Ile Val Leu Glu Glu Tyr Thr Pro Glu His Ala Arg Gly Asp Lys 485,490,495 tac cgt cag cgc caa gtc gca caa acg tta ttg ttg agc gct gcg tct 1536 Tyr Arg Gln Arg Gln Val Ala Gln Thr Leu Leu Phe Ser Ala Ala Ser 500 505 510 cgc gaa gca ctg att gct agc tta aaa gag aca tca gct aac ctt gca 1584 Arg Glu Ala Leu Ile Ser Leu Lys Glu Thr Ser Ala Asn Leu Ala 515,520,525 aac gat agc gtg aat ctt gaa aca ctg gct gaa agc cat ggt tta cgc 1632 Asn Asp Ser Val Asn Leu Glu Thr Leu Ala Glu Ser His Gly Leu Arg 530 535 540 agc atc gaa gta tca cat gca cgt tta ggt cta gct gtt aaa aca ggc 1680 Ser Ile Glu Val Ser His Ala Arg Leu Gly Leu Ala Val Lys Thr Gly 545 550 555 560 gaa gag cta aac acc cag ctt gct CA gcg att tca aac cta gaa agc 1728 Glu Glu Leu Asn Thr Gln Leu Ala Gln Ala Ile Ser Asn Leu Glu Ser 565,570,575 caa act aaa gcg cac tgg cag ctt cct agt ggc aca agc tac cgc gaa 1776 Gln Thr Lys Ala His Trp Gln Leu Ser Gly Thr Ser Tyr Arg Glu 580,585,590 tca gcg ctt gta agc ggc aat gat tca gca aaa gtt gct gca ttg ttt 1824 Leu Val Val Ser Gly Asn Asp Lys Val Val Val Val Phe Phe 595,600,605 gcc ggt caa ggt tca cag tac ctc aac atg ggc cgt gag cta gcg tgc 1872 Gly Gln Gly Ser Gln Tyr Leu Asn Met Gly Arg Glu Leu Ala Cys 610 615 620 cat tac cct gaa atg cgc caca cag tta gcg aaa gcc gat caa gta ttt 1920 His Tyr Pro Glu Met Arg Gln Gln Leu Ala Lys Ala Asp Gln Val Phe 625 630 635 640 ggt cag aat aag aaa aca gca ctg tca cag gtt ctg ttc cct att cca 1968 Gly Gln Asn Lys Lys Thr Ala Leu Served Gln Val Leu Phe Pro Ile Pro 645,650,655 atg ttc aat aaa gaa agt aca caa gca caa gag gct tta ctg act aat 2016 Met Phe Asn Lys Glu Ser Thr Gln Ala Gln Glu Ala Leu Thr Asn 660,665,670 acc gct aat gca cag agt gca atc ​​ggt gtg atg tcg atg ggc cag ttt 2064 Thr Ala Asn Ala Gln Ser Ala Ile Gly Val Met Ser Met Gly Gln Phe 675,680,685 gaa cta cta acg caa gca ggc ttt aaa gcc gac atg gtt gca ggt cac 2112 Glu Leu Leu Thr Gln Ala Gly Phe Lys Ala Asp Met Val Ala Gly His 690,695,700 agc ttc ggt gag tta agt gcc cta tgc gct tct ggt gtt atc tct caa 2160 Ser Phe Gly Glu Leu Ser Ala Leu Cys Ala Ser Gly Val Ile Ser Gln 705 710 715 720 gat gat tac tac cag ctt gct ttt gca cgc ggt aac gca atg gca gca 2208 Asp Asp Tyr Tyr Gln Leu Ala Phe Ala Arg Gly Asn Ala Met Ala Ala 725 730 735 aca cca gca gaa ggt gat agc ggt aca atg tac gct gtt att ctt gac 2256 Thr Pro Ala Glu Gly Asp Ser Gly Thr Met Tyr Ala Val Ile Leu Asp 740,745,750 gct gat aag ctg gca gat gtt gaa aag tgc att agt gca ttt gaa ggc 2304 Asp Lys Leu Ala Asp Val Glu Lys Cys Ile Served Ala Phe Glu Gly 755,760,765 gta agc att gct aat tac aac gca cca aca caa cta gtt att gcg ggc 2352 There Will Be On The Tyr Asn Only Pro Thr Gln Leu Will Only Be On Gly 770,775,780 cct acc gac agt gct caa ctt gct gca aaa gca cta aca gag caa ggc 2400 Pro Thr Asp Ser Al Gln Leu Allele Lys Allocation Thr Glu Gln Gly 785,790,795,800 ttc aaa gcg att cct ctt cct gtt tct ggc gct tc cac acg cca tta 2448 Phe Lys Ala Ile Pro Leu Pro Val Ser Gly Ala Phe His Thr Pro Leu 805 810 815 gtt gct cac gcg caa aaa cct ttt gca gca gct att gat aaa gca acg 2496 Val Ala His Ala Gln Lys Pro Phe Ala Ala Ala Ile Asp Lys Ala Thr 820 825 830 ttc agc act cca gca ttg ccg ttg tat tca aat gca acc ggt gaa ctg 2544 Phe Ser Thr Pro Ala Leu Pro Leu Tyr Ser Asn Ala Thr Gly Glu Leu 835 840 845 cat aag aac gat ggc aag gcc att aag aaa gcg ttc aag caa cat atg 2592 His Lys Asn Asp Gly Lys Ala Ile Lys Lys Ala Phe Lys Gln His Met 850 855 860 ttg caa tct gtt cgt ttc agc aca cag ctt gaa gct atg tat gat gct 2640 Leu Gln Ser Val Arg Phe Ser Thr Gln Leu Glu Ala Met Tyr Asp Ala 865 870 875 880 ggc gca cgt gtc ttt gtt gag ttc gga cca aag aac att cta caa aag 2688 Gly Ala Arg Val Phe Val Glu Phe Gly Pro Lys Asn Ile Leu Gln Lys 885,890,895 ctc gtt gag aag acg tta acc aat aaa gcc gat gag ctt tgc acg atc 2736 Leu Val Glu Lys Thr Leu Thr Asn Lys Ala Asp Glu Leu Cys Thr Ile 900 905 910 agt att aac ccg aac cct aag ggt gat agt gat cag caa tta cgc tta 2784 Ser Ile Asn Pro Asn Pro Lys Gly Asp Ser Asp Gln Gln Leu Arg Leu 915,920,925 gcc gca gtt caa ctc gct gtt gtc ggt atc tcg cta gac aat atc gac 2832 Ala Ala Val Gln Leu Ala Val Val Gly Ile Ser Leu Asp Asn Ile Asp 930,935,940 ccg tat caa gca gag att gcg cca cca gca gca aca tca cca atg aac 2880 Pro Tyr Gln Wing Glu Ile Wing Pro Pro Wing Thr Wing Be Pro Met Asn 945 950 955 960 atc aaa cta aac gcg aat tac atc agt cca gct act cgt gca aaa 2928 Ile Lys Leu Asn Ala Asn Tyr Ile Ser Pro Ala Thr Arg Ala Lys 965,970,975 atg gcg aag tca tta aca act ggc gaa gta agc aca aaa act gaa atc ​​2976 Met Ala Lys Ser Leu Thr Gly Glu Val Ser Thr Lys Thr Glu Ile 980,985,990 GTT GAAAA GTC GTT GAG AAG AAT GTG GAAAA GA GTG ATT AAA ACG 3024 Val Glu Lys Val Val Glu Lys Ile Val Glu Lys Glu Val Ile Lys Thr 995 1000 1005 gaa att cgt gaa gta ccc gtt gct gc gcg cca acg cag gct gta 3069 Glue Ile Arg Glu Val Pro Val Wing Wing Wing Pro Thr Gln Wing Val 1010 1015 1020 act gta cag tca aca gca caa gca gcg cca cag cca gtg gta aca 3114 Thr Val Gln Ser Thr Ala Gln Ala Ala Pro Gln Pro Val Val Thr 1025 1030 1035 aca gcg cca gct caa gtt gtt aca caa gca acg tca caa ctg cca 3159 Thr Ala Pro Ala Gln Val Val Thr Gln Ala Thr Ser Gln Leu Pro 1040 1045 1050 gtc ggc gag gca tcg ttg cat gct ttc ttc agt gca caa cag cag 3204 Val Gly Glu Ala Ser Leu His Ala Phe Phe Ser Ala Gln Gln Gln 1055 1060 1065 gca gct gaa ctt cat cag cag ttc tta gca att cct cag caa tac 3249 Ala Ala Glu Leu His Gln Gln Phe Leu Ala Ile Pro Gln Gln Tyr 1070 1075 1080 ggt gat acg ttc acg gca ttg atg aca gaa caa gct aaa atg gca 3294 Gly Asp Thr Phe Thr Ala Leu Met Thr Glu Gln Ala Lys Met Ala 1085 1090 1095 acg gct ggt att gcg att cca gaa agc cta caa cgt tca atg gag 3339 Thr Ala Gly Ile Ala Ile Pro Glu Ser Leu Gln Arg Ser Met Glu 1100 1105 1110 cta ttc cac cag cac caa gct gaa acg tta aaa gca cat gcc cac 3384 Leu Phe His Gln His Gln Ala Glu Thr Leu Lys Ala His Ala His 1115 1120 1125 tac ctt gaa tta caa gca aac agc aat aac tct gcg tta ggt atg 3429 Tyr Leu Glu Leu Gln Ala Asn Ser Asn Asn Ser Ala Leu Gly Met 1130 1135 1140 ttg act tca caa gcg cct gct cat cag gtt cct gtt tat cag acg 3474 Leu Thr Ser Gln Ala Pro Ala His Gln Val Pro Val Tyr Gln Thr 1145 1150 1155 cca att cag caa gta tca gtg gct ccg gct cct gct gca cca gta 3519 Pro Island Gln Gln Val Be Val Wing Pro Wing Pro Wing Pro Val 1160 1165 1170 gtt acg cca gta gtt gct gcg cca gtc gcg aca cct acg cca att 3564 Val Thr Pro Val Val Ala Ala Pro Val Ala Thr Pro Thr Pro Ile 1175 1180 1185 aag gct gtt att caa act caa tca gcg cct gtc gct tca gca 3609 Lys Ala Val Ile Gln Thr Gln Gln Ser Wing Pro Val Ala Ser Wing 1190 1195 1200 cca atc ​​gcg gca cct gtt aca cag aca gtt aaa cca aca cct gtt 3654 Pro Ile Ala Ala Pro Val Thr Gln Thr Val Lys Pro Thr Pro Val 1205 1210 1215 gtt CA gCA gct gta gca cca gca gca gtt CA act gcg aat 3699 Val Gln Ala Ala Val Ala Pro Gln Ala Ala Val Gln Thr Ala Asn 1220 1225 1230 cca gaa caa gtt atg ctg gaa gtg gtt gcg gag aaa act ggc tac 3744 Pro Glu Gln Val Met Leu Glu Val Val Ala Glu Lys Thr Gly Tyr 1235 1240 1245 cct acc gag atg tta gat ctt gat atg gat atg gaa gca gac cta 3789 Pro Thr Glu Met Leu Asp Leu Asp Met Asp Met Glu Ala Asp Leu 1250 1255 1260 ggt atc gac tcg att aaa cgt gtt gag att cta ggt aca gtg caa 3834 Gly Ile Asp Ser Ile Lys Arg Val Glu Ile Leu Gly Thr Val Gln 1265 1270 1275 gac caa atg cca aac ctg cca gag cta agc cct gaa gat tta gca 3879 Asp Gln Met Pro Asn Leu Pro Glu Leu Ser Pro Glu Asp Leu Ala 1280 1285 1290 gag tgt cgt aca ctg cgc gaa atc ​​gtg act tac atg aac agt aaa 3924 Glu Cys Arg Thr Leu Arg Glu Ile Val Thr Tyr Met Asn Ser Lys 1295 1300 1305 atg cca gca gct gct gca tct gct cca gta acg tca gca tca aac 3969 Met Pro Ala Ala Ala Ala Ser Ala Pro Val Thr Ser Ala Ser Asn 1310 1315 1320 ggc tta gac gca gca caa gtt caa agc aca atg ctt gaa gtg gtt 4014 Gly Leu Asp Ala Ala Gln Val Gln Ser Thr Met Leu Glu Val Val 1325 1330 1335 gca gat aag acg ggt tac cca acc gaa atg ctt gat cta gaa atg 4059 Ala Asp Lys Thr Gly Tyr Pro Thr Glu Met Leu Asp Leu Glu Met 1340 1345 1350 gat atg gaa gca gat ttg ggt atc gac tct att aag cgt gtt gaa 4104 Asp Met Glu Ala Asp Leu Gly Ile Asp Ser Ile Lys Arg Val Glu 1355 1360 1365 att ctt ggt acg gtt caa gac cag cta ccg acg ctt cct gag tta 4149 Ile Leu Gly Thr Val Gln Asp Gln Leu Pro Thr Leu Pro Glu Leu 1370 1375 1380 agc cct gaa gat ttg gct gaa tgt cgt acg cta ggt gaa atc ​​gta 4194 Ser Pro Glu Asp Leu Ala Glu Cys Arg Thr Leu Gly Glu Ile Val 1385 1390 1395 agc tac atg aac agc aag ctt cct gca gcg tct gca gta gct gca 4239 Be Tyr Met Asn Be Lys Leu Pro Wing Be Wing Val Wing Wing 1400 1405 1410 cct gtt gct tct gct cca gtc gcg tca gca tca aac gtt tta gac 4284 Pro Val Wing Be Wing Pro Val Wing Be Wing Be Asn Gly Leu Asp 1415 1420 1425 gca gca CA gtg CA acc aca atg cta gac gtt gtt gca gat aag 4329 Only Gln Only Gln Thr Thr Met Leu Asp Only Only Asp Lys 1430 1435 1440 act ggc tac cca act gaa atg cta gac ctt gca atg gac atg gaa 4374 Thr Gly Tyr Pro Thr Glu Met Leu Asp Leu Ala Met Asp Met Glu 1445 1450 1455 gca gat ttg ggt atc gac tct atc aaa cgt gtt gaa att cta ggt 4419 Only Asp Leu Gly With Asp Ser Leu Gly With Arg Val Glu With Leu Gly 1460 1465 1470 acc gtg caa gac caa cta ccg ggc tta cca gaa ctg aac ccc gaa 4464 Thr Val Gln Asp Gln Lew Pro Gly Lew Pro Glu Lew Asn Pro Glu 1475 1480 1485 gat tta gct gag tgt cgt acg cta ggc gaa atc ​​gtt gat tac atg 4509 Asp With Glu Cys Arg Thr With Gly Glu Ile Val Asp Tyr Met 1490 1495 1500 aac agc aaa tta cct gct gtc tct aca caa aat gta gcg att CA 4554 Asn Will Be Lys Leu Pro Wing Will Be Thr Gln Asn Will Have Ile Gln 1505 1510 1515 aca gct gct cca gtc gcg tca gca tca aac ggt tta gat gca gca 4599 Thr Wing Wing Pro Val Wing Ser Wing Ser Asn Gly Leu Asp Wing Wing 1520 1525 1530 CA GTT CA ggc aca atg ctt gag gtg gtt gcc gat aaa act ggc 4644 Gln Val Gln Gly Thr Met Leu Glu Val Val Ala Asp Lys Thr Gly 1535 1540 1545 tac cca gca gaa atg cta gac ttt gca atg gac atg gaa gca gac 4689 Tyr Pro Ala Glu Met Leu Asp Phe Ala Met Asp Met Glu Ala Asp 1550 1555 1560 ctt ggt atc gac tcg atc aag cgt gtt gaa att cta ggt acc gtg 4734 Leu Gly Ile Asp Ser Ile Lys Arg Val Glu Ile Leu Gly Thr Val 1565 1570 1575 caa gac caa cta ccg ggc tta cct gag ctg aac cct gaa gat tta 4779 Gln Asp Gln Leu Pro Gly Leu Pro Glu Leu Asn Pro Glu Asp Leu 1580 1585 1590 gct gag tgt cgt aca ctg ggc gaa atc gtt gac tac atg aac agc 4824 Ala Glu Cys Arg Thr Leu Gly Glu Ile Val Asp Tyr Met Asn Ser 1595 1600 1605 aaa cta cca gca gcc tct aca caa aat gta gcg gta caa aca gta 4869 Lys Leu Pro Ala Ala Ser Thr Gln Asn Val Ala Val Gln Thr Val 1610 1615 1620 gca gca cca gta gca acg gct cct gca aca aac ggc tta gac gca 4914 Ala Ala Pro Val Ala Thr Ala Pro Ala Thr Asn Gly Leu Asp Ala 1625 1630 1635 GCA CAT GTT CAAAC ACG ATG ATG AAT GTA GTT GCC GAT AAA ACA 4959 Only His Will Gln Asn Thr Met Met Asn Will Only Asp Lys Thr 1640 1645 1650 ggt tat cca gca gaa atg cta gac ctt gca atg gac atg gaa gca 5004 Gly Tyr Pro Ala Glu Met Leu Asp Leu Ala Met Asp Met Glu Ala 1655 1660 1665 gac ctt ggt atc gac tct atc aag cgt gtt gaa att cta ggt acc 5049 Asp Leu Gly With Asp Ser With Lys Arg Val Glu With Leu Gly Thr 1670 1675 1680 gtg caa gac caa cta ccg ggc tg cca gag ctt aac cct gaa gat 5094 Val Gln Asp Gln Leu Pro Gly Leu Pro Glu Leu Asn Pro Glu Asp 1685 1690 1695 tta gcg gag tgt cgt aca ctg ggc gaa atc ​​gtt gct tac atg caa 5139 Glu Alpha Cys Arg Thr Gly Glu Ile Val Val Tyr Met Gln 1700 1705 1710 agc aag ctt tct aat act tca gca gta gca gca cct tct gca cct 5184 Be Lys Leu Be Asn Thr Be Wing Val Wing Pro Be Wing Pro 1715 1720 1725 gct gtt gaa aac ctt gta gaa gcg att gca gaaca agc aat gta 5229 Ala Val Glu Asn Leu Val Glu Ala Ile Ala Glu Thr Ser Asn Val 1730 1735 1740 gag ctt cct cct cac agc gag gtg gcg cta aaa aag tta cca gcg 5274 Glu Leu Pro Pro His Being Glu Val Ala Leu Lys Lys Leu Pro Wing 1745 1750 1755 gta gat aaa tta gta gac tgt ttt tcc aaa gaa gct tgt atc gtg Val Asp Lys Leu Val Asp Cys Phe Ser Lys Glu Ala Cys Ile Val 1760 1765 1770 att acc gat gat ggt cac aat gcg ggt gtt cta gca gaa aag tta 5364 The Thr Asp Asp Gly His Asn Ala Gly Val Leu Ala Glu Lys Leu 1775 1780 1785 agt gca aac ggc ctt caa gtt gct gtt gta cgt agt cct cta tct 5409 Ser Ala Asn Gly Leu Gln Val Ala Val Val Arg Ser Pro Leu Ser 1790 1795 1800 gcc gcg tca ccg tta aac agc gaa atc ​​gcg agc tac aca tta gca 5454 Wing Wing To Be Pro Leo Asn To Be Glu Ile Wing To Be Tyr Thr Leu Wing 1805 1810 1815 agc att gat gac gct agt atc aaa act gtt att tca gac att gag 5499 Asp With Asp Only With Lys Thr Val With Asp With Glu 1820 1825 1830 agc aag caa aaa gaa att ggt gga ttc att cac tta cag cct ctt 5544 Formation of Lys Gln Lys Glu Ile Gly Gly Phe Ile His Leu Gln Pro Leu 1835 1840 1845 gca acc gat gct aaa aca gat aaa gca aca gct gta aca ttg cat 5589 Ala Thr Asp Ala Lys Thr Asp Lys Ala Thr Ala Val Thr Leu His 1850 1855 1860 gca acg gca aaa gaa agc att tct atg gct ttc cta ttc gcg aaa 5634 Ala Thr Ala Lys Glu Ser Ile Ser Met Ala Phe Leu Phe Ala Lys 1865 1870 1875 ttg ctt aaa act cag tta aac gca gca aaa aac cgc agt gcc ttc 5679 Leu Leu Lys Thr Gln Leu Asn Ala Ala Lys Asn Arg Ser Ala Phe 1880 1885 1890 ttt acg gta agt cgt att gat ggt ggc ttt ggt tac ttg aat gca 5724 Phe Thr Val Ser Arg Ile Asp Gly Gly Phe Gly Tyr Leu Asn Ala 1895 1900 1905 gaa caa ctt atc aat gca gaa ttg aac caa gcg gca tta tct ggt 5769 Glu Gln Leu Ile Asn Ala Glu Leu Asn Gln Ala Ala Leu Ser Gly 1910 1915 1920 tta acg aaa aca ttg agc cac gaa tgg tca aca gta ttc tgt cgc 5814 Leu Thr Lys Thr Leu Ser His Glu Trp Ser Thr Val Phe Cys Arg 1925 1930 1935 gca ctg gat gtt gcg cca acg ctt gat gct cgt cat ctt gca gaa 5859 Ala Leu Asp Val Ala Pro Thr Leu Asp Ala Arg His Leu Ala Glu 1940 1945 1950 gca gta aca gcc gaa tta ttc gat atc gat act cac act gtt gag 5904 Ala Val Thr Ala Glu Leu Phe Asp Ile Asp Thr His Thr Val Glu 1955 1960 1965 gtg ggt ctg gct gat gcg aat aac ggc gaa tct ggt cga gca aca 5949 Val Gly Leu Ala Asp Ala Asn Asn Gly Glu Ser Gly Arg Ala Thr 1970 1975 1980 ctg att gca acc aat gca ggt act gct cta aca aaa aat gcc tca 5994 Leu Ile Only Thr Asn Only Gly Thr Only Leu Thr Lys Asn Only On Ser 1985 1990 1995 gca aaa ctg gac aag aac gat aac gtg ctt gtg act ggc ggc gcg 6039 Ala Lys Leu Asp Lys Asn Asp Asn Val Leu Val Thr Gly Gly Ala 2000 2005 2010 aaa ggc gtt acg ttt gaa tgt gca tta aca ctg gct aaa cag tgc 6084 Lys Gly Val Thr Phe Glu Cys Ala Leu Thr Leu Ala Lys Gln Cys 2015 2020 2025 aaa tca cac ttc att ctt gca ggt cgt agt cag cat att acg gca 6129 Lys Ser Phe His Ile Leu Ala Gly Arg Ser Gln His Ile Thr Ala 2030 2035 2040 aac gaa ctg cca gaa tgg gca caa ggt aaa CA gca aac gag cta 6174 Asn Glu Leu Pro Glu Trp Ala Gln Gly Lys Gln Ala Asn Glu Leu 2045 2050 2055 aag cca gca gcc att cgc cat att caa aca tct ggt gag aaa cca 6219 Lys Pro Ala Ala Ile Arg His Ile Gln Thr Ser Gly Glu Lys Pro 2060 2065 2070 aca ccg aag aaa gta gat gcg tta ctc aag cct gta tta agc agc 6264 Thr Pro Lys Lys Val Asp Ala Leu Leu Lys Pro Val Leu Ser Ser 2075 2080 2085 ctt gaa att aac act gct ctt tct gca ttt gct aat gtg ggt gcg 6309 Leu Glu Ile Asn Thr Ala Leu Ser Ala Phe Ala Asn Val Gly Ala 2090 2095 2100 agt gct gaa tac ata agc ctt gac gta tca agc agt gat tct gtt 6354 Ser Ala Glu Tyr Ile Ser Leu Asp Val Ser Ser Ser Asp Ser Val 2105 2110 2115 gct aaa aca ctg tct cag ttc aat gat att aca ggt ctt att cac 6399 Ala Lys Thr Leu Ser Gln Phe Asn Asp Ile Thr Gly Leu Ile His 2120 2125 2130 ggc gca ggc gta ctg gct gac aag cat att ca gat aaa acg ctt 6444 Gly Ala Gly Val Leu Ala Asp Lys His Ile Gln Asp Lys Thr Leu 2135 2140 2145 gat gag tta aac ctt gtt tac ggc act aaa gta ggc ggt ctt gaa 6489 Asp Glu Leu Asn Leu Val Tyr Gly Thr Lys Val Gly Gly Leu Glu 2150 2155 2160 gca gtg ctt aac gca tta aac agc gac aag cta aaa ctg gtt gcg 6534 Ala Val Leu Asn Ala Leu Asn Ser Asp Lys Leu Lys Leu Val Ala 2165 2170 2175 atg ttc tca tca gca gct ggc ttc tac ggc aac act gga caa agc 6579 Met Phe Ser Ser Ala Ala Gly Phe Tyr Gly Asn Thr Gly Gln Ser 2180 2185 2190 gat tac gcg atg tcc aat gaa ata ttg aat aaa gcg gca tta cag 6624 Asp Tyr Only Met Ser Glu Asn With Leu Asn Lys Only With Gln 2195 2200 2205 cta tct gca cgt aac cct gaa gca aaa gta atg agc ttc aac tgg 6669 Leu Ser Ala Arg Asn Pro Glu Ala Lys Val Met Ser Phe Asn Trp 2210 2215 2220 gga ccg tgg gac ggc ggc atg gta aac gca gca tg aag aaa atg 6714 Gly Pro Trp Asp Gly Gly Met Val Asn Ala Ala Leu Lys Lys Met 2225 2230 2235 ttt act gac cgt ggt gta tac gtg att cct ctt caa gca ggt gct 6759 Phe Thr Asp Arg Gly Val Tyr Val Ile Pro Leu Gln Ala Gly Ala 2240 2245 2250 gaa cta ttc agc tct cag ctg cta agt gaa aca ggt atc caa ctg 6804 Glu Leu Phe Ser Gln Leu Leu Ser Glu Thr Gly Ile Gln Leu 2255 2260 2265 ctt gtg ggt aca agc atg caa ggt tca gac aac aag gaa gcc gcc gct 6849 Leu Val Gly Thr Ser Met Gln Gly Ser Asp Asn Lys Glu Ala Ala 2270 2275 2280 gta aaa ag ctt gat gcg gag tct atg cta gta gca agat agt ccg 6894 Val Lys Lys Leu Asp Ala Glu Ser Met Leu Val Ala Lys Ser Pro 2285 2290 2295 ctg aat tca agc att act gta aca cgc gat ctt gac ccg aaa gca 6939 Leu Asn Ser Ser Ile Thr Val Thr Arg Asp Leu Asp Pro Lys Ala 2300 2305 2310 atg cct ttc atc aat gat cac tgc to gcc ggt aac cca gtg tta 6984 Met Pro Phe Ile Asn Asp His Cys Ile Ala Gly Asn Pro Val Leu 2315 2320 2325 ccg aca gtg tgt gcc att caa tgg atg cgt gaa gca gca gag caa 7029 Pro Thr Val Cys Ala Ile Gln Trp Met Arg Glu Ala Ala Glu Gln 2330 2335 2340 ctg tta gga gcg aac gtt act gtt cgc gac tac aaa ctg ctt aaa 7074 Leu Leu Gly Ala Asn Val Thr Val Arg Asp Tyr Lys Leu Leu Lys 2345 2350 2355 ggc gtg atc ttt gat acg aat gaa ata caa acg ctc aca ttg aca 7119 Gly Val Ile Phe Asp Thr Asn Glu Ile Gln Thr Leu Thr Leu Thr 2360 2365 2370 ctg acg cca gac gaa aaa gca acg gat caa atc ​​aaa gca ttg atc 7164 Leu Thr Pro Asp Glu Lys With Three Asp Gln Ile Lys With Leu Ile 2375 2380 2385 agc tgc caa gat cgt cct cag tac aaa gcg atg ctg gtt gta gaa 7209 Ser Cys Gln Asp Arg Pro Gln Tyr Lys Ala Met Leu Val Val Glu 2390 2395 2400 ccc gta cca gca aca caa gct aaa acc ttt gta gcg aat tca aat 7254 Pro Val Pro Ala Thr Gln Ala Lys Thr Phe Val Ala Asn Ser Asn 2405 2410 2415 gaa ccc ata aca gct aaa gcc tta tac agt aat ggc acc ctg 7299 Glu Pro with Thr Thr Ala Lys Ala Leu Tyr Asn Gly Thr Leu 2420 2425 2430 ttc cat ggc cca aga ctg caa ggt att aca acg gtt gaa cgt ttt 7344 Phe His Gly Pro Arg Leu Gln Gly Ile Thr Thr Val Glu Arg Phe 2435 2440 2445 gat gat gct ggt ttg ctc gca cag tgc cag cta cca aca gtg gct Asp Asp Ala Gly Leu Leu Ala Gln Cys Gln Leu Pro Thr Val Ala 2450 2455 2460 gat aca gac tgt ggc gca ttc gtt cca acc caa cac ctt ggt ggt 7434 Asp Thr Asp Cys Gly Ala Phe Val Pro Thr Gln His Leu Gly Gly 2465 2470 2475 tgc cag cct ttc gct gaa gac tac tta tta caa gca atg ttg gtg Cys Gln Pro Phe Ala Glu Asp Tyr Leu Leu Gln Ala Met Leu Val 2480 2485 2490 tgg gcg cgc ttg aag tac ggg gct gca agt cta cct tct gcc att 7524 Trp Wing Arg Leu Lys Tyr Gly Wing To Be Leu Pro To Be Wing Ile 2495 2500 2505 ggt gaa ttt gtt tct tat gaa cca atg caa gcg ggt gat aaa ggt Gly Glu Phe Val Ser Tyr Glu Pro Met Gln Ala Gly Asp Lys Gly 2510 2515 2520 tgg tta gaa ctc gac gta att aaa aat acg acg cgt tca cta caa 7614 Trp of Glu and Asp Val Ile Asn Thr Thr Arg Ser of Gln 2525 2530 2535 gct aat atc tcg ctt tac cat caa gat ggt cgt tta agt gct gtt 7659 Ala Asn Ile Ser Leu Tyr His Gln Asp Gly Arg Leu Ser Ala Val 2540 2545 2550 atg aaa agc gct aaa gta acg atc agt aaa agc cta aat gag gca 7704 Put Lys Ser Ala Lys Val Thr Ile Ser Lys Ser Leu Asn Glu Ala 2555 2560 2565 ttt ttg gtg aag tct gag ca gag aag gag ctt ctg tca tag 7746 Phe Leu Val Lys Ser Glu Pro Glu Lys Glu Leu Leu Ser 2570 2575 2580 <210> 66 <211> 2581 <212> PRT <213> SS9 (Photobacterium profundum SS9) <400> 66 Met Gly Val Lys Arg Arg Leu Met Met Ser Gln Thr Pro Lys Thr Thr 1 5 10 15 Ser Glu Ser Gln Glu Asp Thr Arg Leu Asn Lys Arg Leu Lys Asp Met 20 25 30 Pro Ile Ala Ile Val Gly Met Ala Ser Met Phe Ala Asn Ser Arg Tyr 35 40 45 Leu Asn Lys Phe Trp Asp Leu Ile Ser Glu Lys Ile Asp Ala Ile Thr 50 55 60 Glu Val Pro Glu Thr His Trp Arg Pro Glu Asp Tyr Tyr Asp Ala Asn 65 70 75 80 Lys Ser Thr Pro Asp Lys Ser Tyr Cys Lys Arg Gly Gly Phe Ile Pro 85 90 95 Glu Val Asp Phe Asn Pro Met Glu Phe Gly Leu Pro Pro Asn Ile Leu 100 105 110 Glu Leu Thr Asp Thr Ser Gln Leu Leu Ser Leu Ile Val Ala Lys Glu 115 120 125 Val Leu Ala Asp Ala Lys Leu Pro Glu Thr Tyr Asp Arg Asp Lys Ile 130 135 140 Gly Ile Thr Leu Gly Val Gly Gly Gly Gln Lys Ile Ser Gln Ser Leu 145 150 155 160 Asn Ala Arg Leu Gln Tyr Pro Val Leu Lys Lys Val Phe Lys Asn Ser 165 170 175 Gly Ile Thr Asp Glu Asp Ser Glu Met Leu Ile Lys Lys Phe Gln Asp 180 185 190 Gln Tyr Ile His Trp Glu Glu Asn Ser Phe Pro Gly Ser Leu Gly Asn 195 200 205 Val Ile Ser Gly Arg Ile Ala Asn Arg Phe Asp Leu Gly Gly Met Asn 210 215 220 Cys Val Val Asp Ala Ala Cys Ala Gly Ser Leu Ala Ala Leu Arg Met 225 230 235 240 Ala Leu Ser Glu Leu Val Glu Gly Arg Ser Glu Met Met Ile Thr Gly 245 250 255 Gly Val Cys Thr Asp Asn Ser Pro Thr Met Tyr Met Ser Phe Ser Lys 260 265 270 Thr Pro Ala Phe Thr Thr Asn Glu Thr Ile Gln Pro Phe Asp Ile Asp 275 280 285 Ser Lys Gly Met Met Ile Gly Glu Gly Ile Gly Met Ile Ala Leu Lys 290 295 300 Arg Leu Glu Asp Ala Glu Arg Asp Gly Asp Arg Ile Tyr Ser Val Ile 305 310 315 320 Lys Gly Val Gly Ala Ser Ser Asp Gly Lys Phe Lys Ser Ile Tyr Ala 325 330 335 Pro Arg Pro Glu Gly Gln Ala Lys Ala Leu Lys Arg Ala Tyr Asp Asp 340 345 350 Ala Gly Phe Ala Pro His Thr Leu Gly Leu Leu Glu Ala His Gly Thr 355 360 365 Gly Thr Ala Ala Gly Asp Val Ala Glu Phe Ser Gly Leu Asn Ser Val 370 375 380 Phe Ser Glu Gly Asn Asp Glu Lys Gln His Ile Ala Leu Gly Ser Val 385 390 395 400 Lys Ser Gln Ile Gly His Thr Lys Ser Thr Ala Gly Thr Ala Gly Leu 405 410 415 Ile Lys Ala Ser Leu Ala Leu His His Lys Val Leu Pro Pro Thr Ile 420 425 430 Asn Val Thr Ser Pro Asn Pro Lys Leu Asn Ile Glu Asp Ser Pro Phe 435 440 445 Tyr Leu Asn Thr Gln Thr Arg Pro Trp Met Gln Arg Val Asp Gly Thr 450 455 460 Pro Arg Arg Ala Gly Val Ser Ser Phe Gly Phe Gly Gly Thr Asn Phe 465 470 475 480 His Ile Val Leu Glu Glu Tyr Thr Pro Glu His Ala Arg Gly Asp Lys 485 490 495 Tyr Arg Gln Arg Gln Val Ala Gln Thr Leu Leu Phe Ser Ala Ala Ser 500 505 510 Arg Glu Ala Leu Ile Ala Ser Leu Lys Glu Thr Ser Ala Asn Leu Ala 515 520 525 Asn Asp Ser Val Asn Leu Glu Thr Leu Ala Glu Ser His Gly Leu Arg 530 535 540 Ser Ile Glu Val Ser His Ala Arg Leu Gly Leu Ala Val Lys Thr Gly 545 550 555 560 Glu Glu Leu Asn Thr Gln Leu Ala Gln Ala Ile Ser Asn Leu Glu Ser 565 570 575 Gln Thr Lys Ala His Trp Gln Leu Pro Ser Gly Thr Ser Tyr Arg Glu 580 585 590 Ser Ala Leu Val Ser Gly Asn Asp Ser Ala Lys Val Ala Ala Leu Phe 595 600 605 Ala Gly Gln Gly Ser Gln Tyr Leu Asn Met Gly Arg Glu Leu Ala Cys 610 615 620 His Tyr Pro Glu Met Arg Gln Gln Leu Ala Lys Ala Asp Gln Val Phe 625 630 635 640 Gly Gln Asn Lys Lys Thr Ala Leu Ser Gln Val Leu Phe Pro Ile Pro 645 650 655 Met Phe Asn Lys Glu Ser Thr Gln Ala Gln Glu Ala Leu Leu Thr Asn 660 665 670 Thr Ala Asn Ala Gln Ser Ala Ile Gly Val Met Ser Met Gly Gln Phe 675 680 685 Glu Leu Leu Thr Gln Ala Gly Phe Lys Ala Asp Met Val Ala Gly His 690 695 700 Ser Phe Gly Glu Leu Ser Ala Leu Cys Ala Ser Gly Val Ile Ser Gln 705 710 715 720 Asp Asp Tyr Tyr Gln Leu Ala Phe Ala Arg Gly Asn Ala Met Ala Ala 725 730 735 Thr Pro Ala Glu Gly Asp Ser Gly Thr Met Tyr Ala Val Ile Leu Asp 740 745 750 Ala Asp Lys Leu Ala Asp Val Glu Lys Cys Ile Ser Ala Phe Glu Gly 755 760 765 Val Ser Ile Ala Asn Tyr Asn Ala Pro Thr Gln Leu Val Ile Ala Gly 770 775 780 Pro Thr Asp Ser Ala Gln Leu Ala Ala Lys Ala Leu Thr Glu Gln Gly 785 790 795 800 Phe Lys Ala Ile Pro Leu Pro Val Ser Gly Ala Phe His Thr Pro Leu 805 810 815 Val Ala His Ala Gln Lys Pro Phe Ala Ala Ala Ile Asp Lys Ala Thr 820 825 830 Phe Ser Thr Pro Ala Leu Pro Leu Tyr Ser Asn Ala Thr Gly Glu Leu 835 840 845 His Lys Asn Asp Gly Lys Ala Ile Lys Lys Ala Phe Lys Gln His Met 850 855 860 Leu Gln Ser Val Arg Phe Ser Thr Gln Leu Glu Ala Met Tyr Asp Ala 865 870 875 880 Gly Ala Arg Val Phe Val Glu Phe Gly Pro Lys Asn Ile Leu Gln Lys 885 890 895 Leu Val Glu Lys Thr Leu Thr Asn Lys Ala Asp Glu Leu Cys Thr Ile 900 905 910 Ser Ile Asn Pro Asn Pro Lys Gly Asp Ser Asp Gln Gln Leu Arg Leu 915 920 925 Ala Ala Val Gln Leu Ala Val Val Gly Ile Ser Leu Asp Asn Ile Asp 930 935 940 Pro Tyr Gln Ala Glu Ile Ala Pro Pro Ala Ala Thr Ser Pro Met Asn 945 950 955 960 Ile Lys Leu Asn Ala Ala Asn Tyr Ile Ser Pro Ala Thr Arg Ala Lys 965 970 975 Met Ala Lys Ser Leu Thr Thr Gly Glu Val Ser Thr Lys Thr Glu Ile 980 985 990 Val Glu Lys Val Val Glu Lys Ile Val Glu Lys Glu Val Ile Lys Thr 995 1000 1005 Glu Ile Arg Glu Val Pro Val Ala Ala Ala Pro Thr Gln Ala Val 1010 1015 1020 Thr Val Gln Ser Thr Ala Gln Ala Ala Pro Gln Pro Val Val Thr 1025 1030 1035 Thr Ala Pro Ala Gln Val Val Thr Gln Ala Thr Ser Gln Leu Pro 1040 1045 1050 Val Gly Glu Ala Ser Leu His Ala Phe Phe Ser Ala Gln Gln Gln 1055 1060 1065 Ala Ala Glu Leu His Gln Gln Phe Leu Ala Ile Pro Gln Gln Tyr 1070 1075 1080 Gly Asp Thr Phe Thr Ala Leu Met Thr Glu Gln Ala Lys Met Ala 1085 1090 1095 Thr Ala Gly Ile Ala Ile Pro Glu Ser Leu Gln Arg Ser Met Glu 1100 1105 1110 Leu Phe His Gln His Gln Ala Glu Thr Leu Lys Ala His Ala His 1115 1120 1125 Tyr Leu Glu Leu Gln Ala Asn Ser Asn Asn Ser Ala Leu Gly Met 1130 1135 1140 Leu Thr Ser Gln Ala Pro Ala His Gln Val Pro Val Tyr Gln Thr 1145 1150 1155 Pro Ile Gln Gln Val Ser Val Ala Pro Ala Pro Ala Ala Pro Val 1160 1165 1170 Val Thr Pro Val Val Ala Ala Pro Val Ala Thr Pro Thr Pro Ile 1175 1180 1185 Lys Ala Val Ile Gln Thr Gln Gln Ser Ala Pro Val Ala Ser Ala 1190 1195 1200 Pro Ile Ala Ala Pro Val Thr Gln Thr Val Lys Pro Thr Pro Val 1205 1210 1215 Val Gln Ala Ala Val Ala Pro Gln Ala Ala Val Gln Thr Ala Asn 1220 1225 1230 Pro Glu Gln Val Met Leu Glu Val Val Ala Glu Lys Thr Gly Tyr 1235 1240 1245 Pro Thr Glu Met Leu Asp Leu Asp Met Asp Met Glu Ala Asp Leu 1250 1255 1260 Gly Ile Asp Ser Ile Lys Arg Val Glu Ile Leu Gly Thr Val Gln 1265 1270 1275 Asp Gln Met Pro Asn Leu Pro Glu Leu Ser Pro Glu Asp Leu Ala 1280 1285 1290 Glu Cys Arg Thr Leu Arg Glu Ile Val Thr Tyr Met Asn Ser Lys 1295 1300 1305 With Pro Ala Ala Ala Ala Ser Ala Pro Val Thr Ser Ala Ser Asn 1310 1315 1320 Gly Leu Asp Ala Ala Gln Val Gln Ser Thr Met Leu Glu Val Val 1325 1330 1335 Ala Asp Lys Thr Gly Tyr Pro Thr Glu Met Leu Asp Leu Glu Met 1340 1345 1350 Asp With Glu Ala Asp Leu Gly Ile Asp Ser Ile Lys Arg Val Glu 1355 1360 1365 Ile Leu Gly Thr Val Gln Asp Gln Leu Pro Thr Leu Pro Glu Leu 1370 1375 1380 Ser Pro Glu Asp Leu Ala Glu Cys Arg Thr Leu Gly Glu Ile Val 1385 1390 1395 Ser Tyr With Asn Ser Lys Leu Pro Ala Ala Ser Ala Val Ala Ala 1400 1405 1410 Pro Val Ala Ser Ala Pro Val Ala Ser Ala Ser Asn Gly Leu Asp 1415 1420 1425 Ala Ala Gln Val Gln Thr Thr With Leu Asp Val Val Ala Asp Lys 1430 1435 1440 Thr Gly Tyr Pro Thr Glu Met Leu Asp Leu Ala Met Asp Met Glu 1445 1450 1455 Ala Asp Leu Gly Ile Asp Ser Ile Lys Arg Val Glu Ile Leu Gly 1460 1465 1470 Thr Val Gln Asp Gln Leu Pro Gly Leu Pro Glu Leu Asn Pro Glu 1475 1480 1485 Asp Leu Ala Glu Cys Arg Thr Leu Gly Glu Ile Val Asp Tyr Met 1490 1495 1500 Asn Ser Lys Leu Pro Ala Val Ser Thr Gln Asn Val Ala Ile Gln 1505 1510 1515 Thr Ala Ala Pro Val Ala Ser Ala Ser Asn Gly Leu Asp Ala Ala 1520 1525 1530 Gln Val Gln Gly Thr Met Leu Glu Val Val Ala Asp Lys Thr Gly 1535 1540 1545 Tyr Pro Ala Glu Met Leu Asp Phe Ala Met Asp Met Glu Ala Asp 1550 1555 1560 Leu Gly Ile Asp Ser Ile Lys Arg Val Glu Ile Leu Gly Thr Val 1565 1570 1575 Gln Asp Gln Leu Pro Gly Leu Pro Glu Leu Asn Pro Glu Asp Leu 1580 1585 1590 Ala Glu Cys Arg Thr Leu Gly Glu Ile Val Asp Tyr Met Asn Ser 1595 1600 1605 Lys Leu Pro Ala Ala Ser Thr Gln Asn Val Ala Val Gln Thr Val 1610 1615 1620 Ala Ala Pro Val Ala Thr Ala Pro Ala Thr Asn Gly Leu Asp Ala 1625 1630 1635 Ala His Val Gln Asn Thr Met Met Asn Val Val Ala Asp Lys Thr 1640 1645 1650 Gly Tyr Pro Ala Glu Met Leu Asp Leu Ala Met Asp Met Glu Ala 1655 1660 1665 Asp Leu Gly Ile Asp Ser Ile Lys Arg Val Glu Ile Leu Gly Thr 1670 1675 1680 Val Gln Asp Gln Leu Pro Gly Leu Pro Glu Leu Asn Pro Glu Asp 1685 1690 1695 Leu Ala Glu Cys Arg Thr Leu Gly Glu Ile Val Ala Tyr Met Gln 1700 1705 1710 Ser Lys Leu Ser Asn Thr Ser Ala Val Ala Ala Pro Ser Ala Pro 1715 1720 1725 Ala Val Glu Asn Leu Val Glu Ala Ile Ala Glu Thr Ser Asn Val 1730 1735 1740 Glu Leu Pro Pro His Ser Glu Val Ala Leu Lys Lys Leu Pro Ala 1745 1750 1755 Val Asp Lys Leu Val Asp Cys Phe Ser Lys Glu Ala Cys Ile Val 1760 1765 1770 Ile Thr Asp Asp Gly His Asn Ala Gly Val Leu Ala Glu Lys Leu 1775 1780 1785 Ser Ala Asn Gly Leu Gln Val Ala Val Val Arg Ser Pro Leu Ser 1790 1795 1800 Ala Ala Ser Pro Leu Asn Ser Glu Ile Ala Ser Tyr Thr Leu Ala 1805 1810 1815 Ser Ile Asp Asp Ala Ser Ile Lys Thr Val Ile Ser Asp Ile Glu 1820 1825 1830 Ser Lys Gln Lys Glu Ile Gly Gly Phe Ile His Leu Gln Pro Leu 1835 1840 1845 Ala Thr Asp Ala Lys Thr Asp Lys Ala Thr Ala Val Thr Leu His 1850 1855 1860 Ala Thr Ala Lys Glu Ser Ile Ser Met Ala Phe Leu Phe Ala Lys 1865 1870 1875 Leu Leu Lys Thr Gln Leu Asn Ala Ala Lys Asn Arg Ser Ala Phe 1880 1885 1890 Phe Thr Val Ser Arg Ile Asp Gly Gly Phe Gly Tyr Leu Asn Ala 1895 1900 1905 Glu Gln Leu Ile Asn Ala Glu Leu Asn Gln Ala Ala Leu Ser Gly 1910 1915 1920 Leu Thr Lys Thr Leu Ser His Glu Trp Ser Thr Val Phe Cys Arg 1925 1930 1935 Ala Leu Asp Val Ala Pro Thr Leu Asp Ala Arg His Leu Ala Glu 1940 1945 1950 Ala Val Thr Ala Glu Leu Phe Asp Ile Asp Thr His Thr Val Glu 1955 1960 1965 Val Gly Leu Ala Asp Ala Asn Asn Gly Glu Ser Gly Arg Ala Thr 1970 1975 1980 Leu Ile Ala Thr Asn Ala Gly Thr Ala Leu Thr Lys Asn Ala Ser 1985 1990 1995 Ala Lys Leu Asp Lys Asn Asp Asn Val Leu Val Thr Gly Gly Ala 2000 2005 2010 Lys Gly Val Thr Phe Glu Cys Ala Leu Thr Leu Ala Lys Gln Cys 2015 2020 2025 Lys Ser His Phe Ile Leu Ala Gly Arg Ser Gln His Ile Thr Ala 2030 2035 2040 Asn Glu Leu Pro Glu Trp Ala Gln Gly Lys Gln Ala Asn Glu Leu 2045 2050 2055 Lys Pro Ala Ala Ile Arg His Ile Gln Thr Ser Gly Glu Lys Pro 2060 2065 2070 Thr Pro Lys Lys Val Asp Ala Leu Leu Lys Pro Val Leu Ser Ser 2075 2080 2085 Leu Glu Ile Asn Thr Ala Leu Ser Ala Phe Ala Asn Val Gly Ala 2090 2095 2100 Ser Ala Glu Tyr Ile Ser Leu Asp Val Ser Ser Ser Asp Ser Val 2105 2110 2115 Ala Lys Thr Leu Ser Gln Phe Asn Asp Ile Thr Gly Leu Ile His 2120 2125 2130 Gly Ala Gly Val Leu Ala Asp Lys His Ile Gln Asp Lys Thr Leu 2135 2140 2145 Asp Glu Leu Asn Leu Val Tyr Gly Thr Lys Val Gly Gly Leu Glu 2150 2155 2160 Ala Val Leu Asn Ala Leu Asn Ser Asp Lys Leu Lys Leu Val Ala 2165 2170 2175 Met Phe Ser Ser Ala Ala Gly Phe Tyr Gly Asn Thr Gly Gln Ser 2180 2185 2190 Asp Tyr Ala Met Ser Asn Glu Ile Leu Asn Lys Ala Ala Leu Gln 2195 2200 2205 Leu Ser Ala Arg Asn Pro Glu Ala Lys Val Met Ser Phe Asn Trp 2210 2215 2220 Gly Pro Trp Asp Gly Gly Met Val Asn Ala Ala Leu Lys Lys Met 2225 2230 2235 Phe Thr Asp Arg Gly Val Tyr Val Ile Pro Leu Gln Ala Gly Ala 2240 2245 2250 Glu Leu Phe Ser Ser Gln Leu Leu Ser Glu Thr Gly Ile Gln Leu 2255 2260 2265 Leu Val Gly Thr Ser Met Gln Gly Ser Asp Asn Lys Glu Ala Ala 2270 2275 2280 Val Lys Lys Leu Asp Ala Glu Ser Met Leu Val Ala Lys Ser Pro 2285 2290 2295 Leu Asn Ser Ser Ile Thr Val Thr Arg Asp Leu Asp Pro Lys Ala 2300 2305 2310 Met Pro Phe Ile Asn Asp His Cys Ile Ala Gly Asn Pro Val Leu 2315 2320 2325 Pro Thr Val Cys Ala Ile Gln Trp Met Arg Glu Ala Ala Glu Gln 2330 2335 2340 Leu Leu Gly Ala Asn Val Thr Val Arg Asp Tyr Lys Leu Leu Lys 2345 2350 2355 Gly Val Ile Phe Asp Thr Asn Glu Ile Gln Thr Leu Thr Leu Thr 2360 2365 2370 Leu Thr Pro Asp Glu Lys Ala Thr Asp Gln Ile Lys Ala Leu Ile 2375 2380 2385 Ser Cys Gln Asp Arg Pro Gln Tyr Lys Ala Met Leu Val Val Glu 2390 2395 2400 Pro Val Pro Ala Thr Gln Ala Lys Thr Phe Val Ala Asn Ser Asn 2405 2410 2415 Glu Pro Ile Thr Thr Ala Lys Ala Leu Tyr Ser Asn Gly Thr Leu 2420 2425 2430 Phe His Gly Pro Arg Leu Gln Gly Ile Thr Thr Val Glu Arg Phe 2435 2440 2445 Asp Asp Ala Gly Leu Leu Ala Gln Cys Gln Leu Pro Thr Val Ala 2450 2455 2460 Asp Thr Asp Cys Gly Ala Phe Val Pro Thr Gln His Leu Gly Gly 2465 2470 2475 Cys Gln Pro Phe Ala Glu Asp Tyr Leu Leu Gln Ala Met Leu Val 2480 2485 2490 Trp Ala Arg Leu Lys Tyr Gly Ala Ala Ser Leu Pro Ser Ala Ile 2495 2500 2505 Gly Glu Phe Val Ser Tyr Glu Pro Met Gln Ala Gly Asp Lys Gly 2510 2515 2520 Trp of Glu and Asp Val Ile Asn Thr Thr Arg Ser of Gln 2525 2530 2535 Only Asn with Tyr is Gln Asp Gly Arg with Val 2540 2545 2550 Met Lys Ser Ala Lys Val Thr Ile Ser Lys Ser Leu Asn Glu Ala 2555 2560 2565 Phe Leu Val Lys Ser Glu Pro Glu Lys Glu Leu Leu Ser 2570 2575 2580 <210> 67 <211> 2076 <212> DNA <213> Photobacterium profundum SS9 (Photobacterium profundum SS9) <220> <221> CDS <222> (1)..(2076) <400> 67 atg cca ttg cgc atc gct ctt tta gcc caa gca gc gc gct gct ggg 48 Met Pro Leu Arg Ile Ala Leu Leu Ala Gln Ala Asp Ala Gly 1 5 10 15 ctt tct gcc gat att cta gcg tca tta cca gca att caa cat att gct 96 Leu Ser Wing Asp Ile Leu Wing Ser Leu Pro Wing Ile Gln His Ile Wing 20 25 30 att aat gac aac ttc aat gcc gcg ctt caa act gct att caa gcg gta 144 I Asn Asp Asn Phe Asn Ala Ala Leu Gln Thr Ala Ile Gln Ala Val 35 40 45 aac caa gt cag cta gtt caa ctt acc ctc caa tgt aag ccg aac gaa 192 Asn Gln Gly Gln Leu Val Gln Leu Thr Leu Gln Cys Lys Pro Asn Glu 50 55 60 cca caa cag cgt tta ctg atg ctt agc ggt tta gct gct gct aaa aac 240 Pro Gln Gln Arg Leu Met Leu Ser Gly Leu Ala Ala Ala Lys Asn 65 70 75 80 aaa att cac cct cac gcg tac ctt gca ggt tt gct gaa ggc tct gtt 288 Lys Ile His Pro His Ala Tyr Leu Ala Gly Phe Ala Glu Gly Ser Val 85 90 95 aat agc cta gaa ata gcc ctc aac cag tct cgt cgt caa aat gcc gat 336 Ser Asn To Glu Ile Ala To Asn Gln Ser Arg Arg Gln Asn To Asp 100 105 110 ctc agt cat caa caa aca tct gaa aca tta gct gct gat cag cag ttt 384 Leu Ser His Gln Gln Thr Ser Glu Thr Leu Ala Ala Asp Gln Gln Phe 115 120 125 ctc gct ttc ttt aac atg gtt gat gat att gct cgc cgg aca ctg cac 432 Leu Ala Phe Phe Asn Met Val Asp Asp Ile Ala Arg Arg Thr Leu His 130 135 140 gcg gca gct cat gct gca aac aat gca agc cat tac tgg ttt act gag 480 Ala Ala Ala His Ala Ala Asn Asn Ala Ser His Tyr Trp Phe Thr Glu 145 150 155 160 ccc cat aaa gca cgc gta gct agt tta acg ttt aat gcc aat tct gat 528 Pro His Lys Ala Arg Val Ala Ser Leu Thr Phe Asn Ala Asn Ser Asp 165 170 175 tca gaa agt agc ttg gta tta acg caa gca aca ggg tta caa aaa gcg 576 Ser Glu Ser Ser Leu Val Leu Thr Gln Ala Thr Gly Leu Gln Lys Ala 180 185 190 caa tca tta ctg aac gcc tct cgc tta ttc ttt gtc ctc tca ggg ctg 624 Gln Ser Leu Leu Asn Ala Ser Arg Leu Phe Phe Val Leu Ser Gly Leu 195 200 205 aat gaa ata gaa tta tca gtg CA tta gaa cag cta aag CA cgt tta 672 Asn Glu Ile Glu Leu Ser Val Gln Leu Glu Gln Leu Lys Gln Arg Leu 210 215 220 gct gat tta cct aat gat tta aca cca aat gac at gct gct ctt att 720 Ala Asp Leu Pro Asn Asp Leu Thr Pro Asn Asp Asn Ala Ala Ala Leu Ile 225 230 235 240 gct tta atg act aag aac tta gcg cag tat caa act gac gtt tcg tct 768 Only Met Thr Lys Asn Only Only Gln Tyr Gln Thr Asp Val Ser Ser 245 250 255 tct gcc act tca tcg ata tca cta ccg act atc gtg ttg caa ggc gct 816 To Be Thr To Be There To Be A Leu Pro Thr Island Val Leu Gln Gly Wing 260 265 270 tct gtt acc gct gtt ttg cag gaa ata tct gca atc ​​agt aat gct ttg 864 Be Thr Wing Val Leu Gln Glu Ile Be Wing Island Be Asn Wing Leu 275 280 285 cca aaa gta ata gca gag aaa agt cat tac aaa aca cca gcc ggt agt 912 Pro Lys Val Ile Ala Glu Lys Ser His Tyr Lys Thr Pro Ala Gly Ser 290,295,300 tgt ttc tcg cct gca ccc aat agc aaa ggt ggt gtc act ttt gtc tac 960 Cys Phe Ser Pro Ala Pro Asn Ser Lys Gly Gly Val Thr Phe Val Tyr 305 310 315 320 cca ggt gtt ggt act gta tac cct ggc atg ttc cgt gat ttt cat cag 1008 Pro Gly Val Gly Thr Val Tyr Pro Gly Met Phe Arg Asp Phe His Gln 325 330 335 tat ttc ccc gca ctt ttt gca caa cta gag cgc gaa gga aac ctg aaa 1056 Tyr Phe Pro Ala Leu Phe Ala Gln Leu Glu Arg Glu Gly Asn Leu Lys 340 345 350 gaa atg cta caa gcc gaa aag aca tac ggt gaaaac cca gcc gaa atg 1104 Glu Met Leu Gln Ala Glu Lys Thr Tyr Gly Glu Asn Pro Ala Glu Met 355 360 365 aca ctc ggt gaa ttg gcc att gcc ggt gtt gtt agc agc tac tta tta 1152 Thr Leu Gly Glu Leu Ala Ile Ala Gly Val Gly Ser Ser Tyr Leu Leu 370 375 380 act caa tta ctc tgc gaa gag ttt gcc gtt aag cct gat ttc gct tta 1200 Thr Gln Leu Leu Cys Glu Glu Phe Ala Val Lys Pro Asp Phe Ala Leu 385 390 395 400 ggt tac tct aaa ggt gaa gca tcg atg tgg gcg agt tta ggt gtg tgg 1248 Gly Tyr Ser Lys Gly Glu Ala Ser Met Trp Ala Ser Leu Gly Val Trp 405 410 415 aaa aat ccg cac gca tta atc gaa ctg acc caa acg agc cca ata ttc 1296 Lys Asn Pro His Ala Leu Ile Glu Leu Thr Gln Thr Ser Pro Ile Phe 420 425 430 acc acc gct att tcc ggt aag cta acc gct gtt cgt gaa gca tgg caa 1344 Thr Thr Ala Ile Ser Gly Lys Leu Thr Ala Val Arg Glu Ala Trp Gln 435 440 445 tta aca gat gct gaa gaa att acg tgg aat agc ttt gtt gtt cgc tgt 1392 Leu Thr Asp Ala Glu Glu Ile Thr Trp Asn Ser Phe Val Val Arg Cys 450 455 460 gaa tca gcc acc att gaa gca ttg tg cct gaa ttt ccg cgg gcc tat 1440 Glu Ser Ala Thr Ile Glu Ala Leu Leu Pro Glu Phe Pro Arg Ala Tyr 465 470 475 480 ctt gct att att caa ggt gac act tgt gta tta gct ggt tgt gaa gcg 1488 Leu Wing With Gln Gly Asp Thr Cys Val Leu Wing Gly Cys Glu Ala 485,490,495 acg tgt cgc gct tta ctc aaa aag ctt ggt aaa cgc ggc att gca gcg 1536 Thr Cys Arg Ala Leu Lys Lys Leu Gly Lys Arg Gly Ile Ala Ala Ala 500 505 510 aat cgt gta acc gct atg cac acc acca cca gcg tta agt cag cat tca 1584 Asn Arg Val Thr Ala Met His Thr Pro Ala Leu Ser Gln His Ser 515,520,525 caa gtc acc gag ttt tat act cag cca tta tgt gat gaa cta ccg atg 1632 Gln Val Thr Glu Phe Tyr Thr Gln Pro Leu Cys Asp Glu Leu Pro Met 530 535 540 gat att aaa ttc atc agc gct gct ggg ctg tg cct caa aat caa aac 1680 Asp Ile Lys Phe Ile Ser Ala Ala Gly Leu Leu Pro Gln Asn Gln Asn 545 550 555 560 gtg cct gtt aat atc gat agc caa agt att gcc aat tcc att gcc gat 1728 Val Pro Val Asn Ile Asp Ser Gln Ser Ile Ala Asn Ser Ile Ala Asp 565 570 575 acc ttt tgc aca aca ctc gat ttt acc gct ttg att cgc acc gct cgt 1776 Thr Phe Cys Thr Thr Leu Asp Phe Thr Ala Leu Ile Arg Thr Ala Arg 580 585 590 gaa caa ggc gca cgt tta ttt gtt gaa att ggt gcc gac aga caa acc 1824 Glu Gln Gly Ala Arg Leu Phe Val Glu Ile Gly Ala Asp Arg Gln Thr 595 600 605 agt acg ctt atc gat aag ata aac cgt aca gat aac gta aca act gag 1872 Ser Thr Leu Ile Asp Lys Ile Asn Arg Thr Asp Asn Val Thr Thr Glu 610 615 620 agt tgt act gtc gcg gcg aat gca aaa ggc ggc gaa gat att gtt act 1920 Ser Cys Thr Val Ala Ala Asn Ala Lys Gly Gly Glu Asp Ile Val Thr 625 630 635 640 ttg ctt aaa tgc att gcc cag tta att acg cac caa ata ccg ctg tca 1968 Leu Leu Lys Cys Ile Ala Gln Leu Ile Thr His Gln Ile Pro Leu Ser 645 650 655 ctt tct ccc ctg ctt caa ggg tta gaa gaa caa gtg aat gca ctg aaa 2016 Leu Ser Pro Leu Leu Gln Gly Leu Glu Glu Gln Val Asn Ala Leu Lys 660 665 670 tta cac agt gta tcg tca gcg aat acc aca ccg aac act aca caa gga 2064 Leu His Ser Val Ser Ser Ala Asn Thr Thr Pro Asn Thr Thr Gln Gly 675 680 685 gag about gtg tga 2076 Glu Pro Wave 690 <210> 68 <211> 691 <212> PRT <213> Photobacterium profundum SS9 <400> 68 Met Pro Leu Arg Ile Ala Leu Leu Ala Gln Ala Ala Asp Ala Ala Gly 1 5 10 15 Leu Ser Ala Asp Ile Leu Ala Ser Leu Pro Ala Ile Gln His Ile Ala 20 25 30 Ile Asn Asp Asn Phe Asn Ala Ala Leu Gln Thr Ala Ile Gln Ala Val 35 40 45 Asn Gln Gly Gln Leu Val Gln Leu Thr Leu Gln Cys Lys Pro Asn Glu 50 55 60 Pro Gln Gln Arg Leu Leu Met Leu Ser Gly Leu Ala Ala Ala Lys Asn 65 70 75 80 Lys Ile His Pro His Ala Tyr Leu Ala Gly Phe Ala Glu Gly Ser Val 85 90 95 Asn Ser Leu Glu Ile Ala Leu Asn Gln Ser Arg Arg Gln Asn Ala Asp 100 105 110 Leu Ser His Gln Gln Thr Ser Glu Thr Leu Ala Ala Asp Gln Gln Phe 115 120 125 Leu Ala Phe Phe Asn Met Val Asp Asp Ile Ala Arg Arg Thr Leu His 130 135 140 Ala Ala Ala His Ala Ala Asn Asn Ala Ser His Tyr Trp Phe Thr Glu 145 150 155 160 Pro His Lys Ala Arg Val Ala Ser Leu Thr Phe Asn Ala Asn Ser Asp 165 170 175 Ser Glu Ser Ser Leu Val Leu Thr Gln Ala Thr Gly Leu Gln Lys Ala 180 185 190 Gln Ser Leu Leu Asn Ala Ser Arg Leu Phe Phe Val Leu Ser Gly Leu 195 200 205 Asn Glu Ile Glu Leu Ser Val Gln Leu Glu Gln Leu Lys Gln Arg Leu 210 215 220 Ala Asp Leu Pro Asn Asp Leu Thr Pro Asn Asp Asn Ala Ala Leu Ile 225 230 235 240 Ala Leu Met Thr Lys Asn Leu Ala Gln Tyr Gln Thr Asp Val Ser Ser 245 250 255 Ser Ala Thr Ser Ser Ile Ser Leu Pro Thr Ile Val Leu Gln Gly Ala 260 265 270 Ser Val Thr Ala Val Leu Gln Glu Ile Ser Ala Ile Ser Asn Ala Leu 275 280 285 Pro Lys Val Ile Ala Glu Lys Ser His Tyr Lys Thr Pro Ala Gly Ser 290 295 300 Cys Phe Ser Pro Ala Pro Asn Ser Lys Gly Gly Val Thr Phe Val Tyr 305 310 315 320 Pro Gly Val Gly Thr Val Tyr Pro Gly Met Phe Arg Asp Phe His Gln 325 330 335 Tyr Phe Pro Ala Leu Phe Ala Gln Leu Glu Arg Glu Gly Asn Leu Lys 340 345 350 Glu Met Leu Gln Ala Glu Lys Thr Tyr Gly Glu Asn Pro Ala Glu Met 355 360 365 Thr Leu Gly Glu Leu Path To Path Gly Val Gly Ser Ser Tyr Leu Leu 370 375 380 Thr Gln Leu Leu Cys Glu Glu Phe Ala Val Lys Pro Asp Phe Ala Leu 385 390 395 400 Gly Tyr Ser Lys Gly Glu Path Ser Met Trp Path Ser Leu Gly Val Trp 405 410 415 Lys Asn Pro His Ala Leu To Glu Leu Thr Gln Thr Ser Pro To Phe 420 425 430 Thr Thr Path To Ser Gly Lys Leu Thr Path Val Arg Glu Path Trp Gln 435 440 445 Leu Thr Asp Ala Glu Glu Ile Thr Trp Asn Ser Phe Val Val Arg Cys 450 455 460 Glu Ser Path Thr Ile Glu Path Leu Leu Pro Glu Phe Pro Arg Path Tyr 465 470 475 480 Leu Path Ile Gln Gly Asp Thr Cys Val Leu Path Gly Cys Glu Path 485 490 495 Thr Cys Arg Ala Leu Leu Lys Lys Leu Gly Lys Arg Gly Ile Ala Ala 500 505 510 Asn Arg Val Thr Ala Met His Thr Thr Pro Ala Leu Ser Gln His Ser 515 520 525 Gln Val Thr Glu Phe Tyr Thr Gln Pro Leu Cys Asp Glu Leu Pro Met 530 535 540 Asp Ile Lys Phe Ile Ser Ala Ala Gly Leu Leu Pro Gln Asn Gln Asn 545 550 555 560 Val Pro Val Asn Ile Asp Ser Gln Ser Ile Ala Asn Ser Ile Ala Asp 565 570 575 Thr Phe Cys Thr Thr Leu Asp Phe Thr Ala Leu Ile Arg Thr Ala Arg 580 585 590 Glu Gln Gly Ala Arg Leu Phe Val Glu Ile Gly Ala Asp Arg Gln Thr 595 600 605 Ser Thr Leu Ile Asp Lys Ile Asn Arg Thr Asp Asn Val Thr Thr Glu 610 615 620 Ser Cys Thr Val Ala Ala Asn Ala Lys Gly Gly Glu Asp Ile Val Thr 625 630 635 640 Leu Leu Lys Cys Ile Ala Gln Leu Ile Thr His Gln Ile Pro Leu Ser 645 650 655 Leu Ser Pro Leu Leu Gln Gly Leu Glu Glu Gln Val Asn Ala Leu Lys 660,665,670 Leu His Ser Val Ser Ala Asn Thr Thr Pro Asn Thr Thr Gln Gly 675,680,685 Pro Val Glue 690 <210> 69 <211> 6021 <212> DNA <213> Photobacterium profundum SS9 (Photobacterium profundum SS9) <220> <221> CDS <222> (1)..(6021) <400> 69 atg cat tgc cca gtt aat tac gca cca aat acc gct gtc act ttc tcc 48 Met His Cys Pro Val Asn Tyr Ala Pro Asn Thr Ala Val Thr Phe Ser 1 5 10 15 cct gct tca agg gtt aga aga aca agt gaa tgc gaa att aca cag 96 Pro Only Ser Arg Val Arg Serves Through Glu Cys Through Glu and Three Gln 20 25 30 tgt atc g...

Claims

1. A microorganism capable of producing PUFA, wherein genes encoding the domains described in (a) to (j) below having an activity for synthesizing PUFA, i.e., PUFA-PKS activity, are introduced into a microorganism not having a polyunsaturated fatty acid metabolic pathway, i.e., a PUFA metabolic pathway, in, The polyketide synthase dehydratase, i.e., the PS-DH domain, exhibits higher activity towards 3-hydroxyhexanoyl-ACP than the FabA-like β-hydroxyacyl-ACP dehydratase, i.e., the FabA-DH domain, and the PUFA that can be produced is arachidonic acid, i.e., ARA, or docosapentaenoic acid, i.e., DPA. (a) β-ketoacyl-ACP synthase, i.e., KS domain; (b) malonyl-CoA:ACP acyltransferase, i.e., MAT domain; (c) ACP domain; (d) ketoreductase or KR domain; (e) PS-DH domain; (f) chain elongation factor, i.e., CLF domain; (g) acyltransferase or AT domain; (h) FabA-DH domain; (i) Enoyl ACP reductase, i.e., the ER domain; (j) phosphopantetheinyl transferase or PPT domain, The microorganism without PUFA metabolic pathway is Escherichia coli with a gene deletion encoding acyl-CoA dehydrogenase FadE. The introduced gene is selected from any one of the following genes (1) to (5): (1)phoA, phoB, phoC, phoD, epaE, araB; (2) epaA, phoB, phoC, phoD, epaE, araB; (3) epaA, araB, araC, araD, epaE; (4) phoA, araB, araC, araD, epaE; (5)orfA, orfB, orfC, epaE, araB, The phoA, phoB, phoC and phoD are derived from Photobacterium profundum. The epaA and the epaE are derived from Shewanella oneidensis, The araB, the araC and the araD are derived from Aureispira marina, The orfA, the orfB and the orfC are derived from Schizochytrium sp.

2. A method for producing PUFA or a composition containing PUFA, in, The microorganism according to claim 1 is cultured in a culture medium to produce and accumulate PUFA or a composition containing PUFA in the culture, and the PUFA or the composition containing PUFA is collected from the culture, wherein the PUFA is ARA or DPA.

3. A method for producing PUFA or a composition containing PUFA, in, A PUFA-producing microorganism according to (II) is used, wherein the PUFA that can be produced is ARA or DPA; (II) a PUFA-producing microorganism is a microorganism that has been introduced with genes encoding the domains described in (a) to (j) below having PUFA-PKS activity into a microorganism that does not have a PUFA metabolic pathway, wherein the PS-DH domain exhibits a higher activity toward 3-hydroxyhexanoyl ACP than the FabA-DH domain; (a) KS domain; (b) MAT domain; (c) ACP domain; (d) KR domain; (e) PS-DH domain; (f) CLF domain; (g) AT domain; (h) FabA-DH domain; (i) ER domain; (j) PPT domain, The microorganism without PUFA metabolic pathway is Escherichia coli with a gene deletion encoding acyl-CoA dehydrogenase FadE. The introduced gene is selected from any one of the following genes (1) to (5): (1)phoA, phoB, phoC, phoD, epaE, araB; (2) epaA, phoB, phoC, phoD, epaE, araB; (3) epaA, araB, araC, araD, epaE; (4) phoA, araB, araC, araD, epaE; (5)orfA, orfB, orfC, epaE, araB, The phoA, phoB, phoC and phoD are derived from Photobacterium profundum. The epaA and the epaE are derived from Shewanella oneidensis, The araB, the araC and the araD are derived from Aureispira marina, The orfA, the orfB and the orfC are derived from Schizochytrium sp.

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